ID 128U_DROME STANDARD; PRT; 368 AA. AC P32234; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE GTP-binding protein 128UP. GN 128UP OR GTP-BP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94166747; PubMed=8121394; RA Sommer K.A., Petersen G., Bautz E.K.F.; RT "The gene upstream of DmRP128 codes for a novel GTP-binding protein RT of Drosophila melanogaster."; RL Mol. Gen. Genet. 242:391-398(1994). CC -!- SIMILARITY: BELONGS TO THE GTP1 / OBG FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X71866; CAA50701.1; -. DR PIR; S42582; S42582. DR FlyBase; FBgn0010339; 128up. DR GO; GO:0005525; F:GTP binding; IDA. DR InterPro; IPR006074; GTP1/OBG_dom. DR InterPro; IPR006073; GTP1_OBG. DR InterPro; IPR006169; GTP1_OBG_sub. DR InterPro; IPR005225; Small_GTP. DR InterPro; IPR004095; TGS_dom. DR Pfam; PF01018; GTP1_OBG; 1. DR Pfam; PF02824; TGS; 1. DR PRINTS; PR00326; GTP1OBG. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00905; GTP1_OBG; 1. KW GTP-binding. FT NP_BIND 71 78 GTP (BY SIMILARITY). FT NP_BIND 117 121 GTP (BY SIMILARITY). FT NP_BIND 248 251 GTP (BY SIMILARITY). SQ SEQUENCE 368 AA; 41129 MW; 07C592292BA12A6E CRC64; MITILEKISA IESEMARTQK NKATSAHLGL LKANVAKLRR ELISPKGGGG GTGEAGFEVA KTGDARVGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGCIKYKG AKIQLLDLPG IIEGAKDGKG RGRQVIAVAR TCNLIFMVLD CLKPLGHKKL LEHELEGFGI RLNKKPPNIY YKRKDKGGIN LNSMVPQSEL DTDLVKTILS EYKIHNADIT LRYDATSDDL IDVIEGNRIY IPCIYLLNKI DQISIEELDV IYKIPHCVPI SAHHHWNFDD LLELMWEYLR LQRIYTKPKG QLPDYNSPVV LHNERTSIED FCNKLHRSIA KEFKYALVWG SSVKHQPQKV GIEHVLNDED VVQIVKKV // ID 140U_DROME STANDARD; PRT; 261 AA. AC P81928; Q9VFM8; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE RPII140-upstream protein. GN 140UP OR CG9852. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC TISSUE=Embryo; RX MEDLINE=91276237; PubMed=1905256; RA Sitzler S., Oldenburg I., Petersen G., Bautz E.K.F.; RT "Analysis of the promoter region of the housekeeping gene DmRP140 by RT sequence comparison of Drosophila melanogaster and Drosophila RT virilis."; RL Gene 100:155-162(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ESSENTIAL FOR VIABILITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M62975; AAD40352.2; -. DR EMBL; AE003703; AAF55023.1; -. DR EMBL; AY058577; AAL13806.1; -. DR PIR; JQ1024; JQ1024. DR FlyBase; FBgn0010340; 140up. DR InterPro; IPR003397; Tim17_Tim22. DR Pfam; PF02466; Tim17; 1. KW Transmembrane. FT TRANSMEM 67 87 POTENTIAL. FT TRANSMEM 131 151 POTENTIAL. FT TRANSMEM 183 203 POTENTIAL. FT CARBOHYD 31 31 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 64 64 S -> F (IN REF. 1). SQ SEQUENCE 261 AA; 29182 MW; 5DB78CF6CFC4435A CRC64; MNFLWKGRRF LIAGILPTFE GAADEIVDKE NKTYKAFLAS KPPEETGLER LKQMFTIDEF GSISSELNSV YQAGFLGFLI GAIYGGVTQS RVAYMNFMEN NQATAFKSHF DAKKKLQDQF TVNFAKGGFK WGWRVGLFTT SYFGIITCMS VYRGKSSIYE YLAAGSITGS LYKVSLGLRG MAAGGIIGGF LGGVAGVTSL LLMKASGTSM EEVRYWQYKW RLDRDENIQQ AFKKLTEDEN PELFKAHDEK TSEHVSLDTI K // ID 143E_DROME STANDARD; PRT; 262 AA. AC P92177; Q8IN87; Q9VEA8; DT 15-JUL-1998 (Rel. 36, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 14-3-3 protein epsilon (Suppressor of Ras1 3-9). GN 14-3-3-EPSILON OR 14-3-3E OR SR3-9 OR CG8045. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM D), AND MUTAGENESIS OF GLU-183; PHE-199 RP AND TYR-214. RX MEDLINE=97302963; PubMed=9159394; RA Chang H.C., Rubin G.M.; RT "14-3-3 epsilon positively regulates Ras-mediated signaling in RT Drosophila."; RL Genes Dev. 11:1132-1139(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: POSITIVELY REGULATES RAS-MEDIATED PATHWAYS. ACTS CC DOWNSTREAM OR PARALLEL TO RAF, BUT UPSTREAM OF NUCLEAR FACTORS IN CC RAS SIGNALING. THREE MUTANTS HAVE BEEN ISOLATED, THAT SUPPRESS THE CC ROUGH EYE PHENOTYPE CAUSED BY MUTATED RAS1 (SEV-RAS1 V12). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms may exist; CC Name=A; CC IsoId=P92177-3; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=B; CC IsoId=P92177-2; Sequence=VSP_008203; CC Note=No experimental confirmation available; CC Name=D; CC IsoId=P92177-1; Sequence=VSP_008204; CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U84898; AAC47520.1; -. DR EMBL; U84897; AAC47519.1; -. DR EMBL; AE003721; AAF55519.2; -. DR EMBL; AE003721; AAN13764.1; -. DR EMBL; AE003721; AAN13765.1; -. DR HSSP; P29312; 1A38. DR FlyBase; FBgn0020238; 14-3-3-epsilon. DR GO; GO:0000077; P:DNA damage response, signal transduction re...; IMP. DR GO; GO:0007088; P:regulation of mitosis; IMP. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family; Alternative splicing. FT VARSPLIC 239 239 Missing (in isoform B). FT /FTId=VSP_008203. FT VARSPLIC 239 240 Missing (in isoform D). FT /FTId=VSP_008204. FT MUTAGEN 183 183 E->K: SUPPRESSOR OF SEV-RAS1 V12; FT SUBVIABLE. FT MUTAGEN 199 199 F->Y: SUPPRESSOR OF SEV-RAS1 V12. FT MUTAGEN 214 214 Y->F: SUPPRESSOR OF SEV-RAS1 V12. SQ SEQUENCE 262 AA; 29798 MW; 2C1562208547DA9C CRC64; MTERENNVYK AKLAEQAERY DEMVEAMKKV ASMDVELTVE ERNLLSVAYK NVIGARRASW RIITSIEQKE ENKGAEEKLE MIKTYRGQVE KELRDICSDI LNVLEKHLIP CATSGESKVF YYKMKGDYHR YLAEFATGSD RKDAAENSLI AYKAASDIAM NDLPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQAEEV DPNAGDGEPK EQIQDVEDQD VS // ID 143Z_DROME STANDARD; PRT; 248 AA. AC P29310; O01665; Q9V5G6; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 14-3-3-like protein (Leonardo protein) (14-3-3 zeta). GN 14-3-3-ZETA OR 14-3-3EZ OR LEO OR 14-3-3 OR THAP OR CG17870. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM VI). RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=92241667; PubMed=1349290; RA Swanson K.D., Ganguly R.; RT "Characterization of a Drosophila melanogaster gene similar to the RT mammalian genes encoding the tyrosine/tryptophan hydroxylase RT activator and protein kinase C inhibitor proteins."; RL Gene 113:183-190(1992). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; RX MEDLINE=97302964; PubMed=9159395; RA Kockel L., Vorbrueggen G., Jaeckle H., Mlodzik M., Bohmann D.; RT "Requirement for Drosophila 14-3-3 zeta in Raf-dependent RT photoreceptor development."; RL Genes Dev. 11:1140-1147(1997). RN [3] RP SEQUENCE FROM N.A. (ISOFORM VI). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED IN RAF-DEPENDENT CELL PROLIFERATION AND CC PHOTORECEPTOR DIFFERENTIATION DURING EYE DEVELOPMENT. ACTS CC UPSTREAM OF RAF AND DOWNSTREAM OF RAS, AND IS ESSENTIAL FOR CC VIABILITY. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=VI; CC IsoId=P29310-1; Sequence=Displayed; CC Name=VI'; CC IsoId=P29310-2; Sequence=VSP_000001; CC -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN THE VENTRAL NERVE CC CORD OF THE EMBRYO, AND IN THE NEURAL TISSUES OF THE HEAD. ALSO CC FOUND IN THE REGION POSTERIOR TO THE MORPHOGENETIC FURROW OF THE CC EYE IMAGINAL DISK WHERE CELLS DIFFERENTIATE AS PHOTORECEPTORS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT ALL STAGES OF EMBRYONIC CC AND LARVAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77518; AAA28324.1; -. DR EMBL; Y12573; CAA73152.1; -. DR EMBL; Y12573; CAA73153.1; -. DR EMBL; AE003831; AAM71061.1; -. DR PIR; JC1122; JC1122. DR HSSP; P29312; 1A38. DR FlyBase; FBgn0004907; 14-3-3-zeta. DR GO; GO:0008426; F:protein kinase C inhibitor activity; NAS. DR GO; GO:0007059; P:chromosome segregation; IMP. DR GO; GO:0007611; P:learning and/or memory; IMP. DR GO; GO:0008355; P:olfactory learning; NAS. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Neurogenesis; Multigene family; Alternative splicing. FT VARSPLIC 149 161 QTAYQDAFDISKG -> KNAYQEAFDIAKT (in FT isoform VI'). FT /FTId=VSP_000001. SQ SEQUENCE 248 AA; 28227 MW; C645CF3B10C6701A CRC64; MSTVDKEELV QKAKLAEQSE RYDDMAQAMK SVTETGVELS NEERNLLSVA YKNVVGARRS SWRVISSIEQ KTEASARKQQ LAREYRERVE KELREICYEV LGLLDKYLIP KASNPESKVF YLKMKGDYYR YLAEVATGDA RNTVVDDSQT AYQDAFDISK GKMQPTHPIR LGLALNFSVF YYEILNSPDK ACQLAKQAFD DAIAELDTLN EDSYKDSTLI MQLLRDNLTL WTSDTQGDEA EPQEGGDN // ID 18C_DROME STANDARD; PRT; 215 AA. AC P16909; Q9VPA8; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone-like protein 18C. GN MST77F OR ANON-77F OR 18C OR CG3354. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89107990; PubMed=3215511; RA Kalderon D., Rubin G.M.; RT "Isolation and characterization of Drosophila cAMP-dependent protein RT kinase genes."; RL Genes Dev. 2:1539-1556(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NOT KNOWN. ENCODED IN THE INTRON OF CAMP-DEPENDENT CC PROTEIN KINASE REGULATORY CHAIN TYPE I. CC -!- DEVELOPMENTAL STAGE: IN PUPAE AND IN ADULTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16962; CAA34836.1; -. DR EMBL; AE003592; AAF51647.1; -. DR FlyBase; FBgn0000093; Mst77F. SQ SEQUENCE 215 AA; 24472 MW; 8199C152FA39ACEF CRC64; MSNLKQKDSK PEVAVTKSVK TYKKSIEYVN SDASDIEEDI NRAEDEYASS SGFVNFLRDF KKRYGEYYSN NEIRRAAETR WNEMSFRHRC QYSAEPLDTF HVEPNSVSSL QRSSEGEHRM HSEISGCADT FFGAGGSNSC TPRKENKCSK PRVRKSCPKP RAKTSKQRRS CGKPKPKGAR PRKACPRPRK KMECGKAKAK PRCLKPKSSK PKCSM // ID 2AAA_DROME STANDARD; PRT; 590 AA. AC P36179; Q9VLN3; DT 01-JUN-1994 (Rel. 29, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein phosphatase PP2A, 65 kDa regulatory subunit (Protein DE phosphatase PP2A regulatory subunit A) (PR65). GN PP2A-29B OR CG17291. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92329996; PubMed=1320961; RA Mayer-Jaekel R.E., Baumgartner S., Bilbe G., Ohkura H., Glover D.M., RA Hemmings B.A.; RT "Molecular cloning and developmental expression of the catalytic and RT 65-kDa regulatory subunits of protein phosphatase 2A in RT Drosophila."; RL Mol. Biol. Cell 3:287-298(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PR65 SUBUNIT OF PROTEIN PHOSPHATASE 2A SERVES AS A CC SCAFFOLDING MOLECULE TO COORDINATE THE ASSEMBLY OF THE CATALYTIC CC SUBUNIT AND A VARIABLE REGULATORY B SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA REGULATORY SUBUNIT (PR65) (SUBUNIT A). THE CORE COMPLEX CC ASSOCIATES WITH A THIRD, VARIABLE SUBUNIT (SUBUNIT B), WHICH CC CONFERS DISTINCT PROPERTIES TO THE HOLOENZYME. CC -!- TISSUE SPECIFICITY: EXPRESSION VARIES IN TISSUES THROUGHOUT CC DEVELOPMENT. IN LATE EMBRYONAL DEVELOPMENT IT IS FOUND AT HIGH CC LEVELS IN SNC AND GONADS; IN THIRD INSTAR LARVAE IT IS FOUND IN CC BRAIN, IMAGINAL DISKS AND SALIVARY GLANDS. CC -!- DEVELOPMENTAL STAGE: MOST ABUNDANT DURING EARLY EMBRYOGENESIS. CC EXPRESSED AT LOWER LEVELS IN LARVAE AND ADULT. CC -!- DOMAIN: EACH HEAT REPEAT APPEARS TO CONSIST OF TWO ALPHA HELICES CC JOINED BY A HYDROPHILIC REGION, THE INTRAREPEAT LOOP. THE REPEAT CC UNITS MAY BE ARRANGED LATERALLY TO FORM A ROD-LIKE STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS 15 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86442; AAA28304.1; -. DR EMBL; AE003621; AAF52651.1; -. DR HSSP; P30153; 1B3U. DR FlyBase; FBgn0005776; Pp2A-29B. DR InterPro; IPR008938; ARM. DR InterPro; IPR000357; HEAT. DR Pfam; PF02985; HEAT; 12. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Repeat; Acetylation. FT INIT_MET 0 0 BY SIMILARITY. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT REPEAT 9 47 HEAT 1. FT REPEAT 48 85 HEAT 2. FT REPEAT 86 124 HEAT 3. FT REPEAT 125 162 HEAT 4. FT REPEAT 163 201 HEAT 5. FT REPEAT 202 240 HEAT 6. FT REPEAT 241 279 HEAT 7. FT REPEAT 280 322 HEAT 8. FT REPEAT 323 361 HEAT 9. FT REPEAT 362 400 HEAT 10. FT REPEAT 401 439 HEAT 11. FT REPEAT 440 478 HEAT 12. FT REPEAT 479 517 HEAT 13. FT REPEAT 518 556 HEAT 14. FT REPEAT 557 590 HEAT 15. FT CONFLICT 232 232 S -> T (IN REF. 1). SQ SEQUENCE 590 AA; 65280 MW; ABE4317F248FA37A CRC64; AASDKSVDDS LYPIAVLIDE LKNEDVQLRL NSIKKLSTIA LALGEERTRS ELIPFLTETI YDEDEVLLAL ADQLGNFTSL VGGPEFAMYL IPPLESLATV EETVVRDKAV ESLRTVAAEH SAQDLEIHVV PTLQRLVSGD WFTSRTSACG LFSVCYPRVT QPVKAELRAN FRKLCQDETP MVRRAAANKL GEFAKVVETE YLKSDLIPNF VQLAQDDQDS VRLLAVEACV TSAQLLPQDD VEHLVLPTLR QCASDSSWRV RYMVAEKFVD LQKAVGPEIT RVDLVPAFQY LLKDAEAEVR AAVATKVKDF CANLDKVNQV QIILSSILPY VRDLVSDPNP HVKSALASVI MGLSPMLGAY QTVEQLLPLF LIQLKDECPE VRLNIISNLD CVNDVIGIQQ LSQSLLPAIV ELAEDSKWRV RLAIIEYMPA LAGQLGQEFF DQKLRGLCMG WLNDHVYAIR EAATLNMKKL VEQFGAPWAE QAIIPMILVM SRNKNYLHRM TCLFCLNVLA EVCGTDITTK LLLPTVLLLA ADPVANVRFN VAKTLQKISP FLEASVIDAQ VKPTLDKLNT DTDVDVKHFA AQAIAGIAAA // ID 2ABA_DROME STANDARD; PRT; 499 AA. AC P36872; Q9VH21; Q9VH22; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein phosphatase PP2A, 55 kDa regulatory subunit (Protein DE phosphatase PP2A regulatory subunit B) (PR55) (Twins protein). GN TWS OR PP2A-85F OR AAR OR CG6235. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=93177843; PubMed=8382567; RA Mayer-Jaekel R.E., Ohkura H., Gomes R., Sunkel C.E., Baumgartner S., RA Hemmings B.A., Glover D.M.; RT "The 55 kd regulatory subunit of Drosophila protein phosphatase 2A is RT required for anaphase."; RL Cell 72:621-633(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Oregon-R; TISSUE=Eye imaginal disk; RX MEDLINE=93194062; PubMed=8383623; RA Uemura T., Shiomi K., Togashi S., Takeichi M.; RT "Mutation of twins encoding a regulator of protein phosphatase 2A RT leads to pattern duplication in Drosophila imaginal discs."; RL Genes Dev. 7:429-440(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COULD PERFORM A SUBSTRATE RECOGNITION FUNCTION OR COULD CC BE RESPONSIBLE FOR TARGETING THE ENZYME COMPLEX TO THE APPROPRIATE CC SUBCELLULAR COMPARTMENT. CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA REGULATORY SUBUNIT (PR65) (SUBUNIT A). THE CORE COMPLEX CC ASSOCIATES WITH A THIRD, VARIABLE SUBUNIT (SUBUNIT B), WHICH CC CONFERS DISTINCT PROPERTIES TO THE HOLOENZYME. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=F; CC IsoId=P36872-1; Sequence=Displayed; CC Name=B; Synonyms=C; CC IsoId=P36872-2; Sequence=VSP_005105, VSP_005106; CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -!- SIMILARITY: CONTAINS 7 WD REPEATS. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1, MET-18, MET-33 OR MET-44 CC IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D13004; BAA02367.1; -. DR EMBL; L07581; AAA99870.1; -. DR EMBL; L07583; AAA99871.1; -. DR EMBL; L07585; -; NOT_ANNOTATED_CDS. DR EMBL; L07586; AAB00371.1; -. DR EMBL; L12544; AAB00371.1; JOINED. DR EMBL; L07586; AAB00372.1; -. DR EMBL; L12544; AAB00372.1; JOINED. DR EMBL; AE003685; AAF54498.1; -. DR EMBL; AE003685; AAF54499.3; -. DR EMBL; AY061152; AAL28700.1; -. DR PIR; A45778; A45778. DR FlyBase; FBgn0004889; tws. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS. DR GO; GO:0008601; F:protein phosphatase type 2A, intrinsic regu...; IMP. DR GO; GO:0007447; P:imaginal disc pattern formation; IMP. DR GO; GO:0000090; P:mitotic anaphase; IMP. DR GO; GO:0006470; P:protein amino acid dephosphorylation; ISS. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase tr...; IMP. DR GO; GO:0007423; P:sensory organ development; IMP. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 2. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat; Alternative splicing. FT REPEAT 79 118 WD 1. FT REPEAT 144 185 WD 2. FT REPEAT 228 266 WD 3. FT REPEAT 277 317 WD 4. FT REPEAT 336 374 WD 5. FT REPEAT 391 432 WD 6. FT REPEAT 467 498 WD 7. FT VARSPLIC 1 56 Missing (in isoform B). FT /FTId=VSP_005105. FT VARSPLIC 57 59 PAS -> MAG (in isoform B). FT /FTId=VSP_005106. FT CONFLICT 211 211 K -> M (IN REF. 1; AAA99871). SQ SEQUENCE 499 AA; 56966 MW; D871A7E3058B7286 CRC64; MGRWGRQSPV LEPPDPQMQT TPPPPTLPPR TFMRQSSITK IGNMLNTAIN INGAKKPASN GEASWCFSQI KGALDDDVTD ADIISCVEFN HDGELLATGD KGGRVVIFQR DPASKAANPR RGEYNVYSTF QSHEPEFDYL KSLEIEEKIN KIRWLQQKNP VHFLLSTNDK TVKLWKVSER DKSFGGYNTK EENGLIRDPQ NVTALRVPSV KQIPLLVEAS PRRTFANAHT YHINSISVNS DQETFLSADD LRINLWHLEV VNQSYNIVDI KPTNMEELTE VITAAEFHPT ECNVFVYSSS KGTIRLCDMR SAALCDRHSK QFEEPENPTN RSFFSEIISS ISDVKLSNSG RYMISRDYLS IKVWDLHMET KPIETYPVHE YLRAKLCSLY ENDCIFDKFE CCWNGKDSSI MTGSYNNFFR VFDRNSKKDV TLEASRDIIK PKTVLKPRKV CTGGKRKKDE ISVDCLDFNK KILHTAWHPE ENIIAVAATN NLFIFQDKF // ID 3BP5_DROME STANDARD; PRT; 476 AA. AC Q9V785; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SH3 domain-binding protein 5-like (Parcase protein). GN PCS OR CG7761. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003812; AAF58174.4; -. DR EMBL; AY058328; AAL13557.1; -. DR FlyBase; FBgn0033988; pcs. DR GO; GO:0005737; C:cytoplasm; ISS. DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; ISS. DR GO; GO:0017124; F:SH3-domain binding; ISS. DR GO; GO:0012501; P:programmed cell death; ISS. DR InterPro; IPR007940; SH3_bind_prot5. DR Pfam; PF05276; SH3BP5; 1. KW Hypothetical protein; SH3-binding. FT CONFLICT 34 34 L -> LE (IN REF. 3). SQ SEQUENCE 476 AA; 53637 MW; E070E9311060B191 CRC64; MSSAEDGELD PQIQIELENL NSATDEINKL EIELEANSTF RILLNESTRR LKVSSKKLGN CIEKARPYYE ALDKAREAQI ECQKAAVKFQ RANEIHAAAK ETVALAEQRF MSNSHEWQFD NAWQEMLNHA TQKVMDAETQ KADCHAEHQR LTKLFNAAEQ KLQQLEDRFR RSINKSRPYF EEKQVCQDQL QTQKNRIQEL QQQVAGAKST YSTALRNLER ISEDIHRQRG DFPTPPGPRE PGVGAELNSP TSSALPSLPD FQLELEKCDY PSIAGSQMSL GAKTPQAAAE TEDEEDACDY DETGAGELRG VVDERDLEAL RQKVKILAVR PIEGGDGQQQ NDVWEHELKA TVDKLDHLMM LKETAKRQQT NRLKSTEQRP DSLGAEALKR HCDVVEVKVT SCATTASLPV TPHHQLNHLA PPTPIKKLQQ QLAPLPSVNV SMRELPLLAR LSNELLDRSS AAFGGVRKTL RRRSLE // ID 3C1_DROME STANDARD; PRT; 210 AA. AC P11450; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-NOV-1990 (Rel. 16, Last annotation update) DE Follicle cell protein 3C-1. GN FCP3C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88055846; PubMed=3119397; RA Burke T., Waring G.L., Popodi E., Minoo P.; RT "Characterization and sequence of follicle cell genes selectively RT expressed during vitelline membrane formation in Drosophila."; RL Dev. Biol. 124:441-450(1987). CC -!- FUNCTION: NOT KNOWN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18281; AAA29016.1; -. DR PIR; B27249; B27249. DR FlyBase; FBgn0000644; Fcp3C. SQ SEQUENCE 210 AA; 22370 MW; BD9B918DA4436C6F CRC64; MSSTGVASSS TTAEEDWPTA VEFVIMTTPA SELEASTETI GNNGTTETTV GEAPIIGSSE GSTRSMEPTT ASPLMSTNPS SSSSLVSTIP LPPTAGLHAQ DNQPVPCTCG VFLSSQIPNG LPTKPLIHQE LDHMFPCNAI GRKQCQTKCL ETIVQHLPNS ANIVCSALGH DCHKERAYLF IKNCHNQWVN TNLQAGREYC CRLGFPTVAH // ID 41_DROME STANDARD; PRT; 1698 AA. AC Q9V8R9; Q24440; Q24441; Q24442; Q9V8R8; Q9V8S0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein 4.1 homolog (Coracle protein). GN CORA OR CG11949. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3), AND FUNCTION. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94215495; PubMed=8162854; RA Fehon R.G., Dawson I.A., Artavanis-Tsakonas S.; RT "A Drosophila homologue of membrane-skeleton protein 4.1 is associated RT with septate junctions and is encoded by the coracle gene."; RL Development 120:545-557(1994). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1; 3 AND 4). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 5). RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: AN INTEGRAL COMPONENT OF THE SEPTATE JUNCTION. MAY PLAY CC A ROLE IN CELL-CELL INTERACTIONS THAT ARE NECESSARY FOR PROPER CC DEVELOPMENT. VITAL FOR EMBRYONIC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: SEPTATE JUNCTION IN THE APICAL-LATERAL CC DOMAIN OF EPITHELIAL CELLS DURING EMBRYONIC AND IMAGINAL DISK CC DEVELOPMENT. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; CC IsoId=Q9V8R9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9V8R9-2; Sequence=VSP_000476, VSP_000477, VSP_000479, CC VSP_000480, VSP_000481; CC Name=3; CC IsoId=Q9V8R9-3; Sequence=VSP_000475, VSP_000478, VSP_000479; CC Name=4; CC IsoId=Q9V8R9-4; Sequence=VSP_000476, VSP_000477, VSP_000479; CC Name=5; CC IsoId=Q9V8R9-5; Sequence=VSP_000474, VSP_000478; CC -!- TISSUE SPECIFICITY: AT ONSET OF GERM BAND RETRACTION, EXPRESSION CC IS SEEN IN EPIDERMIS, HINDGUT AND FOREGUT. DURING RETRACTION, CC EXPRESSION EXTENDS TO TRACHEAL BRANCHES AND SALIVARY GLANDS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED WEAKLY IN 4-8 HOUR EMBRYOS, MORE CC ABUNDANT EXPRESSION IN 8-12 HOURS AND REMAINS THROUGHOUT LATER CC EMBRYONIC AND LARVAL STAGES. CC -!- SIMILARITY: CONTAINS 1 FERM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L27467; AAB59187.1; -. DR EMBL; L27468; AAA28742.1; -. DR EMBL; L27469; AAA28743.1; -. DR EMBL; AE003796; AAF57591.1; -. DR EMBL; AE003796; AAF57592.1; -. DR EMBL; AE003796; AAF57593.1; -. DR EMBL; AY070992; AAL48614.1; -. DR PIR; T13800; T13800. DR FlyBase; FBgn0010434; cora. DR GO; GO:0005918; C:septate junction; IDA. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0009790; P:embryonic development; IMP. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Developmental protein; Membrane; Alternative splicing. FT DOMAIN 32 314 FERM. FT DOMAIN 317 434 HYDROPHILIC. FT DOMAIN 404 449 LYS-RICH. FT DOMAIN 731 775 ALA-RICH. FT DOMAIN 1286 1698 CARBOXYL-TERMINAL (CTD). FT DOMAIN 1437 1643 THR-RICH. FT VARSPLIC 1 312 Missing (in isoform 5). FT /FTId=VSP_000474. FT VARSPLIC 409 409 K -> KLMRQSSTGTASASSQSSLEGDYETNLEIEAIEAEP FT PVQ (in isoform 3). FT /FTId=VSP_000475. FT VARSPLIC 409 409 K -> KSSTGTASASSQSSLEGDYETNLEIEAIEAEPPVQ FT (in isoform 2 and isoform 4). FT /FTId=VSP_000476. FT VARSPLIC 482 1290 Missing (in isoform 2 and isoform 4). FT /FTId=VSP_000477. FT VARSPLIC 482 1480 Missing (in isoform 3 and isoform 5). FT /FTId=VSP_000478. FT VARSPLIC 1554 1587 Missing (in isoform 2, isoform 3 and FT isoform 4). FT /FTId=VSP_000479. FT VARSPLIC 1629 1635 VSSKTRT -> GGGGGGI (in isoform 2). FT /FTId=VSP_000480. FT VARSPLIC 1636 1698 Missing (in isoform 2). FT /FTId=VSP_000481. FT CONFLICT 970 970 I -> V (IN REF. 1; AAB59187). SQ SEQUENCE 1698 AA; 184167 MW; 93940FC4F1ACEB83 CRC64; MPAEIKPSAP AEPETPTKSK PKSSSSSHGK PALARVTLLD GSLLDVSIDR KAIGRDVINS ICAGLNLIEK DYFGLTYETP TDPRTWLDLE KPVSKFFRTD TWPLTFAVKF YPPEPSQLKE DITRYHLCLQ VRNDILEGRL PCTFVTHALL GSYLVQSEMG DYDAEEMPTR AYLKDFKIAP NQTAELEDKV MDLHKTHKGQ SPAEAELHYL ENAKKLAMYG VDLHPAKDSE GVDIMLGVCA SGLLVYRDKL RINRFAWPKI LKISYKRHHF YIKIRPGEFE QYESTIGFKL ANHRAAKKLW KSCVEHHTFF RLMTPEPVSK SKMFPVFGST YRYKGRTQAE STNTPVDRTP PKFNRTLSGA RLTSRSMDAL ALAEKEKVAR KSSTLDHRGD RNADGDAHSR SPIKNKKEKD ADKEAKLREK KQKEKEEKER KEREKRELEE KKKAEKAAKA ALAAGAAAGA AVNGNDELND SNKSDKSSGR RGVGIFSSGR KSKSGSPSKD GKDKSGKDKD KEVGRLGLVV TSGLGDNQQD QNLDEAARNA AKNRGSTTPG VTRQYEYAVD NDGNTSPTRK SYTPGGFRYD QDPNSRKSGA DGQEQLSPTS QQKKIGLAFN YAPGNENALK ETAEKLKAGQ LSPRTQDKLN RGQLSPKSRA KLLQDPLLSP TTRAKLQGSA VDAAAVPLSD SQKRSYSPTK GPQGYSSGAP GSYKPISDPT ADFLESQRYN KEPGYVGPSK ADVAAGLAGA AGSKKPGSPT KTGKGAPGAA AAAAAGAAGA AAAAAKPKKR RVKIMVITSK FDPSTKRIDA ENGSIEHSTG ILDPATGLID TKYGVIDPKK GTLEALNTKT GKKEVFQGDV DGKTGNLHLV SGVADPKTGR LDDTLGQIVC ITPQDNPVVE LTVITSRIDP ATGKIDTVNG DVERSLGVLN LDTGLLDTKY GEINTRTGEL KAIDPKSGKI VVSKNVKVDP GTGQITILGI VDPKTNKIDP NQGRLIEVGQ QIDPIVEVTS LAGKFDSKRN IIDPKTAQVE TSGGQFDPKA GKIDTKYGQI DLVKHTITFN DPKSGKTVTR DIKIEPTTGQ IVLKNQVNPK NNKPDKDYAR IISLRIVQQR VDPATKAPIT EVSASKDKDI VVDPKSNQIW VPTGATDPAT KEQQYISSSV DPKTGYVITI YGYLDPKTNE IKKQTKLDPN TIKIEPTSGK IYTATGEVDQ ATGEPLYAAT QVDPESGEVY TKLARVDPKT GKIVIVRILL ISKTDERGRP EEIDPSTCEI DPVSGRVLKF FNKTVYVYNM IDPVTGEIVQ VDPNDPRFAG ARTTVTHTMT LTGEIDPVTG RIKSEYGDID PNTGDIDPAT AVTDPVTGKL ILNYAQIDPS HFGKQAQVQT TTETVPITRQ QFFDGVKHIS KGALRRDSEG SSDDDMTAQY GADQVNEILI GSPAGQAGGK LGKPVSTPTV VKTTTKQVLT KNIDGVTHNV EEEVRNLGTG EVTYSTQEHK ADATPTDLSG AYVTATAVTT RTATTHEDLG KNAKTEQLEE KTVATTRTHD PNKQQQRVVT QEVKTTATVT SGDQYQRRDS VSSTSSGDSG TPIDGPYDGA SVVRTDNQKS PLFTTSATTG PHVESTRVVL GEDTPGFSGH GEIISTQTVS SKTRTVETIT YKTERDGIVE TRVEQKITIQ SDGDPIDHDK ALAEAIQEAT AMNPDMTVEK IEIQQQTQ // ID 5HT1_DROME STANDARD; PRT; 564 AA. AC P20905; Q9VA21; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 5-hydroxytryptamine receptor 1 (5-HT receptor) (Serotonin receptor). GN 5-HT7 OR 5HT-R1 OR CG12073. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=91062395; PubMed=2174167; RA Witz P., Amlaiky N., Plassat J.-L., Maroteaux L., Borrelli E., Hen R.; RT "Cloning and characterization of a Drosophila serotonin receptor that RT activates adenylate cyclase."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8940-8944(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS IS ONE OF THE SEVERAL DIFFERENT RECEPTORS FOR CC 5-HYDROXYTRYPTAMINE (SEROTONIN), A BIOGENIC HORMONE THAT FUNCTIONS CC AS A NEUROTRANSMITTER, A HORMONE, AND A MITOGEN. THE ACTIVITY OF CC THIS RECEPTOR IS MEDIATED BY G PROTEINS WHICH ACTIVATE ADENYLATE CC CYCLASE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: HEAD. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M55533; AAA28305.1; -. DR EMBL; AE003776; AAF57104.1; -. DR FlyBase; FBgn0004573; 5-HT7. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR007455; Serglycin. DR Pfam; PF00001; 7tm_1; 1. DR Pfam; PF04360; Serglycin; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; Repeat. FT TRANSMEM 29 51 0 (POTENTIAL). FT TRANSMEM 165 188 1 (POTENTIAL). FT DOMAIN 189 198 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 199 222 2 (POTENTIAL). FT DOMAIN 223 236 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 237 258 3 (POTENTIAL). FT DOMAIN 259 278 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 279 302 4 (POTENTIAL). FT DOMAIN 303 330 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 331 353 5 (POTENTIAL). FT DOMAIN 354 454 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 455 476 6 (POTENTIAL). FT DOMAIN 477 487 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 488 510 7 (POTENTIAL). FT DOMAIN 511 564 CYTOPLASMIC (POTENTIAL). FT DOMAIN 89 106 9 X 2 AA TANDEM REPEATS OF G-S. FT DISULFID 235 314 BY SIMILARITY. SQ SEQUENCE 564 AA; 60861 MW; 0C8B9F8DA63D8095 CRC64; MALSGQDWRR HQSHRQHRNH RTQGNHQKLI STATLTLFVL FLSSWIAYAA GKATVPAPLV EGETESATSQ DFNSSSAFLG AIASASSTGS GSGSGSGSGS GSGSGSYGLA SMNSSPIAIV SYQGITSSNL GDSNTTLVPL SDTPLLLEEF AAGEFVLPPL TSIFVSIVLL IVILGTVVGN VLVCIAVCMV RKLRRPCNYL LVSLALSDLC VALLVMPMAL LYEVLEKWNF GPLLCDIWVS FDVLCCTASI LNLCAISVDR YLAITKPLEY GVKRTPRRMM LCVGIVWLAA ACISLPPLLI LGNEHEDEEG QPICTVCQNF AYQIYATLGS FYIPLSVMLF VYYQIFRAAR RIVLEEKRAQ THLQQALNGT GSPSAPQAPP LGHTELASSG NGQRHSSVGN TSLTYSTCGG LSSGGGALAG HGSGGGVSGS TGLLGSPHHK KLRFQLAKEK KASTTLGIIM SAFTVCWLPF FILALIRPFE TMHVPASLSS LFLWLGYANS LLNPIIYATL NRDFRKPFQE ILYFRCSSLN TMMRENYYQD QYGEPPSQRV MLGDERHGAR ESFL // ID 5HTA_DROME STANDARD; PRT; 834 AA. AC P28285; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 5-hydroxytryptamine receptor 2A (5-HT receptor) (Serotonin receptor). GN 5-HT1A OR 5HT-R2A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=92155185; PubMed=1310937; RA Saudou F., Boschert U., Amlaiky N., Plassat J.-L., Hen R.; RT "A family of Drosophila serotonin receptors with distinct RT intracellular signalling properties and expression patterns."; RL EMBO J. 11:7-17(1992). CC -!- FUNCTION: THIS IS ONE OF THE SEVERAL DIFFERENT RECEPTORS FOR CC 5-HYDROXYTRYPTAMINE (SEROTONIN), A BIOGENIC HORMONE THAT FUNCTIONS CC AS A NEUROTRANSMITTER, A HORMONE, AND A MITOGEN. THE ACTIVITY OF CC THIS RECEPTOR IS MEDIATED BY G PROTEINS WHICH INHIBIT ADENYLATE CC CYCLASE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11489; CAA77570.1; -. DR PIR; S19155; S19155. DR HSSP; P29274; 1MMH. DR FlyBase; FBgn0004168; 5-HT1A. DR GO; GO:0007198; P:serotonin receptor, adenylate cyclase inhib...; IDA. DR GO; GO:0007208; P:serotonin receptor, phospholipase C activat...; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein. FT DOMAIN 1 230 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 231 253 1 (POTENTIAL). FT DOMAIN 254 263 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 264 285 2 (POTENTIAL). FT DOMAIN 286 300 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 301 322 3 (POTENTIAL). FT DOMAIN 323 341 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 342 364 4 (POTENTIAL). FT DOMAIN 365 391 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 392 413 5 (POTENTIAL). FT DOMAIN 414 752 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 753 776 6 (POTENTIAL). FT DOMAIN 777 785 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 786 808 7 (POTENTIAL). FT DOMAIN 809 834 CYTOPLASMIC (POTENTIAL). FT DOMAIN 108 136 ALA-RICH. FT DOMAIN 707 723 GLN-RICH. FT CARBOHYD 68 68 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 97 97 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 161 161 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 175 175 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 194 194 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 203 203 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 209 209 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 299 378 BY SIMILARITY. SQ SEQUENCE 834 AA; 89549 MW; 8F39D4B6D6ABD585 CRC64; MAHETSFNDA LDYIYIANSM NDRAFLIAEP HPEQPNVDGQ DQDDAELEEL DDMAVTDDGQ LEDTNNNNNS KRYYSSGKRR ADFIGSLALK PPPTDANTTT TTAGSPLATA ALAAAAASAS VAAAAARITA KAAHWALTTK QDATSSPASS PALQLIDMDN NYTNVAVGLG AMLLNDTLLL EGNDSSLFGE MLANRSGHLD LINGTGGLNV TTSKVAEDDF TQLLRMAVTS VLLGLMILVT IIGNVFVIAA IILERNLQNV ANYLVASLAV ADLFVACLVM PLGAVYEISQ GWILGPELCD IWTSCDVLCC TASILHLVAI AVDRYWAVTN IDYIHSRTSN RVFMMIFCVW TAAVIVSLAP QFGWKDPDYL QRIEQQKCMV SQDVSYQVFA TCCTFYVPLM VILALYWKIY QTARKRIHRR RPRPVDAAVN NNQPDGGAAT DTKLHRLRLR LGRFSTAKSK TGSAVGVSGP ASGGRALGLV DGNSTNTVNT VEDTEFSSSN VDSKSRAGVE APSTSGNQIA TVSHLVALAK QQGKSTAKSS AAVNGMAPSG RQEDDGQRPE HGEQEDREEL EDQDEQVGPQ PTTATSATTA AGTNESEDQC KANGVEVLED PQLQQQLEQV QQLQKSVKSG GGGGASTSNA TTITSISALS PQTPTSQGVG IAAAAAGPMT AKTSTLTSCN QSHPLCGTAN ESPSTPEPRS RQPTTPQQQP HQQAHQQQQQ QQQLSSIANP MQKVNKRKET LEAKRERKAA KTLAIITGAF VVCWLPFFVM ALTMPLCAAC QISDSVASLF LWLGYFNSTL NPVIYTIFSP EFRQAFKRIL FGGHRPVHYR SGKL // ID 5HTB_DROME STANDARD; PRT; 645 AA. AC P28286; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 5-hydroxytryptamine receptor 2B (5-HT receptor) (Serotonin receptor). GN 5-HT1B OR 5HT-R2B. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=92155185; PubMed=1310937; RA Saudou F., Boschert U., Amlaiky N., Plassat J.-L., Hen R.; RT "A family of Drosophila serotonin receptors with distinct RT intracellular signalling properties and expression patterns."; RL EMBO J. 11:7-17(1992). CC -!- FUNCTION: THIS IS ONE OF THE SEVERAL DIFFERENT RECEPTORS FOR CC 5-HYDROXYTRYPTAMINE (SEROTONIN), A BIOGENIC HORMONE THAT FUNCTIONS CC AS A NEUROTRANSMITTER, A HORMONE, AND A MITOGEN. THE ACTIVITY OF CC THIS RECEPTOR IS MEDIATED BY G PROTEINS WHICH INHIBIT ADENYLATE CC CYCLASE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11490; CAA77571.1; -. DR PIR; S19156; S19156. DR HSSP; P29274; 1MMH. DR FlyBase; FBgn0004572; 5-HT1B. DR GO; GO:0007198; P:serotonin receptor, adenylate cyclase inhib...; IDA. DR GO; GO:0007208; P:serotonin receptor, phospholipase C activat...; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein. FT DOMAIN 1 123 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 124 145 1 (POTENTIAL). FT DOMAIN 146 155 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 156 177 2 (POTENTIAL). FT DOMAIN 178 192 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 193 214 3 (POTENTIAL). FT DOMAIN 215 233 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 234 256 4 (POTENTIAL). FT DOMAIN 257 283 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 284 305 5 (POTENTIAL). FT DOMAIN 306 563 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 564 587 6 (POTENTIAL). FT DOMAIN 588 596 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 597 619 7 (POTENTIAL). FT DOMAIN 620 645 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 59 59 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 69 69 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 79 79 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 191 270 BY SIMILARITY. SQ SEQUENCE 645 AA; 71070 MW; 351F3021F786DAFF CRC64; MHTLTRPQPR FIYTEIYSRI YIYIYTSEML KTVTTAMAAG DDDVPASILE IELPAILLNE SLFIELNGNL TQLVDTTSNL SQIVWNRSVN GNGNSNTFDL VDDEQERAAV EFWLLVKMIA MAVVLGLMIL VTIIGNVFVI AAIILERNLQ NVANYLVASL AVADLFVACL VMPLGAVYEI SNGWILGPEL CDIWTSCDVL CCTASILHLV AIAADRYWTV TNIDYNNLRT PRRVFLMIFC VWFAALIVSL APQFGWKDPD YMKRIEEQHC MVSQDVGYQI FATCCTFYVP LLVILFLYWK IYIIARKRIQ RRAQKSFNVT LTETDCDSAV RELKKERSKR RAERKRLEAG ERTPVDGDGM GGQLQRRTRK RMRICFGRNT NTANVVAGSE GAVARSMAAI AVDFASLAIT REETEFSTSN YDNKSHAGTE LTTVSSDADD YRTSNANEII TVSQQVAHAT QHHLIASHLN AITPLAQSIA MGGVGCLTTT TPSEKALSGA GTVAGAVAGG SGSGSGEEGA GTEGKNAGVG LGGVLASIAN PHQKLAKRRQ LLEAKRERKA AQTLAIITGA FVICWLPFFV MALTMSLCKE CEIHTAVASL FLWLGYFNST LNPVIYTIFN PEFRRAFKRI LFGRKAAARA RSAKI // ID 60A_DROME STANDARD; PRT; 455 AA. AC P27091; Q9W1I4; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60A protein precursor (Glass bottom boat protein). GN GBB OR 60A OR TGFB-60A OR CG5562. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92021021; PubMed=1924384; RA Wharton K.A., Thomsen G.H., Gelbart W.M.; RT "Drosophila 60A gene, another transforming growth factor beta family RT member, is closely related to human bone morphogenetic proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9214-9218(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92290120; PubMed=1601181; RA Doctor J.S., Jackson P.D., Rashka K.E., Visalli M., Hoffmann F.M.; RT "Sequence, biochemical characterization, and developmental expression RT of a new member of the TGF-beta superfamily in Drosophila RT melanogaster."; RL Dev. Biol. 151:491-505(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBUNIT: HOMODIMER; DISULFIDE-LINKED. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT WITH PEAKS CC OF TRANSCRIPTION DURING EARLY EMBRYOGENESIS, IN PUPAE, AND IN CC ADULT MALES. CC -!- SIMILARITY: BELONGS TO THE TGF-BETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77012; AAA28306.1; -. DR EMBL; M84795; AAA28307.1; -. DR EMBL; AE003462; AAF47075.1; -. DR PIR; A43918; A43918. DR HSSP; P18075; 1BMP. DR FlyBase; FBgn0024234; gbb. DR GO; GO:0008586; P:wing vein morphogenesis; IMP. DR GO; GO:0007474; P:wing vein specification; IMP. DR InterPro; IPR002400; GF_cysknot. DR InterPro; IPR001839; TGFb. DR InterPro; IPR001111; TGFb_N. DR Pfam; PF00019; TGF-beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR PRINTS; PR00438; GFCYSKNOT. DR ProDom; PD000357; TGFb; 1. DR SMART; SM00204; TGFB; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. KW Growth factor; Cytokine; Glycoprotein; Signal. FT SIGNAL 1 36 POTENTIAL. FT PROPEP 37 335 POTENTIAL. FT CHAIN 336 455 60A PROTEIN. FT DISULFID 354 420 BY SIMILARITY. FT DISULFID 383 452 BY SIMILARITY. FT DISULFID 387 454 BY SIMILARITY. FT DISULFID 419 419 INTERCHAIN (BY SIMILARITY). FT CARBOHYD 238 238 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 250 250 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 396 396 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 455 AA; 51687 MW; C8FA795556341F94 CRC64; MSGLRNTSEA VAVLASLGLG MVLLMFVATT PPAVEATQSG IYIDNGKDQT IMHRVLSEDD KLDVSYEILE FLGIAERPTH LSSHQLSLRK SAPKFLLDVY HRITAEEGLS DQDEDDDYER GHRSRRSADL EEDEGEQQKN FITDLDKRAI DESDIIMTFL NKRHHNVDEL RHEHGRRLWF DVSNVPNDNY LVMAELRIYQ NANEGKWLTA NREFTITVYA IGTGTLGQHT MEPLSSVNTT GDYVGWLELN VTEGLHEWLV KSKDNHGIYI GAHAVNRPDR EVKLDDIGLI HRKVDDEFQP FMIGFFRGPE LIKATAHSSH HRSKRSASHP RKRKKSVSPN NVPLLEPMES TRSCQMQTLY IDFKDLGWHD WIIAPEGYGA FYCSGECNFP LNAHMNATNH AIVQTLVHLL EPKKVPKPCC APTRLGALPV LYHLNDENVN LKKYRNMIVK SCGCH // ID 6PGD_DROME STANDARD; PRT; 481 AA. AC P41572; Q9W519; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN PGD OR EG:87B1.4 OR CG3724. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92112041; PubMed=1765265; RA Scott M.J., Lucchesi J.C.; RT "Structure and expression of the Drosophila melanogaster gene RT encoding 6-phosphogluconate dehydrogenase."; RL Gene 109:177-183(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- CATALYTIC ACTIVITY: 6-PHOSPHO-D-GLUCONATE + NADP(+) = D-RIBULOSE CC 5-PHOSPHATE + CO(2) + NADPH. CC -!- PATHWAY: HEXOSE MONOPHOSPHATE SHUNT. CC -!- SIMILARITY: BELONGS TO THE 6-PHOSPHOGLUCONATE DEHYDROGENASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M80598; AAA28786.1; -. DR EMBL; AE003423; AAF45732.1; -. DR EMBL; Z98269; CAB10974.1; -. DR PIR; JH0531; JH0531. DR HSSP; P00349; 2PGD. DR FlyBase; FBgn0004654; Pgd. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD. DR InterPro; IPR006184; 6PGdom_BS. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; Oxidoreductase; Pentose shunt; NADP. FT CONFLICT 206 206 K -> Q (IN REF. 2). SQ SEQUENCE 481 AA; 52491 MW; 85EB7D97547E81B4 CRC64; MSGQADIALI GLAVMGQNLI LNMDEKGFVV CAYNRTVAKV KEFLANEAKD TKVIGADSLE DMVSKLKSPR KVMLLVKAGS AVDDFIQQLV PLLSAGDVII DGGNSEYQDT SRRCDELAKL GLLFVGSGVS GGEEGARHGP SLMPGGHEAA WPLIQPIFQA ICAKADGEPC CEWVGDGGAG HFVKMVHNGI EYGDMQLICE AYHIMKSLGL SADQMADEFG KWNSAELDSF LIEITRDILK YKDGKGYLLE RIRDTAGQKG TGKWTAIAAL QYGVPVTLIG EAVFSRCLSA LKDERVQASS VLKGPSTKAQ VANLTKFLDD IKHALYCAKI VSYAQGFMLM REAARENKWR LNYGGIALMW RGGCIIRSVF LGNIKDAYTS QPELSNLLLD DFFKKAIERG QDSWREVVAN AFRWGIPVPA LSTALSFYDG YRTAKLPANL LQAQRDYFGA HTYELLGQEG QFHHTNWTGT GGNVSASTYQ A // ID 7LES_DROME STANDARD; PRT; 2554 AA. AC P13368; Q9TYI0; Q9U5V7; Q9VZ36; DT 01-JAN-1990 (Rel. 13, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sevenless protein (EC 2.7.1.112). GN SEV OR HD-265 OR CG18085. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88282538; PubMed=2840202; RA Basler K., Hafen E.; RT "Control of photoreceptor cell fate by the sevenless protein requires RT a functional tyrosine kinase domain."; RL Cell 54:299-311(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=88329706; PubMed=3138161; RA Bowtell D.L.L., Simon M.A., Rubin G.M.; RT "Nucleotide sequence and structure of the sevenless gene of RT Drosophila melanogaster."; RL Genes Dev. 2:620-634(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 2349-2408 FROM N.A. RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). RN [5] RP IDENTIFICATION OF FN-III REPEATS. RX MEDLINE=90199889; PubMed=2317871; RA Norton P.A., Hynes R.O., Ress D.J.G.; RT "Sevenless: seven found?"; RL Cell 61:15-16(1990). CC -!- FUNCTION: RECEPTOR FOR AN EXTRACELLULAR SIGNAL REQUIRED TO CC INSTRUCT A CELL TO DIFFERENTIATE INTO A R7 PHOTORECEPTOR. THE CC LIGAND FOR SEV IS THE BOSS (BRIDE OF SEVENLESS) PROTEIN ON THE CC SURFACE OF THE NEIGHBORING R8 CELL. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBUNIT: MAY FORM A COMPLEX WITH DRK AND SOS. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. INSULIN CC RECEPTOR SUBFAMILY. CC -!- SIMILARITY: CONTAINS 7 FIBRONECTIN TYPE III DOMAINS. CC -!- CAUTION: UNCLEAR WHETHER THE POTENTIAL MEMBRANE SPANNING REGION CC NEAR THE N-TERMINUS IS PRESENT AS A TRANSMEMBRANE DOMAIN IN THE CC NATIVE PROTEIN OR SERVES AS A CLEAVED SIGNAL SEQUENCE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03158; AAA28882.1; -. DR EMBL; X13666; CAA31960.1; ALT_INIT. DR EMBL; X13666; CAB55310.1; -. DR EMBL; AE003484; AAF47992.1; ALT_INIT. DR EMBL; AJ002917; CAA05752.1; -. DR PIR; A28912; TVFF7L. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0003366; sev. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0004713; F:protein-tyrosine kinase activity; IDA. DR GO; GO:0045467; P:R7 development; NAS. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003961; FN_III. DR InterPro; IPR000033; Ldl_receptor_rep. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002011; RecepttyrkinsII. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00041; fn3; 6. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00060; FN3; 6. DR SMART; SM00135; LY; 2. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Tyrosine-protein kinase; Receptor; Vision; Transmembrane; KW Glycoprotein; ATP-binding; Phosphorylation; Repeat. FT DOMAIN 1 2123 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2124 2147 POTENTIAL. FT DOMAIN 2148 2554 CYTOPLASMIC (POTENTIAL). FT DOMAIN 311 431 FIBRONECTIN TYPE-III 1. FT DOMAIN 436 528 FIBRONECTIN TYPE-III 2. FT DOMAIN 822 921 FIBRONECTIN TYPE-III 3. FT DOMAIN 1298 1392 FIBRONECTIN TYPE-III 4. FT DOMAIN 1680 1794 FIBRONECTIN TYPE-III 5. FT DOMAIN 1797 1897 FIBRONECTIN TYPE-III 6. FT DOMAIN 1898 1988 FIBRONECTIN TYPE-III 7. FT DOMAIN 2038 2046 POLY-ARG. FT DOMAIN 2209 2485 PROTEIN KINASE. FT NP_BIND 2215 2223 ATP (BY SIMILARITY). FT BINDING 2242 2242 ATP (BY SIMILARITY). FT MOD_RES 2380 2380 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT CARBOHYD 30 30 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 129 129 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 481 481 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 505 505 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 617 617 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 647 647 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 966 966 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1228 1228 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1313 1313 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1353 1353 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1550 1550 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1557 1557 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1639 1639 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1725 1725 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1756 1756 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1804 1804 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1889 1889 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1947 1947 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2073 2073 N-LINKED (GLCNAC...) (POTENTIAL). FT MUTAGEN 2242 2242 K->M: INACTIVATES THE PROTEIN. FT CONFLICT 392 392 V -> M (IN REF. 1). FT CONFLICT 663 663 A -> T (IN REF. 3). FT CONFLICT 1703 1703 N -> H (IN REF. 3). FT CONFLICT 1730 1731 RG -> KE (IN REF. 3). FT CONFLICT 1741 1741 V -> M (IN REF. 3). FT CONFLICT 1823 1823 E -> Q (IN REF. 2). FT CONFLICT 2271 2271 C -> R (IN REF. 1). SQ SEQUENCE 2554 AA; 287022 MW; 09E238A0F27684F8 CRC64; MTMFWQQNVD HQSDEQDKQA KGAAPTKRLN ISFNVKIAVN VNTKMTTTHI NQQAPGTSSS SSNSQNASPS KIVVRQQSSS FDLRQQLARL GRQLASGQDG HGGISTILII NLLLLILLSI CCDVCRSHNY TVHQSPEPVS KDQMRLLRPK LDSDVVEKVA IWHKHAAAAP PSIVEGIAIS SRPQSTMAHH PDDRDRDRDP SEEQHGVDER MVLERVTRDC VQRCIVEEDL FLDEFGIQCE KADNGEKCYK TRCTKGCAQW YRALKELESC QEACLSLQFY PYDMPCIGAC EMAQRDYWHL QRLAISHLVE RTQPQLERAP RADGQSTPLT IRWAMHFPEH YLASRPFNIQ YQFVDHHGEE LDLEQEDQDA SGETGSSAWF NLADYDCDEY YVCEILEALI PYTQYRFRFE LPFGENRDEV LYSPATPAYQ TPPEGAPISA PVIEHLMGLD DSHLAVHWHP GRFTNGPIEG YRLRLSSSEG NATSEQLVPA GRGSYIFSQL QAGTNYTLAL SMINKQGEGP VAKGFVQTHS ARNEKPAKDL TESVLLVGRR AVMWQSLEPA GENSMIYQSQ EELADIAWSK REQQLWLLNV HGELRSLKFE SGQMVSPAQQ LKLDLGNISS GRWVPRRLSF DWLHHRLYFA MESPERNQSS FQIISTDLLG ESAQKVGESF DLPVEQLEVD ALNGWIFWRN EESLWRQDLH GRMIHRLLRI RQPGWFLVQP QHFIIHLMLP QEGKFLEISY DGGFKHPLPL PPPSNGAGNG PASSHWQSFA LLGRSLLLPD SGQLILVEQQ GQAASPSASW PLKNLPDCWA VILLVPESQP LTSAGGKPHS LKALLGAQAA KISWKEPERN PYQSADAARS WSYELEVLDV ASQSAFSIRN IRGPIFGLQR LQPDNLYQLR VRAINVDGEP GEWTEPLAAR TWPLGPHRLR WASRQGSVIH TNELGEGLEV QQEQLERLPG PMTMVNESVG YYVTGDGLLH CINLVHSQWG CPISEPLQHV GSVTYDWRGG RVYWTDLARN CVVRMDPWSG SRELLPVFEA NFLALDPRQG HLYYATSSQL SRHGSTPDEA VTYYRVNGLE GSIASFVLDT QQDQLFWLVK GSGALRLYRA PLTAGGDSLQ MIQQIKGVFQ AVPDSLQLLR PLGALLWLER SGRRARLVRL AAPLDVMELP TPDQASPASA LQLLDPQPLP PRDEGVIPMT VLPDSVRLDD GHWDDFHVRW QPSTSGGNHS VSYRLLLEFG QRLQTLDLST PFARLTQLPQ AQLQLKISIT PRTAWRSGDT TRVQLTTPPV APSQPRRLRV FVERLATALQ EANVSAVLRW DAPEQGQEAP MQALEYHISC WVGSELHEEL RLNQSALEAR VEHLQPDQTY HFQVEARVAA TGAAAGAASH ALHVAPEVQA VPRVLYANAE FIGELDLDTR NRRRLVHTAS PVEHLVGIEG EQRLLWVNEH VELLTHVPGS APAKLARMRA EVLALAVDWI QRIVYWAELD ATAPQAAIIY RLDLCNFEGK ILQGERVWST PRGRLLKDLV ALPQAQSLIW LEYEQGSPRN GSLRGRNLTD GSELEWATVQ PLIRLHAGSL EPGSETLNLV DNQGKLCVYD VARQLCTASA LRAQLNLLGE DSIAGQLAQD SGYLYAVKNW SIRAYGRRRQ QLEYTVELEP EEVRLLQAHN YQAYPPKNCL LLPSSGGSLL KATDCEEQRC LLNLPMITAS EDCPLPIPGV RYQLNLTLAR GPGSEEHDHG VEPLGQWLLG AGESLNLTDL LPFTRYRVSG ILSSFYQKKL ALPTLVLAPL ELLTASATPS PPRNFSVRVL SPRELEVSWL PPEQLRSESV YYTLHWQQEL DGENVQDRRE WEAHERRLET AGTHRLTGIK PGSGYSLWVQ AHATPTKSNS SERLHVRSFA ELPELQLLEL GPYSLSLTWA GTPDPLGSLQ LECRSSAEQL RRNVAGNHTK MVVEPLQPRT RYQCRLLLGY AATPGAPLYH GTAEVYETLG DAPSQPGKPQ LEHIAEEVFR VTWTAARGNG APIALYNLEA LQARSDIRRR RRRRRRNSGG SLEQLPWAEE PVVVEDQWLD FCNTTELSCI VKSLHSSRLL LFRVRARSLE HGWGPYSEES ERVAEPFVSP EKRGSLVLAI IAPAAIVSSC VLALVLVRKV QKRRLRAKKL LQQSRPSIWS NLSTLQTQQQ LMAVRNRAFS TTLSDADIAL LPQINWSQLK LLRFLGSGAF GEVYEGQLKT EDSEEPQRVA IKSLRKGASE FAELLQEAQL MSNFKHENIV CLVGICFDTE SISLIMEHME AGDLLSYLRA ARATSTQEPQ PTAGLSLSEL LAMCIDVANG CSYLEDMHFV HRDLACRNCL VTESTGSTDR RRTVKIGDFG LARDIYKSDY YRKEGEGLLP VRWMSPESLV DGLFTTQSDV WAFGVLCWEI LTLGQQPYAA RNNFEVLAHV KEGGRLQQPP MCTEKLYSLL LLCWRTDPWE RPSFRRCYNT LHAISTDLRR TQMASATADT VVSCSRPEFK VRFDGQPLEE HREHNERPED ENLTLREVPL KDKQLYANEG VSRL // ID 7UP1_DROME STANDARD; PRT; 543 AA. AC P16375; Q9VGB0; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Steroid receptor seven-up type 1. GN SVP OR NR2F3 OR CG11502. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90124631; PubMed=2105166; RA Mlodzik M., Hiromi Y., Weber U., Goodman C.S., Rubin G.M.; RT "The Drosophila seven-up gene, a member of the steroid receptor gene RT superfamily, controls photoreceptor cell fates."; RL Cell 60:211-224(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PUTATIVE RECEPTOR THAT IS REQUIRED IN PHOTORECEPTOR CC CELLS PRECURSORS DURING EYE DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Type 1; CC IsoId=P16375-1; Sequence=Displayed; CC Name=Type 2; CC IsoId=P16376-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN A SUBSET OF NEURAL PRECURSORS. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR2 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28863; AAA62770.1; -. DR EMBL; AE003695; AAF54773.1; -. DR PIR; A32693; A32693. DR HSSP; P19793; 2NLL. DR TRANSFAC; T02741; -. DR FlyBase; FBgn0003651; svp. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR GO; GO:0007510; P:cardioblast cell fate determination; IEP. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Vision; Alternative splicing. FT DNA_BIND 200 265 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 200 220 C4-TYPE. FT ZN_FING 236 260 C4-TYPE. SQ SEQUENCE 543 AA; 57987 MW; 0BC189DCF1A27213 CRC64; MCASPSTAPG FFNPRPQSGA ELSAFDIGLS RSMGLGVPPH SAWHEPPASL GGHLHAASAG PGTTTGSVAT GGGGTTPSSV ASQQSAVIKQ DLSCPSLNQA GSGHHPGIKE DLSSSLPSAN GGSAGGHHSG SGSGSGSGVN PGHGSDMLPL IKGHGQDMLT SIKGQPTGCG STTPSSQANS SHSQSSNSGS QIDSKQNIEC VVCGDKSSGK HYGQFTCEGC KSFFKRSVRR NLTYSCRGSR NCPIDQHHRN QCQYCRLKKC LKMGMRREAV QRGRVPPTQP GLAGMHGQYQ IANGDPMGIA GFNGHSYLSS YISLLLRAEP YPTSRYGQCM QPNNIMGIDN ICELAARLLF SAVEWAKNIP FFPELQVTDQ VALLRLVWSE LFVLNASQCS MPLHVAPLLA AAGLHASPMA ADRVVAFMDH IRIFQEQVEK LKALHVDSAE YSCLKAIVLF TTDACGLSDV THIESLQEKS QCALEEYCRT QYPNQPTRFG KLLLRLPSLR TVSSQVIEQL FFVRLVGKTP IETLIRDMLL SGNSFSWPYL PSM // ID 7UP2_DROME STANDARD; PRT; 746 AA. AC P16376; DT 01-AUG-1990 (Rel. 15, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Steroid receptor seven-up type 2. GN SVP OR NR2F3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90124631; PubMed=2105166; RA Mlodzik M., Hiromi Y., Weber U., Goodman C.S., Rubin G.M.; RT "The Drosophila seven-up gene, a member of the steroid receptor gene RT superfamily, controls photoreceptor cell fates."; RL Cell 60:211-224(1990). CC -!- FUNCTION: PUTATIVE RECEPTOR THAT IS REQUIRED IN PHOTORECEPTOR CC CELLS PRECURSORS DURING EYE DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Type 2; CC IsoId=P16376-1; Sequence=Displayed; CC Name=Type 1; CC IsoId=P16375-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN A SUBSET OF NEURAL PRECURSORS. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR2 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28864; AAA03014.1; -. DR PIR; B32693; B32693. DR HSSP; P19793; 2NLL. DR FlyBase; FBgn0003651; svp. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR GO; GO:0007510; P:cardioblast cell fate determination; IEP. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Vision; Alternative splicing. FT DNA_BIND 200 265 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 200 220 C4-TYPE. FT ZN_FING 236 260 C4-TYPE. SQ SEQUENCE 746 AA; 76830 MW; 7F256AFD4165326D CRC64; MCASPSTAPG FFNPRPQSGA ELSAFDIGLS RSMGLGVPPH SAWHEPPASL GGHLHAASAG PGTTTGSVAT GGGGTTPSSV ASQQSAVIKQ DLSCPSLNQA GSGHHPGIKE DLSSSLPSAN GGSAGGHHSG SGSGSGSGVN PGHGSDMLPL IKGHGQDMLT SIKGQPTGCG STTPSSQANS SHSQSSNSGS QIDSKQNIEC VVCGDKSSGK HYGQFTCEGC KSFFKRSVRR NLTYSCRGSR NCPIDQHHRN QCQYCRLKKC LKMGMRREAV QRGRVPPTQP GLAGMHGQYQ IANGDPMGIA GFNGHSYLSS YISLLLRAEP YPTSRYGQCM QPNNIMGIDN ICELAARLLF SAVEWAKNIP FFPELQVTDQ VALLRLVWSE LFVLNASQCS MPLHVAPLLA AAGLHASPMA ADRVVAFMDH IRIFQEQVEK LKALHVDSAE YSCLKAIVLF TTGKLLDILY KDVPALLTKV SALLGKGSTA SNDDVLAVVR DHLDELNRQE QESQAQQQAP LHLAAFMNCV AGVEAAVQQA EQAQVPTSSA SASVSSPLVP SAGSAFSSCQ AKSAGSEMDL LASLYAQAQA TPPSSGGGDA SGHNNSSGLG ASLPTQSQSG SSSRNLTASP LSTSLATAPA PASASAPAPV PTSSVAQVPV PAPVPVTSSA SSSSLGGGAY QTPSAAAAAA AMFHYQTPPR AAFGSAFDMF HHSTPFGVGV GHAHALAHSS GSGSASFGSP SYRYSPYSLA GSRWQL // ID A29B_DROME STANDARD; PRT; 234 AA. AC O46197; Q9TVT3; Q9TW05; Q9TW06; Q9TW07; Q9U976; Q9U977; Q9U978; AC Q9U979; Q9V3Q5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland protein Acp29AB precursor. GN ACP29AB OR CG17797. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=LA1, LA3, LA4, LA5, LA6, LA9, LA14, LA14, LA15, LA16, LA21, RC LA25, LA34, LA35, M01B, M02B, M08B, M015B, M034A, M036A, M037A, RC M040B, M047A, M052B, M058B, M080B, MA5, MA7, MA8, MA13, MA18, MA20, RC MA21, MA43, MA45, MA48, MA50, MA52, and MA67; RX MEDLINE=99282496; PubMed=10353898; RA Aguade M.; RT "Positive selection drives the evolution of the Acp29AB accessory RT gland protein in Drosophila."; RL Genetics 152:543-551(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=WS1, WS6, WS9, WS12, WS19, WS26, WS47, WS56, ZIM2, ZIM26, RC ZIM29, ZIM30, ZIM32, ZIM37, ZIM42, and ZIM56; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RESPONSIBLE FOR PHYSIOLOGICAL AND BEHAVIORAL CHANGES IN CC MATED FEMALE FLIES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: MAIN CELLS OF THE ACCESSORY GLAND AND IN CC SEMINAL FLUID. CC -!- SIMILARITY: CONTAINS 1 C-TYPE LECTIN FAMILY DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85758; AAB96382.1; -. DR EMBL; AJ240513; CAB53187.1; -. DR EMBL; AJ240514; CAB53188.1; -. DR EMBL; AJ240515; CAB53189.1; -. DR EMBL; AJ240516; CAB53190.1; -. DR EMBL; AJ240517; CAB53191.1; -. DR EMBL; AJ240518; CAB53192.1; -. DR EMBL; AJ240519; CAB53193.1; -. DR EMBL; AJ240520; CAB53194.1; -. DR EMBL; AJ240521; CAB53195.1; -. DR EMBL; AJ240522; CAB53196.1; -. DR EMBL; AJ240523; CAB53197.1; -. DR EMBL; AJ240524; CAB53198.1; -. DR EMBL; AJ240525; CAB53199.1; -. DR EMBL; AJ240526; CAB53200.1; -. DR EMBL; AJ240527; CAB53201.1; -. DR EMBL; AJ240528; CAB53202.1; -. DR EMBL; AJ240529; CAB53203.1; -. DR EMBL; AJ240530; CAB53204.1; -. DR EMBL; AJ240531; CAB53205.1; -. DR EMBL; AJ240532; CAB53206.1; -. DR EMBL; AJ240533; CAB53207.1; -. DR EMBL; AJ240534; CAB53208.1; -. DR EMBL; AJ240535; CAB53209.1; -. DR EMBL; AJ240536; CAB53210.1; -. DR EMBL; AJ240537; CAB53211.1; -. DR EMBL; AJ240538; CAB53212.1; -. DR EMBL; AJ240539; CAB53213.1; -. DR EMBL; AJ240540; CAB53214.1; -. DR EMBL; AJ240541; CAB53215.1; -. DR EMBL; AJ240542; CAB53216.1; -. DR EMBL; AJ240543; CAB53217.1; -. DR EMBL; AJ240544; CAB53218.1; -. DR EMBL; AJ240545; CAB53219.1; -. DR EMBL; AJ240546; CAB53220.1; -. DR EMBL; AJ240547; CAB53221.1; -. DR EMBL; AJ240548; CAB53222.1; -. DR EMBL; AJ240549; CAB53223.1; -. DR EMBL; AJ240550; CAB53224.1; -. DR EMBL; AJ240551; CAB53225.1; -. DR EMBL; AY010527; AAG32559.1; -. DR EMBL; AY010528; AAG32560.1; -. DR EMBL; AY010529; AAG32561.1; -. DR EMBL; AY010530; AAG32562.1; -. DR EMBL; AY010531; AAG32563.1; -. DR EMBL; AY010532; AAG32564.1; -. DR EMBL; AY010533; AAG32565.1; -. DR EMBL; AY010534; AAG32566.1; -. DR EMBL; AY010535; AAG32567.1; -. DR EMBL; AY010536; AAG32568.1; -. DR EMBL; AY010537; AAG32569.1; -. DR EMBL; AY010538; AAG32570.1; -. DR EMBL; AY010539; AAG32571.1; -. DR EMBL; AY010540; AAG32572.1; -. DR EMBL; AY010541; AAG32573.1; -. DR EMBL; AY010542; AAG32574.1; -. DR EMBL; AY010543; AAG32575.1; -. DR EMBL; AE003621; AAF52665.1; -. DR FlyBase; FBgn0015583; Acp29AB. DR GO; GO:0007321; P:sperm displacement; NAS. DR InterPro; IPR001304; Lectin_C. DR Pfam; PF00059; lectin_c; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; FALSE_NEG. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. KW Behavior; Lectin; Signal; Polymorphism. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 234 ACCESSORY GLAND PROTEIN ACP29AB. FT DOMAIN 137 228 C-TYPE LECTIN (LONG FORM). FT CARBOHYD 61 61 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 164 164 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 29 29 K -> N (IN STRAINS MA7, WS16 AND WS26). FT VARIANT 59 59 K -> R (IN STRAINS LA1, LA3, LA4, LA5, FT LA14, LA15, LA16, LA21, LA25, LA34, LA35, FT M01B, M052B, M080B, MA5, MA8, MA13, MA18, FT MA20, MA21, MA45, MA48, MA52, MA67, FT ZIM26, ZIM29, ZIM30, ZIM56, WS6 AND FT WS19). FT VARIANT 105 105 A -> S (IN STRAINS LA16 AND LA35). FT VARIANT 113 113 R -> L (IN STRAINS LA14, LA14, LA16, FT LA35, M02B, M015B, M034A, M036A, M037A, FT M047A, M052B, M058B, M080B, MA5, MA7, FT MA13, MA18, MA20, MA21, MA45, MA48, MA50, FT MA52, MA67, WS1, WS6, WS9, WS12, WS16, FT WS26, WS47, WS56, ZIM2, ZIM26, ZIM29, FT ZIM30, ZIM32, ZIM37, ZIM42 AND ZIM56). FT VARIANT 153 153 K -> M (IN STRAINS BERKELEY, LA13, LA14, FT LA15, LA16, M01B, M08B, M040B, M052B, FT MA5, MA21, MA45, MA52, MA67, ZIM29, FT ZIM30, ZIM42 AND ZIM56). FT VARIANT 214 214 E -> D (IN STRAIN MA7). SQ SEQUENCE 234 AA; 27173 MW; 8954CD3215480F3E CRC64; MYASNLLYLL ALWNLWDLSG GQQDIPNGKA TLPSPQTPQN TIDQIGINQN YWFTYNALKQ NETLAIIDTM EMRIASSLLE FKAQMEIQLQ PLKIIMRHHA SNIKASNNIK MRRFEKVGSR HFHIEKNLMQ TWFEAYVTCR KMNGHLANIQ DEKELDGILA LAPNNSYWID ISKLVENGGT FVSTLTGREP FFVKWKSNQD TKKKNQCVYI YAKEMSYDEC FEKKSFVCQA DQWA // ID A32C_DROME STANDARD; PRT; 329 AA. AC O46203; O46225; Q8T4D3; Q9TY45; Q9VKL2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland protein Acp32CD precursor. GN ACP32CD OR CG4605. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 24-289 FROM N.A. RC STRAIN=WS1, WS9, WS12, WS16, WS17, WS19, WS26, WS47, ZIM5, ZIM10, RC ZIM22, ZIM24, ZIM30, ZIM32, and ZIM35; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). CC -!- FUNCTION: RESPONSIBLE FOR PHYSIOLOGICAL AND BEHAVIORAL CHANGES IN CC MATED FEMALE FLIES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; CC Comment=2 isoforms, Long (shown here) and Short, are produced by CC alternative initiation; CC -!- TISSUE SPECIFICITY: SEMINAL FLUID. CC -!- CAUTION: REF.3 AND REF.4 SEQUENCES DIFFER FROM THAT SHOWN DUE TO CC FRAMESHIFTS. THESE MAY BE A NATURAL FRAMESHIFTS AND THIS PROTEIN CC COULD BE A PSEUDOGENE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85764; AAB96388.1; -. DR EMBL; U85764; AAB96389.1; -. DR EMBL; U90948; AAB96395.1; -. DR EMBL; AE003630; AAF53055.2; ALT_FRAME. DR EMBL; AY089245; AAL89983.1; ALT_FRAME. DR EMBL; AY010544; AAG32576.1; -. DR EMBL; AY010545; AAG32577.2; -. DR EMBL; AY010546; AAG32578.1; -. DR EMBL; AY010547; AAG32579.1; -. DR EMBL; AY010548; AAG32580.1; -. DR EMBL; AY010549; AAG32581.2; -. DR EMBL; AY010550; AAG32582.1; -. DR EMBL; AY010551; AAG32583.1; -. DR EMBL; AY010552; AAG32584.1; -. DR EMBL; AY010553; AAG32585.1; -. DR EMBL; AY010554; AAG32586.1; -. DR EMBL; AY010555; AAG32587.1; -. DR EMBL; AY010556; AAG32588.1; -. DR EMBL; AY010557; AAG32589.1; -. DR EMBL; AY010558; AAG32590.1; -. DR EMBL; AY010559; AAG32591.1; -. DR FlyBase; FBgn0023415; Acp32CD. DR GO; GO:0005576; C:extracellular; TAS. DR GO; GO:0005179; F:hormone activity; NAS. DR GO; GO:0045434; P:negative regulation of female receptivity, ...; NAS. KW Alternative initiation; Signal; Behavior; Polymorphism. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 329 ACCESSORY GLAND PROTEIN ACP32CD, ISOFORM FT LONG. FT CHAIN 89 329 ACCESSORY GLAND PROTEIN ACP32CD, ISOFORM FT SHORT. FT INIT_MET 89 89 FOR ISOFORM SHORT. FT DOMAIN 100 182 GLY-RICH. FT DOMAIN 200 326 ARG-RICH. FT VARIANT 45 45 D -> E (IN STRAINS WS1, WS9, WS16, ZIM5, FT ZIM10, ZIM24, ZIM30, ZIM32 AND FT ZIM35). FT VARIANT 52 52 A -> D (IN STRAINS 7, WS1, WS12, WS16, FT WS17, ZIM10, ZIM22, ZIM32 AND FT ZIM35). FT VARIANT 63 63 A -> T (IN STRAINS 7, WS1, WS9, WS16, FT WS17 AND ZIM10). FT VARIANT 69 69 L -> P (IN STRAINS WS9 AND WS19). FT VARIANT 273 275 TRM -> PRT (IN STRAINS WS9, ZIM30 AND FT ZIM22). FT VARIANT 275 275 M -> T (IN STRAINS WS12, WS17 AND FT WS26). SQ SEQUENCE 329 AA; 35557 MW; 5655CCA73759CFEA CRC64; MPPLLRHCFG HAFIGLPLFN GQEQPRPQSN RFDSGQRRSS LYIRDGRTAR AAQRCSDVAD ADAATHWLLG PVALGQLPEH GALGQKYYMN FAFNNNNPDG EGGTGVDGGG GGAGGGAAGP GGGTGDSPHS QEGDGSAATD NPNDDHATSA DNSLATDGDA IGKKESGGGS DGKSDSKDSS GGNDATPANG HDDDNDDSDR RMPRIDKIRK RRPDRRGSAP ITAITVATRS DRRQLWRAVR AVHLREQREP RTFGSNAGSN QRTMEPVRAV RRTRMPRKWP AKRLLNGQAT CQMDPKLEPR KMTTRRCNTT GRSDHRFARG TLEERRHFN // ID A36D_DROME STANDARD; PRT; 912 AA. AC Q9V3R1; O46198; Q9U9Y5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland protein Acp36DE precursor. GN ACP36DE OR CG7157. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP REVISIONS TO N-TERMINUS AND C-TERMINUS. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 144-889 FROM N.A. RC STRAIN=SENGWA2, SENGWA22, SENGWA29, SENGWA30, SENGWA32, SENGWA37, RC SENGWA51, WSII1, WSII6, WSII9, WSII12, WSII16, WSII19, WSII26, WSII47, RC and WSII49; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). RN [6] RP SEQUENCE OF 401-912 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: RESPONSIBLE FOR PHYSIOLOGICAL AND BEHAVIORAL CHANGES IN CC MATED FEMALE FLIES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: MAIN CELLS OF ACCESSORY GLAND AND SEMINAL CC FLUID. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85759; AAB96383.2; -. DR EMBL; AF157488; AAD40185.1; -. DR EMBL; AE003658; AAF53664.1; -. DR EMBL; AY113344; AAM29349.1; -. DR EMBL; AY010577; AAG37359.1; -. DR EMBL; AY010578; AAG37360.1; -. DR EMBL; AY010579; AAG37361.1; -. DR EMBL; AY010580; AAG37362.1; -. DR EMBL; AY010581; AAG37363.1; -. DR EMBL; AY010582; AAG37364.1; -. DR EMBL; AY010583; AAG37365.1; -. DR EMBL; AY010584; AAG37366.1; -. DR EMBL; AY010585; AAG37367.1; -. DR EMBL; AY010586; AAG37368.1; -. DR EMBL; AY010587; AAG37369.1; -. DR EMBL; AY010588; AAG37370.1; -. DR EMBL; AY010589; AAG37371.1; -. DR EMBL; AY010590; AAG37372.1; -. DR EMBL; AY010591; AAG37373.1; -. DR EMBL; AY010592; AAG37374.1; -. DR EMBL; AF145666; AAD38641.1; -. DR FlyBase; FBgn0011559; Acp36DE. DR GO; GO:0005576; C:extracellular; TAS. DR GO; GO:0005179; F:hormone activity; NAS. DR GO; GO:0045434; P:negative regulation of female receptivity, ...; NAS. KW Signal; Behavior; Polymorphism. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 912 ACCESSORY GLAND PROTEIN ACP36DE. FT DOMAIN 183 897 GLN/SER-RICH. FT VARIANT 148 148 N -> S (IN STRAIN WSII16). FT VARIANT 190 190 A -> V (IN STRAIN WSII16). FT VARIANT 198 198 T -> S (IN STRAINS SENGWA2, SENGWA22, FT SENGWA29, SENGWA32, SENGWA37, SENGWA51, FT WSII19 AND WSII49). FT VARIANT 223 223 MISSING (IN STRAIN SENGWA22). FT VARIANT 231 231 E -> G (IN STRAIN WSII6). FT VARIANT 253 253 Q -> QSQ (IN STRAINS SENGWA2, SENGWA29, FT SENGWA32, SENGWA51, WSII19 AND FT WSII49). FT VARIANT 307 307 E -> G (IN STRAIN WSII6). FT VARIANT 316 316 I -> F (IN STRAIN WSII16). FT VARIANT 325 325 K -> T (IN STRAIN SENGWA37). FT VARIANT 335 335 S -> P (IN STRAIN SENGWA30). FT VARIANT 352 352 Q -> QLLREAQQK (IN STRAINS SENGWA2, FT SENGWA22, SENGWA29, SENGWA30, SENGWA32, FT SENGWA37, SENGWA51, WSII16, WSII19 AND FT WSII49). FT VARIANT 385 385 F -> HQN (IN STRAIN WSII1). FT VARIANT 430 430 V -> I (IN STRAIN WSII16). FT VARIANT 464 464 L -> F (IN STRAINS CANTON-S, SENGWA2, FT SENGWA22, SENGWA29, SENGWA32 AND FT SENGWA51). FT VARIANT 496 496 E -> G (IN STRAIN WSII6). FT VARIANT 507 507 L -> V (IN STRAINS SENGWA22, SENGWA29, FT SENGWA37 AND SENGWA51). FT VARIANT 575 575 L -> Q (IN STRAIN WSII16). FT VARIANT 601 601 S -> I (IN STRAINS WSII26 AND FT WSII49). FT VARIANT 613 613 E -> K (IN STRAIN SENGWA30). FT VARIANT 650 650 P -> A (IN STRAINS SENGWA22, SENGWA30 AND FT WSII16). FT VARIANT 666 666 L -> V (IN STRAINS SENGWA29, SENGWA30, FT SENGWA37 AND SENGWA51). FT VARIANT 670 670 G -> E (IN STRAINS SENGWA29, SENGWA30, FT SENGWA37 AND SENGWA51). FT VARIANT 758 758 T -> A (IN STRAINS SENGWA37 AND FT SENGWA51). FT VARIANT 782 786 MISSING (IN STRAINS SENGWA37 AND FT SENGWA51). FT VARIANT 830 830 Q -> E (IN STRAIN WSII26). FT VARIANT 844 844 Q -> R (IN STRAIN WSII16). SQ SEQUENCE 912 AA; 101921 MW; 81E2C53431EAFBC5 CRC64; MWTLTCQQFI ALILLGTLVP SESFLCKHCF RKNLEKVHES FRDILSPPIF GVNPQPLIEV QQPKVTPKPE SSQVIHVHQP QVILKPIYYP KVDTISTKNQ IGIHGPYSQY PSLLPSANLL GIPNQQLINA QDVLSDKDQK QTQVQNNNLH IRFGVSALRE GRNNPSLETI SRDKVDKISP ALQLQLLRYA DSQSQSQTQS QSASQSESNA SSQFQAQEQS NRLLENPPVS ESQSQSESQS QSESQKQSQS QSQRQQQIQT QLQILRQLQQ KSNEQSAAQS ASQIQSQRQS DSQSNLQLQE QSQSQSEQGK PIQSQIQILQ GLQQKELDDK SASQSQSESK TRQEQQKQLN LQQLEELSSS LSQSRLGLGQ QIQSQLQKNQ LDKQFASQFQ SQSKSQLEQQ MQLQLQSLRQ LQQKQLDEQS ASQSQPQSQV AQQIQSHLQL LRLLQSRLKT QSALKSDLEQ QILLQLKKLT EVQQKQLAEQ PTLRPSSKSQ SPGQLEQQIL LQLQNLLQFQ QNQLKSDTQT QSQLQESKSN SLSQSQSQSQ EQLQLQRDQN LRQLEQIKLE MQNIRELLQK GKSELQTQSD SQRRIHELYQ NILQLNKEKL SYQLKQLKLK ELEDQKKSQA EISKGSNPSN LFIIGQLPSE GKPAPGNQGP SIEPKLVPQP GSLDKLPSGG GLIGKPASTG LYILSPDFND LSDYRDQFRL QQELKKHQNI LSLLQRRQND IKKQQNAQLL LGQQQKEQQA QESINKQQSS SAGSSSQTKL QQDIQSTGAQ GSQQGLQAGS TGLQTSSLQG TESSASQSAA LQRLKEQEQL RIQTENDQKT SSSSSHSNSQ NSQSSSSQSS QASQSEAQRQ EAGNRNTLLL DQSSSKTQSE SKSESSSQSS SHSSSQSTSN SSSNVQSKLQ GESQALLNNL SG // ID A4_DROME STANDARD; PRT; 887 AA. AC P14599; Q9TVV0; Q9U4H3; Q9W5F1; DT 01-APR-1990 (Rel. 14, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Beta-amyloid-like protein precursor. GN APPL OR VND OR BCDNA:GH04413 OR EG:65F1.5 OR CG7727. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89184650; PubMed=2494667; RA Rosen D.R., Martin-Morris L., Luo L., White K.; RT "A Drosophila gene encoding a protein resembling the human RT beta-amyloid protein precursor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:2478-2482(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [6] RP SEQUENCE OF 1-83 FROM N.A. RX MEDLINE=91184006; PubMed=2127912; RA Martin-Morris L.E., White K.; RT "The Drosophila transcript encoded by the beta-amyloid protein RT precursor-like gene is restricted to the nervous system."; RL Development 110:185-195(1990). CC -!- FUNCTION: PROBABLY CORRESPONDS TO THE PROTEIN ENCODED BY THE CC ESSENTIAL LOCUS VND, A GENE REQUIRED FOR EMBRYONIC NERVOUS SYSTEM CC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED IN POST-MITOTIC NEURONS IN THE CC CENTRAL AND PERIPHERAL NERVOUS SYSTEMS. WITHIN THE NERVOUS SYSTEM CC TRANSCRIPTS ARE NOT OBSERVED IN NEUROBLASTS, NEWLY GENERATED CC NEURONS AND AT LEAST ONE CLASS OF PRESUMED GLIAL CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN ALL DEVELOPMENTAL STAGES. CC -!- DOMAIN: THE CLATHRIN-BINDING SITE IS ESSENTIAL FOR ITS ASSOCIATION CC WITH X11-ALPHA, -BETA, AND -GAMMA. THE SEQUENCE SPECIFIC CC RECOGNITION EXTENDS TO PEPTIDE RESIDUES THAT ARE C-TERMINAL TO THE CC NPXY MOTIF. THIS INTERACTION APPEARS TO BE INDEPENDENT OF CC PHOSPHORYLATION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE APP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04516; AAA28874.1; -. DR EMBL; AE003418; AAF45520.2; -. DR EMBL; AL031883; CAA21409.1; -. DR EMBL; AL022139; CAA21409.1; JOINED. DR EMBL; AL022139; CAA18093.1; -. DR EMBL; AL031883; CAA18093.1; JOINED. DR EMBL; AF181628; AAD55414.1; -. DR EMBL; X55774; CAA39294.1; -. DR EMBL; X55775; CAA39294.1; JOINED. DR PIR; A32758; A32758. DR HSSP; P05067; 1MWP. DR FlyBase; FBgn0000108; Appl. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR InterPro; IPR008155; A4_APP. DR InterPro; IPR008154; A4_extra. DR Pfam; PF02177; A4_EXTRA; 1. DR SMART; SM00006; A4_EXTRA; 1. DR PROSITE; PS00319; A4_EXTRA; 1. DR PROSITE; PS00320; A4_INTRA; 1. KW Signal; Transmembrane; Amyloid; Neurogenesis. FT SIGNAL 1 27 POTENTIAL. FT CHAIN 28 887 BETA-AMYLOID-LIKE PROTEIN. FT DOMAIN 28 813 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 814 834 POTENTIAL. FT DOMAIN 835 887 CYTOPLASMIC (POTENTIAL). FT DOMAIN 877 880 CLATHRIN-BINDING (POTENTIAL). FT CARBOHYD 150 150 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 161 161 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 237 237 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 240 240 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 574 574 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 177 177 S -> T (IN REF. 1). FT CONFLICT 229 229 MISSING (IN REF. 1). FT CONFLICT 332 332 V -> M (IN REF. 4). FT CONFLICT 743 743 S -> T (IN REF. 1). SQ SEQUENCE 887 AA; 98332 MW; F0F0855AD65A5275 CRC64; MCAALRRNLL LRSLWVVLAI GTAQVQAASP RWEPQIAVLC EAGQIYQPQY LSEEGRWVTD LSKKTTGPTC LRDKMDLLDY CKKAYPNRDI TNIVESSHYQ KIGGWCRQGA LNAAKCKGSH RWIKPFRCLG PFQSDALLVP EGCLFDHIHN ASRCWPFVRW NQTGAAACQE RGMQMRSFAM LLPCGISVFS GVEFVCCPKH FKTDEIHVKK TDLPVMPAAQ INSANDELVM NDEDDSNDSN YSKDANEDDL DDEDDLMGDD EEDDMVADEA ATAGGSPNTG SSGDSNSGSL DDINAEYDSG EEGDNYEEDG AGSESEAEVE ASWDQSGGAK VVSLKSDSSS PSSAPVAPAP EKAPVKSESV TSTPQLSASA AAFVAANSGN SGTGAGAPPS TAQPTSDPYF THFDPHYEHQ SYKVSQKRLE ESHREKVTRV MKDWSDLEEK YQDMRLADPK AAQSFKQRMT ARFQTSVQAL EEEGNAEKHQ LAAMHQQRVL AHINQRKREA MTCYTQALTE QPPNAHHVEK CLQKLLRALH KDRAHALAHY RHLLNSGGPG GLEAAASERP RTLERLIDID RAVNQSMTML KRYPELSAKI AQLMNDYILA LRSKDDIPGS SLGMSEEAEA GILDKYRVEI ERKVAEKERL RLAEKQRKEQ RAAEREKLRE EKLRLEAKKV DDMLKSQVAE QQSQPTQSST QSQAQQQQQE KSLPGKELGP DAALVTAANP NLETTKSEKD LSDTEYGEAT VSSTKVQTVL PTVDDDAVQR AVEDVAAAVA HQEAEPQVQH FMTHDLGHRE SSFSLRREFA QHAHAAKEGR NVYFTLSFAG IALMAAVFVG VAVAKWRTSR SPHAQGFIEV DQNVTTHHPI VREEKIVPNM QINGYENPTY KYFEVKE // ID A53E_DROME STANDARD; PRT; 120 AA. AC O46199; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland protein Acp53Ea precursor. GN ACP53EA OR CG8622. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=WS1, WS6, WS9, WS12, WS16, WS19, WS26, WS47, WS49, WS56, ZIM2, RC ZIM26, ZIM30, ZIM42, and ZIM56; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RESPONSIBLE FOR PHYSIOLOGICAL AND BEHAVIORAL CHANGES IN CC MATED FEMALE FLIES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: MAIN CELLS OF ACCESSORY GLAND AND SEMINAL CC FLUID. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85760; AAB96384.1; -. DR EMBL; AY010593; AAG37375.1; -. DR EMBL; AY010594; AAG37376.1; -. DR EMBL; AY010595; AAG37377.1; -. DR EMBL; AY010596; AAG37378.1; -. DR EMBL; AY010597; AAG37379.1; -. DR EMBL; AY010598; AAG37380.1; -. DR EMBL; AY010599; AAG37381.1; -. DR EMBL; AY010600; AAG37382.1; -. DR EMBL; AY010601; AAG37383.1; -. DR EMBL; AY010602; AAG37384.1; -. DR EMBL; AY010603; AAG37385.1; -. DR EMBL; AY010604; AAG37386.1; -. DR EMBL; AY010605; AAG37387.1; -. DR EMBL; AY010606; AAG37388.1; -. DR EMBL; AY010607; AAG37389.1; -. DR EMBL; AE003805; AAF57959.1; -. DR FlyBase; FBgn0015584; Acp53Ea. KW Behavior; Signal; Polymorphism. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 120 ACCESSORY GLAND PROTEIN ACP53EA. FT VARIANT 7 7 T -> A (IN STRAIN ZIM56). FT VARIANT 22 22 E -> K (IN STRAINS ZIM26 AND ZIM42). FT VARIANT 27 27 I -> V (IN STRAIN ZIM56). FT VARIANT 70 70 N -> K (IN STRAIN WS9). FT VARIANT 83 83 V -> D (IN STRAIN ZIM30). FT VARIANT 108 108 Y -> C (IN STRAIN ZIM2). SQ SEQUENCE 120 AA; 13607 MW; C576B846B4DC2871 CRC64; MKLIKVTLVF SLLALVFVAQ TEAQNPIWEN WLACNRIGTK ALASLLRETI PTVRNLLNCI DFNPPTDIGN SYLSKLKLYY ELVKRGALDK TQCLIVPLKE SVRLLRPYVK SLETNKCLGE // ID A62F_DROME STANDARD; PRT; 115 AA. AC O46202; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland protein Acp62F precursor. GN ACP62F OR CG1262. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 7-111 FROM N.A. RC STRAIN=ZIM62H-12C, ZIM62H-16C, ZIM62H-28C, ZIM62H-30C, ZIM62H-34C, RC ZIM62I-5C, ZIM62I-10C, ZIM62I-17C, ZIM62I-18C, and ZIM62I-53C; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). CC -!- FUNCTION: RESPONSIBLE FOR PHYSIOLOGICAL AND BEHAVIORAL CHANGES IN CC MATED FEMALE FLIES. MAY CONTRIBUTE TO THE TOXICITY OF SEMINAL CC FLUID AND THE DECREASED LIFE-SPAN OF MATED FEMALES. MAY ALSO CC AFFECT NEUROMUSCULAR EVENTS AFTER MATING CONCERNING SPERM STORAGE CC AND EGG RELEASE. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: SEMINAL FLUID. CC -!- SIMILARITY: SOME, TO P.NIGRIVENTER TX2-6. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85763; AAB96387.1; -. DR EMBL; AE003475; AAF47683.1; -. DR EMBL; AY010608; AAG35367.1; -. DR EMBL; AY010609; AAG35368.1; -. DR EMBL; AY010610; AAG35369.1; -. DR EMBL; AY010611; AAG35370.1; -. DR EMBL; AY010612; AAG35371.1; -. DR EMBL; AY010613; AAG35372.1; -. DR EMBL; AY010614; AAG35373.1; -. DR EMBL; AY010615; AAG35374.1; -. DR EMBL; AY010616; AAG35375.1; -. DR EMBL; AY010617; AAG35376.1; -. DR FlyBase; FBgn0020509; Acp62F. DR GO; GO:0004867; F:serine protease inhibitor activity; IDA. DR GO; GO:0008340; P:determination of adult life span; NAS. DR InterPro; IPR002919; TIL_Cysrich. DR Pfam; PF01826; TIL; 1. KW Behavior; Signal. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 115 ACCESSORY GLAND PROTEIN ACP62F. FT DOMAIN 34 88 TIL. SQ SEQUENCE 115 AA; 12570 MW; 4326AA6F6C32291D CRC64; MTDMWSLKIC ACLGLLLLFK PIDSMGWQGP KVDCTANGTQ TECPVACPET CEYSGNGPCV KMCGAPCVCK PGYVINERIP ACVLRSDCPK DVVRKEDMLL GVSNFKCFSR NYNCS // ID A63F_DROME STANDARD; PRT; 81 AA. AC O46200; Q9VZM3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland protein Acp63F precursor. GN ACP63F OR CG10852. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ZIM63H-12C, ZIM63H-16C, ZIM63H-28C, ZIM63H-30C, ZIM63H-34C, RC ZIM63I-7C, ZIM63I-10C, ZIM63I-18C, and ZIM63I-53C; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RESPONSIBLE FOR PHYSIOLOGICAL AND BEHAVIORAL CHANGES IN CC MATED FEMALE FLIES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: MAIN CELLS OF ACCESSORY GLAND AND SEMINAL CC FLUID. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85761; AAB96385.1; -. DR EMBL; AY010618; AAG37390.1; -. DR EMBL; AY010619; AAG37391.1; -. DR EMBL; AY010620; AAG37392.1; -. DR EMBL; AY010621; AAG37393.1; -. DR EMBL; AY010622; AAG37394.1; -. DR EMBL; AY010623; AAG37395.1; -. DR EMBL; AY010624; AAG37396.1; -. DR EMBL; AY010625; AAG37397.1; -. DR EMBL; AY010626; AAG37398.1; -. DR EMBL; AE003479; AAF47797.1; ALT_SEQ. DR FlyBase; FBgn0015585; Acp63F. KW Behavior; Signal; Polymorphism. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 81 ACCESSORY GLAND PROTEIN ACP63F. FT VARIANT 49 49 N -> K (IN STRAINS BERKELEY AND ZIM63H- FT 30C). FT VARIANT 72 72 L -> V (IN STRAINS ZIM63H-16C, ZIM63H-34C FT AND ZIM63I-7C). FT VARIANT 73 73 H -> Q (IN STRAINS ZIM63H-16C AND ZIM63H- FT 34C). FT VARIANT 73 74 HG -> MA (IN STRAIN ZIM63H-30C). FT VARIANT 75 75 K -> E (IN STRAIN ZIM63H-16C). FT VARIANT 76 76 P -> T (IN STRAIN ZIM63I-7C). SQ SEQUENCE 81 AA; 8969 MW; 0B54787311BA285B CRC64; MKAIIVFILF ISSVHAMSKC NQAIYLNLDP HCGILPDCNL DGPNPSYLNR VSCERKENGK PGFIELIPGK CLHGKPRCSL K // ID A6_DROME STANDARD; PRT; 409 AA. AC O46341; Q9W564; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE A6 protein. GN A6 OR EG:9D2.3 OR CG3771. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-RC; TISSUE=Larva; RX MEDLINE=20013434; PubMed=10546111; RA Makunin I.V., Shestopal S.A., Beliaeva E.S., Ashburner M., RA Khimulev I.F.; RT "Comparison of the molecular and genetic map of the 2B6-2B7-8 of RT Drosophila melanogaster X-chromosome."; RL Genetika 35:1071-1077(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYOGENESIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y16065; CAA76017.1; -. DR EMBL; Y16066; CAA76018.1; -. DR EMBL; AL031025; CAA19836.1; -. DR EMBL; AE003421; AAF45661.2; -. DR EMBL; AY069426; AAL39571.1; -. DR FlyBase; FBgn0023130; a6. DR GO; GO:0001700; P:embryonic development (sensu Insecta); IEP. SQ SEQUENCE 409 AA; 44077 MW; 46FA1A9F93D391AB CRC64; MNQKHSEPFY ISPRLFDNRR LKRRRCRWME RLLEHQRICM ARMRDQVALA SKTDRQLSHL QRRHVASTLQ PDVTIDLLSD DDETPSAGQP AAAGHNRLLI PAPGHRAHRT GRRQAPRRAA THSYPVTDSI LITSDDEHNE QEPSSTARVR SQLSMRSPPP LAPLTQSETI EEVTVSLVPR TSTTANCLTR VSGHPKPCRA STAASNGFAT AEGGEGGNET GCFLEVDVGG GITATLPDET TVHTVIANRI YELSLSKLRE GLAFSGVPEY TNDLMPEQLQ KLSPALRAKV APLVAPSPPT PISLKLSSDL SISLISDEDD CESTGPHVNG GVGTEPVHPV VVAAAEAHAA AKLLKQQQPQ LSVVQHLQYV GGGLAAPVAL ALPVMAANPT SSASVVALPL QLPRRRKLG // ID A70A_DROME STANDARD; PRT; 55 AA. AC P05623; O18659; Q9VU54; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland-specific peptide 70A precursor (Paragonial peptide B). GN ACP70A OR PAPB OR CG17673. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 20-55. RC STRAIN=Oregon-R; RX MEDLINE=88282537; PubMed=3135120; RA Chen P.S., Stumm-Zollinger E., Aigaki T., Balmer J., Bienz M., RA Boehlen P.; RT "A male accessory gland peptide that regulates reproductive behavior RT of female D. melanogaster."; RL Cell 54:291-298(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=M2, M11, M26, M36, M40, M47, M54, M55, and M66; RX MEDLINE=97432799; PubMed=9286679; RA Cirera S., Aguade M.N.; RT "Evolutionary history of the sex-peptide (Acp70A) gene region in RT Drosophila melanogaster."; RL Genetics 147:189-197(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REPRESSES FEMALE SEXUAL RECEPTIVITY AND STIMULATES CC OVIPOSITION. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: MAIN CELLS OF THE ACCESSORY GLANDS OF MALES CC (PARAGONIAL GLAND). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M21201; AAA28816.1; -. DR EMBL; X99407; CAA67784.1; -. DR EMBL; X99408; CAA67785.1; -. DR EMBL; X99409; CAA67786.1; -. DR EMBL; X99410; CAA67787.1; -. DR EMBL; X99411; CAA67788.1; -. DR EMBL; X99413; CAA67790.1; -. DR EMBL; X99415; CAA67792.1; -. DR EMBL; X99416; CAA67793.1; -. DR EMBL; X99418; CAA67795.1; -. DR EMBL; AE003538; AAF49836.1; -. DR PIR; A28911; A28911. DR FlyBase; FBgn0003034; Acp70A. DR GO; GO:0005179; F:hormone activity; NAS. KW Behavior; Hydroxylation; Polymorphism; Signal. FT SIGNAL 1 19 FT CHAIN 20 55 ACCESSORY GLAND-SPECIFIC PEPTIDE 70A. FT MOD_RES 28 28 HYDROXYLATION. FT MOD_RES 32 32 HYDROXYLATION. FT MOD_RES 33 33 CHEMICAL NATURE NOT DETERMINED. FT MOD_RES 34 34 HYDROXYLATION. FT MOD_RES 38 38 HYDROXYLATION. FT VARIANT 19 19 S -> A (IN STRAINS M2, M26, M36, M40, FT M55 AND BERKELEY). SQ SEQUENCE 55 AA; 6378 MW; F6827A1F025BF23D CRC64; MKTLALFLVL VCVLGLVQSW EWPWNRKPTK FPIPSPNPRD KWCRLNLGPA WGGRC // ID A76A_DROME STANDARD; PRT; 386 AA. AC Q9VVW1; O46224; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland protein Acp76A precursor. GN ACP76A OR CG3801. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 22-386 FROM N.A. RC STRAIN=ZIM5, ZIM7C, ZIM10C, ZIM12C, ZIM16C, ZIM18C, ZIM28C, ZIM30C, RC and ZIM53C; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). CC -!- FUNCTION: RESPONSIBLE FOR PHYSIOLOGICAL AND BEHAVIORAL CHANGES IN CC MATED FEMALE FLIES. MAY PLAY A ROLE IN ACCESSORY PROTEIN CC REGULATION AND/OR IN THE COAGULATION OF SEMINAL FLUID TO FORM A CC MATING PLUG. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: MAIN CELLS OF ACCESSORY GLAND AND SEMINAL CC FLUID. CC -!- SIMILARITY: BELONGS TO THE SERPIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U90947; AAB96393.1; -. DR EMBL; AE003518; AAF49196.1; -. DR EMBL; AY010627; AAG38149.1; -. DR EMBL; AY010628; AAG38150.1; -. DR EMBL; AY010629; AAG38151.1; -. DR EMBL; AY010630; AAG38152.1; -. DR EMBL; AY010631; AAG38153.1; -. DR EMBL; AY010632; AAG38154.1; -. DR EMBL; AY010633; AAG38155.1; -. DR EMBL; AY010634; AAG38156.1; -. DR EMBL; AY010635; AAG38157.1; -. DR EMBL; AY010636; AAG38158.1; -. DR FlyBase; FBgn0015586; Acp76A. DR InterPro; IPR000215; Serpin. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Serpin; Serine protease inhibitor; Glycoprotein; Signal; Behavior; KW Polymorphism. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 386 ACCESSORY GLAND PROTEIN ACP76A. FT ACT_SITE 339 340 REACTIVE BOND (BY SIMILARITY). FT CARBOHYD 24 24 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 378 378 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 22 22 Q -> P (IN STRAINS ZIM7C AND FT ZIM12C). FT VARIANT 22 22 Q -> H (IN STRAINS ZIM5C, ZIM10C, ZIM16C, FT ZIM18C, ZIM28C, ZIM30C, ZIM34C AND FT ZIM53C). FT VARIANT 332 337 EVVDDI -> GKRNTR (IN STRAIN FT ZIM28C). FT VARIANT 338 338 D -> N (IN STRAINS CANTON-S AND FT ZIM34C). FT VARIANT 359 359 I -> V (IN STRAINS CANTON-S, ZIM12C AND FT ZIM16C). FT VARIANT 381 381 K -> M (IN STRAINS ZIM5C AND FT ZIM16C). FT CONFLICT 7 7 I -> T (IN REF. 1). FT CONFLICT 64 65 NN -> TI (IN REF. 3). FT CONFLICT 91 91 Y -> S (IN REF. 3). FT CONFLICT 141 141 K -> T (IN REF. 3). FT CONFLICT 145 145 E -> A (IN REF. 3). FT CONFLICT 165 167 NAG -> YAA (IN REF. 3). FT CONFLICT 172 172 A -> S (IN REF. 3). FT CONFLICT 182 182 W -> C (IN REF. 3). FT CONFLICT 191 191 N -> I (IN REF. 3). FT CONFLICT 202 202 Y -> H (IN REF. 3). FT CONFLICT 238 238 N -> Y (IN REF. 3). SQ SEQUENCE 386 AA; 43966 MW; D2640A616B3F0FC8 CRC64; MGNHQVIFLV LCTSLLFQNT IQQNVSFQLI REIDRYTPEN FVLSVLNIEM ILFEIHAAKA VESNNDLERS LIINFGYSEA RQEVLDWGLR YKKASSAKFQ MANKVAVSQK LPLSQKLRLV NEVLMTSAKK YDVTKDVRPS KLMDEWLSSH LDGVLANFVQ EKKLNAGENI VAISGMTVTP LWASHFQSEI NRYFVNNPGT GYASKDPTCV PMMHSLSSFE TMSTDEAKGI YIPFSSANLG MLILLPRKGV TCKDILDNLN NQINVEYNDH KDVHLLLPIF KEKFDYNIAK FFNGINIEDT FKDSAFKSKA KIKINNFRVN HGIRFQPILR LEVVDDIDTG KTETFEVNRP FVFVIKDKIN VYAVGRIENL DGLTDKVNCS KKYADL // ID A95E_DROME STANDARD; PRT; 52 AA. AC P16548; Q9VCB0; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland-specific peptide 95EF precursor (Male accessory gland DE secretory protein 316). GN ACP95EF OR MST95E OR MSP316 OR CG17924. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90228604; PubMed=2109712; RA Dibenedetto A.J., Harada H.A., Wolfner M.F.; RT "Structure, cell-specific expression, and mating-induced regulation RT of a Drosophila melanogaster male accessory gland gene."; RL Dev. Biol. 139:134-148(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS PROTEIN MAY BE A PRECURSOR OF SECRETED PROTEINS CC AND PEPTIDE HORMONES. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: MAIN CELLS OF THE ACCESSORY GLANDS OF MALES. CC -!- DEVELOPMENTAL STAGE: IN VERY LATE PUPAE AND IN ADULTS. CC -!- INDUCTION: BY MATING. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32022; AAD13400.1; -. DR EMBL; AE003746; AAF56263.2; -. DR PIR; A37354; A37354. DR FlyBase; FBgn0002863; Acp95EF. KW Behavior; Hormone; Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 52 ACCESSORY GLAND-SPECIFIC PEPTIDE 95EF. FT CONFLICT 20 20 T -> S (IN REF. 1). SQ SEQUENCE 52 AA; 5405 MW; A44008BD6057FF2B CRC64; MASVKLFFIA ILVVALSLNT SAAVLNPSST AKPRFETKDR KLSAGALQSL AG // ID A98A_DROME STANDARD; PRT; 31 AA. AC O46201; O46226; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland protein Acp98AB precursor. GN ACP98AB OR CG31056. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP SEQUENCE OF 3-31 FROM N.A. RC STRAIN=ZIM5C, ZIM7C, ZIM10C, ZIM12C, ZIM16C, ZIM18C, ZIM28C, ZIM30C, RC ZIM34C, and ZIM53C; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). RN [3] RP SEQUENCE OF 5-31 FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RESPONSIBLE FOR PHYSIOLOGICAL AND BEHAVIORAL CHANGES IN CC MATED FEMALE FLIES. CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85762; AAB96386.1; -. DR EMBL; U90949; AAB96396.1; -. DR EMBL; AY010637; AAG38159.1; -. DR EMBL; AY010638; AAG38160.1; -. DR EMBL; AY010639; AAG38161.1; -. DR EMBL; AY010640; AAG38162.1; -. DR EMBL; AY010641; AAG38163.1; -. DR EMBL; AY010642; AAG38164.1; -. DR EMBL; AY010643; AAG38165.1; -. DR EMBL; AY010644; AAG38166.1; -. DR EMBL; AY010645; AAG38167.1; -. DR EMBL; AY010646; AAG38168.1; -. DR EMBL; AE003762; AAN14125.1; -. DR FlyBase; FBgn0013745; Acp98AB. DR GO; GO:0005576; C:extracellular; TAS. DR GO; GO:0005179; F:hormone activity; NAS. DR GO; GO:0045434; P:negative regulation of female receptivity, ...; NAS. KW Behavior; Signal. FT SIGNAL 1 14 POTENTIAL. FT CHAIN 15 31 ACCESSORY GLAND PROTEIN ACP98AB. SQ SEQUENCE 31 AA; 3693 MW; 67ACC9087ECC4D0D CRC64; MEFPNPVLSR IGRSLRTNKG THYQRMTRMS K // ID AACT_DROME STANDARD; PRT; 924 AA. AC P18091; O46044; O46045; Q24370; Q8T024; Q9W536; Q9W537; DT 01-NOV-1990 (Rel. 16, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-actinin, sarcomeric (F-actin cross linking protein). GN ACTN OR FLIA OR L(1)2CB OR EG.133E12.1 OR CG4376. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM ADULT MUSCLE). RC STRAIN=Canton-S; RX MEDLINE=90277718; PubMed=2112549; RA Fyrberg E.A., Kelly M., Ball E., Fyrberg C., Reedy M.C.; RT "Molecular genetics of Drosophila alpha-actinin: mutant alleles RT disrupt Z disc integrity and muscle insertions."; RL J. Cell Biol. 110:1999-2011(1990). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND ADULT MUSCLE). RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 229-286 FROM N.A. (ISOFORM NON-MUSCLE), AND ALTERNATIVE RP SPLICING. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=92129435; PubMed=1734023; RA Roulier E.M., Fyrberg C., Fyrberg E.; RT "Perturbations of Drosophila alpha-actinin cause muscle paralysis, RT weakness, and atrophy but do not confer obvious nonmuscle RT phenotypes."; RL J. Cell Biol. 116:911-922(1992). CC -!- FUNCTION: F-ACTIN CROSS-LINKING PROTEIN WHICH IS THOUGHT TO ANCHOR CC ACTIN TO A VARIETY OF INTRACELLULAR STRUCTURES. THIS IS A BUNDLING CC PROTEIN. CC -!- SUBUNIT: HOMODIMER, ANTIPARALLEL. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=Long; CC IsoId=P18091-1; Sequence=Displayed; CC Name=Non-muscle; CC IsoId=P18091-2; Sequence=VSP_000712, VSP_000714; CC Name=Larval muscle; Synonyms=C; CC IsoId=P18091-3; Sequence=VSP_000716; CC Name=Adult muscle; Synonyms=B; CC IsoId=P18091-4; Sequence=VSP_000715; CC Name=A; CC IsoId=P18091-5; Sequence=VSP_000713; CC -!- TISSUE SPECIFICITY: LARVAL MUSCLE ISOFORM IS EXPRESSED IN THE CC LARVAL BODY WALL, ADULT MUSCLES OF THE HEAD AND ABDOMEN AND CC SUPERCONTRACTILE MUSCLES OF THE LARVA AND ADULT. ADULT MUSCLE CC ISOFORM ACCUMULATES WITHIN ADULT FIBRILLAR AND TUBULAR MUSCLES. CC -!- DEVELOPMENTAL STAGE: LARVAL MUSCLE ISOFORM IS FOUND IN THE LARVAE CC AND ADULTS, THE ADULT MUSCLE ISOFORM IN ADULTS ONLY. CC -!- SIMILARITY: CONTAINS 1 ACTIN-BINDING DOMAIN. CC -!- SIMILARITY: CONTAINS 2 CALPONIN-HOMOLOGY (CH) DOMAINS. CC -!- SIMILARITY: CONTAINS 2 EF-HAND CALCIUM-BINDING DOMAINS. CC -!- SIMILARITY: CONTAINS 4 SPECTRIN REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51753; CAA36042.1; -. DR EMBL; AL009192; CAA15688.1; -. DR EMBL; AL031765; CAA15688.1; JOINED. DR EMBL; AL009192; CAA15689.1; -. DR EMBL; AL031765; CAA15689.1; JOINED. DR EMBL; AL031765; CAA21120.1; -. DR EMBL; AL009192; CAA21120.1; JOINED. DR EMBL; AL031765; CAA21121.1; -. DR EMBL; AL009192; CAA21121.1; JOINED. DR EMBL; AE003422; AAF45705.2; -. DR EMBL; AE003422; AAF45706.2; -. DR EMBL; AE003422; AAN09068.1; -. DR EMBL; AY069615; AAL39760.1; -. DR EMBL; X64419; CAA45764.1; -. DR PIR; T13413; T13413. DR PIR; T13414; T13414. DR HSSP; Q01082; 1BKR. DR FlyBase; FBgn0000667; Actn. DR InterPro; IPR001589; Actbind_actnin. DR InterPro; IPR001715; Calponin-like. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR002017; Spectrin. DR Pfam; PF00307; CH; 3. DR Pfam; PF00036; efhand; 2. DR Pfam; PF00435; spectrin; 4. DR ProDom; PD000012; EF-hand; 1. DR SMART; SM00033; CH; 2. DR SMART; SM00054; EFh; 2. DR SMART; SM00150; SPEC; 4. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS00018; EF_HAND; 1. KW Actin-binding; Calcium-binding; Repeat; Alternative splicing. FT DOMAIN 1 250 ACTIN-BINDING. FT DOMAIN 34 138 CH 1. FT DOMAIN 147 250 CH 2. FT REPEAT 251 395 SPECTRIN 1. FT REPEAT 396 510 SPECTRIN 2. FT REPEAT 511 631 SPECTRIN 3. FT REPEAT 632 744 SPECTRIN 4. FT CA_BIND 791 802 EF-HAND 1 (BY SIMILARITY). FT CA_BIND 832 843 EF-HAND 2 (BY SIMILARITY). FT VARSPLIC 229 260 Missing (in isoform Non-muscle). FT /FTId=VSP_000712. FT VARSPLIC 231 260 INTPKPDERAIMTYVSCYYHAFQGAQQVGN -> Q (in FT isoform A). FT /FTId=VSP_000713. FT VARSPLIC 261 261 N -> Q (in isoform Non-muscle). FT /FTId=VSP_000714. FT VARSPLIC 258 286 Missing (in isoform Adult muscle). FT /FTId=VSP_000715. FT VARSPLIC 261 286 NTALPDERAVMTYVSSYYHCFSGAQK -> VTHVPEPTRQY FT TYVPNNYN (in isoform Larval muscle). FT /FTId=VSP_000716. FT CONFLICT 409 409 A -> G (IN REF. 1). FT CONFLICT 457 457 C -> Y (IN REF. 1). FT CONFLICT 474 474 S -> C (IN REF. 1). FT CONFLICT 503 503 S -> C (IN REF. 1). FT CONFLICT 574 574 E -> V (IN REF. 1). FT CONFLICT 654 654 L -> R (IN REF. 1). FT CONFLICT 684 691 AVTAIGMG -> VVTPLVWD (IN REF. 1). FT CONFLICT 711 711 Y -> H (IN REF. 1). FT CONFLICT 817 817 D -> E (IN REF. 1). SQ SEQUENCE 924 AA; 107019 MW; 08F8961520328ACE CRC64; MMMENGLSME YGDGYMEQEE EWEREGLLDP AWEKQQKKTF TAWCNSHLRK AGTAIDNIEE DFRNGLKLML LLEVISGETL PKPDRGKMRF HKIANVNKAL DFIASKGVHL VSIGAEEIVD GNLKMTLGMI WTIILRFAIQ DISVEEMTAK EGLLLWCQRK TAPYKNVNVQ NFHLSFKDGL AFCALIHRHR PDLIDYAKLS KDNPLENLNT AFDVAEKYLD IPRMLDPDDL INTPKPDERA IMTYVSCYYH AFQGAQQVGN NTALPDERAV MTYVSSYYHC FSGAQKAETA ANRICKVLKV NQENERLMEE YERLASDLLE WIRRTMPWLN SRQADNSLAG VQKKLEEYRT YRRKHKPPRV EQKAKLETNF NTLQTKLRLS NRPAYLPTEG KTVSDISNSW KGLELAEKAF EEWLLAETMR LERLEHLAQK FKHKADAHED WTRGKEEMLQ SQDFRQCKLN ELKALKKKHE AFESDLAAHQ DRVEQIAAIA QELNTLEYHD CVSVNARCQR ICDQWDRLGA LTQRRRTALD EAERILEKID ILHLEFAKRA APFNNWLDGT REDLVDMFIV HTMEEIQGLI QAHDQFKATL GEADKEFNLI VNLVREVESI VKQHQIPGGL ENPYTTLTAN DMTRKWSDVR QLVPQRDQTL ANELRKQQNN EMLRRQFAEK ANIVGPWIER QMDAVTAIGM GLQGSLEDQL HRLKEYEQAV YAYKPNIEEL EKIHQAVQES MIFENRYTNY TMETLRVGWE QLLTSINRNI NEVENQILTR DSKGISQEQL NEFRSSFNHF DKNRTGRLSP EEFKSCLVSL GYSIGKDRQG DLDFQRILAV VDPNNTGYVH FDAFLDFMTR ESTDTDTAEQ VIDSFRILAA DKPYILPDEL RRELPPDQAE YCIQRMPPYK GPNGVPGALD YMSFSTALYG ETDL // ID ABL_DROME STANDARD; PRT; 1520 AA. AC P00522; DT 21-JUL-1986 (Rel. 01, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tyrosine-protein kinase Abl (EC 2.7.1.112) (D-ash). GN ABL OR DASH OR ABL-1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88174728; PubMed=2832740; RA Henkemeyer M.J., Bennett R.L., Gertler F.B., Hoffmann F.M.; RT "DNA sequence, structure, and tyrosine kinase activity of the RT Drosophila melanogaster Abelson proto-oncogene homolog."; RL Mol. Cell. Biol. 8:843-853(1988). RN [2] RP SEQUENCE OF 374-648 FROM N.A. RX MEDLINE=84082064; PubMed=6317185; RA Hoffmann F.M., Fresco L.D., Hoffman-Falk H., Shilo B.-Z.; RT "Nucleotide sequences of the Drosophila src and abl homologs: RT conservation and variability in the src family oncogenes."; RL Cell 35:393-401(1983). RN [3] RP FUNCTION. RX MEDLINE=98298928; PubMed=9635189; RA Loureiro J., Peifer M.; RT "Roles of Armadillo, a Drosophila catenin, during central nervous RT system development."; RL Curr. Biol. 8:622-632(1998). CC -!- FUNCTION: ARM AND ABL PROTEINS FUNCTION COOPERATIVELY AT ADHERENS CC JUNCTIONS IN BOTH THE CNS AND EPIDERMIS. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. ABL CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19692; AAA28934.1; -. DR EMBL; M19690; AAA28934.1; JOINED. DR EMBL; M19691; AAA28934.1; JOINED. DR EMBL; K01042; AAA28443.1; -. DR PIR; A28128; TVFFA. DR HSSP; P00519; 1AB2. DR FlyBase; FBgn0000017; Abl. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0019897; C:extrinsic to plasma membrane; IDA. DR GO; GO:0005911; C:intercellular junction; IDA. DR GO; GO:0005927; C:muscle tendon junction; IDA. DR GO; GO:0004713; F:protein-tyrosine kinase activity; IDA. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0007417; P:central nervous system development; IGI. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0002009; P:morphogenesis of an epithelium; NAS. DR GO; GO:0008360; P:regulation of cell shape; NAS. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW Transferase; Tyrosine-protein kinase; ATP-binding; Phosphorylation; KW SH2 domain; SH3 domain. FT DOMAIN 204 265 SH3. FT DOMAIN 271 363 SH2. FT DOMAIN 388 644 PROTEIN KINASE. FT NP_BIND 394 402 ATP (BY SIMILARITY). FT BINDING 417 417 ATP (BY SIMILARITY). FT ACT_SITE 509 509 BY SIMILARITY. FT MOD_RES 539 539 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT CONFLICT 374 377 LSPE -> ASAQ (IN REF. 2). FT CONFLICT 645 648 ESSI -> VGDV (IN REF. 2). SQ SEQUENCE 1520 AA; 161836 MW; AD6A5060579FAD7B CRC64; MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NGTKHSSFRG HPGKYHMNLE ALLQSRPLPH IPAGSTRPLF WRIAELQQHQ QDSGGLGLQG SSLGGGHSST TSVFESAHRW TSKENLLAPG PEEDDPQLFV ALYDFQAGGE NQLSLKKGEQ VRILSYNKSG EWCEAHSDSG NVGWVPSNYV TPLNSLEKHS WYHGPISRNA AEYLLSSGIN GSFLVRESES SPGQRSISLR YEGRVYHYRI SEDPDGKVFV TQEAKFNTLA ELVHHHSVPH EGHGLITPLL YPAPKQNKPT VFPLSPEPDE WEICRTDIMM KHKLGGGQYG EVYEAVWKRY GNTVAVKTLK EDTMALKDFL EEAAIMKEMK HPNLVQLIGV CTREPPFYII TEFMSHGNLL DFLRSAGRET LDAVALLYMA TQIASGMSYL ESRNYIHRDL AARNCLVGDN KLVKVADFGL ARLMRDDTYT AHAGAKFPIK WTAPEGLAYN KFSTKSDVWA FGVLLWEIAT YGMSPYPAID LTDVYHKLDK GYRMERPPGC PPEVYDLMRQ CWQWDATDRP TFKSIHHALE HMFQESSITE AVEKQLNANA TSASSSAPST SGVATGGGAT TTTAASGCAS SSSATASLSL TPQMVKKGLP GGQALTPNAH HNDPHQQQAS TPMSETGSTS TKLSTFSSQG KGNVQMRRTT NKQGKQAPAP PKRTSLLSSS RDSTYREEDP ANARCNFIDD LSTNGLARDI NSLTQRYDSE TDPAADPDTD ATGDSLEQSL SQVIAAPVTN KMQHSLHSGG GGGGIGPRSS QQHSSFKRPT GTPVMGNRGL ETRQSKRSQL HSQAPGPGPP STQPHHGNNG VVTSAHPITV GALDVMNVKQ VVNRYGTLPK GARIGAYLDS LEDSSEAAPA LPATAPSLPP ANGHATPPAA RLNPKASPIP PQQMIRSNSS GGVTMQNNAA ASLNKLQRHR TTTEGTMMTF SSFRAGGSSS SPKRSASGVA SGVQPALANL EFPPPPLDLP PPPEEFEGGP PPPPPAPESA VQAIQQHLHA QLPNNGNISN GNGTNNNDSS HNDVSNIAPS VEEASSRFGV SLRKREPSTD SCSSLGSPPE DLKEKLITEI KAAGKDTAPA SHLANGSGIA VVDPVSLLVT ELAESMNLPK PPPQQQQKLT NGNSTGSGFK AQLKKVEPKK MSAPMPKRTA NTIIDFKAHL RRVDKEKEPA TPAPAPATVA VANNANCNTT GTLNRKEDGS KKFSQAMQKT EIKIDVTNSN VEADAGAAGE GDLGKRRSTD DEEQSHTEGL GSGGQGSADM TQSLYEQKPQ IQQKPAVPHK PTKLTIYATP IAKLTEPASS ASSTQISRES ILELVGLLEG SLKHPVNAIA GSQWLQLSDK LNILHNSCVI FAENGAMPPH SKFQFRELVT RVEAQSQHLR SAGSKNVQDN ERLVAEVGQS LRQISNALNR // ID ABRU_DROME STANDARD; PRT; 904 AA. AC Q24174; Q9VKI1; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Abrupt protein (Clueless protein). GN AB OR CLU OR CG4807. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE RP SPLICING, AND MUTAGENESIS OF ARG-585. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=96101593; PubMed=7498790; RA Hu S., Fambrough D., Atashi J.R., Goodman C.S., Crews S.T.; RT "The Drosophila abrupt gene encodes a BTB-zinc finger regulatory RT protein that controls the specificity of neuromuscular connections."; RL Genes Dev. 9:2936-2948(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: EXPRESSION IS VITAL FOR DEVELOPMENT. IN EMBRYOS, MUSCLE CC SPECIFIC EXPRESSION REQUIRED FOR SEGMENTAL NERVE B (SNB) CC MOTONEURON TARGET RECOGNITION WITH VENTRAL LONGITUDINAL MUSCLES. CC HAS A ROLE IN ESTABLISHING AND MAINTAINING EMBRYONIC MUSCLE CC ATTACHMENTS, ADULT SENSORY CELL FORMATION (MACROCHAETAE) AND CC MORPHOGENESIS OF ADULT APPENDAGES (LEGS, ANTENNA ARISTAE, MALE CC EXTERNAL GENITALIA). CC -!- FUNCTION: MAY BE INVOLVED IN TRANSCRIPTIONAL REGULATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q24174-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q24174-2; Sequence=VSP_006823; CC -!- TISSUE SPECIFICITY: EXPRESSED IN CNS MIDLINE CELLS DURING CC EMBRYONIC STAGES 9-13. EXPRESSION ALSO SEEN IN CELLS OF THE CC STOMAGASTRIC NERVOUS SYSTEM. SEGMENTALLY REPEATED STRIPES OF CC ECTODERMAL EXPRESSION APPEAR AT STAGE 11 THAT BECOME UNIFORM BY CC STAGE 12 AND THROUGHOUT EMBRYOGENESIS. EXPRESSED AT VARIABLE CC LEVELS IN SOMATIC MUSCLES FROM STAGE 16 AND IN ALL IMAGINAL DISKS CC DURING LARVAL DEVELOPMENT. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 2 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U43733; AAA86639.1; -. DR EMBL; AE003631; AAF53087.2; -. DR EMBL; AE003631; AAN10774.1; -. DR EMBL; BT001583; AAN71338.1; -. DR FlyBase; FBgn0000011; ab. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003700; F:transcription factor activity; NAS. DR GO; GO:0016203; P:muscle attachment; IMP. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR GO; GO:0007423; P:sensory organ development; IMP. DR GO; GO:0008039; P:synaptic target recognition; IMP. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. KW Transcription regulation; Developmental protein; Nuclear protein; KW DNA-binding; Metal-binding; Zinc; Zinc-finger; Repeat; KW Alternative splicing. FT DOMAIN 103 168 BTB. FT DOMAIN 196 369 ALA/ASN/SER-RICH. FT ZN_FING 544 567 C2H2-TYPE 1. FT ZN_FING 573 596 C2H2-TYPE 2. FT VARSPLIC 356 365 Missing (in isoform Short). FT /FTId=VSP_006823. FT MUTAGEN 585 585 R->C: IN ALLELE AB-CLU2; LETHAL. FT CONFLICT 264 264 H -> P (IN REF. 4). FT CONFLICT 695 695 S -> T (IN REF. 1). FT CONFLICT 888 888 N -> D (IN REF. 4). SQ SEQUENCE 904 AA; 95093 MW; 9DF8F4EDDF8E5CF7 CRC64; MTESTQLQTA ENNNAGVVKM EPPPPATSSV SVSAAAAAHA LSSLSSLTMA ATGSALSPAT PPPSLNLSHQ QQQHQQHYAL KWNDFQSSIL SSFRHLRDEE DFVDVTLACD ERSFTAHKVV LSACSPYFRR LLKANPCEHP IVILRDVRCD DVENLLSFMY NGEVNVSHEQ LPDFLKTAHL LQIRGLADVN GGYPYSKALS AALSHNSSNN NNNNSSSNNS LSNNNNNNNN NAESSNHNKI SSYLSPNQTS AACNNSSNSN SNNHSSSHNN SSSNNISGSL NSSLNSPFSA PQIPPPVTAS SAAAAAAAAA SLTAAVAAAA AATAASAGSS SSAASGQTSG TPAIQELKAS SAASPVRNPN PNPSKASSSN HWDMGEMEGS RKSHLTPPPQ KRIKSADLFR AQHGISPERL LLDREFPVAG QHPLTRNRSG RDTSKDRERN LELRESLLGQ ALENSNGQQA NPKHELGQSA GEDSNSSDTE PSDRGDGQHD GTLDGIDNQR SHSFPNAFLG LQGIPGLLPG PSGINSDFVS RRSLEMRVRA TDPRPCPKCG KIYRSAHTLR THLEDKHTVC PGYRCVLCGT VAKSRNSLHS HMSRQHRGIS TKDLPVLPMP SAFDPELASR LLAKAGVKIS PAELRARASP TGGSGSSGGG GGGGSSQAKL DLSNASGGPM DDAEDSDDDP EDLTTGNGLY GMGGSSSDLS RYHESLLSNF GHARMRNEAA AVAATAAALG QPKDLGVQLP NSNAPGQSLL DTYLQFITEN TFGMGMSQEQ AAAAALRAKM AQLNAMGHSL DNLPPGLLPG QFDLSKLAAG NPAFGQSGPG LTIEPIMRHE QAAGNLSPNR PLALNSGGRM MGHDEMAEND GDMRREGSEP MDLGLDNNQS GSNHEVANSD AEENYSEDEG VHNT // ID ABS_DROME STANDARD; PRT; 619 AA. AC Q9V3C0; Q9U6D0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DEAD-box protein abstrakt. GN ABS OR CG14637. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20171041; PubMed=10704843; RA Schmucker D., Vorbrueggen G., Yeghiayan P., Fan H.Q., Jaeckle H., RA Gaul U.; RT "The drosophila gene abstrakt, required for visual system development, RT encodes a putative RNA helicase of the DEAD box protein family."; RL Mech. Dev. 91:189-196(2000). RN [2] RP SEQUENCE FROM N.A., AND VARIANTS 14B AND 33B. RX MEDLINE=20076860; PubMed=10607561; RA Irion U., Leptin M.; RT "Developmental and cell biological functions of the Drosophila DEAD- RT box protein abstrakt."; RL Curr. Biol. 9:1373-1381(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ATP-DEPENDENT RNA HELICASE. IS ESSENTIAL FOR THE CC DIRECTED AND FASCICULATED EARLY OUTGROWTH OF THE BOLWIG NERVES, AS CC WELL AS FOR ITS NAVIGATION AT LATER STAGES. IS REQUIRED DURING CC POST-TRANSCRIPTIONAL GENE EXPRESSION. PLAYS A ROLE DURING CC MORPHOGENETIC PROCESS, APOPTOSIS AND THE ESTABLISHMENT OF CELL CC POLARITY. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 CCHC-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF212866; AAF19985.1; -. DR EMBL; AF187729; AAF04040.1; -. DR EMBL; AE003607; AAF52165.1; -. DR EMBL; AY051752; AAK93176.1; -. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0015331; abs. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR001878; Znf_CCHC. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00098; zf-CCHC; 1. DR PRINTS; PR00939; C2HCZNFINGER. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00343; ZnF_C2HC; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; FALSE_NEG. DR PROSITE; PS50158; ZF_CCHC; 1. KW ATP-binding; RNA-binding; Helicase; Nuclear protein; Zinc-finger. FT NP_BIND 221 228 ATP (POTENTIAL). FT SITE 340 343 DEAD BOX. FT ZN_FING 577 594 CCHC-TYPE. FT VARIANT 241 241 E -> K (IN ALLELE 14B; TEMPERATURE FT SENSITIVE). FT VARIANT 431 431 V -> M (IN ALLELE 33B; TEMPERATURE FT SENSITIVE). FT CONFLICT 5 5 K -> Q (IN REF. 2). FT CONFLICT 26 30 MISSING (IN REF. 2). SQ SEQUENCE 619 AA; 69487 MW; F148D277A1FD0BEC CRC64; MAHVKRYRRS SKSSEEGDLD NEDYVPYVPV KERKKQHMIK LGRIVQLVSE TAQPKSSSEN ENEDDSQGAH DVETWGRKYN ISLLDQHTEL KKIAEAKKLS AVEKQLREEE KIMESIAQQK ALMGVAELAK GIQYEQPIKT AWKPPRYIRE MSEEEREAVR HELRILVEGE TPSPPIRSFR EMKFPKGILN GLAAKGIKNP TPIQVQGLPT VLAGRDLIGI AFTGSGKTLV FVLPVIMFAL EQEYSLPFER NEGPYGLIIC PSRELAKQTH EIIQHYSKHL QACGMPEIRS CLAMGGLPVS EALDVISRGV HIVVATPGRL MDMLDKKILT LDMCRYLCMD EADRMIDMGF EEDVRTIFSF FKGQRQTLLF SATMPKKIQN FARSALVKPV TINVGRAGAA SMNVTQQVEY VKQEAKVVYL LDCLQKTAPP VLIFAEKKQD VDCIHEYLLL KGVEAVAIHG GKDQEERSRA VDAYRVGKKD VLVATDVASK GLDFPNVQHV INYDMPDDIE NYVHRIGRTG RSNTKGLATT LINKTTEQSV LLDLKHLLIE GKQEVPDFLD ELAPETEHQH LDLGDSHGCT YCGGLGHRIT ECPKLEAVQN KQASNIGRRD YLSNTAADY // ID ACBP_DROME STANDARD; PRT; 86 AA. AC P42281; Q9VS23; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acyl-CoA-binding protein homolog (ACBP) (Diazepam binding inhibitor DE homolog) (DBI). GN DBI OR CG8627. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95021227; PubMed=7935415; RA Kolmer M., Roos C., Tirronen M., Myoehaenen S., Alho H.; RT "Tissue-specific expression of the diazepam-binding inhibitor in RT Drosophila melanogaster: cloning, structure, and localization of the RT gene."; RL Mol. Cell. Biol. 14:6983-6995(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Lagueux M., Bulet P., Hetru C.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS MEDIUM- AND LONG-CHAIN ACYL-COA ESTERS WITH VERY CC HIGH AFFINITY AND MAY FUNCTION AS AN INTRACELLULAR CARRIER OF CC ACYL-COA ESTERS (BY SIMILARITY). MAY BE INVOLVED IN ENERGY CC METABOLISM IN A MANNER THAT DEPENDS ON THE SUBSTRATE USED FOR CC ENERGY PRODUCTION. DBI AND ITS METABOLITES ARE INVOLVED IN THE CC REGULATION OF MULTIPLE BIOLOGICAL PROCESSES. CC -!- TISSUE SPECIFICITY: CARDIA, PART OF THE MALPIGHIAN TUBULES, FAT CC BODY, AND GAMETES OF BOTH SEXES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM THE LARVAL STAGE ONWARDS CC THROUGHOUT THE ADULT STAGE. CC -!- SIMILARITY: BELONGS TO THE ACBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04822; AAA21649.1; -. DR EMBL; U04823; AAA21650.1; -. DR EMBL; X75596; CAA53268.1; -. DR EMBL; AE003560; AAF50607.1; -. DR PIR; A56041; A56041. DR PIR; S38574; S38574. DR HSSP; P07107; 1ACA. DR FlyBase; FBgn0010387; Dbi. DR InterPro; IPR000582; Ac_coA_bind_prot. DR Pfam; PF00887; ACBP; 1. DR PRINTS; PR00689; ACOABINDINGP. DR ProDom; PD351532; Ac_coA_bind_prot; 1. DR PROSITE; PS00880; ACBP; 1. KW Transport; Lipid-binding. FT CONFLICT 55 55 K -> S (IN REF. 2). SQ SEQUENCE 86 AA; 9557 MW; 623986B5566228E1 CRC64; MVSEQFNAAA EKVKSLTKRP SDDEFLQLYA LFKQASVGDN DTAKPGLLDL KGKAKWEAWN KQKGKSSEAA QQEYITFVEG LVAKYA // ID ACES_DROME STANDARD; PRT; 649 AA. AC P07140; Q9VFY0; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acetylcholinesterase precursor (EC 3.1.1.7) (AChE). GN ACE OR CG17907. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87080281; PubMed=3024971; RA Hall L.M.C., Spierer P.; RT "The Ace locus of Drosophila melanogaster: structural gene for RT acetylcholinesterase with an unusual 5' leader."; RL EMBO J. 5:2949-2954(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=MH19, Canton-S, and Oregon-R; TISSUE=Embryo, and Pupae; RX MEDLINE=90064544; PubMed=2511327; RA Fournier D., Karch F., Bride J.-M., Hall L.M.C., Berge J.-B., RA Spierer P.; RT "Drosophila melanogaster acetylcholinesterase gene. Structure, RT evolution and mutations."; RL J. Mol. Biol. 210:15-22(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SUBUNITS. RX MEDLINE=89005711; PubMed=3139459; RA Fournier D., Bride J.-M., Karsch F., Berge J.-B.; RT "Acetylcholinesterase from Drosophila melanogaster. Identification of RT two subunits encoded by the same gene."; RL FEBS Lett. 238:333-337(1988). RN [5] RP POST-TRANSLATIONAL MODIFICATIONS. RX MEDLINE=92112889; PubMed=1730712; RA Mutero A., Fournier D.; RT "Post-translational modifications of Drosophila acetylcholinesterase. RT In vitro mutagenesis and expression in Xenopus oocytes."; RL J. Biol. Chem. 267:1695-1700(1992). CC -!- FUNCTION: RAPIDLY HYDROLYZES CHOLINE RELEASED INTO THE SYNAPSE. CC IT CAN HYDROLYZE BUTYRYLTHIOCHOLINE. CC -!- CATALYTIC ACTIVITY: ACETYLCHOLINE + H(2)O = CHOLINE + ACETATE. CC -!- SUBUNIT: THE ACTIVE ENZYME SEEMS TO BE COMPOSED OF THE NON- CC COVALENT ASSOCIATION OF A 55 KDA AND A 16 KDA POLYPEPTIDE. TWO CC ACTIVE UNITS ARE LINKED TOGETHER BY A DISULFIDE BOND AT THE C- CC TERMINUS OF THE 55 KDA PEPTIDE. CC -!- SUBCELLULAR LOCATION: LINKED TO THE MEMBRANE OF THE NEURONAL CC CHOLINERGIC SYNAPSES BY A GPI-ANCHOR. CC -!- SIMILARITY: BELONGS TO THE TYPE-B CARBOXYLESTERASE/LIPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05893; CAA29326.1; -. DR EMBL; AE003699; AAF54915.1; -. DR PIR; A25363; A25363. DR PDB; 1DX4; 21-JUL-00. DR PDB; 1QO9; 20-JUL-00. DR FlyBase; FBgn0000024; Ace. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR000997; Cholinesterase. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR00878; CHOLNESTRASE. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. KW Hydrolase; Serine esterase; Synapse; Membrane; Nerve; Signal; KW Neurotransmitter degradation; GPI-anchor; Glycoprotein; 3D-structure. FT SIGNAL 1 38 POTENTIAL. FT CHAIN 39 649 ACETYLCHOLINESTERASE. FT CHAIN 39 ? ACETYLCHOLINESTERASE 16 kDa SUBUNIT. FT CHAIN ? 649 ACETYLCHOLINESTERASE 55 kDa SUBUNIT. FT ACT_SITE 276 276 BY SIMILARITY. FT ACT_SITE 405 405 BY SIMILARITY. FT ACT_SITE 518 518 BY SIMILARITY. FT DISULFID 104 131 POTENTIAL. FT DISULFID 330 345 POTENTIAL. FT DISULFID 480 598 POTENTIAL. FT DISULFID 615 615 INTERCHAIN. FT CARBOHYD 126 126 N-LINKED (GLCNAC...). FT CARBOHYD 174 174 N-LINKED (GLCNAC...). FT CARBOHYD 331 331 N-LINKED (GLCNAC...). FT CARBOHYD 531 531 N-LINKED (GLCNAC...). FT CONFLICT 99 99 G -> R (IN REF. 3). SQ SEQUENCE 649 AA; 71785 MW; 5863C73FF99028C0 CRC64; MAISCRQSRV LPMSLPLPLT IPLPLVLVLS LHLSGVCGVI DRLVVQTSSG PVRGRSVTVQ GREVHVYTGI PYAKPPVEDL RFRKPVPAEP WHGVLDATGL SATCVQERYE YFPGFSGEEI WNPNTNVSED CLYINVWAPA KARLRHGRGA NGGEHPNGKQ ADTDHLIHNG NPQNTTNGLP ILIWIYGGGF MTGSATLDIY NADIMAAVGN VIVASFQYRV GAFGFLHLAP EMPSEFAEEA PGNVGLWDQA LAIRWLKDNA HAFGGNPEWM TLFGESAGSS SVNAQLMSPV TRGLVKRGMM QSGTMNAPWS HMTSEKAVEI GKALINDCNC NASMLKTNPA HVMSCMRSVD AKTISVQQWN SYSGILSFPS APTIDGAFLP ADPMTLMKTA DLKDYDILMG NVRDEGTYFL LYDFIDYFDK DDATALPRDK YLEIMNNIFG KATQAEREAI IFQYTSWEGN PGYQNQQQIG RAVGDHFFTC PTNEYAQALA ERGASVHYYY FTHRTSTSLW GEWMGVLHGD EIEYFFGQPL NNSLQYRPVE RELGKRMLSA VIEFAKTGNP AQDGEEWPNF SKEDPVYYIF STDDKIEKLA RGPLAARCSF WNDYLPKVRS WAGTCDGDSG SASISPRLQL LGIAALIYIC AALRTKRVF // ID ACE_DROME STANDARD; PRT; 615 AA. AC Q10714; Q27572; Q9NKE4; Q9TX66; Q9VJV3; DT 01-NOV-1997 (Rel. 35, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Angiotensin-converting enzyme precursor (EC 3.4.15.1) (Dipeptidyl DE carboxypeptidase I) (Kininase II). GN ANCE OR RACE OR BG:DS08220.3 OR CG8827. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=94040210; PubMed=8224398; RA Cornell M.J., Coates D., Isaac R.E.; RT "Characterisation of putative Drosophila angiotensin converting enzyme RT cDNA clones."; RL Biochem. Soc. Trans. 21:243-243(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95293950; PubMed=7775412; RA Cornell M.J., Williams T.A., Lamango N.S., Coates D., Corvol P., RA Soubrier F., Hoheisel J., Lehrach H., Isaac R.E.; RT "Cloning and expression of an evolutionary conserved single-domain RT angiotensin converting enzyme from Drosophila melanogaster."; RL J. Biol. Chem. 270:13613-13619(1995). RN [3] RP REVISIONS. RA Cornell M.J.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96028519; PubMed=7547464; RA Tatei K., Cai H., Ip Y.T., Levine M.; RT "Race: a Drosophila homologue of the angiotensin converting enzyme."; RL Mech. Dev. 51:157-168(1995). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., RA Martin C.H., Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., RA Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [7] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY PLAY A ROLE IN THE CONTRACTIONS OF THE HEART, GUT CC AND TESTES. CC -!- CATALYTIC ACTIVITY: RELEASE OF A C-TERMINAL DIPEPTIDE, CC OLIGOPEPTIDE-|-XAA-XBB, WHEN XAA IS NOT PRO, AND XBB IS NEITHER CC ASP NOR GLU. CONVERTS ANGIOTENSIN I TO ANGIOTENSIN II. CC -!- COFACTOR: BINDS 1 ZINC ION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE AMNIOSEROSA DURING GERM BAND CC ELONGATION, SHORTENING AND HEART MORPHOGENESIS. EXPRESSED IN CC MIDGUT THROUGHOUT EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M2. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U25344; AAB02171.1; -. DR EMBL; U34599; AAC46902.1; -. DR EMBL; AE003408; AAF44834.1; -. DR EMBL; AE003641; AAF53353.2; -. DR EMBL; AY061129; AAL28677.1; -. DR MEROPS; M02.003; -. DR FlyBase; FBgn0012037; Ance. DR GO; GO:0004246; F:peptidyl-dipeptidase A activity; IDA. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR001548; Peptidase_M2. DR Pfam; PF01401; Peptidase_M2; 1. DR PRINTS; PR00791; PEPDIPTASEA. DR ProDom; PD004184; Peptidase_M2; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW Hydrolase; Metalloprotease; Carboxypeptidase; Zinc; KW Glycoprotein; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 615 ANGIOTENSIN-CONVERTING ENZYME. FT METAL 367 367 ZINC (CATALYTIC) (BY SIMILARITY). FT ACT_SITE 368 368 BY SIMILARITY. FT METAL 371 371 ZINC (CATALYTIC) (BY SIMILARITY). FT CARBOHYD 53 53 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 196 196 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 311 311 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 48 51 WAYG -> GPMR (IN REF. 4). FT CONFLICT 141 141 C -> S (IN REF. 4). FT CONFLICT 293 293 G -> A (IN REF. 3). FT CONFLICT 346 346 I -> T (IN REF. 5, 6 AND 7). FT CONFLICT 365 365 V -> E (IN REF. 1). FT CONFLICT 402 402 S -> A (IN REF. 1). FT CONFLICT 414 414 I -> T (IN REF. 1). FT CONFLICT 486 486 S -> T (IN REF. 4). FT CONFLICT 533 533 V -> M (IN REF. 4). FT CONFLICT 547 547 A -> R (IN REF. 3). SQ SEQUENCE 615 AA; 70926 MW; 9E3F9A41C51B9485 CRC64; MRLFLLALLA TLAVTQALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY GSNITDENEK KKNEISAELA KFMKEVASDT TKFQWRSYQS EDLKRQFKAL TKLGYAALPE DDYAELLDTL SAMESNFAKV KVCDYKDSTK CDLALDPEIE EVISKSRDHE ELAYYWREFY DKAGTAVRSQ FERYVELNTK AAKLNNFTSG AEAWLDEYED DTFEQQLEDI FADIRPLYQQ IHGYVRFRLR KHYGDAVVSE TGPIPMHLLG NMWAQQWSEI ADIVSPFPEK PLVDVSAEME KQGYTPLKMF QMGDDFFTSM NLTKLPQDFW DKSIIEKPTD GRDLVCHASA WDFYLIDDVR IKQCTRVTQD QLFTVHHELG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV LSLSVSTPKH LEKIGLLKDY VRDDEARINQ LFLTALDKIV FLPFAFTMDK YRWSLFRGEV DKANWNCAFW KLRDEYSGIE PPVVRSEKDF DAPAKYHISA DVEYLRYLVS FIIQFQFYKS ACIKAGQYDP DNVELPLDNC DIYGSAAAGA AFHNMLSMGA SKPWPDALEA FNGERIMSGK AIAEYFEPLR VWLEAENIKN NVHIGWTTSN KCVSS // ID ACH1_DROME STANDARD; PRT; 567 AA. AC P09478; Q9VC74; DT 01-MAR-1989 (Rel. 10, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acetylcholine receptor protein, alpha-like chain 1 precursor. GN NACR-ALPHA-96AA OR ACRB OR ALS OR ACR96AA OR CG5610. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=88283626; PubMed=2840281; RA Bossy B., Ballivet M., Spierer P.; RT "Conservation of neural nicotinic acetylcholine receptors from RT Drosophila to vertebrate central nervous systems."; RL EMBO J. 7:611-618(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN CC EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND CC LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CNS IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC, LATE PUPAL AND SECOND INSTAR CC LARVAE STAGES. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNEL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07194; CAA30172.1; -. DR EMBL; AE003747; AAF56301.2; -. DR PIR; S00381; ACFFA1. DR FlyBase; FBgn0000036; nAcR-alpha-96Aa. DR InterPro; IPR006029; Neu_channel_memb. DR InterPro; IPR006202; Neur_chan_LBD. DR InterPro; IPR006201; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Multigene family; Polymorphism. FT SIGNAL 1 21 FT CHAIN 22 567 ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA- FT LIKE CHAIN 1. FT DOMAIN 22 240 EXTRACELLULAR. FT TRANSMEM 241 264 FT TRANSMEM 272 290 FT TRANSMEM 306 325 FT DOMAIN 326 513 CYTOPLASMIC. FT TRANSMEM 514 532 FT DISULFID 149 163 BY SIMILARITY. FT DISULFID 222 223 ASSOCIATED WITH RECEPTOR ACTIVATION FT (BY SIMILARITY). FT CARBOHYD 45 45 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 233 233 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 538 538 Y -> H. FT CONFLICT 108 108 L -> H (IN REF. 1). SQ SEQUENCE 567 AA; 64019 MW; 08E1F721FB2A92AC CRC64; MGSVLFAAVF IALHFATGGL ANPDAKRLYD DLLSNYNRLI RPVGNNSDRL TVKMGLRLSQ LIDVNLKNQI MTTNVWVEQE WNDYKLKWNP DDYGGVDTLH VPSEHIWLPD IVLYNNADGN YEVTIMTKAI LHHTGKVVWK PPAIYKSFCE IDVEYFPFDE QTCFMKFGSW TYDGYMVDLR HLKQTADSDN IEVGIDLQDY YISVEWDIMR VPAVRNEKFY SCCEEPYLDI VFNLTLRRKT LFYTVNLIIP CVGISFLSVL VFYLPSDSGE KISLCISILL SLTVFFLLLA EIIPPTSLTV PLLGKYLLFT MMLVTLSVVV TIAVLNVNFR SPVTHRMAPW VQRLFIQILP KLLCIERPKK EEPEEDQPPE VLTDVYHLPP DVDKFVNYDS KRFSGDYGIP ALPASHRFDL AAAGGISAHC FAEPPLPSSL PLPGADDDLF SPSGLNGDIS PGCCPAAAAA AAADLSPTFE KPYAREMEKT IEGSRFIAQH VKNKDKFESV EEDWKYVAMV LDRMFLWIFA IACVVGTALI ILQAPSLYDQ SQPIDILYSK IAKKKFELLK MGSENTL // ID ACH2_DROME STANDARD; PRT; 576 AA. AC P17644; Q9VC73; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acetylcholine receptor protein, alpha-like chain 2 precursor. GN NACR-ALPHA-96AB OR ACRE OR SAD OR ACR96AB OR CG6844. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=90301489; PubMed=2114015; RA Baumann A., Jonas P., Gundelfinger E.D.; RT "Sequence of D alpha 2, a novel alpha-like subunit of Drosophila RT nicotinic acetylcholine receptors."; RL Nucleic Acids Res. 18:3640-3640(1990). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=90353591; PubMed=2117557; RA Jonas P., Baumann A., Merz B., Gundelfinger E.D.; RT "Structure and developmental expression of the D alpha 2 gene RT encoding a novel nicotinic acetylcholine receptor protein of RT Drosophila melanogaster."; RL FEBS Lett. 269:264-268(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=90360975; PubMed=1697262; RA Sawruk E., Schloss P., Betz H., Schmitt B.; RT "Heterogeneity of Drosophila nicotinic acetylcholine receptors: SAD, RT a novel developmentally regulated alpha-subunit."; RL EMBO J. 9:2671-2677(1990). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN CC EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND CC LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CNS IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC AND LATE PUPAL STAGES. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNEL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52274; CAA36517.1; -. DR EMBL; X53583; CAA37652.1; -. DR EMBL; AE003748; AAF56303.1; -. DR EMBL; AY058446; AAL13675.1; -. DR PIR; S11679; ACFFA2. DR FlyBase; FBgn0000039; nAcR-alpha-96Ab. DR InterPro; IPR006029; Neu_channel_memb. DR InterPro; IPR006202; Neur_chan_LBD. DR InterPro; IPR006201; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Multigene family. FT SIGNAL 1 21 PROBABLE. FT CHAIN 22 576 ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA- FT LIKE CHAIN 2. FT DOMAIN 22 261 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 262 285 POTENTIAL. FT TRANSMEM 293 311 POTENTIAL. FT TRANSMEM 327 346 POTENTIAL. FT DOMAIN 347 526 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 527 545 POTENTIAL. FT DISULFID 169 183 BY SIMILARITY. FT DISULFID 243 244 ASSOCIATED WITH RECEPTOR ACTIVATION FT (BY SIMILARITY). FT CARBOHYD 65 65 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 254 254 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 570 570 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 576 AA; 65506 MW; 97D6A46CADC3F42F CRC64; MAPGCCTTRP RPIALLAHIW RHCKPLCLLL VLLLLCETVQ ANPDAKRLYD DLLSNYNRLI RPVSNNTDTV LVKLGLRLSQ LIDLNLKDQI LTTNVWLEHE WQDHKFKWDP SEYGGVTELY VPSEHIWLPD IVLYNNADGE YVVTTMTKAI LHYTGKVVWT PPAIFKSSCE IDVRYFPFDQ QTCFMKFGSW TYDGDQIDLK HISQKNDKDN KVEIGIDLRE YYPSVEWDIL GVPAERHEKY YPCCAEPYPD IFFNITLRRK TLFYTVNLII PCVGISYLSV LVFYLPADSG EKIALCISIL LSQTMFFLLI SEIIPSTSLA LPLLGKYLLF TMLLVGLSVV ITIIILNIHY RKPSTHKMRP WIRSFFIKRL PKLLLMRVPK DLLRDLAANK INYGLKFSKT KFGQALMDEM QMNSGGSSPD SLRRMQGRVG AGGCNGMHVT TATNRFSGLV GALGGGLSTL SGYNGLPSVL SGLDDSLSDV AARKKYPFEL EKAIHNVMFI QHHMQRQDEF NAEDQDWGFV AMVMDRLFLW LFMIASLVGT FVILGEAPSL YDDTKAIDVQ LSDVAKQIYN LTEKKN // ID ACH3_DROME STANDARD; PRT; 521 AA. AC P04755; Q9VZC3; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acetylcholine receptor protein, beta-like chain 1 precursor. GN NACR-BETA-64B OR ACRD OR ARD OR ACR64B OR CG11348/CG12606. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Hermans-Borgmeyer I., Zopf D., Ryseck R.-P., Hovemann B., Betz H., RA Gundelfinger E.D.; RT "Primary structure of a developmentally regulated nicotinic RT acetylcholine receptor protein from Drosophila."; RL EMBO J. 5:1503-1508(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88296842; PubMed=3136037; RA Sawruk E., Hermans-Borgmeyer I., Betz H., Gundelfinger E.D.; RT "Characterization of an invertebrate nicotinic acetylcholine receptor RT gene: the ard gene of Drosophila melanogaster."; RL FEBS Lett. 235:40-46(1988). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=88174720; PubMed=2832736; RA Wadsworth S.C., Rosenthal L.S., Kammermeyer K.L., Potter M.B., RA Nelson D.J.; RT "Expression of a Drosophila melanogaster acetylcholine receptor- RT related gene in the central nervous system."; RL Mol. Cell. Biol. 8:778-785(1988). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN CC EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND CC LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CNS IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC AND LATE PUPAL STAGES. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNEL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04016; CAA27641.1; -. DR EMBL; X07956; CAA30778.1; -. DR EMBL; X07957; CAA30778.1; JOINED. DR EMBL; X07958; CAA30778.1; JOINED. DR EMBL; M20316; AAA28311.1; -. DR EMBL; AE003481; AAF47900.1; -. DR PIR; S03012; ACFFNN. DR FlyBase; FBgn0000038; nAcR-beta-64B. DR InterPro; IPR006029; Neu_channel_memb. DR InterPro; IPR006202; Neur_chan_LBD. DR InterPro; IPR006201; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Multigene family. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 521 ACETYLCHOLINE RECEPTOR PROTEIN, BETA-LIKE FT CHAIN 1. FT DOMAIN 25 235 EXTRACELLULAR. FT TRANSMEM 236 260 FT TRANSMEM 268 286 FT TRANSMEM 302 323 FT DOMAIN 324 481 CYTOPLASMIC. FT TRANSMEM 482 500 FT DISULFID 152 166 BY SIMILARITY. FT CARBOHYD 48 48 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 73 73 V -> I. FT CONFLICT 383 384 EL -> DV (IN REF. 3). SQ SEQUENCE 521 AA; 59901 MW; FF9BA2ABC0C3AA62 CRC64; MESSCKSWLL CSILVLVAFS LVSASEDEER LVRDLFRGYN KLIRPVQNMT QKVGVRFGLA FVQLINVNEK NQVMKSNVWL RLVWYDYQLQ WDEADYGGIG VLRLPPDKVW KPDIVLFNNA DGNYEVRYKS NVLIYPTGEV LWVPPAIYQS SCTIDVTYFP FDQQTCIMKF GSWTFNGDQV SLALYNNKNF VDLSDYWKSG TWDIIEVPAY LNVYEGDSNH PTETDITFYI IIRRKTLFYT VNLILPTVLI SFLCVLVFYL PAEAGEKVTL GISILLSLVV FLLLVSKILP PTSLVLPLIA KYLLFTFIMN TVSILVTVII INWNFRGPRT HRMPMYIRSI FLHYLPAFLF MKRPRKTRLR WMMEMPGMSM PAHPHPSYGS PAELPKHISA IGGKQSKMEV MELSDLHHPN CKINRKVNSG GELGLGDGCR RESESSDSIL LSPEASKATE AVEFIAEHLR NEDLYIQTRE DWKYVAMVID RLQLYIFFIV TTAGTVGILM DAPHIFEYVD QDRIIEIYRG K // ID ACH4_DROME STANDARD; PRT; 519 AA. AC P25162; O18403; Q8IMW6; Q8SXP7; Q9VC71; DT 01-MAY-1992 (Rel. 22, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acetylcholine receptor protein, beta-like chain 2 precursor. GN NACR-BETA-96A OR ACRF OR SBD OR ACR96AC OR CG6798. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE OF 20-519 FROM N.A. (ISOFORM A). RC STRAIN=Canton-S; RX MEDLINE=91032173; PubMed=2121539; RA Sawruk E., Udri C., Betz H., Schmitt B.; RT "SBD, a novel structural subunit of the Drosophila nicotinic RT acetylcholine receptor, shares its genomic localization with two RT alpha-subunits."; RL FEBS Lett. 273:177-181(1990). RN [2] RP SEQUENCE OF 1-65 FROM N.A. RX MEDLINE=97263590; PubMed=9109505; RA Lansdell S.J., Schmitt B., Betz H., Sattelle D.B., Millar N.S.; RT "Temperature-sensitive expression of Drosophila neuronal nicotinic RT acetylcholine receptors."; RL J. Neurochem. 68:1812-1819(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP RNA EDITING. RX MEDLINE=22789647; PubMed=12907802; RA Hoopengardner B., Bhalla T., Staber C., Reenan R.; RT "Nervous system targets of RNA editing identified by comparative RT genomics."; RL Science 301:832-836(2003). CC -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN CC EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND CC LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=P25162-1; Sequence=Displayed; CC Name=B; CC IsoId=P25162-2; Sequence=VSP_007411, VSP_007412; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: CNS IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC AND LATE PUPAL STAGES. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNEL FAMILY. CC -!- CAUTION: REF.5 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 237. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55676; CAA39211.1; -. DR EMBL; Y14678; CAA74994.1; -. DR EMBL; AE003748; AAF56304.1; -. DR EMBL; AE003748; AAN13998.1; -. DR EMBL; AY089498; AAL90236.1; ALT_FRAME. DR PIR; S12899; S12899. DR FlyBase; FBgn0004118; nAcR-beta-96A. DR InterPro; IPR006029; Neu_channel_memb. DR InterPro; IPR006202; Neur_chan_LBD. DR InterPro; IPR006201; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Alternative splicing; Multigene family; RNA editing. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 519 ACETYLCHOLINE RECEPTOR PROTEIN, BETA-LIKE FT CHAIN 2. FT DOMAIN 19 244 EXTRACELLULAR. FT TRANSMEM 245 269 POTENTIAL. FT TRANSMEM 277 295 POTENTIAL. FT TRANSMEM 311 332 POTENTIAL. FT DOMAIN 333 462 CYTOPLASMIC. FT TRANSMEM 463 481 POTENTIAL. FT CARBOHYD 50 50 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 154 168 BY SIMILARITY. FT VARSPLIC 279 304 LCISILVSLTVFFLLLAEIIPPTSLA -> KMDPPNSMIKN FT LRVIPSFLWHVACFC (in isoform B). FT /FTId=VSP_007411. FT VARSPLIC 305 519 Missing (in isoform B). FT /FTId=VSP_007412. FT VARIANT 278 278 T -> A (partial, due to RNA editing). FT CONFLICT 344 344 P -> R (IN REF. 1). SQ SEQUENCE 519 AA; 60140 MW; DDE67674529D2FCB CRC64; MWHWSLLCVF LLVPLANSTA PISFEANPDT KRLYDDLLSN YNRLIRPVVN NTETLTVWLG LKLSQLIEVN LKNQVMTTNL WVKQRWFDYK LRWDPEEYGG VEQLYVPSEH IWVPDIVLYN NWDGNYEVTL MTKATLKYTG EVFWEPPAIY KSSCEMNVEY FPYDEQICFM KFGSWTYNGA QVDLKHLDQI PGSNLVQVGI DLTEFYLSVE WDILEVPATK NEEYYPDTLE PFSDITFKLT MRRKTLFYTV NLIVPCVALT FLTVLVFYLP SDSGEKVTLC ISILVSLTVF FLLLAEIIPP TSLAVPLLGK YLLFTMILVS LSVWTTVCVL NIHFRSPSTH NMSPLVRKLF LHFMPKLMMM RRTQYTLPDY DDSTPSNGYT NEIDVRDSIS DFPSEFKDSQ DGAYDNGMQN SVDSDNVIPR NLTPEVLQAL RAVRFIAQHI KDADKDNEIV EDWKFVSMVL DRFFLWLFTL SCVFGTLAII CQSPSLYDTR SPIDRQLSEI PLRKNNFMLP PDIVRQVLT // ID ACM1_DROME STANDARD; PRT; 722 AA. AC P16395; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Muscarinic acetylcholine receptor DM1. GN ACRC OR MACR-60C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90046926; PubMed=2510174; RA Shapiro R.A., Wakimoto B.T., Subers E.M., Nathanson N.M.; RT "Characterization and functional expression in mammalian cells of RT genomic and cDNA clones encoding a Drosophila muscarinic RT acetylcholine receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9039-9043(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90005981; PubMed=2507354; RA Onai T., Fitzgerald M.G., Arakawa S., Gocayne J.D., Urquhart D.A., RA Hall L.M., Fraser C.M., McCombie W.R., Venter J.C.; RT "Cloning, sequence analysis and chromosome localization of a RT Drosophila muscarinic acetylcholine receptor."; RL FEBS Lett. 255:219-225(1989). CC -!- FUNCTION: THE MUSCARINIC ACETYLCHOLINE RECEPTOR MEDIATES VARIOUS CC CELLULAR RESPONSES, INCLUDING INHIBITION OF ADENYLATE CYCLASE, CC BREAKDOWN OF PHOSPHOINOSITIDES & MODULATION OF POTASSIUM CHANNELS CC THROUGH THE ACTION OF G PROTEINS. PRIMARY TRANSDUCING EFFECT IS CC PI TURNOVER. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27495; AAA85449.1; -. DR EMBL; M23412; AAA28676.1; ALT_INIT. DR PIR; S05661; S05661. DR FlyBase; FBgn0000037; mAcR-60C. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0004981; F:muscarinic acetylcholine receptor activity; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Postsynaptic membrane; Ionic channel; Glycoprotein; Transmembrane; KW Phosphorylation; Multigene family; G-protein coupled receptor. FT DOMAIN 1 26 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 27 49 1 (POTENTIAL). FT DOMAIN 50 60 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 61 81 2 (POTENTIAL). FT DOMAIN 82 100 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 101 120 3 (POTENTIAL). FT DOMAIN 121 140 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 141 162 4 (POTENTIAL). FT DOMAIN 163 184 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 185 208 5 (POTENTIAL). FT DOMAIN 209 634 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 635 656 6 (POTENTIAL). FT DOMAIN 657 672 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 673 693 7 (POTENTIAL). FT DOMAIN 694 722 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 4 4 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 7 7 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 75 75 T -> A (IN REF. 2). FT CONFLICT 119 119 N -> S (IN REF. 2). FT CONFLICT 136 136 G -> R (IN REF. 2). FT CONFLICT 147 147 A -> AA (IN REF. 2). FT CONFLICT 250 250 P -> G (IN REF. 2). FT CONFLICT 346 362 MISSING (IN REF. 2). FT CONFLICT 381 381 G -> A (IN REF. 2). FT CONFLICT 451 451 T -> A (IN REF. 2). FT CONFLICT 606 606 C -> VG (IN REF. 2). FT CONFLICT 614 614 P -> AR (IN REF. 2). FT CONFLICT 654 656 VLI -> CXS (IN REF. 1). FT CONFLICT 688 688 S -> C (IN REF. 2). FT CONFLICT 714 722 EGMVRGVYN -> DFYAASTIR (IN REF. 1). SQ SEQUENCE 722 AA; 78237 MW; FB35417CB2202A61 CRC64; MYGNQTNGTI GFETKGPRYS LASMVVMGFV AAILSTVTVA GNVMVMISFK IDKQLQTISN YFLFSLAIAD FAIGTISMPL FAVTTILGYW PLGPIVCDTW LALDYLASNA SVLNLLIINF DRYFSVTRPL TYRAKGTTNR AAVMIGAWGI SLLLWPPWIY SWPYIEGKRT VPKDECYIQF IETNQYITFG TALAAFYFPV TIMCFLYWRI WRETKKRQKD LPNLQAGKKD SSKRSNSSDE NTVVNHASGP LLAFAQVGGN DHDTWRRPRS ESSADAESVY MTNMVIDSGY HGMHSRKSSI KSTNTIKKSY TCFGSIKEWC IAWWHSGRED SDDFAYEQEE PSDLGYATPV TIETPLQSSV SRCTSMNVMR DNYSMGGSVS GVRPPSILLS DVSPTPLPRP PLASISQLQE MSAVTASTTA NVNTSGNGNG AINNNNNASH NGNGAVNGNG TGNGSGIGLG TTGNATHRDS RTLPVINRIN SRSVSQDSVY TILIRLPSDG ASSNAANGGG GGPGAGAAAS ASLSMQGDCA PSIKMIHEDG PTTTAAAAPL ASAAATRRPL PSRDSEFSLP LGRRMSHAQH DARLLNAKVI PKQLGKAGGG AAGGGCGAHA LMNPNAAKKK KKSQEKRQES KAAKTLSAIL LSFIITWTPY NILVLIKPLT TCSDCIPTEL WDFFYALCYI NSTINPMSYA LCNATFRRTY VRILTCKWHT RNREGMVRGV YN // ID ACPM_DROME STANDARD; PRT; 152 AA. AC Q94519; Q94520; Q9W0G8; Q9W0G9; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acyl carrier protein, mitochondrial precursor (ACP) (NADH-ubiquinone DE oxidoreductase 9.6 kDa subunit) (NADH-ubiquinone oxidoreductase acyl- DE carrier subunit). GN MTACP1 OR ND-ACC OR MTACP OR CG9160. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RA Ragone G., Caizzi R., Caggese C.; RT "Two forms of cDNA and the sequence of Drosophila melanogaster gene RT for acyl-carrier subunit of NADH:ubiquinone oxidoreductase show RT evidence of alternatively spliced forms."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; TISSUE=Testis; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CARRIER OF THE GROWING FATTY ACID CHAIN IN FATTY ACID CC BIOSYNTHESIS (BY SIMILARITY). CC -!- SUBUNIT: COMPLEX I IS COMPOSED OF ABOUT 45 DIFFERENT SUBUNITS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; Synonyms=A; CC IsoId=Q94519-1; Sequence=Displayed; CC Name=1; Synonyms=B; CC IsoId=Q94519-2; Sequence=VSP_000148; CC -!- SIMILARITY: CONTAINS 1 ACYL CARRIER DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ000879; CAA04368.1; -. DR EMBL; AJ000879; CAA04369.1; -. DR EMBL; Y09068; CAA70289.1; -. DR EMBL; Y09069; CAA70290.1; -. DR EMBL; AE003471; AAF47479.1; -. DR EMBL; AE003471; AAF47480.1; -. DR EMBL; AY089404; AAL90142.1; -. DR HSSP; P80643; 1HY8. DR FlyBase; FBgn0011361; mtacp1. DR InterPro; IPR003231; Acyl_carrier. DR InterPro; IPR006163; Pp_bind. DR InterPro; IPR006162; Ppantne_S. DR Pfam; PF00550; pp-binding; 1. DR ProDom; PD000887; Acyl_carrier; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; FALSE_NEG. DR PROSITE; PS50075; ACP_DOMAIN; 1. KW Fatty acid biosynthesis; Phosphopantetheine; Mitochondrion; KW Transit peptide; Oxidoreductase; Alternative splicing. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 152 ACYL CARRIER PROTEIN. FT BINDING 108 108 PHOSPHOPANTETHEINE (POTENTIAL). FT VARSPLIC 51 92 ECRGRWQTQLVRKYSAKPPLSLKLINERVLLVLKLYDKIDP FT S -> KFGVRSYSAKSTIEDIKFRVLKVVSAYDKVTAE FT (in isoform 1). FT /FTId=VSP_000148. FT CONFLICT 63 63 K -> R (IN REF. 3). SQ SEQUENCE 152 AA; 17235 MW; 79C79A8BE1512A54 CRC64; MSFTQIARSC SRLAATLAPR RVASGILIQS QASRMMHRIA VPSMTSQLSQ ECRGRWQTQL VRKYSAKPPL SLKLINERVL LVLKLYDKID PSKLNVESHF INDLGLDSLD HVEVIMAMED EFGFEIPDSD AEKLLKPADI IKYVADKEDV YE // ID ACSA_DROME STANDARD; PRT; 670 AA. AC Q9VP61; Q24226; Q8IH30; Q9VP60; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acetyl-coenzyme A synthetase (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl- DE activating enzyme) (Acetyl-CoA synthetase) (ACS) (AceCS). GN ACCOAS OR CG9390. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B). RA Russell S.R., Heimbeck G.M., Carpenter A.T., Ashburner M.; RT "A Drosophila melanogaster acetyl-CoA-synthetase gene."; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ACTIVATES ACETATE SO THAT IT CAN BE USED FOR LIPID CC SYNTHESIS OR FOR ENERGY GENERATION. CC -!- CATALYTIC ACTIVITY: ATP + ACETATE + COA = AMP + DIPHOSPHATE + CC ACETYL-COA. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q9VP61-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9VP61-2; Sequence=VSP_008310; CC -!- SIMILARITY: BELONGS TO THE ATP-DEPENDENT AMP-BINDING ENZYME CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z46786; CAA86738.1; ALT_INIT. DR EMBL; AE003594; AAF51695.1; -. DR EMBL; AE003594; AAF51696.3; -. DR EMBL; AY089540; AAL90278.1; -. DR EMBL; BT001456; AAN71211.1; -. DR FlyBase; FBgn0012034; AcCoAS. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Alternative splicing; Ligase. FT VARSPLIC 1 146 Missing (in isoform B). FT /FTId=VSP_008310. FT CONFLICT 227 227 C -> S (IN REF. 1). FT CONFLICT 326 326 A -> G (IN REF. 2). SQ SEQUENCE 670 AA; 75959 MW; CE24364755CDBFFC CRC64; MPAEKSIYDP NPAISQNAYI SSFEEYQKFY QESLDNPAEF WSRVAKQFHW ETPADQDKFL KYNFNISKGP ISIKWMEGAS TNLCYNLLDR NVRNGLGDQI AYYWEGNHPD DYSRGLTYRK LLEEVCRFAN VLKDHGIRKG DRVSIYMPMI LELPIAMLAC ARIGAVHSIV FAGFSPDSLA ERMFDCKAKL LITADGAWRG EKPLYLKALC DTALEKVEEM GHSVEKCIVV SHLKRVTPCQ PDHVEEEIPW TDDRDYWWHE EMEDKEPACY PEWMDAEDPL FMLYTSGSTG KPKGVLHTTA GYLLYAATTF KIVFDYKPGD IYWCTADVGW ITGHTYVVYG PLANGATSVI FEGTPFFPGN DRYWSVIDKY KVTQFYTAPT AIRALMKFGE GPVLKHNLSG LKVLGSVGEP INPEAWLWYY KYIGKEQCSI VDTFWQTETG GHVITPLPGA TPMKPGSASF PFFGVKPTLL DECGIEIKGE GEGYLVFSQP WPGMMRTLYN NHERFEDTYF SKFPGYYCTG DGARRDADGY LWITGRVDDM LNVSGHLMST AEVESVLTEH PRVAESAVVS RPHPVKGECL YCFITPNENE VFDQKLISDL KKMVRERIGP FAMPDVIQNA PGLPKTRSGK IMRRVLRKIA VNDRNVGDTS TLADEQIVEQ LFANRPVEAK // ID ACT1_DROME STANDARD; PRT; 376 AA. AC P10987; Q24227; Q9U5X7; Q9W460; DT 01-JUL-1989 (Rel. 11, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin-5C. GN ACT5C OR CG4027. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-84 AND 324-376 FROM N.A. RX MEDLINE=88112795; PubMed=3123314; RA Vigoreaux J.O., Tobin S.L.; RT "Stage-specific selection of alternative transcriptional initiation RT sites from the 5C actin gene of Drosophila melanogaster."; RL Genes Dev. 1:1161-1171(1987). RN [4] RP SEQUENCE OF 1-75 FROM N.A. RX MEDLINE=81210174; PubMed=6263481; RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RT "The actin genes of Drosophila: protein coding regions are highly RT conserved but intron positions are not."; RL Cell 24:107-116(1981). RN [5] RP SEQUENCE OF 1-12 FROM N.A. RX MEDLINE=87064499; PubMed=3097509; RA Bond B.J., Davidson N.; RT "The Drosophila melanogaster actin 5C gene uses two transcription RT initiation sites and three polyadenylation sites to express multiple RT mRNA species."; RL Mol. Cell. Biol. 6:2080-2088(1986). RN [6] RP SEQUENCE OF 366-376 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88193084; PubMed=2896018; RA Rao J.P., Zafar R.S., Sodja A.; RT "Transcriptional activity at the 3' end of the actin gene at 5C on the RT X chromosome of Drosophila melanogaster."; RL Biochim. Biophys. Acta 950:30-44(1988). CC -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED CC IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED CC IN ALL EUKARYOTIC CELLS. CC -!- FUNCTION: MULTIPLE ISOFORMS ARE INVOLVED IN VARIOUS CELLULAR CC FUNCTIONS SUCH AS CYTOSKELETON STRUCTURE, CELL MOBILITY, CC CHROMOSOME MOVEMENT AND MUSCLE CONTRACTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: IN DROSOPHILA THERE ARE 6 CLOSELY RELATED ACTIN CC GENES. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K00667; AAA28316.1; -. DR EMBL; AE003435; AAF46098.1; -. DR EMBL; X06383; CAA29681.1; -. DR EMBL; X06384; CAB61444.1; -. DR EMBL; M13587; AAA28315.1; -. DR EMBL; X07627; CAA30474.1; -. DR PIR; A28258; A28258. DR HSSP; P02570; 2BTF. DR FlyBase; FBgn0000042; Act5C. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Multigene family; Acetylation. FT PROPEP 1 2 REMOVED IN MATURE FORM (BY SIMILARITY). FT CHAIN 3 376 ACTIN-5C. FT MOD_RES 3 3 ACETYLATION (BY SIMILARITY). FT CONFLICT 264 264 Q -> H (IN REF. 1). FT CONFLICT 272 272 A -> S (IN REF. 1). FT CONFLICT 350 350 L -> S (IN REF. 1). FT CONFLICT 358 358 I -> T (IN REF. 1). FT CONFLICT 366 367 SG -> AW (IN REF. 6). SQ SEQUENCE 376 AA; 41822 MW; BDAF13C191BB1BBC CRC64; MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YELPDGQVIT IGNERFRCPE ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK QEYDESGPSI VHRKCF // ID ACT2_DROME STANDARD; PRT; 376 AA. AC P02572; Q24228; Q9V9J4; DT 21-JUL-1986 (Rel. 01, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin-42A. GN ACT42A OR CG12051. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Burn T.C., Tobin S.L.; RL Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 1-160 AND 229-376 FROM N.A. RX MEDLINE=81210174; PubMed=6263481; RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RT "The actin genes of Drosophila: protein coding regions are highly RT conserved but intron positions are not."; RL Cell 24:107-116(1981). RN [5] RP SEQUENCE OF 1-12 FROM N.A. RX MEDLINE=87174783; PubMed=2436146; RA Couderc J.L., Hilal L., Sobier M.L., Dastugue B.; RT "20-Hydroxyecdysone regulates cytoplasmic actin gene expression in RT Drosophila cultured cells."; RL Nucleic Acids Res. 15:2549-2561(1987). RN [6] RP TISSUE SPECIFICITY. RX MEDLINE=90298579; PubMed=1694472; RA Tobin S.L., Cook P.J., Burn T.C.; RT "Transcripts of individual Drosophila actin genes are differentially RT distributed during embryogenesis."; RL Dev. Genet. 11:15-26(1990). CC -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED CC IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED CC IN ALL EUKARYOTIC CELLS. CC -!- FUNCTION: MULTIPLE ISOFORMS ARE INVOLVED IN VARIOUS CELLULAR CC FUNCTIONS SUCH AS CYTOSKELETON STRUCTURE, CELL MOBILITY, CC CHROMOSOME MOVEMENT AND MUSCLE CONTRACTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: ALL CELLS AND TISSUES OF THE DEVELOPING CC EMBRYO. LATER IN DEVELOPMENT, EXPRESSION IS HIGHER IN MIDGUT, CC BRAIN, NERVE CORD, AND GONADS. CC -!- INDUCTION: BY 20-HYDROXYECDYSONE. CC -!- MISCELLANEOUS: IN DROSOPHILA THERE ARE 6 CLOSELY RELATED ACTIN CC GENES. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K00670; AAA28314.1; -. DR EMBL; X54848; CAA38618.1; -. DR EMBL; AE003784; AAF57294.1; -. DR EMBL; X05176; CAA28809.1; -. DR PIR; A03000; A03000. DR PIR; S14851; S14851. DR HSSP; P02570; 2BTF. DR FlyBase; FBgn0000043; Act42A. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Multigene family; Acetylation. FT PROPEP 1 2 REMOVED IN MATURE FORM (BY SIMILARITY). FT CHAIN 3 376 ACTIN-42A. FT MOD_RES 3 3 ACETYLATION (BY SIMILARITY). FT CONFLICT 12 287 MISSING (IN REF. 2). FT CONFLICT 275 275 I -> L (IN REF. 1). SQ SEQUENCE 376 AA; 41823 MW; 7C6D13CC6E42331E CRC64; MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YELPDGQVIT IGNERFRCPE SLFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL SGGTTMYPGI ADRMQKEITA LAPSTMKIKI VAPPERKYSV WIGGSILASL STFQQMWISK QEYDESGPSI VHRKCF // ID ACT3_DROME STANDARD; PRT; 376 AA. AC P53501; Q9W2Q0; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin 57B. GN ACT57B OR CG10067. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=81210174; PubMed=6263481; RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RT "The actin genes of Drosophila: protein coding regions are highly RT conserved but intron positions are not."; RL Cell 24:107-116(1981). RN [2] RP SEQUENCE FROM N.A. RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RL Submitted (JUN-1985) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED CC IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED CC IN ALL EUKARYOTIC CELLS. CC -!- FUNCTION: MULTIPLE ISOFORMS ARE INVOLVED IN VARIOUS CELLULAR CC FUNCTIONS SUCH AS CYTOSKELETON STRUCTURE, CELL MOBILITY, CC CHROMOSOME MOVEMENT AND MUSCLE CONTRACTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: IN DROSOPHILA THERE ARE 6 CLOSELY RELATED ACTIN CC GENES. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K00673; AAA28319.1; -. DR EMBL; K00672; AAA28319.1; JOINED. DR EMBL; AE003452; AAF46640.1; -. DR HSSP; P02570; 2BTF. DR FlyBase; FBgn0000044; Act57B. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Multigene family; Acetylation. FT PROPEP 1 2 REMOVED IN MATURE FORM (BY SIMILARITY). FT CHAIN 3 376 ACTIN-57A. FT MOD_RES 3 3 ACETYLATION (BY SIMILARITY). SQ SEQUENCE 376 AA; 41835 MW; 88F72F339A2B0DF1 CRC64; MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS YELPDGQVIT IGNERFRCPE SLFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANIVM SGGTTMYPGI ADRMQKEITS LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK EEYDESGPGI VHRKCF // ID ACT4_DROME STANDARD; PRT; 376 AA. AC P02574; Q9VNW5; DT 21-JUL-1986 (Rel. 01, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin, larval muscle (Actin-79B). GN ACT79B OR CG7478. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83189087; PubMed=6405041; RA Sanchez F., Tobin S.L., Rdest U., Zulauf E., McCarthy B.J.; RT "Two Drosophila actin genes in detail. Gene structure, protein RT structure and transcription during development."; RL J. Mol. Biol. 163:533-551(1983). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED CC IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED CC IN ALL EUKARYOTIC CELLS. CC -!- FUNCTION: MULTIPLE ISOFORMS ARE INVOLVED IN VARIOUS CELLULAR CC FUNCTIONS SUCH AS CYTOSKELETON STRUCTURE, CELL MOBILITY, CC CHROMOSOME MOVEMENT AND MUSCLE CONTRACTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: IN DROSOPHILA THERE ARE 6 CLOSELY RELATED ACTIN CC GENES. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18827; AAA28317.1; -. DR EMBL; M18828; AAA28317.1; JOINED. DR EMBL; M18829; AAA28318.1; -. DR EMBL; AE003596; AAF51800.1; -. DR HSSP; P02570; 2BTF. DR FlyBase; FBgn0000045; Act79B. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Muscle protein; Multigene family; Acetylation. FT PROPEP 1 2 REMOVED IN MATURE FORM (BY SIMILARITY). FT CHAIN 3 376 ACTIN, LARVAL MUSCLE. FT MOD_RES 3 3 ACETYLATION (BY SIMILARITY). FT CONFLICT 185 185 D -> H (IN REF. 1; AAA28318). FT CONFLICT 326 326 I -> M (IN REF. 1). SQ SEQUENCE 376 AA; 41786 MW; D08BB1B42DE86B94 CRC64; MCDEEASALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDCYVGDEAQ SKRGILSLKY PIEHGIITNW DDMEKVWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS YELPDGQVIT IGNERFRTPE ALFQPSFLGM ESCGIHETVY QSIMKCDVDI RKDLYANNVL SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK QEYDESGPGI VHRKCF // ID ACT5_DROME STANDARD; PRT; 376 AA. AC P10981; Q8MZ23; Q9VFU9; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin-87E. GN ACT87E OR CG18290. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88284330; PubMed=2840338; RA Manseau L.J., Ganetzky B., Craig E.A.; RT "Molecular and genetic characterization of the Drosophila RT melanogaster 87E actin gene region."; RL Genetics 119:407-420(1988). RN [2] RP SEQUENCE FROM N.A. RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED CC IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED CC IN ALL EUKARYOTIC CELLS. CC -!- FUNCTION: MULTIPLE ISOFORMS ARE INVOLVED IN VARIOUS CELLULAR CC FUNCTIONS SUCH AS CYTOSKELETON STRUCTURE, CELL MOBILITY, CC CHROMOSOME MOVEMENT AND MUSCLE CONTRACTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: IN DROSOPHILA THERE ARE 6 CLOSELY RELATED ACTIN CC GENES. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12452; CAA30982.1; -. DR EMBL; K00674; AAA28320.1; -. DR EMBL; AE003700; AAF54950.2; -. DR EMBL; AY113405; AAM29410.1; ALT_SEQ. DR EMBL; AY089587; AAL90325.1; -. DR PIR; S04538; S04538. DR HSSP; P02570; 2BTF. DR FlyBase; FBgn0000046; Act87E. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Multigene family; Acetylation. FT PROPEP 1 2 REMOVED IN MATURE FORM (BY SIMILARITY). FT CHAIN 3 376 ACTIN-87E. FT MOD_RES 3 3 ACETYLATION (BY SIMILARITY). SQ SEQUENCE 376 AA; 41802 MW; 60252541882B0A7F CRC64; MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNA PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS YELPDGQVIT IGNERFRCPE SLFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANIVM SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK QEYDESGPGI VHRKCF // ID ACT6_DROME STANDARD; PRT; 376 AA. AC P02575; P45893; Q9VF62; DT 21-JUL-1986 (Rel. 01, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin, indirect flight muscle (Actin-88F). GN ACT88F OR CG5178. OS Drosophila melanogaster (Fruit fly), OS Drosophila simulans (Fruit fly), and OS Bactrocera dorsalis (Oriental fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7240, 27457; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RL Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=83189087; PubMed=6405041; RA Sanchez F., Tobin S.L., Rdest U., Zulauf E., McCarthy B.J.; RT "Two Drosophila actin genes in detail. Gene structure, protein RT structure and transcription during development."; RL J. Mol. Biol. 163:533-551(1983). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RA Okamoto H., Hiromi Y., Ishikawa E., Yamada T., Isoda K., RA Maekawa H., Hotta Y.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 1-53 FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=81210174; PubMed=6263481; RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RT "The actin genes of Drosophila: protein coding regions are highly RT conserved but intron positions are not."; RL Cell 24:107-116(1981). RN [6] RP SEQUENCE OF 302-356 FROM N.A. (MUTANT IFM(3)7). RC SPECIES=D.melanogaster; RX MEDLINE=85024863; PubMed=6488317; RA Karlik C.C., Coutu M.D., Fyrberg E.A.; RT "A nonsense mutation within the act88F actin gene disrupts myofibril RT formation in Drosophila indirect flight muscles."; RL Cell 38:711-719(1984). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=D.simulans; RX MEDLINE=92380500; PubMed=1511890; RA Beifuss M.J., Durica D.S.; RT "Sequence analysis of the indirect flight muscle actin-encoding gene RT of Drosophila simulans."; RL Gene 118:163-170(1992). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=B.dorsalis; STRAIN=Puna; RX MEDLINE=95038779; PubMed=7951267; RA He M., Haymer D.S.; RT "The actin gene family in the oriental fruit fly Bactrocera dorsalis. RT Muscle specific actins."; RL Insect Biochem. Mol. Biol. 24:891-906(1994). CC -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED CC IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED CC IN ALL EUKARYOTIC CELLS. CC -!- FUNCTION: MULTIPLE ISOFORMS ARE INVOLVED IN VARIOUS CELLULAR CC FUNCTIONS SUCH AS CYTOSKELETON STRUCTURE, CELL MOBILITY, CC CHROMOSOME MOVEMENT AND MUSCLE CONTRACTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: MUSCLE. CC -!- MISCELLANEOUS: ABNORMALITIES IN IFM(3)7 FLIGHT MUSCLES RESULT FROM CC INCORPORATION OF THE MUTANT ACTIN ISOFORM INTO ASSEMBLING CC MYOFIBRILS. CC -!- MISCELLANEOUS: IN DROSOPHILA THERE ARE 6 CLOSELY RELATED ACTIN CC GENES. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18826; AAA28323.1; -. DR EMBL; K02065; AAA28322.1; -. DR EMBL; AB003910; BAA20058.1; -. DR EMBL; AE003709; AAF55198.1; -. DR EMBL; M18830; AAA28321.1; -. DR EMBL; M87274; -; NOT_ANNOTATED_CDS. DR EMBL; L12253; AAA62341.1; -. DR PIR; A03003; ATFF8. DR PIR; JC1246; JC1246. DR HSSP; P02570; 1HLU. DR FlyBase; FBgn0000047; Act88F. DR FlyBase; FBgn0012823; Dsim\Act88F. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Muscle protein; Multigene family; Acetylation. FT PROPEP 1 2 REMOVED IN MATURE FORM (BY SIMILARITY). FT CHAIN 3 376 ACTIN, INDIRECT FLIGHT MUSCLE. FT MOD_RES 3 3 ACETYLATION (BY SIMILARITY). FT VARIANT 357 376 MISSING (IN MUTANT IFM(3)7). FT CONFLICT 200 200 S -> T (IN REF. 2). FT CONFLICT 213 213 I -> T (IN REF. 2). FT CONFLICT 226 226 Q -> D (IN REF. 2). FT CONFLICT 320 320 A -> T (IN REF. 2). FT CONFLICT 345 345 S -> L (IN REF. 2). FT CONFLICT 369 369 G -> S (IN REF. 2). SQ SEQUENCE 376 AA; 41699 MW; C64C33A1674B7886 CRC64; MCDDDAGALV IDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGF ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANSVL SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK QEYDESGPGI VHRKCF // ID ACTU_DROME STANDARD; PRT; 398 AA. AC P45890; Q9VXQ9; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin-like protein 13E (Actin-related protein 6) (dArp6). GN ACTR13E OR ACRP OR CG11678. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94141930; PubMed=8308899; RA Frankel S., Heintzelman M.B., Artavanis-Tsakonas S., Mooseker M.S.; RT "Identification of a divergent actin-related protein in Drosophila."; RL J. Mol. Biol. 235:1351-1356(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: NUCLEAR. LOCALIZED ON CENTRIC CC HETEROCHROMATIN. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. ARP6 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L25314; AAA17685.1; -. DR EMBL; AE003500; AAF48499.1; -. DR EMBL; AY058726; AAL13955.1; -. DR PIR; S44028; S44028. DR FlyBase; FBgn0011741; Actr13E. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR SMART; SM00268; ACTIN; 1. KW Structural protein; Cytoskeleton; Nuclear protein. SQ SEQUENCE 398 AA; 45414 MW; 71905627B3F0FC05 CRC64; MANAVVVLDN GAHTAKVGLA NQDEPHVVPN CIMKAKSERR RAFVGNQIDE CRDTSALYYI LAFQRGYLLN WHTQKTVWDY IFSKDGIGCS LENRNIVITE PQMNFQSIQE ATLEILFEEY KVDGVYKTTA ADLAAFNYVA DSEERTTMES LNCIIIDVGY SFTHVVPFVL GRRVLQGIRR IDMGGKALTN QLKELISYRH LNVMDESHVV NQIKEDVCFV AEDFKQAMQV HYSEEKRREV TVDYVLPDFT TVKRGYVRVP GKPREDEEQQ QMVSLCNERF TVPELLFNPS DIGVQQVGIP EAVADCLKAC PWEAHRELLL NILIVGGSAQ FPGFLPRLKR DLRALVPDDL EVSLICPEDP VRYAWYGGKE VATSPNFEEF VYTQDDYEEY GFQGINQR // ID ACTY_DROME STANDARD; PRT; 376 AA. AC P45891; Q9V7T9; DT 01-NOV-1995 (Rel. 32, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin-like protein 53D. GN ARP53D OR ACTR53D OR CG5409. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94343534; PubMed=8064864; RA Fyrberg C., Ryan L., Kenton M., Fyrberg E.A.; RT "Genes encoding actin-related proteins of Drosophila melanogaster."; RL J. Mol. Biol. 241:498-503(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: TESTIS SPECIFIC. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. ARP1 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78487; CAA55239.1; -. DR EMBL; AE003805; AAF57954.1; -. DR PIR; S47986; S47986. DR FlyBase; FBgn0011743; Arp53D. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Cytoskeleton. FT CONFLICT 63 66 AAAR -> RQPE (IN REF. 1). FT CONFLICT 148 149 YA -> CT (IN REF. 1). SQ SEQUENCE 376 AA; 42030 MW; BD4860016F4E2259 CRC64; MSSEVDSNSH HAAVVIDNGS GVCKAGFSPE DTPRAVFPSI VGRPRHLNVL LDSVIGDSVI GEAAARKRGI LTLKYPIEHG MVKNWDEMEM VWQHTYELLR ADPMDLPALL TEAPLNPKKN REKMTEIMFE HFQVPAFYVA VQAVLSLYAT GRTVGIVVDS GDGVTHTVPI YEGFALPHAC VRVDLAGRDL TDYLCKLLLE RGVTMGTSAE REIVREIKEK LCYVSMNYAK EMDLHGKVET YELPDGQKIV LGCERFRCPE ALFQPSLLGQ EVMGIHEATH HSITNCDMDL RKDMYANIVL SGGTTMFRNI EHRFLQDLTE MAPPSIRIKV NASPDRRFSV WTGGSVLASL TSFQNMWIDS LEYEEVGSAI VHRKCF // ID ACTZ_DROME STANDARD; PRT; 376 AA. AC P45889; Q9VG37; DT 01-NOV-1995 (Rel. 32, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin-like protein 87C. GN ARP87C OR ACTR87C OR CG6174. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94343534; PubMed=8064864; RA Fyrberg C., Ryan L., Kenton M., Fyrberg E.A.; RT "Genes encoding actin-related proteins of Drosophila melanogaster."; RL J. Mol. Biol. 241:498-503(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. ARP1 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78488; CAA55240.1; -. DR EMBL; AE003696; AAF54853.1; -. DR EMBL; AY070666; AAL48137.1; -. DR PIR; S47988; S47988. DR FlyBase; FBgn0011745; Arp87C. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Cytoskeleton. FT CONFLICT 261 262 VL -> AV (IN REF. 1). SQ SEQUENCE 376 AA; 42719 MW; EC7ACFE7A5F99962 CRC64; MEPYDVVVNQ PVVIDNGSGV IKAGFAGEHI PKCRFPNYIG RPKHVRVMAG ALEGDIFVGP KAEEHRGLLS IRYPMEHGIV TDWNDMERIW SYIYSKEQLA TFTEDHPVLL TEAPLNPRRN REKAAEFFFE GINAPALFVS MQAVLSLYAT GRVTGVVLDS GDGVTHAVPI YEGFAMPHSI MRVDIAGRDV TRYLKTLIRR EGFNFRSTAE FEIVRSIKEK VCYLATNPQK EETVETEKFA YKLPDGKIFE IGPARFRAPE VLFRPDLLGE ECEGIHDVLM YSIEKSDMDL RKMLYQNIVL SGGSTLFKGF GDRLLSELKK HSAKDLKIRI AAPQERLYST WMGGSILASL DTFKKMWISK REYEEEGQKA VHRKTF // ID ACYP_DROME STANDARD; PRT; 119 AA. AC P56544; Q9V3K1; DT 15-JUL-1998 (Rel. 36, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acylphosphatase (EC 3.6.1.7) (Acylphosphate phosphohydrolase). GN ACYP OR ACP OR ACPDRO OR CG16870. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98416044; PubMed=9744795; RA Pieri A., Magherini F., Liguri G., Raugei G., Taddei N., RA Bozzetti M.P., Cecchi C., Ramponi G.; RT "Drosophila melanogaster acylphosphatase: a common ancestor for RT acylphosphatase isoenzymes of vertebrate species."; RL FEBS Lett. 433:205-210(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: AN ACYL PHOSPHATE + H(2)O = A FATTY ACID ANION CC + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- MISCELLANEOUS: OPTIMUM PH IS 5.3-6.3. CC -!- SIMILARITY: BELONGS TO THE ACYLPHOSPHATASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ243543; CAB48386.1; -. DR EMBL; AE003408; AAF44835.1; -. DR EMBL; AE003641; AAF53355.1; -. DR HSSP; P00818; 1APS. DR FlyBase; FBgn0025115; Acyp. DR InterPro; IPR001792; Acylphosphatase. DR Pfam; PF00708; Acylphosphatase; 1. DR PRINTS; PR00112; ACYLPHPHTASE. DR ProDom; PD001884; Acylphosphatase; 1. DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1. DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1. KW Acetylation; Hydrolase. FT INIT_MET 0 0 BY SIMILARITY. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT ACT_SITE 22 22 POTENTIAL. FT ACT_SITE 40 40 POTENTIAL. SQ SEQUENCE 119 AA; 13566 MW; 803197175FA37795 CRC64; ATHNVHSCEF EVFGRVQGVN FRRHALRKAK TLGLRGWCMN SSRGTVKGYI EGRPAEMDVM KEWLRTTGSP LSSIEKVEFS SQRERDRYGY ANFHIKPDPH ENRPVHEGLG SSSSHHDSN // ID ADA_DROME STANDARD; PRT; 940 AA. AC P91926; O01937; Q86P64; Q9VPP4; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-adaptin homolog. GN ALPHA-ADAPTIN OR CG4260. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=97236497; PubMed=9118220; RA Gonzalez-Gaitan M.A., Jaeckle H.; RT "Role of Drosophila alpha-adaptin in presynaptic vesicle recycling."; RL Cell 88:767-776(1997). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=97431776; PubMed=9285813; RA Dornan S.C., Jackson A.P., Gay N.J.; RT "Alpha-adaptin, a marker for endocytosis, is expressed in complex RT patterns during Drosophila development."; RL Mol. Biol. Cell 8:1391-1403(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 93-940 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ADAPTINS ARE COMPONENTS OF THE ADAPTER COMPLEXES CC WHICH LINK CLATHRIN TO RECEPTORS IN COATED VESICLES. CLATHRIN- CC ASSOCIATED PROTEIN COMPLEXES ARE BELIEVED TO INTERACT WITH THE CC CYTOPLASMIC TAILS OF MEMBRANE PROTEINS, LEADING TO THEIR SELECTION CC AND CONCENTRATION. ALPHA ADAPTIN IS A SUBUNIT OF THE PLASMA CC MEMBRANE ADAPTER (BY SIMILARITY). CC -!- SUBUNIT: ASSEMBLY PROTEIN COMPLEX 2 (AP-2) IS A HETEROTETRAMER CC COMPOSED OF TWO LARGE CHAINS (ALPHA AND BETA), A MEDIUM CHAIN CC (AP50) AND A SMALL CHAIN (AP17). CC -!- SUBCELLULAR LOCATION: COMPONENT OF THE COAT SURROUNDING THE CC CYTOPLASMIC FACE OF COATED VESICLES IN THE PLASMA MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ADAPTOR COMPLEXES LARGE SUBUNIT CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11104; CAA71991.1; -. DR EMBL; Y13092; CAA73533.1; -. DR EMBL; AE003589; AAF56103.2; -. DR EMBL; BT003458; AAO39461.1; ALT_INIT. DR FlyBase; FBgn0015567; alpha-Adaptin. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR InterPro; IPR008152; A/G_adapt_C. DR InterPro; IPR002553; Adaptin_N. DR InterPro; IPR003164; Alpha_adaptin_C. DR InterPro; IPR009028; AP2_adap_app. DR InterPro; IPR008938; ARM. DR Pfam; PF01602; Adaptin_N; 1. DR Pfam; PF02296; Alpha_adaptin_C; 1. DR Pfam; PF02883; Alpha_adaptinC2; 1. KW Coated pits. FT DOMAIN 644 715 ASN-RICH. FT CONFLICT 207 207 T -> A (IN REF. 5). FT CONFLICT 325 325 N -> E (IN REF. 2). FT CONFLICT 489 489 A -> P (IN REF. 2). FT CONFLICT 587 587 S -> N (IN REF. 2). FT CONFLICT 708 708 MISSING (IN REF. 2). FT CONFLICT 711 712 LF -> VS (IN REF. 2). FT CONFLICT 722 723 EM -> GK (IN REF. 2). FT CONFLICT 741 743 LFY -> FSN (IN REF. 2). FT CONFLICT 877 877 Q -> P (IN REF. 2). SQ SEQUENCE 940 AA; 105619 MW; F745045CD2C1D9C5 CRC64; MAPVRGDGMR GLAVFISDIR NCKSKEAEVK RINKELANIR SKFKGDKTLD GYQKKKYVCK LLFIFLLGHD IDFGHMEAVN LLSSNKYSEK QIGYLFISVL VNTNSDLIRL IIQSIKNDLQ SRNPVHVNLA LQCIANIGSR DMAESFSNEI PKLLVSGDTM DVVKQSAALC LLRLFRSSPD IIPGGEWTSR IIHLLNDQHM GVVTAATSLI DALVKRNPDE YKGCVNLAVS RLSRIVTASY TDLQDYTYYF VPAPWLSVKL LRLLQNYNPV TEEAGVRARL NETLETILNK AQEPPKSKKV QHSNAKNAVL FEAINLIIHS DSEPNLLVRA CNQLGQFLSN RETNLRYLAL ESMCHLATSE FSHEEVKKHQ EVVILSMKME KDVSVRQMAV DLLYAMCDRG NAEEIVQEML NYLETADYSI REEMVLKVAI LAEKYATDYT WYVDVILNLI RIAGDYVSEE VWYRVIQIVI NREEVQGYAA KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDSRSAPL VQFKLLHSKY HLCSPMTRAL LLSTYIKFIN LFPEIRTNIQ DVFRQHSNLR SADAELQQRA SEYLQLSIVA STDVLATVLE EMPSFPERES SILAVLKKKK PGRVPENEIR ESKSPAPLTS AAQNNALVNN SHSKLNNSNA NTDLLGLSTP PSNNIGSGSN SNSTLIDVLG DMYGSNSNNN SSAVYNTKKF LFKNNGVLFE NEMLQIGVKS EFRQNLGRLG LFYGNKTQVP LTNFNPVLQW SAEDALKLNV QMKVVEPTLE AGAQIQQLLT AECIEDYADA PTIEISFRYN GTQQKFSIKL PLSVNKFFEP TEMNAESFFA RWKNLSGEQQ RSQKVFKAAQ PLDLPGARNK LMGFGMQLLD QVDPNPDNMV CAGIIHTQSQ QVGCLMRLEP NKQAQMFRLT VRASKETVTR EICDLLTDQF // ID ADD_DROME STANDARD; PRT; 1034 AA. AC P54362; O16015; O45031; Q9VY96; DT 01-OCT-1996 (Rel. 34, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable delta-adaptin (Garnet protein) (Delta adaptin subunit of AP- DE 3). GN G OR CG10986/CG11197. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97447555; PubMed=9303295; RA Ooi C.E., Moreira J.E., Dell'Angelica E.C., Poy G., Wassarman D.A., RA Bonifacino J.S.; RT "Altered expression of a novel adaptin leads to defective pigment RT granule biogenesis in the Drosophila eye color mutant garnet."; RL EMBO J. 16:4508-4518(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20123182; PubMed=10659786; RA Lloyd V.K., Sinclair D.A., Wennberg R., Warner T.S., Honda B.M., RA Grigliatti T.A.; RT "A genetic and molecular characterization of the garnet gene of RT Drosophila melanogaster."; RL Genome 42:1183-1193(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Lloyd V.K.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PART OF THE AP-3 COMPLEX, AN ADAPTER-RELATED COMPLEX CC WHICH IS NOT CLATHRIN-ASSOCIATED. THE COMPLEX IS ASSOCIATED WITH CC THE GOLGI REGION AS WELL AS MORE PERIPHERAL STRUCTURES. IT CC FACILITATES THE BUDDING OF VESICLES FROM THE GOLGI MEMBRANE AND CC MAY BE DIRECTLY INVOLVED IN TRAFFICKING TO LYSOSOMES (BY CC SIMILARITY). CC -!- FUNCTION: MAY BE A COAT PROTEIN INVOLVED IN THE FORMATION OF CC SPECIALIZED STRUCTURES LIKE PIGMENT GRANULES. CC -!- SUBUNIT: ASSEMBLY PROTEIN COMPLEX 3 (AP-3) IS A HETEROTETRAMER CC COMPOSED OF TWO LARGE CHAINS (DELTA AND BETA3), A MEDIUM CHAIN CC (MU3) AND A SMALL CHAIN (SIGMA3). CC -!- SUBCELLULAR LOCATION: COMPONENT OF THE COAT SURROUNDING THE CC CYTOPLASMIC FACE OF COATED VESICLES LOCATED AT THE GOLGI COMPLEX CC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ADAPTOR COMPLEXES LARGE SUBUNIT CC FAMILY. CC -!- CAUTION: SEQUENCES IN REF.2 AND REF.3 CONTAIN INTRONIC SEQUENCES CC AND ARE INCOMPLETE AT 5' AND 3' ENDS. SEQUENCES EXTENSIVELY DIFFER CC FROM THAT SHOWN AT POSITIONS 1-269, 546, AND 840-1034. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF002164; AAC14585.1; -. DR EMBL; AF044287; AAC01743.1; ALT_SEQ. DR EMBL; U31351; AAB97618.1; ALT_SEQ. DR EMBL; AE003493; AAF48307.2; -. DR FlyBase; FBgn0001087; g. DR GO; GO:0030123; C:AP-3 adaptor complex; NAS. DR GO; GO:0005783; C:endoplasmic reticulum; IDA. DR GO; GO:0005795; C:Golgi stack; IDA. DR GO; GO:0005798; C:Golgi vesicle; NAS. DR GO; GO:0008057; P:eye pigment granule morphogenesis (sensu Dr...; IMP. DR GO; GO:0006895; P:Golgi to endosome transport; NAS. DR GO; GO:0006727; P:ommochrome biosynthesis; IMP. DR InterPro; IPR002553; Adaptin_N. DR InterPro; IPR008938; ARM. DR Pfam; PF01602; Adaptin_N; 1. KW Golgi stack; Protein transport; Transport. FT DOMAIN 767 785 LYS-RICH. FT CONFLICT 395 395 D -> T (IN REF. 2). FT CONFLICT 423 423 L -> V (IN REF. 2). FT CONFLICT 442 445 QLLD -> RTTY (IN REF. 2). FT CONFLICT 461 465 MTNLL -> IDQSA (IN REF. 2). FT CONFLICT 694 695 QR -> GQ (IN REF. 2). FT CONFLICT 701 701 E -> D (IN REF. 1). FT CONFLICT 869 869 L -> S (IN REF. 4). FT CONFLICT 910 910 P -> S (IN REF. 4). SQ SEQUENCE 1034 AA; 114845 MW; ECE1B7A34DC5F8F1 CRC64; MALKKVKGNF FERMFDKNLT DLVRGIRNNK DNEAKYISTC IEEIKQELRQ DNISVKCNAV AKLTYIQMLG YDISWAGFNI IEVMSSSRFT CKRIGYLAAS QCFHPDSELL MLTTNMIRKD LNSQNQYDAG VALSGLSCFI SPDLSRDLAN DIMTLMSSTK PYLRMKAVLM MYKVFLRYPE ALRPAFPKLK EKLEDPDPGV QSAAVNVICE LARKNPKNYL PLAPIFFKLM TTSTNNWMLI KIIKLFGALT PLEPRLGKKL IEPLTNLIHS TSAMSLLYEC INTVIAVLIS ISSGMPNHSA SIQLCVQKLR ILIEDSDQNL KYLGLLAMSK ILKTHPKSVQ AHKDLILACL DDKDESIRLR ALDLLYGMVS KKNLMEIVKR LLGHMERAEG SAYRDELLYK VIEICAQSSY LYVTNFEWYL TVLVELIQLE AGSRHGRLIA EQLLDVAIRV PVVRQFAVNE MTNLLDTFTV SAQSNSMYEV LYAAAWIVGE FAGELEDAEK TLNILLRPRL LPGHIQGVYV QNVIKLFARL ATTCLELQDL PGLVTLCDHV LDKLQHFNGS SDIEVQERAN SACMLIEMLR NQLSTSTDAM AMDTTTEGGI PPLAIEIVQE MTLLFTGELI PVAPKAQRKV PLPDGLDLDE WINAPPPEDA ASSSSSEHDK DELFVSATQA GTGADGGEKR RQSLELTPEQ LERQRMARLI EQSNNPHYLK STPTASGASN ADQYDNIDDI PITELPLDME GVAALRVGIT KRSDKYLQEQ QAAQGSKDGK KKHKKGKKSK KAKNKVAYNS SSESEGEPKP LHIVNTTLDM PEGVSMSDSE DKDGKYDPND PHRALDIELD ITEFEAPAVR SASKKSAADK ENLKTPADLA GGGNAAKKDR KKDKDKDKER KVKREHRESK RERKEAAVQP VIDLIDADTP TPSPSHISAT SNNNNTSTVL PDAPKHHKKK KNKEKTTDEA PDALATATGS SIIDVGGEEA SEVASKVHKK KHKKEKSQRK EKKKASESAS VSAIVSIGDY EQPLGISTPS KEIL // ID ADF1_DROME STANDARD; PRT; 253 AA. AC P05552; Q9V9C4; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Transcription factor ADF-1 (ADH distal factor 1). GN ADF1 OR CG15845. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92115725; PubMed=1731341; RA England B.P., Admon A., Tjian R.; RT "Cloning of Drosophila transcription factor Adf-1 reveals homology to RT Myb oncoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 89:683-687(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP CHARACTERIZATION. RX MEDLINE=90202990; PubMed=2318884; RA England B.P., Heberlein U., Tjian R.; RT "Purified Drosophila transcription factor, Adh distal factor-1 RT (Adf-1), binds to sites in several Drosophila promoters and activates RT transcription."; RL J. Biol. Chem. 265:5086-5094(1990). CC -!- FUNCTION: MAY PLAY AN IMPORTANT ROLE NOT ONLY IN THE REGULATION OF CC ADH EXPRESSION BUT ALSO IN THE TRANSCRIPTION OF OTHER GENES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: O-GLYCOSYLATED; CONTAINS N-ACETYLGLUCOSAMINE SIDE CHAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37787; AAA28325.1; -. DR EMBL; AE003789; AAF57370.1; -. DR EMBL; AY069387; AAL39532.1; -. DR PIR; A38201; A38201. DR TRANSFAC; T00008; -. DR FlyBase; FBgn0000054; Adf1. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0008345; P:larval locomotory behavior; NAS. DR GO; GO:0007613; P:memory; IMP. DR GO; GO:0008355; P:olfactory learning; NAS. DR GO; GO:0007416; P:synaptogenesis; IMP. DR InterPro; IPR006578; MADF. DR SMART; SM00595; MADF; 1. KW Transcription regulation; DNA-binding; Nuclear protein. SQ SEQUENCE 253 AA; 29220 MW; 852B288E39B92DF9 CRC64; MDKLDANLEQ QFDLNLIEAV KLNPVIYDRS HYNYKHFVRK AQTWKQIAET LGVPEQKCTK RWKSLRDKFA REMKLCQESR WRYFKQMQFL VDSIRQYRES LLGKCANGSQ SANQVADPSQ QQQAQQQTVV DIFAQPFNGS ATTSAQALTH PHEITVTSDA QLATAVGKDQ KPYFYEPPLK RERSEEEHSD NMLNTIKIFQ NNVSQAVSAE DQSFGMVVTD MLNTLGVRQK AEAKVHIIKY LTDMQLLAQH NKY // ID ADHR_DROME STANDARD; PRT; 272 AA. AC P91615; Q24230; Q9VJS2; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alcohol dehydrogenase related 31 kDa protein. GN ADHR OR ADH-DUP OR CG3484. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91200630; PubMed=1673107; RA Kreitman M., Hudson R.R.; RT "Inferring the evolutionary histories of the Adh and Adh-dup loci in RT Drosophila melanogaster from patterns of polymorphism and RT divergence."; RL Genetics 127:565-582(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Brogna S., Ashburner M.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE SHORT-CHAIN DEHYDROGENASES/REDUCTASES CC (SDR) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78384; CAA55152.1; -. DR EMBL; X98338; CAA66982.1; -. DR EMBL; AE003644; AAF53404.1; -. DR HSSP; P10807; 1B16. DR FlyBase; FBgn0000056; Adhr. DR InterPro; IPR002198; ADH_short. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. KW Oxidoreductase. FT NP_BIND 11 34 NAD OR NADP (BY SIMILARITY). FT ACT_SITE 152 152 BY SIMILARITY. FT CONFLICT 127 127 M -> I (IN REF. 1). SQ SEQUENCE 272 AA; 30273 MW; 6FD2B13EEE2FAEA6 CRC64; MFDLTGKHVC YVADCGGIAL ETSKVLMTKN IAKLAILQST ENPQAIAQLQ SIKPSTQIFF WTYDVTMARE DMKKYFDEVM VQMDYIDVLI NGATLCDENN IDATINTNLT GMMNTVATVL PYMDRKMGGT GGLIVNVTSV IGLDPSPVFC AYSASKFGVI GFTRSLADPL YYSQNGVAVM AVCCGPTRVF VDRELKAFLE YGQSFADRLR RAPCQSTSVC GQNIVNAIER SENGQIWIAD KGGLELVKLH WYWHMADQFV HYMQSNDEED QD // ID ADHX_DROME STANDARD; PRT; 378 AA. AC P46415; Q9VGV2; DT 01-NOV-1995 (Rel. 32, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alcohol dehydrogenase class III (EC 1.1.1.1) (Glutathione-dependent DE formaldehyde dehydrogenase) (EC 1.2.1.1) (FDH) (FALDH) (Octanol DE dehydrogenase) (EC 1.1.1.73). GN FDH OR GFD OR ODH OR CG6598. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95045575; PubMed=7957234; RA Luque T., Atrian S., Danielsson O., Joernvall H., Gonzalez-Duarte R.; RT "Structure of the Drosophila melanogaster glutathione-dependent RT formaldehyde dehydrogenase/octanol dehydrogenase gene (class III RT alcohol dehydrogenase). Evolutionary pathway of the alcohol RT dehydrogenase genes."; RL Eur. J. Biochem. 225:985-993(1994). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=94255452; PubMed=8197167; RA Danielsson O., Atrian S., Luque T., Hjelmqvist L., Gonzalez-Duarte R., RA Joernvall H.; RT "Fundamental molecular differences between alcohol dehydrogenase RT classes."; RL Proc. Natl. Acad. Sci. U.S.A. 91:4980-4984(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CLASS-III ADH IS REMARKABLY INEFFECTIVE IN OXIDIZING CC ETHANOL, BUT IT READILY CATALYZES THE OXIDATION OF LONG-CHAIN CC PRIMARY ALCOHOLS AND THE OXIDATION OF S-(HYDROXYMETHYL) CC GLUTATHIONE. CC -!- CATALYTIC ACTIVITY: AN ALCOHOL + NAD(+) = AN ALDEHYDE OR KETONE + CC NADH. CC -!- CATALYTIC ACTIVITY: FORMALDEHYDE + GLUTATHIONE + NAD(+) = S- CC FORMYLGLUTATHIONE + NADH. CC -!- CATALYTIC ACTIVITY: 1-OCTANOL + NAD(+) = 1-OCTANAL + NADH. CC -!- COFACTOR: BINDS 2 ZINC IONS PER SUBUNIT (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ZINC-CONTAINING ALCOHOL DEHYDROGENASE CC FAMILY. CLASS-III SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U07799; AAA57187.1; -. DR EMBL; U07641; AAB02520.1; -. DR EMBL; AE003689; AAF54571.1; -. DR PIR; S51357; S51357. DR HSSP; P11766; 1TEH. DR FlyBase; FBgn0011768; Fdh. DR GO; GO:0004327; F:formaldehyde dehydrogenase (glutathione) ac...; IDA. DR InterPro; IPR002328; ADH_zinc. DR InterPro; IPR002085; Adh_zn_family. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS00059; ADH_ZINC; 1. KW Oxidoreductase; Zinc; Metal-binding; NAD; Multigene family; KW Acetylation. FT INIT_MET 0 0 PROBABLE. FT MOD_RES 1 1 ACETYLATION (PROBABLE). FT METAL 47 47 ZINC 1 (CATALYTIC) (BY SIMILARITY). FT METAL 69 69 ZINC 1 (CATALYTIC) (BY SIMILARITY). FT METAL 99 99 ZINC 2 (BY SIMILARITY). FT METAL 102 102 ZINC 2 (BY SIMILARITY). FT METAL 105 105 ZINC 2 (BY SIMILARITY). FT METAL 113 113 ZINC 2 (BY SIMILARITY). FT METAL 176 176 ZINC 1 (CATALYTIC) (BY SIMILARITY). SQ SEQUENCE 378 AA; 40258 MW; 5EB01468A45CB8F8 CRC64; SATEGKVITC KAAVAWEAKK PLVIEDIEVA PPKAHEVRIK ITATGVCHTD AFTLSGADPE GLFPVVLGHE GAGIVESVGE GVTNFKAGDH VIALYIPQCN ECKFCKSGKT NLCQKIRLTQ GAGVMPEGTS RLSCKGQQLF HFMGTSTFAE YTVVADISLT KINEKAPLEK VCLLGCGIST GYGAALNTAK VEAGSTCAVW GLGAVGLAVG LGCKKAGAGK IYGIDINPDK FELAKKFGFT DFVNPKDVAD KGSIQNYLID LTDGGFDYTF ECIGNVNTMR SALEATHKGW GTSVVIGVAG AGQEISTRPF QLVVGRVWKG SAFGGWRSVS DVPKLVEDYL KKDLLVDEFI THELPLSQIN EAFDLMHKGE SIRSIIKY // ID ADH_DROME STANDARD; PRT; 255 AA. AC P00334; Q27332; Q27579; Q27596; Q95TC8; Q9NKC0; Q9VJS3; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alcohol dehydrogenase (EC 1.1.1.1). GN ADH OR BG:DS01486.8 OR CG3481. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ADH-S ALLELE). RX MEDLINE=81247357; PubMed=6789320; RA Benyajati C., Place A.R., Powers D.A., Sofer W.; RT "Alcohol dehydrogenase gene of Drosophila melanogaster: relationship RT of intervening sequences to functional domains in the protein."; RL Proc. Natl. Acad. Sci. U.S.A. 78:2717-2721(1981). RN [2] RP SEQUENCE FROM N.A. (ADH-NB ALLELE). RX MEDLINE=83116945; PubMed=6818527; RA Kubli E., Schmidt T., Martin P.F., Sofer W.; RT "In vitro suppression of a nonsense mutant of Drosophila RT melanogaster."; RL Nucleic Acids Res. 10:7145-7152(1982). RN [3] RP SEQUENCE FROM N.A. (ADH-S AND ADH-F ALLELES). RX MEDLINE=83271489; PubMed=6410283; RA Kreitman M.; RT "Nucleotide polymorphism at the alcohol dehydrogenase locus of RT Drosophila melanogaster."; RL Nature 304:412-417(1983). RN [4] RP SEQUENCE FROM N.A. (ADH-NB ALLELE). RX MEDLINE=85293092; PubMed=3928896; RA Martin P.F., Place A.R., Pentz E., Sofer W.; RT "UGA nonsense mutation in the alcohol dehydrogenase gene of RT Drosophila melanogaster."; RL J. Mol. Biol. 184:221-229(1985). RN [5] RP SEQUENCE FROM N.A. (ADH-JA-F AND ADH-AF-S ALLELES). RX MEDLINE=87031527; PubMed=3021568; RA Kreitman M.E., Aguade M.; RT "Excess polymorphism at the Adh locus in Drosophila melanogaster."; RL Genetics 114:93-110(1986). RN [6] RP SEQUENCE FROM N.A. (ADH-N4 ALLELE). RX MEDLINE=87231091; PubMed=3108863; RA Chia W., Savakis C., Karp R., Ashburner M.; RT "Adhn4 of Drosophila melanogaster is a nonsense mutation."; RL Nucleic Acids Res. 15:3931-3931(1987). RN [7] RP SEQUENCE FROM N.A. (ADH-F-CHD ALLELE). RC TISSUE=Embryo; RX MEDLINE=88316978; PubMed=3137352; RA Collet C.; RT "Recent origin for a thermostable alcohol dehydrogenase allele of RT Drosophila melanogaster."; RL J. Mol. Evol. 27:142-146(1988). RN [8] RP SEQUENCE FROM N.A. (ADH-71K ALLELE). RX MEDLINE=91087763; PubMed=2124644; RA Eisses K.T., Andriesse A.J., de Boer A.D., Thorig G.E.W., RA Weisbeek P.J.; RT "Analysis of the gene encoding the multifunctional alcohol RT dehydrogenase allozyme ADH-71k of Drosophila melanogaster."; RL Mol. Biol. Evol. 7:459-469(1990). RN [9] RP SEQUENCE FROM N.A. (ADH-S ALLELE). RX MEDLINE=91200630; PubMed=1673107; RA Kreitman M., Hudson R.R.; RT "Inferring the evolutionary histories of the Adh and Adh-dup loci in RT Drosophila melanogaster from patterns of polymorphism and RT divergence."; RL Genetics 127:565-582(1991). RN [10] RP SEQUENCE FROM N.A. (ADH-F ALLELE). RC STRAIN=NC16, KA12, and RI32; RX MEDLINE=92077396; PubMed=1683848; RA Laurie C.C., Bridgham J.T., Choudhary M.; RT "Associations between DNA sequence variation and variation in RT expression of the Adh gene in natural populations of Drosophila RT melanogaster."; RL Genetics 129:489-499(1991). RN [11] RP SEQUENCE FROM N.A. (ADH-H3; ADH-H12; ADH-H13; ADH-H18; ADH-H21; RP ADH-K15; ADH-K30; ADH-K35; ADH-K37 AND ADH-K82 ALLELES). RC STRAIN=Zimbabwe; RX MEDLINE=20073050; PubMed=10605124; RA Begun D., Betancourt A., Langley C., Stephan W.; RT "Is the fast/slow allozyme variation at the Adh locus of Drosophila RT melanogaster an ancient balanced polymorphism?"; RL Mol. Biol. Evol. 16:1816-1819(1999). RN [12] RP SEQUENCE FROM N.A. (ADH-S ALLELE). RC STRAIN=Canton-S; RA Brogna S., Ashburner M.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [13] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [14] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [15] RP SEQUENCE FROM N.A. (ADH-S ALLELE). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [16] RP SEQUENCE OF 51-255 FROM N.A. (ADH-NLA248 ALLELE). RX MEDLINE=86143824; PubMed=2419573; RA Chia W., Savakis C., Karp R., Pelham H., Ashburner M.; RT "Mutation of the Adh gene of Drosophila melanogaster containing an RT internal tandem duplication."; RL J. Mol. Biol. 186:679-688(1985). RN [17] RP SEQUENCE OF 140-255 FROM N.A. (ADH-F ALLELE). RX MEDLINE=81124290; PubMed=6780981; RA Benyajati C., Wang N., Reddy A., Weinberg E., Sofer W.; RT "Alcohol dehydrogenase in Drosophila: isolation and characterization RT of messenger RNA and cDNA clone."; RL Nucleic Acids Res. 8:5649-5667(1980). RN [18] RP SEQUENCE (ADH-F' ALLELE). RX MEDLINE=80043174; PubMed=115502; RA Retzios A.D., Thatcher D.R.; RT "Chemical basis of the electrophoretic variation observed at the RT alcohol dehydrogenase locus of Drosophila melanogaster."; RL Biochimie 61:701-704(1979). RN [19] RP SEQUENCE (ADH-F; ADH-S; ADH-UF AND ADH-N11 ALLELES), AND ACETYLATION. RX MEDLINE=84256516; PubMed=6821373; RA Thatcher D.R.; RT "The complete amino acid sequence of three alcohol dehydrogenase RT alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila RT melanogaster."; RL Biochem. J. 187:875-886(1980). RN [20] RP ERRATUM. RA Thatcher D.R.; RL Biochem. J. 191:895-895(1980). RN [21] RP SEQUENCE OF 207-224 (ADH-F-CHD ALLELE). RX MEDLINE=81247428; PubMed=6789328; RA Chambers G.K., Laver W.G., Campbell S., Gibson J.B.; RT "Structural analysis of an electrophoretically cryptic alcohol RT dehydrogenase variant from an Australian population of Drosophila RT melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 78:3103-3107(1981). RN [22] RP MUTAGENESIS. RX MEDLINE=90212596; PubMed=2108721; RA Chen Z., Lu L., Shirley M., Lee W.R., Chang S.H.; RT "Site-directed mutagenesis of glycine-14 and two 'critical' cysteinyl RT residues in Drosophila alcohol dehydrogenase."; RL Biochemistry 29:1112-1118(1990). RN [23] RP MUTAGENESIS OF TYR-152 AND LYS-156. RX MEDLINE=93213802; PubMed=8461298; RA Chen Z., Jiang J.C., Lin Z.-G., Lee W.R., Baker M.E., Chang S.H.; RT "Site-specific mutagenesis of Drosophila alcohol dehydrogenase: RT evidence for involvement of tyrosine-152 and lysine-156 in RT catalysis."; RL Biochemistry 32:3342-3346(1993). RN [24] RP MUTAGENESIS OF GLY-129; GLY-132; TYR-152; LYS-156 AND GLY-183. RX MEDLINE=93202283; PubMed=8454065; RA Cols N., Marfany G., Atrian S., Gonzalez-Duarte R.; RT "Effect of site-directed mutagenesis on conserved positions of RT Drosophila alcohol dehydrogenase."; RL FEBS Lett. 319:90-94(1993). RN [25] RP MUTAGENESIS OF TYR-152. RX MEDLINE=92371633; PubMed=1505661; RA Albalat R., Gonzalez-Duarte R., Atrian S.; RT "Protein engineering of Drosophila alcohol dehydrogenase. The RT hydroxyl group of Tyr152 is involved in the active site of the RT enzyme."; RL FEBS Lett. 308:235-239(1992). CC -!- CATALYTIC ACTIVITY: AN ALCOHOL + NAD(+) = AN ALDEHYDE OR KETONE + CC NADH. CC -!- ENZYME REGULATION: INHIBITED BY 2,2,2-TRIFLUOROETHANOL AND CC PYRAZOLE. CC -!- SUBUNIT: HOMODIMER. CC -!- POLYMORPHISM: VIRTUALLY ALL NATURAL POPULATIONS OF THIS SPECIES CC ARE POLYMORPHIC FOR 2 ELECTROPHORETICALLY DISTINGUISHABLE ALLELES, CC ADH-S AND ADH-F. THE SEQUENCE OF THE ADH-S ALLELE IS SHOWN. OTHER CC NATURALLY OCURRING ALLELES INCLUDE ADH-JA-F, ADH-AF-S, ADH-F-CHD, CC ADH-71K, ADH-UF AND ADH-F'. ARTIFICIALLY INDUCED MUTATIONS CC INCLUDE ADH-NB, ADH-NLA248, ADH-N4 AND ADH-N11. CC -!- SIMILARITY: BELONGS TO THE SHORT-CHAIN DEHYDROGENASES/REDUCTASES CC (SDR) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M36580; AAA28331.1; -. DR EMBL; Z00030; CAA77330.1; -. DR EMBL; M17827; AAA28341.1; -. DR EMBL; M17828; AAA28342.1; -. DR EMBL; M19547; AAA70210.1; -. DR EMBL; M17830; AAA28343.1; -. DR EMBL; M17831; AAA28344.1; -. DR EMBL; M17832; AAA28345.1; -. DR EMBL; M17833; AAA28346.1; -. DR EMBL; M17834; AAA28347.1; -. DR EMBL; M17835; AAA28348.1; -. DR EMBL; M17836; AAA28349.1; -. DR EMBL; M17837; AAA70212.1; -. DR EMBL; X60791; CAA43204.1; -. DR EMBL; X60792; CAA43205.1; -. DR EMBL; U20765; AAA88817.1; -. DR EMBL; X78384; CAA55151.1; -. DR EMBL; X98338; CAA66981.1; -. DR EMBL; M57239; AAA28330.1; -. DR EMBL; M22210; AAA28338.1; -. DR EMBL; X60793; CAA43206.1; -. DR EMBL; M17845; AAA28363.1; -. DR EMBL; AF175211; AAF00229.1; -. DR EMBL; AF175212; AAF00230.1; -. DR EMBL; AF175213; AAF00231.1; -. DR EMBL; AF175214; AAF00232.1; -. DR EMBL; AF175215; AAF00233.1; -. DR EMBL; AF175216; AAF00234.1; -. DR EMBL; AF175217; AAF00235.1; -. DR EMBL; AF175218; AAF00236.1; -. DR EMBL; AF175219; AAF00237.1; -. DR EMBL; AF175220; AAF00238.1; -. DR EMBL; AE003410; AAF44882.1; -. DR EMBL; AY060227; AAL25266.1; -. DR EMBL; AE003644; AAF53403.1; -. DR PIR; A93309; DEFFA. DR HSSP; P10807; 1B16. DR FlyBase; FBgn0000055; Adh. DR InterPro; IPR002198; ADH_short. DR InterPro; IPR000205; NAD_BS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. KW Oxidoreductase; NAD; Acetylation; Polymorphism. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT NP_BIND 11 34 NAD (BY SIMILARITY). FT ACT_SITE 152 152 FT VARIANT 8 8 N -> V (IN ALLELE ADH-UF). FT VARIANT 45 45 A -> V (IN STRAIN NC16). FT VARIANT 45 45 A -> D (IN ALLELE ADH-UF). FT VARIANT 51 51 A -> E (IN ALLELE ADH-F'). FT VARIANT 70 70 A -> S (IN STRAIN NC16). FT VARIANT 192 192 K -> T (in allele ADH-F, allele ADH-F- FT CHD, allele ADH-71K, allele ADH-JA-F and FT in strain Berkeley). FT VARIANT 214 214 P -> S (in allele ADH-F-CHD and allele FT ADH-71K). FT MUTAGEN 14 14 G->V: COMPLETE LOSS OF ACTIVITY. FT MUTAGEN 14 14 G->A: 31% DECREASE IN ACTIVITY. FT MUTAGEN 14 14 G->D: LOSS OF ACTIVITY; IN ADH-N11. FT MUTAGEN 129 129 G->C: COMPLETE LOSS OF ACTIVITY. FT MUTAGEN 132 132 G->I: COMPLETE LOSS OF ACTIVITY. FT MUTAGEN 135 135 C->A: NO DECREASE IN ACTIVITY. FT MUTAGEN 152 152 Y->F,H,E,Q: COMPLETE LOSS OF ACTIVITY. FT MUTAGEN 152 152 Y->C: RETAINS ONLY 0.25% ACTIVITY. FT MUTAGEN 156 156 K->I: COMPLETE LOSS OF ACTIVITY. FT MUTAGEN 156 156 K->R: RETAINS ONLY 2.2% ACTIVITY. FT MUTAGEN 183 183 G->L: COMPLETE LOSS OF ACTIVITY. FT MUTAGEN 218 218 C->A: NO DECREASE IN ACTIVITY. FT CONFLICT 33 33 MISSING (IN REF. 13). SQ SEQUENCE 255 AA; 27630 MW; CA7DF929E0007296 CRC64; SFTLTNKNVI FVAGLGGIGL DTSKELLKRD LKNLVILDRI ENPAAIAELK AINPKVTVTF YPYDVTVPIA ETTKLLKTIF AQLKTVDVLI NGAGILDDHQ IERTIAVNYT GLVNTTTAIL DFWDKRKGGP GGIICNIGSV TGFNAIYQVP VYSGTKAAVV NFTSSLAKLA PITGVTAYTV NPGITRTTLV HKFNSWLDVE PQVAEKLLAH PTQPSLACAE NFVKAIELNQ NGAIWKLDLG TLEAIQWTKH WDSGI // ID ADRO_DROME STANDARD; PRT; 466 AA. AC Q9V3T9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NADPH:adrenodoxin oxidoreductase, mitochondrial precursor DE (EC 1.18.1.2) (Adrenodoxin reductase) (AR) (Ferredoxin-NADP(+) DE reductase). GN DARE OR CG12390. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=W1118; TISSUE=Head, and Testis; RX MEDLINE=99429818; PubMed=10498693; RA Freeman M.R., Dobritsa A., Gaines P., Segraves W.A., Carlson J.R.; RT "The dare gene: steroid hormone production, olfactory behavior, and RT neural degeneration in Drosophila."; RL Development 126:4591-4602(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR SYNTHESIS OF STEROID HORMONES, FOR CC OLFACTORY SENSORY BEHAVIOR AND COMPLETION OF THE SECOND LARVAL CC MOLT (A STEROID MEDIATED DEVELOPMENTAL TRANSITION) AND CC PUPARIATION. CC -!- CATALYTIC ACTIVITY: REDUCED ADRENODOXIN + NADP(+) = OXIDIZED CC ADRENODOXIN + NADPH. CC -!- COFACTOR: FAD. CC -!- PATHWAY: CHOLESTEROL SIDE-CHAIN-CLEAVAGE SYSTEM. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN PROTHORACIC GLAND CC OF THE LARVAL RING GLAND AND NURSE CELLS OF THE ADULT OVARY. LOW CC EXPRESSION IS ALL ADULT TISSUES EXAMINED. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF168685; AAD50819.1; -. DR EMBL; AE003826; AAF58678.1; -. DR HSSP; P08165; 1E6E. DR FlyBase; FBgn0015582; dare. DR InterPro; IPR000759; Adrndx_reductase. DR InterPro; IPR000103; Pyridine_redox_2. DR PRINTS; PR00419; ADXRDTASE. DR PRINTS; PR00469; PNDRDTASEII. KW Electron transport; Oxidoreductase; Flavoprotein; NADP; FAD; KW Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 466 NADPH:ADRENODOXIN OXIDOREDUCTASE. SQ SEQUENCE 466 AA; 51352 MW; 64D7C1FF0F1CAFD6 CRC64; MGINCLNIFR RGLHTSSARL QVIQSTTPTK RICIVGAGPA GFYAAQLILK QLDNCVVDVV EKLPVPFGLV RFGVAPDHPE VKNVINTFTK TAEHPRLRYF GNISLGTDVS LRELRDRYHA VLLTYGADQD RQLELENEQL DNVISARKFV AWYNGLPGAE NLAPDLSGRD VTIVGQGNVA VDVARMLLSP LDALKTTDTT EYALEALSCS QVERVHLVGR RGPLQAAFTI KELREMLKLP NVDTRWRTED FSGIDMQLDK LQRPRKRLTE LMLKSLKEQG RISGSKQFLP IFLRAPKAIA PGEMEFSVTE LQQEAAVPTS STERLPSHLI LRSIGYKSSC VDTGINFDTR RGRVHNINGR ILKDDATGEV DPGLYVAGWL GTGPTGVIVT TMNGAFAVAK TICDDINTNA LDTSSVKPGY DADGKRVVTW DGWQRINDFE SAAGKAKGKP REKIVSIEEM LRVAGV // ID ADT_DROME STANDARD; PRT; 299 AA. AC Q26365; P91614; Q26254; Q95S30; Q9VZ70; DT 15-JUL-1998 (Rel. 36, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ADP,ATP carrier protein (ADP/ATP translocase) (Adenine nucleotide DE translocator) (ANT) (Stress sensitive B protein). GN SESB OR A/A-T OR CG16944. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92389367; PubMed=1387687; RA Louvi A., Tsitilou S.G.; RT "A cDNA clone encoding the ADP/ATP translocase of Drosophila RT melanogaster shows a high degree of similarity with the mammalian RT ADP/ATP translocases."; RL J. Mol. Evol. 35:44-50(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94350065; PubMed=7520869; RA Hutter P., Karch F.; RT "Molecular analysis of a candidate gene for the reproductive RT isolation between sibling species of Drosophila."; RL Experientia 50:749-762(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Zhang Y.Q., Davis A.W., Roote J., Herrmann S., Ashburner M.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, Ovary, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CATALYZES THE EXCHANGE OF ADP AND ATP ACROSS THE CC MITOCHONDRIAL INNER MEMBRANE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE MITOCHONDRIAL CARRIER FAMILY. CC -!- SIMILARITY: CONTAINS 3 SOLCAR REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S43651; AAB23114.1; -. DR EMBL; S71762; AAB31734.3; -. DR EMBL; Y10618; CAA71628.1; -. DR EMBL; AE003484; AAF47957.1; -. DR EMBL; AY060978; AAL28526.1; -. DR EMBL; AY070894; AAL48516.1; -. DR FlyBase; FBgn0003360; sesB. DR GO; GO:0005743; C:mitochondrial inner membrane; IEP. DR GO; GO:0006839; P:mitochondrial transport; IMP. DR InterPro; IPR002067; Mit_carrier. DR InterPro; IPR001993; Mitoch_carrier. DR Pfam; PF00153; mito_carr; 3. DR PRINTS; PR00926; MITOCARRIER. DR PROSITE; PS50920; SOLCAR; 3. KW Mitochondrion; Inner membrane; Repeat; Transmembrane; Transport. FT TRANSMEM 14 31 1 (POTENTIAL). FT TRANSMEM 75 93 2 (POTENTIAL). FT TRANSMEM 119 136 3 (POTENTIAL). FT TRANSMEM 177 196 4 (POTENTIAL). FT TRANSMEM 215 232 5 (POTENTIAL). FT TRANSMEM 274 292 6 (POTENTIAL). FT REPEAT 8 100 SOLCAR 1. FT REPEAT 113 202 SOLCAR 2. FT REPEAT 213 298 SOLCAR 3. FT CONFLICT 18 19 GI -> QV (IN REF. 1 AND 2). FT CONFLICT 81 81 I -> Y (IN REF. 1). FT CONFLICT 201 201 MISSING (IN REF. 1 AND 2). FT CONFLICT 267 267 G -> A (IN REF. 2). FT CONFLICT 268 269 TG -> P (IN REF. 1 AND 2). FT CONFLICT 270 270 A -> S (IN REF. 1). FT CONFLICT 270 270 A -> C (IN REF. 2). SQ SEQUENCE 299 AA; 32909 MW; D51F3E2A70BD59E8 CRC64; MGKDFDAVGF VKDFAAGGIS AAVSKTAVAP IERVKLLLQV QHISKQISPD KQYKGMVDCF IRIPKEQGFS SFWRGNLANV IRYFPTQALN FAFKDKYKQV FLGGVDKNTQ FWRYFAGNLA SGGAAGATSL CFVYPLDFAR TRLAADTGKG GQREFTGLGN CLTKIFKSDG IVGLYRGFGV SVQGIIIYRA AYFGFYDTAR GMLPDPKNTP IYISWAIAQV VTTVAGIVSY PFDTVRRRMM MQSGRKATEV IYKNTLHCWA TIAKQEGTGA FFKGAFSNIL RGTGGAFVLV LYDEIKKVL // ID ADXH_DROME STANDARD; PRT; 172 AA. AC P37193; Q8MYT2; Q9VSW8; DT 01-OCT-1994 (Rel. 30, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Adrenodoxin-like protein, mitochondrial precursor. GN FDXH OR CG4205. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88118925; PubMed=3123699; RA Pauli D., Tonka C.H.; RT "A Drosophila heat shock gene from locus 67B is expressed during RT embryogenesis and pupation."; RL J. Mol. Biol. 198:235-240(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP IDENTIFICATION. RA Rudd K.E.; RL Unpublished observations (JUL-1994). CC -!- COFACTOR: BINDS 1 2FE-2S CLUSTER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ADRENODOXIN / PUTIDAREDOXIN FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06542; CAB55551.1; ALT_SEQ. DR EMBL; AE003552; AAF50293.2; -. DR EMBL; AY113620; AAM29625.1; -. DR HSSP; P00257; 1E6E. DR FlyBase; FBgn0011769; Fdxh. DR InterPro; IPR001055; Adrenodoxin. DR InterPro; IPR001041; Ferredoxin. DR Pfam; PF00111; fer2; 1. DR PRINTS; PR00355; ADRENODOXIN. DR PROSITE; PS00814; ADX; 1. KW Metal-binding; Iron-sulfur; Iron; 2Fe-2S; Electron transport; KW Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 172 ADRENODOXIN-LIKE PROTEIN. FT METAL 94 94 IRON-SULFUR (2FE-2S) (BY SIMILARITY). FT METAL 100 100 IRON-SULFUR (2FE-2S) (BY SIMILARITY). FT METAL 103 103 IRON-SULFUR (2FE-2S) (BY SIMILARITY). FT METAL 140 140 IRON-SULFUR (2FE-2S) (BY SIMILARITY). FT CONFLICT 159 172 TRNFYVDGHKPKPH -> PGTSTSMGTSPSHINIIVISRII FT NNI (IN REF. 1). FT CONFLICT 161 161 N -> D (IN REF. 4). SQ SEQUENCE 172 AA; 19733 MW; 9D70F51572562E2F CRC64; MFCLLLRRSA VHNSCKLISK QIAKPAFYTP HNALHTTIPR RHGEFEWQDP KSTDEIVNIT YVDKDGKRTK VQGKVGDNVL YLAHRHGIEM EGACEASLAC TTCHVYVQHD YLQKLKEAEE QEDDLLDMAP FLRENSRLGC QILLDKSMEG MELELPKATR NFYVDGHKPK PH // ID AEF1_DROME STANDARD; PRT; 308 AA. AC P39413; Q9VP37; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Adult enhancer factor 1 (AEF-1). GN AEF1 OR CG5683. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=92375078; PubMed=1508206; RA Falb D., Maniatis T.; RT "Drosophila transcriptional repressor protein that binds specifically RT to negative control elements in fat body enhancers."; RL Mol. Cell. Biol. 12:4093-4103(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TRANSCRIPTIONAL REPRESSOR THAT BINDS SPECIFICALLY TO FAT CC BODY-SPECIFIC ENHANCERS, NAMELY THE ADULT ADH ENHANCER (AAE) AND CC THE ENHANCER THAT CONTROLS YOLK PROTEIN GENE EXPRESSION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: FOUND IN ALL TISSUES EXAMINED INCLUDING THE CC OVARY AND THE FAT BODY. CC -!- DEVELOPMENTAL STAGE: HIGHER LEVELS ARE FOUND IN THIRD-INSTAR CC LARVAE AND IN ADULTS. CC -!- SIMILARITY: CONTAINS 4 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M90755; -; NOT_ANNOTATED_CDS. DR EMBL; AE003594; AAF51722.1; -. DR EMBL; AY060435; AAL25474.1; -. DR PIR; A44496; A44496. DR HSSP; P08046; 1A1H. DR TRANSFAC; T01513; -. DR FlyBase; FBgn0005694; Aef1. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 4. DR ProDom; PD000003; Znf_C2H2; 2. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. KW Transcription regulation; Repressor; DNA-binding; Nuclear protein; KW Zinc-finger; Metal-binding; Repeat. FT DOMAIN 56 76 GLN-RICH (OPA-REPEAT). FT DOMAIN 71 76 POLY-GLN. FT DOMAIN 105 127 ALA-RICH. FT DOMAIN 132 135 POLY-PRO. FT ZN_FING 184 206 C2H2-TYPE 1. FT ZN_FING 212 234 C2H2-TYPE 2. FT ZN_FING 240 262 C2H2-TYPE 3. FT ZN_FING 268 290 C2H2-TYPE 4. SQ SEQUENCE 308 AA; 33782 MW; 54F04D90B6FC4250 CRC64; MMHIKSLPHA HAAATAMSSN CDIVIVAAQP QTTIANNNNN ETVTQATHPA HMAAVQQQQQ QQQQQQQQHH QQQQQQSSGP PSVPPPPTEL PLPFQMHLSG ISAEAHSAAQ AAAMAAAQAA AAQAAAAEQQ QPPPPTSHLT HLTTHSPTTI HSEHYLANGH SEHPGEGNAA VGVGGAVREP EKPFHCTVCD RRFRQLSTLT NHVKIHTGEK PYKCNVCDKT FRQSSTLTNH LKIHTGEKPY NCNFCPKHFR QLSTLANHVK IHTGEKPFEC VICKKQFRQS STLNNHIKIH VMDKVYVPVK IKTEEDEG // ID AKHD_DROME STANDARD; PRT; 79 AA. AC P17975; Q9VZH6; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Adipokinetic hormone precursor (dAKH) (Hypertrehalosaemic hormone) DE (HRTH). GN AKH OR CG1171. OS Drosophila melanogaster (Fruit fly), and OS Protophormia terraenovae (Black blowfly) (Nestling-sucking blowfly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 34676; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=95394250; PubMed=7664975; RA Noyes B.E., Schaffer M.H.; RT "Identification and expression of the Drosophila adipokinetic hormone RT gene."; RL Mol. Cell. Endocrinol. 109:133-141(1995). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 23-30, AND AMIDATION. RC SPECIES=D.melanogaster; STRAIN=Oregon-R; TISSUE=Thorax; RX MEDLINE=90351346; PubMed=2117437; RA Schaffer M.H., Noyes B.E., Slaughter C.A., Thorne G.C., Gaskell S.J.; RT "The fruitfly Drosophila melanogaster contains a novel charged RT adipokinetic-hormone-family peptide."; RL Biochem. J. 269:315-320(1990). RN [4] RP SEQUENCE OF 23-30, AND AMIDATION. RC SPECIES=D.melanogaster; TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). RN [5] RP SEQUENCE OF 23-30, AND AMIDATION. RC SPECIES=P.terraenovae; TISSUE=Corpora cardiaca; RX MEDLINE=90351345; PubMed=2386478; RA Gaede G., Wilps H., Kellner R.; RT "Isolation and structure of a novel charged member of the RT red-pigment-concentrating hormone-adipokinetic hormone family of RT peptides isolated from the corpora cardiaca of the blowfly Phormia RT terraenovae (Diptera)."; RL Biochem. J. 269:309-313(1990). CC -!- FUNCTION: PROBABLY CAUSES A MARKED INCREASE IN HEMOLYMPH CC CARBOHYDRATE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE AKH / HRTH / RPCH FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L23764; AAB00099.1; -. DR EMBL; AE003480; AAF47846.1; -. DR PIR; A58656; A58656. DR PIR; S11545; S11545. DR FlyBase; FBgn0004552; Akh. DR GO; GO:0005184; F:neuropeptide hormone activity; IDA. DR InterPro; IPR002047; AKH. DR PROSITE; PS00256; AKH; 1. KW Neuropeptide; Amidation; Cleavage on pair of basic residues; Signal; KW Pyrrolidone carboxylic acid. FT SIGNAL 1 22 FT PEPTIDE 23 30 ADIPOKINETIC HORMONE. FT PROPEP 34 79 FT MOD_RES 23 23 PYRROLIDONE CARBOXYLIC ACID. FT MOD_RES 30 30 AMIDATION (G-31 PROVIDE AMIDE GROUP). SQ SEQUENCE 79 AA; 8843 MW; 6EE12D5C71941494 CRC64; MNPKSEVLIA AVLFMLLACV QCQLTFSPDW GKRSVGGAGP GTFFETQQGN CKTSNEMLLE IFRFVQSQAQ LFLDCKHRE // ID ALF_DROME STANDARD; PRT; 360 AA. AC P07764; P29841; Q24236; Q24237; Q8IMS1; Q8MQQ4; Q9VBG2; Q9VBG3; DT 01-AUG-1988 (Rel. 08, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fructose-bisphosphate aldolase (EC 4.1.2.13). GN ALD OR CG6058. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS BETA AND GAMMA). RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=92123202; PubMed=1732743; RA Kim J., Yim J.J., Wang S., Dorsett D.; RT "Alternate use of divergent forms of an ancient exon in the RT fructose-1,6-bisphosphate aldolase gene of Drosophila RT melanogaster."; RL Mol. Cell. Biol. 12:773-783(1992). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS ALPHA; BETA AND GAMMA), AND TISSUE RP SPECIFICITY. RC STRAIN=Oregon-R; RX MEDLINE=93123199; PubMed=1339430; RA Kai T., Sugimoto Y., Kusakabe T., Zhang R., Koga K., Hori K.; RT "Gene structure and multiple mRNA species of Drosophila melanogaster RT aldolase generating three isozymes with different enzymatic RT properties."; RL J. Biochem. 112:677-688(1992). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS ALPHA; BETA AND GAMMA). RC STRAIN=Oregon-R; RX MEDLINE=92156139; PubMed=1740444; RA Shaw-Lee R., Lissemore J.L., Sullivan D.T., Tolan D.R.; RT "Alternative splicing of fructose 1,6-bisphosphate aldolase RT transcripts in Drosophila melanogaster predicts three isozymes."; RL J. Biol. Chem. 267:3959-3967(1992). RN [4] RP SEQUENCE FROM N.A. (ISOFORM ALPHA), SEQUENCE OF 353-360 (ISOFORM RP ALPHA), AND CHARACTERIZATION. RC STRAIN=Oregon-R; RX MEDLINE=96063611; PubMed=7487099; RA Sugimoto Y., Kusakabe T., Kai T., Okamura T., Koga K., Hori K.; RT "Analysis of the in vitro translation product of a novel-type RT Drosophila melanogaster aldolase mRNA in which two carboxyl-terminal RT exons remain unspliced."; RL Arch. Biochem. Biophys. 323:361-366(1995). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [7] RP SEQUENCE FROM N.A. (ISOFORMS BETA AND GAMMA). RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [8] RP SEQUENCE (ISOFORM GAMMA), AND ACETYLATION. RX MEDLINE=85121864; PubMed=3918528; RA Malek A.A., Suter F.X., Frank G., Brenner-Holzach O.; RT "Amino acid sequence of an invertebrate FBP aldolase (from Drosophila RT melanogaster)."; RL Biochem. Biophys. Res. Commun. 126:199-205(1985). RN [9] RP SEQUENCE (ISOFORM GAMMA). RX MEDLINE=89024658; PubMed=3140728; RA Malek A.A., Hy M., Honegger A., Rose K., Brenner-Holzach O.; RT "Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: RT primary structure analysis, secondary structure prediction, and RT comparison with vertebrate aldolases."; RL Arch. Biochem. Biophys. 266:10-31(1988). RN [10] RP PRELIMINARY SEQUENCE OF 169-271. RX MEDLINE=82205133; PubMed=6805442; RA Brenner-Holzach O., Zumsteg C.; RT "Fructose 1,6-bisphosphate aldolase of Drosophila melanogaster: RT comparative sequence analyses around the substrate-binding lysyl RT residue."; RL Arch. Biochem. Biophys. 214:89-101(1982). RN [11] RP CHARACTERIZATION. RX MEDLINE=96015167; PubMed=8537310; RA Zhang R., Kai T., Sugimoto Y., Kusakabe T., Takasaki Y., Koga K., RA Hori K.; RT "Drosophila melanogaster aldolase: characterization of the isozymes RT alpha, beta, and gamma generated from a single gene."; RL J. Biochem. 118:183-188(1995). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=92070498; PubMed=1959612; RA Hester G., Brenner-Holzach O., Rossi F.A., Struck-Donatz M., RA Winterhalter K.H., Smit J.D.G., Piontek K.; RT "The crystal structure of fructose-1,6-bisphosphate aldolase from RT Drosophila melanogaster at 2.5-A resolution."; RL FEBS Lett. 292:237-242(1991). CC -!- FUNCTION: MAY TAKE PART IN DEVELOPMENTAL STAGE-SPECIFIC OR TISSUE CC -SPECIFIC SUGAR-PHOSPHATE METABOLISMS. PROTEIN ACTS ON TWO CC SUBSTRATES FRUCTOSE 1,6-BISPHOSPHATE AND FRUCTOSE 1-PHOSPHATE CC (LIKE OTHER CLASS I ALDOLASES). PH PROFILE: HIGHEST ACTIVITY FOR CC ISOZYME ALPHA IS AT PH 7.2 TO 7.8 AND FOR ISOZYMES BETA AND GAMMA CC AT 7.2 TO 7.5. THERMOSTABILITY OF THE ISOZYMES, CALCULATED AS THE CC TEMPERATURE CAUSING HALF MAXIMAL STABILITY, IS 42-43 DEGREES CC CELSIUS FOR ISOZYMES ALPHA AND BETA AND 45 DEGREES CELSIUS FOR CC ISOZYME GAMMA. CC -!- CATALYTIC ACTIVITY: D-FRUCTOSE 1,6-BISPHOSPHATE = GLYCERONE CC PHOSPHATE + D-GLYCERALDEHYDE 3-PHOSPHATE. CC -!- PATHWAY: GLYCOLYSIS; SIXTH STEP. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Two additional mRNAs also exist (Alpha-Beta and CC Beta-Gamma). The translation product of Alpha-Beta mRNA is CC isoform Alpha; CC Name=Gamma; Synonyms=4C, B, C, D, F; CC IsoId=P07764-1; Sequence=Displayed; CC Name=Alpha; Synonyms=4A, A, E; CC IsoId=P07764-2; Sequence=VSP_000223; CC Name=Beta; Synonyms=4B, H; CC IsoId=P07764-3; Sequence=VSP_000221; CC -!- TISSUE SPECIFICITY: ISOZYME GAMMA IS MAINLY EXPRESSED IN THE HEADS CC AND PARTLY IN THE THORAXES OF ADULT FLIES. ISOZYME ALPHA IS CC EXPRESSED IN ALL ADULT TISSUES. ISOZYME BETA IS MAINLY EXPRESSED CC IN ADULT ABDOMINAL REGIONS AND IS ALSO EXPRESSED IN LESSER AMOUNTS CC IN OTHER PARTS OF THE BODY AND IN EARLIER DEVELOPMENTAL STAGES. CC ISOZYME ALPHA-BETA SHOWS STRONG EXPRESSION IN THE ABDOMENS OF CC ADULTS. ISOZYME BETA-GAMMA IS EXPRESSED IN ADULT HEADS. CC -!- DEVELOPMENTAL STAGE: ISOZYME GAMMA IS FIRST DETECTED DURING LATE CC EMBRYOGENESIS, IS PRESENT THROUGH LARVAL STAGES, DECLINES IN CC ABUNDANCE DURING PUPAL STAGES AND IS MAXIMUM AT ECLOSION. ISOZYME CC BETA IS ABUNDANT DURING THE EARLIEST STAGES OF EMBRYOGENESIS, CC DECLINES IN AMOUNT AND INCREASES PRIOR TO HATCHING. ISOZYME ALPHA CC IS FOUND ONLY DURING THE ADULT STAGE. EXPRESSION CORRELATES TO CC DIETARY BEHAVIOR: HIGH DIETARY ACTIVITY IN THE LARVAE AND ADULTS CC CAUSES ACTIVE GLYCOLYSIS AND HIGH EXPRESSION LEVELS. ISOZYME CC ALPHA-BETA IS DETECTED IN THE PUPAE AND ADULTS AND ISOZYME BETA- CC GAMMA IN THE ADULT. CC -!- SIMILARITY: BELONGS TO CLASS I FRUCTOSE-BISPHOSPHATE ALDOLASE CC FAMILY. CC -!- CAUTION: REF.1 (CAA42666) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -!- CAUTION: REF.5 (AAN14380) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -!- CAUTION: REF.7 (AAM75045) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC FRAMESHIFTS IN POSITIONS 266 AND 332. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60064; CAA42666.1; ALT_SEQ. DR EMBL; X60064; CAA42667.1; -. DR EMBL; X60064; CAA42668.1; -. DR EMBL; D10446; BAA01236.1; -. DR EMBL; D10446; BAA01237.1; -. DR EMBL; D10446; BAA01238.1; -. DR EMBL; M98351; AAA99428.1; -. DR EMBL; M98351; AAA99427.1; -. DR EMBL; M98351; AAA99426.1; -. DR EMBL; D10762; BAA01592.1; -. DR EMBL; AE003755; AAF56579.1; -. DR EMBL; AE003755; AAN14380.1; ALT_SEQ. DR EMBL; AE003755; AAN14384.1; -. DR EMBL; AY058667; AAL13896.1; -. DR EMBL; AY128452; AAM75045.1; ALT_FRAME. DR PIR; A42027; ADFFR. DR PIR; A42263; A42263. DR PIR; B42027; ADFF. DR PIR; B42263; B42263. DR PIR; C42263; C42263. DR PDB; 1FBA; 31-JAN-94. DR FlyBase; FBgn0000064; Ald. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA. DR GO; GO:0006096; P:glycolysis; IDA. DR InterPro; IPR000741; Aldolase_I. DR Pfam; PF00274; glycolytic_enzy; 1. DR ProDom; PD001128; Aldolase_I; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. KW Lyase; Schiff base; Glycolysis; Acetylation; 3D-structure; KW Alternative splicing. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT BINDING 55 55 C-1-PHOSPHATE GROUP OF THE SUBSTRATE. FT BINDING 146 146 C-1-PHOSPHATE GROUP OF THE SUBSTRATE. FT BINDING 229 229 SCHIFF-BASE WITH DIHYDROXYACETONE-P. FT ACT_SITE 360 360 ESSENTIAL FOR ENHANCED ACTIVITY OF THE FT ENZYME TOWARD FRUCTOSE 1,6-BISPHOSPHATE FT AS COMPARED WITH FRUCTOSE 1-PHOSPHATE. FT VARSPLIC 334 360 GDAAQGKYVAGSAGAGSGSLFVANHAY -> SQACQGIYVP FT GSIPSFAGNANLFVAQHKY (in isoform Beta). FT /FTId=VSP_000221. FT VARSPLIC 335 360 DAAQGKYVAGSAGAGSGSLFVANHAY -> EAACGNYTAGS FT VKGFAGKDTLHVDDHRY (in isoform Alpha). FT /FTId=VSP_000223. FT CONFLICT 39 39 M -> H (IN REF. 2 AND 4). FT CONFLICT 110 110 K -> E (IN REF. 1). FT CONFLICT 180 180 Q -> E (IN REF. 2 AND 4). FT CONFLICT 200 200 R -> G (IN REF. 1). FT CONFLICT 250 250 A -> T (IN REF. 1). FT HELIX 9 22 FT TURN 23 23 FT TURN 25 26 FT STRAND 28 32 FT HELIX 36 45 FT TURN 46 47 FT HELIX 52 63 FT TURN 64 64 FT HELIX 67 71 FT TURN 72 72 FT STRAND 73 78 FT HELIX 80 83 FT TURN 84 84 FT STRAND 86 86 FT TURN 88 89 FT STRAND 92 92 FT HELIX 93 99 FT TURN 100 101 FT STRAND 103 107 FT STRAND 112 114 FT TURN 116 117 FT STRAND 122 124 FT TURN 128 129 FT HELIX 130 139 FT TURN 140 141 FT STRAND 142 151 FT HELIX 160 179 FT TURN 180 181 FT STRAND 183 190 FT HELIX 198 218 FT TURN 219 220 FT HELIX 223 225 FT STRAND 227 228 FT TURN 237 238 FT HELIX 244 258 FT TURN 261 262 FT STRAND 265 268 FT TURN 271 272 FT HELIX 275 285 FT TURN 286 287 FT STRAND 295 300 FT HELIX 302 304 FT TURN 305 305 FT HELIX 306 312 FT TURN 313 314 FT TURN 317 318 FT HELIX 319 336 FT TURN 337 339 FT TURN 343 346 SQ SEQUENCE 360 AA; 38916 MW; 7F64A1BF11244CE2 CRC64; TTYFNYPSKE LQDELREIAQ KIVAPGKGIL AADESGPTMG KRLQDIGVEN TEDNRRAYRQ LLFSTDPKLA ENISGVILFH ETLYQKADDG TPFAEILKKK GIILGIKVDK GVVPLFGSED EVTTQGLDDL AARCAQYKKD GCDFAKWRCV LKIGKNTPSY QSILENANVL ARYASICQSQ RIVPIVEPEV LPDGDHDLDR AQKVTETVLA AVYKALSDHH VYLEGTLLKP NMVTAGQSAK KNTPEEIALA TVQALRRTVP AAVTGVTFLS GGQSEEEATV NLSAINNVPL IRPWALTFSY GRALQASVLR AWAGKKENIA AGQNELLKRA KANGDAAQGK YVAGSAGAGS GSLFVANHAY // ID ALLS_DROME STANDARD; PRT; 151 AA. AC Q9VC44; Q9NB67; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Allatostatins Ast precursor [Contains: Drostatin 1; Drostatin 2; DE Drostatin 3; Drostatin 4; Drostatin 5]. GN AST OR BCDNA:RE16553 OR CG13633. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=20351237; PubMed=10891383; RA Lenz C., Williamson M., Grimmelikhuijzen C.J.P.; RT "Molecular cloning and genomic organization of an Allatostatin RT preprohormone from Drosophila melanogaster."; RL Biochem. Biophys. Res. Commun. 273:1126-1131(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 68-78; 92-99 AND 138-148, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- FUNCTION: MAY ACT AS A NEUROTRANSMITTER OR NEUROMODULATOR. CC -!- SIMILARITY: BELONGS TO THE ALLATOSTATIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF263923; AAF97792.1; -. DR EMBL; AE003749; AAF56331.1; -. DR EMBL; AY071110; AAL48732.1; -. DR PIR; JC7325; JC7325. DR FlyBase; FBgn0015591; Ast. DR GO; GO:0016086; F:allatostatin; NAS. DR GO; GO:0005184; F:neuropeptide hormone activity; NAS. DR GO; GO:0005102; F:receptor binding; NAS. DR GO; GO:0045968; P:negative regulation of juvenile hormone bio...; NAS. DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS. KW Neuropeptide; Signal; Cleavage on pair of basic residues; Amidation. FT SIGNAL 1 21 POTENTIAL. FT PROPEP 22 54 FT PEPTIDE 57 64 DROSTATIN 1 (POTENTIAL). FT PEPTIDE 68 78 DROSTATIN 5. FT PEPTIDE 81 88 DROSTATIN 2 (POTENTIAL). FT PEPTIDE 92 99 DROSTATIN 3. FT PROPEP 103 135 FT PEPTIDE 138 148 DROSTATIN 4. FT MOD_RES 64 64 AMIDATION (G-65 PROVIDE AMIDE GROUP) FT (POTENTIAL). FT MOD_RES 88 88 AMIDATION (G-89 PROVIDE AMIDE GROUP) FT (POTENTIAL). FT MOD_RES 99 99 AMIDATION (G-100 PROVIDE AMIDE GROUP). FT MOD_RES 148 148 AMIDATION (G-149 PROVIDE AMIDE GROUP). FT CONFLICT 9 9 L -> I (IN REF. 1). FT CONFLICT 15 15 C -> G (IN REF. 1). SQ SEQUENCE 151 AA; 16852 MW; 1EC8A90494184C96 CRC64; MNSLHAHLLL LAVCCVGYIA SSPVIGQDQR SGDSDADVLL AADEMADNGG DNIDKRVERY AFGLGRRAYM YTNGGPGMKR LPVYNFGLGK RSRPYSFGLG KRSDYDYDQD NEIDYRVPPA NYLAAERAVR PGRQNKRTTR PQPFNFGLGR R // ID AL_DROME STANDARD; PRT; 408 AA. AC Q06453; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Homeobox protein aristaless. GN AL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=93138380; PubMed=8093690; RA Schneitz K., Spielmann P., Noll M.; RT "Molecular genetics of aristaless, a prd-type homeo box gene involved RT in the morphogenesis of proximal and distal pattern elements in a RT subset of appendages in Drosophila."; RL Genes Dev. 7:114-129(1993). CC -!- FUNCTION: INVOLVED IN THE MORPHOGENESIS OF PROXIMAL AND DISTAL CC PATTERN ELEMENTS IN A SUBSET OF APPENDAGES. APPEARS ALSO TO HAVE A CC ROLE IN EARLY IMAGINAL DISK DEVELOPMENT. ARISTALESS MUTANTS CC DISPLAY A REDUCTION IN SIZE OF THE ARISTA AND SCUTELLUM, A CC REDUCTION OR COMPLETE ABSENCE OF THE TARSAL CLAWS, IRREGULARITIES CC OF THE STERNOPLEURAL BRISTLES AND OF THE WING VEIN, AND A BENDING CC OF THE WING BLADE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: EXPRESSED DURING EMBRYONIC DEVELOPMENT, IN CC DISTINCT EPIDERMAL PATTERNS IN HEAD, THORAX AND ABDOMEN AND IN AN CC ENDODERMAL PATTERN IN THE ANTERIOR INTESTINAL TRACT. CC -!- DEVELOPMENTAL STAGE: FIRST EXPRESSED IN 4-8 HR-OLD EMBRYOS, PEAKS CC IN 8-12 HR-OLD EMBRYOS AND CONTINUES THROUGH DEVELOPMENT UP TO CC LATE LARVAL STAGE. IN THE HEAD REGION, DETECTED AT STAGE 10 IN THE CC MAXILLARY AND LABIAL SEGMENT PRIMORDIA, AND IN LATER STAGES, IN CC THE PROSPECTIVE ANTENNAL AND MANDIBULAR SEGMENT. IN THE EPIDERMIS, CC EXPRESSION IS SEEN FROM STAGE 11 IN THORACIC AND ABDOMINAL LATERAL CC PATCHES. EXPRESSION IN THE INTESTINAL TRACT BEGINS AT STAGE 13, CC CONTINUES THROUGH STAGES 14 AND 15 IN THE ENDODERM OF THE ANTERIOR CC MIDGUT AND AT STAGE 16, IS FOUND IN THE POSTERIOR END. EXPRESSION CC IN THE IMAGINAL DISKS IS SEEN FROM LATE THIRD-INSTAR LARVAE IN CC THE PROSPECTIVE THORAX, CLAW ORGAN, ANTENNA, SCUTELLUM AND WING CC BLADE. CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- SIMILARITY: CONTAINS 1 OAR DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08401; AAA28840.1; -. DR HSSP; P06601; 1FJL. DR FlyBase; FBgn0000061; al. DR InterPro; IPR003654; Homeo_OAR. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF03826; OAR; 1. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS50803; OAR; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DNA_BIND 85 144 HOMEOBOX. FT DOMAIN 378 391 OAR. FT DOMAIN 251 283 PRO-RICH. FT DOMAIN 290 360 GLN/PRO-RICH. FT DOMAIN 362 366 POLY-PRO. SQ SEQUENCE 408 AA; 43644 MW; 99F5C8CF787EF99F CRC64; MGISEEIKLE ELPQEAKLAH PDAVVLVDRA PGSSAASAGA ALTVSMSVSG GAPSGASGAS GGTNSPVSDG NSDCEADEYA PKRKQRRYRT TFTSFQLEEL EKAFSRTHYP DVFTREELAM KIGLTEARIQ VWFQNRRAKW RKQEKVGPQS HPYNPYLPGG AATMQTVVGA ALPPNPFTHL GFQLRKPFDA QHAANLAAFR YPHLSAAPMI PSGYFNQFQR APPHMLPHGM AGMYSPSSSF QSLLANMTAV PRGPPLGKPP ALLVGSPDLH SPNHMLASPP TSPASGHASQ HQQHPTAHPP PPQAPPQMPV GVQPAQLSPQ QLVGIALTQQ ASSLSPTQTS PVALTLSHSP QRQLPPPSHQ APPPPPRAAT PPEDRRTSSI AALRLKAREH ELKLELLRQN GHGNDVVS // ID AMAL_DROME STANDARD; PRT; 333 AA. AC P15364; Q9V3A5; DT 01-APR-1990 (Rel. 14, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Amalgam protein precursor. GN AMA OR BG:DS00276.6 OR CG2198. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=89028670; PubMed=3141062; RA Seeger M.A., Haffley L., Kaufman T.C.; RT "Characterization of amalgam: a member of the immunoglobulin RT superfamily from Drosophila."; RL Cell 55:589-600(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Celniker S.E., Pfeiffer B.D., Knafels J., Martin C.H., Mayeda C.A., RA Palazzolo M.J.; RT "Complete sequence of the Antennapedia complex of Drosophila."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR CC (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 IMMUNOGLOBULIN-LIKE V-TYPE DOMAIN. CC -!- SIMILARITY: CONTAINS 2 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23561; AAA28367.1; -. DR EMBL; AE001572; AAD19797.1; -. DR EMBL; AE003674; AAF54084.1; -. DR EMBL; AY051911; AAK93335.1; -. DR PIR; A31923; A31923. DR FlyBase; FBgn0000071; Ama. DR GO; GO:0005886; C:plasma membrane; IDA. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR Pfam; PF00047; ig; 3. DR SMART; SM00408; IGc2; 2. DR PROSITE; PS50835; IG_LIKE; 3. KW Immunoglobulin domain; Glycoprotein; Membrane; GPI-anchor; Signal; KW Repeat. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 ? AMALGAM PROTEIN. FT PROPEP ? 333 REMOVED IN MATURE FORM (POTENTIAL). FT DOMAIN 25 128 IG-LIKE V-TYPE. FT DOMAIN 139 223 IG-LIKE C2-TYPE 1. FT DOMAIN 230 323 IG-LIKE C2-TYPE 2. FT DISULFID 46 117 PROBABLE. FT DISULFID 161 208 PROBABLE. FT DISULFID 251 307 PROBABLE. FT CARBOHYD 45 45 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 308 308 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 83 83 Q -> K (IN REF. 1). SQ SEQUENCE 333 AA; 36387 MW; F644753DE3DB25F1 CRC64; MARLRLLIGL IFCLAISLDS VLSAPVISQI SKDVVASVGD SVEFNCTVEE VGQLSVSWAK RPSESDTNSV VLSMRNILSL PDQRYNVTVT EGPKTGSAIY TFRIQNIEVS DMGPYECQVL VSATEKVTKK LSLQIKTPPV IAENTPKSTL VTEGQNLELT CHANGFPKPT ISWAREHNAV MPAGGHLLAE PTLRIRSVHR MDRGGYYCIA QNGEGQPDKR LIRVEVEFRP QIAVQRPKIA QMVSHSAELE CSVQGYPAPT VVWHKNGVPL QSSRHHEVAN TASSSGTTTS VLRIDSVGEE DFGDYYCNAT NKLGHADARL HLFQTVIPVP SLS // ID AMN_DROME STANDARD; PRT; 170 AA. AC Q24049; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Amnesiac neuropeptide precursor. GN AMN. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; TISSUE=Head; RX MEDLINE=95273960; PubMed=7754370; RA Feany M.B., Quinn W.G.; RT "A neuropeptide gene defined by the Drosophila memory mutant RT amnesiac."; RL Science 268:869-872(1995). CC -!- FUNCTION: REQUIRED FOR ASSOCIATIVE LEARNING AND MEMORY. CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U22825; AAC46587.2; -. DR FlyBase; FBgn0000076; amn. DR GO; GO:0005184; F:neuropeptide hormone activity; NAS. DR GO; GO:0019933; P:cAMP-mediated signaling; NAS. DR GO; GO:0007611; P:learning and/or memory; IMP. DR GO; GO:0008016; P:regulation of heart rate; NAS. DR GO; GO:0045473; P:response to ethanol (sensu Insecta); NAS. KW Neuropeptide; Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 170 AMNESIAC NEUROPEPTIDE. SQ SEQUENCE 170 AA; 19410 MW; 66D79604DC0445A7 CRC64; MLWRCTAYYC FTLFFLLFRA SALRRRVVSG SKGSAALALC RQFEQLSASR RERAEECRTT QLRYHYHRNG AQSRSLCAAV LCCKRSYIPR PNFSCFSLVF PVGQRFAAAR TRFGPTLVAS WPLCNDSETK VLTKWPSCSL IGRRSVPRGQ PKFSRENPRA LSPSLLGEMR // ID AMOS_DROME STANDARD; PRT; 198 AA. AC Q9Y0A7; Q9VJ76; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Basic helix-loop-helix transcription factor Amos (Reduced olfactory DE organs protein) (Rough eye protein) (Absent MD neurons and olfactory DE sensilla protein) (Amos protein). GN AMOS OR ROI OR ROLO OR CG10393. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC STRAIN=Oregon-R; RX MEDLINE=20170246; PubMed=10707973; RA Goulding S.E., zur Lage P., Jarman A.P.; RT "Amos, a proneural gene for Drosophila olfactory sense organs that is RT regulated by lozenge."; RL Neuron 25:69-78(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=20170245; PubMed=10707972; RA Huang M.L., Hsu C.H., Chien C.T.; RT "The proneural gene amos promotes multiple dendritic neuron formation RT in the Drosophila peripheral nervous system."; RL Neuron 25:57-67(2000). CC -!- FUNCTION: TRANSCRIPTION FACTOR INVOLVED IN EARLY NEUROGENESIS. CC PROMOTES MULTIPLE DENDRITIC (MD) NEURON FORMATION. REQUIRED FOR CC OLFACTORY SENSILLA. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. INTERACTS WITH DAUGHTERLESS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: DURING EMBRYONIC DEVELOPMENT, AMOS IS CC EXPRESSED IN PATCHES OF ECTODERMAL CELLS, AND THE EXPRESSION IS CC QUICKLY RESTRICTED TO SENSORY ORGAN PRECURSORS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF166113; AAD45410.1; -. DR EMBL; AE003659; AAF53678.1; -. DR HSSP; P25912; 1HLO. DR FlyBase; FBgn0003270; amos. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Nuclear protein; Transcription regulation; Developmental protein; KW Neurogenesis. FT DOMAIN 111 128 SER-RICH. FT DNA_BIND 138 150 BASIC DOMAIN. FT DOMAIN 151 191 HELIX-LOOP-HELIX MOTIF. FT CONFLICT 25 25 S -> G (IN REF. 1). SQ SEQUENCE 198 AA; 22569 MW; F1D22AF2BA1C670B CRC64; MLTNNELMEQ FYFPDEAPAI PEFLSNDTFQ QLEQLMYQQE FSTSDSQSDG ANSCSLEMYY DTPSVLELEH MLNAQEQQQH HLQANPLGKN QGRSPRYWNK QQRSKPYDKL STSMSSSTSS ASSSSSSSAG FGGEVLKKRR LAANARERRR MNSLNDAFDK LRDVVPSLGH DRRLSKYETL QMAQAYIGDL VTLLSRDY // ID AMYA_DROME STANDARD; PRT; 494 AA. AC P08144; Q27582; Q27583; Q27584; Q27887; Q961R0; Q969D2; Q9BH42; AC Q9BH55; Q9BPT4; Q9BPT5; Q9BPT6; Q9BPT7; Q9BPT8; Q9BPT9; Q9BPU0; AC Q9BPU1; Q9V7Y8; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-amylase A precursor (EC 3.2.1.1) (1,4-alpha-D-glucan DE glucanohydrolase). GN AMY-P OR AMYA OR CG18730/CG18640. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=87066719; PubMed=3024105; RA Boer P.H., Hickey D.A.; RT "The alpha-amylase gene in Drosophila melanogaster: nucleotide RT sequence, gene structure and expression motifs."; RL Nucleic Acids Res. 14:8399-8411(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=1420#1, AO168, J87, KO123, KO140, L16, TN22, TN256, and TN329; RX MEDLINE=96042908; PubMed=8536971; RA Inomata N., Shibata H., Okuyama E., Yamazaki T.; RT "Evolutionary relationships and sequence variation of alpha-amylase RT variants encoded by duplicated genes in the Amy locus of Drosophila RT melanogaster."; RL Genetics 141:237-244(1995). RN [3] RP SEQUENCE FROM N.A., AND VARIANTS. RC STRAIN=JP-1, JP-5, JP-15, JP-35, JP-55, JP-60, JP-65, JP-70, JP-75, RC JP-84, JP-169, JP-186, JP-190, KN-3, KN-7, KN-9, KN-10, KN-12, KN-15, RC KN-17, KN-21, KN-22, KN-23, KN-27, and KN-28; RX MEDLINE=21100343; PubMed=11156987; RA Araki H., Inomata N., Yamazaki T.; RT "Molecular evolution of duplicated amylase gene regions in Drosophila RT melanogaster: evidence of positive selection in the coding regions and RT selective constraints in the cis-regulatory regions."; RL Genetics 157:667-677(2001). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- COFACTOR: BINDS 1 CALCIUM ION AND 1 CHLORIDE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- POLYMORPHISM: AT LEAST 6 ELECTROPHORETIC ISOZYMES ARE KNOWN: AMY1, CC AMY2, AMY3, AMY4, AMY5 AND AMY6. STRAINS J87 AND KO123 EXPRESS CC AMY2; KO140 AND 1420#1 EXPRESS AMY4; L16 EXPRESSES AMY5. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04569; CAA28238.1; -. DR EMBL; L22716; AAA92226.1; -. DR EMBL; L22719; AAA92229.1; -. DR EMBL; L22721; AAA92231.1; -. DR EMBL; L22725; AAA92235.1; -. DR EMBL; L22726; AAA92239.1; -. DR EMBL; L22729; AAA92240.1; -. DR EMBL; L22731; AAA92234.1; -. DR EMBL; L22733; AAA92241.1; -. DR EMBL; L22735; AAA92236.1; -. DR EMBL; AB042862; BAB32503.1; -. DR EMBL; AB042863; BAB32504.1; -. DR EMBL; AB042864; BAB32505.1; -. DR EMBL; AB042865; BAB32506.1; -. DR EMBL; AB042866; BAB32507.1; -. DR EMBL; AB042867; BAB32508.1; -. DR EMBL; AB042868; BAB32509.1; -. DR EMBL; AB042869; BAB32510.1; -. DR EMBL; AB042870; BAB32511.1; -. DR EMBL; AB042871; BAB32512.1; -. DR EMBL; AB042872; BAB32513.1; -. DR EMBL; AB042873; BAB32514.1; -. DR EMBL; AB042874; BAB32515.1; -. DR EMBL; AB042875; BAB32516.1; -. DR EMBL; AB042876; BAB32517.1; -. DR EMBL; AB042877; BAB32518.1; -. DR EMBL; AB042878; BAB32519.1; -. DR EMBL; AB042879; BAB32520.1; -. DR EMBL; AB042880; BAB32521.1; -. DR EMBL; AB042881; BAB32522.1; -. DR EMBL; AB042882; BAB32523.1; -. DR EMBL; AB042883; BAB32524.1; -. DR EMBL; AB042884; BAB72090.1; -. DR EMBL; AB042885; BAB72091.1; -. DR EMBL; AB042886; BAB72092.1; -. DR EMBL; AB043043; BAB32541.1; -. DR EMBL; AE003804; AAF57896.1; -. DR EMBL; AY051425; AAK92849.1; -. DR PIR; S58956; S58956. DR PIR; S58957; S58957. DR PIR; S58958; S58958. DR PIR; S58965; S58965. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0000079; Amy-p. DR InterPro; IPR006589; Alp_amyl_cat_sub. DR InterPro; IPR006048; Alpha_amyl_C. DR InterPro; IPR006047; Alpha_amyl_cat. DR InterPro; IPR006046; Glyco_hydro_13. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. KW Carbohydrate metabolism; Hydrolase; Glycosidase; Calcium-binding; KW Chloride; Signal; Pyrrolidone carboxylic acid; Polymorphism. FT SIGNAL 1 18 FT CHAIN 19 494 ALPHA-AMYLASE A. FT MOD_RES 19 19 PYRROLIDONE CARBOXYLIC ACID (BY FT SIMILARITY). FT ACT_SITE 204 204 BY SIMILARITY. FT ACT_SITE 241 241 BY SIMILARITY. FT ACT_SITE 306 306 BY SIMILARITY. FT METAL 116 116 CALCIUM (BY SIMILARITY). FT METAL 165 165 CALCIUM (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT METAL 174 174 CALCIUM (BY SIMILARITY). FT METAL 208 208 CALCIUM (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT BINDING 202 202 CHLORIDE (BY SIMILARITY). FT BINDING 304 304 CHLORIDE (BY SIMILARITY). FT BINDING 343 343 CHLORIDE (BY SIMILARITY). FT DISULFID 46 102 BY SIMILARITY. FT DISULFID 153 167 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 448 460 BY SIMILARITY. FT VARIANT 11 11 A -> S (IN STRAIN KN-28). FT VARIANT 16 16 A -> V (IN STRAINS KN-22 AND KN-23). FT VARIANT 71 71 S -> R (IN STRAINS KN-3, KN-9, KN-10 AND FT L16). FT VARIANT 121 121 D -> G (IN STRAINS TN256, 1420#1 AND FT KO140). FT VARIANT 121 121 D -> N (IN STRAINS KN-3, KN-9, KN-10 AND FT L16). FT VARIANT 138 138 S -> T (IN STRAINS JP-75, KN-7, KN-15, FT KN-17, KN-21 AND KN-23). FT VARIANT 144 144 Y -> H (IN STRAIN CANTON-S). FT VARIANT 156 156 S -> R (IN STRAINS 1420#1, KN-3, KN-9, FT KN-10, KO140, L16 AND TN256). FT VARIANT 181 181 Y -> N (IN STRAIN CANTON-S). FT VARIANT 231 231 A -> S (IN STRAINS JP-70, KN-17 AND KN- FT 21). FT VARIANT 278 278 D -> N (IN STRAINS 1420#1, KO140, KN-3, FT KN-9, KN-10 AND L16). FT VARIANT 284 284 T -> I (IN STRAIN KN-21). FT VARIANT 398 398 T -> A (IN STRAINS 1420#1, J87, JP-60, FT JP-70, JP-75, KO123, KO140, KN-9, KN-15, FT KN-17, KN-21, L16 AND TN256). FT VARIANT 401 401 S -> L (IN STRAIN BERKELEY). FT VARIANT 403 403 E -> A (IN STRAINS J87, JP-60 AND KO123). FT VARIANT 465 465 V -> I (IN STRAIN 1420#1). FT VARIANT 474 474 S -> Y (IN STRAIN KN-23). FT VARIANT 476 476 N -> Y (IN STRAINS BERKELEY, JP-1, JP-5, FT JP-15, JP-35, JP-55, JP-65, JP-84, KN-12, FT KN-22 AND KN-27). SQ SEQUENCE 494 AA; 53745 MW; B477D3B44754C298 CRC64; MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGYAGVQV SPVNENAVKD SRPWWERYQP ISYKLETRSG NEEQFASMVK RCNAVGVRTY VDVVFNHMAA DGGTYGTGGS TASPSSKSYP GVPYSSLDFN PTCAISNYND ANEVRNCELV GLRDLNQGNS YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKNLNTDHGF ASGSKAYIVQ EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF TDTDQGPPTT DGHNIASPIF NSDNSCSGGW VCEHRWRQIY NMVAFRNTVG SDEIQNWWDN GSNQISFSRG SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRASINIGSS EDDGVLAIHV NAKL // ID AMYB_DROME STANDARD; PRT; 494 AA. AC P81641; Q27578; Q27581; Q27585; Q27882; Q27885; Q27897; Q9V7Z0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-amylase B precursor (EC 3.2.1.1) (1,4-alpha-D-glucan DE glucanohydrolase). GN AMY-D OR AMYB OR CG17876. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=TN329; RA Okuyama E., Yamazaki T.; RT "Nucleotide sequences of the duplicated Amylase structural genes in RT Drosophila melanogaster."; RL Proc. Jpn. Acad., B, Phys. Biol. Sci. 64:274-277(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=1420#1, AO168, KO123, KO140, J87, L16, TN22, TN256, and TN329; RX MEDLINE=96042908; PubMed=8536971; RA Inomata N., Shibata H., Okuyama E., Yamazaki T.; RT "Evolutionary relationships and sequence variation of alpha-amylase RT variants encoded by duplicated genes in the Amy locus of Drosophila RT melanogaster."; RL Genetics 141:237-244(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 1-22 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=87066719; PubMed=3024105; RA Boer P.H., Hickey D.A.; RT "The alpha-amylase gene in Drosophila melanogaster: nucleotide RT sequence, gene structure and expression motifs."; RL Nucleic Acids Res. 14:8399-8411(1986). RN [5] RP SEQUENCE OF 1-13 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92313312; PubMed=1616481; RA Hawley S.A., Doane W.W., Norman R.A.; RT "Molecular analysis of cis-regulatory sequences at the alpha-amylase RT locus in Drosophila melanogaster."; RL Biochem. Genet. 30:257-277(1992). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- COFACTOR: BINDS 1 CALCIUM ION AND 1 CHLORIDE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- POLYMORPHISM: AT LEAST 6 ELECTROPHORETIC ISOZYMES ARE KNOWN: AMY1, CC AMY2, AMY3, AMY4, AMY5 AND AMY6. STRAINS KO123 EXPRESSES AMY1; CC J87 EXPRESSES AMY3; 1420#1, L16 AND TN256 EXPRESS AMY6. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X84405; CAA59126.1; -. DR EMBL; L22717; AAA92227.1; -. DR EMBL; L22718; AAA92228.1; -. DR EMBL; L22720; AAA92230.1; -. DR EMBL; L22724; AAA92232.1; -. DR EMBL; L22727; AAA92233.1; -. DR EMBL; L22728; AAA92242.1; -. DR EMBL; L22730; AAA92237.1; -. DR EMBL; L22732; AAA92243.1; -. DR EMBL; L22734; AAA92238.1; -. DR EMBL; AE003804; AAF57894.1; -. DR EMBL; X04570; CAA28239.1; -. DR EMBL; X84410; CAA59130.1; -. DR PIR; S58951; S58951. DR PIR; S58954; S58954. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0000078; Amy-d. DR InterPro; IPR006589; Alp_amyl_cat_sub. DR InterPro; IPR006048; Alpha_amyl_C. DR InterPro; IPR006047; Alpha_amyl_cat. DR InterPro; IPR006046; Glyco_hydro_13. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. KW Carbohydrate metabolism; Hydrolase; Glycosidase; Calcium-binding; KW Chloride; Signal; Pyrrolidone carboxylic acid; Polymorphism. FT SIGNAL 1 18 FT CHAIN 19 494 ALPHA-AMYLASE B. FT MOD_RES 19 19 PYRROLIDONE CARBOXYLIC ACID (BY FT SIMILARITY). FT ACT_SITE 204 204 BY SIMILARITY. FT ACT_SITE 241 241 BY SIMILARITY. FT ACT_SITE 306 306 BY SIMILARITY. FT METAL 116 116 CALCIUM (BY SIMILARITY). FT METAL 165 165 CALCIUM (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT METAL 174 174 CALCIUM (BY SIMILARITY). FT METAL 208 208 CALCIUM (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT BINDING 202 202 CHLORIDE (BY SIMILARITY). FT BINDING 304 304 CHLORIDE (BY SIMILARITY). FT BINDING 343 343 CHLORIDE (BY SIMILARITY). FT DISULFID 46 102 BY SIMILARITY. FT DISULFID 153 167 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 448 460 BY SIMILARITY. FT VARIANT 11 11 A -> S (IN STRAINS OREGON-R AND FT BERKELEY). FT VARIANT 71 71 S -> R (IN STRAINS 1420#1, KO123, TN22 FT AND TN256). FT VARIANT 121 121 D -> G (IN STRAINS 1420#1, KO123, TN22 FT AND TN256). FT VARIANT 138 138 S -> T (IN STRAIN L16). FT VARIANT 156 156 S -> R (IN STRAINS 1420#1, KO123, TN22 FT AND TN256). FT VARIANT 278 278 D -> N (IN STRAINS 1420#1, AO168, J87, FT KO123, TN22 AND TN256). FT VARIANT 398 398 T -> A (IN STRAIN BERKELEY). FT VARIANT 401 401 S -> L (IN STRAIN BERKELEY). FT VARIANT 403 403 E -> A (IN STRAINS 1420#1, AO168, J87, FT KO123, TN22 AND TN256). FT VARIANT 410 410 N -> S (IN STRAIN BERKELEY). FT VARIANT 465 465 V -> I (IN STRAIN KO140). FT VARIANT 476 476 Y -> N (IN STRAINS 1420#1, AO168, KO123, FT KO140, J87, L16, TN22 AND TN256). SQ SEQUENCE 494 AA; 53794 MW; B477CB031754C298 CRC64; MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGYAGVQV SPVNENAVKD SRPWWERYQP ISYKLETRSG NEEQFASMVK RCNAVGVRTY VDVVFNHMAA DGGTYGTGGS TASPSSKSYP GVPYSSLDFN PTCAISNYND ANEVRNCELV GLRDLNQGNS YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKNLNTDHGF ASGSKAYIVQ EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF TDTDQGPPTT DGHNIASPIF NSDNSCSGGW VCEHRWRQIY NMVAFRNTVG SDEIQNWWDN GSNQISFSRG SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRASIYIGSS EDDGVLAIHV NAKL // ID AMYR_DROME STANDARD; PRT; 493 AA. AC O18408; Q9V7S3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL OR CG8221. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98284020; PubMed=9618501; RA Da Lage J.-L., Renard E., Chartois F., Lemeunier F., Cariou M.-L.; RT "Amyrel, a paralogous gene of the amylase gene family in Drosophila RT melanogaster and the Sophophora subgenus."; RL Proc. Natl. Acad. Sci. U.S.A. 95:6848-6853(1998). RN [2] RP REVISIONS. RA Da Lage J.-L.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- COFACTOR: BINDS 1 CALCIUM ION AND 1 CHLORIDE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: MIDGUT AND FAT BODY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING SECOND AND THIRD LARVAL CC INSTARS, BUT NOT IN THE ADULT. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF022713; AAD09147.2; -. DR EMBL; U69607; AAD08845.1; -. DR EMBL; AY052055; AAK93479.1; -. DR EMBL; AE003806; AAF57971.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0020506; Amyrel. DR InterPro; IPR006589; Alp_amyl_cat_sub. DR InterPro; IPR006048; Alpha_amyl_C. DR InterPro; IPR006047; Alpha_amyl_cat. DR InterPro; IPR006046; Glyco_hydro_13. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. KW Carbohydrate metabolism; Hydrolase; Glycosidase; Calcium-binding; KW Chloride; Signal; Pyrrolidone carboxylic acid. FT SIGNAL 1 19 BY SIMILARITY. FT CHAIN 20 493 ALPHA-AMYLASE-RELATED PROTEIN. FT MOD_RES 20 20 PYRROLIDONE CARBOXYLIC ACID (BY FT SIMILARITY). FT ACT_SITE 207 207 BY SIMILARITY. FT ACT_SITE 244 244 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT METAL 117 117 CALCIUM (BY SIMILARITY). FT METAL 168 168 CALCIUM (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT METAL 177 177 CALCIUM (BY SIMILARITY). FT METAL 211 211 CALCIUM (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT BINDING 205 205 CHLORIDE (BY SIMILARITY). FT BINDING 307 307 CHLORIDE (BY SIMILARITY). FT BINDING 342 342 CHLORIDE (BY SIMILARITY). FT DISULFID 47 103 BY SIMILARITY. FT DISULFID 156 170 BY SIMILARITY. FT DISULFID 375 381 BY SIMILARITY. FT DISULFID 417 440 POTENTIAL. FT DISULFID 447 459 BY SIMILARITY. FT CONFLICT 2 2 S -> F (IN REF. 4). FT CONFLICT 7 7 A -> T (IN REF. 1 AND 4). FT CONFLICT 18 18 V -> L (IN REF. 4). FT CONFLICT 69 69 I -> L (IN REF. 4). FT CONFLICT 127 127 V -> A (IN REF. 4). FT CONFLICT 157 157 V -> E (IN REF. 4). FT CONFLICT 253 253 D -> V (IN REF. 1 AND 4). FT CONFLICT 310 310 S -> N (IN REF. 1 AND 4). FT CONFLICT 340 340 T -> I (IN REF. 1 AND 4). FT CONFLICT 358 358 R -> Q (IN REF. 1 AND 4). FT CONFLICT 466 467 MS -> VN (IN REF. 1 AND 4). SQ SEQUENCE 493 AA; 55354 MW; 0175C85CD56BECCC CRC64; MSKFALALTL CLAGSLSVAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS GDFDGVVVGT AGTEAEPSKK SFPGVPYTAQ DFHPTCVITD WNDRFQVQQC ELVGLKDLDQ SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF IFQEVIDHGH ETDSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TDWGFLPSGQ ALTFVDNHDS QRDAGAVLNY KSPRQYKMAT AFHLAYPYGT SRVMSSFAFD DHDTPPPRDA QERIISPEFD ADGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN KGFLAINNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTMSENG YGYIHIGSDD FDGVLALHVD AKV // ID ANA_DROME STANDARD; PRT; 474 AA. AC Q26307; Q9V524; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Anachronism protein precursor. GN ANA OR CG8084. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye imaginal disk; RX MEDLINE=93327423; PubMed=7916657; RA Ebens A.J., Garren H., Cheyette B.N.R., Zipursky S.L.; RT "The Drosophila anachronism locus: a glycoprotein secreted by glia RT inhibits neuroblast proliferation."; RL Cell 74:15-27(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NEGATIVELY REGULATES PROLIFERATION OF NEURONAL PRECURSOR CC CELLS, THEREBY CONTROLLING THE TIMING OF POSTEMBRYONIC CC NEUROGENESIS. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: SYNTHESIZED IN SOME GLIAL CELLS AND SECRETED. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S63815; AAB27582.1; -. DR EMBL; AE003834; AAF58998.1; -. DR FlyBase; FBgn0011746; ana. KW Glycoprotein; Signal; Developmental protein; Neurogenesis. FT SIGNAL 1 33 POTENTIAL. FT CHAIN 34 474 ANACHRONISM PROTEIN. FT DOMAIN 453 462 POLY-HIS. FT CARBOHYD 54 54 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 62 62 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 73 73 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 116 116 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 144 144 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 342 342 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 388 388 A -> G (IN REF. 1). SQ SEQUENCE 474 AA; 54015 MW; FE8A43042BB595A1 CRC64; MASAMRGEKC ERSRIRELVL ILSLITMAGD SRATPFDPSF FIEGVQSEVV NPFNRTILNR FNLTEEQILS IQNRSNPNMR DDSAQSSNQQ YLQQVATQRL NDIFKRVQKA ISNEPNGSAS KEKAGFPICN AETTNPEDWS LGNNVTLQFA SSVFISNNDD RLSSALLRLY KTNPGQTREH NPGQASTQPI STENPGNTAP NCAEQPPVGP QIRVTVSIVH QQRKKQRKKR TCNTAMLSSS STGWVEIDVK CALAYWEQQH RQQLRQQQPL QPQLTASVVG ILMIEVHDDE ENLLRPGLYF APPTCDQADI AVPWSVYRTE PFKSHLASWT LPRKPRLDIF FNGSNSMKNS YNTPKSRAFI ESTTSNSPTI DNQLDESGEY ESQQRVHAPL VHHRRHHHNH QQPESESESA QLEAEIEAEE LMSSASNSEQ QMEPISNHHR HRTGHHHPHH QLHQHHHHHH RHTKHHRIPA HKQE // ID ANDP_DROME STANDARD; PRT; 57 AA. AC P21663; O16822; O16823; O16824; Q9VA90; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Andropin precursor. GN ANP OR ANR OR CG1361. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=91114699; PubMed=1899226; RA Samakovlis C., Kylsten P., Kimbrell D.A., Engstroem A., Hultmark D.; RT "The andropin gene and its product, a male-specific antibacterial RT peptide in Drosophila melanogaster."; RL EMBO J. 10:163-169(1991). RN [2] RP SEQUENCE FROM N.A., AND VARIANTS. RC STRAIN=B009, B141, B205, B316, Z10, Z18, Z22, and Z24; RX MEDLINE=97476321; PubMed=9335607; RA Clark A.G., Wang L.; RT "Molecular population genetics of Drosophila immune system genes."; RL Genetics 147:713-724(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K-1, K-2, K-3, K-4, and K-5; RX MEDLINE=21962106; PubMed=11965438; RA Date-Ito A., Kasahara K., Sawai H., Chigusa S.I.; RT "Rapid evolution of the male-specific antibacterial protein andropin RT gene in Drosophila."; RL J. Mol. Evol. 54:665-670(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MALE-SPECIFIC PEPTIDE WITH MODERATE ACTIVITY AGAINST CC GRAM-POSITIVE BACTERIA. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: EJACULATORY DUCT OF ADULT MALES. CC -!- INDUCTION: IN RESPONSE TO MATING. CC -!- SIMILARITY: STRUCTURALLY RELATED TO CECROPINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16972; CAA34842.1; -. DR EMBL; X56726; CAA40046.1; -. DR EMBL; AF018985; AAB82482.1; -. DR EMBL; AF018986; AAB82483.1; -. DR EMBL; AF018987; AAB82484.1; -. DR EMBL; AF018988; AAB82485.1; -. DR EMBL; AF018989; AAB82486.1; -. DR EMBL; AF018990; AAB82487.1; -. DR EMBL; AF018991; AAB82488.1; -. DR EMBL; AF018992; AAB82489.1; -. DR EMBL; AB047046; BAB78551.1; -. DR EMBL; AB047047; BAB78552.1; -. DR EMBL; AB047048; BAB78553.1; -. DR EMBL; AB047049; BAB78554.1; -. DR EMBL; AB047050; BAB78555.1; -. DR EMBL; AE003773; AAF57024.1; -. DR PIR; S13450; S13450. DR FlyBase; FBgn0000094; Anp. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0008224; F:Gram-positive antibacterial peptide activity; IDA. DR GO; GO:0003798; F:male-specific antibacterial peptide activity; IDA. DR GO; GO:0006965; P:anti-Gram-positive bacterial polypeptide in...; IDA. DR GO; GO:0006962; P:male-specific antibacterial humoral response; IDA. KW Insect immunity; Antibiotic; Signal; Polymorphism. FT SIGNAL 1 23 POTENTIAL. FT PEPTIDE 24 57 ANDROPIN. FT VARIANT 9 9 V -> F (IN STRAIN B316). FT VARIANT 34 34 N -> S (IN STRAIN B205). FT VARIANT 44 44 I -> V (IN STRAIN B316). FT VARIANT 48 48 K -> N (IN STRAIN Z22). SQ SEQUENCE 57 AA; 6151 MW; EEA8CCCF59A09AB5 CRC64; MKYFVVLVVL ALILAISVGP SDAVFIDILD KVENAIHNAA QVGIGFAKPF EKLINPK // ID ANGE_DROME STANDARD; PRT; 354 AA. AC Q24239; Q9W1L3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Angel protein (Angel 39) (ANG39). GN ANGEL OR CG12273. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=96404965; PubMed=8809105; RA Kurzik-Dumke U., Zengerle A.; RT "Identification of a novel Drosophila melanogaster gene, angel, a RT member of a nested gene cluster at locus 59F4,5."; RL Biochim. Biophys. Acta 1308:177-181(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, HIGHEST CC EXPRESSION SEEN IN SECOND INSTAR LARVAE, PUPAE AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE CCR4/NOCTURIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X85743; CAA59746.1; -. DR EMBL; AE003461; AAF47045.1; -. DR EMBL; AY058301; AAL13530.1; -. DR PIR; S71925; S71925. DR FlyBase; FBgn0016762; angel. DR InterPro; IPR005135; Exo_endo_phos. DR Pfam; PF03372; Exo_endo_phos; 1. KW Developmental protein. FT CONFLICT 37 37 A -> T (IN REF. 1). FT CONFLICT 353 353 V -> A (IN REF. 1). SQ SEQUENCE 354 AA; 40306 MW; 1AABE3F3F393C56B CRC64; MYRSLLHNVS LKATSRIIRR SVSSQAKGAS GKRKQKAKEM ESSHDRNRRW TSLGNQAEGR DPHKCSSFKV VSYNILAQDL LLEHLFLYVG IPHEFLSWQR RQQNLLRELL KLDPDILCLQ EMQFDHLPVL VQRLRMGNGK KLAYVYKKKT GCRTDGCAIV YDSSKFELLD HQAVELYDQA VALLNRDNVA LFARFRFKKQ QEQQKEFVVA TTHLLFNTKR SDVRCAQVER ILEELQSFST DTPIVLTGDF NSLPDSSPIE FLVGKNGDVD STACPEPLHF EIIDSGEGTA STYQNEWVIV DYILRSLGSR SRHKLLPLSV YSLPSINRCI GAGQIPNYRL GSDHYALGAV FTVV // ID ANX9_DROME STANDARD; PRT; 324 AA. AC P22464; Q9VDF3; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Annexin IX. GN ANNIX OR CG5730. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 29-324 FROM N.A. RX MEDLINE=90293092; PubMed=2141610; RA Johnston P.A., Perin M.S., Reynolds G.A., Wasserman S.A., RA Suedhof T.C.; RT "Two novel annexins from Drosophila melanogaster. Cloning, RT characterization, and differential expression in development."; RL J. Biol. Chem. 265:11382-11388(1990). CC -!- DOMAIN: A PAIR OF ANNEXIN REPEATS MAY FORM ONE BINDING SITE FOR CC CALCIUM AND PHOSPHOLIPID. CC -!- SIMILARITY: BELONGS TO THE ANNEXIN FAMILY. CC -!- SIMILARITY: CONTAINS 4 ANNEXIN REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003733; AAF55841.1; -. DR EMBL; M34068; AAA28370.1; -. DR PIR; A42234; LUFF9. DR HSSP; P26256; 1AEI. DR FlyBase; FBgn0000083; AnnIX. DR InterPro; IPR001464; Annexin. DR Pfam; PF00191; annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR ProDom; PD000143; Annexin; 4. DR SMART; SM00335; ANX; 4. DR PROSITE; PS00223; ANNEXIN; 3. KW Annexin; Calcium/phospholipid-binding; Repeat. FT REPEAT 30 90 ANNEXIN 1. FT REPEAT 102 162 ANNEXIN 2. FT REPEAT 185 246 ANNEXIN 3. FT REPEAT 261 321 ANNEXIN 4. FT CONFLICT 268 268 M -> L (IN REF. 2). SQ SEQUENCE 324 AA; 36057 MW; 6DBF1021A7CC0DCA CRC64; MSSAEYYPFK CTPTVYPADP FDPVEDAAIL RKAMKGFGTD EKAIIEILAR RGIVQRLEIA EAFKTSYGKD LISDLKSELG GKFEDVILAL MTPLPQFYAQ ELHDAISGLG TDEEAIIEIL CTLSNYGIKT IAQFYEQSFG KSLESDLKGD TSGHFKRLCV SLVQGNRDEN QGVDEAAAIA DAQALHDAGE GQWGTDESTF NSILITRSYQ QLRQIFLEYE NLSGNDIEKA IKREFSGSVE KGFLAIVKCC KSKIDYFSER LHDSMAGMGT KDKTLIRIIV SRSEIDLGDI KEAFQNKYGK SLESWIKEDA ETDIGYVLVT LTAW // ID ANXX_DROME STANDARD; PRT; 320 AA. AC P22465; Q27586; Q9W5W5; DT 01-AUG-1991 (Rel. 19, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Annexin X. GN ANNX OR CG9579. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90293092; PubMed=2141610; RA Johnston P.A., Perin M.S., Reynolds G.A., Wasserman S.A., RA Suedhof T.C.; RT "Two novel annexins from Drosophila melanogaster. Cloning, RT characterization, and differential expression in development."; RL J. Biol. Chem. 265:11382-11388(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95225982; PubMed=7710691; RA Benevolenskaya E.V., Nurminsky D.I., Gvozdev V.A.; RT "Structure of the Drosophila melanogaster annexin X gene."; RL DNA Cell Biol. 14:349-357(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 199-320 FROM N.A. RC STRAIN=GT WA; RA Benevolenskaya E.V., Gvozdev V.A.; RL Submitted (XXX-1995) to the EMBL/GenBank/DDBJ databases. CC -!- DOMAIN: A PAIR OF ANNEXIN REPEATS MAY FORM ONE BINDING SITE FOR CC CALCIUM AND PHOSPHOLIPID. CC -!- SIMILARITY: BELONGS TO THE ANNEXIN FAMILY. CC -!- SIMILARITY: CONTAINS 4 ANNEXIN REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M34069; AAA28371.1; -. DR EMBL; X78323; CAA55126.1; -. DR EMBL; AE002611; AAF45380.1; -. DR EMBL; L41945; AAB51186.1; -. DR EMBL; AY061328; AAL28876.1; -. DR HSSP; P08758; 1AVR. DR FlyBase; FBgn0000084; AnnX. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA. DR InterPro; IPR001464; Annexin. DR Pfam; PF00191; annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR ProDom; PD000143; Annexin; 4. DR SMART; SM00335; ANX; 4. DR PROSITE; PS00223; ANNEXIN; 2. KW Annexin; Calcium/phospholipid-binding; Repeat. FT REPEAT 24 84 ANNEXIN 1. FT REPEAT 96 156 ANNEXIN 2. FT REPEAT 180 241 ANNEXIN 3. FT REPEAT 256 316 ANNEXIN 4. FT CONFLICT 216 216 V -> E (IN REF. 5). FT CONFLICT 235 235 H -> HD (IN REF. 5). FT CONFLICT 291 291 R -> Q (IN REF. 5). FT CONFLICT 303 303 A -> AD (IN REF. 1). SQ SEQUENCE 320 AA; 35590 MW; FF204A52B7B8268E CRC64; MEYKPVPTVK DAAPFDASQD AQVLRAAMKG FGTDEQEIID VLVGRSNQQR QTIKAVYEAE FERDLVDDLK DELGGKFEDV IVGLMMPPVE YLCKQLHAAM AGIGTEEATL VEILCTKTNE EMAQIVAVYE ERYQRPLAEQ MCSETSGFFR RLLTLIVTGV RDGLDTPVDV GQAKEQAAQL YSAGEAKLGT DEEVFNRIMS HASFPQLRLV FEEYKVLSGQ TIEQAIKHEM SDELHEAMMA IVECVQSPAA FFANRLYKAM NGAGTDDATL IRIIVSRSEI DLETIKQEFE RIYNRTLHSA VVAETSGDYK RALTALLGSA // ID AP1_DROME STANDARD; PRT; 289 AA. AC P18289; Q9V5G4; DT 01-NOV-1990 (Rel. 16, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor AP-1 (Jun-related antigen) (dJRA) (dJun). GN JRA OR JUN OR CG2275. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90349599; PubMed=1696724; RA Zhang K., Chaillet J.R., Perkins L.A., Halazonetis T.D., Perrimon N.; RT "Drosophila homolog of the mammalian jun oncogene is expressed during RT embryonic development and activates transcription in mammalian RT cells."; RL Proc. Natl. Acad. Sci. U.S.A. 87:6281-6285(1990). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=90337318; PubMed=2116361; RA Perkins K.K., Admon A., Patel N., Tjian R.; RT "The Drosophila Fos-related AP-1 protein is a developmentally RT regulated transcription factor."; RL Genes Dev. 4:822-834(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=97367956; PubMed=9224723; RA Kockel L., Zeitlinger J., Staszewski L., Mlodzik M., Bohmann D.; RT "Jun in Drosophila development: redundant and nonredundant functions RT and regulation by two MAPK signal transduction pathways."; RL Genes Dev. 11:1748-1758(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TRANSCRIPTION FACTOR AP-1 BINDS AND RECOGNIZE THE CC ENHANCER DNA SEQUENCE: TGA(C/G)TCA. CC -!- SUBUNIT: AP-1/DJRA INTERACTS WITH AP-1/DFRA TO FORM A DIMER. CC DFRA-DJRA COMPLEX IS BOUND MORE STABLY TO THE AP-1 SITE THAN CC EITHER OF THE TWO PROTEINS ALONE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING EMBRYONIC DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE BZIP FAMILY. JUN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M36181; AAA28650.1; -. DR EMBL; X54144; CAA38083.1; -. DR EMBL; Y12573; CAA73154.1; -. DR EMBL; AE003831; AAM71059.1; -. DR EMBL; AY058562; AAL13791.1; -. DR PIR; A36011; TVFFJD. DR HSSP; P05412; 1FOS. DR TRANSFAC; T01996; -. DR FlyBase; FBgn0001291; Jra. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0007254; P:JNK cascade; IGI. DR GO; GO:0046844; P:micropyle formation; IMP. DR InterPro; IPR008917; Euk_transcr_DNA. DR InterPro; IPR005643; JNK. DR InterPro; IPR002112; Leuzip_Jun. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF00170; bZIP; 1. DR Pfam; PF03957; Jun; 1. DR PRINTS; PR00043; LEUZIPPRJUN. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW Transcription regulation; DNA-binding; Activator; Nuclear protein. FT DNA_BIND 217 239 BASIC MOTIF. FT DOMAIN 240 261 LEUCINE-ZIPPER. FT CONFLICT 267 268 QL -> HV (IN REF. 1 AND 3). SQ SEQUENCE 289 AA; 31021 MW; FCCA13A6D2AF32BF CRC64; MKTPVSAAAN LSIQNAGSSG ATAIQIIPKT EPVGEEGPMS LDFQSPNLNT STPNPNKRPG SLDLNSKSAK NKRIFAPLVI NSPDLSSKTV NTPDLEKILL SNNLMQTPQP GKVFPTKAGP VTVEQLDFGR GFEEALHNLH TNSQAFPSAN SAANSAANNT TAAAMTAVNN GISGGTFTYT NMTEGFSVIK DEPVNQASSP TVNPIDMEAQ EKIKLERKRQ RNRVAASKCR KRKLERISKL EDRVKVLKGE NVDLASIVKN LKDHVAQLKQ QVMEHIAAGC TVPPNSTDQ // ID APH1_DROME STANDARD; PRT; 238 AA. AC Q9VQG2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gamma-secretase subunit Aph-1 (Presenilin stabilization factor). GN APH-1 OR PSF OR CG2855. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Lee H.-J., Kim T.-W.; RT "PSF is essential for gamma-secretase activity and stabilization of RT presenilin and nicastrin."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION. RX MEDLINE=22105644; PubMed=12110170; RA Francis R., McGrath G., Zhang J., Ruddy D.A., Sym M., Apfeld J., RA Nicoll M., Maxwell M., Hai B., Ellis M.C., Parks A.L., Xu W., Li J., RA Gurney M., Myers R.L., Himes C.S., Hiebsch R., Ruble C., Nye J.S., RA Curtis D.; RT "aph-1 and pen-2 are required for Notch pathway signaling, RT gamma-secretase cleavage of betaAPP, and presenilin protein RT accumulation."; RL Dev. Cell 3:85-97(2002). RN [5] RP FUNCTION IN THE GAMMA-SECRETASE COMPLEX, AND INTERACTION WITH PEN-2; RP PSN AND NCT. RX MEDLINE=22547312; PubMed=12660785; RA Takasugi N., Tomita T., Hayashi I., Tsuruoka M., Niimura M., RA Takahashi Y., Thinakaran G., Iwatsubo T.; RT "The role of presenilin cofactors in the gamma-secretase complex."; RL Nature 422:438-441(2003). CC -!- FUNCTION: ESSENTIAL SUBUNIT OF THE GAMMA-SECRETASE COMPLEX, AN CC ENDOPROTEASE COMPLEX THAT CATALYZES THE INTRAMEMBRANE CLEAVAGE OF CC INTEGRAL MEMBRANE PROTEINS SUCH AS NOTCH. IT PROBABLY REPRESENTS A CC STABILIZING COFACTOR FOR THE PRESENILIN HOMODIMER THAT PROMOTES CC THE FORMATION OF A STABLE COMPLEX. CC -!- SUBUNIT: COMPONENT OF THE GAMMA-SECRETASE COMPLEX, A COMPLEX CC COMPOSED OF A PRESENILIN/PSN HOMODIMER, NICASTRIN (NCT), APH-1 AND CC PEN-2. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE APH-1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF508786; AAN63815.1; -. DR EMBL; AE003582; AAF51212.1; -. DR EMBL; AY051658; AAK93082.1; -. DR FlyBase; FBgn0031458; aph-1. KW Transmembrane. FT TRANSMEM 6 26 1 (POTENTIAL). FT TRANSMEM 32 52 2 (POTENTIAL). FT TRANSMEM 53 73 3 (POTENTIAL). FT TRANSMEM 105 125 4 (POTENTIAL). FT TRANSMEM 152 172 5 (POTENTIAL). FT TRANSMEM 178 198 6 (POTENTIAL). FT TRANSMEM 201 221 7 (POTENTIAL). SQ SEQUENCE 238 AA; 26437 MW; C61A24518DCA150F CRC64; MTLPEFFGCT FIAFGPPFAL FVFTIANDPV RIIILIAAAF FWLLSLLISS LWYALIPLKE FLAFGVVFSV CFQEAFRYII YRILRSTEQG LHAVAEDTRV TDNKHILAYV SGLGFGIISG MFALVNVLAD MSGPGTMGLK GGTELFFVTS AAQALSIILL HTFWSVIFFN AFDTNNYIHI GYVVFSHLFV SLITLLNANE LYTTTLLINY LVTILTGVLA FRVAGGTSRS FRKFITCQ // ID APH4_DROME STANDARD; PRT; 596 AA. AC Q24238; Q8IMH0; Q8SXW6; Q9VA19; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alkaline phosphatase 4 precursor (EC 3.1.3.1). GN APH-4 OR CG1462. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC TISSUE=Head; RX MEDLINE=20094770; PubMed=10628988; RA Yang M.Y., Wang Z., MacPherson M., Dow J.A.T., Kaiser K.; RT "A novel Drosophila alkaline phosphatase specific to the ellipsoid RT body of the adult brain and the lower Malpighian (renal) tubule."; RL Genetics 154:285-297(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: IMPORTANT ROLE IN NEURAL AND RENAL EPITHELIAL FUNCTION. CC -!- CATALYTIC ACTIVITY: AN ORTHOPHOSPHORIC MONOESTER + H(2)O = AN CC ALCOHOL + PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR (BY CC SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q24238-1; Sequence=Displayed; CC Name=B; CC IsoId=Q24238-2; Sequence=VSP_007002; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: ELLIPSOID BODY RING NEURONS IN THE ADULT BRAIN CC AND IN THE LOWER MALPIGHIAN TUBULE AND URETER. CC -!- DEVELOPMENTAL STAGE: HIGHEST ABUNDANCE DURING LARVAL STAGE (PRIOR CC TO THE SECRETION OF PUPAL CUTICLE) AND ADULT STAGE. CC -!- SIMILARITY: BELONGS TO THE ALKALINE PHOSPHATASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98402; CAA67052.1; -. DR EMBL; AE003776; AAF57106.1; -. DR EMBL; AE003776; AAN14265.1; -. DR EMBL; AY075544; AAL68351.1; -. DR FlyBase; FBgn0016123; Aph-4. DR GO; GO:0046658; C:extrinsic to plasma membrane, GPI-anchored; ISS. DR GO; GO:0004035; F:alkaline phosphatase activity; NAS. DR GO; GO:0042045; P:epithelial fluid transport; IMP. DR GO; GO:0007399; P:neurogenesis; IEP. DR InterPro; IPR001952; Alk_phosphtse. DR Pfam; PF00245; alk_phosphatase; 1. DR PRINTS; PR00113; ALKPHPHTASE. DR ProDom; PD001868; Alk_phosphtse; 2. DR SMART; SM00098; alkPPc; 1. DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1. KW Hydrolase; Zinc; Magnesium; Phosphorylation; Transmembrane; KW Glycoprotein; GPI-anchor; Signal; Alternative splicing; Lipoprotein. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 570 ALKALINE PHOSPHATASE 4. FT PROPEP 571 596 REMOVED IN MATURE FORM. FT DISULFID 539 550 BY SIMILARITY. FT LIPID 570 570 GPI-anchor amidated asparagine FT (Potential). FT TRANSMEM 571 591 POTENTIAL. FT MOD_RES 144 144 PHOSPHORYLATION (BY SIMILARITY). FT ACT_SITE 144 144 BY SIMILARITY. FT METAL 92 92 MAGNESIUM (BY SIMILARITY). FT METAL 93 93 ZINC 2 (BY SIMILARITY). FT METAL 202 202 MAGNESIUM (BY SIMILARITY). FT METAL 204 204 MAGNESIUM (BY SIMILARITY). FT METAL 369 369 MAGNESIUM (BY SIMILARITY). FT METAL 374 374 ZINC 1 (BY SIMILARITY). FT METAL 378 378 ZINC 1 (BY SIMILARITY). FT METAL 415 415 ZINC 2 (BY SIMILARITY). FT METAL 416 416 ZINC 2 (BY SIMILARITY). FT METAL 418 418 ZINC 1 (BY SIMILARITY). FT METAL 504 504 ZINC 1 (BY SIMILARITY). FT CARBOHYD 262 262 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 297 297 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 401 401 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 464 464 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 470 470 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 94 Missing (in isoform B). FT /FTId=VSP_007002. FT CONFLICT 200 200 I -> N (IN REF. 4). FT CONFLICT 358 358 G -> D (IN REF. 1). FT CONFLICT 375 375 Q -> H (IN REF. 1). FT CONFLICT 495 496 AT -> EP (IN REF. 1). FT CONFLICT 538 596 GCLGPAKDFDDSCEDHKDGQKDRPLDKPNPKRNGATVVGAS FT LIPILTAATAAILRGRGL -> AVWVPPRTSMTPVRITRMG FT KRIGRWTNPIQREVAPLLWEPP (IN REF. 1). SQ SEQUENCE 596 AA; 65262 MW; 333F3345BEFBAEFB CRC64; MHCLVILGFL LGSLVAFSWA GVTTQPPPLI RTLSAGGDIG PQFDVGKTKE PEDAEFWHNV GLRQLEKTIK QAQRVKEDSY QKKARNIIIF IGDGMGISTI SAGRIYKGQY LKHGYGEEET LVFDDFPNTG MAKTYNVDKQ VPDSAGTATA IFSGSKTHYG AIGMDATRSK KNGQQGRVQS VMEWAQKEGK RTGVVTTTRI THATPAATYA HIYDRDWECD TEVPAESVGF HVDIARQLVE NAPGNRFNVI LGGGMSPMGI LNASEVKTTI FEGPTETICT RGDNRNLPAE WLAHHANDTV PPALVHNRKD LLNVNVKKVD HLMGLFRNNH ITYSIAREAG EPSLQEMTET ALGILERGDE SNGFVLLVEG GRIDQGHHMN YARAALHELY EFDLAIQAAV NNTDPDETLI LVTADHSHAV TFNGYALRGA DILGTANSHE KNDPMFYETI SYANGPGYWD HLANDSRPQN SSNMWMPLKH FTAEERAAPT YRHLATVPRK DETHGGEDVA VFAYGPGSSL IRGVFEQNYL AYVMSYAGCL GPAKDFDDSC EDHKDGQKDR PLDKPNPKRN GATVVGASLI PILTAATAAI LRGRGL // ID APTE_DROME STANDARD; PRT; 469 AA. AC P29673; Q8T9D4; Q9V9H5; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Apterous protein. GN AP OR CG8376. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92249766; PubMed=1349545; RA Cohen B., McGuffin M.E., Pfeifle C., Segal D., Cohen S.M.; RT "Apterous, a gene required for imaginal disc development in RT Drosophila encodes a member of the LIM family of developmental RT regulatory proteins."; RL Genes Dev. 6:715-729(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92398973; PubMed=1524829; RA Bourgouin C., Lundgren S.E., Thomas J.B.; RT "Apterous is a Drosophila LIM domain gene required for the RT development of a subset of embryonic muscles."; RL Neuron 9:549-561(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR THE NORMAL DEVELOPMENT OF THE WING AND CC HALTER IMAGINAL DISKS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN PNS AND CNS. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- SIMILARITY: CONTAINS 2 LIM ZINC-BINDING DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65158; CAA46276.1; -. DR EMBL; M92841; AAA28673.1; -. DR EMBL; AE003785; AAM68357.1; -. DR EMBL; AY069815; AAL39960.1; -. DR EMBL; BT005201; AAO61758.1; -. DR PIR; JH0718; JH0718. DR HSSP; P32965; 1CTL. DR TRANSFAC; T01074; -. DR FlyBase; FBgn0000099; ap. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0007559; P:histolysis; IMP. DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IMP. DR GO; GO:0007517; P:muscle development; IMP. DR GO; GO:0007399; P:neurogenesis; IMP. DR GO; GO:0006350; P:transcription; IMP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR001781; LIM. DR InterPro; IPR007107; LIM_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00412; LIM; 2. DR ProDom; PD000010; Homeobox; 1. DR ProDom; PD000094; LIM; 2. DR SMART; SM00389; HOX; 1. DR SMART; SM00132; LIM; 2. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 2. DR PROSITE; PS50023; LIM_DOMAIN_2; 2. KW Homeobox; DNA-binding; Nuclear protein; Developmental protein; KW Repeat; LIM domain; Metal-binding; Zinc. FT DOMAIN 148 200 LIM 1. FT DOMAIN 210 263 LIM 2. FT DNA_BIND 367 426 HOMEOBOX. FT CONFLICT 14 14 MISSING (IN REF. 4). SQ SEQUENCE 469 AA; 52053 MW; FA9B43B8C7B9B22D CRC64; MGVCTEERPV MHWQQSARFL GPGAREKSPT PPVAHQGSNQ CGSAAGANNN HPLFRACSSS SCPDICDHST KPFGNAYGTE SFRSYETADR ATFEDSAAKF SISRSRTDCT EVSDETTSGI SFKTEPFGPP SSPESTSDSK ITRNLDDCSG CGRQIQDRFY LSAVEKRWHA SCLQCYACRQ PLERESSCYS RDGNIYCKND YYSFFGTRRC SRCLASISSN ELVMRARNLV FHVNCFCCTV CHTPLTKGDQ YGIIDALIYC RTHYSIAREG DTASSSMSAT YPYSAQFGSP HNDSSSPHSD PSRSIVPTGI FVPASHVING LPQPARQKGR PRKRKPKDIE AFTANIDLNT EYVDFGRGSH LSSSSRTKRM RTSFKHHQLR TMKSYFAINH NPDAKDLKQL SQKTGLPKRV LQVWFQNARA KWRRMMMKQD GSGLLEKGEG ALDLDSISVH SPTSFILGGP NSTPPLNLD // ID APT_DROME STANDARD; PRT; 182 AA. AC P12426; Q9W069; DT 01-OCT-1989 (Rel. 12, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Adenine phosphoribosyltransferase (EC 2.4.2.7) (APRT). GN APRT OR CG18315. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88137948; PubMed=3125085; RA Johnson D.H., Edstroem J.-E., Burnett J.B., Friedman T.B.; RT "Cloning of a Drosophila melanogaster adenine RT phosphoribosyltransferase structural gene and deduced amino acid RT sequence of the enzyme."; RL Gene 59:77-86(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93261421; PubMed=8492806; RA Johnson D.H.; RT "Adenine phosphoribosyltransferase genes in two Drosophila species: RT dosage compensation, a nuclear matrix attachment site, and a novel RT intron position."; RL Mol. Gen. Genet. 238:383-389(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CATALYZES A SALVAGE REACTION RESULTING IN THE FORMATION CC OF AMP, THAT IS ENERGICALLY LESS COSTLY THAN DE NOVO SYNTHESIS. CC -!- CATALYTIC ACTIVITY: AMP + DIPHOSPHATE = ADENINE + 5-PHOSPHO- CC ALPHA-D-RIBOSE 1-DIPHOSPHATE. CC -!- PATHWAY: PURINE SALVAGE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE PURINE/PYRIMIDINE CC PHOSPHORIBOSYLTRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18432; AAA28377.1; -. DR EMBL; L06280; AAA57204.1; -. DR EMBL; AE003473; AAF47589.1; -. DR EMBL; AY119066; AAM50926.1; -. DR PIR; A29596; A29596. DR FlyBase; FBgn0000109; Aprt. DR InterPro; IPR002375; Pr/py_rp_transf. DR InterPro; IPR000836; PRTransferase. DR Pfam; PF00156; Pribosyltran; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. KW Transferase; Glycosyltransferase; Purine salvage. FT CONFLICT 64 64 V -> I (IN REF. 1 AND 2). FT CONFLICT 111 111 I -> S (IN REF. 1 AND 2). FT CONFLICT 148 148 G -> R (IN REF. 1 AND 2). FT CONFLICT 160 160 V -> VV (IN REF. 1). SQ SEQUENCE 182 AA; 19690 MW; E69C129905AE4745 CRC64; MSPSISAEDK LDYVKSKIGE YPNFPKEGIL FRDIFGALTD PKACVYLRDL LVDHIRESAP EAEVIVGLDS RGFLFNLLIA TELGLGCAPI RKKGKLAGEV VSVEYKLEYG IDTFELQKSA IKPGQKVVVV DDLLATGGSL VAATELIGKV GGVVVESLVV MELVGLEGRK RLDGKVHSLI KY // ID AQP_DROME STANDARD; PRT; 245 AA. AC Q9V5Z7; Q24148; Q8MKY6; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Aquaporin. GN DRIP OR CG9023. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE OF 82-191 FROM N.A. RC STRAIN=Oregon-R; TISSUE=Malpighian tubules; RA Dow J.A.T., Kelly D.C., Davies S.A., Maddrell S.H.P., Brown D.; RT "A member of the major intrinsic protein family in Drosophila RT tubules."; RL J. Physiol. (Lond) 489:110-110(1995). CC -!- FUNCTION: FORMS A WATER-SPECIFIC CHANNEL (BY SIMILARITY). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=a; CC IsoId=Q9V5Z7-1; Sequence=Displayed; CC Name=2; Synonyms=b; CC IsoId=Q9V5Z7-2; Sequence=VSP_007787; CC Note=No experimental confirmation available; CC -!- DOMAIN: AQUAPORINS CONTAIN TWO TANDEM REPEATS EACH CONTAINING CC THREE MEMBRANE-SPANNING DOMAINS AND A PORE-FORMING LOOP WITH THE CC SIGNATURE MOTIF ASN-PRO-ALA (NPA). CC -!- SIMILARITY: BELONGS TO THE MIP/AQUAPORIN (TC 1.A.8) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003826; AAF58643.2; -. DR EMBL; AE003826; AAM68740.1; ALT_INIT. DR EMBL; U38807; AAA81324.1; -. DR HSSP; P29972; 1FQY. DR FlyBase; FBgn0015872; Drip. DR GO; GO:0016021; C:integral to membrane; ISS. DR GO; GO:0015250; F:water channel activity; ISS. DR GO; GO:0030104; P:water homeostasis; ISS. DR InterPro; IPR000425; MIP. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR ProDom; PD000295; MIP_family; 1. DR TIGRFAMs; TIGR00861; MIP; 1. DR PROSITE; PS00221; MIP; 1. KW Transport; Repeat; Transmembrane; Alternative splicing. FT DOMAIN 1 26 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 27 46 1 (POTENTIAL). FT DOMAIN 47 51 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 52 72 2 (POTENTIAL). FT DOMAIN 73 94 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 95 115 3 (POTENTIAL). FT DOMAIN 116 132 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 133 153 4 (POTENTIAL). FT DOMAIN 154 163 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 164 184 5 (POTENTIAL). FT DOMAIN 185 205 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 206 226 6 (POTENTIAL). FT DOMAIN 227 245 CYTOPLASMIC (POTENTIAL). FT SITE 76 78 NPA 1. FT SITE 192 194 NPA 2. FT VARSPLIC 1 6 Missing (in isoform 2). FT /FTId=VSP_007787. FT CONFLICT 122 129 GDLGVSSF -> ATWSILL (IN REF. 3). FT CONFLICT 191 191 M -> T (IN REF. 3). SQ SEQUENCE 245 AA; 25575 MW; 611AA17CFE3B807C CRC64; MVEKTEMSKF VGVADITENK KIWRMLLGEL VGTFFLIFVG VGSTTSGSVP QIAFTFGLTV ATIAQGLGHL SGCHINPAVT LGFLIVGEIS ILKAAFYIIV QCVGAIAGAA VIKVALDGVA GGDLGVSSFD PSLNCAQAVL IEALITFILV FVVKAVSDPG RQDIKGSAPL AVGLAIAAGH LCAIKLSGAS MNPARSFGPA VVQGVWTYHW VYWVGPIAGG LLAGIIYRLI FKVRKGDDET DSYDF // ID AR34_DROME STANDARD; PRT; 301 AA. AC Q9VIM5; Q95T07; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable ARP2/3 complex 34 kDa subunit (P34-ARC). GN ARC-P34 OR CG10954. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PART OF A COMPLEX IMPLICATED IN THE CONTROL OF ACTIN CC POLYMERIZATION IN CELLS (BY SIMILARITY). CC -!- SUBUNIT: BELONGS TO A COMPLEX COMPOSED OF ARP2, ARP3, P41-ARC, CC P34-ARC, P21-ARC, P20-ARC AND P16-ARC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ARPC3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003666; AAF53892.2; -. DR EMBL; AY060391; AAL25430.1; -. DR FlyBase; FBgn0032859; Arc-p34. DR InterPro; IPR007188; P34-arc. DR Pfam; PF04045; p34-Arc; 1. KW Cytoskeleton. SQ SEQUENCE 301 AA; 35104 MW; BD1C82C1343CA5AF CRC64; MILLEINNRI IEETLLVKYR NAQAGLKPES IDIRIADFDG VLYHISNVNG DKTKVRISIS LKFYKQLQEH GADELLKREY GSLLTDTEEG YNVSVLINLE EIPEDCEQIA KRIGLLKRNC FASVFEKYFD YQEQGEEGQK RAVINYRNDE TLYVEAKPDR VTVVFSTIFR DEDDVIIGKV FMQELREGRR ASHTAPQVLF SHREPPLELA NTDARVGDNI GYVTFVLFPR HTNKETRDNT INLIHMFRDY LHYHIKCSKA YIHSRMRAKT SDFLKVLNRA RPEPKNTEKK TITGRTFKRI D // ID ARA_DROME STANDARD; PRT; 717 AA. AC Q24248; Q9VTZ9; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein araucan. GN ARA OR CG10571. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96180722; PubMed=8620542; RA Gomez-Skarmeta J.-L., del Corral R.D., de la Calle-Mustienes E., RA Ferres-Marco D., Modolell J.; RT "Araucan and caupolican, two members of the novel iroquois complex, RT encode homeoproteins that control proneural and vein-forming genes."; RL Cell 85:95-110(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONTROLS PRONEURAL AND VEIN FORMING GENES. POSITIVE CC TRANSCRIPTIONAL CONTROLER OF AC-SC (ACHAETE-SCUTE). MAY ACT AS AN CC ACTIVATOR THAT INTERACTS WITH THE TRANSCRIPTIONAL COMPLEX CC ASSEMBLED ON THE AC AND SC PROMOTERS AND PARTICIPATES IN CC TRANSCRIPTION INITIATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- MISCELLANEOUS: 'ARAUCAN' IS NAMED AFTER THE ARAUCANIAN AMERICAN- CC INDIAN TRIBE, ALSO CALLED MOHAWKS, WHO SHAVED ALL BUT A MEDIAL CC STRIPE OF HAIRS ON THE HEAD. CC -!- SIMILARITY: BELONGS TO THE TALE/IRO HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95179; CAA64486.1; -. DR EMBL; AE003540; AAF49896.1; -. DR HSSP; P41778; 1DU6. DR FlyBase; FBgn0015904; ara. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0045893; P:positive regulation of transcription, DNA-d...; NAS. DR GO; GO:0007474; P:wing vein specification; IGI. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Activator; DNA-binding; Homeobox; KW Nuclear protein; Developmental protein. FT DOMAIN 99 102 POLY-GLY. FT DNA_BIND 255 317 HOMEOBOX (TALE-TYPE). FT DOMAIN 328 332 POLY-ASP. FT DOMAIN 400 403 POLY-GLY. FT DOMAIN 492 507 POLY-GLN. FT DOMAIN 561 574 POLY-GLN. FT DOMAIN 599 609 POLY-GLN. FT DOMAIN 691 698 POLY-SER. FT CONFLICT 130 130 MISSING (IN REF. 1). SQ SEQUENCE 717 AA; 75421 MW; BFF09BCB7EF7C711 CRC64; MAAYTQFGYG GFPSASQLLP PSVQTTEDAS ANVNVNVNEA LVMTNAPAMS PTGGQDCQGS QPSGGAGGDA SSGALSPNAL SQNSNAATVV GAGGGSSAGG GGPADLATGG SLDGNGVGTT PTAGGAGGGG SCCENGRPIM TDPVSGQTVC SCQYDSARLA LSSYSRLPAA SVGVYGTPYP STDQNPYQSI GVDSSAFYSP LSNPYGLKDT GAGPEMGAWT SAGLQPTTGY YSYDPMSAYG GLLVSNSSYG ASYDLAARRK NATRESTATL KAWLNEHKKN PYPTKGEKIM LAIITKMTLT QVSTWFANAR RRLKKENKMT WEPKNRTDDD DDALVSDDEK DKEDLEPSKG SQGSVSLAKD ETKEEEDAID EDQKCLGQAN ILRAGFGYPS AGSGSGGYPG GGGSSSGHPG GYHPYHHQHP AYYQAGQQGG MLPFHGENSK LQTDLGDPKN QLGRDCGVPI PATKPKIWSL ADTVGCKTPP PAYMGHQSMP LQQQQQQQQQ QQQAQHQYPP SEAGRDQQLF NGAAAPYLRP HTTAYGGFLG ATTQQLHTTN NSIPYSNMPP QQQQPQQQQQ QLQQGGTIHT TGSSSGPIIP LQFHNRHPQQ QQQLQQQSQS TASQRAMGFL EAQPDTPPQT PPNMKVLSGA LSLLPTATQV PMTATCRSSN AFGFPASGYP MNFSARLGEY SPRDDYSSGN SSSSSSSSPQ LQRNEAMFKP LFKKFTN // ID ARF1_DROME STANDARD; PRT; 181 AA. AC P35676; Q9VNQ2; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ADP-ribosylation factor 1. GN ARF79F OR ARF1 OR LARF1 OR CG8385. OS Drosophila melanogaster (Fruit fly), and OS Locusta migratoria (Migratory locust). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7004; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=93283383; PubMed=8507638; RA Murtagh J.J. Jr., Lee F.-J.S., Deak P., Hall L.M., Monaco L., RA Lee C.M., Stevens L.A., Moss J., Vaughan M.; RT "Molecular characterization of a conserved, guanine RT nucleotide-dependent ADP-ribosylation factor in Drosophila RT melanogaster."; RL Biochemistry 32:6011-6018(1993). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=L.migratoria; RA Hannan F.L., Evans P.D.; RT "Locust ADP-ribosylation factor 1 (lARF) mRNA, complete cds."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTP-BINDING PROTEIN THAT FUNCTIONS AS AN ALLOSTERIC CC ACTIVATOR OF THE CHOLERA TOXIN CATALYTIC SUBUNIT, AN ADP- CC RIBOSYLTRANSFERASE. INVOLVED IN PROTEIN TRAFFICKING; MAY MODULATE CC VESICLE BUDDING AND UNCOATING WITHIN THE GOLGI APPARATUS. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. ARF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S62079; AAB27066.1; -. DR EMBL; AE003599; AAF51871.1; -. DR EMBL; AY060375; AAL25414.1; -. DR EMBL; U90609; AAF21238.1; -. DR PIR; A49520; A49520. DR HSSP; P32889; 1RRF. DR FlyBase; FBgn0010348; Arf79F. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00025; arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW GTP-binding; Multigene family; Myristate; Protein transport; KW Golgi stack; Lipoprotein. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 N-myristoyl glycine (Potential). FT NP_BIND 23 30 GTP (BY SIMILARITY). FT NP_BIND 66 70 GTP (BY SIMILARITY). FT NP_BIND 125 128 GTP (BY SIMILARITY). SQ SEQUENCE 181 AA; 20556 MW; 685C5F4DB7DE6BF6 CRC64; GNVFANLFKG LFGKKEMRIL MVGLDAAGKT TILYKLKLGE IVTTIPTIGF NVETVEYKNI SFTVWDVGGQ DKIRPLWRHY FQNTQGLIFV VDSNDRERIG EAREELMRML AEDELRDAVL LIFANKQDLP NAMNAAEITD KLGLHSLRNR NWYIQATCAT SGDGLYEGLD WLSNQLKNAN R // ID ARF2_DROME STANDARD; PRT; 179 AA. AC P40945; Q9V499; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ADP-ribosylation factor 2. GN ARF102F OR ARF2 OR CG11027. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94342342; PubMed=8063793; RA Lee F.-J.S., Stevens L.A., Hall L.M., Murtagh J.J. Jr., Kao Y.L., RA Moss J., Vaughan M.; RT "Characterization of class II and class III ADP-ribosylation factor RT genes and proteins in Drosophila melanogaster."; RL J. Biol. Chem. 269:21555-21560(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GTP-BINDING PROTEIN THAT FUNCTIONS AS AN ALLOSTERIC CC ACTIVATOR OF THE CHOLERA TOXIN CATALYTIC SUBUNIT, AN ADP- CC RIBOSYLTRANSFERASE. INVOLVED IN PROTEIN TRAFFICKING; MAY MODULATE CC VESICLE BUDDING AND UNCOATING WITHIN THE GOLGI APPARATUS. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. ARF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L25062; AAA53667.1; -. DR EMBL; AE003846; AAF59383.1; -. DR PIR; A53859; A53859. DR HSSP; P32889; 1RRF. DR FlyBase; FBgn0013749; Arf102F. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00025; arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW GTP-binding; Multigene family; Myristate; Protein transport; KW Golgi stack; Lipoprotein. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 N-myristoyl glycine (Potential). FT NP_BIND 23 30 GTP (BY SIMILARITY). FT NP_BIND 66 70 GTP (BY SIMILARITY). FT NP_BIND 125 128 GTP (BY SIMILARITY). SQ SEQUENCE 179 AA; 20485 MW; 03D5F85B0839C044 CRC64; GLTISSLLTR LFGKKQMRIL MVGLDAAGKT TILYKLKLGE IVTTIPTIGF NVETVEYKNI CFTVWDVGGQ DKIRPLWRHY FQNTQGLIFV VDSNDRDRIT EAERELQNML QEDELRDAVL LVFANKQDLP NAMTAAELTD KLRLNQLRNR HWFIQSTCAT QGHGLYEGLD WLSAELAKK // ID ARF3_DROME STANDARD; PRT; 174 AA. AC P40946; Q9V7B0; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ADP-ribosylation factor 3. GN ARF51F OR ARF3 OR CG8156. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94342342; PubMed=8063793; RA Lee F.-J.S., Stevens L.A., Hall L.M., Murtagh J.J. Jr., Kao Y.L., RA Moss J., Vaughan M.; RT "Characterization of class II and class III ADP-ribosylation factor RT genes and proteins in Drosophila melanogaster."; RL J. Biol. Chem. 269:21555-21560(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GTP-BINDING PROTEIN THAT FUNCTIONS AS AN ALLOSTERIC CC ACTIVATOR OF THE CHOLERA TOXIN CATALYTIC SUBUNIT, AN ADP- CC RIBOSYLTRANSFERASE. INVOLVED IN PROTEIN TRAFFICKING; MAY MODULATE CC VESICLE BUDDING AND UNCOATING WITHIN THE GOLGI APPARATUS. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. ARF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L25063; AAA28378.1; -. DR EMBL; L25064; AAA53668.1; -. DR EMBL; AE003811; AAM68532.1; -. DR PIR; B53859; B53859. DR HSSP; P32889; 1RRF. DR FlyBase; FBgn0013750; Arf51F. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR InterPro; IPR006688; ARF. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00025; arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW GTP-binding; Multigene family; Myristate; Protein transport; KW Golgi stack; Lipoprotein. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 N-myristoyl glycine (Potential). FT NP_BIND 19 26 GTP (BY SIMILARITY). FT NP_BIND 62 66 GTP (BY SIMILARITY). FT NP_BIND 121 124 GTP (BY SIMILARITY). FT CONFLICT 42 42 P -> G (IN REF. 1). SQ SEQUENCE 174 AA; 19874 MW; 6F998DC9280B796A CRC64; GKLLSKIFGN KEMRILMLGL DAAGKTTILY KLKLGQSVTT IPTVGFNVET VTYKNVKFNV WDVGGQDKIR PLWRHYYTGT QGLIFVVDCA DRDRIDEART ELHRIINDRE MRDAIILIFA NKQDLPDAMK PHEIQEKLGL TRIRDRNWYV QPSCATSGDG LSEGLIWLTS NHKL // ID ARI1_DROME STANDARD; PRT; 503 AA. AC Q94981; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ariadne-1 protein (Ari-1). GN ARI-1 OR ARI OR CG5659. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., CHARACTERIZATION, AND MUTAGENESIS. RC STRAIN=Oregon-R; RX MEDLINE=20341325; PubMed=10880484; RA Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A.; RT "Ariadne-1: a vital Drosophila gene is required in development and RT defines a new conserved family of ring-finger proteins."; RL Genetics 155:1231-1244(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Deslattes Mays A., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., RA Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., RA Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., RA Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., RA Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., RA Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., RA Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., RA Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., RA Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., RA Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., RA Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., RA Pollard J., Puri V., Reese M.G., Reinert K., Remington K., RA Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., RA Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., RA Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., RA Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., RA Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., RA Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MIGHT ACT AS AN E3 UBIQUITIN-PROTEIN LIGASE, OR AS PART CC OF E3 COMPLEX, WHICH ACCEPTS UBIQUITIN FROM SPECIFIC E2 UBIQUITIN- CC CONJUGATING ENZYMES, SUCH AS UBCD10/UBE2L3, AND THEN TRANSFERS IT CC TO SUBSTRATES. CC -!- SUBUNIT: INTERACTS WITH UBCD10. CAN FORM DIMERS. CC -!- SUBCELLULAR LOCATION: MAINLY CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED, WITH PROMINENT LEVELS IN THE CC NERVOUS SYSTEM AND FEMALE GONADS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN ALL TISSUES THROUGHOUT CC DEVELOPMENT, WITH MAXIMUM LEVELS REACHED DURING METAMORPHOSIS AND CC MAINTAINED IN THE ADULT. CC -!- SIMILARITY: CONTAINS 2 RING-TYPE ZINC FINGERS. CC -!- SIMILARITY: CONTAINS 1 IBR-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98309; CAA66953.1; -. DR EMBL; X98310; CAA66954.1; -. DR EMBL; AE003507; AAF48807.1; -. DR FlyBase; FBgn0017418; ari-1. DR InterPro; IPR002867; Znf_C6HC. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF01485; IBR; 1. DR SMART; SM00647; IBR; 2. DR SMART; SM00184; RING; 2. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW Ubl conjugation pathway; Zinc-finger; Repeat; Coiled coil. FT DOMAIN 22 27 ASP-RICH (ACIDIC). FT ZN_FING 133 182 RING-TYPE 1. FT ZN_FING 203 264 IBR-TYPE. FT ZN_FING 291 336 RING-TYPE 2. FT DOMAIN 133 201 INTERACTION WITH UBCD10. FT DOMAIN 341 361 COILED COIL (POTENTIAL). FT MUTAGEN 150 150 C->Y: IN ARI1-2; LETHAL PHENOTYPE AND FT LOSS OF INTERACTION WITH UBCD10. FT MUTAGEN 309 309 C->Y: IN ARI1-3; LETHAL PHENOTYPE AND NO FT LOSS OF INTERACTION WITH UBCD10. SQ SEQUENCE 503 AA; 58932 MW; 0AECCE256CF5EC00 CRC64; MDSDNDNDFC DNVDSGNVSS GDDGDDDFGM EVDLPSSADR QMDQDDYQYK VLTTDEIVQH QREIIDEANL LLKLPTPTTR ILLNHFKWDK EKLLEKYFDD NTDEFFKCAH VINPFNATEA IKQKTSRSQC EECEICFSQL PPDSMAGLEC GHRFCMPCWH EYLSTKIVAE GLGQTISCAA HGCDILVDDV TVANLVTDAR VRVKYQQLIT NSFVECNQLL RWCPSVDCTY AVKVPYAEPR RVHCKCGHVF CFACGENWHD PVKCRWLKKW IKKCDDDSET SNWIAANTKE CPRCSVTIEK DGGCNHMVCK NQNCKNEFCW VCLGSWEPHG SSWYNCNRYD EDEAKTARDA QEKLRSSLAR YLHYYNRYMN HMQSMKFENK LYASVKQKME EMQQHNMSWI EVQFLKKAVD ILCQCRQTLM YTYVFAYYLK KNNQSMIFED NQKDLESATE MLSEYLERDI TSENLADIKQ KVQDKYRYCE KRCSVLLKHV HEGYDKEWWE YTE // ID ARI2_DROME STANDARD; PRT; 509 AA. AC O76924; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ariadne-2 protein (Ari-2). GN ARI-2 OR ARI2 OR TRIAD1 OR CG5709. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20341325; PubMed=10880484; RA Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A.; RT "Ariadne-1: a vital Drosophila gene is required in development and RT defines a new conserved family of ring-finger proteins."; RL Genetics 155:1231-1244(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Deslattes Mays A., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., RA Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., RA Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., RA Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., RA Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., RA Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., RA Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., RA Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., RA Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., RA Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., RA Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., RA Pollard J., Puri V., Reese M.G., Reinert K., Remington K., RA Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., RA Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., RA Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., RA Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., RA Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., RA Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MIGHT ACT AS AN E3 UBIQUITIN-PROTEIN LIGASE, OR AS PART CC OF E3 COMPLEX, WHICH ACCEPTS UBIQUITIN FROM SPECIFIC E2 UBIQUITIN- CC CONJUGATING ENZYMES, SUCH AS UBCD10/UBE2L3, AND THEN TRANSFERS IT CC TO SUBSTRATES. CC -!- SUBUNIT: INTERACTS WITH UBCD10. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 2 RING-TYPE ZINC FINGERS. CC -!- SIMILARITY: CONTAINS 1 IBR-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ010169; CAA09030.1; -. DR EMBL; AE003456; AAF46823.1; -. DR FlyBase; FBgn0025186; ari-2. DR InterPro; IPR002867; Znf_C6HC. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF01485; IBR; 1. DR SMART; SM00647; IBR; 2. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Ubl conjugation pathway; Nuclear protein; Coiled coil; Zinc-finger; KW Repeat. FT DOMAIN 2 64 ASP/GLU-RICH (ACIDIC). FT DOMAIN 123 128 POLY-ALA. FT ZN_FING 153 202 RING-TYPE 1. FT DOMAIN 222 284 IBR-TYPE. FT ZN_FING 314 358 RING-TYPE 2. FT DOMAIN 387 410 COILED COIL (POTENTIAL). FT DOMAIN 452 503 COILED COIL (POTENTIAL). SQ SEQUENCE 509 AA; 58627 MW; 9FB82E5ACF05E900 CRC64; MDSDIEMDME SDNDGEYDDD YDYYNTGEDC DVERLDPKRA DPEYFEYECL TVEDIEKLLN ERVEKLNTIL QITPSLAKVL LLEHQWNNVA VVEKYRQDAN ALLVTARIKP PSVAVTDTAS TSAAAASAQL LRLGSSGYKT TASATPQYRS QMCPVCASSQ LGDKFYSLAC GHSFCKDCWT IYFETQIFQG ISTQIGCMAQ MCNVRVPEDL VLTLVTRPVM RDKYQQFAFK DYVKSHPELR FCPGPNCQII VQSSEISAKR AICKACHTGF CFRCGMDYHA PTDCQVIKKW LTKCADDSET ANYISAHTKD CPKCHICIEK NGGCNHMQCF NCKHDFCWMC LGDWKTHGSE YYECSRYKDN PNIANESVHV QAREALKKYL HYYERWENHS KSLKLEQQTI DRLRQRINSK VMNGSGTWID WQYLFNAAAL LAKCRYTLQY TYPYAYYMEA GSRKNLFEYQ QAQLEAEIEN LSWKIERAET TDLGDLENQM DIAEKRRTTL LKDFFPVDA // ID ARL1_DROME STANDARD; PRT; 180 AA. AC P25160; Q9VUW7; DT 01-MAY-1992 (Rel. 22, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GTP-binding ADP-ribosylation factor homolog 1 protein. GN ARF72A OR ARL1 OR ARL OR CG6025. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91195304; PubMed=1901655; RA Tamkun J.W., Kahn R.A., Kissinger M., Brizuela B.J., Rulka C., RA Scott M.P., Kennison J.A.; RT "The arflike gene encodes an essential GTP-binding protein in RT Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 88:3120-3124(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: BINDS AND HYDROLYZES GTP. DOES NOT ACT AS AN ALLOSTERIC CC ACTIVATOR OF THE CHOLERA TOXIN CATALYTIC SUBUNIT. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. ARF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M61127; AAA28365.1; -. DR EMBL; AE003529; AAF49556.2; -. DR EMBL; BT001460; AAN71215.1; -. DR PIR; A40438; A40438. DR HSSP; P32889; 1HUR. DR FlyBase; FBgn0000115; Arf72A. DR GO; GO:0005525; F:GTP binding; IDA. DR InterPro; IPR006688; ARF. DR InterPro; IPR003579; GTPase_Rab. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR006687; SAR1. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00025; arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00178; SAR; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW GTP-binding; Multigene family. FT NP_BIND 23 30 GTP (BY SIMILARITY). FT NP_BIND 66 70 GTP (BY SIMILARITY). FT NP_BIND 125 128 GTP (BY SIMILARITY). SQ SEQUENCE 180 AA; 20247 MW; D9B1DE83D37201C5 CRC64; MGGVLSYFRG LLGSREMRIL ILGLDGAGKT TILYRLQVGE VVTTIPTIGF NVEQVTYKNL KFQVWDLGGQ TSIRPYWRCY YSNTDAIIYV VDSADRDRIG ISKDELLYML REEELAGAIL VVLANKQDMD GCMTVAEVHH ALGLENLKNR TFQIFKTSAT KGEGLDQAMD WLSNTLQSRK // ID ARL2_DROME STANDARD; PRT; 184 AA. AC Q06849; Q9VHS1; DT 01-JUN-1994 (Rel. 29, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GTP-binding ADP-ribosylation factor homolog 2 protein. GN ARF84F OR ARL2 OR CG7435. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94022293; PubMed=8415637; RA Clark J., Moore L., Krasinskas A., Way J., Battey J., Tamkun J., RA Kahn R.A.; RT "Selective amplification of additional members of the RT ADP-ribosylation factor (ARF) family: cloning of additional human and RT Drosophila ARF-like genes."; RL Proc. Natl. Acad. Sci. U.S.A. 90:8952-8956(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: DOES NOT ACT AS AN ALLOSTERIC ACTIVATOR OF THE CHOLERA CC TOXIN CATALYTIC SUBUNIT. CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. ARF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L14923; AAA74629.1; -. DR EMBL; AE003678; AAF54228.1; -. DR HSSP; P32889; 1HUR. DR FlyBase; FBgn0004908; Arf84F. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001019; Gprotein_alpha. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00025; arf; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW GTP-binding; Multigene family. FT NP_BIND 23 30 GTP (BY SIMILARITY). FT NP_BIND 66 70 GTP (BY SIMILARITY). FT NP_BIND 125 128 GTP (BY SIMILARITY). SQ SEQUENCE 184 AA; 20834 MW; F1C8894BE74466B6 CRC64; MGFLTVLKKM RQKEREMRIL LLGLDNAGKT TILKRFNGEP IDTISPTLGF NIKTLEHNGY TLNMWDVGGQ KSLRSYWRNY FESTDGLVWV VDSADRMRLE SCGQELQVLL QEERLAGATL LVLCNKQDLP GALSSNEIKE ILHLEDITTH HWLVAGVSAV TGEKLLSSMD WLIADIAKRI FTLD // ID ARME_DROME STANDARD; PRT; 173 AA. AC Q9XZ63; Q9VEW4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ARMET-like protein precursor. GN ARP-LIKE OR CG7013. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20062184; PubMed=10597048; RA Goo J.H., Ahn Y., Park O.K., Park W.J.; RT "Selection of Drosophila genes encoding secreted and membrane RT proteins."; RL Mol. Cells 9:564-568(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE ARMET FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF132912; AAD32615.1; -. DR EMBL; AE003713; AAF55303.1; -. DR EMBL; AY061080; AAL28628.1; -. DR FlyBase; FBgn0027095; ARP-like. KW Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 173 ARMET-LIKE PROTEIN. FT CONFLICT 74 74 MISSING (IN REF. 1). SQ SEQUENCE 173 AA; 20136 MW; E734A191F51F15D2 CRC64; MKTWYMVVVI GFLATLAQTS LALKEEDCEV CVKTVRRFAD SLDDSTKKDY KQIETAFKKF CKAQKNKEHR FCYYLGGLEE SATGILNELS KPLSWSMPAE KICEKLKKKD AQICDLRYEK QIDLNSVDLK KLKVRDLKKI LNDWDESCDG CLEKGDFIKR IEELKPKYSR SEL // ID ARM_DROME STANDARD; PRT; 843 AA. AC P18824; O02371; Q9W546; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Armadillo segment polarity protein. GN ARM OR EG:86E4.6 OR CG11579. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM CYTOPLASMIC). RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=89211895; PubMed=2707602; RA Riggleman B., Wieschaus E., Schedl P.; RT "Molecular analysis of the armadillo locus: uniformly distributed RT transcripts and a protein with novel internal repeats are associated RT with a Drosophila segment polarity gene."; RL Genes Dev. 3:96-113(1989). RN [2] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND ALTERNATIVE RP SPLICING. RC TISSUE=Head; RX MEDLINE=98298928; PubMed=9635189; RA Loureiro J., Peifer M.; RT "Roles of Armadillo, a Drosophila catenin, during central nervous RT system development."; RL Curr. Biol. 8:622-632(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM CYTOPLASMIC). RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [6] RP PHOSPHORYLATION. RX MEDLINE=95113174; PubMed=7529201; RA Peifer M., Pai L.-M., Casey M.; RT "Phosphorylation of the Drosophila adherens junction protein RT Armadillo: roles for wingless signal and zeste-white 3 kinase."; RL Dev. Biol. 166:543-556(1994). RN [7] RP SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=96234672; PubMed=8666669; RA McCartney B.M., Fehon R.G.; RT "Distinct cellular and subcellular patterns of expression imply RT distinct functions for the Drosophila homologues of moesin and the RT neurofibromatosis 2 tumor suppressor, merlin."; RL J. Cell Biol. 133:843-852(1996). CC -!- FUNCTION: ISOFORM NEURAL MAY ASSOCIATE WITH CADN AND PARTICIPATE CC IN THE TRANSMISSION OF DEVELOPMENTAL INFORMATION. CAN ASSOCIATE CC WITH ALPHA-CATENIN. ISOFORM CYTOPLASMIC ACCUMULATES THROUGH WG CC SIGNALING. ARM FUNCTION IN WG SIGNAL TRANSDUCTION IS REQUIRED CC EARLY IN DEVELOPMENT FOR DETERMINATION OF NEUROBLAST FATE. ARM AND CC ABL PROTEINS FUNCTION COOPERATIVELY AT ADHERENS JUNCTIONS IN BOTH CC THE CNS AND EPIDERMIS. CC -!- SUBUNIT: INTERACTS WITH MER AND MOE AT THE ADHERENS JUNCTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND MEMBRANE-ASSOCIATED; INNER CC SURFACE OF CELL MEMBRANE AND ADHERENS JUNCTION. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Cytoplasmic; Synonyms=A, B; CC IsoId=P18824-1; Sequence=Displayed; CC Name=Neural; CC IsoId=P18824-2; Sequence=VSP_006738; CC -!- TISSUE SPECIFICITY: ISOFORM CYTOPLASMIC IS PREDOMINANT BEFORE GERM CC BAND RETRACTION, AFTER RETRACTION AND, DURING LARVAL STAGES, IT IS CC FOUND IN HIGH LEVELS IN SPECIFIC CELLS ALONG THE CNS MIDLINE. CC ISOFORM NEURAL IS FIRST SEEN AFTER GERM BAND RETRACTION IN THE CC AXON TRACTS OF THE CNS, ALSO PRESENT IN AXONS DURING LARVAL STAGES CC AND ACCUMULATES IN THE MOTOR NEURONS OF THE SEGMENTAL AND CC INTERSEGMENTAL NERVES AS THEY EXIT THE CNS. BOTH ISOFORMS CC ACCUMULATE IN THE PNS. CC -!- DEVELOPMENTAL STAGE: PRESENT AT ALL STAGES, BUT REACHED THE CC HIGHEST LEVELS DURING EARLY TO MID-EMBRYOGENESIS. CC -!- PTM: PHOSPHORYLATED ON SER, THR AND TYR RESIDUES. LEVEL OF CC PHOSPHORYLATION VARIES BOTH DURING EMBRYONIC DEVELOPMENT AND FROM CC EMBRYONIC TISSUE TO TISSUE. SGG IS REQUIRED FOR PHOSPHORYLATION CC AND WG SIGNAL NEGATIVELY REGULATES ARM PHOSPHORYLATION. CC HYPOPHOSPHORYLATED FORM OF ARM INCREASES IN STEADY-STATE LEVELS. CC -!- SIMILARITY: BELONGS TO THE BETA-CATENIN FAMILY. CC -!- SIMILARITY: CONTAINS 13 ARM REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54468; CAA38350.1; -. DR EMBL; AF001213; AAB58731.1; -. DR EMBL; AE003422; AAF45688.2; -. DR EMBL; AL021106; CAA15946.1; -. DR EMBL; AL021086; CAA15946.1; JOINED. DR EMBL; AL021086; CAA15935.1; -. DR EMBL; AL021106; CAA15935.1; JOINED. DR PIR; T12689; T12689. DR HSSP; Q02248; 1DOW. DR TRANSFAC; T02977; -. DR FlyBase; FBgn0000117; arm. DR GO; GO:0005912; C:adherens junction; IDA. DR GO; GO:0005915; C:zonula adherens; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR InterPro; IPR008938; ARM. DR InterPro; IPR000225; Armadillo. DR Pfam; PF00514; Armadillo_seg; 7. DR SMART; SM00185; ARM; 12. DR PROSITE; PS50176; ARM_REPEAT; 9. KW Developmental protein; Segmentation polarity protein; Repeat; KW Cell adhesion; Membrane; Cytoskeleton; Structural protein; KW Phosphorylation; Wnt signaling pathway; Alternative splicing. FT DOMAIN 1 158 ASP/GLU-RICH (ACIDIC). FT REPEAT 159 200 ARM 1. FT REPEAT 201 242 ARM 2. FT REPEAT 243 284 ARM 3. FT REPEAT 285 326 ARM 4. FT REPEAT 327 368 ARM 5. FT REPEAT 369 410 ARM 6. FT REPEAT 411 449 ARM 7. FT REPEAT 450 496 ARM 8. FT REPEAT 497 538 ARM 9. FT REPEAT 539 584 ARM 10. FT REPEAT 585 608 ARM 11. FT REPEAT 609 647 ARM 12. FT REPEAT 648 689 ARM 13 (INCOMPLETE). FT DOMAIN 690 843 ASP/GLU-RICH (ACIDIC). FT VARSPLIC 718 843 LGPEEAYEGLYGQGPPSVHSSHGGRAFHQQGYDTLPIDSMQ FT GLEISSPVGGGGAGGAPGNGGAVGGASGGGGNIGAIPPSGA FT PTSPYSMDMDVGEIDAGALNFDLDAMPTPPNDNNNLAAWYD FT TDC -> ILYQ (in isoform Neural). FT /FTId=VSP_006738. SQ SEQUENCE 843 AA; 91152 MW; 40DAD6FB83163049 CRC64; MSYMPAQNRT MSHNNQYNPP DLPPMVSAKE QTLMWQQNSY LGDSGIHSGA VTQVPSLSGK EDEEMEGDPL MFDLDTGFPQ NFTQDQVDDM NQQLSQTRSQ RVRAAMFPET LEEGIEIPST QFDPQQPTAV QRLSEPSQML KHAVVNLINY QDDAELATRA IPELIKLLND EDQVVVSQAA MMVHQLSKKE ASRHAIMNSP QMVAALVRAI SNSNDLESTK AAVGTLHNLS HHRQGLLAIF KSGGIPALVK LLSSPVESVL FYAITTLHNL LLHQDGSKMA VRLAGGLQKM VTLLQRNNVK FLAIVTDCLQ ILAYGNQESK LIILASGGPN ELVRIMRSYD YEKLLWTTSR VLKVLSVCSS NKPAIVDAGG MQALAMHLGN MSPRLVQNCL WTLRNLSDAA TKVEGLEALL QSLVQVLGST DVNVVTCAAG ILSNLTCNNQ RNKATVCQVG GVDALVRTII NAGDREEITE PAVCALRHLT SRHVDSELAQ NAVRLNYGLS VIVKLLHPPS RWPLIKAVIG LIRNLALCPA NHAPLREHGA IHHLVRLLMR AFQDTERQRS SIATTGSQQP SAYADGVRME EIVEGTVGAL HILARESHNR ALIRQQSVIP IFVRLLFNEI ENIQRVAAGV LCELAADKEG AEIIEQEGAT GPLTDLLHSR NEGVATYAAA VLFRMSEDKP QDYKKRLSIE LTNSLLREDN NIWANADLGM GPDLQDMLGP EEAYEGLYGQ GPPSVHSSHG GRAFHQQGYD TLPIDSMQGL EISSPVGGGG AGGAPGNGGA VGGASGGGGN IGAIPPSGAP TSPYSMDMDV GEIDAGALNF DLDAMPTPPN DNNNLAAWYD TDC // ID ARNT_DROME STANDARD; PRT; 644 AA. AC O15945; O16167; O44082; Q24461; Q9VHI2; DT 15-DEC-1998 (Rel. 37, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Aryl hydrocarbon receptor nuclear translocator homolog (dARNT) DE (Tango protein) (Hypoxia-inducible factor 1 beta). GN TGO OR ARNT OR HIF-1-BETA OR CG11987. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND SUBUNIT. RC TISSUE=Embryo; RX MEDLINE=98040551; PubMed=9374395; RA Ohshiro T., Saigo K.; RT "Transcriptional regulation of breathless FGF receptor gene by RT binding of TRACHEALESS/dARNT heterodimers to three central midline RT elements in Drosophila developing trachea."; RL Development 124:3975-3986(1997). RN [2] RP SEQUENCE FROM N.A., FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=97427859; PubMed=9284047; RA Zelzer E., Wappner P., Shilo B.-Z.; RT "The PAS domain confers target gene specificity of Drosophila RT bHLH/PAS proteins."; RL Genes Dev. 11:2079-2089(1997). RN [3] RP SEQUENCE FROM N.A., FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=98072332; PubMed=9409674; RA Sonnenfeld M., Ward M., Nystroem G., Mosher J., Stahl S., Crews S.; RT "The Drosophila tango gene encodes a bHLH-PAS protein that is RT orthologous to mammalian Arnt and controls CNS midline and tracheal RT development."; RL Development 124:4571-4582(1997). RN [4] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Embryo, Head, and Pupae; RX MEDLINE=20050848; PubMed=10581393; RA Ma E., Haddad G.G.; RT "Isolation and characterization of the hypoxia-inducible factor 1beta RT in Drosophila melanogaster."; RL Brain Res. Mol. Brain Res. 73:11-16(1999). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP SEQUENCE OF 586-623 FROM N.A. RX MEDLINE=87051745; PubMed=2877746; RA Frigerio G., Burri M., Bopp D., Baumgartner S., Noll M.; RT "Structure of the segmentation gene paired and the Drosophila PRD gene RT set as part of a gene network."; RL Cell 47:735-746(1986). CC -!- FUNCTION: TGO/TRH HETERODIMERS ARE INVOLVED IN THE CONTROL OF CC BREATHLESS EXPRESSION. PLAYS A ROLE IN THE CELLULAR OR TISSUE CC RESPONSE TO OXYGEN DEPRIVATION. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. HETERODIMER WITH AHR, TRH OR SIM. CC -!- TISSUE SPECIFICITY: AT STAGE 11, EXPRESSION IS DETECTED IN CC TRACHEAL PITS. AT LATER STAGES, STRONG EXPRESSION IS ALSO DETECTED CC IN THE CNS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY IN CC PUPAE AT A LOW LEVEL. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PAS (PER-ARNT-SIM) DIMERIZATION DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PAS-ASSOCIATED C-TERMINAL (PAC) DOMAIN. CC -!- CAUTION: REF.6 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 607. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB002556; BAA22868.1; -. DR EMBL; AF016053; AAB69695.1; -. DR EMBL; AF020426; AAB88882.1; -. DR EMBL; AF154417; AAD38396.1; -. DR EMBL; AE003681; AAF54329.1; -. DR EMBL; M14550; AAA28838.1; ALT_FRAME. DR HSSP; P22415; 1AN4. DR FlyBase; FBgn0015014; tgo. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IDA. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR001067; Nuc_translocat. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS_domain. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00989; PAS; 2. DR PRINTS; PR00785; NCTRNSLOCATR. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR TIGRFAMs; TIGR00229; sensory_box; 2. DR PROSITE; PS50888; HLH; 1. DR PROSITE; PS50112; PAS; 2. KW Nuclear protein; DNA-binding; Transcription regulation; Activator; KW Repeat. FT DNA_BIND 14 26 BASIC DOMAIN. FT DOMAIN 27 67 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 85 156 PAS 1. FT DOMAIN 271 341 PAS 2. FT DOMAIN 346 389 PAC. FT DOMAIN 23 26 POLY-ARG. FT DOMAIN 396 399 POLY-ALA. FT DOMAIN 404 415 POLY-GLN. FT DOMAIN 457 464 POLY-GLN. FT DOMAIN 517 524 POLY-GLN. FT DOMAIN 568 572 POLY-PRO. FT CONFLICT 110 110 V -> M (IN REF. 1). FT CONFLICT 412 413 MISSING (IN REF. 1 AND 5). FT CONFLICT 467 467 G -> R (IN REF. 1). FT CONFLICT 490 490 P -> T (IN REF. 2). FT CONFLICT 616 634 EFSDMLQMLDHTPTTFEDL -> GVLRYAADVGSHADHV FT (IN REF. 2). SQ SEQUENCE 644 AA; 71731 MW; 3203C7D583CA93FA CRC64; MDEANIQDKE RFASRENHCE IERRRRNKMT AYITELSDMV PTCSALARKP DKLTILRMAV AHMKALRGTG NTSSDGTYKP SFLTDQELKH LILEAADGFL FVVSCDSGRV IYVSDSVTPV LNYTQSDWYG TSLYEHIHPD DREKIREQLS TQESQNAGRI LDLKSGTVKK EGHQSSMRLS MGARRGFICR MRVGNVNPES MVSGHLNRLK QRNSLGPSRD GTNYAVVHCT GYIKNWPPTD MFPNMHMERD VDDMSSHCCL VAIGRLQVTS TAANDMSGSN NQSEFITRHA MDGKFTFVDQ RVLNILGYTP TELLGKICYD FFHPEDQSHM KESFDQVLKQ KGQMFSLLYR ARAKNSEYVW LRTQAYAFLN PYTDEVEYIV CTNSSGKTMH GAPLDAAAAH TPEQVQQQQQ QQQEQHVYVQ AAPGVDYARR ELTPVGSATN DGMYQTHMLA MQAPTPQQQQ QQQQRPGSAQ TTPVGYTYDT THSPYSAGGP SPLAKIPKSG TSPTPVAPNS WAALRPQQQQ QQQQPVTEGY QYQQTSPARS PSGPTYTQLS AGNGNRQQAQ PGAYQAGPPP PPNAPGMWDW QQAGGHPHPP HPTAHPHHPH AHPGGPAGAG QPQGQEFSDM LQMLDHTPTT FEDLNINMFS TPFE // ID ARP2_DROME STANDARD; PRT; 394 AA. AC P45888; Q9VXF3; DT 01-NOV-1995 (Rel. 32, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin-like protein 2 (Actin-like protein 14D). GN ARP14D OR ACTR14D OR CG9901. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94343534; PubMed=8064864; RA Fyrberg C., Ryan L., Kenton M., Fyrberg E.A.; RT "Genes encoding actin-related proteins of Drosophila melanogaster."; RL J. Mol. Biol. 241:498-503(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PART OF A COMPLEX IMPLICATED IN THE CONTROL OF ACTIN CC POLYMERIZATION IN CELLS (BY SIMILARITY). CC -!- SUBUNIT: BELONGS TO A COMPLEX COMPOSED OF ARP2, ARP3, P41-ARC, CC P34-ARC, P21-ARC, P20-ARC AND P16-ARC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. ARP2 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78486; CAA55238.1; -. DR EMBL; AE003502; AAF48621.1; -. DR EMBL; AY061256; AAL28804.1; -. DR PIR; S47987; S47987. DR FlyBase; FBgn0011742; Arp14D. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Cytoskeleton. FT CONFLICT 2 2 D -> DR (IN REF. 1). FT CONFLICT 90 90 D -> E (IN REF. 1). FT CONFLICT 143 144 VL -> AW (IN REF. 1). SQ SEQUENCE 394 AA; 44702 MW; 46BE0026B169B9A1 CRC64; MDSKGRNVIV CDNGTGFVKC GYAGSNFPTH IFPSMVGRPM IRAVNKIGDI EVKDLMVGDE ASQLRSLLEV SYPMENGVVR NWDDMCHVWD YTFGPKKMDI DPTNTKILLT EPPMNPTKNR EKMIEVMFEK YGFDSAYIAI QAVLTLYAQG LISGVVIDSG DGVTHICPVY EEFALPHLTR RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRIMKEKL CYIGYDIEME QRLALETTVL VESYTLPDGR VIKVGGERFE APEALFQPHL INVEGPGIAE LAFNTIQAAD IDIRPELYKH IVLSGGSTMY PGLPSRLERE IKQLYLERVL KNDTEKLAKF KIRIEDPPRR KDMVFIGGAV LAEVTKDRDG FWMSKQEYQE QGLKVLQKLQ KISH // ID ARP3_DROME STANDARD; PRT; 418 AA. AC P32392; Q9VSD5; DT 01-OCT-1993 (Rel. 27, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Actin-like protein 3 (Actin-like protein 66B) (Actin-2). GN ARP66B OR ACTR66B OR CG7558. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94099775; PubMed=8274139; RA Fyrberg C., Fyrberg E.A.; RT "A Drosophila homologue of the Schizosaccharomyces pombe act2 gene."; RL Biochem. Genet. 31:329-341(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PART OF A COMPLEX IMPLICATED IN THE CONTROL OF ACTIN CC POLYMERIZATION IN CELLS (BY SIMILARITY). CC -!- SUBUNIT: BELONGS TO A COMPLEX COMPOSED OF ARP2, ARP3, P41-ARC, CC P34-ARC, P21-ARC, P20-ARC AND P16-ARC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. ARP3 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X71789; CAA50674.1; -. DR EMBL; AE003556; AAF50488.1; -. DR EMBL; AY051859; AAK93283.1; -. DR FlyBase; FBgn0011744; Arp66B. DR GO; GO:0030037; P:cell cycle dependent actin filament reorgan...; IPI. DR GO; GO:0030589; P:pseudocleavage (sensu Insecta); IPI. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Cytoskeleton. FT CONFLICT 69 69 A -> R (IN REF. 1). FT CONFLICT 176 176 H -> D (IN REF. 1). FT CONFLICT 203 203 F -> L (IN REF. 1). SQ SEQUENCE 418 AA; 47032 MW; D8EAA080ED81513A CRC64; MAGRLPACVI DVGTGYSKLG FAGNKEPQFI IPSAIAIKES ARVGDTNTRR ITKGIEDLDF FIGDEAFDAT GYSIKYPVRH GLVEDWDLME RFLEQCVFKY LRAEPEDHYF LLTEPPLNTP ENREYTAEIM FETFNVPGLY IAVQAVLALA ASWASRSAEE RTLTGIVVDS GDGVTHVIPV AEGYVIGSCI KHIPIAGRNI TSFIQSLLRE REVGIPPEQS LETAKAIKEK HCYICPDIAK EFAKYDTEPG KWIRNFSGVN TVTKAPFNVD VGYERFLGPE IFFHPEFSNP DFTIPLSEIV DNVIQNCPID VRRPLYNNIV LSGGSTMFKD FGRRLQRDIK RSVDTRLRIS ENLSEGRIKP KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKAAY EEYGPSICRH NPVFGTMT // ID ARRA_DROME STANDARD; PRT; 364 AA. AC P15372; Q9VJA8; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Phosrestin II (Arrestin A) (Arrestin 1). GN ARR1 OR ARRA OR CG5711. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=90138925; PubMed=1689056; RA Smith D.P., Sheih B.-H., Zuker C.S.; RT "Isolation and structure of an arrestin gene from Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1003-1007(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90138926; PubMed=2105491; RA Hyde D.R., Mecklenburg K.L., Pollock J.A., Vihtelic T.S., Benzer S.; RT "Twenty Drosophila visual system cDNA clones: one is a homolog of RT human arrestin."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1008-1012(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP PHOSPHORYLATION. RX MEDLINE=91282780; PubMed=1905538; RA Matsumoto H., Yamada T.; RT "Phosrestins I and II: arrestin homologs which undergo differential RT light-induced phosphorylation in the Drosophila photoreceptor in RT vivo."; RL Biochem. Biophys. Res. Commun. 177:1306-1312(1991). RN [6] RP FUNCTION. RX MEDLINE=93303590; PubMed=8316831; RA Dolph P.J., Ranganathan R., Colley N.J., Hardy R.W., Socolich M., RA Zuker C.S.; RT "Arrestin function in inactivation of G protein-coupled receptor RT rhodopsin in vivo."; RL Science 260:1910-1916(1993). CC -!- FUNCTION: REGULATES PHOTORECEPTOR CELL DEACTIVATION. ARR1 AND ARR2 CC PROTEINS ARE MEDIATORS OF RHODOPSIN INACTIVATION AND ARE ESSENTIAL CC FOR THE TERMINATION OF THE PHOTOTRANSDUCTION CASCADE. CC -!- TISSUE SPECIFICITY: EXPRESSED SPECIFICALLY AND ABUNDANTLY IN THE CC PHOTORECEPTORS. INNER AND OUTER SEGMENTS, AND THE INNER PLEXIFORM CC REGIONS OF THE RETINA. CC -!- PTM: PHOSPHORYLATED, BUT DOES NOT UNDERGO LIGHT-INDUCED CC PHOSPHORYLATION. CC -!- SIMILARITY: BELONGS TO THE ARRESTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30177; -; NOT_ANNOTATED_CDS. DR EMBL; M30140; AAA28380.1; -. DR EMBL; AE003657; AAF53644.1; -. DR EMBL; AY061824; AAL27635.1; -. DR PIR; A34867; A34867. DR HSSP; P08168; 1CF1. DR FlyBase; FBgn0000120; Arr1. DR GO; GO:0005624; C:membrane fraction; IDA. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0016060; P:metarhodopsin inactivation; IGI. DR InterPro; IPR000698; Arrestin. DR InterPro; IPR007110; Ig-like. DR Pfam; PF00339; arrestin; 1. DR Pfam; PF02752; arrestin_C; 1. DR PRINTS; PR00309; ARRESTIN. DR ProDom; PD002099; Arrestin; 1. DR PROSITE; PS00295; ARRESTINS; 1. KW Sensory transduction; Vision; Phosphorylation. SQ SEQUENCE 364 AA; 40771 MW; 0DCC764C4F890FC2 CRC64; MVVNFKVFKK CSPNNMITLY MNRRDFVDSV TQVEPIDGII VLDDEYVRQN RKIFVQLVCN FRYGREDDEM IGLRFQKELT LVSQQVCPPQ KQDIQLTKMQ ERLLKKLGSN AYPFVMQMPP SSPASVVLQQ KASDESQPCG VQYFVKIFTG DSDCDRSHRR STINLGIRKV QYAPTKQGIQ PCTVVRKDFL LSPGELELEV TLDKQLYHHG EKISVNICVR NNSNKVVKKI KAMVQQGVDV VLFQNGQFRN TIAFMETSEG CPLNPGSSLQ KVMYLVPTLV ANCDRAGIAV EGDIKRKDTA LASTTLIASQ DARDAFGIIV SYAVKVKLFL GALGGELCAE LPFILMHPKP SRKAQLEAEG SIEA // ID ARRB_DROME STANDARD; PRT; 401 AA. AC P19107; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Phosrestin I (Arrestin B) (Arrestin 2) (49 kDa arrestin-like protein). GN ARRB OR ARR2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90232360; PubMed=2158671; RA Yamada T., Takeuchi Y., Kmoroi N., Kobayashi H., Sakai Y., Hotta Y., RA Matsumoto H.; RT "A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an RT arrestin homolog."; RL Science 248:483-486(1990). RN [2] RP PHOSPHORYLATION, AND PROBABLE FUNCTION. RX MEDLINE=91282780; PubMed=1905538; RA Matsumoto H., Yamada T.; RT "Phosrestins I and II: arrestin homologs which undergo differential RT light-induced phosphorylation in the Drosophila photoreceptor in RT vivo."; RL Biochem. Biophys. Res. Commun. 177:1306-1312(1991). RN [3] RP PHOSPHORYLATION SITE. RX MEDLINE=94242441; PubMed=8185954; RA Matsumoto H., Kurien B.T., Takagi Y., Kahn E.S., Kinumi T., Komori N., RA Yamada T., Hayashi F., Isono K., Pak W.L.; RT "Phosrestin I undergoes the earliest light-induced phosphorylation by RT a calcium/calmodulin-dependent protein kinase in Drosophila RT photoreceptors."; RL Neuron 12:997-1010(1994). CC -!- FUNCTION: PROBABLY PLAYS AN IMPORTANT ROLE IN THE PHOTORECEPTOR CC TRANSDUCTION. CC -!- TISSUE SPECIFICITY: INNER AND OUTER SEGMENTS, AND THE INNER CC PLEXIFORM REGIONS OF THE RETINA. CC -!- PTM: UNDERGOES LIGHT-INDUCED PHOSPHORYLATION. CC -!- SIMILARITY: BELONGS TO THE ARRESTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32141; AAA28833.1; -. DR PIR; A34856; A34856. DR HSSP; P08168; 1CF1. DR FlyBase; FBgn0000121; Arr2. DR GO; GO:0005624; C:membrane fraction; IDA. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0005625; C:soluble fraction; IDA. DR GO; GO:0016060; P:metarhodopsin inactivation; IMP. DR InterPro; IPR000698; Arrestin. DR InterPro; IPR007110; Ig-like. DR Pfam; PF00339; arrestin; 1. DR Pfam; PF02752; arrestin_C; 1. DR PRINTS; PR00309; ARRESTIN. DR ProDom; PD002099; Arrestin; 1. DR PROSITE; PS00295; ARRESTINS; 1. KW Sensory transduction; Vision; Phosphorylation. FT MOD_RES 366 366 PHOSPHORYLATION (BY CAMK). FT VARIANT 109 109 S -> N. SQ SEQUENCE 401 AA; 44975 MW; D925F39132FCA751 CRC64; MVVSVKVFKK ATPNGKVTFY LGRRDFIDHI DYCDPVDGVI VVEPDYLKNR KVFGQLATTY RYGREEDEVM GVKFSKELIL CREQIVPMTN PNMEMTPMQE KLVRKLGSSA HPFTFHFPPN SPSSVTLQQE GDDNGKPLGV EYTIRAFVGD SEDDRQHKRS MVSLVIKKLQ YAPLNRGQRL PSSLVSKGFT FSNGKISLEV TLDREIYYHG EKTAATVQVS NNSKKSVKSI KCFIVQHTEI TMVNAQFSKH VAQLETKEGC PITPGANLTK TFYLIPLAAN NKDRHGIALD GHLKDEDVNL ASSTMVQEGK STGDACGIVI SYSVRIKLNC GTLGGEMQTD VPFKLLQPAP GTIEKKRSNA MKKMKSIEQH RNVKGYYQDD DDNIVFEDFA KMRMNNVNMA D // ID AST3_DROME STANDARD; PRT; 257 AA. AC P09774; Q24387; DT 01-MAR-1989 (Rel. 10, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Achaete-scute complex protein T3 (Lethal of sc) (Lethal of DE scute protein). GN L(1)SC OR T3 OR L'SC OR EG:198A6.2 OR CG3839. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89052675; PubMed=2461300; RA Alonso M.C., Cabrera C.V.; RT "The achaete-scute gene complex of Drosophila melanogaster comprises RT four homologous genes."; RL EMBO J. 7:2585-2591(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=94357065; PubMed=8076513; RA Martin-Bermudo M.D., Gonzalez F., Dominguez M., Rodriguez I., RA Ruiz-Gomez M., Romani S., Modolell J., Jimenez F.; RT "Molecular characterization of the lethal of scute genetic function."; RL Development 118:1003-1012(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- FUNCTION: AS-C PROTEINS ARE INVOLVED IN THE DETERMINATION OF THE CC NEURONAL PRECURSORS IN THE PERIPHERAL NERVOUS SYSTEM AND THE CC CENTRAL NERVOUS SYSTEM. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. CC -!- TISSUE SPECIFICITY: L(1)SC, SC AND AC STRONGLY LABEL THE CC PRESUMPTIVE STOMATOGASTRIC NERVOUS SYSTEM, WHILE ASE IS MORE CC PROMINENT IN THE PRESUMPTIVE PROCEPHALIC LOBE. CC -!- MISCELLANEOUS: AS-C PROTEINS ARE EXPRESSED FIRST EARLIER IN CC ECTODERM AND THEN IN THE INTERNALIZED NEUROBLASTS, WHILE T8 IS CC EXPRESSED IN PRESUMPTIVE NEURAL PRECURSORS, ONCE THEY HAVE CC SEGREGATED FROM THE ECTODERM. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12549; CAA31065.1; -. DR EMBL; X71806; CAA50680.1; -. DR EMBL; AE003417; AAF45500.1; -. DR EMBL; AL024453; CAA19656.1; -. DR PIR; S01165; S01165. DR TRANSFAC; T00003; -. DR FlyBase; FBgn0002561; l(1)sc. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Neurogenesis; Differentiation; Developmental protein; DNA-binding. FT DNA_BIND 86 96 BASIC DOMAIN. FT DOMAIN 97 146 HELIX-LOOP-HELIX MOTIF. FT CONFLICT 198 198 H -> R (IN REF. 1). SQ SEQUENCE 257 AA; 28972 MW; 1AEC8FA0B3144F87 CRC64; MTSICSSKFQ QQHYQLTNSN IFLLQHQHHH QTQQHQLIAP KIPLGTSQLQ NMQQSQQSNV GPMLSSQKKK FNYNNMPYGE QLPSVARRNA RERNRVKQVN NGFVNLRQHL PQTVVNSLSN GGRGSSKKLS KVDTLRIAVE YIRGLQDMLD DGTASSTRHI YNSADESSND GSSYNDYNDS LDSSQQFLTG ATQSAQSHSY HSASPTPSYS GSEISGGGYI KQELQEQDLK FDSFDSFSDE QPDDEELLDY ISSWQEQ // ID AST4_DROME STANDARD; PRT; 345 AA. AC P10084; O76890; DT 01-MAR-1989 (Rel. 10, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Achaete-scute complex protein T4 (Scute protein). GN SC OR T4 OR EG:198A6.1 OR CG3827. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=87273503; PubMed=3111716; RA Villares R., Cabrera C.V.; RT "The achaete-scute gene complex of D. melanogaster: conserved domains RT in a subset of genes required for neurogenesis and their homology to RT myc."; RL Cell 50:415-424(1987). RN [2] RP REVISIONS. RA Villares R.; RL Submitted (SEP-1988) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP FUNCTION. RX MEDLINE=90059894; PubMed=2583094; RA Torres M., Sanchez L.; RT "The scute (T4) gene acts as a numerator element of the X: a signal RT that determines the state of activity of sex-lethal in Drosophila."; RL EMBO J. 8:3079-3086(1989). CC -!- FUNCTION: AS-C PROTEINS ARE INVOLVED IN THE DETERMINATION OF THE CC NEURONAL PRECURSORS IN THE PERIPHERAL NERVOUS SYSTEM AND THE CC CENTRAL NERVOUS SYSTEM. ALSO INVOLVED IN SEX DETERMINATION AND CC DOSAGE COMPENSATION. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. CC -!- TISSUE SPECIFICITY: L(1)SC, SC AND AC STRONGLY LABEL THE CC PRESUMPTIVE STOMATOGASTRIC NERVOUS SYSTEM, WHILE ASE IS MORE CC PROMINENT IN THE PRESUMPTIVE PROCEPHALIC LOBE. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17119; AAA28313.1; -. DR EMBL; AE003417; AAF45499.1; -. DR EMBL; AL024453; CAA19657.1; -. DR PIR; B43731; B43731. DR TRANSFAC; T00004; -. DR FlyBase; FBgn0004170; sc. DR GO; GO:0008407; P:bristle morphogenesis; NAS. DR GO; GO:0007399; P:neurogenesis; IGI. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR GO; GO:0007540; P:sex determination, establishment of X:A ratio; NAS. DR GO; GO:0007530; P:sex determination; IMP. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Neurogenesis; Differentiation; Developmental protein. FT DNA_BIND 102 112 BASIC DOMAIN. FT DOMAIN 113 163 HELIX-LOOP-HELIX MOTIF. FT CONFLICT 161 161 R -> S (IN REF. 1). FT CONFLICT 213 213 T -> R (IN REF. 1). FT CONFLICT 219 219 L -> V (IN REF. 1). SQ SEQUENCE 345 AA; 38155 MW; DE68E49A8CCF16EB CRC64; MKNNNNTTKS TTMSSSVLST NETFPTTINS ATKIFRYQHI MPAPSPLIPG GNQNQPAGTM PIKTRKYTPR GMALTRCSES VSSLSPGSSP APYNVDQSQS VQRRNARERN RVKQVNNSFA RLRQHIPQSI ITDLTKGGGR GPHKKISKVD TLRIAVEYIR RLQDLVDDLN GGSNIGANNA VTQLQLCLDE SSSHSSSSST CSSSGHNTYY QNTISVSPLQ QQQQLQRQQF NHQPLTALSL NTNLVGTSVP GGDAGCVSTS KNQQTCHSPT SSFNSSMSFD SGTYEGVPQQ ISTHLDRLDH LDNELHTHSQ LQLKFEPYEH FQLDEEDCTP DDEEILDYIS LWQEQ // ID AST5_DROME STANDARD; PRT; 201 AA. AC P10083; Q9W5G4; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Achaete-scute complex protein T5 (Achaete). GN AC OR T5 OR EG:125H10.3 OR CG3796. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=87273503; PubMed=3111716; RA Villares R., Cabrera C.V.; RT "The achaete-scute gene complex of D. melanogaster: conserved domains RT in a subset of genes required for neurogenesis and their homology to RT myc."; RL Cell 50:415-424(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: AS-C PROTEINS ARE INVOLVED IN THE DETERMINATION OF THE CC NEURONAL PRECURSORS IN THE PERIPHERAL NERVOUS SYSTEM AND THE CC CENTRAL NERVOUS SYSTEM. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. CC -!- TISSUE SPECIFICITY: L(1)SC, SC AND AC STRONGLY LABEL THE CC PRESUMPTIVE STOMATOGASTRIC NERVOUS SYSTEM, WHILE ASE IS MORE CC PROMINENT IN THE PRESUMPTIVE PROCEPHALIC LOBE. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17120; AAA28312.1; -. DR EMBL; AL023873; CAA19641.1; -. DR EMBL; AE003417; AAF45498.1; -. DR PIR; A43731; A43731. DR TRANSFAC; T00005; -. DR FlyBase; FBgn0000022; ac. DR GO; GO:0008407; P:bristle morphogenesis; NAS. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Neurogenesis; Differentiation; Developmental protein; DNA-binding. FT DNA_BIND 27 37 BASIC DOMAIN. FT DOMAIN 38 91 HELIX-LOOP-HELIX MOTIF. SQ SEQUENCE 201 AA; 22753 MW; AAA906600CA764C0 CRC64; MALGSENHSV FNDDEESSSA FNGPSVIRRN ARERNRVKQV NNGFSQLRQH IPAAVIADLS NGRRGIGPGA NKKLSKVSTL KMAVEYIRRL QKVLHENDQQ KQKQLHLQQQ HLHFQQQQQH QHLYAWHQEL QLQSPTGSTS SCNSISSYCK PATSTIPGAT PPNNFHTKLE ASFEDYRNNS CSSGTEDEDI LDYISLWQDD L // ID AST8_DROME STANDARD; PRT; 486 AA. AC P09775; Q9W5G2; DT 01-MAR-1989 (Rel. 10, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Achaete-scute complex protein T8 (Asense). GN ASE OR T8 OR EG:165H7.2 OR CG3258. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90059952; PubMed=2510998; RA Gonzalez F., Romani S., Cubas P., Modolell J., Campuzano S.; RT "Molecular analysis of the asense gene, a member of the achaete-scute RT complex of Drosophila melanogaster, and its novel role in optic lobe RT development."; RL EMBO J. 8:3553-3562(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 67-486 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89052675; PubMed=2461300; RA Alonso M.C., Cabrera C.V.; RT "The achaete-scute gene complex of Drosophila melanogaster comprises RT four homologous genes."; RL EMBO J. 7:2585-2591(1988). CC -!- FUNCTION: INVOLVED IN THE DETERMINATION OF THE NEURONAL PRECURSORS CC OF OPTIC LOBES IN THE CENTRAL NERVOUS SYSTEM. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. CC -!- TISSUE SPECIFICITY: L(1)SC, SC AND AC STRONGLY LABEL THE CC PRESUMPTIVE STOMATOGASTRIC NERVOUS SYSTEM, WHILE ASE IS MORE CC PROMINENT IN THE PRESUMPTIVE PROCEPHALIC LOBE. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN IN THE N- AND CC C-TERMINUS DUE TO FRAMESHIFTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52892; CAA37074.1; -. DR EMBL; AL009188; CAA15673.1; -. DR EMBL; AE003417; AAF45502.1; -. DR EMBL; X12550; CAA31066.1; ALT_FRAME. DR PIR; S06949; S06949. DR TRANSFAC; T00006; -. DR FlyBase; FBgn0000137; ase. DR GO; GO:0007399; P:neurogenesis; IGI. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Neurogenesis; Differentiation; Developmental protein; DNA-binding. FT DOMAIN 8 22 PRO-RICH. FT DNA_BIND 162 172 BASIC DOMAIN. FT DOMAIN 173 224 HELIX-LOOP-HELIX MOTIF. SQ SEQUENCE 486 AA; 53222 MW; 17D5A1A0B9A5B222 CRC64; MAALSFSPSP PPKENPKENP NPGIKTTLKP FGKITVHNVL SESGANALQQ HIANQNTIIR KIRDFGMLGA VQSAAASTTN TTPISSQRKR PLGESQKQNR HNQQNQQLSK TSVPAKKCKT NKKLAVERPP KAGTISHPHK SQSDQSFGTP GRKGLPLPQA VARRNARERN RVKQVNNGFA LLREKIPEEV SEAFEAQGAG RGASKKLSKV ETLRMAVEYI RSLEKLLGFD FPPLNSQGNS SGSGDDSFMF IKDEFDCLDE HFDDSLSNYE MDEQQTVQQT LSEDMLNPPQ ASDLLPSLTT LNGLQYIRIP GTNTYQLLTT DLLGDLSHEQ KLEETAASGQ LSRSPVPQKV VRSPCSSPVS PVASTELLLQ TQTCATPLQQ QVIKQEYVST NISSSSNAQT SPQQQQQVQN LGSSPILPAF YDQEPVSFYD NVVLPGFKKE FSDILQQDQP NNTTAGCLSD ESMIDAIDWW EAHAPKSNGA CTNLSV // ID ASX_DROME STANDARD; PRT; 1669 AA. AC Q9V727; O76930; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polycomb protein Asx (Additional sex combs). GN ASX OR CG8787. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Imaginal disks; RX MEDLINE=98146384; PubMed=9477319; RA Sinclair D.A.R., Milne T.A., Hodgson J.W., Shellard J., Salinas C.A., RA Kyba M., Randazzo F., Brock H.W.; RT "The Additional sex combs gene of Drosophila encodes a chromatin RT protein that binds to shared and unique Polycomb group sites on RT polytene chromosomes."; RL Development 125:1207-1216(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP INTERACTION WITH TAN. RX MEDLINE=21290825; PubMed=11397012; RA Dietrich B.H., Moore J., Kyba M., dosSantos G., McCloskey F., RA Milne T.A., Brock H.W., Krause H.M.; RT "Tantalus, a novel ASX-interacting protein with tissue-specific RT functions."; RL Dev. Biol. 234:441-453(2001). CC -!- FUNCTION: ATYPICAL POLYCOMB GROUP PROTEIN, WHICH MAY BE INVOLVED CC IN BOTH POLYCOMB GROUP (PCG) AND TRITHORAX GROUP (TRXG) COMPLEXES. CC PCG AND TRXG PROTEINS ACT BY FORMING MULTIPROTEIN COMPLEXES, WHICH CC ARE RESPECTIVELY REQUIRED TO MAINTAIN THE TRANSCRIPTIONALLY CC REPRESSIVE AND TRANSCRIPTIONALLY ACTIVE STATE OF HOMEOTIC GENES CC THROUGHOUT DEVELOPMENT. PCG AND TRXG PROTEIN COMPLEXES ARE NOT CC REQUIRED TO INITIATE REPRESSION AND ACTIVATION, BUT TO MAINTAIN IT CC DURING LATER STAGES OF DEVELOPMENT. BOTH COMPLEXES PROBABLY ACT CC VIA METHYLATION OF HISTONES, RENDERING CHROMATIN HERITABLY CHANGED CC IN ITS EXPRESSIBILITY. CC -!- SUBUNIT: INTERACTS WITH TAN. CC -!- SUBCELLULAR LOCATION: NUCLEAR; ASSOCIATED WITH CHROMATIN. CC COLOCALIZES WITH MANY PCG SITES ON POLYTENE CHROMOSOMES. IT ALSO CC ASSOCIATES WITH MANY UNIQUE SITES ON POLYTENE CHROMOSOMES. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN NURSE CELLS AND DEPOSITED CC IN OOCYTES LATE IN OOGENESIS. UBIQUITOUS IN EARLY EMBRYOS. LATE CC EMBRYOS SHOW HIGHER LEVELS IN CNS AND NEURECTODERM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC EARLY EMBRYOS HAVE HIGH LEVELS OF EXPRESSION, THIS DROPS OFF AND CC ZYGOTIC EXPRESSION BEGINS AT 3-6 HOUR EMBRYOS. EXPRESSION LEVELS CC ARE LOW IN LARVAE AND MEDIUM IN PUPAE AND ADULTS. CC -!- DOMAIN: CONTAINS TWO LEU-XAA-XAA-LEU-LEU (LXXLL) MOTIFS, WHICH MAY CC BE REQUIRED FOR AN ASSOCIATION WITH NUCLEAR RECEPTORS (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ASX FAMILY. CC -!- SIMILARITY: CONTAINS 1 PHD-TYPE ZINC FINGER. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC FRAMESHIFTS IN POSITIONS 608 AND 719. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ001164; CAA04568.1; ALT_FRAME. DR EMBL; AE003814; AAF58239.1; -. DR FlyBase; FBgn0000142; Asx. DR GO; GO:0000785; C:chromatin; IEP. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0016563; F:transcriptional activator activity; NAS. DR GO; GO:0016564; F:transcriptional repressor activity; NAS. DR GO; GO:0045498; P:sex comb development; TAS. DR InterPro; IPR001965; Znf_PHD. DR PROSITE; PS01359; ZF_PHD_1; FALSE_NEG. DR PROSITE; PS50016; ZF_PHD_2; FALSE_NEG. KW Transcription regulation; Repressor; Nuclear protein; Zinc; KW Metal-binding; Zinc-finger; Repeat; Developmental protein. FT ZN_FING 1632 1669 PHD-TYPE (ATYPICAL). FT DOMAIN 8 12 POLY-THR. FT DOMAIN 122 126 POLY-GLN. FT DOMAIN 129 152 ALA-RICH. FT DOMAIN 638 715 SER-RICH. FT DOMAIN 747 751 POLY-GLN. FT DOMAIN 862 1202 GLN-RICH. FT DOMAIN 1287 1290 POLY-THR. FT DOMAIN 1520 1524 POLY-HIS. FT DOMAIN 1527 1536 POLY-GLN. FT SITE 224 228 LXXLL MOTIF 1. FT SITE 244 248 LXXLL MOTIF 2. FT CONFLICT 14 15 SQ -> CE (IN REF. 1). FT CONFLICT 187 187 K -> N (IN REF. 1). FT CONFLICT 1253 1253 S -> T (IN REF. 1). FT CONFLICT 1520 1520 MISSING (IN REF. 1). SQ SEQUENCE 1669 AA; 179841 MW; F65D87398D67D321 CRC64; MKTITPDTTT TTSSQHQQLL IPQADQHHQP MLQQQSLLAA PPPTMIMEHV NLVDDDEKDP LALEQLEVSP STKHTHSLRR HLPRIIVKPI PPEKKPMAPS EEAAVSTAPA PPTRLICSRR IQQQQQVKAA AAAAAAAAAA AAAAAAAAQA QATSSYPSAI SPGSKAGTSQ ASTMREVLAS IPGFSVKPRR RSNKKLTTAA QIEQTKDGKI DLETPDSILA STNLRALLNK QTFSLLPPLY QYNLIQLLPS VDREASELEQ PSSSASGGSP SEAIRLSASC LNNEFFARAC LEWRERLSEG EFTPENQLKL KTEAEREKNK LDPWKLKHFE PFWGEKNSRG KDKDKLESDC KNQKLSASIK SEPKPPATSQ QKPLQQATCD NETELKFDLS TKCETTSAKT TVAVAVADKS STFPPTGSQN NVLNEQQRRV LKRPSSSPSQ RKQAPTTIAT INLDDDLDEL PSTSKDSKQP KMDEIVPNAS GNVVAAPMVD VVDHSAVEMK IKDEQQHQRQ HQPLINSTCD KIEPSECSKE MIVAMKQVDS KEDVDSIASA AAMPAIAAVT PHTPKPEALA PNPDVANQFV SYLQNVELAA ETKAPLDNSN EADITTGTNS HDFVFSDTID HAYFQEHQST INHNFFTSSS SSNTATTAAN KLEEHSDKPE DSPLPIASSI SGSTPASSIT STSCTSSSSS SASMSSSCSS SNSGSTTTAP TTSSSAGAPT APLTLAAAAE TTLANVQAML STVAKLQQQQ QELPVELNSN EMYQHVQHDW NFGDIKLSSS QSSGDQQRNL SHEAIDLMDV VQDADVIDDI MHNDVCHDVL GDEDEGDQEE DEDDEVVECM TEEQQLIDED SEAVREIVDK LQQHQQQQNQ QQHHQQLHIQ DVVQLAQHSF MPQAHSEFGN DIGQEMLCDA VPMSAAEMEV SSTVITNSSN SNDSSNNISL CSSTNSLTIN QMPHQASQQP QQNAQSNAQQ QRQILVDSNG QIIGNFLLQQ QRQQQQQQLL QQFTLQAAAA QQQQQQQQQH QQQQQQQQQA TSSNSLGKTL PVALRNGTQQ FLSPNLIAQQ HQQQQQQQLE QHQQQATAQQ KHQQIQQFAL QQAQLHQRQL LAQAANNNLL QQQQQQQQNV ALPTTQAKFI AKPLNIISMT RPANASPTTA ATTANTASIP SAYANVVAVT GAQQQQSPPV PAPQQQTVQQ QQLANHNSNM QQLPNVLTMK TLPPSGVPTT IAQQRLQPKM PTGKGRKATS NRLPPGAVNL ERSYQICQAV IQNSPNRENL KAQLRPPAAI LNQHQPTTTT APAPINPVTL NVSTVAATPM SNITTATGSM AAAVAAAPPQ NVLKQEELLV SGAVGAGALP AGLPPNVMGV GRPGVYKVIG PRMSGFPRKK YVQRKPSPTT LIRHVFSPGP GGATATAQQL QMLQQHHQST TSPVPVQNPQ QPAPEQLIHQ NGNGQYVLVH RANVGAADNQ APRASSAPPM HQNQFVTVQN PLHSINGIPM GGRGRPASVD TTAGSGNVIA PPISATDALH HHHHEMQQQQ QHQQPQPLGN VGAAANIVRR NIAAGPNIAY IDGSNTNSSA VALMEAGNNY IVTTNASPTA APSPINQQPQ SQPTGTQHQH PLLQLHQTGE NTPPGNEATA TANNCACSLN AMVICQQCGA FCHDDCIGAA KLCVACVIR // ID ATB1_DROME STANDARD; PRT; 309 AA. AC Q24046; Q8MR34; Q9VM86; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Sodium/potassium-transporting ATPase beta-1 chain (Sodium/potassium- DE dependent ATPase beta-1 subunit) (Protein nervana 1). GN NRV1 OR CG9258. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=95296317; PubMed=7777518; RA Sun B., Salvaterra P.M.; RT "Two Drosophila nervous system antigens, Nervana 1 and 2, are RT homologous to the beta subunit of Na+,K(+)-ATPase."; RL Proc. Natl. Acad. Sci. U.S.A. 92:5396-5400(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=95310960; PubMed=7540667; RA Sun B., Salvaterra P.M.; RT "Characterization of nervana, a Drosophila melanogaster neuron- RT specific glycoprotein antigen recognized by anti-horseradish RT peroxidase antibodies."; RL J. Neurochem. 65:434-443(1995). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=98311194; PubMed=9648860; RA Sun B., Wang W., Salvaterra P.M.; RT "Functional analysis and tissue-specific expression of Drosophila RT Na+,K+-ATPase subunits."; RL J. Neurochem. 71:142-151(1998). CC -!- FUNCTION: THIS IS THE NON-CATALYTIC COMPONENT OF THE ACTIVE CC ENZYME, WHICH CATALYZES THE HYDROLYSIS OF ATP COUPLED WITH THE CC EXCHANGE OF NA AND K IONS ACROSS THE PLASMA MEMBRANE. THE BETA CC SUBUNIT REGULATES, THROUGH ASSEMBLY OF ALPHA/BETA HETERODIMERS, CC THE NUMBER OF SODIUM PUMPS TRANSPORTED TO THE PLASMA MEMBRANE. CC -!- SUBUNIT: COMPOSED OF TWO SUBUNITS: ALPHA (CATALYTIC) AND BETA (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN (PROBABLE). CC -!- TISSUE SPECIFICITY: IN EMBRYOS, IT IS EXPRESSED IN THE NEURONS OF CC THE CNS AND PNS, IN GARLAND CELLS AND POSTERIOR SPIRACLES. IN CC ADULTS, IT IS CONCENTRATED IN THE THORAX AND ABDOMEN (MUSCLE CC TISSUE, DIGESTIVE SYSTEM AND MALPIGHIAN TUBULES) AND WEAKLY CC EXPRESSED IN THE HEAD. EXPRESSION IS DIFFUSE IN THE NERVOUS CC SYSTEM. CC -!- DEVELOPMENTAL STAGE: EXPRESSION IN EMBRYOS IS FIRST SEEN 12 HOURS CC AFTER OVIPOSITION, PEAKS AT 24 HOURS AND DECREASES TO A LOW LEVEL CC BY 48 HOURS. LOW LEVELS ARE SEEN DURING LARVAL AND EARLY PUPAL CC DEVELOPMENT. LEVELS INCREASE DURING LATE PUPAE TO MAXIMAL AT THE CC ADULT STAGE. CC -!- SIMILARITY: BELONGS TO THE NA+/K+ AND H+/K+ ATPASES BETA CHAIN CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U22438; AAC46608.1; -. DR EMBL; AE003615; AAF52437.1; -. DR EMBL; AY122147; AAM52659.1; -. DR FlyBase; FBgn0015776; nrv1. DR InterPro; IPR000402; Na/K_ATPase_beta. DR Pfam; PF00287; Na_K-ATPase; 1. DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; FALSE_NEG. DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; FALSE_NEG. KW Sodium/potassium transport; Transmembrane; Glycoprotein; KW Signal-anchor; Multigene family. FT DOMAIN 1 45 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 46 66 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 67 309 EXTRACELLULAR (POTENTIAL). FT DISULFID 143 155 BY SIMILARITY. FT DISULFID 165 179 BY SIMILARITY. FT DISULFID 225 282 BY SIMILARITY. FT CARBOHYD 133 133 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 205 205 D -> N (IN REF. 3). FT CONFLICT 219 220 QQ -> HE (IN REF. 1). FT CONFLICT 226 226 N -> F (IN REF. 1). FT CONFLICT 295 295 V -> A (IN REF. 1). SQ SEQUENCE 309 AA; 35309 MW; 35EA43910B86D84F CRC64; MSKNNGKGAK GEFEFPQPAK KQTFSEMIYN PQEGTFFGRT GKSWSQLLLF YTIFYIVLAA LFTICMQGLL STISDTEPKW KLQDSLIGTN PGLGFRPLSE QTERGSVIAF DGKKPAESDY WIELIDDFLR DYNHTEGRDM KHCGFGQVLE PTDVCVVNTD LFGGCSKANN YGYKTNQPCI FLKLNKIFGW IPEVYDKEEK DMPDDLKKVI NETKTEERQQ VWVSCNGHLG KDKENFQNIR YFPSQGFPSY YYPFLNQPGY LSPLVAVQFN SPPKGQMLDV ECRAWAKNIQ YSGSVRDRKG SVTFQILLD // ID ATB2_DROME STANDARD; PRT; 323 AA. AC Q24048; Q24047; Q9VM84; Q9VM85; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Sodium/potassium-transporting ATPase beta-2 chain (Sodium/potassium- DE dependent ATPase beta-2 subunit) (Protein nervana 2). GN NRV2 OR CG9261. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=95296317; PubMed=7777518; RA Sun B., Salvaterra P.M.; RT "Two Drosophila nervous system antigens, Nervana 1 and 2, are RT homologous to the beta subunit of Na+,K(+)-ATPase."; RL Proc. Natl. Acad. Sci. U.S.A. 92:5396-5400(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2.2). RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=95310960; PubMed=7540667; RA Sun B., Salvaterra P.M.; RT "Characterization of nervana, a Drosophila melanogaster neuron- RT specific glycoprotein antigen recognized by anti-horseradish RT peroxidase antibodies."; RL J. Neurochem. 65:434-443(1995). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=98311194; PubMed=9648860; RA Sun B., Wang W., Salvaterra P.M.; RT "Functional analysis and tissue-specific expression of Drosophila RT Na+,K+-ATPase subunits."; RL J. Neurochem. 71:142-151(1998). CC -!- FUNCTION: THIS IS THE NON-CATALYTIC COMPONENT OF THE ACTIVE CC ENZYME, WHICH CATALYZES THE HYDROLYSIS OF ATP COUPLED WITH THE CC EXCHANGE OF NA AND K IONS ACROSS THE PLASMA MEMBRANE. THE BETA CC SUBUNIT REGULATES, THROUGH ASSEMBLY OF ALPHA/BETA HETERODIMERS, CC THE NUMBER OF SODIUM PUMPS TRANSPORTED TO THE PLASMA MEMBRANE. CC -!- SUBUNIT: COMPOSED OF TWO SUBUNITS: ALPHA (CATALYTIC) AND BETA (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2.2; CC IsoId=Q24048-1; Sequence=Displayed; CC Name=2.1; CC IsoId=Q24048-2; Sequence=VSP_000350; CC -!- TISSUE SPECIFICITY: IN EMBRYOS, IT IS EXPRESSED IN THE NEURONS OF CC THE CNS AND PNS, IN GARLAND CELLS AND POSTERIOR SPIRACLES. IN CC ADULTS, IT SHOWS A NERVOUS SYSTEM SPECIFIC DISTRIBUTION: OPTIC CC LOBES, BRAIN, THORACIC GANGLIA AND AXONAL PATHWAYS IN THE LEG. CC BOTH ISOFORMS CONCENTRATE IN THE ADULT HEAD, ISOFORM 2.2 BEING CC PREDOMINANT. BOTH ISOFORMS ARE WEAKLY EXPRESSED IN THE THORAX AND CC VERY POORLY EXPRESSED IN THE ABDOMEN. CC -!- DEVELOPMENTAL STAGE: EXPRESSION IN EMBRYOS IS FIRST SEEN 12 HOURS CC AFTER OVIPOSITION, PEAKS AT 24 HOURS AND DECREASES TO A LOW LEVEL CC BY 48 HOURS. LOW LEVELS ARE SEEN DURING LARVAL AND EARLY PUPAL CC DEVELOPMENT. LEVELS INCREASE DURING LATE PUPAE TO MAXIMAL AT THE CC ADULT STAGE. CC -!- SIMILARITY: BELONGS TO THE NA+/K+ AND H+/K+ ATPASES BETA CHAIN CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U22439; AAC46609.1; -. DR EMBL; U22440; AAC46610.1; -. DR EMBL; AE003615; AAF52438.2; -. DR EMBL; AE003615; AAN10600.1; -. DR EMBL; AY060289; AAL25328.1; -. DR FlyBase; FBgn0015777; nrv2. DR InterPro; IPR000402; Na/K_ATPase_beta. DR Pfam; PF00287; Na_K-ATPase; 1. DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; FALSE_NEG. DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; FALSE_NEG. KW Sodium/potassium transport; Transmembrane; Glycoprotein; KW Signal-anchor; Multigene family; Alternative splicing. FT DOMAIN 1 50 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 51 71 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 72 323 EXTRACELLULAR (POTENTIAL). FT DISULFID 153 165 BY SIMILARITY. FT DISULFID 175 189 BY SIMILARITY. FT DISULFID 241 298 BY SIMILARITY. FT CARBOHYD 180 180 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 206 206 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 46 MPTITEDCIDGFQQYYSRPPERPKKKSLKQMVYDSEDNSYF FT GRSMD -> MSKPVPMSPSFVDEDLHNLRKPKPFKLGQFLY FT NTEDGTVMGRDRS (in isoform 2.1). FT /FTId=VSP_000350. FT CONFLICT 162 162 G -> A (IN REF. 1). FT CONFLICT 307 307 H -> R (IN REF. 1). SQ SEQUENCE 323 AA; 37283 MW; 8926A9D1FC48D6EF CRC64; MPTITEDCID GFQQYYSRPP ERPKKKSLKQ MVYDSEDNSY FGRSMDSWAK IGIFYVAFYG VLAALVAICM WAFFQTLDPR IPKWTLDRSL IGTNPGLGFR PLPPVDNVES TLIWYKGTQH ENYKHWTDSL DDFLAVYKVP GLTPGRGQNI YNCDYNQPPP KGQVCDVDIK TWSPCTKENN YSYHKSAPCI FLKLNKIYGW IPEYYNRSND LPANMPASLK TYIAEVEKTQ PEKLNTIWVS CEGENPADQE NIGAVNYLPI RGFPGYFYPY QNSEGYLSPL VAVHFQRPKR GIIINVECRA WARNIIHDRK ERIGSVHYEL LID // ID ATC1_DROME STANDARD; PRT; 1020 AA. AC P22700; Q9W1G2; Q9W1G3; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type DE (EC 3.6.3.8) (Calcium pump). GN CA-P60A OR CG3725. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91097592; PubMed=2148477; RA Magyar A., Varadi A.; RT "Molecular cloning and chromosomal localization of a RT sarco/endoplasmic reticulum-type Ca2(+)-ATPase of Drosophila RT melanogaster."; RL Biochem. Biophys. Res. Commun. 173:872-877(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 357-513 FROM N.A. RX MEDLINE=90092469; PubMed=2557235; RA Varadi A., Gilmore-Heber M., Benz E.J. Jr.; RT "Amplification of the phosphorylation site-ATP-binding site cDNA RT fragment of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila RT melanogaster by polymerase chain reaction."; RL FEBS Lett. 258:203-207(1989). CC -!- FUNCTION: THIS MAGNESIUM-DEPENDENT ENZYME CATALYZES THE HYDROLYSIS CC OF ATP COUPLED WITH THE TRANSPORT OF CALCIUM. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + CA(2+)(CIS) = ADP + PHOSPHATE + CC CA(2+)(TRANS). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. SARCOPLASMIC AND CC ENDOPLASMIC RETICULUM. CC -!- SIMILARITY: BELONGS TO THE CATION TRANSPORT ATPASES FAMILY (P-TYPE CC ATPASES). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M62892; AAB00735.1; -. DR EMBL; AE003462; AAF47104.1; -. DR EMBL; X17472; CAA35505.1; -. DR PIR; A36691; A36691. DR HSSP; P04191; 1EUL. DR FlyBase; FBgn0004551; Ca-P60A. DR InterPro; IPR001757; ATPase_E1-E2. DR InterPro; IPR005782; Calcium_ATPase. DR InterPro; IPR006068; Cation_ATPase_C. DR InterPro; IPR004014; Cation_ATPase_N. DR InterPro; IPR008250; E1-E2_ATPase_reg. DR InterPro; IPR005834; Hydrolase. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1. DR TIGRFAMs; TIGR01494; ATPase_P-type; 7. DR PROSITE; PS00154; ATPASE_E1_E2; 1. KW Hydrolase; Calcium transport; Transmembrane; Phosphorylation; KW ATP-binding; Metal-binding; Magnesium; Calcium-binding. FT DOMAIN 1 48 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 49 69 1 (BY SIMILARITY). FT DOMAIN 70 89 LUMENAL (BY SIMILARITY). FT TRANSMEM 90 110 2 (BY SIMILARITY). FT DOMAIN 111 253 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 254 273 3 (BY SIMILARITY). FT DOMAIN 274 295 LUMENAL (BY SIMILARITY). FT TRANSMEM 296 313 4 (BY SIMILARITY). FT DOMAIN 314 757 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 758 777 5 (BY SIMILARITY). FT DOMAIN 778 787 LUMENAL (BY SIMILARITY). FT TRANSMEM 788 808 6 (BY SIMILARITY). FT DOMAIN 809 828 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 829 851 7 (BY SIMILARITY). FT DOMAIN 852 897 LUMENAL (BY SIMILARITY). FT TRANSMEM 898 917 8 (BY SIMILARITY). FT DOMAIN 918 930 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 931 949 9 (BY SIMILARITY). FT DOMAIN 950 964 LUMENAL (BY SIMILARITY). FT TRANSMEM 965 985 10 (BY SIMILARITY). FT DOMAIN 986 1020 CYTOPLASMIC (BY SIMILARITY). FT MOD_RES 351 351 PHOSPHORYLATION (BY SIMILARITY). FT METAL 703 703 MAGNESIUM (BY SIMILARITY). FT METAL 707 707 MAGNESIUM (BY SIMILARITY). FT METAL 304 304 CALCIUM 2 (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT METAL 305 305 CALCIUM 2 (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT METAL 307 307 CALCIUM 2 (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT METAL 309 309 CALCIUM 2 (BY SIMILARITY). FT METAL 768 768 CALCIUM 1 (BY SIMILARITY). FT METAL 771 771 CALCIUM 1 (BY SIMILARITY). FT METAL 796 796 CALCIUM 2 (BY SIMILARITY). FT METAL 799 799 CALCIUM 1 (BY SIMILARITY). FT METAL 800 800 CALCIUM 1 (BY SIMILARITY). FT METAL 800 800 CALCIUM 2 (BY SIMILARITY). FT METAL 908 908 CALCIUM 1 (BY SIMILARITY). FT CONFLICT 302 302 L -> V (IN REF. 1). FT CONFLICT 357 357 T -> L (IN REF. 3). SQ SEQUENCE 1020 AA; 111700 MW; 6A62D350BF316984 CRC64; MEDGHSKTVE QSLNFFGTDP ERGLTLDQIK ANQKKYGPNE LPTEEGKSIW QLVLEQFDDL LVKILLLAAI ISFVLALFEE HEETFTAFVE PLVILLILIA NAVVGVWQER NAESAIEALK EYEPEMGKVV RQDKSGIQKV RAKEIVPGDL VEVSVGDKIP ADIRITHIYS TTLRIDQSIL TGESVSVIKH TDAIPDPRAV NQDKKNILFS GTNVAAGKAR GVVIGTGLST AIGKIRTEMS ETEEIKTPLQ QKLDEFGEQL SKVISVICVA VWAINIGHFN DPAHGGSWIK GAIYYFKIAV ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ MSVSRMFIFD KVEGNDSSFL EFEMTGSTYE PIGEVFLNGQ RIKAADYDTL QELSTICIMC NDSAIDYNEF KQAFEKVGEA TETALIVLAE KLNSFSVNKS GLDRRSAAIA CRGEIETKWK KEFTLEFSRD RKSMSSYCTP LKASRLGTGP KLFVKGAPEG VLERCTHARV GTTKVPLTSA LKAKILALTG QYGTGRDTLR CLALAVADSP MKPDEMDLGD STKFYQYEVN LTFVGVVGML DPPRKEVFDS IVRCRAAGIR VIVITGDNKA TAEAICRRIG VFAEDEDTTG KSYSGREFDD LSPTEQKAAV ARSRLFSRVE PQHKSKIVEF LQSMNEISAM TGDGVNDAPA LKKAEIGIAM GSGTAVAKSA AEMVLADDNF SSIVSAVEEG RAIYNNMKQF IRYLISSNIG EVVSIFLTAA LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKP PRKADEGLIS GWLFFRYMAI GFYVGAATVG AAAWWFVFSD EGPKLSYWQL THHLSCLGGG DEFKGVDCKI FSDPHAMTMA LSVLVTIEML NAMNSLSENQ SLITMPPWCN LWLIGSMALS FTLHFVILYV DVLSTVFQVT PLSAEEWITV MKFSIPVVLL DETLKFVARK IADGESPIYK MHGIVLMWAV FFGLLYAMML // ID ATE1_DROME STANDARD; PRT; 462 AA. AC O96539; Q9V906; Q9V907; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Arginyl-tRNA--protein transferase 1 (EC 2.3.2.8) (R-transferase 1) DE (Arginyltransferase 1) (Arginine-tRNA--protein transferase 1). GN ATE1 OR CG9204. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=99077957; PubMed=9858543; RA Kwon Y.T., Kashina A.S., Varshavsky A.; RT "Alternative splicing results in differential expression, activity, RT and localization of the two forms of arginyl-tRNA-protein transferase, RT a component of the N-end rule pathway."; RL Mol. Cell. Biol. 19:182-193(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: INVOLVED IN THE POSTTRANSLATIONAL CONJUGATION OF CC ARGININE TO THE N-TERMINAL ASPARTATE OR GLUTAMATE OF A PROTEIN. CC THIS ARGINYLATION IS REQUIRED FOR DEGRADATION OF THE PROTEIN VIA CC THE UBIQUITIN PATHWAY. DOES NOT ARGINYLATE CYSTEINE RESIDUES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: L-ARGINYL-TRNA + PROTEIN = TRNA + L-ARGINYL- CC PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=A; CC IsoId=O96539-1; Sequence=Displayed; CC Name=B; CC IsoId=O96539-2; Sequence=VSP_000339; CC Name=C; CC IsoId=O96539-3; Sequence=VSP_000338, VSP_000340; CC -!- SIMILARITY: BELONGS TO THE R-TRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF079101; AAD12369.1; -. DR EMBL; AE003793; AAF57496.2; -. DR EMBL; AE003793; AAF57497.2; -. DR EMBL; AE003793; AAF57498.1; -. DR FlyBase; FBgn0025720; Ate1. DR InterPro; IPR007472; ATE_C. DR InterPro; IPR007471; ATE_N. DR Pfam; PF04377; ATE_C; 1. DR Pfam; PF04376; ATE_N; 1. KW Transferase; Acyltransferase; Ubl conjugation pathway; KW Alternative splicing. FT VARSPLIC 106 210 GDGDGEADADYAIVAPEVTASEPQPQLPDKSPPVINVEQVA FT SLATAQRKPTKQATAAAVEAPTLGSNKSSLLSSSAAAPISN FT KPCKKAKQMRLDRRLAKLGDSAS -> DEAGNCCRGGSSYV FT GVQQIITLIFISRSTDLKQAVQEGQADAIGSTAGQAGRLGL FT LLNEIPYPGKDTSRLLEHGQRDKQTSAKAALNSRLRRRVPA FT DPAPEFCAL (in isoform C). FT /FTId=VSP_000338. FT VARSPLIC 175 181 Missing (in isoform B). FT /FTId=VSP_000339. FT VARSPLIC 211 462 Missing (in isoform C). FT /FTId=VSP_000340. FT CONFLICT 455 462 ASAWDRLR -> LRGTVSDDDIIIEYSKLVGKECARRM FT (IN REF. 1). SQ SEQUENCE 462 AA; 52818 MW; B994157874EF8307 CRC64; MSLSIVSYYG SQQSKCGYCA GANCSLSHGM HAYQLDCRDY QDLIDRGWRR CGYYCYKLRN QETCCPCYTI KCNGLEFKLS KSNKRILRRI NRFLRDGKRE SKPEAGDGDG EADADYAIVA PEVTASEPQP QLPDKSPPVI NVEQVASLAT AQRKPTKQAT AAAVEAPTLG SNKSSLLSSS AAAPISNKPC KKAKQMRLDR RLAKLGDSAS YSTKSLTQEK TLRDFLNTDS ETNKHRLKLR LIHVYDDEFR RTLPQSFALY KKYQISIHND PPKDQDAYKE HLQATPLQNE KPWDGPEMGY GSFHQQYWLD DKLIAVGVID ILPGCVSSVY FFYDPDYSFL SLGTYGSLRE IELVQSLAEK VPSLKYYYMG FYIHSCPKMR YKGKLSPSYL LCPETYEWLP LTDVIRAKLD EHKYQRLNED PAARDVNEFL MEHLDEVKLL LGGRTRTDYK HFRQASAWDR LR // ID ATNA_DROME STANDARD; PRT; 1041 AA. AC P13607; O61494; Q86MY6; Q86MY7; Q86MY8; Q86MY9; Q86MZ0; Q8IN40; AC Q8T0L8; Q9VDG6; Q9VDG7; Q9VDG8; DT 01-JAN-1990 (Rel. 13, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sodium/potassium-transporting ATPase alpha chain (EC 3.6.3.9) (Sodium DE pump) (Na+/K+ ATPase). GN ATP-ALPHA OR NA-P OR CG5670. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=89231618; PubMed=2540956; RA Lebovitz R.M., Takeyasu K., Fambrough D.M.; RT "Molecular characterization and expression of the (Na+ + K+)-ATPase RT alpha-subunit in Drosophila melanogaster."; RL EMBO J. 8:193-202(1989). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Head; RX MEDLINE=98311194; PubMed=9648860; RA Sun B., Wang W., Salvaterra P.M.; RT "Functional analysis and tissue-specific expression of Drosophila RT Na+,K+-ATPase subunits."; RL J. Neurochem. 71:142-151(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM 3). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 400-524 FROM N.A. RX MEDLINE=90092469; PubMed=2557235; RA Varadi A., Gilmore-Heber M., Benz E.J. Jr.; RT "Amplification of the phosphorylation site-ATP-binding site cDNA RT fragment of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila RT melanogaster by polymerase chain reaction."; RL FEBS Lett. 258:203-207(1989). RN [7] RP SEQUENCE OF 1-8 FROM N.A. RA Feng Y., Fambrough D.M.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP SEQUENCE OF 1-35 AND 835-865 FROM N.A., FUNCTION, ALTERNATIVE RP SPLICING, AND MUTAGENESIS OF ASP-1020 AND GLU-1021. RX MEDLINE=22486896; PubMed=12598616; RA Palladino M.J., Bower J.E., Kreber R., Ganetzky B.; RT "Neural dysfunction and neurodegeneration in Drosophila Na+/K+ ATPase RT alpha subunit mutants."; RL J. Neurosci. 23:1276-1286(2003). CC -!- FUNCTION: THIS IS THE CATALYTIC COMPONENT OF THE ACTIVE ENZYME, CC WHICH CATALYZES THE HYDROLYSIS OF ATP COUPLED WITH THE EXCHANGE OF CC NA AND K IONS ACROSS THE PLASMA MEMBRANE. THIS ACTION CREATES THE CC ELECTROCHEMICAL GRADIENT OF NA AND K, PROVIDING THE ENERGY FOR CC ACTIVE TRANSPORT OF VARIOUS NUTRIENTS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + NA(+)(IN) + K(+)(OUT) = ADP + CC PHOSPHATE + NA(+)(OUT) + K(+)(IN). CC -!- SUBUNIT: COMPOSED OF THREE SUBUNITS: ALPHA (CATALYTIC), BETA AND CC GAMMA. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Exon 6 has 4 mutually exclusive forms (6a, 6b, 6c and CC 6d). Additional isoforms may exist; CC Name=1; Synonyms=A; CC IsoId=P13607-1; Sequence=Displayed; CC Name=2; Synonyms=B, C; CC IsoId=P13607-2; Sequence=VSP_000417; CC Name=3; Synonyms=D; CC IsoId=P13607-3; Sequence=VSP_000417, VSP_008077, VSP_008078; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=P13607-4; Sequence=VSP_008074; CC Name=5; CC IsoId=P13607-5; Sequence=VSP_008075; CC Name=6; CC IsoId=P13607-6; Sequence=VSP_000418; CC Name=7; CC IsoId=P13607-7; Sequence=VSP_008076; CC -!- SIMILARITY: BELONGS TO THE CATION TRANSPORT ATPASES FAMILY (P-TYPE CC ATPASES). SUBFAMILY IIC. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14476; CAA32638.1; -. DR EMBL; AF044974; AAC05260.1; -. DR EMBL; AE003732; AAF55825.3; -. DR EMBL; AE003732; AAF55826.2; -. DR EMBL; AE003732; AAF55827.3; -. DR EMBL; AY069184; AAL39329.1; -. DR EMBL; X17471; CAA35504.1; -. DR EMBL; U55767; AAB01189.1; -. DR EMBL; AY174097; AAO33930.1; -. DR EMBL; AY174097; AAO33931.1; -. DR EMBL; AY174097; AAO33932.1; -. DR EMBL; AY174097; AAO33933.1; -. DR EMBL; AY174098; AAO33929.1; -. DR PIR; S03632; S03632. DR HSSP; P04191; 1EUL. DR FlyBase; FBgn0002921; Atp-alpha. DR InterPro; IPR001757; ATPase_E1-E2. DR InterPro; IPR006069; Cation_ATPase. DR InterPro; IPR006068; Cation_ATPase_C. DR InterPro; IPR004014; Cation_ATPase_N. DR InterPro; IPR008250; E1-E2_ATPase_reg. DR InterPro; IPR005834; Hydrolase. DR InterPro; IPR005775; Na/K_ATPase_alph. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00121; NAKATPASE. DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1. DR TIGRFAMs; TIGR01494; ATPase_P-type; 5. DR PROSITE; PS00154; ATPASE_E1_E2; 1. KW Hydrolase; Sodium/potassium transport; Transmembrane; KW Phosphorylation; ATP-binding; Alternative splicing. FT TRANSMEM 115 135 POTENTIAL. FT TRANSMEM 147 167 POTENTIAL. FT TRANSMEM 312 332 POTENTIAL. FT TRANSMEM 338 358 POTENTIAL. FT TRANSMEM 808 828 POTENTIAL. FT TRANSMEM 870 890 POTENTIAL. FT TRANSMEM 935 955 POTENTIAL. FT TRANSMEM 970 990 POTENTIAL. FT MOD_RES 394 394 PHOSPHORYLATION (PROBABLE). FT BINDING 526 526 ATP (BY SIMILARITY). FT VARSPLIC 1 8 MALRSDYE -> MSAQ (in isoform 4). FT /FTId=VSP_008074. FT VARSPLIC 1 39 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_000417. FT VARSPLIC 835 865 VPAISLAYEHAEADIMKRPPRDPFNDKLVNS -> IPAISL FT AYEGPEADIMKRRPRNPEIDNLVNE (in isoform 5). FT /FTId=VSP_008075. FT VARSPLIC 835 865 VPAISLAYEHAEADIMKRPPRDPFNDKLVNS -> IPAISL FT AYEQAESDIMKRQPRDPYRDNLVNR (in isoform 7). FT /FTId=VSP_008076. FT VARSPLIC 836 878 PAISLAYEHAEADIMKRPPRDPFNDKLVNSRLISMAYGQIG FT MI -> SLDLCPKPKLHRRLKLKLLLSQYHSSKLYSYTSCS FT PSQLIVKN (in isoform 3). FT /FTId=VSP_008077. FT VARSPLIC 879 1041 Missing (in isoform 3). FT /FTId=VSP_008078. FT VARSPLIC 844 865 HAEADIMKRPPRDPFNDKLVNS -> TAESDIMKRQPRNPF FT QDKLVNE (in isoform 6). FT /FTId=VSP_000418. FT MUTAGEN 1020 1020 D->N: IN ALLELE ATP-ALPHA-DTS2; FT HOMOZYGOUS LETHAL AND TEMPERATURE FT DEPENDENT BANG SENSITIVE PARALYSIS, FT SHORTENED LIFE SPAN AND NEURODEGENERATION FT WHEN HETEROZYGOUS. FT MUTAGEN 1021 1021 E->K: IN ALLELE ATP-ALPHA-DTS1; FT HOMOZYGOUS LETHAL AND TEMPERATURE FT DEPENDENT BANG SENSITIVE PARALYSIS, FT SHORTENED LIFE SPAN AND FT NEURODEGENERATION WHEN HETEROZYGOUS. FT CONFLICT 69 69 L -> M (IN REF. 1). FT CONFLICT 85 85 K -> R (IN REF. 1). FT CONFLICT 97 97 MISSING (IN REF. 1). FT CONFLICT 112 113 KN -> ED (IN REF. 1). FT CONFLICT 117 118 GF -> V (IN REF. 1). FT CONFLICT 163 163 I -> V (IN REF. 1). FT CONFLICT 192 192 E -> G (IN REF. 2). FT CONFLICT 196 197 LT -> PS (IN REF. 1). FT CONFLICT 207 208 DV -> VL (IN REF. 1). FT CONFLICT 211 212 VK -> LE (IN REF. 1). FT CONFLICT 216 221 RIPADI -> LIPLVY (IN REF. 1). FT CONFLICT 228 228 N -> D (IN REF. 1). FT CONFLICT 270 272 GTA -> ALP (IN REF. 1). FT CONFLICT 290 290 G -> A (IN REF. 1). FT CONFLICT 299 299 MISSING (IN REF. 1). FT CONFLICT 402 402 N -> T (IN REF. 6). FT CONFLICT 429 429 Y -> C (IN REF. 5). FT CONFLICT 488 488 I -> N (IN REF. 6). FT CONFLICT 811 811 F -> S (IN REF. 1). FT CONFLICT 843 843 E -> D (IN REF. 1). SQ SEQUENCE 1041 AA; 115604 MW; B2DD36B2E9029F43 CRC64; MALRSDYEHG RADSYRVATV IATDDDNRTA DGQYKSRRKM PAKVNKKENL DDLKQELDID FHKISPEELY QRFQTHPENG LSHAKAKENL ERDGPNALTP PKQTPEWVKF CKNLFGGFAM LLWIGAILCF VAYSIQASTS EEPADDNLYL GIVLSAVVIV TGIFSYYQES KSSKIMESFK NMVPQFATVI REGEKLTLRA EDLVLGDVVE VKFGDRIPAD IRIIEARNFK VDNSSLTGES EPQSRGAEFT HENPLETKNL AFFSTNAVEG TAKGVVISCG DHTVMGRIAG LASGLDTGET PIAKEIHHFI HLITGVAVFL GVTFFVIAFI LGYHWLDAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA SKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIIEADT TEDQSGVQYD RTSPGFKALS RIATLCNRAE FKGGQDGVPI LKKEVSGDAS EAALLKCMEL ALGDVMNIRK RNKKIAEVPF NSTNKYQVSI HETEDTNDPR YLLVMKGAPE RILERCSTIF INGKEKVLDE EMKEAFNNAY MELGGLGERV LGFCDFMLPS DKYPNGFKFN TDDINFPIDN LRFVGLMSMI DPPRAAVPDA VAKCRSAGIK VIMVTGDHPI TAKAIAKSVG IISEGNETVE DIAQRLNIPV SEVNPREAKA AVVHGAELRD VSSDQLDEIL RYHTEIVFAR TSPQQKLIIV EGCQRMGAIV AVTGDGVNDS PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEISPFLA FILCDIPLPL GTVTILCIDL GTDMVPAISL AYEHAEADIM KRPPRDPFND KLVNSRLISM AYGQIGMIQA AAGFFVYFVI MAENGFLPKK LFGIRKMWDS KAVNDLTDSY GQEWTYRDRK TLEYTCHTAF FISIVVVQWA DLIICKTRRN SIFQQGMRNW ALNFGLVFET VLAAFLSYCP GMEKGLRMYP LKLVWWFPAI PFALAIFIYD ETRRFYLRRN PGGWLEQETY Y // ID ATO_DROME STANDARD; PRT; 312 AA. AC P48987; Q9VHU0; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Atonal protein. GN ATO OR CG7508. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; RX MEDLINE=93313961; PubMed=8324823; RA Jarman A.P., Grau Y., Jan L.Y., Jan Y.N.; RT "Atonal is a proneural gene that directs chordotonal organ formation RT in the Drosophila peripheral nervous system."; RL Cell 73:1307-1321(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=94255014; PubMed=8196767; RA Jarman A.P., Grell E.H., Ackerman L., Jan L.Y., Jan Y.N.; RT "Atonal is the proneural gene for Drosophila photoreceptors."; RL Nature 369:398-400(1994). CC -!- FUNCTION: DEVELOPMENTAL PROTEIN INVOLVED IN NEUROGENESIS. REQUIRED CC FOR THE FORMATION OF CHORDOTONAL ORGANS AND PHOTORECEPTORS. SEEMS CC TO BIND TO E BOXES. SPECIFICALLY REQUIRED FOR THE PHOTORECEPTOR R8 CC SELECTION. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. FORMS A HETERODIMER WITH DAUGHTERLESS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: PRONEURAL CLUSTERS AND SENSE ORGAN PRECURSORS CC OF THE CHORDOTONAL ORGANS, OPTIC FURROW OF THE EYE-ANTENNAL DISK CC AND DEVELOPING BRAIN LOBE. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L36646; AAA21879.1; -. DR EMBL; AE003678; AAF54209.1; -. DR PIR; A40708; A40708. DR FlyBase; FBgn0010433; ato. DR GO; GO:0007420; P:brain development; IMP. DR GO; GO:0007173; P:EGF receptor signaling pathway; IGI. DR GO; GO:0007605; P:hearing; IMP. DR GO; GO:0007438; P:oenocyte development; IMP. DR GO; GO:0007422; P:peripheral nervous system development; NAS. DR GO; GO:0045464; P:R8 cell fate specification; NAS. DR GO; GO:0007224; P:smoothened signaling pathway; IGI. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Neurogenesis; Differentiation; Developmental protein; Nuclear protein; KW Transcription regulation; DNA-binding. FT DNA_BIND 255 267 BASIC DOMAIN. FT DOMAIN 268 308 HELIX-LOOP-HELIX MOTIF. FT CONFLICT 149 149 G -> A (IN REF. 1). SQ SEQUENCE 312 AA; 34116 MW; 069479287438F456 CRC64; MSSSEIYRYY YKTSEDLQGF KTAAAEPYFN PMAAYNPGVT HYQFNGNTLA SSSNYLSANG FISFEQASSD GWISSSPASH RSESPEYVDL NTMYNGGCNN MAQNQQYGMI MEQSVVSTAP AIPVASPPAV EVMGSSNVGT CKTIPASAGP KPKRSYTKKN QPSTTATSTP TAAAESSASV NLYTEEFQNF DFDNSALFDD SVEDDEDLML FSGGEDFDGN DGSFDLADGE NQDAAAGGSG KKRRGKQITP VVKRKRRLAA NARERRRMQN LNQAFDRLRQ YLPCLGNDRQ LSKHETLQMA QTYISALGDL LR // ID ATP6_DROME STANDARD; PRT; 224 AA. AC P00850; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE ATP synthase A chain (EC 3.6.3.14) (Protein 6). GN ATP6 OR ATPASE6. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83245048; PubMed=6408489; RA de Bruijn M.H.L.; RT "Drosophila melanogaster mitochondrial DNA, a novel organization and RT genetic code."; RL Nature 304:234-241(1983). CC -!- FUNCTION: KEY COMPONENT OF THE PROTON CHANNEL; IT MAY PLAY A CC DIRECT ROLE IN THE TRANSLOCATION OF PROTONS ACROSS THE MEMBRANE. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(1) HAS FIVE CC SUBUNITS: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), EPSILON(1). CF(0) CC HAS THREE MAIN SUBUNITS: A, B AND C. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ATPASE A CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01404; AAB59242.1; -. DR EMBL; U37541; AAC47815.1; -. DR PIR; A01053; PWFF6. DR FlyBase; FBgn0013672; mt:ATPase6. DR InterPro; IPR000568; ATPsynt_Asub. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. SQ SEQUENCE 224 AA; 25227 MW; 54DB86B5953B91DD CRC64; MMTNLFSVFD PLAIFNFSLN WLSTFLGLLM IPSIYWLMPS RYNIMWNSIL LTLHKEFKTL LGPSGHNGST FIFISLFSLI LFNNFMGLFP YIFTSTSHLT LTLSLALPLW LCFMLYGWIN HTQHMFAHLV PQGTPAILMP FMVCIETISN IIRPGTLAVR LTANMIAGHL LLTLLGNTGS SMSYMLMTFL LMAQIALLVL ESAVAMIQSY VFAVLSTLYS SEVN // ID ATP8_DROME STANDARD; PRT; 53 AA. AC P03932; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ATP synthase protein 8 (EC 3.6.3.14) (ATPase subunit 8) (A6L). GN MT:ATPASE8 OR MTATP8 OR ATP8 OR ATPASE8. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83245048; PubMed=6408489; RA de Bruijn M.H.L.; RT "Drosophila melanogaster mitochondrial DNA, a novel organization and RT genetic code."; RL Nature 304:234-241(1983). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Zimbabwe 53; RX MEDLINE=20363871; PubMed=10903372; RA Ballard J.W.O.; RT "Comparative genomics of mitochondrial DNA in members of the RT Drosophila melanogaster subgroup."; RL J. Mol. Evol. 51:48-63(2000). CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT CC (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- SIMILARITY: BELONGS TO THE ATPASE PROTEIN 8 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01404; AAB59241.1; -. DR EMBL; U37541; AAC47814.1; -. DR EMBL; AF200828; AAF77229.1; -. DR EMBL; AF200829; AAF77241.1; -. DR PIR; A01066; PWFF8. DR FlyBase; FBgn0013673; mt:ATPase8. DR InterPro; IPR001421; ATPase8_mit. DR Pfam; PF00895; ATP-synt_8; 1. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. SQ SEQUENCE 53 AA; 6364 MW; 45D2C68AA437FC23 CRC64; MPQMAPISWL LLFIIFSITF ILFCSINYYS YMPNSPKSNE LKNINLNSMN WKW // ID ATPA_DROME STANDARD; PRT; 552 AA. AC P35381; Q94512; Q9W1Z7; DT 01-JUN-1994 (Rel. 29, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ATP synthase alpha chain, mitochondrial precursor (EC 3.6.3.14) DE (Protein bellwether). GN BLW OR ATPSYN-ALPHA OR CG3612. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Testis; RX MEDLINE=98200891; PubMed=9540069; RA Talamillo A., Chisholm A.A.K., Garesse R., Jacobs H.T.; RT "Expression of the nuclear gene encoding mitochondrial ATP synthase RT subunit alpha in early development of Drosophila and sea urchin."; RL Mol. Biol. Rep. 25:87-94(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 472-491 FROM N.A. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- FUNCTION: PRODUCES ATP FROM ADP IN THE PRESENCE OF A PROTON CC GRADIENT ACROSS THE MEMBRANE. THE ALPHA CHAIN IS A REGULATORY CC SUBUNIT. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(1) HAS FIVE CC SUBUNITS: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), EPSILON(1). CF(0) CC HAS THREE MAIN SUBUNITS: A, B AND C. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE ATPASE ALPHA/BETA CHAINS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y07894; CAA69202.1; -. DR EMBL; AE003458; AAF46903.1; -. DR HSSP; P19483; 1BMF. DR FlyBase; FBgn0011211; blw. DR InterPro; IPR005294; ATP_synthF1_alph. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR000790; ATPase_a_C. DR InterPro; IPR009005; F1_ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR ProDom; PD001099; ATPase_aC; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; CF(1); Hydrogen ion transport; KW Hydrolase; ATP-binding; Mitochondrion; Transit peptide. FT TRANSIT 1 47 MITOCHONDRION (POTENTIAL). FT CHAIN 48 552 ATP SYNTHASE ALPHA CHAIN. FT NP_BIND 211 218 ATP (POTENTIAL). FT ACT_SITE 412 412 BY SIMILARITY. SQ SEQUENCE 552 AA; 59421 MW; 68DB3E77A4726FEA CRC64; MSIFSARLAS SVARNLPKAA NQVACKAAYP AASLAARKLH VASTQRSAEI SNILEERILG VAPKADLEET GRVLSIGDGI ARVYGLNNIQ ADEMVEFSSG LKGMALNLEP DNVGVVVFGN DKLIKQGDIV KRTGAIVDVP VGDELLGRVV DALGNAIDGK GAINTKDRFR VGIKAPGIIP RVSVREPMQT GIKAVDSLVP IGRGQRELII GDRQTGKTAL AIDTIINQKR FNEAQDESKK LYCIYVAIGQ KRSTVAQIVK RLTDSGAMGY SVIVSATASD AAPLQYLAPY SGCAMGEYFR DKGKHALIIY DDLSKQAVAY RQMSLLLRRP PGREAYPGDV FYLHSRLLER AAKMSPAMGG GSLTALPVIE TQAGDVSAYI PTNVISITDG QIFLETELFY KGIRPAINVG LSVSRVGSAA QTKAMKQVAG SMKLELAQYR EVAAFAQFGS DLDAATQQLL NRGVRLTELL KQGQYVPMAI EDQVAVIYCG VRGHLDKMDP AKITKFEKEF LQHIKTSEQA LLDTIAKDGA ISEASDAKLK DIVAKFMSTF QG // ID ATPB_DROME STANDARD; PRT; 505 AA. AC Q05825; DT 01-FEB-1994 (Rel. 28, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE ATP synthase beta chain, mitochondrial precursor (EC 3.6.3.14). GN ATPSYN-BETA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93384603; PubMed=8373413; RA Pena P., Garesse R.; RT "The beta subunit of the Drosophila melanogaster ATP synthase: cDNA RT cloning, amino acid analysis and identification of the protein in RT adult flies."; RL Biochem. Biophys. Res. Commun. 195:785-791(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). CC -!- FUNCTION: PRODUCES ATP FROM ADP IN THE PRESENCE OF A PROTON CC GRADIENT ACROSS THE MEMBRANE. THE BETA CHAIN IS THE CATALYTIC CC SUBUNIT. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(1) HAS FIVE CC SUBUNITS: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), EPSILON(1). CF(0) CC HAS THREE MAIN SUBUNITS: A, B AND C. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE ATPASE ALPHA/BETA CHAINS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X71013; CAA50332.1; ALT_INIT. DR PIR; JN0760; JN0760. DR HSSP; P00829; 1BMF. DR FlyBase; FBgn0010217; ATPsyn-beta. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR005722; ATP_synthF1_beta. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR009005; F1_ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; CF(1); Hydrogen ion transport; KW Hydrolase; ATP-binding; Mitochondrion; Transit peptide. FT TRANSIT 1 31 MITOCHONDRION (POTENTIAL). FT CHAIN 32 505 ATP SYNTHASE BETA CHAIN. FT NP_BIND 183 190 ATP (BY SIMILARITY). SQ SEQUENCE 505 AA; 54139 MW; 92FA3E7AF1F919A2 CRC64; MFALRAASKA DKNLLPFLGQ LSRSHAAKAA KAAAAANGKI VAVIGAVVDV QFDDNLPPIL NALEVDNRSP RLVLEVAQHL GENTVRTIAM DGTEGLVRGQ KVLDTGYPIR IPVGAETLGR IINVIGEPID ERGPIDTDKT AAIHAEAPEF VQMSVEQEIL VTGIKVVDLL APYAKGGKIG LFGGAGVGKT VLIMELINNV AKAHGGYSVF AGVGERTREG NDLYNEMIEG GVISLKDKTS KVALVYGQMN EPPGARARVA LTGLTVAEYF RDQEGQDVLL FIDNIFRFTQ AGSEVSALLG RIPSAVGYQP TLATDMGSMQ ERITTTKKGS ITSVQAIYVP ADDLTDPAPA TTFAHLDATT VLSRAIAELG IYPAVDPLDS TSRIMDPNII GQEHYNVARG VQKILQDYKS LQDIIAILGM DELSEEDKLT VARARKIQRF LSQPFQVAEV FTGHAGKLVP LEQTIKGFSA ILAGDYDHLP EVAFYMVGPI EEVCRKADRL AKEAA // ID ATPF_DROME STANDARD; PRT; 243 AA. AC Q94516; Q9VT43; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ATP synthase B chain, mitochondrial precursor (EC 3.6.3.14) (FO-ATP DE synthase subunit B). GN ATPSYN-BETA OR ATPSYN-B OR CG11154. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 60-243 FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(1) HAS FIVE CC SUBUNITS: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), EPSILON(1). CF(0) CC HAS THREE MAIN SUBUNITS: A, B AND C. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003551; AAF50212.1; -. DR EMBL; Y08967; CAA70164.1; -. DR FlyBase; FBgn0019644; ATPsyn-b. DR InterPro; IPR008688; Mt_ATP-synth_B. DR Pfam; PF05405; Mt_ATP-synt_B; 1. KW Hydrogen ion transport; CF(0); Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 243 ATP SYNTHASE B CHAIN. FT CONFLICT 184 186 KRR -> NRP (IN REF. 2). SQ SEQUENCE 243 AA; 27357 MW; 683F66EB4CF1F150 CRC64; MFSRAALLTA QRPLTVAATR SAAAAAAPGG AIERRQRPEH PGKVRLGFLP EEWFQFFYNK TGVTGPYTFG VGLITYLCSK EIYVMEHEYY SGLSLGIMAI IAVKKLGPVI AKWADGEIDK IESEWKEGRE AELKVLSDAI EAEKKEQWRA DGALLLMEAK KENIALQLEA AFRERAMNVY SEVKRRLDYQ VECRHVERRL SQKHMVNWIT TNVLASISPQ QEKETLNKCI ADLSALALRV KSA // ID ATPG_DROME STANDARD; PRT; 297 AA. AC O01666; Q9VAH8; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ATP synthase gamma chain, mitochondrial precursor (EC 3.6.3.14). GN ATPSYN-GAMMA OR CG7610. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-169 FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). CC -!- FUNCTION: PRODUCES ATP FROM ADP IN THE PRESENCE OF A PROTON CC GRADIENT ACROSS THE MEMBRANE. THE GAMMA CHAIN IS BELIEVED TO BE CC IMPORTANT IN REGULATING ATPASE ACTIVITY AND THE FLOW OF PROTONS CC THROUGH THE CF(0) COMPLEX. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(1) HAS FIVE CC SUBUNITS: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), EPSILON(1). CF(0) CC HAS THREE MAIN SUBUNITS: A, B AND C. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE ATPASE GAMMA CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003771; AAF56932.1; -. DR EMBL; Y12701; CAA73233.1; -. DR FlyBase; FBgn0020235; ATPsyn-gamma. DR InterPro; IPR000131; ATPase_gamma. DR Pfam; PF00231; ATP-synt; 1. DR PRINTS; PR00126; ATPASEGAMMA. DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1. DR PROSITE; PS00153; ATPASE_GAMMA; 1. KW ATP synthesis; CF(1); Hydrogen ion transport; Hydrolase; KW Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 297 ATP SYNTHASE GAMMA CHAIN. SQ SEQUENCE 297 AA; 32871 MW; B648B8D614E01FCE CRC64; MMMQRTQLLL PLAMEATMLA QQQRGMATLK MISIRLKSVK NIQKITQSMK MVSAAKYARA ERDLKAARPY GIGAQQFFEK TEIQPDEKAE PKKLLIAVTS DRGLCGAVHT GVARLIRGEL AQDEANTKVF CVGDKSRAIL SRLYGKNILM VANEVGRLPP TFLDASKIAN EVLQTGYDYT EGKIVYNRFK SVVSYQCSTL PIFSGSTVEK SEKLAVYDSL DSDVVKSYLE FSLASLIFYT MKEGACSEQS SRMTAMDNAS KNAGEMIDKL TLTFNRTRQA VITRELIEII SGAAALT // ID ATPO_DROME STANDARD; PRT; 209 AA. AC Q24439; Q9VFA4; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ATP synthase oligomycin sensitivity conferral protein, mitochondrial DE precursor (EC 3.6.3.14) (OSCP). GN OSCP OR CG4307. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS PROTEIN SEEMS TO BE PART OF THE STALK THAT LINKS CC CF(0) TO CF(1). IT EITHER TRANSMITS CONFORMATIONAL CHANGES FROM CC CF(0) INTO CF(1) OR IS IMPLICATED IN PROTON CONDUCTION. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(1) HAS FIVE CC SUBUNITS: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), EPSILON(1). CF(0) CC HAS THREE MAIN SUBUNITS: A, B AND C. CC -!- SIMILARITY: BELONGS TO THE ATPASE DELTA CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99666; CAA67980.1; -. DR EMBL; AE003708; AAF55156.1; -. DR EMBL; AY058261; AAL13490.1; -. DR FlyBase; FBgn0016691; Oscp. DR InterPro; IPR000711; ATPsynt_OSCP. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1. DR PROSITE; PS00389; ATPASE_DELTA; FALSE_NEG. KW Hydrolase; ATP synthesis; CF(1); Hydrogen ion transport; KW Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 209 ATP SYNTHASE OLIGOMYCIN SENSITIVITY FT CONFERRAL PROTEIN. FT CONFLICT 191 191 D -> N (IN REF. 1). SQ SEQUENCE 209 AA; 22422 MW; 50040CE844DFCAB2 CRC64; MASINKLALL SRTLSSAAAQ ATVKPPVQVF GLEGRYATAL YSAASKLSQL DQVEKDLTAL QATIRSDKKL REYVTSPIIN KKVMATALKE ASEKLRFAPA TVNLLGLLAD NGRLKKLDTV INAYKTIMAA HRGEVVCEVV TAKPLDASQS KQLEGALKSF LKGNESLKIT SRVDPSIIGG LIVSIGDKYV DMSIATKVKL YTDVIQTAA // ID ATPQ_DROME STANDARD; PRT; 178 AA. AC Q24251; Q9VE03; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ATP synthase D chain, mitochondrial (EC 3.6.3.14). GN ATPSYN-D OR CG6030. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT CC (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. IT HAS NO CC APPARENT BACTERIAL HOMOLOG AND ITS EXACT FUNCTION IS UNKNOWN. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(0) SEEMS TO CC HAVE NINE SUBUNITS: A, B, C, D, E, F, G, F6 AND 8 (OR A6L). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99667; CAA67981.1; -. DR EMBL; AE003725; AAF55633.1; -. DR FlyBase; FBgn0016120; ATPsyn-d. DR InterPro; IPR008689; Mt_ATP-synth_D. DR Pfam; PF05873; Mt_ATP-synt_D; 1. KW Hydrogen ion transport; CF(0); Mitochondrion. FT CONFLICT 99 99 S -> N (IN REF. 1). SQ SEQUENCE 178 AA; 20201 MW; 3671667150BE02A3 CRC64; MAARRIAQSS INWSALAERV PANQKSSFGA FKTKSDIYVR AVLANPECPP QIDWANYKKL VPVAGLVDSF QKQYEALKVP YPQDKVSSQV DAEIKASQSE IDAYKKASEQ RIQNYQKEIA HLKSLLPYDQ MTMEDYRDAF PDSALDPLNK PTFWPHTPEE QVGYKSKEQL EAEAQGHH // ID ATPR_DROME STANDARD; PRT; 106 AA. AC Q24407; Q9VCN0; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ATP synthase coupling factor 6, mitochondrial precursor (EC 3.6.3.14) DE (F6). GN ATPSYN-CF6 OR CG4412. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC CC COMPONENT (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. CC F6 SEEMS TO BE PART OF THE STALK THAT LINKS CF(0) TO CF(1). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(0) SEEMS TO CC HAVE NINE SUBUNITS: A, B, C, D, E, F, G, F6 AND 8 (OR A6L). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99665; CAA67979.1; -. DR EMBL; AE003743; AAF56127.1; -. DR FlyBase; FBgn0016119; ATPsyn-Cf6. DR InterPro; IPR008387; ATP_synth_F6. DR Pfam; PF05511; ATP-synt_F6; 1. KW Hydrogen ion transport; CF(0); Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 106 ATP SYNTHASE COUPLING FACTOR 6. SQ SEQUENCE 106 AA; 11936 MW; 08E1B074EB34E94B CRC64; MLSQSLLSGM RVLRTEARRN FGIVAPALNK ASDPIQQLFL DKVREYKQKS AGGKLVDSNP DIERELKTEL DRVAKQFGSD GKTDMLKFPE FQFPDVKVDP ITQAPQ // ID ATRX_DROME STANDARD; PRT; 1311 AA. AC Q9GQN5; Q9VBQ8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcriptional regulator ATRX homolog (X-linked nuclear protein) DE (dXNP) (d-xnp). GN XNP OR CG4548. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Cardoso C., Usseglio F., Villard L., Manfruelli P., Rothbacher U., RA Aragnol D., Pradel J., Fontes M.; RT "d-xnp: Drosophila melanogaster xnp/atr-x gene."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COULD BE A GLOBAL TRANSCRIPTIONAL REGULATOR. MODIFIES CC GENE EXPRESSION BY AFFECTING CHROMATIN (POTENTIAL). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE SNF2/RAD54 HELICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF217802; AAG40586.1; -. DR EMBL; AE003752; AAF56471.1; -. DR EMBL; AY058592; AAL13821.1; -. DR FlyBase; FBgn0039338; XNP. DR InterPro; IPR001410; DEAD. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR000330; SNF2_N. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00176; SNF2_N; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. KW DNA repair; Nuclear protein; DNA-binding; Helicase; ATP-binding. FT NP_BIND 489 496 ATP (POTENTIAL). FT SITE 615 618 DEGH BOX. FT DOMAIN 69 74 POLY-SER. FT DOMAIN 162 165 POLY-GLU. FT DOMAIN 301 307 POLY-GLU. FT CONFLICT 785 785 N -> T (IN REF. 1). SQ SEQUENCE 1311 AA; 148218 MW; 71B78942468D4A6B CRC64; MGKKNPNARH TDAATPLTTD DSNSSSVSRR ESATESKSAS ESESSPPRSN TKQSRTHKNV KASGKATVSS SSDSDQAVAN SSANDEEKEP VCKIRIVPLE KLLASPKTKE RPSRGSQQKN VTINDSSDEE PLKGSKLVLP ARKSRNKNAS IIELSDSEEV DEEEESLLVA IPLPKEAQQT KPEKNSSKAS KESIEKRQKA QKEATTSSAR AIRSVNGTRR GSLSSERSSR ASSSRAESPP RPKRCVVRLK RVSLPKTKPA QKPKKMSSDS EEAATTSKKS RQRRSKSESE ADSDYEAPAA EEEEEEERKS SGDEEEAANS SDSEVMPQRK RRRKKSESDK GSSDFEPEEK QKKKGRKRIK KTSSGESDGD GDDDKQKNKR KHIRKIIKTK DLDLTTKEAA KEEDDRRKRI EDRQKLYNRI FVKSESVEIN ELVLDFDEES KKALLQVDKG LLKKLKPHQV AGVKFMWDAC FETLKESQEK PGSGCILAHC MGLGKTLQVV TLSHTLLVNT RRTGVDRVLI ISPLSTVNNW AREFTSWMKF ANRNDIEVYD ISRYKDKPTR IFKLNEWFNE GGVCILGYDM YRILANEKAK GLRKKQREQL MQALVDPGPD LVVCDEGHLL KNEKTSISKA VTRMRTKRRI VLTGTPLQNN LREYYCMIQF VKPNLLGTYK EYMNRFVNPI TNGQYTDSTE RDLRLMKHRS HILHKLLEGC IQRRDYSVLA PYLPPKHEYV VYTTLSELQQ KLYGYYMTTH REQSGGDVVG KGARLFQDFQ DLRRIWTHPM NLRVNSDNVI AKRLLSNDDS DMEGFICDET DEDEAASNSS DSCETFKSDA SMSGLAASSG KVKKRKTRNG NAGGGDSDSD LEMLGGLGGG SSVQKDDPSE WWKPFVEERE LNNVHHSPKL LILLRLLQQC EAIGDKLLVF SQSLQSLDVI EHFLSLVDSN TKNYEFEGDV GDFKGCWTSG KDYFRLDGSC SVEQREAMCK QFNNITNLRA RLFLISTRAG GLGINLVAAN RVVIFDVSWN PSHDTQSIFR VYRFGQIKPC YIYRLIAMGT MEQKVYERQV AKQATAKRVI DEQQISRHYN QTDLMELYSY ELKPSTEREM PILPKDRLFA EILTEHEKLI FKYHEHDSLL EQEEHENLTE EERKSAWAEY EAEKTRTVQA SQYMSYDRNA FGNQVMGQFG NASGSVTSNK IFGFRSDILL QLLNMKISKD HQELNQNQVI QLVPTYLQQL YNEMNNGDPT MYKDLLNLHS NIVHPSGMYM NPLLYANQNP NAAGYNQGTG GVPPMAGGSV AHGPPAAPAP GFEPDKVYEI D // ID ATTA_DROME STANDARD; PRT; 224 AA. AC P45884; Q9V750; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Attacin A precursor. GN ATTA OR CG10146. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95261391; PubMed=7742836; RA Aasling B., Dushay M.S., Hultmark D.; RT "Identification of early genes in the Drosophila immune response by RT PCR-based differential display: the Attacin A gene and the evolution RT of attacin-like proteins."; RL Insect Biochem. Mol. Biol. 25:511-518(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=20231730; PubMed=10767526; RA Dushay M.S., Roethele J.B., Chaverri J.M., Dulek D.E., Syed S.K., RA Kitami T., Eldon E.D.; RT "Two attacin antibacterial genes of Drosophila melanogaster."; RL Gene 246:49-57(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: HEMOLYMPH ANTIBACTERIAL PROTEIN. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: SOME TO DIPTERICINS, AND TO SARCOTOXINS II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z46893; CAA86995.1; -. DR EMBL; AF220544; AAF70455.1; -. DR EMBL; AE003813; AAF58215.1; -. DR FlyBase; FBgn0012042; AttA. DR GO; GO:0008225; F:Gram-negative antibacterial peptide activity; IEP. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IEP. DR InterPro; IPR005521; Attacin_C. DR InterPro; IPR005520; Attacin_N. DR Pfam; PF03769; Attacin_C; 1. DR Pfam; PF03768; Attacin_N; 1. KW Insect immunity; Antibiotic; Hemolymph; Multigene family; Signal. FT SIGNAL 1 20 POTENTIAL. FT PROPEP 21 34 POTENTIAL. FT CHAIN 35 224 ATTACIN A. FT CONFLICT 3 3 K -> N (IN REF. 3). FT CONFLICT 22 24 MISSING (IN REF. 3). SQ SEQUENCE 224 AA; 23239 MW; 6B1965557847BBBA CRC64; MQKTSILIVA LVALFAITEA LPSLPTTGPI RVRRQVLGGS LTSNPAGGAD ARLDLTKGIG NPNHNVVGQV FAAGNTQSGP VTTGGTLAYN NAGHGASLTK THTPGVKDVF QQEAHANLFN NGRHNLDAKV FASQNKLANG FEFQRNGAGL DYSHINGHGA SLTHSNFPGI GQQLGLDGRA NLWSSPNRAT TLDLTGSASK WTSGPFANQK PNFGAGLGLS HHFG // ID ATTB_DROME STANDARD; PRT; 218 AA. AC Q9V751; Q95NV4; Q95U95; Q95U96; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Attacin B precursor. GN ATTB OR ATTB1 OR CG18372. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20231730; PubMed=10767526; RA Dushay M.S., Roethele J.B., Chaverri J.M., Dulek D.E., Syed S.K., RA Kitami T., Eldon E.D.; RT "Two attacin antibacterial genes of Drosophila melanogaster."; RL Gene 246:49-57(2000). RN [2] RP SEQUENCE FROM N.A., AND VARIANTS. RC STRAIN=2CPA-1, 2CPA-7, 2CPA-12, 2CPA-14, 2CPA-43, 2CPA-46, 2CPA-51, RC 2CPA-103, 2CPA-105, 2CPA-118, 2CPA-122, and 2CPA-129; RX MEDLINE=21518597; PubMed=11606542; RA Lazzaro B.P., Clark A.G.; RT "Evidence for recurrent paralogous gene conversion and exceptional RT allelic divergence in the Attacin genes of Drosophila melanogaster."; RL Genetics 159:659-671(2001). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: HEMOLYMPH ANTIBACTERIAL PROTEIN. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: SOME TO DIPTERICINS, AND TO SARCOTOXINS II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF220546; AAF71234.1; -. DR EMBL; AY056867; AAL23652.1; -. DR EMBL; AY056868; AAL23653.1; -. DR EMBL; AY056869; AAL23654.1; -. DR EMBL; AY056870; AAL23655.1; -. DR EMBL; AY056871; AAL23656.1; -. DR EMBL; AY056872; AAL23657.1; -. DR EMBL; AY056873; AAL23658.1; -. DR EMBL; AY056874; AAL23659.1; -. DR EMBL; AY056875; AAL23660.1; -. DR EMBL; AY056876; AAL23661.1; -. DR EMBL; AY056877; AAL23662.1; -. DR EMBL; AY056878; AAL23663.1; -. DR EMBL; AE003813; AAF58214.1; -. DR FlyBase; FBgn0041581; AttB. DR GO; GO:0005576; C:extracellular; TAS. DR GO; GO:0003797; F:antibacterial peptide activity; IEP. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IEP. DR InterPro; IPR005521; Attacin_C. DR InterPro; IPR005520; Attacin_N. DR Pfam; PF03769; Attacin_C; 1. DR Pfam; PF03768; Attacin_N; 1. KW Insect immunity; Antibiotic; Hemolymph; Multigene family; Signal; KW Polymorphism. FT SIGNAL 1 17 POTENTIAL. FT PROPEP 18 28 POTENTIAL. FT CHAIN 29 218 ATTACIN B. FT VARIANT 108 108 A -> D (IN STRAIN 2CPA-7). FT VARIANT 138 138 Q -> P (IN STRAIN 2CPA-122). FT CONFLICT 154 154 A -> G (IN REF. 3). SQ SEQUENCE 218 AA; 22583 MW; 3FA9B53E0C739BCA CRC64; MQKTSILILA LFAIAEAVPT TGPIRVRRQV LGGSLASNPA GGADARLNLS KGIGNPNHNV VGQVFAAGNT QSGPVTTGGT LAYNNAGHGA SLTKTHTPGV KDVFQQEAHA NLFNNGRHNL DAKVFASQNK LANGFEFQRN GAGLDYSHIN GHGASLTHSN FPGIGQQLGL DGRANLWSSP NRATTLDLTG SASKWTSGPF ANQKPNFGAG LGLSHHFG // ID ATU_DROME STANDARD; PRT; 725 AA. AC Q94546; Q9VNE6; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Another transcription unit protein. GN ATU OR CG1433. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Eye-antennal disk; RX MEDLINE=98133889; PubMed=9475742; RA Frolov M.V., Benevolenskaya E.V., Birchler J.A.; RT "Regena (Rga), a Drosophila homolog of the global negative RT transcriptional regulator CDC36 (NOT2) from yeast, modifies gene RT expression and suppresses position effect variegation."; RL Genetics 148:317-329(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U75467; AAB18341.1; -. DR EMBL; AE003602; AAF51991.1; -. DR EMBL; AY075403; AAL68232.1; -. DR FlyBase; FBgn0019637; Atu. DR InterPro; IPR007149; Leo1. DR Pfam; PF04004; Leo1; 1. FT DOMAIN 10 356 ARG/SER-RICH (RS DOMAIN). FT DOMAIN 664 722 GLY/SER-RICH. FT CONFLICT 2 11 GSQNSDDDSG -> MGSQNSDDDS (IN REF. 1). FT CONFLICT 79 79 G -> A (IN REF. 1). FT CONFLICT 99 99 S -> T (IN REF. 1). FT CONFLICT 309 309 D -> G (IN REF. 1). FT CONFLICT 626 626 A -> R (IN REF. 1). SQ SEQUENCE 725 AA; 77421 MW; 16C8FE9EBB48861C CRC64; MGSQNSDDDS GSSGSSRSGS RSVTPQGGSA PGSQRSRRSG SGSDRSRSGS RSSRSRSGSG SPRSARSGSA ESRHSQLSGS ARSKRSRSAH SRRSGSARSR KSGTPESPQS HRSGSLQSRK SGSPQSRRSG SPQSRKSGST HSRRSGSAHS RRSGSARSRK SGSAQSDRSE SRSRSHSGSL KGNEESRSNS PNLQIDVERA NSKSGSRSRS RSRSGSRTSR SRSKTGTPSP NRSRSGSASG SGSDVGVPKK KARKASGSDQ EKKKSGSDSD IEESPTKAKK SRLIDTDSDS NQDVGKKAPA AADIFGDADD ISDDEDEAGP AARKSPVRSK SRSQSKSHSH SRSMSHSRSR SRSRSRDKVE SQVESAPKED EPEPLPETRI DVEIPRISAD LGKEQHFIKL PNFLSVVTHP FDPETYEDEI DEEETMDEEG RQRIKLKVSN TIRWREYMNN KGDMVRESNA RFVRWSDGSM SLHLGNEIFD AYRQPLLGDH NHLFVRQGTG LQGQSVFRTK LTFRPHSTES FTHKKMTMSL ADRSSKTSGI KILTQVGKDP TTDRPTQLRE EEAKLRQAMR NQHKSLPKKK KPGAGEPLIG GGTSSYQHDE GSDDENAISL SAIKNRYKKG SGAGQAEVKA STIYSSDEDE GSDFEARRSK KVDKAKASKA LRDSDSESDA GSAKSGHSNK SGGEGGSASG SENEGSQKSG GGSSKSASGS GSGSGSGSGS GSDND // ID AXN_DROME STANDARD; PRT; 745 AA. AC Q9V407; Q9XYC1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Axin (Axis inhibition protein) (dAxin) (d-Axin). GN AXN OR CG7926. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=99174088; PubMed=10073940; RA Hamada F., Tomoyasu Y., Takatsu Y., Nakamura M., Nagai S.-I., RA Suzuki A., Fujita F., Shibuya H., Toyoshima K., Ueno N., Akiyama T.; RT "Negative regulation of Wingless signaling by D-axin, a Drosophila RT homolog of axin."; RL Science 283:1739-1742(1999). RN [2] RP SEQUENCE FROM N.A. RA Ruel L., Anthopoulos N., Goncalves J., Manoukian A.S., Woodgett J.R.; RT "A Drosophila homolog of the axin gene is involved in the transduction RT of the wingless signal regulating the stability of the armadillo RT protein."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP FUNCTION. RX MEDLINE=99387984; PubMed=10457025; RA Willert K., Logan C.Y., Arora A., Fish M., Nusse R.; RT "A Drosophila Axin homolog, Daxin, inhibits Wnt signaling."; RL Development 126:4165-4173(1999). CC -!- FUNCTION: INHIBITOR OF THE WG SIGNALING PATHWAY. DOWN-REGULATES CC BETA-CATENIN (ARMADILLO=ARM). PROBABLY FACILITATE THE CC PHOSPHORYLATION OF BETA-CATENIN AND APC BY GSK-3B (ZESTE-WHITE CC 3=ZW3). CC -!- SUBUNIT: INTERACTS WITH ZW3 AND ARM. THE INTERACTION BETWEEN AXN CC AND ARM OCCURS VIA THE ARMADILLO REPEATS CONTAINED IN ARM. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: UBIQUITOUSLY EXPRESSED THROUGHOUT THE CC DEVELOPMENT. CC -!- SIMILARITY: CONTAINS 1 RGS DOMAIN. CC -!- SIMILARITY: CONTAINS 1 DIX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF086811; AAD24886.1; -. DR EMBL; AF091813; AAF21293.1; -. DR EMBL; AE003772; AAF56993.1; -. DR FlyBase; FBgn0026597; Axn. DR GO; GO:0007455; P:eye-antennal disc metamorphosis; IMP. DR GO; GO:0016055; P:Wnt receptor signaling pathway; IGI. DR InterPro; IPR001158; DIX. DR InterPro; IPR000342; Regl_Gprotein. DR Pfam; PF00778; DIX; 1. DR ProDom; PD003639; DIX; 1. DR ProDom; PD001580; Regl_Gprotein; 1. DR SMART; SM00315; RGS; 1. DR PROSITE; PS50841; DIX; 1. DR PROSITE; PS50132; RGS; 1. KW Developmental protein; Wnt signaling pathway. FT DOMAIN 54 172 RGS. FT DOMAIN 640 646 POLY-SER. FT DOMAIN 663 745 DIX. FT CONFLICT 454 454 R -> Q (IN REF. 1). FT CONFLICT 644 645 MISSING (IN REF. 1). SQ SEQUENCE 745 AA; 81718 MW; 31A502528CEE84BA CRC64; MSGHPSGIRK HDDNECSGPR PPVPGEESRV KKMTEGVADT SKNSSPSYLN WARTLNHLLE DRDGVELFKK YVEEEAPAYN DHLNFYFACE GLKQQTDPEK IKQIIGAIYR FLRKSQLSIS DDLRAQIKAI KTNPEIPLSP HIFDPMQRHV EVTIRDNIYP TFLCSEMYIL YIQQMSAQQE RCTSSGATGS GSAGSSGSGG SSLAGACALP PTTASGKQQL PQLVPPGAFI NLPVSSVSGP PAGTCSASGS VYGPSTSASS SGSISATDTL PRSSTLPTLH EDSVLSLCDD FEKVQMQEGG GSLGSGSVGA GARAPDYPIR LTRDLLIATQ KRRLEIRPPG AHGYVYNPST TNTSYVPNSR VDSERASVSS GGRTDSDTMS ISSCSMDGRP YIQRRHSSTE SKAIRQSAMA NKETNTFQVI PRTQRLHSNE HRPLKEEELV SLLIPKLEEV KRKRDLEERA RERNPGAALL TNERSSASDR AFAEAIREKF ALDEDNDQDI LDQHVSRVWK DQTPHRSPGT MSPCPPIPSR RRTATHDSGM VSDGAMSLSG HSMKHSKSMP DHSSCSRKLT NKWPSMNTDS GISMFSADTV TKYKDASSRS GSSTASKLEE AKRRLEDEPR RSRRYAQPPM QHLSQQPLAS FSSSSSGGSI SLPHQPPPLP AKPPETIVVF SFCEEPVPYR IKIPGTQPTL RQFKDYLPRR GHFRFFFKTH CEDPDSPVIQ EEIVNDSDIL PLFGDKAMGL VKPSD // ID B3GI_DROME STANDARD; PRT; 306 AA. AC O97422; Q8IRS6; Q95SR5; DT 16-OCT-2001 (Rel. 40, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase I DE (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase I) DE (Glucuronosyltransferase-I) (DmGlcAT-I) (UDP-GlcUA:Gal Beta-1,3-Gal-R DE glucuronyltransferase) (GlcUAT-I). GN GLCAT-I OR BCDNA:GH05057 OR EG:EG0007.5 OR CG32775. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, COFACTOR, AND DEVELOPMENTAL STAGE. RX MEDLINE=22513909; PubMed=12511570; RA Kim B.-T., Tsuchida K., Lincecum J., Kitagawa K., Bernfield M., RA Sugahara K.; RT "Identification and characterization of three Drosophila melanogaster RT glucuronyltransferases responsible for the synthesis of the conserved RT glycosaminoglycan-protein linkage region of proteoglycans: two novel RT homologs exhibit broad specificity toward oligosaccharides from RT proteoglycans, glycoproteins, and glycosphingolipids."; RL J. Biol. Chem. 278:9116-9124(2003). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN THE BIOSYNTHESIS OF L2/HNK-1 CARBOHYDRATE CC EPITOPE ON BOTH GLYCOLIPIDS AND GLYCOPROTEINS. SHOWS STRICT CC SPECIFICITY FOR GAL BETA1-3GAL BETA1-4XYL, EXHIBITING NEGLIGIBLE CC INCORPORATION INTO OTHER GALACTOSIDE SUBSTRATES. CC -!- CATALYTIC ACTIVITY: UDP-GLUCURONATE + 3-BETA-D-GALACTOSYL-4- CC BETA-D-GALACTOSYL-O-BETA-D-XYLOSYLPROTEIN = UDP + 3-BETA-D- CC GLUCURONOSYL-3-BETA-D-GALACTOSYL-4-BETA-D-GALACTOSYL-O-BETA-D- CC XYLOSYLPROTEIN. CC -!- COFACTOR: MANGANESE. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT LOW LEVELS FROM EARLY EMBRYOS TO CC ADULTS; MAXIMAL EXPRESSION IN THIRD INSTAR LARVAE. CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 43. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB080695; BAC65095.1; -. DR EMBL; AL033125; CAA21824.1; ALT_SEQ. DR EMBL; AE003430; AAN09117.1; -. DR EMBL; AY060634; AAL28182.1; -. DR HSSP; O94766; 1FGG. DR FlyBase; FBgn0066114; GlcAT-I. DR InterPro; IPR005027; Glyco_trans_43. DR Pfam; PF03360; Glyco_transf_43; 1. KW Transferase; Glycoprotein; Transmembrane; Signal-anchor; Golgi stack; KW Manganese; Multigene family. FT DOMAIN 1 11 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 12 29 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 30 306 LUMENAL (POTENTIAL). FT ACT_SITE 252 252 CATALYTIC BASE (BY SIMILARITY). FT METAL 163 163 MANGANESE (BY SIMILARITY). FT CARBOHYD 90 90 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 55 55 V -> L (IN REF. 1 AND 2). SQ SEQUENCE 306 AA; 35071 MW; 69910A46534218B0 CRC64; MSEVRIRPRQ VLILIIVFLV VLMMVHRNGK RTCQGPEYLQ AMFVQGDTLP TIYAVTPTYP RPAQKAELTR LSHLFMLLPH LHWIIVEDTN ATTPLVRNLL DRAGLEKRST LLNIKTPSEF KLKGKDPNWI KPRGVEQRNL ALAWLRNHVD VDRHSIVFFM DDDNSYSTEL FAEMSKIERG RVGVWPVGLV GGLMVERPLL TEDGTKVTGF NAAWRPERPF PIDMAAFAIS MDLFIRNPQA TFSYEVQRGY QESEILRHLT TRDQLQPLAN RCTDVLVWHT RTEKTKLAAE EALLKKGQRS DGGMEV // ID B3GP_DROME STANDARD; PRT; 479 AA. AC Q9VTG7; Q8MSC2; Q95RU4; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase P DE (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase P) DE (Glucuronosyltransferase-P) (GlcAT-P) (UDP-glucuronosyltransferase-P) DE (DmGlcAT-BSII). GN GLCAT-P OR GLCAT-BSII OR CG6207. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM C). RX MEDLINE=22513909; PubMed=12511570; RA Kim B.-T., Tsuchida K., Lincecum J., Kitagawa K., Bernfield M., RA Sugahara K.; RT "Identification and characterization of three Drosophila melanogaster RT glucuronyltransferases responsible for the synthesis of the conserved RT glycosaminoglycan-protein linkage region of proteoglycans: two novel RT homologs exhibit broad specificity toward oligosaccharides from RT proteoglycans, glycoproteins, and glycosphingolipids."; RL J. Biol. Chem. 278:9116-9124(2003). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS A AND C). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN THE BIOSYNTHESIS OF L2/HNK-1 CARBOHYDRATE CC EPITOPE ON BOTH GLYCOLIPIDS AND GLYCOPROTEINS. ENZYME HAS A BROAD CC SPECIFICITY. CC -!- CATALYTIC ACTIVITY: UDP-GLUCURONATE + 3-BETA-D-GALACTOSYL-4- CC BETA-D-GALACTOSYL-O-BETA-D-XYLOSYLPROTEIN = UDP + 3-BETA-D- CC GLUCURONOSYL-3-BETA-D-GALACTOSYL-4-BETA-D-GALACTOSYL-O-BETA-D- CC XYLOSYLPROTEIN. CC -!- COFACTOR: MANGANESE. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=B; CC IsoId=Q9VTG7-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q9VTG7-2; Sequence=VSP_050626; CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM EARLY EMBRYOS TO ADULTS; CC MAXIMAL EXPRESSION IN THIRD INSTAR LARVAE THROUGH TO ADULTHOOD. CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 43. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB080697; BAC65097.1; -. DR EMBL; AE003545; AAF50082.1; -. DR EMBL; AY061135; AAL28683.1; ALT_INIT. DR EMBL; AY118925; AAM50785.1; -. DR HSSP; O94766; 1FGG. DR FlyBase; FBgn0036144; GlcAT-P. DR InterPro; IPR005027; Glyco_trans_43. DR InterPro; IPR006162; Ppantne_S. DR Pfam; PF03360; Glyco_transf_43; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. KW Transferase; Glycoprotein; Transmembrane; KW Signal-anchor; Golgi stack; Manganese; KW Multigene family; Alternative splicing. FT DOMAIN 1 34 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 35 50 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 51 479 LUMENAL (POTENTIAL). FT ACT_SITE 418 418 CATALYTIC BASE (BY SIMILARITY). FT METAL 335 335 MANGANESE (BY SIMILARITY). FT CARBOHYD 90 90 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 97 97 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 98 98 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 271 271 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 460 460 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 68 230 Missing (in isoform C). FT /FTId=VSP_050626. SQ SEQUENCE 479 AA; 52556 MW; CA40D003D1303CB2 CRC64; MKGGNYTSLG TCSGINVSGN VAGTRKMSLG KSIKMYLTIF ILTTCIYMAL YQYHISREPF AASEVVKHQE KSSSYIASYL WSPISLLMAN SSSNTNNNST TTSTTTTTAP TTPTTTTTTT VGSVGQKLGA SSISSIRMVS LAATIPSFKS TLSESRSVSL GGHQKTATVK TSTTITTRTT ASGLATTKLS ATTRTTAKTS AKLSAATTPT ASHMENGYKT RPTFVAASLP PPLYIITPTY RRPEQLAELT RLGYTLKHVV NLLWLVIEDA NKTNPLVGHT LDRIGVPYEY MVAPMPEKYK QTKKAKPRGV SNRNRGLEYL REHATEGVLY FADDDNTYDI SIFEQMRYIS KVAMWPVGLV TKTGVSSPII QAGKLVGYYD GWIGGRKYPV DMAGFAVSVK FLKERPNAQM PFKPGYEEDG FLRSLAPLDD AEIELLADEC RDILTWHTQT KKNAPAQALN RTRYKNTNLE HIDRLLVRP // ID B3GS_DROME STANDARD; PRT; 409 AA. AC Q9VLA1; Q868Q3; Q8IPE6; Q95U07; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase S DE (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase S) DE (Glucuronosyltransferase-S) (GlcAT-S) (UDP-glucuronosyltransferase-S) DE (DmGlcAT-BSI). GN GLCAT-S OR GLCAT-BSI OR CG3881. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 22-409 FROM N.A. (ISOFORM B), FUNCTION, COFACTOR, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=22513909; PubMed=12511570; RA Kim B.-T., Tsuchida K., Lincecum J., Kitagawa K., Bernfield M., RA Sugahara K.; RT "Identification and characterization of three Drosophila melanogaster RT glucuronyltransferases responsible for the synthesis of the conserved RT glycosaminoglycan-protein linkage region of proteoglycans: two novel RT homologs exhibit broad specificity toward oligosaccharides from RT proteoglycans, glycoproteins, and glycosphingolipids."; RL J. Biol. Chem. 278:9116-9124(2003). CC -!- FUNCTION: INVOLVED IN THE BIOSYNTHESIS OF L2/HNK-1 CARBOHYDRATE CC EPITOPE ON BOTH GLYCOLIPIDS AND GLYCOPROTEINS. ENZYME HAS A BROAD CC SPECIFICITY. CC -!- CATALYTIC ACTIVITY: UDP-GLUCURONATE + 3-BETA-D-GALACTOSYL-4- CC BETA-D-GALACTOSYL-O-BETA-D-XYLOSYLPROTEIN = UDP + 3-BETA-D- CC GLUCURONOSYL-3-BETA-D-GALACTOSYL-4-BETA-D-GALACTOSYL-O-BETA-D- CC XYLOSYLPROTEIN. CC -!- COFACTOR: MANGANESE. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=b; CC IsoId=Q9VLA1-1; Sequence=Displayed; CC Name=a; CC IsoId=Q9VLA1-2; Sequence=VSP_050624, VSP_050625; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM EARLY EMBRYOS TO ADULTS; CC MAXIMAL EXPRESSION IN THIRD INSTAR LARVAE THROUGH TO ADULTHOOD. CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 43. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 27 AND 44. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003625; AAF52795.2; -. DR EMBL; AE003625; AAF52794.2; -. DR EMBL; AY058399; AAL13628.1; -. DR EMBL; AB080696; BAC65096.1; ALT_FRAME. DR HSSP; O94766; 1FGG. DR FlyBase; FBgn0032135; GlcAT-S. DR InterPro; IPR005027; Glyco_trans_43. DR Pfam; PF03360; Glyco_transf_43; 1. KW Transferase; Glycoprotein; Transmembrane; KW Signal-anchor; Golgi stack; Manganese; KW Multigene family; Alternative splicing. FT DOMAIN 1 53 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 54 73 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 74 409 LUMENAL (POTENTIAL). FT ACT_SITE 318 318 CATALYTIC BASE (BY SIMILARITY). FT METAL 235 235 MANGANESE (BY SIMILARITY). FT CARBOHYD 102 102 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 223 223 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 338 338 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 82 Missing (in isoform a). FT /FTId=VSP_050624. FT VARSPLIC 83 93 EDSEEGSHHGL -> MNLFENENKVK (in isoform FT a). FT /FTId=VSP_050625. FT CONFLICT 23 23 P -> S (IN REF. 2). SQ SEQUENCE 409 AA; 46711 MW; D3CB9DBD5C666A3B CRC64; MSSARLLESQ TSDEDNEDIE RRPHQSHSRS CSNNTTPTHP PHPMVRKGGV ARRICLIGGA LFLLLVALCY LTLSGDTRLG GSEDSEEGSH HGLDSMNFRP LNETVHICSE SYEDRRQFMQ DKPQSDYVQL PVIYFVTPTY PRREQIPELT RLAHTLLHIP RLHWLVADDQ EKCNDYMDTL LYRFGMPFTH MVSPMPSKFR NEKPAPRGVA NRRAALQWIR QHNLTNGILY FGDDDNTYDL RLFSEIRKTQ RVSMFPVGLI ADYGVSGPVV RKGKVVAFLD SWVAGRRWPV DMAGFAVNLE YMAQYPYVNM PYKPGYEEDL FLRSIGLQMN LIEPRGNNCT EILVWHTQTK SKKLGMVRLE SKYLDDRSNL GALLHNLKLM GVTSTTESEG RNALISKNGR ENPHSKILS // ID BAB1_DROME STANDARD; PRT; 977 AA. AC Q9W0K7; Q23968; Q8MR78; Q9U1H7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bric-a-brac protein 1. GN BAB1 OR BAB OR CG9097/CG13910. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Larva, and Ovary; RX MEDLINE=21969340; PubMed=11973274; RA Couderc J.L.G., Godt D., Zollman S., Chen J., Li M., Tiong S., RA Cramton S.E., Sahut-Barnola I., Laski F.A.; RT "The bric a brac locus consists of two paralogous genes encoding RT BTB/POZ domain proteins and acts as a homeotic and morphogenetic RT regulator of imaginal development in Drosophila."; RL Development 129:2419-2433(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 99-225 FROM N.A. RX MEDLINE=95280944; PubMed=7760839; RA Chen W., Zollman S., Couderc J.L., Laski F.A.; RT "The BTB domain of bric a brac mediates dimerization in vitro."; RL Mol. Cell. Biol. 15:3424-3429(1995). CC -!- FUNCTION: PROBABLY ACTS AS A TRANSCRIPTIONAL REGULATOR. REQUIRED CC FOR THE SPECIFICATION OF THE TARSAL SEGMENT. ALSO INVOLVED IN CC ANTENNA DEVELOPMENT. CC -!- SUBUNIT: MAY FORM DIMERS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=Q9W0K7-1; Sequence=Displayed; CC Name=A; CC IsoId=Q9W0K7-2; Sequence=VSP_007015, VSP_007016; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: LEG IMAGINAL DISK AT THE CENTRAL REGION OF THE CC TARSUS AND IN EYE ANTENNA DISK AT THE BASAL CYLINDER. CC -!- MISCELLANEOUS: 'BRIC-A-BRAC' MEANS 'JUMBLE' IN FRENCH (REFERRING CC TO THE MUTANT OVARY PHENOTYPE). CC -!- SIMILARITY: CONTAINS 1 A.T HOOK DNA-BINDING REPEAT. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 1 HELIX-TURN-HELIX PSQ-TYPE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ252082; CAB64385.1; -. DR EMBL; AE003470; AAF47439.2; -. DR EMBL; AY122075; AAM52587.1; -. DR EMBL; U01333; AAA87052.1; -. DR FlyBase; FBgn0004870; bab1. DR InterPro; IPR000637; AT_hook. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007889; HTH_psq. DR Pfam; PF00651; BTB; 1. DR Pfam; PF05225; HTH_psq; 1. DR SMART; SM00225; BTB; 1. DR PROSITE; PS50097; BTB; 1. KW Nuclear protein; DNA-binding; Transcription regulation; KW Alternative splicing. FT DOMAIN 127 192 BTB. FT DNA_BIND 569 614 H-T-H MOTIF PSQ-TYPE. FT DNA_BIND 621 632 A.T HOOK. FT VARSPLIC 513 526 AKMMENSHAWMGAT -> VSSCGDFPLANVST (in FT isoform A). FT /FTId=VSP_007015. FT VARSPLIC 527 977 Missing (in isoform A). FT /FTId=VSP_007016. FT CONFLICT 66 66 K -> R (IN REF. 1). FT CONFLICT 188 189 IN -> VS (IN REF. 1). FT CONFLICT 221 221 A -> R (IN REF. 1 AND 5). FT CONFLICT 257 257 A -> G (IN REF. 1). FT CONFLICT 264 265 KL -> NV (IN REF. 1). FT CONFLICT 283 284 QQ -> HE (IN REF. 1). FT CONFLICT 362 362 D -> E (IN REF. 1). FT CONFLICT 444 444 R -> M (IN REF. 1). FT CONFLICT 763 763 N -> S (IN REF. 1). FT CONFLICT 846 846 Q -> QQQ (IN REF. 1). FT CONFLICT 862 862 A -> V (IN REF. 1). SQ SEQUENCE 977 AA; 103324 MW; A7676B72A43126C5 CRC64; MASAQAETNV GLASEQGPVA QRQRKGTGSG ADSPKSNRSS PTQQEEKRIK SEDRTSPTGG AKDEDKESQG HAVAGGGGSS PVSSPQGRSS SVASPSSSSQ QFCLRWNNYQ TNLTTIFDQL LQNECFVDVT LACDGRSMKA HKMVLSACSP YFQTLLAETP CQHPIVIMRD VNWSDLKAIV EFMYRGEINV SQDQIGPLLR IAEMLKVRGL ADVTHMEAAT AAAAAASSER MPSSPKESTS TSRTEHDRER EAEELLAFMQ PEKKLRTSDW DPAELRLSPL ERQQGRNVRK RRWPSADTIF NPPAPPSPLS SLIAAERMEL EQKERERQRD CSLMTPPPKP PMSSGSTVGA TRRLETAIHA LDMPSPAATP GPLSRSSRPH SQSPQQQQAQ QQGQLPLPLP LHPHHHASPA PHPSQTAGSA HHPASPAGDS RFPLGPAAAM AAARELSGLG PGPSAEPRLP PPPPHHHGGG GVGGGGVGGG GAGGVGSGGG SSLADDLEIK PGIAEMIREE ERAKMMENSH AWMGATGSTL AADSYQYQLQ SMWQKCWNTN QNLMHHMRFR ERGPLKSWRP ETMAEAIFSV LKEGLSLSQA ARKYDIPYPT FVLYANRVHN MLGPSIDGGP DLRPKGRGRP QRILLGIWPD EHIKGVIKTV VFRDTKDIKD ESLAAHMPPY GRHSPAFPLQ DLPLSYPGAS GALAGAPSSM ACPNGSGPQT GVGVAGEQHM SQETAAAVAA VAHNIRQQMQ MAAVPPGLFN LPPHPGVGGG VGNVPGAAGG RASISPALSS GSGPRHAPSP CGPAGLLPNL PPSMAVALHH QQQQQAAHHH MQQLHLQQQQ AHLHHHQQQQ QQQQQQHHQG GHQVAHKSGF GASSSSSASS SSMGQHHAPK AKSSPLRSET PRLHSPLGDL GLDMASYKRE FSPSRLFAED LAELVGASVS SSSSSAAAAT APPERSAGAA SAATGADAPS SSSSGGIKVE PITTTSE // ID BAB2_DROME STANDARD; PRT; 1067 AA. AC Q9W0K4; Q24001; Q9U1H3; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bric-a-brac protein 2. GN BAB2 OR BTBII OR CG9102/CG13911. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryo, and Ovary; RX MEDLINE=21969340; PubMed=11973274; RA Couderc J.L.G., Godt D., Zollman S., Chen J., Li M., Tiong S., RA Cramton S.E., Sahut-Barnola I., Laski F.A.; RT "The bric a brac locus consists of two paralogous genes encoding RT BTB/POZ domain proteins and acts as a homeotic and morphogenetic RT regulator of imaginal development in Drosophila."; RL Development 129:2419-2433(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 196-310 FROM N.A. RX MEDLINE=95024186; PubMed=7938017; RA Zollman S., Godt D., Prive G.G., Couderc J.L., Laski F.A.; RT "The BTB domain, found primarily in zinc finger proteins, defines an RT evolutionarily conserved family that includes several developmentally RT regulated genes in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10717-10721(1994). CC -!- FUNCTION: PROBABLY ACTS AS A TRANSCRIPTIONAL REGULATOR. REQUIRED CC FOR THE SPECIFICATION OF THE TARSAL SEGMENT. ALSO INVOLVED IN CC ANTENNA DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: LEG IMAGINAL DISK AT THE CENTRAL REGION OF THE CC TARSUS AND IN EYE ANTENNA DISK AT THE BASAL CYLINDER. CC -!- MISCELLANEOUS: 'BRIC-A-BRAC' MEANS 'JUMBLE' IN FRENCH (REFERING TO CC THE MUTANT OVARY PHENOTYPE). CC -!- SIMILARITY: CONTAINS 1 A.T HOOK DNA-BINDING REPEAT. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 1 HELIX-TURN-HELIX PSQ-TYPE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ252173; CAB64388.1; -. DR EMBL; AE003470; AAF47442.2; -. DR EMBL; U14399; AAA50834.1; -. DR FlyBase; FBgn0025525; bab2. DR InterPro; IPR000637; AT_hook. DR InterPro; IPR000210; BTB_POZ. DR Pfam; PF00651; BTB; 1. DR SMART; SM00225; BTB; 1. DR PROSITE; PS50097; BTB; 1. KW Nuclear protein; DNA-binding; Transcription regulation. FT DOMAIN 223 288 BTB. FT DNA_BIND 645 690 H-T-H MOTIF PSQ-TYPE. FT DNA_BIND 697 708 A.T HOOK. FT CONFLICT 858 858 A -> R (IN REF. 1). SQ SEQUENCE 1067 AA; 114661 MW; 7DBFC7681D507FC0 CRC64; MDMTKQIVDF EIKSELIGEI DQFEASDYTM APPEEPKMVE ESPQLGHLED QNRKYSPERE VEPTLQDPSE VVDQMQKDTE SVGEVKSPEK DVETELVKSK ASPMNDQALT PPPRPLTSSE VVGLRDPEHT ELRMCLEAKK SRSLPVSPQP QPNLKLAGSA LFEFGQRSSP VETKIKTNPE TKPPRRKIVP PSGEGQQFCL RWNNYQSNLT NVFDELLQSE SFVDVTLSCE GHSIKAHKMV LSACSPYFQA LFYDNPCQHP IIIMRDVSWS DLKALVEFMY KGEINVCQDQ INPLLKVAET LKIRGLAEVS AGRGEGGASA LPMSAFDDED EEEELASATA ILQQDGDADP DEEMKAKRPR LLPEGVLDLN QRQRKRSRDG SYATPSPSLQ GGESEISERG SSGTPGQSQS QPLAMTTSTI VRNPFASPNP QTLEGRNSAM NAVANQRKSP APTATGHSNG NSGAAMHSPP GGVAVQSALP PHMAAIVPPP PSAMHHHAQQ LAAQHQLAHS HAMASALAAA AAGAGAAGAG GAGSGSGSGA SAPTGGTGVA GSGAGAAVGS HHDDMEIKPE IAEMIREEER AKMIESGGHG GWMGAAAAAT GAASVAADSY QYQLQSMWQK CWNTNQQNLV QQLRFRERGP LKSWRPEAMA EAIFSVLKEG LSLSQAARKF DIPYPTFVLY ANRVHNMLGP SLDGGADPRP KARGRPQRIL LGMWPEELIR SVIKAVVFRD YREIKEDMSA HQYANGQGHG TYIGGGTTTN GYHSAAAAKL AAQNAALAPP DAGSPLSSMT ETLRRQILSQ QQQHQQHHQQ QAHHQQQPSH HQQQSPHAQS MNMYKSPAYL QRSEIEDQVS AAAAVAAAAA KHQQQQGERR GSENLPDLSA LGLMGLPGLN VMPSRGSGGG SGGAAPNSAA SYARELSRER ERDRERERER ELSRQYGSQS RGSSSGSGSA KSLTASQRPG AASPYSAAHY AKHQASAYNK RFLESLPAGI DLEAFANGLL QKSVNKSPRF EDFFPGPGQD MSELFANPDA SAAAAAAAYA PPGAIRESPL MKIKLEQQHA TELPHED // ID BAM_DROME STANDARD; PRT; 442 AA. AC P22745; Q9VBV0; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bag-of-marbles protein (BAM protein). GN BAM OR CG10422. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=FS(3)NEO61; TISSUE=Ovary; RX MEDLINE=91122627; PubMed=2279698; RA McKearin D.M., Spradling A.C.; RT "Bag-of-marbles: a Drosophila gene required to initiate both male and RT female gametogenesis."; RL Genes Dev. 4:2242-2251(1990). RN [2] RP REVISIONS TO 99-113. RA McKearin D.M.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED TO INITIATE BOTH MALE AND FEMALE GAMETOGENESIS. CC MAY REGULATE CYSTOBLAST CELL DIVISIONS. CC -!- TISSUE SPECIFICITY: IN CYSTOBLASTS AND/OR VERY EARLY CYSTOCYTES IN CC OVARY AND TESTIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56202; CAA39662.1; -. DR EMBL; AE003751; AAF56427.1; -. DR FlyBase; FBgn0000158; bam. DR GO; GO:0045169; C:fusome; IDA. DR GO; GO:0045170; C:spectrosome; IDA. DR GO; GO:0007282; P:cystoblast cell division; IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0045478; P:fusome organization and biogenesis; IMP. FT DOMAIN 402 434 GLU/SER/PRO/THR-RICH (PEST REGION). FT CONFLICT 239 239 A -> S (IN REF. 1). FT CONFLICT 439 439 R -> A (IN REF. 1). SQ SEQUENCE 442 AA; 50275 MW; D2FE2BCFC249F254 CRC64; MLNARDVCPE GNDDQQLDHN FKQMEEHLAL MVEGNENEDP RKATCEYEDT NEDGATCTSG VLSEIQENFG RLRLCDVTAP LLEFHGLDCL QQIQKRSRHF AFDGSPAKKS RSGGVLVTGP KQKQLQKENV WNRKSKGSAS ADNIEKLPIT IEKLHMIGLH GDCLEHNAVL RLMNLFRSLH DHLTADLGFS RQNSMPSDYL FDMPVKSTMP KSLNVRYQLQ VLCTKVERFL VQQRRTLEAN RHFDFEKYDE CDKLLKGFAS YLDNFKLLLK PKMRNRNGNS GSNADKFHTQ RMERLLIGLR DWIKAAHLSV HVFNWEMDLE HRYSGAMTES HKSLNERAIL LSGAELRAAE ARGISAEDLF IAQRYKLGGP IYCVLEQHEF LSALIANPET YFPPSVVAIC GPQKLGAVSM EQPSASEEEF EETEEVPSSP PRHTGRVPRF RS // ID BCL9_DROME STANDARD; PRT; 1469 AA. AC Q961D9; Q9V4D2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bcl-9 homolog (Legless protein). GN LGS OR BCL9 OR CG2041. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 6-1469 FROM N.A., AND MUTAGENESIS OF GLY-514; LEU-534 AND RP ILE-537. RX MEDLINE=21952490; PubMed=11955446; RA Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S., RA Murone M., Zuellig S., Basler K.; RT "Wnt/wingless signaling requires BCL9/legless-mediated recruitment of RT pygopus to the nuclear beta-catenin-TCF complex."; RL Cell 109:47-60(2002). CC -!- FUNCTION: INVOLVED IN SIGNAL TRANSDUCTION THROUGH THE WNT PATHWAY. CC -!- SUBUNIT: BINDS TO ARM AND PYGO. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003844; AAF59345.2; -. DR EMBL; AY051651; AAK93075.1; -. DR EMBL; AF457205; AAL91368.1; -. DR FlyBase; FBgn0039907; lgs. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0030528; F:transcription regulator activity; IPI. DR GO; GO:0030177; P:positive regulation of Wnt receptor signali...; IPI. DR GO; GO:0007367; P:segment polarity determination; IMP. KW Nuclear protein; Developmental protein; Segmentation polarity protein; KW Wnt signaling pathway. FT DOMAIN 511 555 ARM-BINDING. FT DOMAIN 1134 1173 ASN-RICH. FT DOMAIN 1340 1449 GLN-RICH. FT DOMAIN 1162 1169 POLY-ASN. FT MUTAGEN 514 514 G->E: IN ALLELE LGS-21L. FT MUTAGEN 534 534 L->F: IN ALLELE LGS-17E; SEGMENT POLARITY FT PHENOTYPE. FT MUTAGEN 537 537 I->K: IN ALLELE LGS-17P. SQ SEQUENCE 1469 AA; 153759 MW; 5672E01B7200ED08 CRC64; MLSTTMPRSP TQQQPQPNSD ASSTSASGSN PGAAIGNGDS AASRSSPKTL NSEPFSTLSP DQIKLTPEEG TEKSGLSTSD KAATGGAPGS GNNLPEGQTM LRQNSTSTIN SCLVASPQNS SEHSNSSNVS ATVGLTQMVD CDEQSKKNKC SVKDEEAEIS SNKAKGQAAG GGCETGSTSS LTVKEEPTDV LGSLVNMKKE ERENHSPTMS PVGFGSIGNA QDNSATPVKI ERISNDSTTE KKGSSLTMNN DEMSMEGCNQ LNPDFINESL NNPAISSILV SGVGPIPGIG VGAGTGNLLT ANANGISSGS SNCLDYMQQQ NHIFVFSTQL ANKGAESVLS GQFQTIIAYH CTQPATKSFL EDFFMKNPLK INKLQRHNSV GMPWIGMGQV GLTPPNPVAK ITQQQPHTKT VGLLKPQFNQ HENSKRSTVS APSNSFVDQS DPMGNETELM CWEGGSSNTS RSGQNSRNHV DSISTSSESQ AIKILEAAGV DLGQVTKGSD PGLTTENNIV SLQGVKVPDE NLTPQQRQHR EEQLAKIKKM NQFLFPENEN SVGANVSSQI TKIPGDLMMG MSGGGGGSII NPTMRQLHMP GNAKSELLSA TSSGLSEDVM HPGDVISDMG AVIGCNNNQK TSVQCGSGVG VVTGTTAAGV NVNMHCSSSG APNGNMMGSS TDMLASFGNT SCNVIGTAPD MSKEVLNQDS RTHSHQGGVA QMEWSKIQHQ FFEERLKGGK PRQVTGTVVP QQQTPSGSGG NSLNNQVRPL QGPPPPYHSI QRSASVPIAT QSPNPSSPNN LSLPSPRTTA AVMGLPTNSP SMDGTGSLSG SVPQANTSTV QAGTTTVLSA NKNCFQADTP SPSNQNRSRN TGSSSVLTHN LSSNPSTPLS HLSPKEFESF GQSSAGDNMK SRRPSPQGQR SPVNSLIEAN KDVRFAASSP GFNPHPHMQS NSNSALNAYK MGSTNIQMER QASAQGGSVQ FSRRSDNIPL NPNSGNRPPP NKMTQNFDPI SSLAQMSQQL TSCVSSMGSP AGTGGMTMMG GPGPSDINIE HGIISGLDGS GIDTINQNNC HSMNVVMNSM GPRMLNPKMC VAGGPNGPPG FNPNSPNGGL RENSIGSGCG SANSSNFQGV VPPGARMMGR MPVNFGSNFN PNIQVKASTP NTIQYMPVRA QNANNNNNNG ANNVRMPPSL EFLQRYANPQ MGAVGNGSPI CPPSASDGTP GMPGLMAGPG AGGMLMNSSG EQHQNKITNN PGASNGINFF QNCNQMSIVD EEGGLPGHDG SMNIGQPSMI RGMRPHAMRP NVMGARMPPV NRQIQFAQSS DGIDCVGDPS SFFTNASCNS AGPHMFGSAQ QANQPKTQHI KNIPSGMCQN QSGLAVAQGQ IQLHGQGHAQ GQSLIGPTNN NLMSTAGSVS ATNGVSGINF VGPSSTDLKY AQQYHSFQQQ LYATNTRSQQ QQHMHQQHQS NMITMPPNLS PNPTFFVNK // ID BCN_DROME STANDARD; PRT; 92 AA. AC O46098; Q9U5X3; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bcn92 protein. GN BCN92 OR BCDNA:RE57896 OR EG:87B1.6 OR CG3717. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 1-67 FROM N.A. RX MEDLINE=95220670; PubMed=7705632; RA Cirera S., Martin-Campos J.M., Segarra C., Aguade M.; RT "Molecular characterization of the breakpoints of an inversion fixed RT between Drosophila melanogaster and D. subobscura."; RL Genetics 139:321-326(1995). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003423; AAF45733.1; -. DR EMBL; Z98269; CAB10976.1; -. DR EMBL; AY071542; AAL49164.1; -. DR EMBL; Z46608; CAB56152.1; -. DR PIR; T13609; T13609. DR FlyBase; FBgn0013432; bcn92. DR InterPro; IPR008011; Complex1_LYR. DR Pfam; PF05347; Complex1_LYR; 1. KW Coiled coil. FT DOMAIN 48 68 COILED COIL (POTENTIAL). SQ SEQUENCE 92 AA; 10961 MW; 95EBE6BE1B3AE820 CRC64; MSTRRQAITL YRNLLRESEK LPSYNFRMYA ARKIRDTFRA NRSTRDFAEI DRQMAEGQQN LELIRRQVII GHLYSADKLV IENKKTLKPS DD // ID BGB_DROME STANDARD; PRT; 184 AA. AC Q24040; Q9W0B9; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Big brother protein. GN BGB OR CG7959. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96182097; PubMed=8622696; RA Golling G., Li L., Pepling M., Stebbins M., Gergen J.P.; RT "Drosophila homologs of the proto-oncogene product PEBP2/CBF beta RT regulate the DNA-binding properties of Runt."; RL Mol. Cell. Biol. 16:932-942(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REGULATES THE DNA-BINDING PROPERTIES OF RUNT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CBF-BETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U22177; AAB03676.1; -. DR EMBL; AE003472; AAF47533.1; ALT_INIT. DR TRANSFAC; T02222; -. DR FlyBase; FBgn0013753; Bgb. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003713; F:transcription co-activator activity; IDA. DR InterPro; IPR003417; CBF_beta. DR Pfam; PF02312; CBF_beta; 1. KW Nuclear protein. FT CONFLICT 112 112 E -> D (IN REF. 1). SQ SEQUENCE 184 AA; 21792 MW; 2703CA5B91E04A9D CRC64; MPRVVPDQKS KFESDELFRR LSRESEVRYT GYRERSIEER QVRFMNGCRE GHTEASFVAS GTNLQLVFNA NQNPYLHDKE CDFDKEHGKV HIKSYFIMNG VCVRFRGWID LERLDGVGCL EYDERRAMHE DAILRDQIDR YNQRLREFED TKRAYRDNRQ DEMEAVRRGV ASGGIGVGAS MWRR // ID BGCN_DROME STANDARD; PRT; 1215 AA. AC Q9W1I2; Q9W1I3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Benign gonial cell neoplasm protein. GN BGCN OR B(2)GCN OR CG30170/CG10331. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=20384590; PubMed=10924476; RA Ohlstein B., Lavoie C.A., Vef O., Gateff E., McKearin D.M.; RT "The Drosophila cystoblast differentiation factor, benign gonial cell RT neoplasm, is related to DExH-box proteins and interacts genetically RT with bag-of-marbles."; RL Genetics 155:1809-1819(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: ESSENTIAL CYSTOBLAST DIFFERENTIATION FACTOR REQUIRED FOR CC BAM FUNCTION IN ASYMMETRIC DIVISION OF THE GERMLINE STEM CELLS. CC -!- TISSUE SPECIFICITY: EXPRESSED IN TESTIS AND IN 5-8 GERMLINE STEM CC CELLS OF OVARIES, IMMEDIATELY ADJACENT TO TERMINAL FILAMENT. CC -!- SIMILARITY: SOME SIMILARTIES TO DEXH-BOX PROTEINS BUT OUTSIDE OF CC THE HELICASE DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ANK REPEAT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF255662; AAF91348.1; -. DR EMBL; AE003462; AAF47077.2; -. DR FlyBase; FBgn0004581; bgcn. DR GO; GO:0007292; P:female gamete generation; IMP. DR InterPro; IPR002110; ANK. DR InterPro; IPR007502; Helicase_dom. DR Pfam; PF00023; ank; 2. DR Pfam; PF04408; HA2; 1. DR SMART; SM00248; ANK; 2. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. KW Developmental protein; ANK repeat. FT REPEAT 407 439 ANK. SQ SEQUENCE 1215 AA; 139278 MW; 11F83C1B3816F2CD CRC64; MNHIIQDKYI PQQLLYFLAG RRCCQQFPCT FRTSEHEAFA NNARSLGLRS QVVHVNGNSC VKVYKQACRH YLEEPKTLVL SSGATLNMFT LLSRKSLMGK EDLELYADLV SMKANASDLP SLHLPLPAIR PPNLRFWTEA QLNFLTAFLG HSLSDEILQS LYASRVIVYN AALCWDKSVF LPLVILDDCR NKKSNVKIMC IERQAILATY NSQRTANFFG EQLGETVGIQ LPYFSAVSSS TFIIYSTAQY FLRSLTSQQF RNISHLVVND VHLHDPYTDI LLSEIRMALS SHQNLRVVLL SQMGNPKKFT DFFGEGLQLN MIKQPEVAPR VSYLNELHSC IALAGIHKGP DIYKEIPEAF RANNPRNEQM DKCLQAYGEL GTDAALRPFL YAVNYDLAPV NYRHSLTGKT AVHFASELNK ANHLRLLLFM GADPYIVDLF QQNAISLAAM NGNHECIDVL NSYSLHGYVV KSAKPDFVDY DLIIDIMYLL RTKPEYSPGE YSPGNILIIL PTYYHIVKLN YMILSHCLTG SLQECSIFLL YDNMRNDYLQ ALVNASDETV KVVLATDIIE SLCLKVPFKY QIDTACRLNN VYDTTSCSGD DRFEWVAKDA LLRRELILQP NKGDVQCFRL ISKEAYEELS ETSQPSLQTM QLDKICLAVK LLSPNTIISE YLGITISPPP LINVHHAVQF LKKIDVLDDA EDVTWLGCRL MDIPVSCQLG RMLIFGILLR CLDPILTIVS SLSTADPLGI PFTEDIDNLW DRFTIYIQNS IKKERTYLSD NQFSDHFIFV RLYKEWQNRM HNRTPPLYLK DEYEFMLNGL MEQLTSIRSE IVSSLRAANL IHSRGKLSMN NLNQMSCNWH MVKAALTGGM YPNIYAVDTR KSSLKSAFSG NVSMHPNTVL RDFLEPLNIS AQSFRTPWIV CNRQKSHIVY ATLVVPLAVA MFSGHPRIRL SPICDSEMSL TDRNVNVFID EWIWMVMSKA TAEMVMRTRY YFFKMYHDLL KHCSELDMWR RDCEPVSQYT VLTDTLSKIF ESEDGFVGFF KPPPITFLPT PQLPSLYLLS VNAHFSWARE VEENMLSKPH HFNSHFIERQ FFVLYAGGDC EEFHSRNTPA FIESVLGKFV RPIDTPNRHI FVILYRKDPD MMLSISRAKF VNGVFMLQEY FRNNIPVFEI LDACVSLNVQ TPVFDGRLMS ALIDKRVGNL IMELFAFRHH WIHKR // ID BIB_DROME STANDARD; PRT; 700 AA. AC P23645; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Neurogenic protein big brain. GN BIB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90245091; PubMed=1692392; RA Rao Y., Jan L.Y., Jan Y.N.; RT "Similarity of the product of the Drosophila neurogenic gene big RT brain to transmembrane channel proteins."; RL Nature 345:163-167(1990). CC -!- FUNCTION: MAY MEDIATE INTERCELLULAR COMMUNICATION; MAY FUNCTION BY CC ALLOWING THE TRANSPORT OF CERTAIN MOLECULES AND THEREBY SENDING CC A SIGNAL FOR AN EXODERMAL CELL TO BECOME AN EPIDERMOBLAST INSTEAD CC OF A NEUROBLAST. MUTATION IN BIB GENE UNDERLIES "BIG BRAIN" CC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- DOMAIN: AQUAPORINS CONTAIN TWO TANDEM REPEATS EACH CONTAINING CC THREE MEMBRANE-SPANNING DOMAINS AND A PORE-FORMING LOOP WITH THE CC SIGNATURE MOTIF ASN-PRO-ALA (NPA). CC -!- SIMILARITY: BELONGS TO THE MIP/AQUAPORIN (TC 1.A.8) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53275; CAB37863.1; -. DR PIR; S09699; S09699. DR HSSP; P29972; 1FQY. DR FlyBase; FBgn0000180; bib. DR GO; GO:0007498; P:mesoderm development; IMP. DR GO; GO:0007399; P:neurogenesis; NAS. DR InterPro; IPR000425; MIP. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR ProDom; PD000295; MIP_family; 1. DR TIGRFAMs; TIGR00861; MIP; 1. DR PROSITE; PS00221; MIP; 1. KW Neurogenesis; Transport; Developmental protein; Repeat; Transmembrane. FT TRANSMEM 72 93 POTENTIAL. FT TRANSMEM 98 118 POTENTIAL. FT TRANSMEM 144 167 POTENTIAL. FT TRANSMEM 190 208 POTENTIAL. FT TRANSMEM 214 234 POTENTIAL. FT TRANSMEM 257 273 POTENTIAL. FT SITE 126 128 NPA 1. FT SITE 238 240 NPA 2. FT DOMAIN 439 451 POLY-GLN. FT DOMAIN 487 534 GLN-RICH. FT DOMAIN 658 690 POLY-GLN. SQ SEQUENCE 700 AA; 76951 MW; 3390A683F96D5B6B CRC64; MADESLHTVP LEHNIDYHIV TLFERLEAMR KDSHGGGHGV NNRLSSTLQA PKRSMQAEIR TLEFWRSIIS ECLASFMYVF IVCGAAAGVG VGASVSSVLL ATALASGLAM ATLTQCFLHI SGAHINPAVT LALCVVRSIS PIRAAMYITA QCGGGIAGAA LLYGVTVPGY QGNLQAAISH SAALAAWERF GVEFILTSLV VLCYFVSTDP MKKFMGNSAA SIGCAYSACC FVSMPYLNPA RSLGPSFVLN KWDSHWVYWF GPLVGGMASG LVYEYIFNSR NRNLRHNKGS IDNDSSSIHS EDELNYDMDM EKPNKYQQSQ GTYPRGQSNG NGGGQAAGNG QHQAANMGQM PGVVANAGQG NYCQNLYTAP PLSSKYDQQQ EPLYGGTRSL YCRSPTLTRS NLNRSQSVYA KSNTAINRDI VPRPGPLVPA QSLYPMRTQQ QQQQQQQQQQ QVASAPQSSH LQNQNVQNQM QQRSESIYGM RGSMRGQQQP IQQQQQQQQQ QLQQQQPNMG VQQQQMQPPP QMMSDPQQQP QGFQPVYGTR TNPTPMDGNH KYDRRDPQQM YGVTGPRNRG QSAQSDDSSY GSYHGSAVTP PARHPSVEPS PPPPPMLMYA PPPQPNAAHP QPIRTQSERK VSAPVVVSQP AACAVTYTTS QGSAVTAQQQ QQQQQQQQQQ QQQQQQQQQQ QQMMMQQQQQ HYGMLPLRPN // ID BICD_DROME STANDARD; PRT; 782 AA. AC P16568; Q9VJD5; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytoskeleton-like bicaudal D protein. GN BICD OR CG6605. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90075232; PubMed=2590944; RA Wharton R.P., Struhl G.; RT "Structure of the Drosophila BicaudalD protein and its role in RT localizing the the posterior determinant nanos."; RL Cell 59:881-892(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90152340; PubMed=2576013; RA Suter B., Romberg L.M., Steward R.; RT "Bicaudal-D, a Drosophila gene involved in developmental asymmetry: RT localized transcript accumulation in ovaries and sequence similarity RT to myosin heavy chain tail domains."; RL Genes Dev. 3:1957-1968(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THIS PROTEIN IS ESSENTIAL FOR DIFFERENTIATION. IT CC MAY PLAY A ROLE IN LOCALIZING OF NANOS (A MATERNAL DETERMINANT) CC ACTIVITY IN OOCYTES. BICD MUTATIONS CAUSE NANOS MISLOCALIZATION CC AND THUS BICAUDAL DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: OOGENESIS. CC -!- SIMILARITY: BELONGS TO THE BICD FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M31684; AAA28393.1; -. DR EMBL; X51652; CAA35964.1; -. DR EMBL; AE003655; AAF53616.1; -. DR EMBL; AY069452; AAL39597.1; -. DR PIR; A34219; A34219. DR FlyBase; FBgn0000183; BicD. DR GO; GO:0007293; P:egg chamber formation (sensu Insecta); IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0007294; P:oocyte cell fate determination (sensu Insecta); IMP. DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP. KW Cytoskeleton; Coiled coil; Developmental protein. FT DOMAIN 3 263 COILED COIL (POTENTIAL). FT DOMAIN 319 477 COILED COIL (POTENTIAL). FT DOMAIN 601 746 COILED COIL (POTENTIAL). FT CONFLICT 296 296 A -> S (IN REF. 1). FT CONFLICT 318 318 L -> P (IN REF. 1). FT CONFLICT 477 477 H -> R (IN REF. 1). SQ SEQUENCE 782 AA; 88953 MW; 5A71776171DF58E6 CRC64; MSSASNNGPS ADQSVQDLQM EVERLTRELD QVSSASAQSA QYGLSLLEEK SALQQKCEEL ETLYDNTRHE LDITQEALTK FQTSQKVTNK TGIEQEDALL NESAARETSL NLQIFDLENE LKQLRHELER VRNERDRMLQ ENSDFGRDKS DSEADRLRLK SELKDLKFRE TRMLSEYSEL EEENISLQKQ VSSLRSSQVE FEGAKHEIRR LTEEVELLNQ QVDELANLKK IAEKQMEEAL ETLQGEREAK YALKKELDGH LNRESMYHIS NLAYSIRSNM EDNASNNSDG EEENLALKRL EADLSTELKS PDGTKCDLFS EIHLNELKKL EKQLESMESE KTHLTANLRE AQTSLDKSQN ELQNFMSRLA LLAAHVDALV QLKKQIDVKE QGKEGGQKKD ELEQQLRALI SQYANWFTLS AKEIDGLKTD IAELQKGLNY TDATTTLRNE VTNLKNKLLA TEQKSLDLQS DVQTLTHISQ NAGQSLGSAR STLVALSDDL AQLYHLVCTV NGETPTRVLL DHKTDDMSFE NDSLTAIQSQ FKSDVFIAKP QIVEDLQGLA DSVEIKKYVD TVSDQIKYLK TAVEHTIDMN KHKIRSEGGD ALEKVNTEEM EELQEQIVKL KSLLSVKREQ IGTLRNVLKS NKQTAEVALT NLKSKYENEK IIVSDTMSKL RNELRLLKED AATFSSLRAM FAARCEEYVT QVDDLNRQLE AAEEEKKTLN QLLRLAVQQK LALTQRLEEM EMDREMRHVR RPMPAQRGTS GKSSFSTRPS SRNPASSNAN PF // ID BLM_DROME STANDARD; PRT; 1487 AA. AC Q9VGI8; Q9Y062; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bloom's syndrome protein homolog (EC 3.6.1.-) (Dmblm) (Mutagen- DE sensitive protein 309) (RecQ helicase homolog). GN MUS309 OR BLM OR CG6920. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND REPEATS. RC STRAIN=Canton-S; RX MEDLINE=99160561; PubMed=10049920; RA Kusano K., Berres M.E., Engels W.R.; RT "Evolution of the RECQ family of helicases: a Drosophila homolog, RT Dmblm, is similar to the human Bloom syndrome gene."; RL Genetics 151:1027-1039(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PARTICIPATES IN DNA REPLICATION AND REPAIR. EXHIBITS A CC MAGNESIUM-DEPENDENT ATP-DEPENDENT DNA-HELICASE ACTIVITY THAT CC UNWINDS SINGLE- AND DOUBLE-STRANDED DNA IN A 3'-5' DIRECTION (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE HELICASE FAMILY. RECQ SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HRDC DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U92536; AAD41441.1; -. DR EMBL; AE003692; AAF54691.1; -. DR FlyBase; FBgn0002906; mus309. DR GO; GO:0004003; F:ATP dependent DNA helicase activity; IDA. DR GO; GO:0000731; P:DNA repair synthesis; IMP. DR GO; GO:0006302; P:double-strand break repair; IMP. DR InterPro; IPR001410; DEAD. DR InterPro; IPR002464; DEAH_box. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR002121; HRDC. DR InterPro; IPR004589; RecQ. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00570; HRDC; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR TIGRFAMs; TIGR00614; recQ_fam; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. KW Hydrolase; Helicase; ATP-binding; DNA-binding; DNA replication; KW Repeat; Nuclear protein. FT DOMAIN 89 138 2 X 24AA REPEATS OF L-D-L-S-V-S-P-L-A-E- FT L-[SP]-A-K-K-K-[YS]-[AD]-R-D-[SP]-P-P-K- FT P. FT REPEAT 89 112 1. FT REPEAT 115 138 2. FT DOMAIN 225 230 POLY-PRO. FT DOMAIN 464 467 POLY-SER. FT DOMAIN 1283 1363 HRDC. FT DOMAIN 1369 1372 POLY-GLU. FT DOMAIN 1416 1432 NUCLEAR LOCALIZATION SIGNAL (BY FT SIMILARITY). FT NP_BIND 759 766 ATP (BY SIMILARITY). FT SITE 865 868 DEAH BOX. FT CONFLICT 98 98 K -> E (IN REF. 1). FT CONFLICT 110 110 K -> P (IN REF. 1). FT CONFLICT 126 126 L -> P (IN REF. 1). FT CONFLICT 134 136 SPK -> PPP (IN REF. 1). FT CONFLICT 169 169 Q -> P (IN REF. 1). FT CONFLICT 222 222 P -> S (IN REF. 1). FT CONFLICT 299 299 Y -> N (IN REF. 1). FT CONFLICT 417 417 M -> V (IN REF. 1). FT CONFLICT 459 459 Q -> R (IN REF. 1). FT CONFLICT 471 471 S -> C (IN REF. 1). FT CONFLICT 496 496 H -> P (IN REF. 1). FT CONFLICT 594 594 D -> G (IN REF. 1). FT CONFLICT 614 614 G -> A (IN REF. 1). FT CONFLICT 805 805 K -> E (IN REF. 1). FT CONFLICT 1116 1116 E -> G (IN REF. 1). SQ SEQUENCE 1487 AA; 166077 MW; 07361B8005E29432 CRC64; MSKKPVAQRK QLTLSSFIGL DGNSQSQPKS RAASVRSKPP AVYNPIFLDA SSSDDETTEI SSQSNNGTIA TKKSSRDPRT AKLKKHTYLD LSVSPLAKLS AKKYARDSPK KPTSLDLSVS PLAELLAKKS DRDSPKKPVQ NENSYTYRGL SESPVENKSI GDTLRKPPQK ERKTSIVWLS DSPEKKVTQN ERKILDSPLQ RFSFEDFPNK ENGNRHHLLT LPDSPPPPQP VKKPEKTMWQ NETKTIQDKD SPANPLVSNN LASISTLLDS SRAPNTYKGS SRNLFEDSPE KSGSGEQGYK LGSAKENEIP TKPATASLER NSVTSSPSPA APLKPRYSVA FDNSLADYLK DLAQNDNFSI DPNKQNTETL KSTLGFFRNT YVELMEKYCS LIDQIPAMHF NEIAGFQPNT FLKLKVMRQK FKARTQLVQN SLDKKESQLK AEQEALEKEE IEMQAEQAQQ TVLSSSSPEK SRPIMPLPKV QEIKDEKIPN RNQLIHDLCG EPDNFSPPSS PRDTQLIPKR QQLINDLCGE PDDFSPPSKQ NDPHLLRKCE ELVHDLCEEP DDYLAQSMML DGDLEEEQLN GPTQGTTTSG MDDDEDDLEG LLAEIEDEHQ KMQGRRSEFN GYSYKELEAV KVKEKHKETP INISLDDDGF PEYDEAMFEQ MHSQAAANKS RVSSAGPSTS KSVVPTKQTS ALHSQKLSGN FHANVHNDGI TGEFDGQKFE HSTRLMHGLS YSFGLKSFRP NQLQVINATL LGNDCFVLMP TGGGKSLCYQ LPAILTEGVT IVISPLKSLI FDQINKLASL DICAKSLSGE QKMADVMAIY RDLESQPPMV KLLYVTPEKI SSSARFQDTL DTLNSNNYIS RFVIDEAHCV SQWGHDFRPD YKKLGVLKKR FPNVPTIALT ATATPRVRLD ILAQLNLKNC KWFLSSFNRS NLRYRVLPKK GVSTLDDISR YIRSKPQHFS GIIYCLSRKE CDETSKKMCK DGVRAVSYHA GLTDTDRESR QKDWLTGKMR VICATVAFGM GIDKPDVRFV LHYSLPKSIE GYYQEAGRAG RDGDVADCIL YYNYSDMLRI KKMLDSDKAL QYNVKKIHVD NLYRIVGYCE NLTDCRRAQQ LDYFGEHFTS EQCLENRETA CDNCINKRAY KAVDALEHAR KAARAVKDLC SGRSRFTLLH IADVLKGSKI KKIIDFNHHK TPHHGVLKDW DKNDVHRLLR KMVIDGFLRE DLIFTNDFPQ AYLYLGNNIS KLMEGTPNFE FAVTKNAKEA KAAVGSVSDG ATSSTADGQS GMREIHERCY TDLLDLCRTI ASQRNVTMAS IMNIQALKSM AETLPITEKD MCSIPHVTKA NFDKYGAKLL EITSNYASEK LLMQAVLDEE EEQAAAKQRP STSGWNNESV DWDMAVASQG NANTSGASGF NSFRAGKRKK IYKSGASKRY KTSTTSPAAR KTTSARGRGG RAGAKRAESS ASSASGWKSK KTGNSFGFDL MPLPGSK // ID BLP_DROME STANDARD; PRT; 141 AA. AC Q9VF08; Q9GP65; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Black pearl protein. GN BLP OR CG5268. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=21100436; PubMed=11179663; RA Becker S., Gehrsitz A., Bork P., Buchner S., Buchner E.; RT "The black-pearl gene of Drosophila defines a novel conserved protein RT family and is required for early larval survival."; RL Gene 262:15-22(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ESSENTIAL FOR LARVAL DEVELOPMENT. CC -!- TISSUE SPECIFICITY: EXPRESSED IN DISTINCT CELLS IN THE EMBRYONIC CC AND LARVAL NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: HIGHLY EXPRESSED IN EARLY EMBRYOS. CC -!- SIMILARITY: BELONGS TO THE UPF0108 (MAGMAS) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ278732; CAC20095.1; -. DR EMBL; AE003711; AAF55254.1; -. DR EMBL; AY071034; AAL48656.1; -. DR FlyBase; FBgn0038387; blp. DR GO; GO:0002168; P:larval development (sensu Insecta); IMP. DR InterPro; IPR005341; UPF0108. DR Pfam; PF03656; UPF0108; 1. DR ProDom; PD311402; UPF0108; 1. KW Developmental protein. FT CONFLICT 35 35 A -> V (IN REF. 1). FT CONFLICT 85 87 QVN -> HVI (IN REF. 1). SQ SEQUENCE 141 AA; 15730 MW; 92981D4E1E1DB204 CRC64; MAKYIAQIIV LGAQAVGRAF TKALRQEIAA SQEAARRAGG GKQGDKSAES NLRTGMTLEE AKQILNIDDP KNVDAITKNY EHLFQVNERS KGGSFYIQSK VFRAKERLDH EIKAHEQPRS SNTEAAQDTA EESQSRSRQR R // ID BNB_DROME STANDARD; PRT; 442 AA. AC P29746; Q9VWQ0; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bangles and beads protein. GN BNB OR CG7088. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90126372; PubMed=2693037; RA Ng S.C., Perkins L.A., Conboy G., Perrimon N., Fishman M.C.; RT "A Drosophila gene expressed in the embryonic CNS shares one RT conserved domain with the mammalian GAP-43."; RL Development 105:629-638(1989). RN [2] RP REVISIONS. RX MEDLINE=92201643; PubMed=1551578; RA Eberl D.F., Perkins L.A., Engelstein M., Hilliker A.J., Perrimon N.; RT "Genetic and developmental analysis of polytene section 17 of the X RT chromosome of Drosophila melanogaster."; RL Genetics 130:569-583(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY PLAY AN IMPORTANT ROLE DURING DEVELOPMENT. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE EMBRYONIC CNS, IN SETS OF CC CELLS THAT ARE SEGMENTALLY REITERATED ALONG THE PERIPHERY OF THE CC NERVOUS SYSTEM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63828; CAA45323.1; -. DR EMBL; AE003510; AAF48888.1; -. DR EMBL; AY060682; AAL28230.1; -. DR PIR; A43555; A43555. DR FlyBase; FBgn0001090; bnb. KW Neurone. SQ SEQUENCE 442 AA; 45815 MW; 8EB67F77656A1200 CRC64; MKCQLLFVAT VCLASVWALP VPDEEVAIQP DSGAKAELLT KTVLPTAVEP APLKPEAEKP AETKTIEAKA AVPEQPDVNA NPSPSTPAAE PAKEINSVEL KSSAPDVETA PAIPEKKTLP EEAKPAQENA PVEAEKKQEK TARTEAEPTV EAQPQATKAI EQAPEAPAAN AEVQKQVVDE VKPQEPKIDA KSAEEPAIPA VVAAEKETPV PEQPARQERI NEIEQKDAKK DAAVAEEPAK AAEATPTAAP EAATKSDSNI QVIAPEKKSI ESSPAAAAAS PAAQAAQAKS GEAPKPVDQQ KSTETVAESA PVLKTNAPLA PAGATKVTEA VKEQEKEQPA ADTAAKALPE QKKTEETAAP AGAPEPTAAV APAAVPEAKK IDEAPAAETV VKGEEAIAKP IAQSPSAEPK KSSEEKSDKS ESKVDESSES KESEESSESK EN // ID BNK_DROME STANDARD; PRT; 303 AA. AC P40794; Q9VA03; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bottleneck protein. GN BNK OR CG1480. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94006568; PubMed=8402919; RA Schejter E.D., Wieschaus E.; RT "Bottleneck acts as a regulator of the microfilament network RT governing cellularization of the Drosophila embryo."; RL Cell 75:373-385(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTS AS A REGULATOR OF THE MICROFILAMENT NETWORK CC GOVERNING CELLULARIZATION OF THE EMBRYO. DETERMINES THE TIMING OF CC A KEY CONFORMATIONAL TRANSITION IN THE CORTICAL MICROFILAMENT CC NETWORK: THE PROPER COORDINATION OF MEMBRANE INVAGINATION AND CC BASAL CLOSURE OF THE CELLS. TO DO THIS, BNK POSSIBLY PHYSICALLY CC LINKS NEIGHBORING CONTRACTILE UNITS OF THE EARLY CYCLE 14 CC MICROFILAMENT NETWORK IN A MANNER THAT PREVENTS BASAL CONSTRICTION CC UNTIL THE PROPER STAGE HAS BEEN REACHED. BNK TOGETHER WITH NULLO CC AND SRY-ALPHA MAY PROVIDE AUXILIARY FUNCTIONS, BY ACTING BOTH TO CC STABILIZE A LARGE AND DYNAMIC MICROFILAMENT STRUCTURE AND REGULATE CC ITS FUNCTIONS. CC -!- SUBCELLULAR LOCATION: COLOCALIZES WITH THE STRUCTURAL TRANSITIONS CC IN THE MICROFILAMENT NETWORK DURING CELLULARIZATION. ASSOCIATION CC IS OBSERVED ONLY WHEN THE NETWORK ASSUMES AN ALIGNED AND TIGHTLY CC APPOSED HEXAGONAL CONFIGURATION. CC -!- TISSUE SPECIFICITY: RESTRICTED TO THE BLASTODERM. CC -!- DEVELOPMENTAL STAGE: OBSERVED EXCLUSIVELY IN THE LATE SYNCTIAL AND CC CELLULAR BLASTODERM STAGES OF DEVELOPMENT. TRANSCRIPTS ARE FIRST CC DETECTED DURING NUCLEAR DIVISION CYCLE 11. THEY REACH A STRONG CC PEAK AT CYCLE 14 AND FROM THEN ON GRADUALLY DECLINE UNTIL THEY CC ARE NO LONGER DETECTABLE AT THE END OF CELLULARIZATION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U01035; AAC46467.1; -. DR EMBL; AE003777; AAF57125.1; -. DR PIR; A49072; A49072. DR FlyBase; FBgn0004389; bnk. DR GO; GO:0005884; C:actin filament; IDA. DR GO; GO:0016044; P:membrane organization and biogenesis; NAS. KW Cytoskeleton; Developmental protein. FT DOMAIN 108 137 GLN-RICH. FT CONFLICT 115 115 R -> Q (IN REF. 1). SQ SEQUENCE 303 AA; 33566 MW; 46E337ADC566C23B CRC64; MSISTFNFQF YNYKLSPSSP GFGSTASRSS SSCISELEMD IDEDMSAQPT ITSTPKPRFT SQLAVELAKT EPGNGISPLR PKLHTAQKRW SMELREKVLE MSKRNNGQEK PQTARQQEQR QPQEQPLQQE ELQHQQQEPT VTDKINFFNK LTNTFESGFS KLMPQASSTN NRFIAMLRTA RPQNVATTTA NSSTANSFLG SDHSLSGSVT GQVPPPKPKR LSATTAQFAT PHVPAMGVGK GGSQRKCSLR RKPSMDKSRA TISRQSSSAS VRTQNHAIME DLSLVVPVRL RIAEYEQRIS MSA // ID BOSS_DROME STANDARD; PRT; 896 AA. AC P22815; Q9VBJ5; DT 01-AUG-1991 (Rel. 19, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bride of sevenless protein precursor. GN BOSS OR CG8285. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91115074; PubMed=2276620; RA Hart A.C., Kraemer H., van Vactor D.L. Jr., Paidhungat M., RA Zipursky S.L.; RT "Induction of cell fate in the Drosophila retina: the bride of RT sevenless protein is predicted to contain a large extracellular RT domain and seven transmembrane segments."; RL Genes Dev. 4:1835-1847(1990). RN [2] RP REVISIONS. RA Kraemer H.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP FUNCTION. RX MEDLINE=91312442; PubMed=1857416; RA Kraemer H., Cagan R.L., Zipursky S.L.; RT "Interaction of bride of sevenless membrane-bound ligand and the RT sevenless tyrosine-kinase receptor."; RL Nature 352:207-212(1991). CC -!- FUNCTION: ACTS AS A LIGAND FOR SEVENLESS TYROSINE-KINASE RECEPTOR CC DURING EYE DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED EXCLUSIVELY BY R8 PHOTORECEPTOR CC CELLS AND IS INTERNALIZED IN A SEV-DEPENDENT MANNER BY R7 CELLS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55887; CAA39373.1; -. DR EMBL; AE003754; AAF56539.1; -. DR FlyBase; FBgn0000206; boss. DR GO; GO:0005902; C:microvillus; IDA. DR GO; GO:0005118; F:sevenless binding; IGI. DR GO; GO:0045467; P:R7 development; NAS. DR GO; GO:0045470; P:R8-mediated photoreceptor organization; NAS. DR InterPro; IPR002956; Bride_of_7less. DR InterPro; IPR000337; GPCR_Mgr. DR Pfam; PF00003; 7tm_3; 1. DR PRINTS; PR01223; BRIDEOF7LESS. KW Transmembrane; Glycoprotein; Vision; Signal. FT SIGNAL 1 31 POTENTIAL. FT CHAIN 32 896 BRIDE OF SEVENLESS PROTEIN. FT DOMAIN 32 530 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 531 554 POTENTIAL. FT TRANSMEM 570 588 POTENTIAL. FT TRANSMEM 615 637 POTENTIAL. FT TRANSMEM 655 676 POTENTIAL. FT TRANSMEM 693 712 POTENTIAL. FT TRANSMEM 728 748 POTENTIAL. FT TRANSMEM 759 781 POTENTIAL. FT DOMAIN 782 896 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 307 307 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 474 474 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 485 485 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 896 AA; 99950 MW; 580AEBC0FA208E24 CRC64; MKVMDALQSG RRKPLPVALL CILVTVFCVL ECHGADLTSP TKKSAPLRIT KPQPTSQQAK PISITTRAPT TVASTTDDEV SSSVDGQLAP LISSTTEGPS SGTTASLVPE ICLNGLQLTV NSADEGTVIR KQEEFVKILE GDVVLSVLTK DPDSALFVIN RVNQANLIMA DFEIGIRAIS IDNASLAENL LIQEVQFLQQ CTTYSMGIFV DWELYKQLES VIKDLEYNIW PIPGTRAHLF PKVAHLLHQM PWGEKIASVE IATETLEMYN EFMEAARQEH MCLMHFKSDD NVYIMFGNKL ASHFKENGTL FSVPTDRTDD EFLADLPNRA FVLMENEIDL STAVELDATP TALDEILIGK SVLPSRVLSF AGSIIDLMNW LRGSLSKHCK RGEEHDLYVL ESCFNFLNFI EDWRTSEYRQ AHDTAEILSL LLMRKLGTAM NFQMYQKKVL TLDKITGESR TELREIASQN FVTNVTTYYH YNRDNHTSLE LKTKFGQVFN CQYSAGDNRR YPFLFDGESV MFWRIKMDTW VATGLTAAIL GLIATLAILV FIVVRISLGD VFEGNPTTSI LLLLSLILVF CSFVPYSIEY VGEQRNSHVT FEDAQTLNTL CAVRVFIMTL VYCFVFSLLL CRAVMLASIG SEGGFLSHVN GYIQAVICAF SVVAQVGMSV QLLVVMHVAS ETVSCENIYY GRWLWGLLAY DFALLCCVGA LIPSIYRSQR NYREGILIVI GSVLIMVIWV AWIALSLFGD EWRDAAIPLG LQASGWAVLV GILIPRTFLI VRGIERSDIA QALPSLTSLA FAQNNQYSSE QSVYECVNPA MRHCSQDEVN HQSPSEIPTL PLRGGGPRRQ QFFANLRQAN ANINPQRPPP RPQQSPSRSS VSSLPPSPDH NKITRF // ID BRC1_DROME STANDARD; PRT; 727 AA. AC Q01295; O46065; O46066; Q01293; Q01296; Q9W571; Q9W574; DT 01-NOV-1995 (Rel. 32, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Broad-complex core-protein isoforms 1/2/3/4/5. GN BR OR BR-C OR EG:17A9.1 OR EG:25D2.1 OR EG:123F11.1 OR GN CG11491/CG11511/CG11514. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., CHARACTERIZATION, AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; TISSUE=Larva; RX MEDLINE=92077389; PubMed=1743483; RA DiBello P.R., Withers D.A., Bayer C.A., Fristrom J.W., Guild G.M.; RT "The Drosophila Broad-Complex encodes a family of related proteins RT containing zinc fingers."; RL Genetics 129:385-397(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS 1; 4 AND 5). RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP DEVELOPMENTAL STAGE, AND CHARACTERIZATION OF ISOFORMS. RC TISSUE=Imaginal disks, and Larva; RX MEDLINE=96299417; PubMed=8660872; RA Bayer C.A., Holley B., Fristrom J.W.; RT "A switch in broad-complex zinc-finger isoform expression is regulated RT posttranscriptionally during the metamorphosis of Drosophila imaginal RT discs."; RL Dev. Biol. 177:1-14(1996). RN [6] RP DEVELOPMENTAL STAGE. RX MEDLINE=94038699; PubMed=8223281; RA Huet F., Ruiz C., Richards G.; RT "Puffs and PCR: the in vivo dynamics of early gene expression during RT ecdysone responses in Drosophila."; RL Development 118:613-627(1993). RN [7] RP CHARACTERIZATION OF ISOFORMS, AND MUTATIONAL ANALYSIS. RX MEDLINE=97384928; PubMed=9242423; RA Bayer C.A., von Kalm L., Fristrom J.W.; RT "Relationships between protein isoforms and genetic functions RT demonstrate functional redundancy at the Broad-Complex during RT Drosophila metamorphosis."; RL Dev. Biol. 187:267-282(1997). CC -!- FUNCTION: BROAD-COMPLEX PROTEINS ARE REQUIRED FOR PUFFING AND CC TRANSCRIPTION OF SALIVARY GLAND LATE GENES DURING METAMORPHOSIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=BRCORE-TNT1-Q1-Z1; CC IsoId=Q01295-1; Sequence=Displayed; CC Name=2; Synonyms=BRCORE-Q1-Z1; CC IsoId=Q01295-2; Sequence=VSP_006836; CC Name=3; Synonyms=BRCORE-Q2-Z1; CC IsoId=Q01295-3; Sequence=VSP_006835; CC Name=4; Synonyms=BRCORE-Z2; CC IsoId=Q01295-4; Sequence=VSP_006837, VSP_006838; CC Name=5; Synonyms=BRCORE-NS-Z3; CC IsoId=Q01295-5; Sequence=VSP_006839; CC Name=6; Synonyms=BRCORE-Z4; CC IsoId=Q24206-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: ISOFORMS Z1 ACCUMULATE SLOWLY IN MID INSTAR CC LARVAE SALIVARY GLANDS AT BEGINNING OF ECDYSONE RESPONSE (94-114 CC HOURS OF DEVELOPMENT AT PUFF STAGE 1) AND BECOME THE PREDOMINANT CC ISOFORM AFTER 6 HOURS. LEVELS DIMINISH AT PUFF STAGE 2 AND ARE CC MODERATELY ABUNDANT IN LATE LARVAE FROM STAGES 3-10. IN PREPUPAE, CC TRANSCRIPTS APPEAR AT PUFF STAGE 15 ONWARDS, REACHING MAXIMUM AT CC STAGES 18-20. IN GUT, LEVELS REMAIN CONSTANT BETWEEN STAGES 1-11. CC IN MALPIGHIAN TUBULES, Z1 ISOFORMS ARE SEEN AT STAGES 3 AND 7, BUT CC NOT AT STAGE 11. IN FAT BODY AND WING DISKS, LOW LEVELS INCREASE CC BETWEEN STAGES 3 AND 11. ISOFORM Z2 ACCUMULATES TO A HIGH LEVEL AT CC THE BEGINNING OF THE ECDYSONE RESPONSE DURING PUFF STAGE 1 AND CC ABRUPTLY DISAPPEARS AFTER SEVERAL HOURS. IN PREPUPAE, TRANSCRIPTS CC ARE REINDUCED AT LOW LEVELS. LOW LEVELS ARE SEEN IN THE MALPIGHIAN CC TUBULES, GUT AND FAT BODY BETWEEN STAGES 1-11 AND HIGH LEVELS IN CC THE WING DISK. ISOFORM Z3; IN MID INSTAR LARVAL SALIVARY GLAND CC TRANSCRIPT ACCUMULATES TO A HIGH LEVEL AT THE BEGINNING OF THE CC ECDYSONE RESPONSE, 94-98 HOURS OF DEVELOPMENT IN PUFF STAGE 1, AND CC ABRUPTLY DISAPPEARS AFTER SEVERAL HOURS. LEVELS INCREASE BY PUFF CC STAGE 3 REMAINING ABUNDANT IN LATE LARVAE UNTIL STAGE 10, THEN CC DIMINISH BY STAGE 11. IN PREPUPAE, TRANSCRIPTS ARE ABUNDANT AND CC INCREASE DURING PUFF STAGES 11-14 AND 18-20. HIGH LEVELS ARE SEEN CC IN MALPIGHIAN TUBULES, GUT AND FAT BODY BETWEEN STAGES 1-11 AND CC LOW LEVELS IN WING DISK. CC -!- INDUCTION: PRIMARY RESPONSE TO 20-HYDROXYECDYSONE IN THIRD INSTAR CC LARVAL IMAGINAL DISKS. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 2 C2H2-TYPE ZINC FINGERS. CC -!- CAUTION: REF.4 (CAA15629) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54666; CAA38477.1; -. DR EMBL; X54665; CAA38476.1; -. DR EMBL; X54663; CAA38474.1; -. DR EMBL; X54664; CAA38475.1; -. DR EMBL; AE003421; AAF45648.1; -. DR EMBL; AE003421; AAF45651.2; -. DR EMBL; AE003421; AAN09054.1; -. DR EMBL; AL009146; CAA15629.1; ALT_SEQ. DR EMBL; AL009146; CAA15626.1; -. DR EMBL; AL009146; CAA15628.1; -. DR PIR; S21912; S21912. DR PIR; S21913; S21913. DR PIR; S21914; S21914. DR TRANSFAC; T01478; -. DR TRANSFAC; T01479; -. DR FlyBase; FBgn0000210; br. DR GO; GO:0006914; P:autophagy; IMP. DR GO; GO:0007459; P:photoreceptor fate commitment (sensu Drosop...; IMP. DR GO; GO:0007458; P:progression of morphogenetic furrow (sensu ...; IMP. DR GO; GO:0009613; P:response to pest/pathogen/parasite; IMP. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. KW Nuclear protein; DNA-binding; Developmental protein; Zinc-finger; KW Metal-binding; Alternative splicing. FT DOMAIN 32 97 BTB. FT ZN_FING 636 659 C2H2-TYPE 1. FT ZN_FING 666 689 C2H2-TYPE 2. FT DOMAIN 203 207 POLY-ALA. FT DOMAIN 265 268 POLY-ASN. FT DOMAIN 439 444 POLY-THR. FT DOMAIN 451 460 POLY-ASN. FT DOMAIN 479 490 POLY-THR. FT DOMAIN 533 543 POLY-GLN. FT DOMAIN 546 558 POLY-GLN. FT DOMAIN 565 568 POLY-GLN. FT DOMAIN 596 603 POLY-ALA. FT DOMAIN 714 720 POLY-GLN. FT VARSPLIC 432 478 Missing (in isoform 3). FT /FTId=VSP_006835. FT VARSPLIC 432 495 Missing (in isoform 2). FT /FTId=VSP_006836. FT VARSPLIC 433 514 KLTTNATTTTTTINNSITNNNNNNNNNNYDYSLPTKNSNSQ FT KTPSPTTTTLTTPTTTTPTRPTAITSASGICGLNLSTFAAN FT -> NSPKKLFSCQLCGKLLCSKASLKRHIADKHAVRQEEYR FT CAICERVYCSRNSLMTHIYTYHKSRPGEMEMKDIKLYNQFN FT SSI (in isoform 4). FT /FTId=VSP_006837. FT VARSPLIC 515 727 Missing (in isoform 4). FT /FTId=VSP_006838. FT VARSPLIC 433 727 KLTTNATTTTTTINNSITNNNNNNNNNNYDYSLPTKNSNSQ FT KTPSPTTTTLTTPTTTTPTRPTAITSASGICGLNLSTFAAN FT GSSSGGSNGGLSMTALLPQQQQQQQQQHQMSQQQQQQQQQQ FT QQQGNSSSGQQQQPNGILACSTPKANTPTTTQQQMYAAVMA FT AAASASASTSGSANSSLNNSNSTLNTSGGLNNSASGGDDFR FT CNPCNKNLSSLTRLKRHIQNVHMRPTKEPVCNICKRVYSSL FT NSLRNHKSIYHRNLKQPKQEPGVGATQAAANSFYHQQHQQQ FT QLNHHSSS -> PHSITRSAATSPTSSTSSPPSPPTALISP FT TSSLKGSLAAAVYSLHSHAHGHVLGHATSPPRPGSVGSSVG FT SNLCTSTSMGCGVNSGNNSGNNNGNNANNNSNNGNATNNNN FT NSSSSSTSPGSQATAAGGTVTQAGTPPLPLRMPPPTSGGIN FT EPQECPYCRRTFSCYYSLKRHFQDKHEQSDTLYVCEFCHRR FT YRTKNSLTTHKSLQHRGSSGMLKRLLKTTAIKHGLVGHGHG FT HGHVHHPHAHHHALSHPRTSLYDFTSELGQPPPGIQ (in FT isoform 5). FT /FTId=VSP_006839. FT CONFLICT 230 230 V -> L (IN REF. 1). FT CONFLICT 457 459 MISSING (IN REF. 2). FT CONFLICT 460 460 N -> NN (IN REF. 1). SQ SEQUENCE 727 AA; 77393 MW; 97BBA20F3BD734D6 CRC64; MDDTQHFCLR WNNYQSSITS AFENLRDDEA FVDVTLACEG RSIKAHRVVL SACSPYFREL LKSTPCKHPV ILLQDVNFMD LHALVEFIYH GEVNVHQKSL QSFLKTAEVL RVSGLTQQQA EDTHSHLAQI QNLANSGGRT PLNTHTQSLP HPHHGSLHDD GGSSTLFSRQ GAGSPPPTAV PSLPSHINNQ LLKRMAMMHR SSAAAAAEET SHAFKRLRGS DNSLPLSGAV GSGSNNNSPD LPPLHARSAS PQQTPADFST IKHHNNNNTP PLKEEKRNGP TGNGNSGNGN GNGNGASNGN GISISDKLGS LTPSPLARAG ADDVKSEPMD MVCSNNNANA NDEHSNDSTG EHDANRSSSG DGGKGSLSSG NDEEIGDGLA SHHAAPQFIM SPAENKMFHA AAFNFPNIDP SALLGLNTQL QQSGDLAVSP QGKLTTNATT TTTTINNSIT NNNNNNNNNN YDYSLPTKNS NSQKTPSPTT TTLTTPTTTT PTRPTAITSA SGICGLNLST FAANGSSSGG SNGGLSMTAL LPQQQQQQQQ QHQMSQQQQQ QQQQQQQQGN SSSGQQQQPN GILACSTPKA NTPTTTQQQM YAAVMAAAAS ASASTSGSAN SSLNNSNSTL NTSGGLNNSA SGGDDFRCNP CNKNLSSLTR LKRHIQNVHM RPTKEPVCNI CKRVYSSLNS LRNHKSIYHR NLKQPKQEPG VGATQAAANS FYHQQHQQQQ LNHHSSS // ID BRC4_DROME STANDARD; PRT; 880 AA. AC Q24206; O46064; Q9W575; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Broad-complex core-protein isoform 6. GN BR OR BR-C OR EG:17A9.1 OR EG:25D2.1 OR EG:123F11.1 OR GN CG11491/CG11514. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., DEVELOPMENTAL STAGE, AND CHARACTERIZATION OF RP ISOFORMS. RC TISSUE=Imaginal disks, and Larva; RX MEDLINE=96299417; PubMed=8660872; RA Bayer C.A., Holley B., Fristrom J.W.; RT "A switch in broad-complex zinc-finger isoform expression is regulated RT posttranscriptionally during the metamorphosis of Drosophila imaginal RT discs."; RL Dev. Biol. 177:1-14(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP CHARACTERIZATION OF ISOFORMS, AND MUTATIONAL ANALYSIS. RX MEDLINE=97384928; PubMed=9242423; RA Bayer C.A., von Kalm L., Fristrom J.W.; RT "Relationships between protein isoforms and genetic functions RT demonstrate functional redundancy at the Broad-Complex during RT Drosophila metamorphosis."; RL Dev. Biol. 187:267-282(1997). CC -!- FUNCTION: BROAD-COMPLEX PROTEINS ARE REQUIRED FOR PUFFING AND CC TRANSCRIPTION OF SALIVARY GLAND LATE GENES DURING METAMORPHOSIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=6; Synonyms=BCORE-Z4; CC IsoId=Q24206-1; Sequence=Displayed; CC Name=1; Synonyms=BCORE-TNT1-Q1-Z1; CC IsoId=Q01295-1; Sequence=External; CC Name=2; Synonyms=BCORE-Q1-Z1; CC IsoId=Q01295-2; Sequence=External; CC Name=3; Synonyms=BCORE-Q2-Z1; CC IsoId=Q01295-3; Sequence=External; CC Name=4; Synonyms=BCORE-Z2; CC IsoId=Q01295-4; Sequence=External; CC Name=5; Synonyms=BCORE-NS-Z3; CC IsoId=Q01295-5; Sequence=External; CC -!- DEVELOPMENTAL STAGE: ACCUMULATES TO A HIGH LEVEL AT THE BEGINNING CC OF THE ECDYSONE RESPONSE, DURING THE METAMORPHOSIS OF IMAGINAL CC DISKS IN PUFF STAGE 1, AND ABRUPTLY DISAPPEARS AFTER SEVERAL CC HOURS. CC -!- INDUCTION: INDUCED AS A PRIMARY RESPONSE TO 20-HYDROXYECDYSONE IN CC THIRD INSTAR LARVAL IMAGINAL DISKS. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 2 C2H2-TYPE ZINC FINGERS. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN IN POSITIONS 534 CC TO 619 AND 656 TO 694 DUE TO FRAMESHIFTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U51585; AAB09760.1; ALT_FRAME. DR EMBL; AL009146; CAA15627.1; -. DR EMBL; AE003421; AAF45647.1; -. DR TRANSFAC; T01480; -. DR FlyBase; FBgn0000210; br. DR GO; GO:0006914; P:autophagy; IMP. DR GO; GO:0007459; P:photoreceptor fate commitment (sensu Drosop...; IMP. DR GO; GO:0007458; P:progression of morphogenetic furrow (sensu ...; IMP. DR GO; GO:0009613; P:response to pest/pathogen/parasite; IMP. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. KW Nuclear protein; DNA-binding; Developmental protein; KW Zinc-finger; Metal-binding; Alternative splicing. FT DOMAIN 32 97 BTB. FT ZN_FING 710 733 C2H2-TYPE 1. FT ZN_FING 740 763 C2H2-TYPE 2. FT DOMAIN 203 207 POLY-ALA. FT DOMAIN 265 268 POLY-ASN. FT DOMAIN 458 466 POLY-ASN. FT DOMAIN 584 589 POLY-PRO. FT DOMAIN 618 621 POLY-ALA. FT DOMAIN 798 803 POLY-ALA. FT DOMAIN 821 833 POLY-ALA. FT DOMAIN 862 867 POLY-GLN. FT CONFLICT 436 436 G -> D (IN REF. 1). FT CONFLICT 621 621 MISSING (IN REF. 1). FT CONFLICT 624 624 A -> R (IN REF. 1). FT CONFLICT 661 662 AV -> L (IN REF. 1). FT CONFLICT 678 678 MISSING (IN REF. 1). FT CONFLICT 722 723 KL -> NV (IN REF. 1). SQ SEQUENCE 880 AA; 92305 MW; 500C0A4A38663AAF CRC64; MDDTQHFCLR WNNYQSSITS AFENLRDDEA FVDVTLACEG RSIKAHRVVL SACSPYFREL LKSTPCKHPV ILLQDVNFMD LHALVEFIYH GEVNVHQKSL QSFLKTAEVL RVSGLTQQQA EDTHSHLAQI QNLANSGGRT PLNTHTQSLP HPHHGSLHDD GGSSTLFSRQ GAGSPPPTAV PSLPSHINNQ LLKRMAMMHR SSAAAAAEET SHAFKRLRGS DNSLPLSGAV GSGSNNNSPD LPPLHARSAS PQQTPADFST IKHHNNNNTP PLKEEKRNGP TGNGNSGNGN GNGNGASNGN GISISDKLGS LTPSPLARAG ADDVKSEPMD MVCSNNNANA NDEHSNDSTG EHDANRSSSG DGGKGSLSSG NDEEIGDGLA SHHAAPQFIM SPAENKMFHA AAFNFPNIDP SALLGLNTQL QQSGDLAVSP QGGSTGSLLS GVIVPGGSGG TPSNSSSNNN NNNSNNQQQK VEQQSSPHQL LQQQHHSTPH TNSPQLKQEQ PKSGGGSCKS SDLHIAAGSE RSLSRSSQGM PDAGGHSATP SPTAAYHKRE RERERERERE RERERERSLD HERDLERPGG TGSPPPPPPS HHSHFGQHPL SLLPSHHQLH ATHHELSAAA AHHAHAHAHA AHAHALARAG SPMEHHHLLH HRRASLSPSG AVSSASGAGG RGGGAGGPGG PGGSLLSSVR AQDVAQANRL LLPLPLNACH RCDVCGKLLS TKLTLKRHKE QQHLQPLNNA VCNLCHKVFR TLNSLNNHKS IYHRRQKNHH SYFHHGAGVS QAGSPGSRLH QSLSSLSAAA AAANNSVNVG GGSVGGAGGN AVAAAAAAAA AAAELLLSPI VGAAAVAGGT ASSTLQLAAA HQQQQQQSSP GIVKPCMDFL // ID BRH1_DROME STANDARD; PRT; 544 AA. AC Q24255; Q9VX54; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein B-H1 (Homeobox BarH1 protein). GN B-H1 OR BARH1 OR CG5529. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; RX MEDLINE=91239564; PubMed=1674606; RA Saigo K., Emori Y., Sone M., Akimaru H., Takayama E., RA Higashijima S.I., Ishimaru S., Kojima T.; RT "Identification of a different-type homeobox gene, BarH1, possibly RT causing Bar (B) and Om(1D) mutations in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4343-4347(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; RX MEDLINE=92112035; PubMed=1346120; RA Higashijima S., Kojima T., Michiue T., Ishimaru S., Emori Y., RA Saigo K.; RT "Dual Bar homeo box genes of Drosophila required in two photoreceptor RT cells, R1 and R6, and primary pigment cells for normal eye RT development."; RL Genes Dev. 6:50-60(1992). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=92275345; PubMed=1350558; RA Higashijima S., Michiue T., Emori Y., Saigo K.; RT "Subtype determination of Drosophila embryonic external sensory organs RT by redundant homeo box genes BarH1 and BarH2."; RL Genes Dev. 6:1005-1018(1992). RN [6] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=99169089; PubMed=10068639; RA Sato M., Kojima T., Michiue T., Saigo K.; RT "Bar homeobox genes are latitudinal prepattern genes in the developing RT Drosophila notum whose expression is regulated by the concerted RT functions of decapentaplegic and wingless."; RL Development 126:1457-1466(1999). RN [7] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=20115430; PubMed=10648235; RA Kojima T., Sato M., Saigo K.; RT "Formation and specification of distal leg segments in Drosophila by RT dual Bar homeobox genes, BarH1 and BarH2."; RL Development 127:769-778(2000). CC -!- FUNCTION: B-H1 AND B-H2 ARE REGULATED BY MEMBERS OF THE WG CC SIGNALING PATHWAY; WG AND DPP. B-H1 AND B-H2 ARE COEXPRESSED AND CC FUNCTIONALLY REQUIRED IN R1 AND R6 RECEPTOR CELLS AND PRIMARY CC PIGMENT CELLS FOR NORMAL EYE DEVELOPMENT. COEXPRESSION IS ALSO CC REQUIRED FOR THE FATE DETERMINATION OF EXTERNAL SENSORY ORGANS, CC FORMATION OF NOTAL MICROCHAETAE, FORMATION OF PRESUTURAL CC MACROCHAETAE, ANTENNAL DEVELOPMENT AND FOR DISTAL LEG CC MORPHOGENESIS; SEGMENTATION AND SPECIFICATION OF TARSAL SEGMENTS CC 3-5. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: B-H1 AND B-H2 ARE ABUNDANT IN THE EYE-ANTENNA CC IMAGINAL DISK. EXPRESSED IN R1 AND R6 CELLS THROUGHOUT LARVAL CC STAGE UNTIL 30 HOURS AFTER PUPARIUM FORMATION, AT WHICH TIME CC EXPRESSION IS SEEN IN THE ANTERIOR AND POSTERIOR PRIMARY PIGMENT CC CELLS. COEXPRESSED IN EMBRYONIC GLIAL CELLS, NEURONS OF THE CNS CC AND PNS, MOST LATITUDINAL ANTERIOR CELLS OF THE DEVELOPING NOTUM CC AND THE CENTRAL CIRCULAR REGION OF THE LEG AND ANTENNAL IMAGINAL CC DISK THROUGHOUT LARVAL DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: COEXPRESSED AT HIGH LEVELS WITH B-H1 IN CC EMBRYO AND PUPAE AND AT LOW LEVELS IN LARVAE. CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M73079; AAA28382.1; -. DR EMBL; M73259; AAA28382.1; JOINED. DR EMBL; M73078; AAA28382.1; JOINED. DR EMBL; AE003505; AAF48726.1; -. DR EMBL; AY058309; AAL13538.1; -. DR HSSP; P14653; 1B72. DR TRANSFAC; T03926; -. DR FlyBase; FBgn0011758; B-H1. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003700; F:transcription factor activity; NAS. DR GO; GO:0008407; P:bristle morphogenesis; IMP. DR GO; GO:0008057; P:eye pigment granule morphogenesis (sensu Dr...; IMP. DR GO; GO:0007455; P:eye-antennal disc metamorphosis; IMP. DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IMP. DR GO; GO:0007467; P:photoreceptor differentiation (sensu Drosop...; IMP. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR GO; GO:0008052; P:sensory organ determination; IMP. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00032; ANTENNAPEDIA; FALSE_NEG. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW DNA-binding; Homeobox; Developmental protein; Vision; Nuclear protein. FT SITE 406 501 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 297 357 HOMEOBOX. FT DOMAIN 19 174 HIS-RICH. FT DOMAIN 105 136 ASN-RICH. FT DOMAIN 187 227 ALA-RICH. FT DOMAIN 474 526 PRO-RICH. FT CONFLICT 45 45 P -> A (IN REF. 1). FT CONFLICT 66 66 A -> E (IN REF. 1). FT CONFLICT 218 218 A -> R (IN REF. 1). FT CONFLICT 412 412 MISSING (IN REF. 1). FT CONFLICT 486 486 V -> G (IN REF. 1). FT CONFLICT 504 504 A -> R (IN REF. 1). SQ SEQUENCE 544 AA; 56083 MW; BB536E3B00124926 CRC64; MKDSMSILTQ TPSEPNAAHP QLHHHLSTLQ QQHHQHHLHY GLQPPAVAHS IHSTTTMSSG GSTTTASGIG KPNRSRFMIN DILAGSAAAA FYKQQQHHQQ LHHHNNNNNS GSSGGSSPAH SNNNNNINGD NCEASNVAGV GVLPSALHHP QPHPPTHPHT HPHALMHPHG KLGHFPPTAG GNGLNVAQYA AAMQQHYAAA AAAAAARNNA AAAAAAAAAA AAAGVAAPPV DGGVDGGVGL APPAGGDLDD SSDYHEENED CDSGNMDDHS VCSNGGKDDD GNSVKSGSTS DMSGLSKKQR KARTAFTDHQ LQTLEKSFER QKYLSVQERQ ELAHKLDLSD CQVKTWYQNR RTKWKRQTAV GLELLAEAGN FAAFQRLYGG SPYLGAWPYA AAAGAAHGAT PHTNIDIYYR QAAAAAAMQK PLPYNLYAGV PSVGVGVGVG VGPAPFSHLS ASSSLSSLSS YYQSAAAAAS AANPGGPHPV APPPSVGGGS PPSGLVKPIP AHSASASPPP RPPSTPSPTL NPGSPPGRSV DSCSQSDDED QIQV // ID BRH2_DROME STANDARD; PRT; 645 AA. AC Q24256; Q24257; Q9VX55; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox B-H2 protein (Homeobox BarH2 protein). GN B-H2 OR BARH2 OR CG5488. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Canton-S; TISSUE=Pupae; RX MEDLINE=92112035; PubMed=1346120; RA Higashijima S., Kojima T., Michiue T., Ishimaru S., Emori Y., RA Saigo K.; RT "Dual Bar homeo box genes of Drosophila required in two photoreceptor RT cells, R1 and R6, and primary pigment cells for normal eye RT development."; RL Genes Dev. 6:50-60(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobrry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=92275345; PubMed=1350558; RA Higashijima S., Michiue T., Emori Y., Saigo K.; RT "Subtype determination of Drosophila embryonic external sensory organs RT by redundant homeo box genes BarH1 and BarH2."; RL Genes Dev. 6:1005-1018(1992). RN [4] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=99169089; PubMed=10068639; RA Sato M., Kojima T., Michiue T., Saigo K.; RT "Bar homeobox genes are latitudinal prepattern genes in the developing RT Drosophila notum whose expression is regulated by the concerted RT functions of decapentaplegic and wingless."; RL Development 126:1457-1466(1999). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=20115430; PubMed=10648235; RA Kojima T., Sato M., Saigo K.; RT "Formation and specification of distal leg segments in Drosophila by RT dual Bar homeobox genes, BarH1 and BarH2."; RL Development 127:769-778(2000). CC -!- FUNCTION: B-H1 AND B-H2 ARE REGULATED BY MEMBERS OF THE WG CC SIGNALING PATHWAY; WG AND DPP. B-H1 AND B-H2 ARE COEXPRESSED AND CC FUNCTIONALLY REQUIRED IN R1 AND R6 RECEPTOR CELLS AND PRIMARY CC PIGMENT CELLS FOR NORMAL EYE DEVELOPMENT. COEXPRESSION IS ALSO CC REQUIRED FOR THE FATE DETERMINATION OF EXTERNAL SENSORY ORGANS, CC FORMATION OF NOTAL MICROCHAETAE, FORMATION OF PRESUTURAL CC MACROCHAETAE, ANTENNAL DEVELOPMENT AND FOR DISTAL LEG CC MORPHOGENESIS; SEGMENTATION AND SPECIFICATION OF TARSAL SEGMENTS CC 3-5. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: B-H1 AND B-H2 ARE ABUNDANT IN THE EYE-ANTENNA CC IMAGINAL DISK. EXPRESSED IN R1 AND R6 CELLS THROUGHOUT LARVAL CC STAGE UNTIL 30 HOURS AFTER PUPARIUM FORMATION, AT WHICH TIME CC EXPRESSION IS SEEN IN THE ANTERIOR AND POSTERIOR PRIMARY PIGMENT CC CELLS. COEXPRESSED IN EMBRYONIC GLIAL CELLS, NEURONS OF THE CNS CC AND PNS, MOST LATITUDINAL ANTERIOR CELLS OF THE DEVELOPING NOTUM CC AND THE CENTRAL CIRCULAR REGION OF THE LEG AND ANTENNAL IMAGINAL CC DISK THROUGHOUT LARVAL DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: COEXPRESSED AT HIGH LEVELS WITH B-H1 IN CC EMBRYO AND PUPAE AND AT LOW LEVELS IN LARVAE. CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M82884; AAA28383.2; -. DR EMBL; M82887; AAB59218.1; -. DR EMBL; M82885; AAB59218.1; JOINED. DR EMBL; M82886; AAB59218.1; JOINED. DR EMBL; AE003505; AAF48725.1; -. DR PIR; A41726; A41726. DR HSSP; P14653; 1B72. DR TRANSFAC; T03927; -. DR FlyBase; FBgn0004854; B-H2. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003700; F:transcription factor activity; NAS. DR GO; GO:0008407; P:bristle morphogenesis; IMP. DR GO; GO:0008057; P:eye pigment granule morphogenesis (sensu Dr...; IMP. DR GO; GO:0007455; P:eye-antennal disc metamorphosis; IMP. DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IMP. DR GO; GO:0007467; P:photoreceptor differentiation (sensu Drosop...; IMP. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR GO; GO:0008052; P:sensory organ determination; IMP. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00032; ANTENNAPEDIA; FALSE_NEG. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Vision; Wnt signaling pathway; Developmental protein; Nuclear protein; KW DNA-binding; Homeobox. FT SITE 458 463 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 378 438 HOMEOBOX. FT DOMAIN 10 85 ALA-RICH. FT DOMAIN 101 204 GLN-RICH. FT DOMAIN 107 256 HIS-RICH. FT DOMAIN 272 321 ASN-RICH. FT DOMAIN 283 377 SER-RICH. FT DOMAIN 447 578 ALA-RICH. FT DOMAIN 607 644 GLU-RICH. FT CONFLICT 121 123 MISSING (IN REF. 1; AAB59218). FT CONFLICT 229 229 T -> P (IN REF. 1; AAB59218). FT CONFLICT 288 289 MISSING (IN REF. 1; AAB59218). FT CONFLICT 375 375 S -> N (IN REF. 1; AAB59218). SQ SEQUENCE 645 AA; 69950 MW; CF99E12F7ECBB133 CRC64; MTTMPPEMSA TTAAPVGSAP SATAHHPAAV GGGMPRPASP AVGSNTTTAT ATTATRSRFM ITDILAGAAA ASAAAAAAAA ALAAASSGGG RGSPTDSERE QSLVAQHHHH HQQQQQHHHH QQQQQQQQHQ QAALQQYIVQ QQQLLRFERE REREREREHY RERHSPPGNN PYAHHPMPPH LLAHFPPAHY AVLQQQQQQQ QQQQHPHPHH LQLERERLEA LHRHGHGLTG DPAQHLSHLS HLSHQQHHPH LHHPMHDERS RSPLMLQQLG GNGGNNNNNN NNSSSASNNN NNNNNSASAN SNIISGNSSS SNNNNGSGNG NMLLGGPGSS ISGDQASTID DSDSDDCGGK DDDGDDSMKN GSSANGDSSS HLSLSLSKKQ RKARTAFTDH QLQTLEKSFE RQKYLSVQDR MELANKLELS DCQVKTWYQN RRTKWKRQTA VGLELLAEAG NYAAFQRLYG GATPYLSAWP YAAAAAAQSP HGATPSAIDI YYRQAAAAAA MQKPSLPASY RMYQSSIPPG MSLPGMPAPP PPGAAPMLSG YYAAAAAAAA SAGAQQQQQQ PPAASRSPAT SQSANSEADC ERTSSSSRQR LITPSPPLNP GSPPHRERIN EEEDRERDEE RDIERERERE RERDEDDEEE LALEV // ID BRM_DROME STANDARD; PRT; 1638 AA. AC P25439; Q9VUW5; Q9VUW6; DT 01-MAY-1992 (Rel. 22, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Homeotic gene regulator (Brahma protein). GN BRM OR CG5942/CG18438. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RX MEDLINE=92154670; PubMed=1346755; RA Tamkun J.W., Deuring R., Scott M.P., Kissinger M., Pattatucci A.M., RA Kaufman T.C., Kennison J.A.; RT "Brahma: a regulator of Drosophila homeotic genes structurally RT related to the yeast transcriptional activator SNF2/SWI2."; RL Cell 68:561-572(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP IDENTIFICATION IN A BRAHMA COMPLEX WITH OSA AND SNR1. RX MEDLINE=20069333; PubMed=10601025; RA Collins R.T., Furukawa T., Tanese N., Treisman J.E.; RT "Osa associates with the Brahma chromatin remodeling complex and RT promotes the activation of some target genes."; RL EMBO J. 18:7029-7040(1999). RN [7] RP IDENTIFICATION IN A BRAHMA COMPLEX WITH OSA; OSA; MOR; SNR1; DALAO; RP BAP55; BAP60 AND BAP47, AND FUNCTION AS COACTIVATOR. RX MEDLINE=20270023; PubMed=10809665; RA Kal A.J., Mahmoudi T., Zak N.B., Verrijzer C.P.; RT "The Drosophila brahma complex is an essential coactivator for the RT trithorax group protein zeste."; RL Genes Dev. 14:1058-1071(2000). CC -!- FUNCTION: TRANSCRIPTIONAL REGULATOR. ACT AS COACTIVATOR, ASSISTING CC ONE OR MORE DEDICATED TRANSCRIPTIONAL ACTIVATORS OF ANTC AND BXC CC HOMEOTIC GENE CLUSTERS. CAN COUNTERACT THE REPRESSIVE EFFECT OF CC POLYCOMB PROTEIN. ATPASE SUBUNIT OF THE BRAHMA COMPLEX, A CC MULTIPROTEIN COMPLEX WHICH IS THE EQUIVALENT OF THE YEAST SWI/SNF CC COMPLEX AND ACTS BY REMODELLING THE CHROMATIN BY CATALYZING AN CC ATP-DEPENDENT ALTERATION IN THE STRUCTURE OF NUCLEOSOMAL DNA. THIS CC COMPLEX CAN BOTH SERVE AS A TRANSCRIPTIONAL COACTIVATOR OR CC COREPRESSOR, DEPENDING OF THE CONTEXT. CC -!- SUBUNIT: COMPONENT OF THE BRAHMA COMPLEX, WHICH IS COMPOSED OF CC BRM, OSA, MOR, SNR1/BAP45, BAP111/DALAO, BAP55, BAP60 AND BAP47. CC INTERACTS WITH PNR AND CHI VIA ITS EHD DOMAIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; Synonyms=A, B; CC IsoId=P25439-1; Sequence=Displayed; CC Name=Short; Synonyms=C, D; CC IsoId=P25439-2; Sequence=VSP_000555; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: HIGHEST EXPRESSION IN UNFERTILIZED EGGS AND CC EARLY EMBRYOS. CC -!- MISCELLANEOUS: 'BRAHMA' MEANS 'FATE' IN INDIA. CC -!- SIMILARITY: CONTAINS 1 BROMODOMAIN. CC -!- SIMILARITY: BELONGS TO THE SNF2/RAD54 HELICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M85049; AAA19661.1; -. DR EMBL; AE003529; AAN11773.1; -. DR EMBL; AE003529; AAF49558.3; -. DR EMBL; AY095048; AAM11376.1; -. DR EMBL; BT009972; AAQ22441.1; -. DR PIR; A42091; A42091. DR FlyBase; FBgn0000212; brm. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR000330; SNF2_N. DR Pfam; PF00439; bromodomain; 1. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00176; SNF2_N; 1. DR PRINTS; PR00503; BROMODOMAIN. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. KW Developmental protein; Transcription regulation; Chromatin regulator; KW Nuclear protein; Activator; Bromodomain; Helicase; ATP-binding; KW Alternative splicing. FT DOMAIN 201 390 GLN/PRO-RICH. FT NP_BIND 798 805 ATP (POTENTIAL). FT SITE 900 903 DEGH BOX. FT DOMAIN 1385 1392 ASP/GLU-RICH (ACIDIC). FT DOMAIN 1394 1404 ARG/LYS-RICH (BASIC). FT DOMAIN 1405 1410 ASP/GLU-RICH (ACIDIC). FT DOMAIN 1415 1432 ARG/LYS-RICH (BASIC). FT DOMAIN 1443 1513 BROMODOMAIN. FT DOMAIN 1631 1638 POLY-ASP. FT VARSPLIC 81 85 IFSKG -> S (in isoform Short). FT /FTId=VSP_000555. FT CONFLICT 687 687 D -> Y (IN REF. 1). SQ SEQUENCE 1638 AA; 185088 MW; A4494B29F4F2E42A CRC64; MASPSPANSP MPPPQAPSPM APPSQSPAPS PHSPYPHQQP GPLQGPPPPG HPGAYGHPMQ HGPPGQGPPG HHMPPHHQGM IFSKGPHMGM QMPPTGPNMS PYQTHGMPPN APTQPCIVSP GGPPGGPPPP ERSSQENLHA LQRAIDSMEE KGLQEDPRYS QLLAMRATSK HQHLNGNQVN LLRTQITAYR LLARNKPISM QMQQALQAAQ QQPPPGPPIG PPGAPGGPPP GSQHAGQPPV PPQQQQQPPP SAGTPPQCST PPASNPYGPP VPGQKMQVAP PPPHMQQGQP LPPQPPQVGG PPPIQQQQPP QQQQQQSQPP PPEPHQHQLP NGGKPLSMGP SGGQPLIPSS PMQPQVRGTL PGMPPGSQVP QPGGGPQRQV PPAGMPMPKP NRITTVAKPV GLDPITLLQE RENRIAARIS LRMQELQRLP ATMSEDLRLQ AAIELRALRV LNFQRQLRME FVQCTRRDTT LETALNIKLY KRTKRQGLRE ARATEKLEKQ QKLEAERKRR QKHLEFLAAV LQHGKDLREF HRNNKAQLAR MNKAVMNHHA NAEREQKKEQ ERIEKERMRR LMAEDEEGYR KLIDQKKDKR LAFLLSQTDE YISNLTQMVK QHKDDQMKKK EEEGKRLIQF KKELLMSGEY IGIDEGSIVA DMRVHVVEQC TGKKLTGDDA PMLKHLHRWL NMHPGWDWID DEEDSCGSND DHKPKVEEQP TATEDATDKA QATGNDEDAK DLITKAKVED DEYRTEEQTY YSIAHTIHEK VVEQASIMVN GTLKEYQIKG LEWLVSLYNN NLNGILADEM GLGKTIQTIS LVTYLMDRKK VMGPYLIIVP LSTLPNWVLE FEKWAPAVGV VSYKGSPQGR RLLQNQMRAT KFNVLLTTYE YVIKDKAVLA KIQWKYMIID EGHRMKNHHC KLTQVLNTHY IAPYRLLLTG TPLQNKLPEL WALLNFLLPS IFKSCSTFEQ WFNAPFATTG EKVELNEEET ILIIRRLHKV LRPFLLRRLK KEVEHQLPDK VEYIIKCDMS ALQRVLYKHM QSKGVLLTDG SEKGKHGKGG AKALMNTIVQ LRKLCNHPFM FQHIEEKYCD HTGGHGVVSG PDLYRVSGKF ELLDRILPKL KATNHRVLLF CQMTQCMTII EDYLGWRQFG YLRLDGTTKA EDRGELLRKF NAKGSDVFVF LLSTRAGGLG LNLQTADTVV IFDSDWNPHQ DLQAQDRAHR IGQRNEVRVL RLMTVNSVEE RILAAARYKL NMDEKVIQAG MFDQKSTGSE RQQFLQTILH QDDNEEEEEN EVPDDEMINM MIARSEEEIE IFKRMDAERK KEDEEIHPGR ERLIDESELP DWLTKDDDEV ERFHYQYDED TILGRGSRQR KEVDYTDSLT EKEWLKAIDD GAEFDEEEEE DDSKRKRRKR KNRKEESDDD SLILKRRRRQ NLDKRSKKQM HKIMSAVIKH NQDGRTLSEP FMKLPSRQRL PDYYEIIKRP VDIKKILQRI EDCKYADLNE LEKDFMQLCQ NAQIYNEEAS LIYLDSIALQ KVFVGARQRI TAAADAAAVA AGDNTGEAHG NGGSDNSDND DDDGGDDGSD DEEIATTSAA AVKMKLKLNK SLASAPATPT QSSSNVSSGA ATTSKKQTRR KRSQKKYTIS DDDDDDMD // ID BROW_DROME STANDARD; PRT; 675 AA. AC P12428; Q24264; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Brown protein. GN BW. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89218981; PubMed=3149712; RA Dreesen T.D., Johnson D.H., Henikoff S.; RT "The brown protein of Drosophila melanogaster is similar to the white RT protein and to components of active transport complexes."; RL Mol. Cell. Biol. 8:5206-5215(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95044127; PubMed=7956072; RA Martin-Morris L.E., Loughney K., Kershisnik E.O., Poortinga G., RA Henikoff S.; RT "Characterization of sequences responsible for trans-inactivation of RT the Drosophila brown gene."; RL Cold Spring Harb. Symp. Quant. Biol. 58:577-584(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=IG281; RA Nitasaka E., Green M.M., Yamazaki T.; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PART OF A MEMBRANE-SPANNING PERMEASE SYSTEM NECESSARY CC FOR THE TRANSPORT OF PIGMENT PRECURSORS INTO PIGMENT CELLS CC RESPONSIBLE FOR EYE COLOR. BROWN AND WHITE DIMERIZE FOR THE CC TRANSPORT OF GUANINE. CC -!- SUBUNIT: HETERODIMER OF BROWN WITH WHITE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M20630; AAA28397.1; -. DR EMBL; L23543; AAC37214.1; -. DR EMBL; L05635; AAA28398.1; -. DR PIR; A31399; FYFFB. DR FlyBase; FBgn0000241; bw. DR GO; GO:0006727; P:ommochrome biosynthesis; IMP. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transporter. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. KW Pigment; ATP-binding; Transmembrane; Transport. FT NP_BIND 66 73 ATP (BY SIMILARITY). FT TRANSMEM 423 441 POTENTIAL. FT TRANSMEM 454 474 POTENTIAL. FT TRANSMEM 504 522 POTENTIAL. FT TRANSMEM 531 552 POTENTIAL. FT TRANSMEM 565 583 POTENTIAL. FT TRANSMEM 645 665 POTENTIAL. FT VARIANT 28 28 D -> A. FT VARIANT 274 274 L -> I. FT VARIANT 331 331 E -> Q. FT VARIANT 407 407 R -> P. FT VARIANT 638 638 N -> T. FT CONFLICT 44 44 R -> P (IN REF. 3). SQ SEQUENCE 675 AA; 75943 MW; 81DEBDF856F4F174 CRC64; MQESGGSSGQ GGPSLCLEWK QLNYYVPDQE QSNYSFWNEC RKKRELRILQ DASGHMKTGD LIAILGGSGA GKTTLLAAIS QRLRGNLTGD VVLNGMAMER HQMTRISSFL PQFEINVKTF TAYEHLYFMS HFKMHRRTTK AEKRQRVADL LLAVGLRDAA HTRIQQLSGG ERKRLSLAEE LITDPIFLFC DEPTTGLDSF SAYSVIKTLR HLCTRRRIAK HSLNQVYGED SFETPSGESS ASGSGSKSIE MEVVAESHES LLQTMRELPA LGVLSNSPNG THKKAAICSI HQPTSDIFEL FTHIILMDGG RIVYQGRTEQ AAKFFTDLGY ELPLNCNPAD FYLKTLADKE GKENAGAVLR AKYEHETDGL YSGSWLLARS YSGDYLKHVQ NFKKIRWIYQ VYLLMVRFMT EDLRNIRSGL IAFGFFMITA VTLSLMYSGI GGLTQRTVQD VGGSIFMLSN EMIFTFSYGV TYIFPAALPI IRREVGEGTY SLSAYYVALV LSFVPVAFFK GYVFLSVIYA SIYYTRGFLL YLSMGFLMSL SAVAAVGYGV FLSSLFESDK MASECAAPFD LIFLIFGGTY MNVDTVPGLK YLSLFFYSNE ALMYKFWIDI DNIDCPVNED HPCIKTGVEV LQQGSYRNAD YTYWLDCFSL VVVAVIFHIV SFGLVRRYIH RSGYY // ID BRO_DROME STANDARD; PRT; 177 AA. AC Q24039; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Brother protein. GN BRO. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96182097; PubMed=8622696; RA Golling G., Li L., Pepling M., Stebbins M., Gergen J.P.; RT "Drosophila homologs of the proto-oncogene product PEBP2/CBF beta RT regulate the DNA-binding properties of Runt."; RL Mol. Cell. Biol. 16:932-942(1996). CC -!- FUNCTION: REGULATES THE DNA-BINDING PROPERTIES OF RUNT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CBF-BETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U22176; AAB03675.1; -. DR TRANSFAC; T02221; -. DR FlyBase; FBgn0013755; Bro. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003713; F:transcription co-activator activity; IDA. DR InterPro; IPR003417; CBF_beta. DR Pfam; PF02312; CBF_beta; 1. KW Nuclear protein. SQ SEQUENCE 177 AA; 20945 MW; 675764CA7D45FCBA CRC64; MPRVVPDQRS KFDSDELFRR LSRESEVRYT GYRERAMEER RMRFVNDCRK GYAEISMVAS GTNLQLYFNA NHNPYAQEQD CDFERERGKV HLRSSFIMNG VCVRFRGWVD LDRLDGAACL DFDEQRAQQE DAQLQEQIQS YNQRMAESRR IYHTPQTPPE DHHHRGGPSL PRGPMGW // ID BSG2_DROME STANDARD; PRT; 741 AA. AC P11929; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-MAR-1992 (Rel. 21, Last annotation update) DE Blastoderm specific protein 25D. GN BSG25D. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87174755; PubMed=3104878; RA Boyer P.D., Mahoney P.A., Lengyel J.A.; RT "Molecular characterization of bsg25D: a blastoderm-specific locus of RT Drosophila melanogaster."; RL Nucleic Acids Res. 15:2309-2325(1987). CC -!- DEVELOPMENTAL STAGE: BLASTODERM SPECIFIC. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04896; CAA28582.1; -. DR PIR; A26572; A26572. DR FlyBase; FBgn0000228; Bsg25D. KW Developmental protein. SQ SEQUENCE 741 AA; 84428 MW; 9ED8CE9F7FE2CD9F CRC64; MEVSADPYEQ KLYQMFRSCE TQCGLLDEKS LLKLCSLLEL RDQGSALIAS LGGSHQLGVS FGQFKEALLN FLGSEFDERS LVITDEPLNN TYIESPPESS DREVSPKLVV GTKKYGRRSR PQQGIYELSV TDSDNTDEDQ LQQQQNQRSL NGCDELGVQQ LETISVHSIM EAWELASIPN TRNLLHVLGF DEEEEVNLQQ LTKALEEELR GIDGDHEQSN MLRALAALQA TELGNYRLAY RQQHEENLKL RADNKAANQR VALLAVEVDE RHASLEDNSK KQVQQLEQRH ASMVREITLR MTNDRDHWTS MTGKLEAQLK SLEQEEIRLR TELELVRTEN TELESEQQKA HIQITELLEQ NIKLNQELAQ RSSSIGGTPE HSPLRPRRHS EDKEEEMLQL MEKLAALQME NAQLRDKTDE LTIEIESLNV ELIRSKTKAK KQEKQEKQED QESAATATKR RGDSPSKTHL TEESPRLGKQ RKCTEGEQSD ASNSGDWLAL NSELQRSQSQ DEELTSLRQR VAELEEELKA AKEGRSLTPE SRSKELETSL EQMQRAYEDC EDYWQTKLSE ERQLFEKERQ IYEDEQHESD KKFTELMEKV REYEEQFSKD GRLSPIDERD MLEQQYSELE AEAAQLRSSS IQMLEEKAQE ISSLQSEIED LRQRLGESVE ILTGACELTS ESVAQLSAEA GKSPASSPIS YLWLQSTIQE PAKSLADSKD EATASAIELL GGSPSHKTAS R // ID BSH_DROME STANDARD; PRT; 287 AA. AC Q04787; Q9VIS2; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Brain-specific homeobox protein. GN BSH OR CG10604. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93321621; PubMed=8101170; RA Jones B., McGinnis W.; RT "A new Drosophila homeobox gene, bsh, is expressed in a subset of RT brain cells during embryogenesis."; RL Development 117:793-806(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY PLAY A ROLE IN THE DETERMINATION AND FUNCTION OF CC CELL TYPES IN THE BRAIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: BRAIN. THE PROTEIN ACCUMULATES IN CC APPROXIMATELY 30 CELLS IN EACH BRAIN HEMISPHERE. ONE OF THESE CC CELLS IS CLOSELY ASSOCIATED WITH THE TERMINUS OF THE LARVAL VISUAL CC NERVE (BOLWIG'S NERVE). CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING EMBRYOGENESIS WITH VERY LOW CC LEVELS FOUND IN THE LARVA AND ADULT. CC -!- SIMILARITY: BELONGS TO THE DISTAL-LESS HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L06475; AAB59219.1; ALT_SEQ. DR EMBL; AE003664; AAF53843.2; -. DR HSSP; P14653; 1B72. DR FlyBase; FBgn0000529; bsh. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DOMAIN 35 49 PRO-RICH. FT DNA_BIND 132 191 HOMEOBOX. SQ SEQUENCE 287 AA; 31069 MW; 7B4B9E17CA038F2A CRC64; MHSTPRSNHH SRHGTSHYNG DQISQQLGSG AAQHPPVPTT QPQPPPPPPL NGGSGASNGV LYPNAPYTDH GFLQMTLGYL SPSSGTYKSV DPYFLSQASL FGGAPFFGAP GCVPELALGL GMGVNALRHC RRRKARTVFS DPQLSGLEKR FEGQRYLSTP ERVELATALG LSETQVKTWF QNRRMKHKKQ LRRRDNANEP VDFSRSEPGK QPGEATSSSG DSKHGKLNPG SVGGTPTQPT SEQQLQMCLM QQGYSTDDYS DLEADSGDED NSSDVDIVGD AKLYQLT // ID BTD_DROME STANDARD; PRT; 644 AA. AC Q24266; Q9W319; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor BTD (Buttonhead protein). GN BTD OR CG12653. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=94081952; PubMed=8259212; RA Wimmer E.A., Jaeckle H., Pfeifle C., Cohen S.M.; RT "A Drosophila homologue of human Sp1 is a head-specific segmentation RT gene."; RL Nature 366:690-694(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE DEVELOPMENT OF THE ANTENNAL, CC INTERCALARY AND MANDIBULAR SEGMENTS OF THE HEAD. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: FIRST EXPRESSED IN A STRIPE COVERING THE HEAD CC ANLAGEN OF THE SYNCITIAL BLASTODERM EMBRYO, PERSISTS THROUGH CC GASTRULATION AND DECAYS DURING GERM BAND EXTENSION. EXPRESSED CC LATER IN DEVELOPMENT IN A COMPLEX SPATIALLY RESTRICTED PATTERN. CC -!- SIMILARITY: CONTAINS 3 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z29361; CAA82545.1; -. DR EMBL; AE003448; AAF46518.1; -. DR HSSP; P08047; 1SP2. DR FlyBase; FBgn0000233; btd. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 3. DR ProDom; PD000003; Znf_C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. KW Transcription regulation; Activator; Zinc-finger; Metal-binding; KW DNA-binding; Nuclear protein; Repeat. FT ZN_FING 333 357 C2H2-TYPE 1. FT ZN_FING 363 385 C2H2-TYPE 2. FT ZN_FING 391 413 C2H2-TYPE 3. FT DOMAIN 14 89 GLN-RICH. FT DOMAIN 208 220 POLY-ALA. FT DOMAIN 431 434 POLY-ALA. FT DOMAIN 486 492 POLY-PRO. FT DOMAIN 499 502 POLY-THR. FT DOMAIN 515 519 POLY-SER. FT DOMAIN 530 536 POLY-SER. FT DOMAIN 596 599 POLY-SER. SQ SEQUENCE 644 AA; 68581 MW; A0DB98C2AF938452 CRC64; MIDAACNYLN PYAQQHQAQQ QQHAQHQQHA QQQQHHLHMQ QAQHHLHLSH QQAQQQHMQH LTQQQQQQQQ QQQQQQQQQQ QQQQPQQQQH DFLSAAALLS APPSLSGSSS GSSSGSSPLY GKPPMKLELP YPQASSTGTA SPNSSIQSAP SSASVSPSIF PSPAQSFASI SASPSTPTTT LAPPTTAAAG ALAGSPTSSS PSSSAASAAA AAAAAAAAAA DLGAAAVASA AYGWNTAYSG LGPARSQFPY AQYASDYYGN AVGMSSSAAW FSHQERLYQP WSSQSYPGFN FDDIAFQTQL QRRSVRCTCP NCTNEMSGLP PIVGPDERGR KQHICHIPGC ERLYGKASHL KTHLRWHTGE RPFLCLTCGK RFSRSDELQR HGRTHTNYRP YACPICSKKF SRSDHLSKHK KTHFKDKKSK KVLAAEAKEQ AAAAIKLEKK EKKSGKPLTP PVEFKQEQPD TTPLVNYAPY ANLYQHSTSA GSSVNPPPPP PPLFQQQMTT TTSSAAASFV EQPWSSSSSR AIQPATTSAS SSSSSSASSP AAAVVSAIGS ASSPAASATA LAQHHYAALA MQSESQLAAE YGLTMSGLAS GASQDSSSSC HMKSEYAASY PADFGAGTAS YGYPHPHPHH HNAWAAAYHP HATA // ID BTHD_DROME STANDARD; PRT; 249 AA. AC Q9VYB0; Q8MRZ5; Q962X5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Selenoprotein BthD. GN BTHD OR CG11177. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RX MEDLINE=21380129; PubMed=11389138; RA Martin-Romero F.J., Kryukov G.V., Lobanov A.V., Carlson B.A., RA Lee B.J., Gladyshev V.N., Hatfield D.L.; RT "Selenium metabolism in Drosophila: selenoproteins, selenoprotein RT mRNA expression, fertility, and mortality."; RL J. Biol. Chem. 276:29798-29804(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN A REDOX-RELATED PROCESS (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: HIGH LEVELS IN EMBRYOS AND LOW IN LARVAE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF396455; AAK72982.1; -. DR EMBL; AE003493; AAF48293.3; -. DR EMBL; AY119185; AAM51045.1; ALT_SEQ. DR FlyBase; FBgn0030501; BthD. KW Selenium; Selenocysteine; Redox-active center. FT DISULFID 34 37 REDOX-ACTIVE (BY SIMILARITY). FT SE_CYS 37 37 FT CONFLICT 114 114 Q -> R (IN REF. 2). FT CONFLICT 129 129 T -> I (IN REF. 2). FT CONFLICT 134 134 S -> L (IN REF. 2). FT CONFLICT 145 145 I -> L (IN REF. 2). FT CONFLICT 161 161 K -> E (IN REF. 2). SQ SEQUENCE 249 AA; 27727 MW; 57DC0BFD9ACBF4AF CRC64; MPPKRNKKAE APIAERDAGE ELDPNAPVLY VEHCRSCRVF RRRAEELHSA LRERGLQQLQ LQLNALGAPR RGAFELSLSA GGMGKQEQVA LWSGLKRGPP RARKFPTVEE VYDQIVGILG DQQESKEQTN TQKSSKIDLP GSEAIASPKK SESTEEAQEN KAPTSTSTSR KSKKEQKSEE EPTQVDSKEA KQSKELVKTK RQPKAQKKQA KASESQEEVA EDKPPSSQKR KRTTRSSTDE ATAGAKRRR // ID BTKL_DROME STANDARD; PRT; 786 AA. AC P08630; O45032; O76132; O76133; P11361; Q8T0A0; Q9VLQ2; Q9VLQ3; DT 01-AUG-1988 (Rel. 08, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase Btk29A (EC 2.7.1.112) (Dsrc28C). GN BTK29A OR SRC29A OR SRC2 OR TEC29 OR CG8049. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=87257924; PubMed=3110602; RA Gregory R.J., Kammermeyer K.L., Vincent W.S. III, Wadsworth S.G.; RT "Primary sequence and developmental expression of a novel Drosophila RT melanogaster src gene."; RL Mol. Cell. Biol. 7:2119-2127(1987). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S, and Oregon-R; TISSUE=Head; RX MEDLINE=99263011; PubMed=10330180; RA Baba K., Takeshita A., Majima K., Ueda R., Kondo S., Juni N., RA Yamamoto D.; RT "The Drosophila Bruton's tyrosine kinase (Btk) homolog is required for RT adult survival and male genital formation."; RL Mol. Cell. Biol. 19:4405-4413(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 199-789 FROM N.A. (ISOFORM 1). RC TISSUE=Eye-antennal disk; RX MEDLINE=98325396; PubMed=9660966; RA Guarnieri D.J., Dodson G.S., Simon M.A.; RT "SRC64 regulates the localization of a Tec-family kinase required RT for Drosophila ring canal growth."; RL Mol. Cell 1:831-840(1998). RN [7] RP SEQUENCE OF 552-684 FROM N.A. RX MEDLINE=85215606; PubMed=3923437; RA Wadsworth S.C., Madhavan K., Bilodeau-Wentworth D.; RT "Maternal inheritance of transcripts from three Drosophila src-related RT genes."; RL Nucleic Acids Res. 13:2153-2170(1985). RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=98322240; PubMed=9655810; RA Dodson G.S., Guarnieri D.J., Simon M.A.; RT "Src64 is required for ovarian ring canal morphogenesis during RT Drosophila oogenesis."; RL Development 125:2883-2892(1998). RN [9] RP SIMILARITY WITH BTK SUBFAMILY. RA Sjolander K.; RL Unpublished observations (JUL-1997). CC -!- FUNCTION: REQUIRED FOR PROPER RING CANAL DEVELOPMENT. ALSO CC REQUIRED FOR THE DEVELOPMENT OF MALE GENITALIA AND FOR ADULT CC SURVIVAL. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: RING CANALS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; CC IsoId=P08630-1; Sequence=Displayed; CC Name=1; CC IsoId=P08630-2; Sequence=VSP_004964, VSP_004965; CC -!- TISSUE SPECIFICITY: RING CANALS IN THE EGG CHAMBERS AND IMAGINAL CC DISKS OF THIRD-INSTAR LARVAE. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC PREDOMINANTLY IN EARLY TO MIDDLE EMBRYOGENESIS, IN LARVAE AND CC ADULT FEMALES. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. TEC CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS CC IN POSITIONS IN THE N-TERMINAL SEQUENCE OF ISOFORM 1 AND IN CC POSITIONS 222-245. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16599; AAA28912.1; ALT_FRAME. DR EMBL; AB009840; BAA24063.1; -. DR EMBL; AB009841; BAA24064.1; -. DR EMBL; AE003620; AAF52631.3; -. DR EMBL; AE003620; AAF52632.2; -. DR EMBL; AY069457; AAL39602.1; -. DR EMBL; AY128441; AAM75034.1; -. DR EMBL; AF044337; AAB99858.1; -. DR EMBL; X02305; CAA26170.1; -. DR PIR; A23051; A23051. DR PIR; A27807; TVFFDS. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0003502; Btk29A. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0045172; C:ring canal (sensu Drosophila); IDA. DR GO; GO:0004713; F:protein-tyrosine kinase activity; ISS. DR GO; GO:0007620; P:copulation; NAS. DR GO; GO:0007619; P:courtship behavior; NAS. DR GO; GO:0008340; P:determination of adult life span; IMP. DR GO; GO:0008258; P:head involution; IMP. DR GO; GO:0007485; P:male genital morphogenesis (sensu Holometab...; IMP. DR GO; GO:0007301; P:ovarian ring canal formation; IDA. DR GO; GO:0006468; P:protein amino acid phosphorylation; ISS. DR InterPro; IPR001849; PH. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00169; PH; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW Tyrosine-protein kinase; Proto-oncogene; Phosphorylation; Transferase; KW ATP-binding; SH3 domain; SH2 domain; Alternative splicing. FT DOMAIN 14 27 SER-RICH. FT DOMAIN 41 184 PH. FT DOMAIN 231 264 SER-RICH. FT DOMAIN 263 289 GLY-RICH. FT DOMAIN 342 402 SH3. FT DOMAIN 410 503 SH2. FT DOMAIN 526 779 PROTEIN KINASE. FT NP_BIND 532 540 ATP (BY SIMILARITY). FT BINDING 554 554 ATP (BY SIMILARITY). FT ACT_SITE 647 647 BY SIMILARITY. FT MOD_RES 677 677 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT VARSPLIC 1 183 Missing (in isoform 1). FT /FTId=VSP_004964. FT VARSPLIC 184 231 EDSNTPKSYRYHPGLWSGKKWSCCKGLSRTTFGCRAAAHWR FT EANNNPS -> MIPCVSLAETSVIGNMKERVKEMKVFGCRL FT NFWNHIGHSLTSSKTKEG (in isoform 1). FT /FTId=VSP_004965. FT CONFLICT 243 243 S -> A (IN REF. 1). FT CONFLICT 317 317 T -> N (IN REF. 1 AND 2). FT CONFLICT 352 353 PF -> LG (IN REF. 1). FT CONFLICT 363 363 L -> VG (IN REF. 1). FT CONFLICT 365 365 K -> KQ (IN REF. 3). FT CONFLICT 398 400 KPK -> QAE (IN REF. 1). FT CONFLICT 414 414 D -> Y (IN REF. 1). FT CONFLICT 524 525 ME -> IQ (IN REF. 1). FT CONFLICT 589 589 S -> T (IN REF. 1 AND 6). FT CONFLICT 657 657 S -> F (IN REF. 6). FT CONFLICT 681 684 GGTK -> AEPS (IN REF. 6). SQ SEQUENCE 786 AA; 87392 MW; E2BCE122E6AAA0AA CRC64; MMGTKHRNSH VNGSIKSSSS LRSSSKSFQA KMDLMSERLY DVVKSGSMVK RAQNKKRFTP VNYKHRWFEL TKRTFSYFDV ENVERRRERG RIHLKGVRLV EEATVSGEGG DPFAPDGYPF QVGYCEISAS ANSHQLENGN GGGSGVGIEG QQSGRAVPQY TLYVIANSEK ERSEWIRAIR QVCEDSNTPK SYRYHPGLWS GKKWSCCKGL SRTTFGCRAA AHWREANNNP SNGSSPAQNS TRSISPNSST TNSQFSLQHN SSGSLGGGVG GGLGGGGSLG LGGGGGGGGS CTPTSLQPQS SLTTFKQSPT LLNGNGTLLD ANMPGGIPTP GTPNSKAKDN SHFVKLVVAL YPFKAIEGGD LSLEKNAEYE VIDDSQEHWW KVKDALGNVG YIPSNYVKPK ALLGLERYEW YVGDMSRQRA ESLLKQGDKE GCFVVRKSST KGLYTLSLHT KVPQSHVKHY HIKQNARCEY YLSEKHCCET IPDLINYHRH NSGGLACRLK SSPCDRPVPP TAGLSHDKWE IHPMELMLME ELGSGQFGVV RRGKWRGSID TAVKMMKEGT MSEDDFIEEA KVMTKLQHPN LVQLYGVCSK HRPIYIVTEY MKHGSLLNYL RRHEKTLIGN MGLLLDMCIQ VSKGMTYLER HNYIHRDLAA RNCLVGSENV VKVADFGLAR YVLDDQYTSS GGTKFPIKWA PPEVLNYTRF SSKSDVWAYG VLMWEIFTCG KMPYGRLKNT EVVERVQRGI ILEKPKSCAK EIYDVMKLCW SHGPEERPAF RVLMDQLALV AQTLTD // ID BUN1_DROME STANDARD; PRT; 224 AA. AC Q24522; O02431; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Bunched protein, class 1 isoform (Shortsighted protein). GN BUN OR SHS. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND RP FUNCTION. RC TISSUE=Eye-antennal disk; RX MEDLINE=96038094; PubMed=7555710; RA Treisman J.E., Lai Z.-C., Rubin G.M.; RT "Shortsighted acts in the decapentaplegic pathway in Drosophila eye RT development and has homology to a mouse TGF-beta-responsive gene."; RL Development 121:2835-2845(1995). RN [2] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND FUNCTION. RC TISSUE=Ovary; RX MEDLINE=97398458; PubMed=9256356; RA Dobens L., Hsu T., Twombly V., Gelbart W.M., Raftery L.A., RA Kafatos F.C.; RT "The Drosophila bunched gene is a homologue of the growth factor RT stimulated mammalian TSC-22 sequence and is required during RT oogenesis."; RL Mech. Dev. 65:197-208(1997). CC -!- FUNCTION: PROBABLE TRANSCRIPTION FACTOR REQUIRED FOR PERIPHERAL CC NERVOUS SYSTEM MORPHOGENESIS, EYE DEVELOPMENT AND OOGENESIS. MAY CC BE REQUIRED FOR THE TRANSMISSION OF THE DPP SIGNAL AND FOR A CC MORPHOGENETIC MOVEMENT OF THE MEDULLA IN THE BRAIN THAT REORIENTS CC THE SECOND OPTIC LOBE RELATIVE TO THE FIRST. PLAYS A ROLE IN CC DETERMINING PROPER DORSAL CELL FATES LEADING TO THE FORMATION OF CC THE DORSAL APPENDAGES. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=Class 1; CC IsoId=Q24522-1; Sequence=Displayed; CC Name=Class 2; CC IsoId=Q24523-1; Sequence=External; CC Name=Class 3; CC IsoId=Q24523-2; Sequence=External; CC -!- TISSUE SPECIFICITY: ANTERIOR DORSAL FOLLICLE CELLS AT STAGES 10-12 CC OF OOGENESIS. CC -!- SIMILARITY: BELONGS TO THE TSC-22/DIP/BUN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L42511; AAC41607.1; -. DR EMBL; AF003342; AAB61239.1; ALT_INIT. DR HSSP; P80220; 1DIP. DR FlyBase; FBgn0010460; bun. DR GO; GO:0007422; P:peripheral nervous system development; NAS. DR InterPro; IPR000580; TSC-22_Dip_Bun. DR Pfam; PF01166; TSC22; 1. DR ProDom; PD007152; TSC-22_Dip_Bun; 1. DR PROSITE; PS01289; TSC22; 1. KW Transcription regulation; Nuclear protein; Alternative splicing. FT DOMAIN 8 11 POLY-ASN. FT DOMAIN 82 103 LEUCINE-ZIPPER. FT DOMAIN 207 214 POLY-ALA. FT CONFLICT 30 30 Q -> E (IN REF. 2). FT CONFLICT 34 34 R -> C (IN REF. 2). FT CONFLICT 100 100 N -> H (IN REF. 2). FT CONFLICT 106 106 N -> K (IN REF. 2). FT CONFLICT 122 123 AA -> PR (IN REF. 2). FT CONFLICT 188 188 E -> G (IN REF. 2). FT CONFLICT 192 192 V -> G (IN REF. 2). SQ SEQUENCE 224 AA; 23239 MW; 7ED7866EE05CB97B CRC64; MKTETGSNNN NTTVVNMDFD MYPSISGKQQ DPVREVVMKY IDYFLPDASG TSAVAIDNKI EQAMDLVKSH LMIAVREEVE VLKERISELM DKINKLELEN SILKSNIPQE TLQQLQLQLQ LAAPPATPAI QAAPAVQSVV APAAAGQAVQ QQAAGAVAVT GVATSPASAV VPTSIPNGSA ENGSSAVESA AVSVEQQVQQ VQQVTSAAAA AAAASVVTAN GPMS // ID BUN2_DROME STANDARD; PRT; 1211 AA. AC Q24523; Q9VK78; Q9VK79; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bunched protein, class 2/class 3 isoforms (Shortsighted protein). GN BUN OR SHS OR CG5461. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM CLASS 2), SUBCELLULAR LOCATION, AND RP FUNCTION. RC TISSUE=Eye-antennal disk; RX MEDLINE=96038094; PubMed=7555710; RA Treisman J.E., Lai Z.-C., Rubin G.M.; RT "Shortsighted acts in the decapentaplegic pathway in Drosophila eye RT development and has homology to a mouse TGF-beta-responsive gene."; RL Development 121:2835-2845(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS CLASS 2 AND CLASS 3). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE TRANSCRIPTION FACTOR REQUIRED FOR PERIPHERAL CC NERVOUS SYSTEM MORPHOGENESIS, EYE DEVELOPMENT AND OOGENESIS. MAY CC BE REQUIRED FOR THE TRANSMISSION OF THE DPP SIGNAL AND FOR A CC MORPHOGENETIC MOVEMENT OF THE MEDULLA IN THE BRAIN THAT REORIENTS CC THE SECOND OPTIC LOBE RELATIVE TO THE FIRST. PLAYS A ROLE IN CC DETERMINING PROPER DORSAL CELL FATES LEADING TO THE FORMATION OF CC THE DORSAL APPENDAGES. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=Class 2; CC IsoId=Q24523-1; Sequence=Displayed; CC Name=Class 1; CC IsoId=Q24522-1; Sequence=External; CC Name=Class 3; CC IsoId=Q24523-2; Sequence=VSP_006670; CC -!- SIMILARITY: BELONGS TO THE TSC-22/DIP/BUN FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L42512; AAC41608.1; -. DR EMBL; AE003636; AAF53200.1; ALT_SEQ. DR EMBL; AE003636; AAF53201.1; ALT_SEQ. DR PIR; T13804; T13804. DR HSSP; P80220; 1DIP. DR FlyBase; FBgn0010460; bun. DR GO; GO:0007422; P:peripheral nervous system development; NAS. DR InterPro; IPR000580; TSC-22_Dip_Bun. DR Pfam; PF01166; TSC22; 1. DR ProDom; PD007152; TSC-22_Dip_Bun; 1. DR PROSITE; PS01289; TSC22; 1. KW Transcription regulation; Nuclear protein; Alternative splicing. FT DOMAIN 15 31 POLY-GLN. FT DOMAIN 76 86 ALA-RICH. FT DOMAIN 97 102 POLY-GLN. FT DOMAIN 237 241 POLY-SER. FT DOMAIN 249 254 POLY-GLN. FT DOMAIN 261 265 POLY-SER. FT DOMAIN 306 321 POLY-HIS. FT DOMAIN 322 328 POLY-GLN. FT DOMAIN 348 356 POLY-GLY. FT DOMAIN 607 619 POLY-GLN. FT DOMAIN 661 668 POLY-GLN. FT DOMAIN 743 746 POLY-ALA. FT DOMAIN 759 765 POLY-GLN. FT DOMAIN 795 801 POLY-GLN. FT DOMAIN 817 822 POLY-GLN. FT DOMAIN 832 838 POLY-ALA. FT DOMAIN 884 891 POLY-ALA. FT DOMAIN 927 947 GLN-RICH. FT DOMAIN 1001 1005 POLY-ALA. FT DOMAIN 1011 1014 POLY-ALA. FT DOMAIN 1069 1090 LEUCINE-ZIPPER. FT DOMAIN 1194 1201 POLY-ALA. FT VARSPLIC 1 109 Missing (in isoform Class 3). FT /FTId=VSP_006670. FT CONFLICT 10 10 K -> E (IN REF. 1). FT CONFLICT 328 328 MISSING (IN REF. 1). FT CONFLICT 801 801 Q -> QQQ (IN REF. 1). FT CONFLICT 1189 1195 QQVTSAA -> TS (IN REF. 2). SQ SEQUENCE 1211 AA; 125299 MW; 9925A9159A7051B0 CRC64; MAENQSAASK DSGHQQQHQQ QQQQQHQQHQ QPLATTSVTA ASTTSVLANQ SPTNSQASSP ENSQEALPLL RRQQSAAAAT VAAAAATVAA TTSGTSQQQQ QQHRNSISNM FDRTVNAKFK PASSNAGPGN NPVRRNSMLT PSRGVTIGGT GGNIRKLTKV SSLTSNHHFA VCYPPSNIYQ NSNNAGSNSA LQRTTSESLR LNMMSRVAAG ATPTTVSRAS SNSSLATSTS TSLAPKSSSS SGGSNSTPQQ QQQQLVSSNN SSSSSNNSFT KASSPNNNGA RSVGGAATSA ATGTTAAAGS HHHQPHHHHH HHHHHHQHHN HQQQQQQQTS LSQGHASLTV AGGSASAGGG GGGGSGSSSG TAAGGTNRKP KTTSSFEITS VTVGHPKLNA AGDTGDESAD DLDESHTDDN SRITDLENET PSMSEDTFSK EEVYYANNAL STNAPVIPTS SQYGLVVVDP IAPSLGQTIQ NVQVNVSDNI INVVSGAVTP GGTKKKDDIK ETQHRSERFK VVKIESTEPF KRGRWMCMDY LDHSSVGNGG NNNEKTGSST SEAHAATTDG GAAGVGAGSE APAHKTTQSM ILPPTQKLNE NHLEANSTDA NWNYAEQQQQ QQQQQQQQQT IVGNALTKTL PVALRNVSRS SSVTRSPNAT VEFLSPNLLA QQQQQQQQLF DSVNANAASS PNPAGDPNNM DYARTAAMQL HQTLQQLKQR EDAMDVPPGA GGYANYQNGG DSAVGAASNN NSAAAATGES QLSTSYVEQQ QQQQQPLSPA PLTPQAAPTF AAVAAGQSPN FQLEQQQQQQ QATSQIDGIV PQPFNPQQQQ QQTPQQSTAQ QAAAAANATS AVTAPPPQQT SNTSNAAVTT GQGQTMPLLS HMTSYEQQQP NLGAAAAAAA AGGTAATSVA APQAIPTLQL QSAPSTIADP QQLMVPQQQQ QQQHQEEQQQ QPQQQQQPLP PANIASASAN NSNLNLTNTN VVATGEATTN ALTLTDEQAT AALAAAFATG AAAAATGATS AAAATQQQIQ QLQQQPNAES ETESASGTSA VAIDNKIEQA MDLVKSHLMI AVREEVEVLK ERISELMDKI NKLELENSIL KSNIPQETLQ QLQLQLQLAA PPATPAIQAA PAVQSVVAPA AAGQAVQQQA AGAVAVTGVA TSPASAVVPT SIPNGSAENG SSAVESAAVS VEQQVQQVQQ VTSAAAAAAA ASVVTANGPM S // ID BX42_DROME STANDARD; PRT; 547 AA. AC P39736; Q9W390; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Puff specific protein Bx42. GN BX42 OR CG8264. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=93048378; PubMed=1424996; RA Wieland C., Mann S., von Besser H., Saumweber H.; RT "The Drosophila nuclear protein Bx42, which is found in many puffs on RT polytene chromosomes, is highly charged."; RL Chromosoma 101:517-525(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY PLAY A ROLE IN CHROMATIN STRUCTURE AND FUNCTION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: TWO TRANSCRIPTS ARE DETECTED OF SIZES 1.9 AND CC 2.2 KB. BOTH ARE DETECTED SOON AFTER FERTILIZATION AND SHOW CC RELATIVELY CONSTANT EXPRESSION DURING THE FIRST 2/3 OF CC EMBRYOGENESIS. IN 0-3 HR EMBRYOS, THE SMALLER TRANSCRIPT IS CC PREDOMINANT AND THE LEVELS OF THE TWO TRANSCRIPTS ARE SOMEWHAT CC REDUCED AT THE LATER STAGES OF DEVELOPMENT, BUT THEY ARE FOUND IN CC APPROXIMATELY CONSTANT AMOUNTS DURING LARVAL, PUPAL AND ADULT CC STAGES. THE SMALLER TRANSCRIPT IS SUSPECTED TO BE A MATERNAL CC TRANSCRIPT. CC -!- SIMILARITY: BELONGS TO THE SNW FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64536; CAA45834.1; -. DR EMBL; AE003446; AAF46444.2; -. DR EMBL; AY113364; AAM29369.1; -. DR PIR; A56575; A56575. DR FlyBase; FBgn0004856; Bx42. DR InterPro; IPR004015; SKIP_SNW. DR Pfam; PF02731; SKIP_SNW; 1. KW Nuclear protein; DNA-binding. FT DOMAIN 177 343 SNW. FT DOMAIN 383 462 SH2-LIKE DOMAIN. FT DOMAIN 209 236 PRO-RICH. FT DOMAIN 125 155 ASP/GLU-RICH (ACIDIC). FT DOMAIN 300 400 ASP/GLU-RICH (ACIDIC). SQ SEQUENCE 547 AA; 61156 MW; 01399EA291C9D557 CRC64; MSLSSLLPTP TNAIWDREDE RRLVARGAPK IGALVSAKIA APPYGQRKDW VPHTDADFGD GGAFPEIHVA QYPLGLGAPG NVGKKSDALA VRLDDKGKVK YDAIARQGHG KDKIVYSSIS QLLPAEVLAE DADELQRPDE ETVMETTEET RLALEKLTNQ KITSALPVRH AQKAGPAQYI RYTPSQQGDT FNSGAKQRVI RMVEAQLDPM EPPKFRINKK IPRGPPSPPA PVLHSPSRKV TVKEQKEWKI PPCISNWKNA KGYTIPLDKR LAADGRGLQQ VHINEKFAKM AEALYIADRK AREAVEARSQ LEKKLAQKEK EKKEDMLRMM AQRAREERAG LRNPEAAEPS GSGATGSEVR ERNDLRAERQ RERQRDRNLQ RAAPEKRSKL QKERERDISE QIALGLPAKS AGNGETLFDQ RLFNTTKGMD SGYGDDEAYN VYDKPWRDSN TLGAHIYRPS KQADSDNYGG DLDAIVNTKR FVPDKQFSGA SKEAAAGQRS GPVEFEKEED PFGLDQFLNM AKKAPKRAEE KNNERSSHSD RKRSKRD // ID BYN_DROME STANDARD; PRT; 697 AA. AC P55965; Q9VTQ7; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE T-related protein (Trp) (Brachyenteron protein). GN BYN OR TRG OR CG7260. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=95047361; PubMed=7958884; RA Kispert A., Herrmann B.G., Leptin M., Reuter R.; RT "Homologs of the mouse Brachyury gene are involved in the RT specification of posterior terminal structures in Drosophila, RT Tribolium, and Locusta."; RL Genes Dev. 8:2137-2150(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE SPECIFICATION OF THE HINDGUT AND ANAL CC PADS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: FIRST EXPRESSED AT THE BEGINNING OF NUCLEAR CC CYCLE 14 IN THE POSTERIOR TERMINAL REGION. AS CELLULARIZATION CC PROCEEDS, EXPRESSION BECOMES CONFINED TO A RING AREA ENCOMPASSING CC THE PRIMORDIUM OF THE HINDGUT AND ANAL PADS. EXPRESSION IS CC MAINTAINED IN THIS REGION UNTIL THE END OF EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 T-BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S74163; AAB32396.2; -. DR EMBL; AE003543; AAF49989.1; ALT_INIT. DR PIR; A55160; A55160. DR HSSP; P24781; 1XBR. DR FlyBase; FBgn0011723; byn. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP. DR GO; GO:0007494; P:midgut development; IMP. DR InterPro; IPR008967; P53-like. DR InterPro; IPR001699; TF_T-box. DR Pfam; PF00907; T-box; 1. DR PRINTS; PR00937; TBOX. DR SMART; SM00425; TBOX; 1. DR PROSITE; PS01283; TBOX_1; 1. DR PROSITE; PS01264; TBOX_2; 1. DR PROSITE; PS50252; TBOX_3; 1. KW Developmental protein; Transcription regulation; DNA-binding; KW Nuclear protein. FT DOMAIN 22 34 POLY-GLY. FT DNA_BIND 96 264 T-BOX. FT DOMAIN 291 298 POLY-ALA. FT DOMAIN 395 402 POLY-SER. FT DOMAIN 582 585 POLY-ALA. FT CONFLICT 321 321 E -> G (IN REF. 1). FT CONFLICT 426 426 S -> P (IN REF. 1). SQ SEQUENCE 697 AA; 72117 MW; C30FD62E20F936D5 CRC64; MTTSHILSAV DPTTGLSGNV SGGGGGGGAG GGAGSGSPQH VTHNGHGHGH GLGGVAAVSG GGASVSGNGG HRVVGGAGSP NELDRNLRIS LDDRELWLRF QNLTNEMIVT KNGRRMFPVV KISASGLDPA AMYTVLLEFV QIDSHRWKYV NGEWVPGGKA EVPPSNPIYV HPESPNFGAH WMKEPISFAK VKLTNKTNGN GQIMLNSLHK YEPRVHLVRV GSEQRHVVTY PFPETQFIAV TAYQNEEVTS LKIKYNPFAK AFLDAKERPD TLYPHDTHYG WLIPPPTHYT AAAAAVAAPP PLSIAQSHGL VASCPSVSSA ESVGPSSGGS CDRYGRSLSS RSVAPTRTTP YSRPRVVSGS GSNGSAGNAS STSPQPPSAP QTPTSLHSTS TGSVSTSVSS SSGGGIGSAP STGCFSSSYA QSGFMSVDAS PTASVFSYPS SWQSNGNYWN ATSVPGPMPM NVCSGRNISS HNSPSPTNGS PSYTTSSPSY TIHHLTPHSH QYNMAQTDIY GTGVGVGGGA GTTGSPQAAY GAAAHQVYHP TPTSPTHQLY TNAVLNAPSA LSYSASGWHN GSGAEYGLYQ NAAAAYYQPE YIPLEIGYAT HPLEPVDVSK TLDDPQAAMY KPSDEQGSVI TLECASSSLK SSHDIKIESS SLEHAGERGT VGGGAAVVSV PTAVVNGAPA VAADTWTPLT PPQSTLQ // ID BYS_DROME STANDARD; PRT; 436 AA. AC P51406; Q9W3N3; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bys protein. GN BYS OR CG1430. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 1-240 FROM N.A. RA Stewart M.J., Denell R.; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 1-35 FROM N.A. RX MEDLINE=93204998; PubMed=8384310; RA Stewart M.J., Denell R.; RT "Mutations in the Drosophila gene encoding ribosomal protein S6 cause RT tissue overgrowth."; RL Mol. Cell. Biol. 13:2524-2535(1993). CC -!- SIMILARITY: BELONGS TO THE BYSTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003442; AAF46289.1; -. DR EMBL; AY061176; AAL28724.1; -. DR EMBL; L02076; AAA28401.1; -. DR EMBL; L02074; AAD20894.1; -. DR FlyBase; FBgn0010292; bys. DR InterPro; IPR007955; Bystin. DR Pfam; PF05291; Bystin; 1. FT CONFLICT 222 240 LSQAMAQRFYNLVLLPRVR -> ARVAGNGPRGSITWCSCH FT E (IN REF. 3). SQ SEQUENCE 436 AA; 49966 MW; 62616795138A305D CRC64; MGKPKKANVA TIKNVNLEKQ ITEGRVAKNK NKDKVKLRAE ESANIDARSS QKILAAAKLQ QLELDEENFP SLVTVKKVNF SLNDGHVKED EEVNETDLMA DLDMDEDDVA AFERFQQPAQ EGKRTLHLSK MIMQKIQEKE ADIHTKISDE GSLKIEEIDP KVKEMYEGVR DVLKRYRSGK IPKAFKIIPK LRNWEQILFI TEPHNWSAAA MFQGTRIFCS VLSQAMAQRF YNLVLLPRVR DDLCEYKKLN MHLYNALKRA LFKPAAFMKG IILPLLEGGD CTLREAIIFG SVVARSSIPV LHSSACLLKI CEMAYSGANS IFIRYFLDKR YALPYRVVDA AVFHFLRFEN DKRELPVLWH QSLLTFAQRY KNDISSEQRD ALLQLLKKKS HFKITPDVRR ELQAASCRDV EMMETDNGLA GQPAKMYTDA DVEYEG // ID C131_DROME STANDARD; PRT; 492 AA. AC Q9VFJ0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 313a1 (EC 1.14.-.-) (CYPCCCXIIIA1). GN CYP313A1 OR CG3360. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003705; AAF55065.2; -. DR FlyBase; FBgn0038236; Cyp313a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 2. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 438 438 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 492 AA; 56533 MW; C713D3CC574B0DEE CRC64; MLTINLLLAV GALFWIYFLW SRRRLYFLML KIPGPIGLPI LGSSLENIIT YKRKLSFRTK YLNKYGSTIL TWMGPVPFIV TRDPKVVEDI FSSPDCHNKS QHIVNAITSC MGNGLLGKQD PHWLDRRKHF NPSFKQDLLL SFFHIFDAET KVLMNLLDTY VDKGEIDVVP EMLRWSFKIA AQTTMGSEVK HDEHFKNGSL VESFESLISH STLNILMPLV QNRMISKICG YDKLRADNFS RIQKMLDNVV NKKVNPLPKT DSDPESNIVI NRAMELYRKG DITYMDVKSE CCIMIAAGYD TSALTVYHAL FLLANHPEHQ EAVFEELNGV FPDAGHFGIT YPDMQKLDYL ERVIKETLRL IPAIPITARE TKNDVRLSNG VLIPKGVVIG IDMFHTHRNP EVWGPDADNF NPDNFLAENM EQKHPYAYIP FARGKRNCIG SKYAMMSSKF ALCRILRNYK ISTSTLYKDL VYVDNMTMKL AEYPRLKLQR RG // ID C132_DROME STANDARD; PRT; 493 AA. AC Q9VGB4; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 313a2 (EC 1.14.-.-) (CYPCCCXIIIA2). GN CYP313A2 OR CG10094. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003695; AAF54769.3; -. DR FlyBase; FBgn0038006; Cyp313a2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 438 438 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 493 AA; 56623 MW; 73B4DE8BAF994156 CRC64; MIVIQLLIAA SLILWIRFLW SRRKLYMLMM QLPGRMGLPL LGNSVRYLII SRGKMSSRTT YMDKHGSTYM AWIGTTPIVI TRDPKIAEKV LTSPFCINRS SQTTNALALS MGYGLLTLQG SKWMARRKHM NPAFKHSVLL SFLPIFNAET DLLVSVFDSF VGQGEKDVLS DLIRWSFAIA TQTTLGTDVT KDDNFENDAI LKTYQSMLRL TIINIFVPFV QNKIVSKLFG LEWLRRRDAS AINKMINNIL DKKLNSNPEN YCESELKTVI HRAIELFRND EMSLMELGAE CSSMVLAAFE TSAHTVYYAL VLLAMFPEHQ EMVFNEIKEH FPLAKGIEVT HTDLQQLVYL DRVLNETLRL MPSVPFSSRE TLEDLRLSNG VVIPKGMTIS IDIFNTQRNT DYWGSEAAQF NPENFLPEKI HDRHPYAFIP FSKGKRNCIG WRYGLMSSKL ALVKILRNYK LKTSFPYENL EFVDHMVIKL AQSPQLAFER RTL // ID C133_DROME STANDARD; PRT; 492 AA. AC Q9VGB3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 313a3 (EC 1.14.-.-) (CYPCCCXIIIA3). GN CYP313A3 OR CG10093. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003695; AAF54770.3; -. DR FlyBase; FBgn0038007; Cyp313a3. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 438 438 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 492 AA; 56195 MW; 2836D13953C3B4DC CRC64; MDTFQLLLAV GVCFWIYFLW SRRRLYMMHF KIPGPMGLPI LGIAFEYLIT YKRKMSIRTK YMDIYGSTCL VWVGPTPFVI TRDPKIAEEI FLSPECLNRS SIFSKPVNSC TGDGLLSLEA SKWVDRRKNL NPAFKQNVLL SFLPIFNSEA KTLVAFLDSL VGQGEKKVRD DIVRWSFRIA TQTTVGTDVK KDASFKNDSV LKSYETFMKI IVMNVLLPFT HNKIFSTLGG FETQKALAKS NVNKMIGTIV DKKLMTKPES GSQPEITSVI NKAIELHRNG EMSREEVQSE CCSFVVAAFE TTGDTVYHAL ILLAMFPEHQ DTVYQELKEL FPVAGDFEVT YDDLQRMVFL ERVVNETLRL IPSVPFTPRE TIRDFRLSSG VVIPKGVGIG IDIFATHRNR DHWGTDPSSF NPDHFLPDNV RDRHPYAYIP FSKGRRNCIG WKYGLMSSKL ALSKILRNCK VSTSFRYEDL EFVDNIGMEL AQSPGLEFHR RT // ID C134_DROME STANDARD; PRT; 478 AA. AC Q9VG40; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 313a4 (EC 1.14.-.-) (CYPCCCXIIIA4). GN CYP313A4 OR CG6802. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003696; AAF54850.3; -. DR FlyBase; FBgn0038076; Cyp313a4. DR InterPro; IPR001128; Cytochrome_P450. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 424 424 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 478 AA; 55243 MW; 6A731FB1E026CB30 CRC64; MLTWTLWCGL LFLLWIYFLW SRRRFYLLTL KIPGPLGYPI LGMAHWLMRR EDILNAFGCF LDKHGPTIFS WLGPIPFMIV SDPQVVQDIF TSPHCVNKGI IYKAVDDGAG VGLFSLKDPR WSIHRKLLNP AFGHKVLLSF LPIFNRETAL LLDQLEPLQD DGEKDLIPLL QSFTLGIATQ TTMGSDVKDE ESFRSNSLLG RYQCRFCRQL AGKESHYYQA KTEIRQFIRK IIERKLAEDE MGALPSIQSN DKNLFLNLVT DLMRRGVFTL KNVEDESNII VFGAFETTAN AVYYTLMLLA MFPEYQERAF EEIKTIFPNT GDFDVSYADT QQMVYLDLIL NESMRVIPPV PVVSRQTSQD LKLSNGIVVP KGVQIAIDIY HMHRSKKIWG PDAETFNPDH FLPHNIQDKH PYAYIPFTKG IRNCIGWRYA LISAKVTLAK LLRNYRFKTS FPFENLYFVE DITMKLKSVP LLELQKRT // ID C135_DROME STANDARD; PRT; 487 AA. AC Q9VGB5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 313a5 (EC 1.14.-.-) (CYPCCCXIIIA5). GN CYP313A5 OR CG15807. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003695; AAF54768.2; -. DR FlyBase; FBgn0038005; Cyp313a5. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 433 433 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 487 AA; 55618 MW; 77D2493E8F93B017 CRC64; MLTLQIFEAF AIILCVYFLW SRRRFYIMML KLPGPMGFPF IGLAFEYIRL KRKIRLRTIL FKIYGKTVLT WIGLTPVLVT CEPKILEDIF TSPNCSNRSS VVDKAISSCL GLGLLTLKNN HWNERRKLLL PSFKNNAVLS FVPVLNNEAN FLVTLLAEFV DGGDINLLPE LNKWSFKIAA QITMGDEVRN QANYQNGNLL ESYKALNNLI PIGVVMPWLR NKYLGKLFSY EKRRLEAATQ SNAFIKDIID KKLSSTDNSS EPALIDRILN LVRIGELSYD DVMGEFSNII FAASDTLSIT VNNVLILMAM FPKYQDNVFE ELAEVFPSGG EFEASHADLE KLVKLDRVLH ETMRLIPAVP LLIRQTSHSI QLSNGFYIPE GVTLMIDIFH THRNKDIWGP QANAFNPDNF LPENKRARPP YSYLPFSKGK KTCLGWKLSL ISAKLALAKI LRNYMLSTTF LYKDLRFIDN TTMKLAEQPL LAVKRRI // ID C190_DROME STANDARD; PRT; 1690 AA. AC Q9VJE5; O44929; Q8INY8; Q8MSD0; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Restin homolog (Cytoplasmic linker protein 190) (Microtubule binding DE protein 190) (d-CLIP-190). GN CLIP-190 OR CG5020. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Embryo, and Ovary; RX MEDLINE=98139549; PubMed=9472041; RA Lantz V.A., Miller K.G.; RT "A class VI unconventional myosin is associated with a homologue of a RT microtubule-binding protein, cytoplasmic linker protein-170, in RT neurons and at the posterior pole of Drosophila embryos."; RL J. Cell Biol. 140:897-910(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX MEDLINE=20530668; PubMed=11076973; RA Sisson J.C., Field C., Ventura R., Royou A., Sullivan W.; RT "Lava lamp, a novel peripheral Golgi protein, is required for RT Drosophila melanogaster cellularization."; RL J. Cell Biol. 151:905-918(2000). CC -!- FUNCTION: TOGETHER CLIP-190 AND JAR MAY COORDINATE THE INTERACTION CC BETWEEN THE ACTIN AND MICROTUBULE CYTOSKELETON. MAY LINK ENDOCYTIC CC VESICLES TO MICROTUBULES. MAY PLAY A ROLE IN FORMATION OF FURROWS CC DURING CELLULARIZATION. CC -!- SUBUNIT: INTERACTS WITH LVA. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC; MICROTUBULE-ASSOCIATED. LVA- CC CLIP-190 COMPLEXES ARE FOUND AT THE GOLGI. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=Q9VJE5-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9VJE5-2; Sequence=VSP_050479; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q9VJE5-3; Sequence=VSP_050480; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: SPECIFICALLY EXPRESSED AT THE TIP OF THE CC FURROW IN CELLULARIZING BLASTODERMS. CLIP-190 AND JAR ARE CC COEXPRESSED AT SEVERAL TIMES IN DEVELOPMENT AND IN A NUMBER OF CC TISSUES, INCLUDING EMBRYONIC AXONAL NEURON PROCESSES AND POSTERIOR CC POLE. CC -!- SIMILARITY: CONTAINS 2 CAP-GLY DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF041382; AAB96783.1; -. DR EMBL; AE003655; AAF53604.1; -. DR EMBL; AE003655; AAF53605.2; -. DR EMBL; AE003655; AAN10987.1; -. DR EMBL; AY118896; AAM50756.1; -. DR FlyBase; FBgn0020503; CLIP-190. DR GO; GO:0005938; C:cell cortex; IDA. DR GO; GO:0005794; C:Golgi apparatus; IDA. DR GO; GO:0005875; C:microtubule associated complex; IDA. DR GO; GO:0003779; F:actin binding; IDA. DR GO; GO:0008017; F:microtubule binding; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0007349; P:cellularization; IMP. DR InterPro; IPR000938; CAP-Gly. DR Pfam; PF01302; CAP_GLY; 2. DR PROSITE; PS00845; CAP_GLY_1; FALSE_NEG. DR PROSITE; PS50245; CAP_GLY_2; 2. KW Cytoskeleton; Golgi stack; Microtubule; Actin-binding; Coiled coil; KW Repeat; Alternative splicing. FT DOMAIN 143 185 CAP-GLY 1. FT DOMAIN 260 302 CAP-GLY 2. FT DOMAIN 378 468 COILED COIL (POTENTIAL). FT DOMAIN 484 660 COILED COIL (POTENTIAL). FT DOMAIN 488 1452 GLU-RICH. FT DOMAIN 667 916 COILED COIL (POTENTIAL). FT DOMAIN 926 981 COILED COIL (POTENTIAL). FT DOMAIN 1001 1121 COILED COIL (POTENTIAL). FT DOMAIN 1158 1549 COILED COIL (POTENTIAL). FT DOMAIN 1200 1461 GLN-RICH. FT DOMAIN 1565 1600 COILED COIL (POTENTIAL). FT VARSPLIC 348 348 Missing (in isoform B). FT /FTId=VSP_050479. FT VARSPLIC 1 109 MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIP FT TPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPK FT SGPPPREATSMSRESDDNLSSINSAYT -> MSRESDDNLS FT SINSAYTDLYQETVRRFTRSSLSPTPDWDRFSPARRSLKSE FT AGSRASYDYYLEATGRRRSS (in isoform FT C). FT /FTId=VSP_050480. FT CONFLICT 207 207 S -> N (IN REF. 1). FT CONFLICT 420 420 D -> G (IN REF. 1). FT CONFLICT 492 492 K -> Q (IN REF. 1). FT CONFLICT 561 561 E -> A (IN REF. 1). FT CONFLICT 614 614 T -> S (IN REF. 1). FT CONFLICT 683 683 S -> I (IN REF. 1). FT CONFLICT 692 692 N -> Q (IN REF. 1). FT CONFLICT 717 717 M -> K (IN REF. 1). FT CONFLICT 769 769 F -> L (IN REF. 1). FT CONFLICT 787 787 Q -> E (IN REF. 1). FT CONFLICT 881 881 Q -> E (IN REF. 1). FT CONFLICT 907 909 HLL -> QLQ (IN REF. 1). FT CONFLICT 920 920 G -> E (IN REF. 1). FT CONFLICT 929 929 C -> Y (IN REF. 1). SQ SEQUENCE 1690 AA; 189063 MW; D6F7916A9C532F16 CRC64; MSDDTSASGG TSAPFPSPVT ADPEPGATAS KLPGPIRSNI PTPATSGTGI PQPSKMKAPS SFGSTGSVSK IGRPCCNHTT PKSGPPPREA TSMSRESDDN LSSINSAYTD NSSAVLTANT EQFIIGQRVW LGGTRPGQIA FIGDTHFAAG EWAGVVLDEP NGKNDGCVSG KRYFQCEPKR GIFSRLTRLT TYPLAGAQTP TSPLAKSSPD RSRTVSPTAS IRSSMLRSPG IGGKNGMAVG DRVIVSSGFG SRPGILRYLG ETQFAPGNWC GVELDEPSGK NDGTVDDIRY FECKPKYGVF VPIAKVSLSP SSKKTRLSRT GSRESLTSIG TMNSIATTAT SRMRMNAQQR KSSTPVKPIL ATPKSQFSMQ DLLREKQQHV EKLMVERDLD REDAQNQALQ LQKNINELKA RIVELESALD NERKKTEELQ CSIDEAQFCG DELNAQSQVY KEKIHDLESK ITKLVSATPS LQSILPPDLP SDDGALQEEI AKLQEKMTIQ QKEVESRIAE QLEEEQRLRE NVKYLNEQIA TLQSELVSKD EALEKFSLSE CGIENLRREL ELLKEENEKQ AQEAQAEFTR KLAEKSVEVL RLSSELQNLK ATSDSLESER VNKTDECEIL QTEVRMRDEQ IRELNQQLDE VTTQLNVQKA DSSALDDMLR LQKEGTEEKS TLLEKTEKEL VQSKEQAAKT LNDKEQLEKQ ISDLKQLAEQ EKLVREMTEN AINQIQLEKE SIEQQLALKQ NELEDFQKKQ SESEVHLQEI KAQNTQKDFE LVESGESLKK LQQQLEQKTL GHEKLQAALE ELKKEKETII KEKEQELQQL QSKSAESESA LKVVQVQLEQ LQQQAAASGE EGSKTVAKLH DEISQLKSQA EETQSELKST QSNLEAKSKQ LEAANGSLEE EAKKSGHLLE QITKLKSEVG ETQAALSSCH TDVESKTKQL EAANAALEKV NKEYAESRAE ASDLQDKVKE ITDTLHAELQ AERSSSSALH TKLSKFSDEI ATGHKELTSK ADAWSQEMLQ KEKELQELRQ QLQDSQDSQT KLKAEGERKE KSFEESIKNL QEEVTKAKTE NLELSTGTQT TIKDLQERLE ITNAELQHKE KMASEDAQKI ADLKTLVEAI QVANANISAT NAELSTVLEV LQAEKSETNH IFELFEMEAD MNSERLIEKV TGIKEELKET HLQLDERQKK FEELEEKLKQ AQQSEQKLQQ ESQTSKEKLT EIQQSLQELQ DSVKQKEELV QNLEEKVRES SSIIEAQNTK LNESNVQLEN KTSCLKETQD QLLESQKKEK QLQEEAAKLS GELQQVQEAN GDIKDSLVKV EELVKVLEEK LQAATSQLDA QQATNKELQE LLVKSQENEG NLQGESLAVT EKLQQLEQAN GELKEALCQK ENGLKELQGK LDESNTVLES QKKSHNEIQD KLEQAQQKER TLQEETSKLA EQLSQLKQAN EELQKSLQQK QLLLEKGNEF DTQLAEYQKV IDEMDDAASV KSALLEQLQN RVAELETALR QANDAQKTAY LETKELRRQL ESLELEKSRE VLSLKAQMNG ASSRSGKGDE VESLDIETSL AKINFLNSII ADMQQKNDAL KAKVQTLETL PMDFTKPHAF DALTKRKPAP RLFCDICDEF DQHDTEDCPI QGSEDQDYST PSSESNNNEK ERKLPAPRKY CDSCEVFGHD TSECADDETY // ID C1TC_DROME STANDARD; PRT; 934 AA. AC O96553; Q8T0P2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE C-1-tetrahydrofolate synthase, cytoplasmic (C1-THF synthase) DE [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); DE Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9); DE Formyltetrahydrofolate synthetase (EC 6.3.4.3)]. GN PUG OR CG4067. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=99054704; PubMed=9832531; RA Rong Y.S., Golic K.G.; RT "Dominant defects in Drosophila eye pigmentation resulting from a RT euchromatin-heterochromatin fusion gene."; RL Genetics 150:1551-1566(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 569-933 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: 5,10-METHYLENETETRAHYDROFOLATE + NADP(+) = CC 5,10-METHENYLTETRAHYDROFOLATE + NADPH. CC -!- CATALYTIC ACTIVITY: 5,10-METHENYLTETRAHYDROFOLATE + H(2)O = 10- CC FORMYLTETRAHYDROFOLATE. CC -!- CATALYTIC ACTIVITY: ATP + FORMATE + TETRAHYDROFOLATE = ADP + CC PHOSPHATE + 10-FORMYLTETRAHYDROFOLATE. CC -!- PATHWAY: NECESSARY FOR THE BIOSYNTHESIS OF PURINES, THYMYDYLATE, CC METHIONINE, HISTIDINE, PANTOTHENATE, AND FORMYL TRNA-MET. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: PRESENT IN ALL TISSUES. CC -!- MISCELLANEOUS: THIS TRIFUNCTIONAL ENZYME CONSISTS OF TWO MAJOR CC DOMAINS: A N-TERMINAL PART, CONTAINING THE METHYLENE-THF CC DEHYDROGENASE AND THE METHENYL-THF CYCLOHYDROLASE ACTIVITIES AND A CC LARGER FORMYL-THF SYNTHETASE DOMAIN. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; TO OTHER DEHYDROGENASE/ CC CYCLOHYDROLASE ENZYMES OR DOMAINS. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; STRONG TO OTHER CC FORMYLTETRAHYDROFOLATE SYNTHETASE DOMAINS OR ENZYMES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF082097; AAC78847.1; -. DR EMBL; AE003688; AAG22140.1; -. DR EMBL; AY069146; AAL39291.1; ALT_INIT. DR HSSP; P11586; 1A4I. DR FlyBase; FBgn0020385; pug. DR InterPro; IPR000559; Fmtethyd_synth. DR InterPro; IPR000672; THF_Dhg_Cyh. DR Pfam; PF01268; FTHFS; 1. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR ProDom; PD002300; THF_Dhg_Cyh; 1. DR PROSITE; PS00721; FTHFS_1; 1. DR PROSITE; PS00722; FTHFS_2; FALSE_NEG. DR PROSITE; PS00766; THF_DHG_CYH_1; FALSE_NEG. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. KW Hydrolase; Ligase; Oxidoreductase; NADP; Multifunctional enzyme; KW One-carbon metabolism; ATP-binding; Purine biosynthesis; KW Amino-acid biosynthesis; Methionine biosynthesis; KW Histidine biosynthesis. FT DOMAIN 1 304 METHYLENETETRAHYDROFOLATE DEHYDROGENASE FT AND CYCLOHYDROLASE (BY SIMILARITY). FT DOMAIN 305 934 FORMYLTETRAHYDROFOLATE SYNTHETASE (BY FT SIMILARITY). FT NP_BIND 379 386 ATP (BY SIMILARITY). SQ SEQUENCE 934 AA; 99626 MW; 42CC88A69A4D5345 CRC64; MSGAKIISGT AVAKSIREEL RNEVTAMSKQ LADFVPGLRI VQVGGREDSN VYIRMKIKAA TEIGIDAAHV QLPRSITEVE LLDKINDLNE DPRVHGIIVQ MPLDCDTPID SHRITDAVSP EKDVDGLHTV NEGRLAIGDL GGFLPCTPWG CLELIRRSGV EIAGARAVVL GRSKIVGTPA AELLKWANAT VTVCHSKTRN LEEITRSADI LVVGIGVAEM VKGSWIKPGA VVIDCGINVK PDASKASGSK LVGDVDYAEA LQVAGHLTPV PGGVGPMTVA MLMKNTVRSA ARFLERLAKS QWALQTLPLK PQRPVPSDIV IARAQKPKDI AVLAKEIGLE AREVSLYGNK KAKISLSVLE RLKDKEVGHY VVVAGMTPTP LGEGKTTTLM GLVQALGAHK LRNTMAALRQ PSQGPTFGIK GGAAGGGYAQ VIPMEEFNLH LTGDIHAVSA ANNLLAAQLD TRIFHENTQK DKALYDRLVP AIKGQRKFSP IQLRRLQKLG ITKTDPDTLT ADEYGPFARL DIDPDTIMWE RVVDINDRYL RTITVGQSPT EKGISRETRF SISVASEIMA VLALSRSLED MKQRLADMVV AFDKRGKPVT ADDLGVTGAL AVLLKDALEP NLMQSLEGTP VLVHAGPFAN IAHGCNSIIA DEVGLKLVGK NGFVCTEAGF GSDIGMEKFC NIKCRTSGRK PNAMVLVATV RAIKMHGGGA PVTPGAPLNK QYTEENLELV QKGLPNLLQH IENGKAFGMP VVVSLNAHSA DTPAEHELVK KAALEAGAFA AVVSTHWADG GAGAVQLADA VIKACEQGNQ FRLLYDLELP LVDKMNKIAT TMYGAGKVVL SPAAEEKVKR LTDAGFGNLP ICMSKVSGSF TGDAKIKGAP KGFTLDVEDV YVSAGAGFVV AMCGEVTKMP GLPTRPAIYD IDLNTETGEI EGLF // ID C301_DROME STANDARD; PRT; 553 AA. AC Q9V6D6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 301a1, mitochondrial precursor (EC 1.14.-.-) DE (CYPCCCIA1). GN CYP301A1 OR CG8587. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003821; AAF58492.1; -. DR FlyBase; FBgn0033753; Cyp301a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Mitochondrion; KW Transit peptide; Hypothetical protein. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 553 PROBABLE CYTOCHROME P450 301A1. FT METAL 502 502 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 553 AA; 62824 MW; 11C1606FED169574 CRC64; MNNLSLKAWR STVSCGPNLR QCVPRISGAG SRRAQCRESS TGVATCPHLA DSEEASAPRI HSTSEWQNAL PYNQIPGPKP IPILGNTWRL MPIIGQYTIS DVAKISSLLH DRYGRIVRFG GLIGRPDLLF IYDADEIEKC YRSEGPTPFR PSMPSLVKYK SVVRKDFFGD LGGVVGVHGE PWREFRSRVQ KPVLQLSTIR RYLQPLEVIT EDFLVRCENL LDENQELPED FDNEIHKWSL ECIGRVALDT RLGCLESNLK PDSEPQQIID AAKYALRNVA TLELKAPYWR YFPTPLWTRY VKNMNFFVGV CMKYIQSATE RLKTQDPSLR AGEPSLVEKV ILSQKDEKIA TIMALDLILV GIDTISMAVC SMLYQLATRP VDQQKVHEEL KRLLPDPNTP LTIPLLDQMH HLKGFIKEVF RMYSTVIGNG RTLMEDSVIC GYQVPKGVQA VFPTIVTGNM EEYVTDAATF RPERWLKPQH GGTPGKLHPF ASLPYGYGAR MCLGRRFADL EMQILLAKLL RNYKLEYNHK PLDYAVTFMY APDGPLRFKM TRV // ID C302_DROME STANDARD; PRT; 489 AA. AC Q9NGX9; Q9VZJ0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome P450 302a1, mitochondrial precursor (EC 1.14.-.-) DE (Disembodied protein). GN DIB OR CYP302A1 OR CG12028. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=20433232; PubMed=10976044; RA Chavez V.M., Marques G., Delbecque J.P., Kobayashi K., RA Hollingsworth M., Burr J., Natzle J.E., O'Connor M.B.; RT "The Drosophila disembodied gene controls late embryonic morphogenesis RT and codes for a cytochrome P450 enzyme that regulates embryonic RT ecdysone levels."; RL Development 127:4115-4126(2000). CC -!- FUNCTION: REGULATES EMBRYONIC ECDYSONE LEVELS. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003480; AAF47831.2; -. DR EMBL; AF237560; AAF60174.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0000449; dib. DR GO; GO:0007391; P:dorsal closure; IMP. DR GO; GO:0006697; P:ecdysone biosynthesis; IMP. DR GO; GO:0008362; P:embryonic cuticle biosynthesis (sensu Insecta); IMP. DR GO; GO:0008258; P:head involution; IMP. DR GO; GO:0007494; P:midgut development; IMP. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Mitochondrion; KW Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 489 CYTOCHROME P450 302A1. FT METAL 434 434 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 186 186 C -> S (IN REF. 2). FT CONFLICT 205 205 R -> S (IN REF. 2). FT CONFLICT 252 252 S -> G (IN REF. 2). FT CONFLICT 255 255 L -> M (IN REF. 2). FT CONFLICT 327 327 R -> K (IN REF. 2). FT CONFLICT 394 394 A -> R (IN REF. 2). SQ SEQUENCE 489 AA; 55573 MW; AE1E5A97E79E502B CRC64; MLTKLLKISC TSRQCTFAKP YQAIPGPRGP FGMGNLYNYL PGIGSYSWLR LHQAGQDKYE KYGAIVRETI VPGQDIVWLY DPKDIALLLN ERDCPQRRSH LALAQYRKSR PDVYKTTGLL PTNGPEWWRI RAQVQKELSA PKSVRNFVRQ VDGVTKEFIR FLQESRNGGA IDMLPKLTRL NLELTCLLTF GARLQSFTAQ EQDPRSRSTR LMDAAETTNS CILPTDQGLQ LWRFLETPSF RKLSQAQSYM ESVALELVEE NVRNGSVGSS LISAYVKNPE LDRSDVVGTA ADLLLAGIDT TSYASAFLLY HIARNPEVQQ KLHEEARRVL PSAKDELSMD ALRTDITYTR AVLKESLRLN PIAVGVGRIL NQDAIFSGYF VPKGTTVVTQ NMVACRLEQH FQDPLRFQPD RWLQHRSALN PYLVLPFGHG MRACIARRLA EQNMHILLLR LLREYELIWS GSDDEMGVKT LLINKPDAPV LIDLRLRRE // ID C303_DROME STANDARD; PRT; 503 AA. AC Q9V399; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 303a1 (EC 1.14.-.-) (CYPCCCIIIA1). GN CYP303A1 OR L(2)35FB OR BG:DS02740.6 OR CG4163. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003415; AAF44996.1; -. DR EMBL; AE003650; AAF53514.1; -. DR HSSP; P00179; 1DT6. DR FlyBase; FBgn0001992; Cyp303a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 448 448 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 503 AA; 57877 MW; FD81F4A33861FE92 CRC64; MFYTVIWIFC ATLLAILFGG VRKPKRFPPG PAWYPIVGSA LQVSQLRCRL GMFCKVIDVF ARQYVNPYGF YGLKIGKDKV VIAYTNDAIS EMMTNEDIDG RPDGIFYRLR TFNSRLGVLL TDGEMWVEQR RFILRHLKNF GFARSGMMDI VHNEATCLLQ DLKDKVLKSG GKQTRIEMHD LTSVYVLNTL WCMLSGRRYE PGSPEITQLL ETFFELFKNI DMVGALFSHF PLLRFIAPNF SGYNGFVESH RSLYTFMSKE IELHRLTYKN YDEPRDLMDS YLRAQDEGND EKGMFSDQSL LAICLDMFLA GSETTNKSLG FCFMHLVLQP EIQERAFQEI KEVVGLERIP EWSRDRTKLP YCEAITLEAV RMFMLHTFGI PHRAVCDTRL SGYEIPKDTM VIACFRGMLI NPVDFPDPES FNPDRYLFDG HLKLPEAFNP FGFGRHRCMG DLLGRQNLFM FTTTVLQNFK MVAIPGQVPE EVPLEGATAA VKPYDIMLVA REQ // ID C304_DROME STANDARD; PRT; 510 AA. AC Q9VG17; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 304a1 (EC 1.14.-.-) (CYPCCCIVA1). GN CYP304A1 OR CG7241. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003698; AAG22150.1; -. DR HSSP; P00179; 1DT6. DR FlyBase; FBgn0038095; Cyp304a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 454 454 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 510 AA; 58790 MW; 3E20A106ADEF3BF5 CRC64; MITETLLTIC AAVFLCLSYR YAVGRPSGFP PGPPKIPLFG SYLFMLIINF KYLHKAALTL SRWYKSDIIG LHVGPFPVAV VHSADGVREI LNNQVFDGRP QLFVAAMRDP GQDVRGIFFQ DGPLWKEQRR FILRYLRDFG FGRRFDQLEL VIQEQLNDML DLIRNGPKYP HEHEMVKSGG YRVLLPLLFN PFSANAHFYI VYNECLSREE MGKLVKLCQM GIQFQRNADD YGKMLSIIPW IRHIWPEWSG YNKLNESNLF VRQFFADFVD KYLDSYEEGV ERNFMDVYIA EMRRGPGYGF NRDQLIMGLV DFSFPAFTAI GVQLSLLVQY LMLYPAVLRR VQNEIDEVVG CGRLPNLEDR KNLPFTEATI REGLRIETLV PSDVPHKALE DTELLGYRIP KDTIVVPSLY AFHSDARIWS DPEQFRPERF LDADGKLCLK LDVSLPFGAG KRLCAGETFA RNMLFLVTAT MCQHFDFVLG PNDRLPDLSQ NLNGLIISPP DFWLQLQDRH // ID C305_DROME STANDARD; PRT; 504 AA. AC Q9VW43; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 305a1 (EC 1.14.-.-) (CYPCCCVA1). GN CYP305A1 OR CG8733. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003515; AAF49108.1; -. DR EMBL; AY051626; AAK93050.1; -. DR HSSP; P00179; 1DT6. DR FlyBase; FBgn0036910; Cyp305a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 450 450 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 504 AA; 57719 MW; DD3F60A8B143CD4F CRC64; MSALIFLCAI LIGFVIYSLI SSARRPKNFP PGPRFVPWLG NTLQFRKEAS AVGGQHILFE RWAKDFRSDL VGLKLGREYV VVALGHEMVK EVQLQEVFEG RPDNFFLRLR TMGTRKGITC TDGQLWYEHR HFAMKQMRNV GYGRSQMEHH IELEAEELLG QLERTEEQPI EPVTWLAQSV LNVLWCLIAG KRIARQEDGT LRRLLDLMNR RSKLFDICGG LLAQFPWLRH VAPDRTGYNL IQQLNTELYG FFMDTIEEHR RQLAKDPSPA ESDLIYAYLQ EMKDRSAGGE SSTFNETQLV MTILDFFIAG SQTTSNTINL ALMVLAMRPD VQEKLFSQVT ASVAAASTDA FPHLSRREAF DYMDAFIMEV QRFFHITPIT GPRRALWATK LGGYDIPKNA TILISLRSVH LDKEHWKDPL EFRPERFIDS AGKCFKDEYF MPFGMGRRRC LGDALARACI FSFLVRIVQH FSVVLPAGES PSMVLLPGIT LTPKPYKVQF VKRT // ID C306_DROME STANDARD; PRT; 574 AA. AC Q9VWR5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 306a1 (EC 1.14.-.-) (CYPCCCVIA1). GN CYP306A1 OR CG6578. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003509; AAF48873.1; -. DR HSSP; P00179; 1DT6. DR FlyBase; FBgn0030948; Cyp306a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 505 505 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 574 AA; 65177 MW; 9A8A3E1747101700 CRC64; MSADIVDIGH TGWMPSVQSL SILLVPGALV LVILYLCERQ CNDLMGAPPP GPWGLPFLGY LPFLDARAPH KSLQKLAKRY GGIFELKMGR VPTVVLSDAA LVRDFFRRDV MTGRAPLYLT HGIMGGFGII CAQEDIWRHA RRETIDWLKA LGMTRRPGEL RARLERRIAR GVDECVRLFD TEAKKSCASE VNPLPALHHS LGNIINDLVF GITYKRDDPD WLYLQRLQEE GVKLIGVSGV VNFLPWLRHL PANVRNIRFL LEGKAKTHAI YDRIVEACGQ RLKEKQKVFK ELQEQKRLQR QLEKEQLRQS KEADPSQEQS EADEDDEESD EEDTYEPECI LEHFLAVRDT DSQLYCDDQL RHLLADLFGA GVDTSLATLR WFLLYLAREQ RCQRRLHELL LPLGPSPTLE ELEPLAYLRA CISETMRIRS VVPLGIPHGC KENFVVGDYF IKGGSMIVCS EWAIHMDPVA FPEPEEFRPE RFLTADGAYQ APPQFIPFSS GYRMCPGEEM ARMILTLFTG RILRRFHLEL PSGTEVDMAG ESGITLTPTP HMLRFTKLPA VEMRHAPDGA VVQD // ID C307_DROME STANDARD; PRT; 543 AA. AC Q9VRM7; Q8SZ84; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 307a1 (EC 1.14.-.-) (CYPCCCVIIA1). GN CYP307A1 OR CG10594. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 505. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003565; AAF50766.3; -. DR EMBL; AY071053; AAL48675.1; ALT_FRAME. DR FlyBase; FBgn0035618; Cyp307a1. DR InterPro; IPR001128; Cytochrome_P450. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 485 485 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 543 AA; 62447 MW; F61DE137A0F5C219 CRC64; MLAALIYTIL AILLSVLATS YICIIYGVKR RVLQPVKTKN STEINHNAYQ KYTQAPGPRP WPIIGNLHLL DRYRDSPFAG FTALAQQYGD IYSLTFGHTR CLVVNNLELI REVLNQNGKV MSGRPDFIRY HKLFGGERSN SLALCDWSQL QQKRRNLARR HCSPREFSCF YMKMSQIGCE EMEHWNRELG NQLVPGEPIN IKPLILKACA NMFSQYMCSL RFDYDDVDFQ QIVQYFDEIF WEINQGHPLD FLPWLYPFYQ RHLNKIINWS STIRGFIMER IIRHRELSVD LDEPDRDFTD ALLKSLLEDK DVSRNTIIFM LEDFIGGHSA VGNLVMLVLA YIAKNVDIGR RIQEEIDAII EEENRSINLL DMNAMPYTMA TIFEVLRYSS SPIVPHVATE DTVISGYGVT KGTIVFINNY VLNTSEKFWV NPKEFNPLRF LEPSKEQSPK NSKGSDSGIE SDNEKLQLKR NIPHFLPFSI GKRTCIGQNL VRGFGFLVVV NVMQRYNISS HNPSTIKISP ESLALPADCF PLVLTPREKI GPL // ID C308_DROME STANDARD; PRT; 490 AA. AC Q9VWR2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 308a1 (EC 1.14.-.-) (CYPCCCVIIIA1). GN CYP308A1 OR CG6585. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003509; AAF48876.2; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0030949; Cyp308a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 2. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 431 431 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 490 AA; 55712 MW; B0D4386D7216B787 CRC64; MLPLVLFILL AATLLFWKWQ GNHWRRLGLE APFGWPLVGN MLDFALGRRS YGEIYQEIYT RNPGLKYVGF YRLFNEPAIL VRDQELLRQI LVGRNFADCA DNAVYVDHQR DVLASHNPFI ANGDRWRVLR ADLVPLFTPS RVRQTLPHVA RACQLLRDQV PLGRFEAKDL ATRYTLQVVA SAIFGLDAHC LGIHMRVAHE PSRWLEWLAP LFQPSVWSLL ETMSLLHTPR LGRLIGHRYV PLPLQHWFRE LVEARSGGDN LLQWLAESKR GLGKEELAGH ATTLLLEGYE TSAMLLAFAL YELALNEDAQ RRLHIELDEV AQRHAGNLID PVALGELRYS EAALLEALRL HPAMQALQKR CTKTFTLPDQ KSGASSELKV HLGTVLVLPV QAIHLDPALY PAPNQFRPER FLNQPPMGCR FLGFGAGPRM CPGMRLGLLQ TKAALTTLLQ DHCVQLADED QCRVEVSPLT FLTASRNGIW LSFKRRTRRY // ID C310_DROME STANDARD; PRT; 492 AA. AC Q9VJ71; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 310a1 (EC 1.14.-.-) (CYPCCCXA1). GN CYP310A1 OR CG10391. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003659; AAF53683.1; -. DR FlyBase; FBgn0032693; Cyp310a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 428 428 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 492 AA; 57113 MW; 0869EACF56A21DBD CRC64; MWLLLPILLY SAVFLSVRHI YSHWRRRGFP SEKAGITWSF LQKAYRREFR HVEAICEAYQ SGKDRLLGIY CFFRPVLLVR NVELAQTILQ QSNGHFSELK WDYISGYRRF NLLEKLAPMF GTKRLSEMFG QVQKVGDHLI HHLLDRQGQG CPQEVDIQQK LRVYSVNIIA NLIYGLDINN FEHEDHILTS YLSHSQASIQ SFTLGRLPQK SSYTYRLRDL IKQSVELRED HGLIRKDILQ LLVRFRNGNE VSGDKWQLEP INDADKLLSI KRLAKVAEDL LKVSLDAVAS TVTFTLLEIL QEPLIVEKLR AEIKELSNEN GQLKFEELNG LRYMDMCLKE TLRKYPPLPI IERVCRKSYS LPNSKFTIDE GKTLMVPLLA MHRDEKYFSE PMKYKPLRFL QTANDVGQCE DKTKSNVFIG FGIGGSQCVG QNFAKLVIKV ALIKLLQNFH LELDANQVKT LKVSHRPAPF IHTKDGLKVK LKRREINTKF YS // ID C311_DROME STANDARD; PRT; 483 AA. AC Q9VYQ7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable cytochrome P450 311a1 (EC 1.14.-.-) (CYPCCCXIA1). GN CYP311A1 OR CG1488. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003488; AAN09641.1; -. DR FlyBase; FBgn0030367; Cyp311a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 430 430 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 483 AA; 54789 MW; 553329201989BF3F CRC64; MALWPLLLIT LTIWILVRKW TLLRLGSSLP GPWAFPLLGN AQMVGKLRPE YIFLVFTELR DRFGATYRLR LGPQLWVFLH SAEETRQALH DPTLRKADTF MQLEPLIGNG LLISHGAHWT RQRRLLTPAF QPQLLRSFAP AIGGHVERLV GRLGATRGAF LEVTEPLFAC LLDAIVDTSM GAQLDTQSVD HSPIIQAFHL SSKLLFKRMI NPLLSSDWIF QRTQLWRDLD EQLQVIHSQM ESVIEKRAKE LLDMGEPAGR AHNLLDTLLL AKFEGQSLSR REIRDEINTF VFAGVDTTTA AMSFVLYALA KFPETQTRLR KELQDVALDE TTDLDALNGL PYLEALIKEV LRLYTIVPTT GRQTTQSTEI GGRTYCAGVT LWINMYGLAH DKEYYPDPYA FKPERWLPED GAVAPPAFSY IPFSGGPHVC IGRRYSLLLM KLLTARLVRE FQMELSPEQA PLRLEAQMVL KAQQGINVSF LKQ // ID C312_DROME STANDARD; PRT; 510 AA. AC Q9VVN6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 312a1 (EC 1.14.-.-) (CYPCCCXIIA1). GN CYP312A1 OR CG5137. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003521; AAF49275.1; -. DR FlyBase; FBgn0036778; Cyp312a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 455 455 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 510 AA; 58804 MW; 6973570BF911E4E0 CRC64; MFWLGFGLLL LALSLYLLYV FERQSRIDRL THKWPAPPAL PFIGHLHILA KLVGPHPLRR ATEMINEHLH DHRAKLWMGT KLYLVDCNPK DIQALCSAQQ LLQKTNDYRV FENWLCEGLF TSGFEKWSHR RKIVMPAFNY TMIKQFVAVF EKQSRILLTN VAKFAESGDQ IDFLQLISCF TLDTICETAL GVSVGSQSSA KSEYLDAVKS ILVIIDKRLK NIFYRNSFIF KRTSHYKREQ ELIKTLHGFT EGIIQKRIDE INQDAENRNY QSSDAELDGV KRTLCFLDTL LLSKGPDGKP LTVKDIREEV DTIIFGGFDL TATTLNFFMY NMTLHPEHQQ RCREEVWSVC GKDKSEPISI EQVRQLEFLE ACIKETLRMY PSGPLTARKA TANCTINDFF IPKGSDVIIS PIYMGRCKDF FPDPMVFKPD RWAIGAEPKI EATTFIPFMA GARSCMGQRY AMVMLKMVLA HLLRNFLFEP LGERQVKLKL NFVITLHTVE PYLCRAKNLD // ID C313_DROME STANDARD; PRT; 502 AA. AC Q9VHP4; Q8SZA9; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 313b1 (EC 1.14.-.-) (CYPCCCXIIIB1). GN CYP313B1 OR CG9716. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003679; AAF54257.2; -. DR EMBL; AY070999; AAL48621.1; -. DR FlyBase; FBgn0037601; Cyp313b1. DR InterPro; IPR001128; Cytochrome_P450. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 449 449 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 502 AA; 58221 MW; 22F00A5B0F7E242A CRC64; MLASIILSGW LLLAWLYFLW SRRRYYKVAW QLRGPIGWPL IGMGLQMMNP ETFLQYMDGL SRQFKAPFIS WMGTSCFLYI NDPHSVEQIL NSTHCTNKGD FYRFMSSAIG DGLFTSSSPR WHKHRRLINP AFGRQILSNF LPIFNAEAEV LLQKLELEGV QHGKRLEIYQ ILKKIVLEAA CQTTMGKKMN FQHDGSLCIF KAYNGLTEVC VKRMLSPWLY PDLIYRRSGL FRLQQKVVGI LFGFIEQLLE PIVSVVAANS NPDQQRSEME MRGKSKAIFI EQVREHVERG QLSWQDVRDE ANVTIAATFE TTSTALYFTI LCLAMHPCYQ EKLHKELVTE LPPSGDINLE QLQRLEYTEM VINEAMRLFA PVPMVLRSAD QDIQLKRGDG EFLIPRGTQI GIDIYNMQRD ERVWGPLSRT YNPDAHFGLD SPQRHAFAFV PFTKGLRMCI GYRYAQMLMK LLLARIFRSY RISTEARLEE LLVKGNISLK LKDYPLCRVE RR // ID C314_DROME STANDARD; PRT; 433 AA. AC Q9VUF8; Q8T483; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 314a1 (EC 1.14.-.-) (CYPCCCXIVA1). GN CYP314A1 OR CG13478. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003534; AAF49727.2; -. DR EMBL; AY089309; AAL90047.1; -. DR FlyBase; FBgn0036432; Cyp314a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 381 381 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 433 AA; 49016 MW; 21A4C62F0940D147 CRC64; MPSNVPIVHL YNRDDLEKVL KYPSKYPFRP PTEIIVMYRQ SRPDRYASVG IVNEQGPMWQ RLRSSLTSSI TSPRVLQNFL PALNAVCDDF IELLRARRDP DTLVVPNFEE LANLMGLEAV CTLMLGRRMG FLAIDTKQPQ KISQLAAAVK QLFISQRDSY YGLGLWKYFP TKTYRDFARA EDLIYDVISE IIDHELEELK KSAACEDDEA AGLRSIFLNI LELKDLDIRD KKSAIIDFIA AGIETLANTL LFVLSSVTGD PGAMPRILSE FCEYRDTNIL QDALTNATYT KACIQESYRL RPTAFCLARI LEEDMELSGY SLNAGTVVLC QNMIACHKDS NFQGAKQFTP ERWIDPATEN FTVNVDNASI VVPFGVGRRS CPGKRFVEME VVLLLAKMVL AFDVSFVKPL ETEFEFLLAP KTPLSLRLSD RVF // ID C315_DROME STANDARD; PRT; 520 AA. AC Q9VGH1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 315a1 (EC 1.14.-.-) (CYPCCCXVA1) (Shadow DE protein). GN SAD OR CYP315A1 OR CG14728. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003693; AAF54711.1; -. DR FlyBase; FBgn0003312; sad. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 466 466 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 520 AA; 59630 MW; 6DC4A2CCD8E07BC6 CRC64; MTEKRERPGP LRWLRHLLDQ LLVRILSLSL FRSRCDPPPL QRFPATELPP AVAAKYVPIP RVKGLPVVGT LVDLIAAGGA THLHKYIDAR HKQYGPIFRE RLGGTQDAVF VSSANLMRGV FQHEGQYPQH PLPDAWTLYN QQHACQRGLF FMEGAEWLHN RRILNRLLLN GNLNWMDVHI ESCTRRMVDQ WKRRTAEAAA IPLAESGEIR SYELPLLEQQ LYRWSIEVLC CIMFGTSVLT CPKIQSSLDY FTQIVHKVFE HSSRLMTFPP RLAQILRLPI WRDFEANVDE VLREGAAIID HCIRVQEDQR RPHDEALYHR LQAADVPGDM IKRIFVDLVI AAGDTTAFSS QWALFALSKE PRLQQRLAKE RATNDSRLMH GLIKESLRLY PVAPFIGRYL PQDAQLGGHF IEKDTMVLLS LYTAGRDPSH FEQPERVLPE RWCIGETEQV HKSHGSLPFA IGQRSCIGRR VALKQLHSLL GRCAAQFEMS CLNEMPVDSV LRMVTVPDRT LRLALRPRTE // ID C316_DROME STANDARD; PRT; 478 AA. AC Q9VS78; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 316a1 (EC 1.14.-.-) (CYPCCCXVIA1). GN CYP316A1 OR CG8540. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003558; AAF50550.2; -. DR FlyBase; FBgn0035790; Cyp316a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 427 427 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 478 AA; 55682 MW; D2F01D2FF9C9EE87 CRC64; MILTATFICF CLASAFNYFR ARRQRSLIKN LKGPFTWPLM GAMHKLLFLT PINFFQRSTE YLTKYGTFSR CWVFHRLFIP LADLELSRQL LENDTHLETG YELMKDWLVG GVLMCQSEQW QKRHSLISGL FDKGNLEQLI DLSRHQTEQL LQKLAKQADQ KVFDIWYTVS PIVLDLMVMT TCGAKPSEEY SKNLKDLSEI YRKRFLSLQS ANRFNYWLSS PFMRKRQNRL IKRLNDEHNN LMAMHQSQNQ LKIENGLDIY QLRPIPLKDH KSLLEILLES KDPQLTGEEI CGELNTCNYL GYQLCSPALC FCLVTIARNP SVQQKCLDEL NLAQIKDQGW DLEKLNYLDA VLHETMRLYP PQVIVGRQLK KDFPYNAELP CGSEIYINLY ELQRNEVRYP KANHFDAQRF LDSPPELLSY SLGPRCCPAR KFSMQLLKTL LAPILANFEV LPYGDEVRLD LRLVLGSSNG FQLALKPR // ID C317_DROME STANDARD; PRT; 518 AA. AC Q9V776; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 317a1 (EC 1.14.-.-) (CYPCCCXVIIA1). GN CYP317A1 OR CG17453. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Nelson B.; RL Unpublished observations (SEP-2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003812; AAF58184.1; ALT_SEQ. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0033982; Cyp317a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 461 461 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 518 AA; 60321 MW; 84792C97D4FAD32A CRC64; MWIIFLIIGL LVLGLLVLLI IAARYQRDYW RYLDIPHERP KKLWPIIRQI MTQTLSTEAM KAEHYSAIYK KFKGSGPFCG FYALLQPRAL ILDRELIRQI MIKDFWNFND RGLYCNQKSD PLSGDLYALR GESWKEMRQK LDPSLEGDRM SLLYDCLYEE AEQLLLTVNS TLMSQPHSTV HIQKIMRRYV LSSLAKCVFG LNAEQRKTYP LEDFEQMTEL ALNSHKHGYL MNLMMIRFPN FCRMLRMRRT PKQAEEYFIK LLTSIVEQRE TSGKPQKDYL QLLIDVKALE FITYQYEADK ELGAHLQNEL AAHADVFLKA GYEQTANTLS YVLYELALHP ELQVRVREEV KKAIERHDGH ITHEGIKSLS FMGQVINETL RMHPITPYIL RRTLNDYAVP DHPKYILVKE LFLIIPTHAI HHDPDIYPDP EEFKPDRWSG PRDSLQEQGT WFGFGVGARS CIGIQFAQLQ LRLALALLLS EYEFSLNTRK PLINLEDGIA LTLMPLGVIE PGNEERAV // ID C318_DROME STANDARD; PRT; 528 AA. AC Q9VYQ5; Q9VYQ6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 318a1 (EC 1.14.-.-) (CYPCCCXVIIIA1) DE (Fragments). GN CYP318A1 OR CG1786/CG11364. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003488; AAF48136.2; -. DR FlyBase; FBgn0030369; Cyp318a1. DR InterPro; IPR001128; Cytochrome_P450. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT NON_CONS 210 211 FT METAL 469 469 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 528 AA; 60754 MW; 02B291E7545E2E1D CRC64; MCCLQSTTLD RKKNASWNRS AIVGSDTSDA PEHCPLCGAL LAVLLAWQQR KCWRLIWQLN GWRGVIQQPV LWLLLCINLH PNSILEKVSQ YRVHFQRPLA VLVGTRVLLY IDDPAGMECV LNAPECLDKT FLQDGFFVRR GLLHARGQKW KLRRKQLNPA FSHNIVASFF DVFNSVGNQM VEQFQTQTNL HGQAVKFTAA EDLLSRAVLE EESKKCAKLL EDFVGGIVRT KHRNWRLRDA VGGEKSGEDA SNGWQRRIFI EQIFQLAANG EMTLEEIMDE AQSMVLVVGL KISYLNTIYF IFYCNFQSFE TVSNSIMLAL LCLATNKGDC QRRLLAEIRA LVPDVGQVGL EQLQQLRYLD AFVSESLRLL ATVPMNLRHV SRDFRLAGRQ HETIVPQNSI VVLDTFNMQR DERWWGANAR QFDPQRFLDQ EEEQLSKGHN DSGSGEKRRQ RDRRHSYSFL PFSNGLRSCI GRRYGLFIMK VFLVKLITNF DFQSDFELEK LQFVENISLK FKNADDILLT IQPKKEST // ID C391_DROME STANDARD; PRT; 506 AA. AC Q9VQD2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 309a1 (EC 1.14.-.-) (CYPCCCIXA1). GN CYP309A1 OR CG9964. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003582; AAF51243.2; -. DR EMBL; AY071367; AAL48989.1; -. DR FlyBase; FBgn0031432; Cyp309a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 452 452 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 506 AA; 57362 MW; C501CA70E567A0EA CRC64; MFTLVGLCLT IVHVAFAVVY FYLTWYHKYW DKRGVVTAEP LTILGSYPGI LINKSRSLIL DVQDVYNKYK DKYRTVGTFI TRQPQLLVLD PALAHEILVD KFSHFRDTIT SSFVGHNPDD KYVAGSPFFS AGDKWKRLRS ENVGGLTPSR LKMAYSIWEQ SGRKLVEYIE RARREQGDII ETRDLAYRFT ANAMADFIWG IDAGSLSGKV GEIGDFQKTS TDWSAHAFSS MIRFNKTLVA IFVRKLFSMR FFTKATDEFF LRLTQDAVNL RQGGSGEGRT DYLSHLIQLQ QRGNSIHDSV GHALTVHLDG FETSGAVLYH MLYSLSEHHE EQEKLRSEIL EALASEGQIS YDQINNLPYL DQCFNESLRL TTPIGFFMRI CTKPTQINLG DDKTLDLEPG VTVMVPAYQY HHDNDIYPEA SEFRPDRFEN GAASVLTKRG CFLPFGDGPR ICLGMRVGQL SVKTAIVHIL SNYQVEQMKK VPLGADSGMG IFLNGDVELK YTKLQK // ID C392_DROME STANDARD; PRT; 538 AA. AC P82713; Q8T422; Q9VQD3; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 309a2 (EC 1.14.-.-) (CYPCCCIXA2). GN CYP309A2 OR CG18559. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003582; AAF51242.3; -. DR EMBL; AY089391; AAL90129.1; -. DR FlyBase; FBgn0041337; Cyp309a2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 483 483 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 130 130 S -> G (IN REF. 3). FT CONFLICT 240 240 M -> L (IN REF. 3). FT CONFLICT 248 248 E -> Q (IN REF. 3). FT CONFLICT 373 373 C -> S (IN REF. 3). FT CONFLICT 419 419 R -> K (IN REF. 3). SQ SEQUENCE 538 AA; 62375 MW; B9F459671C8C6DB7 CRC64; MMPERFSFDF RPIDQYWTRA KGACSNTKRG NMYILASLAL ILLHLLVLPI YLYLTWHHKY WRKRGLVTAR PLTLLGTYPG LLTRKSNLVF DVQKIYDKYK GKHRAVGVFV TRQPQILVLD PELAHEVLVS NFRCYKDSLQ SSYLRHAKWD KYARLNPFWA SGQSWRRLRT DAQAGISGSR LRQAYNIWEQ GGQMLTEYMT QQVAEKNNIL ETRDLCFRYT AHVMADFIWG IDAGTLTRPM EQPNKVQEMA SKWTSYAFYM LTLFMATIVA PCSRLLLRFR FYPKETDEFF SNLTKESIEL RLKAGDSTRT DYLSHLLQLR DQKQATHDDL VGHALTVMLD GYDTSGTALL HALYYLAENP AVQQKLRVEI LSCMASEKSL DFEKLSSLQY LEQVIYESLR LSSLIPQYTK VCTLPTVIRL SESKSLDVEV GMTIMIPNYQ FHHDKQYFPE PEAFKPERFD NGAYQELMRK GIFLPFSDGP RICMGVPLAM LTLKSALVHI LSNFQVVRGR DRLIPKGDSG FGVVLQGDVN LEYRRFFR // ID C3G_DROME STANDARD; PRT; 1571 AA. AC O77086; Q9W3W3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-releasing factor 2 (CRK SH3-binding GNRP). GN C3G OR CG3126. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM SHORT), AND CHARACTERIZATION. RC TISSUE=Eye imaginal disk; RX MEDLINE=99094900; PubMed=9878058; RA Ishimaru S., Gaul U., Hanafusa H.; RT "Activation of the Drosophila C3G leads to cell fate changes and RT overproliferation during development, mediated by the RAS-MAPK RT pathway and RAP1."; RL EMBO J. 18:145-155(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 1036-1571 FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: GUANINE NUCLEOTIDE-RELEASING PROTEIN THAT BINDS TO SH3 CC DOMAIN OF CRK. TRANSDUCES SIGNALS FROM CRK TO ACTIVATE RAS. ALSO CC INVOLVED IN MAPK ACTIVATION. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=O77086-1; Sequence=Displayed; CC Name=Short; CC IsoId=O77086-2; Sequence=VSP_001823; CC -!- TISSUE SPECIFICITY: UBIQUITOUS. CC -!- DEVELOPMENTAL STAGE: THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: CONTAINS 1 N-TERMINAL RAS-GEF DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RAS-GEF DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 39. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 1366. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF053358; AAC35280.1; ALT_FRAME. DR EMBL; AE003438; AAF46200.2; -. DR EMBL; AY113355; AAM29360.1; ALT_FRAME. DR FlyBase; FBgn0026145; C3G. DR GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; IMP. DR GO; GO:0007265; P:RAS protein signal transduction; IMP. DR InterPro; IPR008937; Ras_GEF. DR InterPro; IPR000651; RasGEFN. DR InterPro; IPR001895; RasGRF_CDC25. DR Pfam; PF00617; RasGEF; 1. DR Pfam; PF00618; RasGEFN; 1. DR SMART; SM00147; RasGEF; 1. DR SMART; SM00229; RasGEFN; 1. DR PROSITE; PS00720; RASGEF; 1. DR PROSITE; PS50009; RASGEF_CAT; 1. DR PROSITE; PS50212; RASGEF_NTER; 1. KW Guanine-nucleotide releasing factor; SH3-binding; KW Developmental protein; Alternative splicing. FT DOMAIN 49 69 HIS-RICH. FT DOMAIN 186 193 POLY-GLY. FT DOMAIN 195 198 POLY-SER. FT DOMAIN 213 216 POLY-PRO. FT DOMAIN 238 247 POLY-GLY. FT DOMAIN 639 644 POLY-GLN. FT DOMAIN 699 702 POLY-ALA. FT DOMAIN 735 802 SER-RICH. FT DOMAIN 787 791 POLY-THR. FT DOMAIN 806 814 POLY-GLN. FT DOMAIN 815 818 POLY-THR. FT DOMAIN 1170 1292 N-TERMINAL RAS-GEF. FT DOMAIN 1462 1465 POLY-SER. FT SITE 546 556 SH3-BINDING (POTENTIAL). FT SITE 820 831 SH3-BINDING (POTENTIAL). FT SITE 924 935 SH3-BINDING (POTENTIAL). FT SITE 986 997 SH3-BINDING (POTENTIAL). FT VARSPLIC 668 718 Missing (in isoform Short). FT /FTId=VSP_001823. FT CONFLICT 19 19 H -> Y (IN REF. 1). FT CONFLICT 93 93 N -> S (IN REF. 1). FT CONFLICT 154 154 E -> V (IN REF. 1). FT CONFLICT 202 202 I -> T (IN REF. 1). FT CONFLICT 243 243 G -> GAG (IN REF. 1). FT CONFLICT 450 453 RYSG -> HYRR (IN REF. 1). FT CONFLICT 477 477 V -> I (IN REF. 1). FT CONFLICT 807 807 L -> Q (IN REF. 1). FT CONFLICT 818 818 T -> TT (IN REF. 1). FT CONFLICT 851 851 V -> A (IN REF. 1). FT CONFLICT 1004 1004 S -> N (IN REF. 1). FT CONFLICT 1092 1092 L -> M (IN REF. 2). FT CONFLICT 1127 1127 P -> A (IN REF. 2). FT CONFLICT 1311 1311 G -> S (IN REF. 2). SQ SEQUENCE 1571 AA; 172049 MW; B9EF9E8670457684 CRC64; MPQFDESFLS DCALADRWHF YSYTVKQLPP HPSPKPNRNR NPYPSGASHD DHQHQLHHHH HQQHHHNHHR LWKTQRQSWS PRDTNNNHSL TSNNCNCNSS NTCNSISATG NTLHSIKFHR RRKYKKLARL ALSTPAIPLQ MDVDVDVNVT VDREFDMEMD TPVPLKNAVC HGSISSPSTP GTCSSGIGVG GGGCSSSSNN SINSGSYSTA CTPPPPTHQH HSQHQQLQGT PGGSSRVGGA GAGGGGGVPP APPSAGSSGH KNSLKGTKLA RRARSFKDDL IEKISLMRTT NNTLGRSHSP HSPRTKHGTK APPTTEEVLR STQTLETHVK DISNALKHFR DVILKKKLEV LPGNGTVILE TIASMYSVIQ TYTLNENSAI MSSATLQVYQ SLGKLIKLCD EVMLSEDSGE CASLSNENVR EVIDLLEDAV RNLVTLAQGK LKEQDQCAFR YSGSGLGGIG AAAEIMGAVT ASPGASVPGT GVMRVSAAES AAQRTSLPDI ALTPKERDIL EQHNVNPMRG SHSTESILRD TSPPPKPPLP NRASNPPPLP PKRRSQPSAS AGTVGVGCSS STSTSNQASP LPYAQSHNIS LNSDLDCSSN ISLLNYGVDR LSVRSRSPDE NSQCSFDSAL NHSREEEDQQ QQHQHLRSFP KLAAMMDEDM DKMVSYSAAI DDKTQTPLST GGGIAGVAGG TGGAGEGVAA AASGDGETNS NRHSNESGFV SMREFRTSTQ TTDYSVQSST KSSSSNSEIA FSISESTAVG SSSEYQQISQ LVSHSQRHIS SSSSSCTTTT TSSSTTTGYG SSEVEQLQQQ QQQQTTTTPA DLAPALPPKS IQRSSLTRHD SPGVGDELDE VQSSSGWASH RSSQSEVAEL RQLSPLHHLN HHPHTASAGQ LQQWHSKHHS LIEGPRLQLA GSGSCSAFDQ RHLDQEPPPL PIKKKHILAY MEICSASTRS IEQHRHTMHA CNISRNISHS QTMNIMPMSK ELSPELEMPP ALPPKNYKQR KATSMVASPT LQPVIVTTPP PSPKPTLGEN GSTGRPDSRM ATVCEELNDA VASEDAMPEP RSPVLDSNEN VSAVDDGQTF YCHSHQLPAA ELEMSEDASS ADNQPITTPQ VLEEQEEPTA ESRPLVPVHE SVKPANVDED EEAERADMLI NMLEEVNITR YLILKKREED GPEVKGGYID ALIVHASRVQ KVADNAFCEA FITTFRTFIQ PIDVIEKLTH RYTYFFCQVQ DNKQKAAKET FALLVRVVND LTSTDLTSQL LSLLVEFVYQ LVCSGQLYLA KLLRNKFVEK VTLYKEPKVY GFVGELGGAG GVGGAGIAGS GGCSGTAGGG NQPSLLDLKS LEIAEQMTLL DAELFTKIEI PEVLLFAKDQ CEEKSPNLNK FTEHFNKMSY WARSKILRLQ DAKEREKHVN KFIKIMKHLR KMNNYNSYLA LLSALDSGPI RRLEWQKGIT EEVRSFCALI DSSSSFRAYR QALAETNPPC IPYIGLILQD LTFVHVGNQD YLSKGVINFS KRWQQYNIID NMKRFKKCAY PFRRNERIIR FFDNFKDFMG EEEMWQISEK IKPRGRRPVN Y // ID C49A_DROME STANDARD; PRT; 589 AA. AC Q9V5L3; Q8MZH1; Q8SY18; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 49a1 (EC 1.14.-.-) (CYPXLIXA1). GN CYP49A1 OR CG18377/CG12894. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=Q9V5L3-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9V5L3-2; Sequence=VSP_000616, VSP_000617, VSP_000618; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q9V5L3-3; Sequence=VSP_000616, VSP_000617; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003829; AAF58791.3; -. DR EMBL; AE003829; AAF58793.2; -. DR EMBL; AE003829; AAM68760.1; -. DR EMBL; AY075453; AAL68266.1; -. DR EMBL; AY102688; AAM27517.1; ALT_SEQ. DR FlyBase; FBgn0033524; Cyp49a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Alternative splicing; Hypothetical protein. FT METAL 536 536 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT VARSPLIC 1 174 Missing (in isoform B and isoform C). FT /FTId=VSP_000616. FT VARSPLIC 175 177 MPH -> MEL (in isoform B and isoform C). FT /FTId=VSP_000617. FT VARSPLIC 336 589 Missing (in isoform B). FT /FTId=VSP_000618. FT CONFLICT 461 461 S -> N (IN REF. 3; AAL68266). SQ SEQUENCE 589 AA; 65901 MW; A0DE2D1118807817 CRC64; MSGLRKTSIA LMRRSTSSTT ILPHSGGVGG AVSPPSSGVG VATEIEKSIA MQRLRTGESS NPKKLNVSQQ PVTSVATTRT TASSLPAETT SSPAAAVRPY SEVPGPYPLP LIGNSWRFAP LIGTYKISDL DKVMNELHVN YGKMAKVGGL IGHPDLLFVF DGDEIRNIFK KEEAMPHRPS MPSLRHYKGD LRRDFFGDVA GLIGVHGPKW EAFRQEVQHI LLQPQTAKKY IPPLNDIASE FMGRIELMRD EKDELPANFL HELYKWALES VGRVSLDTRL GCLSPEGSEE AQQIIEAINT FFWAVPELEL RMPLWRIYPT KAYRSFVKAL DQFTAICMKN IGKTMDKADA DEARGLSKSE ADISIVERIV RKTGNRKLAA ILALDLFLVG VDTTSVAASS TIYQLAKNPD KQKKLFDELQ KVFPHREADI NQNVLEQMPY LRACVKETLR MRPVVIANGR SLQSDAVING YHVPKGTHVI FPHLVVSNDP AYFPEPKRFL PERWLKQSTD AAGCPHANQK IHPFVSLPFG FGRRMCVGRR FAEIELHTLL AKIFRKYKVS YNSGEFVYRV NSTYIPQSPL NFKLTLRDE // ID C4A1_DROME STANDARD; PRT; 509 AA. AC Q9VMS9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4ac1 (EC 1.14.-.-) (CYPIVAC1). GN CYP4AC1 OR CG14032. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003609; AAF52232.1; -. DR EMBL; AY051602; AAK93026.1; -. DR FlyBase; FBgn0031693; Cyp4ac1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 454 454 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 509 AA; 59185 MW; 0DA7F612D1A6D149 CRC64; MWIALLGIPI LLAVLTLLLK HINKTYFILS LTKRVRTEDG SPLESKVAIM PGKTRFGNNL DILNFTPASV FNFVRESTAK AKGQNYLWYF LYAPMYNVVR PEEAEEVFQS TKLITKNVVY ELIRPFLGDG LLISTDHKWH SRRKALTPAF HFNVLQSFLG IFKEECKKFL NVLEKNLDAE LELNQVIPPF TLNNICETAL GVKLDDMSEG NEYRKAIHAI EEVLIQRVCN PLMYYNWYFF VYGDYRKHLQ NLRIVHDFSS RIIERKRQQF QQKQLGEVDE FGRKQRYAML DTLLAAEADG QIDHQGICDE VNTFMFEGYD TTSTCLIFTL LMLALHEDVQ KKCYEEVENL PEDSDDISMF QFNKLVYLEC VIKESLRMFP SVPFIGRQCV EETVVNGMVM PKDTQISIHI YDIMRDPRHF PKPDLFQPDR FLPENTVNRH PFAYVPFSAG QRNCIGQKFA ILEMKVLLAA VIRNFKLLPA TQLEDLTFEN GIVLRTQENI KVKLSKRVK // ID C4A2_DROME STANDARD; PRT; 497 AA. AC Q9VMS8; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4ac2 (EC 1.14.-.-) (CYPIVAC2). GN CYP4AC2 OR CG17970. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003609; AAF52233.3; -. DR FlyBase; FBgn0031694; Cyp4ac2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 441 441 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 497 AA; 57723 MW; 93BCF2183957DA04 CRC64; MFLEVLFAAP LVIFIFRKLW AHLNRTYFIL SLCKRIRTED GSLLESKIYV APSKTRFGNN FDLVNFTSES IFNFMRDASA KAKGRNYLWY FFHAPMYNIV RAEEAEEILQ SSKLITKNMI YELLKPFLGE GLLISTALSI FREECNKLVK VLHQSVNMEL ELNQVIPQFT LNNVCGNAIN VIAETALGVK LDDLSEGIRY RQSIHAIEEV MQQRLCNPFF YNIVYFFLFG DYRKQVNNLK IAHEFSSNII EKRRSLFKSN QLGQEDEFGK KQRYAMLDTL LAAEADGQID HQGICDEVNT FMFEGYDTTS TCLIFTLLML ALHEDVQKKC YEEIKYLPDD SDDISVFQFN ELVYMECVIK ESLRLFPSVP FIGRRCVEEG VVNGLIMPKN TQINIHLYEI MRDARHFSNP KMFQPDRFFP ENTVNRHPFA FVPFSAGQRN CIGQKFAILE IKVLLAAVIR NFKILPVTLL DDLTFENGIV LRTKQNIKVK LVHRENK // ID C4A3_DROME STANDARD; PRT; 509 AA. AC Q9VMS7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4ac3 (EC 1.14.-.-) (CYPIVAC3). GN CYP4AC3 OR CG14031. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003609; AAF52234.2; -. DR EMBL; AY061002; AAL28550.1; -. DR FlyBase; FBgn0031695; Cyp4ac3. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 454 454 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 509 AA; 58821 MW; 01DF7D926C91E537 CRC64; MWIALLGSSL LIGALWLLLR QLNKTYFILS LCKRVRTADG SPLESKVFVV PGKTRFGNNL DLLNLTPANI FSYIRESTAK ANGQNYIWNF LFAPEYNIVR AEDAEEIFQS TKITTKNMSY ELIRPFLGDG LLISIDQKWH TRRKTLTPAF HFNILQSFLS IFKEESKKFI KILDKNVGFE LELNQIIPQF TLNNICETAL GVKLDDMSEG NEYRKAIHDF EIVFNQRMCN PLMFFNWYFF LFGDYKKYSR ILRTIHGFSS GIIQRKRQQF KQKQLGQVDE FGKKQRYAML DTLLAAEAEG KIDHQGICDE VNTFMFGGYD TTSTSLIFTL LLLALHADVQ ERCYEELQDL PEDIDEVSMF QFNELIHLEC VIKESLRLFP SAPIIGRTCI EESVMNGLVL PKNAQISIHI YDIMRDARHF PKPNQFLPER FLPENSVNRH PFAFVPFSAG PRNCIGQKFG VLEIKVLLAA VIRNFKLLPA TQLEDLTFEN GIVLRTQQNI KVKFEARVK // ID C4AA_DROME STANDARD; PRT; 514 AA. AC Q9V7G5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4aa1 (EC 1.14.-.-) (CYPIVAA1). GN CYP4AA1 OR CG8302. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003808; AAF58091.1; -. DR FlyBase; FBgn0034053; Cyp4aa1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 454 454 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 514 AA; 58975 MW; CB84E46C73ED7B3A CRC64; MHLRLLSPPQ LERTTNLELC SILILLVISL SIYTFYATLN TYLRSVLLSL RLTGPPSLPF LGNCMLVTDK DLMRRCAGKA FDLYGSLVRI WVLLFPFFAV LEPEDLQVIL SSKKHTNKVF FYRLMHNFLG DGLITSSGSK WSNHRRLIQP AFHHNLLEKF IDTFVDASQS LYENLDAEAV GTEINIAKYV NNCVLDILNE AVLGVPIKKR GQDVAMMEDS PFRQGKIMMP ARFTQPWLLL DGIYHWTKMA NDELNQKKRL NDFTRKMIQR RRQIQNNNNG NSERKCLLDH MIEISESNRD FTEEDIVNEA CTFMLAGQDS VGAAVAFTLF LLTQNPECQD RCVLELATIF EDSNRAPTMT DLHEMRYMEM CIKEALRLYP SVPLIARKLG EEVRLAKHTL PAGSNVFICP YATHRLAHIY PDPEKFQPER FSPENSENRH PYAFLPFSAG PRYCIGNRFA IMEIKTIVSR LLRSYQLLPV TGKTTIAATF RITLRASGGL WVRLKERDHP LIAH // ID C4AD_DROME STANDARD; PRT; 516 AA. AC Q9V4T3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4ad1 (EC 1.14.-.-) (CYPIVAD1). GN CYP4AD1 OR CG2110. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003837; AAF59092.1; -. DR EMBL; AY061058; AAL28606.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0033292; Cyp4ad1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 445 445 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 516 AA; 58870 MW; 648EA22492AF58C7 CRC64; MFLIAIAIIL ATILVFKGVR IFNYIDHMAG IMEMIPGPTP YPFVGNLFQF GLKPAEYPKK VLQYCRKYDF QGFRSLVFLQ YHMMLSDPAE IQNILSSSSL LYKEHLYSFL RPWLGDGLLT SSGARWLKHQ KLYAPAFERS AIEGYLRVVH RTGGQFVQKL DVLSDTQEVF DAQELVAKCT LDIVCENATG QDSSSLNGET SDLHGAIKDL CDVVQERTFS IVKRFDALFR LTSYYMKQRR ALSLLRSELN RIISQRRHQL AAENTCQQGQ PINKPFLDVL LTAKLDGKVL KEREIIEEVS TFIFTGHDPI AAAISFTLYT LSRHSEIQQK AAEEQRRIFG ENFAGEADLA RLDQMHYLEL IIRETLRLYP SVPLIARTNR NPIDINGTKV AKCTTVIMCL IAMGYNEKYF DDPCTFRPER FENPTGNVGI EAFKSVPFSA GPRRCIAEKF AMYQMKALLS QLLRRFEILP AVDGLPPGIN DHSREDCVPQ SEYDPVLNIR VTLKSENGIQ IRLRKR // ID C4AE_DROME STANDARD; PRT; 496 AA. AC O46054; Q24129; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4ae1 (EC 1.14.-.-) (CYPIVAE1). GN CYP4AE1 OR CYP4E4 OR EG:152A3.6 OR CG10755. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 309-434 FROM N.A. RC STRAIN=Haag-79; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003423; AAF45742.1; -. DR EMBL; AL009194; CAA15700.1; -. DR EMBL; AY058450; AAL13679.1; -. DR EMBL; U34331; AAA80665.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0015036; Cyp4ae1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 443 443 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 319 319 L -> P (IN REF. 4). SQ SEQUENCE 496 AA; 56274 MW; BD0DB620F008EB68 CRC64; MLVVLLVALL VTRLVASLFR LALKELRHPL QGVVPSVSRV PLLGAAWQMR SFQPDNLHDK FAEYVKRFGR SFMGTVLGHV VMVTAEPRHI DALLQGQHQL KKGTMYFALR GWLGDGLLLS RGKEWHTMRK IITPTFHFSI LEQFVEVFDR QSSILVERLR TLSYGNEVVN IYPLVGLAAL DIITETAMGV NVDAQGADSE VVHAVKDLTN ILATRFMRPH LLFPHLFRLC WPSGFRKQQA GVICLHEFTN GIIEQRRRLL AREANQDKPT KPHALLDTLL RATVDGQPLT DKQIRDEVNT FIFEGHDTTT SAVSFCLYLL SRHEAVQQKL FEELRMHYGQ DLFRGVILSD FATLPYLSCV VKESLRLYPP IPAVARCLEK DLVIDEGYIP VGTNVVVLLW QLLRDEAIFT DPLVFQPERH LGEEAPRLSP YSYIPFSAGP RNCIGQKFAL LEMKTMVTKV IRHYQLLPMG ADVEPSIKIV LRSKSGVNVG LRPRLY // ID C4C3_DROME STANDARD; PRT; 535 AA. AC Q9VA27; Q24121; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome P450 4c3 (EC 1.14.-.-) (CYPIVC3). GN CYP4C3 OR CG1438. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 347-472 FROM N.A. RC STRAIN=Haag-79; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003775; AAF57098.1; -. DR EMBL; BT010108; AAQ22577.1; -. DR EMBL; U34323; AAA80657.1; -. DR FlyBase; FBgn0015032; Cyp4c3. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 481 481 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 535 AA; 60757 MW; 0C78200AC2D35979 CRC64; MSSKVITSLM AESILLSKVG QVISGYSPIT VFLLGSILIF LVVYNKRRSR LVKYIEKIPG PAAMPFLGNA IEMNVDHDEL FNRVIGMQKL WGTRIGINRV WQGTAPRVLL FEPETVEPIL NSQKFVNKSH DYDYLHPWLG EGLLTSTDRK WHSRRKILTP AFHFKILDDF IDVFNEQSAV LARKLAVEVG SEAFNLFPYV TLCTLDIVCE TAMGRRIYAQ SNSESEYVKA VYGIGSIVQS RQAKIWLQSD FIFSLTAEYK LHQSYINTLH GFSNMVIRER KAELAILQEN NNNNNNNAPD AYDDVGKKKR LAFLDLLIDA SKEGTVLSNE DIREEVDTFM FEGHDTTSAA ISWTLFLLGC HPEYQERVVE ELDSIFGDDK ETPATMKNLM DMRYLECCIK DSLRLFPSVP MMARMVGEDV NIGGKIVPAG TQAIIMTYAL HRNPRVFPKP EQFNPDNFLP ENCAGRHPFA YIPFSAGPRN CIGQKFAILE EKAVISTVLR KYKIEAVDRR EDLTLLGELI LRPKDGLRVK ITPRD // ID C4D1_DROME STANDARD; PRT; 512 AA. AC P33269; O18644; O18653; O18664; Q9W515; Q9W516; DT 01-FEB-1994 (Rel. 28, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4d1 (EC 1.14.-.-) (CYPIVD1). GN CYP4D1 OR CYT-P450-D1 OR EG:87B1.1 OR CG3656. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=92297166; PubMed=1605861; RA Gandhi R., Varak E., Goldberg M.L.; RT "Molecular analysis of a cytochrome P450 gene of family 4 on the RT Drosophila X chromosome."; RL DNA Cell Biol. 11:397-404(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CAM-1, CAM-2, CAM-3, CAM-8, CAM-9, CAM-12, CAM-14, CAM-19, RC CAM-38, CAM-41, CAM-42, CAM-44, and CAM-48; RA Phillips K.S., Begun D.J., Aquadro C.F.; RT "Evidence for non-neutral evolution around the cytochrome p450 gene RT cluster on the Drosophila melanogaster X chromosome."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN THE METABOLISM OF INSECT HORMONES AND IN THE CC BREAKDOWN OF SYNTHETIC INSECTICIDES. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P33269-1; Sequence=Displayed; CC Name=Short; CC IsoId=P33269-2; Sequence=VSP_000614; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, WITH THE CC HIGHEST LEVELS OCCURRING DURING LATE LARVAL STAGES, THEN FALLING CC DRASTICALLY DURING PUPARIATION. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67645; CAA47887.1; -. DR EMBL; Z98269; CAB10972.1; -. DR EMBL; AF016992; AAB71155.1; -. DR EMBL; AF016993; AAB71156.1; -. DR EMBL; AF016994; AAB71157.1; -. DR EMBL; AF016995; AAB71158.1; -. DR EMBL; AF016996; AAB71159.1; -. DR EMBL; AF016997; AAB71160.1; -. DR EMBL; AF016998; AAB71161.1; -. DR EMBL; AF016999; AAB71162.1; -. DR EMBL; AF017000; AAB71163.1; -. DR EMBL; AF017001; AAB71164.1; -. DR EMBL; AF017002; AAB71165.1; -. DR EMBL; AF017003; AAB71166.1; -. DR EMBL; AF017004; AAB71167.1; -. DR EMBL; AE003423; AAF45736.1; -. DR EMBL; AE003423; AAF45737.1; -. DR PIR; S25707; S25707. DR PIR; T13611; T13611. DR FlyBase; FBgn0005670; Cyp4d1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Alternative splicing; Polymorphism. FT METAL 456 456 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT VARSPLIC 1 186 MFLVIGAILASALFVGLLLYHLKFKRLIDLISYMPGPPVLP FT LVGHGHHFIGKPPHEMVKKIFEFMETYSKDQVLKVWLGPEL FT NVLMGNPKDVEVVLGTLRFNDKAGEYKALEPWLKEGLLVSR FT GRKWHKRRKIITPAFHFKILDQFVEVFEKGSRDLLRNMEQD FT RLKHGESGFSLYDWINLCTMDT -> MWLLLSLVLLLAIIA FT LEMRRFLRNMRTIPGPLPLPLLGNAHIFLGLTPAEACLKIG FT ELAERHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKS FT QEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPY FT VEIFDRQSLRLVEELALRISRGQERINLGEAIHLCALDA FT (in isoform Short). FT /FTId=VSP_000614. FT VARIANT 170 170 E -> D (IN STRAINS CAM-2, CAM-3, CAM-8, FT CAM-12, CAM-41, CAM-44, CAM-48 AND FT BERKELEY). FT VARIANT 426 426 S -> I (IN STRAINS CAM-8, CAM-44, CAM-48 FT AND BERKELEY). FT CONFLICT 68 68 Y -> I (IN REF. 1). FT CONFLICT 316 316 E -> K (IN REF. 1). FT CONFLICT 468 509 AIVANVLRHYEVDFVGDSSEPPVLIAELILRTKEPLMFKVR FT E -> PSWPMCSGTTRLTLWATSFGTTRADRRTYSAYQGPL FT SSRCG (IN REF. 1). SQ SEQUENCE 512 AA; 58691 MW; F7B089734231A6A3 CRC64; MFLVIGAILA SALFVGLLLY HLKFKRLIDL ISYMPGPPVL PLVGHGHHFI GKPPHEMVKK IFEFMETYSK DQVLKVWLGP ELNVLMGNPK DVEVVLGTLR FNDKAGEYKA LEPWLKEGLL VSRGRKWHKR RKIITPAFHF KILDQFVEVF EKGSRDLLRN MEQDRLKHGE SGFSLYDWIN LCTMDTICET AMGVSINAQS NADSEYVQAV KTISMVLHKR MFNILYRFDL TYMLTPLARA EKKALNVLHQ FTEKIIVQRR EELIREGSSQ ESSNDDADVG AKRKMAFLDI LLQSTVDERP LSNLDIREEV DTFMFEGHDT TSSALMFFFY NIATHPEAQK KCFEEIRSVV GNDKSTPVSY ELLNQLHYVD LCVKETLRMY PSVPLLGRKV LEDCEINGKL IPAGTNIGIS PLYLGRREEL FSEPNSFKPE RFDVVTTAEK LNPYAYIPFS AGPRNCIGQK FAMLEIKAIV ANVLRHYEVD FVGDSSEPPV LIAELILRTK EPLMFKVRER VY // ID C4D2_DROME STANDARD; PRT; 501 AA. AC Q27589; O18651; O18674; O46053; Q27588; Q9W514; DT 15-DEC-1998 (Rel. 37, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4d2 (EC 1.14.-.-) (CYPIVD2). GN CYP4D2 OR EG:152A3.4 OR CG3466. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94296569; PubMed=8024706; RA Frolov M.V., Alatortsev V.E.; RT "Cluster of cytochrome P450 genes on the X chromosome of Drosophila RT melanogaster."; RL DNA Cell Biol. 13:663-668(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 4-501 FROM N.A. RC STRAIN=CAM-1, CAM-2, CAM-3, CAM-8, CAM-9, CAM-12, CAM-14, CAM-19, RC CAM-38, CAM-41, CAM-42, CAM-44, and CAM-48; RA Phillips K.S., Begun D.J., Aquadro C.F.; RT "Evidence for non-neutral evolution around the cytochrome p450 gene RT cluster on the Drosophila melanogaster X chromosome."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE METABOLISM OF INSECT HORMONES AND IN CC THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75955; CAA53568.1; -. DR EMBL; Z23005; CAA80549.1; -. DR EMBL; AL009194; CAA15698.1; -. DR EMBL; AE003423; AAF45741.1; -. DR EMBL; AF017006; AAB71169.1; -. DR EMBL; AF017007; AAB71170.1; -. DR EMBL; AF017008; AAB71171.1; -. DR EMBL; AF017009; AAB71172.1; -. DR EMBL; AF017010; AAB71173.1; -. DR EMBL; AF017011; AAB71174.1; -. DR EMBL; AF017012; AAB71175.1; -. DR EMBL; AF017013; AAB71176.1; -. DR EMBL; AF017014; AAB71177.1; -. DR EMBL; AF017015; AAB71178.1; -. DR EMBL; AF017016; AAB71179.1; -. DR EMBL; AF017017; AAB71180.1; -. DR EMBL; AF017018; AAB71181.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0011576; Cyp4d2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Polymorphism. FT METAL 449 449 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT VARIANT 163 163 K -> M (IN STRAINS CAM-44, CAM-48 AND FT BERKELEY). FT CONFLICT 2 25 MISSING (IN REF. 2). FT CONFLICT 30 30 I -> A (IN REF. 1; CAA80549). FT CONFLICT 160 160 A -> R (IN REF. 1). FT CONFLICT 487 500 LRSANGVHLGLKPR -> CGRPTAFIL (IN REF. 1). SQ SEQUENCE 501 AA; 57914 MW; 8F8D98DBF39FD1A2 CRC64; MLGVVGVLLL VAFATLLLWD FLWRRRGNGI LPGPRPLPFL GNLLMYRGLD PEQIMDFVKK NQRKYGRLYR VWILHQLAVF STDPRDIEFV LSSQQHITKN NLYKLLNCWL GDGLLMSTGR KWHGRRKIIT PTFHFKILEQ FVEIFDQQSA VMVEQLQSRA DGKTPINIFP VICLTALDII AETAMGTKIN AQKNPNLPYV QAVNDVTNIL IKRFIHAWQR VDWIFRLTQP TEAKRQDKAI KVMHDFTENI IRERRETLVN NSKETTPEEE VNFLGQKRRM ALLDVLLQST IDGAPLSDED IREEVDTFMF EGHDTTTSAI SFCLYEISRH PEVQQRLQQE IRDVLGEDRK SPVTLRDLGE LKFMENVIKE SLRLHPPVPM IGRWFAEDVE IRGKHIPAGT NFTMGIFVLL RDPEYFESPD EFRPERFDAD VPQIHPYAYI PFSAGPRNCI GQKFAMLEMK STVSKLLRHF ELLPLGPEPR HSMNIVLRSA NGVHLGLKPR A // ID C4D8_DROME STANDARD; PRT; 463 AA. AC Q9VS79; Q24127; Q95TY3; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4d8 (EC 1.14.-.-) (CYPIVD8). GN CYP4D8 OR CG4321. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 273-400 FROM N.A. RC STRAIN=Haag-79; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003558; AAF50549.2; -. DR EMBL; AY058442; AAL13671.1; -. DR EMBL; U34329; AAA80663.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0015033; Cyp4d8. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 409 409 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 291 291 A -> E (IN REF. 4). FT CONFLICT 393 393 R -> C (IN REF. 4). SQ SEQUENCE 463 AA; 53286 MW; 8EFC16CCC5E4D4A4 CRC64; MQLMLRLNPK TFIKVGREYV LKFGHLQRVW IFNRLLIMSG DAELNEQLLS SQEHLVKHPV YKVLGQWLGN GLLLSDGKVW HQRRKIITPT FHFSILEQFV EVFDQQSNIC VQRLAQKANG NTFDVYRSIC AAALDIIAET AMGTKIYAQA NESTPYAEAV NECTALLSWR FMSVYLQVEL LFTLTHPHLK WRQTQLIRTM QEFTIKVIEK RRQALEDQQS KLMDTADEDV GSKRRMALLD VLLMSTVDGR PLTNDEIREE VDTFMFEGHD TTTSALSFCL HELSRHPEVQ AKMLEEIVQV LGTDRSRPVS IRDLGELKYM ECVIKESLRM YPPVPIVGRK LQTDFKYTHS VHGDGVIPAG SEIIIGIFGV HRQPETFPNP DEFIPERHEN GSRVAPFKMI PFSAGPRNCI GQKFAQLEMK MMLAKIVREY ELLPMGQRVE CIVNIVLRSE TGFQLGMRKR KHN // ID C4DE_DROME STANDARD; PRT; 507 AA. AC O46051; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4d14 (EC 1.14.-.-) (CYPIVD14). GN CYP4D14 OR EG:152A3.2 OR CG3540. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003423; AAF45740.1; -. DR EMBL; AL009194; CAA15696.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0023541; Cyp4d14. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 454 454 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 507 AA; 57480 MW; 01D33A556CA969A4 CRC64; MYLELFAILL ATALAWDYMR KRRHNKMYAE AGIRGPKSYP LVGNAPLLIN ESPKTIFDMQ FRLIAEFGKN IKTQMLGESG FMTADSKMIE AIMSSQQTIQ KNNLYSLLVN WLGDGLLISQ GKKWFRRRKI ITPAFHFKIL EDFVEVFDQQ SATMVQKLYD RADGKTVINM FPVACLCAMD IIAETAMGVK INAQLQPQFT YVQSVTTASA MLAERFMNPL QRLDFTMKLF YPKLLDKLND AVKNMHDFTN SVITERRELL QKAIADGGDA DAALLNDVGQ KRRMALLDVL LKSTIDGAPL SNDDIREEVD TFMFEGHDTT TSSIAFTCYL LARHPEVQAR VFQEVRDVIG DDKSAPVTMK LLGELKYLEC VIKESLRLFP SVPIIGRYIS QDTVLDGKLI PADSNVIILI YHAQRDPDYF PDPEKFIPDR FSMERKGEIS PFAYTPFSAG PRNCIGQKFA MLEMKSTISK MVRHFELLPL GEEVQPVLNV ILRSTTGINC GLKPRVY // ID C4DK_DROME STANDARD; PRT; 510 AA. AC Q9W011; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4d20 (EC 1.14.-.-) (CYPIVD20). GN CYP4D20 OR CG16761. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003475; AAF47649.1; -. DR FlyBase; FBgn0035344; Cyp4d20. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 455 455 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 510 AA; 58213 MW; 1AB7D265899ACCBF CRC64; MWLTLITGAL ILLLTWDFGR KRQRVLAFEK SAIPGPISIP ILGCGLQALH LGAENIIGWV GEKFDKYGKT FRFWILGESL IYTKDLQYFE TILSSTTLLE KGQLYEYLRP FLNDGLLVST GRKWHARRKI FTHAFHFKVL EHYVEIMDRH SSVMVDNLRK VADGKTAVDM LKYVSLAALD VITEAAMGVQ VNAQNDPDFP YIKALKSVVY IQPDRMFRFS RRYNWLFPLA APLLHRQLLS DIRVMHDFTD KVISERRETV RRAKADGTYR PLSLGDAEIG SKSQMALLDI LLQSSINNQP LSDADIREEV DTFMFEGDDT TSSGVSHALY AIARHPEVQQ RIFEELQRVL GPDASAPVTQ AQLQDLKYLD CVIKETMRLY PPVPAIGRHA QKELEIGDKT IPANTSIYLV LYYAHRDANY FPDPLSFRPE RFLEDQEQGH NTFAYVPFSA GPKNCIGQKF AVLEMKVLIS KVLRFYELLP LGEELKPMLN FILRSASGIN VGLRPRKALR // ID C4DL_DROME STANDARD; PRT; 511 AA. AC Q9VLZ7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4d21 (EC 1.14.-.-) (CYPIVD21). GN CYP4D21 OR CG6730. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003618; AAF52531.1; -. DR FlyBase; FBgn0031925; Cyp4d21. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 456 456 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 511 AA; 58264 MW; DF130D0C603BDA50 CRC64; MWILLGIAVL IMTLVWDNSR KQWRVNTFEK SRILGPFTIP IVGNGLQALT LRPENFIQRF GDYFNKYGKT FRLWILGECL IYTKDLKYFE SILSSSTLLK KAHLYRFLRD FLGDGLLLST GNKWTSRRKV LAPAFHFKCL ENFVEIMDRN SGIMVEKLKN YADGKTCVDL FKFVSLEALD VTTETAMGVQ VNAQNEPNFP YTKALKSVVY IESKRLASVS MRYNWLFPLA APLVYRRLQK DIAIMQDFTD KVIRERRAIL ERARADGTYK PLIMGDDDIG GKAKMTLLDI LLQATIDNKP LSDVDIREEV DVFIFAGDDT TTSGVSHALH AISRHPKVQE CIYEELVSVL GPDPDASVTQ TKLLELKYLD CVIKETMRLH PPVPILGRYI PEDLKIGEIT IPGNTSILLM PYYVYRDPEY FPDPLVFKPE RWMDMKTTSN TPPLAYIPFS SGPKNCIGQK FANLQMKALI SKVIRHYELL PLGADLKATY TFILSSSTGN NVGLKPRTRV K // ID C4E1_DROME STANDARD; PRT; 531 AA. AC Q9V4T5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4e1 (EC 1.14.-.-) (CYPIVE1). GN CYP4E1 OR CG2062. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003837; AAF59090.1; -. DR FlyBase; FBgn0015034; Cyp4e1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 444 444 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 531 AA; 61086 MW; 42D45A86B59DB905 CRC64; MWIVLCAFLA LPLFLVTYFE LGLLRRKRML NKFQGPSMLP LVGNAHQMGN TPTEILNRFF GWWHEYGKDN FRYWIGYYSN IMVTNPKYME FILSSQTLIS KSDVYDLTHP WLGLGLLTST GSKWHKHRKM ITPAFHFNIL QDFHEVMNEN STKFIDQLKK VADGGNIFDF QEEAHYLTLD VICDTAMGVS INAMENRSSS VVQAFKDITY TIKMRAFSPW KRNKYLFHFA PEYPEYSKTL KTLQDFTNEI IAKRIEVRKS GLEVGIKADE FSRKKMAFLD TLLSSKVDGR PLTSQELYEE VSTFMFEGHD TTTSGVGFAV YLLSRHPDEQ EKLFNEQCDV MGASGLGRDA TFQEISTMKH LDLFIKEAQR LYPSVPFIGR FTEKDYVIDG DIVPKGTTLN LGLLMLGYND RVFKDPHKFQ PERFDREKPG PFEYVPFSAG PRNCIGQKFA LLEIKTVVSK IIRNFEVLPA LDELVSKDGY ISTTLGLQPA EKKSRDAHNH KYDPILSASM TLKSENGLHL RMKQRLVCDS T // ID C4E2_DROME STANDARD; PRT; 526 AA. AC Q27606; Q24130; Q24291; Q9V4T4; DT 15-DEC-1998 (Rel. 37, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4e2 (EC 1.14.-.-) (CYPIVE2). GN CYP4E2 OR CG2060. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE OF 42-526 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=97128322; PubMed=8972915; RA Pittendrigh B.R., Mocelin G., Andreev O., Ffrench-Constant R.H.; RT "The sequence of a Drosophila Cyp4e2 cytochrome P450-encoding cDNA."; RL Gene 179:295-296(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 42-444 FROM N.A. RC STRAIN=Raleigh DDTR; RA Amichot M., Brun A., Cuany A., Lemouel T., Berge J.; RT "Cloning and expression study of CYP4E2 a novel P450 gene in RT Drosophila."; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 312-435 FROM N.A. RC STRAIN=Haag-79; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arniaz R., Pittendrigh B., RA Ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U56957; AAC47424.1; -. DR EMBL; AE003837; AAF59091.1; -. DR EMBL; AY058518; AAL13747.1; -. DR EMBL; X86076; CAA60032.1; -. DR EMBL; U34332; AAA80666.1; -. DR PIR; JC5236; JC5236. DR PIR; S57646; S57646. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0014469; Cyp4e2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 444 444 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 256 256 E -> K (IN REF. 4). FT CONFLICT 302 302 S -> D (IN REF. 4). SQ SEQUENCE 526 AA; 60692 MW; A13DD43C4F4F4D52 CRC64; MWFVLYIFLA LPLLLVAYLE LSTFRRRRVL NKFNGPRGLP LMGNAHQMGK NPSEILDTVF SWWHQYGKDN FVFWIGTYSN VLVTSSKYLE FILSSQTLIT KSDIYQLTHP WLGLGLLTST GSKWHKHRKM ITPAFHFNIL QDFHEVMNEN STKFIKHLKT VAAGDNIFDF QEQAHYLTLD VICDTAMGVS INAMENRSSS IVQAFKDMCY NINMRAFHPL KRNELLYRLA PDYPAYSRTL KTLQDFTNEI IAKRIEAHKS GAVSTNAGDE FTRKKMAFLD TLLSSTIDGR PLNSKELYEE VSTFMFEGHD TTTSGVSFAV YLLSRHQDEQ RKLFKEQREV MGNSELGRDA TFQEISQMKY LDLFIKEAQR VYPSVPFIGR FTEKDYVIDG DLVPKGTTLN LGLVMLGYNE KVFKDPHKFR PERFELEKPG PFEYVPFSAG PRNCIGQKFA LLEIKTVVSK IIRNFEVLPA LDELVSKDGY ISTTIGLPDA ERKKRDPYRH KYDPILSAVL TLKSENGLYI RLKERH // ID C4E3_DROME STANDARD; PRT; 526 AA. AC Q9VL92; Q24128; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4e3 (EC 1.14.-.-) (CYPIVE3). GN CYP4E3 OR CG4105. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 312-433 FROM N.A. RC STRAIN=Haag-79; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003626; AAF52804.1; -. DR EMBL; U34330; AAA80664.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0015035; Cyp4e3. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 443 443 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 526 AA; 60882 MW; 993BCEEAFCDFF6CC CRC64; MWLAVLALLV LPLITLVYFE RKASQRRQLL KEFNGPTPVP ILGNANRIGK NPAEILSTFF DWWYDYGKDN FLFWIGYSSH IVMTNPKQLE YILNSQQLIQ KSTIYDLLHP WLGHGLLTSF GSKWHKHRKM ITPSFHFNIL QDFHEVMNEN SAKFMTQLKK ASAGDTIIDF QEHANYLTLD VICDTAMGVP INAMEQRDSS IVQAFRDMCY NINMRAFHPF KRSNRVFSLT PEFSAYQKTL KTLQDFTYDI IEKRVYALQN GGSKEDHDPS LPRKKMAFLD TLLSSTIDGR PLTRQEIYEE VSTFMFEGHD TTTSGVSFSV YLLSRHPDVQ RKLYREQCEV MGHDMNRSVS FQEIAKMKYL DLFIKEAQRV YPSVPFIGRY CDKDYDINGS IVPKGTTLNL ALILLGYNDR IFKDPHHFRP ERFEEEKPAP FEYLPFSAGP RNCIGQKFAL LELKTVISKV VRSFEVLPAV DELVSTDGRL NTYLGLAPDE KLKREAGRHK YDPILSAVLT LKSDNGLHLR LRERRS // ID C4G1_DROME STANDARD; PRT; 556 AA. AC Q9V3S0; Q24126; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4g1 (EC 1.14.-.-) (CYPIVG1). GN CYP4G1 OR EG:165H7.1 OR CG3972. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE OF 361-488 FROM N.A. RC STRAIN=Haag-79; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003417; AAF45503.1; -. DR EMBL; AL009188; CAA15672.1; -. DR EMBL; U34328; AAA80662.1; -. DR PIR; S70623; S70623. DR FlyBase; FBgn0010019; Cyp4g1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 497 497 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 556 AA; 62970 MW; 7C9B82A6D787BD3E CRC64; MAVEVVQETL QQAASSSSTT VLGFSPMLTT LVGTLVAMAL YEYWRRNSRE YRMVANIPSP PELPILGQAH VAAGLSNAEI LAVGLGYLNK YGETMKAWLG NVLLVFLTNP SDIELILSGH QHLTKAEEYR YFKPWFGDGL LISNGHHWRH HRKMIAPTFH QSILKSFVPT FVDHSKAVVA RMGLEAGKSF DVHDYMSQTT VDILLSTAMG VKKLPEGNKS FEYAQAVVDM CDIIHKRQVK LLYRLDSIYK FTKLREKGDR MMNIILGMTS KVVKDRKENF QEESRAIVEE ISTPVASTPA SKKEGLRDDL DDIDENDVGA KRRLALLDAM VEMAKNPDIE WNEKDIMDEV NTIMFEGHDT TSAGSSFALC MMGIHKDIQA KVFAEQKAIF GDNMLRDCTF ADTMEMKYLE RVILETLRLY PPVPLIARRL DYDLKLASGP YTVPKGTTVI VLQYCVHRRP DIYPNPTKFD PDNFLPERMA NRHYYSFIPF SAGPRSCVGR KYAMLKLKVL LSTIVRNYIV HSTDTEADFK LQADIILKLE NGFNVSLEKR QYATVA // ID C4GF_DROME STANDARD; PRT; 574 AA. AC Q9VYY4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4g15 (EC 1.14.-.-) (CYPIVG15). GN CYP4G15 OR CG11715. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Oregon-R; TISSUE=Larva; RX MEDLINE=20351238; PubMed=10891384; RA Maibeche-Coisne M., Monti-Dedieu L., Aragon S., Dauphin-Villemant C.; RT "A new cytochrome P450 from Drosophila melanogaster, CYP4G15, RT expressed in the nervous system."; RL Biochem. Biophys. Res. Commun. 273:1132-1137(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLY INVOLVED IN STEROID HORMONES BIOSYNTHESIS. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN LARVAL BRAIN CORTEX CELLS AND CC RING GLANDS AND WEAKLY IN LARVAL DIGESTIVE SYSTEM AND ADULT CC NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF159624; AAF76522.1; -. DR EMBL; AE003486; AAF48049.1; -. DR EMBL; AY060719; AAL28267.1; -. DR PIR; JC7327; JC7327. DR FlyBase; FBgn0030304; Cyp4g15. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 519 519 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 320 322 VAG -> WRD (IN REF. 1). FT CONFLICT 336 336 D -> N (IN REF. 1). FT CONFLICT 344 344 E -> K (IN REF. 1). SQ SEQUENCE 574 AA; 65380 MW; 3131878D3023DCF7 CRC64; MEVLKKDAAL GSPSSVFYFL LLPTLVLWYI YWRLSRAHLY RLAGRLPGPR GLPIVGHLFD VIGPASSVFR TVIRKSAPFE HIAKMWIGPK LVVFIYDPRD VELLLSSHVY IDKASEYKFF KPWLGDGLLI STGQKWRSHR KLIAPTFHLN VLKSFIELFN ENSRNVVRKL RAEDGRTFDC HDYMSEATVE ILLETAMGVS KKTQDKSGFE YAMAVMRMCD ILHARHRSIF LRNEFVFTLT RYYKEQGRLL NIIHGLTTKV IRSKKAAFEQ GTRGSLAQCE LKAAALERER EQNGGVDQTP STAGSDEKDR EKDKEKASPV AGLSYGQSAG LKDDLDVEDN DIGEKKRLAF LDLMLESAQN GALITDTEIK EQVDTIMFEG HDTTAAGSSF FLSLMGIHQD IQDRVLAELD SIFGDSQRPA TFQDTLEMKY LERCLMETLR MYPPVPLIAR ELQEDLKLNS GNYVIPRGAT VTVATVLLHR NPKVYANPNV FDPDNFLPER QANRHYYAFV PFSAGPRSCV GRKYAMLKLK ILLSTILRNY RVYSDLTESD FKLQADIILK REEGFRVRLQ PRTS // ID C4P1_DROME STANDARD; PRT; 513 AA. AC Q9V558; Q24125; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 4p1 (EC 1.14.-.-) (CYPIVP1). GN CYP4P1 OR CG10842. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 325-450 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003834; AAF58962.1; -. DR EMBL; U34327; AAA80661.1; -. DR PIR; S70624; S70624. DR FlyBase; FBgn0015037; Cyp4p1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 459 459 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 513 AA; 59432 MW; F3D7500719BAF2C4 CRC64; MIILWLILAL SALLYWLHRA NKDYHILSFF TKRIRLKDGT PVEIIAPIAK GKTIFGNTLD LYGRDHAGVF NYSRERAKEM GTSYIEYVFG KAIYNIIDAD SAENVLNHPN LITKGLVYNF LHPFLRTGLL TSTGKKWHAR RKMLTPTFHF NILNQFQEIF KTESQKFLLQ FEGQDEVTIT LHDVIPRFTL NSICETAMGV KLDEMAEKGD RYRENFSQIE ECFIRRLSNP LLWGDKLFEM FAAKDFASAL DVVHRFSSEI IAKRRDLLKD ELDKSSSTAD DDGFVSKKRF AMLDTLIYAE KDGLIDHIGI CEEVDTLMFE GYDTTSIGLI FGLMNMSLNP DKQELCYQEI QEHIDDDLSN LDVGQLNKLK YLEYFMKETT RLFPSVPIMG REAVQETELA NGLILPKGAQ ITIHVFDIHR NAKYWDSPEE FRPERFLPEN VQDRHTYAYV PFSAGQRNCI GKKYAMQEMK TLMVVLLKQF KVLKAIDPQK IVFHTGITLR TQDKIRVKLV RRT // ID C4P2_DROME STANDARD; PRT; 520 AA. AC Q9V557; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4p2 (EC 1.14.-.-) (CYPIVP2). GN CYP4P2 OR CG1944. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003834; AAF58963.1; ALT_SEQ. DR EMBL; AY051564; AAK92988.1; -. DR FlyBase; FBgn0033395; Cyp4p2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 464 464 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 520 AA; 60459 MW; 8A61C66DC47620B1 CRC64; MMICLLWISV AILVVIHWIY KVNKDYNILA FFARRVQTKD GKPLDSLVPM IKGRTVFANC FDLLGKDTDQ VFTHLRQLAK NSGDSYLQYS MGFSNFNVID AHNAANILNH PNLITKGVIY NFLHPFLRTG VLTATEKKWH TRRSMLTRTF HLDILNQFQE IFIAESLKFV SQFQGQNEVV VSLKDRISRF TLNSICETAM GIKLDEMAEK GDRYRANFHI IDEGLTRRIV NPLYWDDCVY NMFTGHKYNA ALKVVHEFSR EIIAKRRVLL EEELENRRAT QTADDDICVI RKKRFAMLDT LICAEKDGLI DDIGISEEVD TLMAEGYDTT SIGLVFGLMN MSLYAAEQEL CYQEIQEHIL DDLSNLNLSQ LSKLNYLGYF IKETMRLYPS IPIMGRQTLQ ETELENGLIL PKRSQINIHV FDIHRNPKYW ESPEEFRPER FLPQNCLKRH PYAYIPFSAG QRNCIGQKYA MQEMKTLMVV ILKHFKILPV IDPKSIVFQV GITLRFKNKI KVKLVRRNCV // ID C4P3_DROME STANDARD; PRT; 515 AA. AC Q9V559; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4p3 (EC 1.14.-.-) (CYPIVP3). GN CYP4P3 OR CG10843. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003834; AAF58961.2; -. DR FlyBase; FBgn0033397; Cyp4p3. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 461 461 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 515 AA; 59651 MW; B150DFC110F7921E CRC64; MLILWLVGAF IVLIQWIYRL NRDYCILGFF AKRIRTKNGQ NPESIAPLVK GSTIFANSFD LYGKDHSGVF EHSRDCAKKL GKSYAEYAMG TAIYNVIDAD SAERVLNDPN LINKGTIYDF LHPFLRTGLL TSTGKKWHAR RKMLSPTFHF NILNQFQEIF ITESLKFLEQ FKGNDEAIIS LNEVIPRFTL NSICETAMGV KLDEMAEKGD RYRENFRQIE ECFIRRMSNP LLWSDTLFKM FAEKDYASAL DVVHGFSSEI IAKRRDQLND EIDSRGNTQT AEDELFTSKK RFAMLDTLIL AEKDGLIDHI GICEEVDTLM FEGYDTTSIG LMFGLMNMSL YPEEQEKCYQ EIQANIDDEL NILNIGQLNK LKNLEYFIKE TMRLFPSVPA MGRETTRETE LSNGLILPKG SQIFVHVFDI HRNPEYWDSP EEFRPERFLP ENSQNRHTYA YIPFSAGQRN CIGQKFAMQE MKTLMVALLK QFQILPEIDP KTIVFQTGLT LRTKNQIHVK LVRRK // ID C4S3_DROME STANDARD; PRT; 495 AA. AC Q9VXY0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 4s3 (EC 1.14.-.-) (CYPIVS3). GN CYP4S3 OR CG9081. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 87:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003498; AAF48426.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0030615; Cyp4s3. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 436 436 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 495 AA; 57189 MW; 4AE96B1BFF502891 CRC64; MSTLALVAFV LWAAFLRYLP KILNFLRLQR FAKTLPGPTI GELIANVKKG EILNWLKELR EKHGPVFRIW FGKDLMVMFT DPEDIKQLLG NNQLLTKSRN YELLEPWLGK GLLTNGGESW HRRRKLLTPG FHFRILSEFK EPMEENCRIL VRRLRTKANG ESFDIYPYIT LFALDAICET AMGIKKHAQL QSDSEYVQAV QSICRVMHKQ SFSFWQRLNV FFKHTKPGKE REAALKVLHD ETNRVIRLRR EQLIQERNEW KPEAEQDDVG AKRRLAFLDM LLLTQMEGGA ELSDTDIREE VDTFMFEGHD TTSSAIAFAL SLLSKNPDVQ QRAFEEASEL EGREKESMPY LEAVIKETLR IYPSVPFFSR KVLEDLEVGK LTVPKGASIS CLIYMLHRDP KNFPDPERFD PDRFLVNEKQ MHPFAFAAFS AGPRNCIGQK FAMLELKTSL AMLLRSYRFL PDKDHQPKPL AELVTKSGNG IRLRILPRDE NGTTA // ID C6A2_DROME STANDARD; PRT; 506 AA. AC P33270; P91669; Q9V9A2; DT 01-FEB-1994 (Rel. 28, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 6a2 (EC 1.14.-.-) (CYPVIA2) (P450-B1). GN CYP6A2 OR CYT-P450-B1 OR CG9438. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=91-C; RX MEDLINE=92279225; PubMed=1317576; RA Waters L.C., Zelhof A.C., Shaw B.J., Ch'Ang L.-Y.; RT "Possible involvement of the long terminal repeat of transposable RT element 17.6 in regulating expression of an insecticide resistance- RT associated P450 gene in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 89:4855-4859(1992). RN [2] RP ERRATUM. RX MEDLINE=93101696; PubMed=1465460; RA Waters L.C., Zelhof A.C., Shaw B.J., Ch'Ang L.Y.; RL Proc. Natl. Acad. Sci. U.S.A. 89:12209-12209(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1; RA Dunkov B.C., Feyereisen R.; RT "Drosophila melanogaster Cyp6a2 gene."; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A., AND FUNCTION. RC STRAIN=Canton-S; RX MEDLINE=98068841; PubMed=9407006; RA Dunkov B.C., Guzov V.M., Mocelin G., Shotkoski F., Brun A., RA Amichot M., Ffrench-Constant R.H., Feyereisen R.; RT "The Drosophila cytochrome P450 gene Cyp6a2: structure, localization, RT heterologous expression, and induction by phenobarbital."; RL DNA Cell Biol. 16:1345-1356(1997). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP SEQUENCE OF 352-383 FROM N.A. RX MEDLINE=96194881; PubMed=8625948; RA Saner C., Weibel B., Wurgler F.E., Sengstag C.; RT "Metabolism of promutagens catalyzed by Drosophila melanogaster RT CYP6A2 enzyme in Saccharomyces cerevisiae."; RL Environ. Mol. Mutagen. 27:46-58(1996). CC -!- FUNCTION: IS INVOLVED IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES CC AND MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M88009; AAA28438.1; -. DR EMBL; S51248; AAB24525.1; -. DR EMBL; U78088; AAB36782.1; -. DR EMBL; AE003790; AAM70832.1; -. DR EMBL; S81983; AAB36460.1; -. DR PIR; A45378; A47198. DR FlyBase; FBgn0000473; Cyp6a2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 451 451 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 31 31 V -> L (IN REF. 1 AND 4). FT CONFLICT 191 191 A -> R (IN REF. 1, 3 AND 4). FT CONFLICT 283 284 RV -> SSF (IN REF. 1 AND 4). SQ SEQUENCE 506 AA; 58685 MW; D6FFDE4AA81CD660 CRC64; MFVLIYLLIA ISSLLAYLYH RNFNYWNRRG VPHDAPHPLY GNMVGFRKNR VMHDFFYDYY NKYRKSGFPF VGFYFLHKPA AFIVDTQLAK NILIKDFSNF ADRGQFHNGR DDPLTQHLFN LDGKKWKDMR QRLTPTFTSG KMKFMFPTVI KVSEEFVKVI TEQVPAAQNG AVLEIKELMA RFTTDVIGTC AFGIECNTLR TPVSDFRTMG QKVFTDMRHG KLLTMFVFSF PKLASRLRMR MMPEDVHQFF MRLVNDTIAL RERENFKRND FMNLLIELKQ KGRVTLDNGE VIEGMDIGEL AAQVFVFYVA GFETSSSTMS YCLYELAQNQ DIQDRLRNEI QTVLEEQEGQ LTYESIKAMT YLNQVISETL RLYTLVPHLE RKALNDYVVP GHEKLVIEKG TQVIIPACAY HRDEDLYPNP ETFDPERFSP EKVAARESVE WLPFGDGPRN CIGMRFGQMQ ARIGLAQIIS RFRVSVCDTT EIPLKYSPMS IVLGTVGGIY LRVERI // ID C6A8_DROME STANDARD; PRT; 506 AA. AC Q27593; Q9V775; DT 15-DEC-1998 (Rel. 37, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 6a8 (EC 1.14.-.-) (CYPVIA8). GN CYP6A8 OR CG10248. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC STRAIN=91-R; RX MEDLINE=97128822; PubMed=8973362; RA Maitra S., Dombrowski S.M., Waters L.C., Ganguly R.; RT "Three second chromosome-linked clustered Cyp6 genes show RT differential constitutive and barbital-induced expression in RT DDT-resistant and susceptible strains of Drosophila melanogaster."; RL Gene 180:165-171(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN THE METABOLISM OF INSECT HORMONES AND IN THE CC BREAKDOWN OF SYNTHETIC INSECTICIDES. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L46859; AAB05550.1; -. DR EMBL; AE003813; AAF58185.2; -. DR PIR; JC5320; JC5320. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0013772; Cyp6a8. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 451 451 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 4 4 T -> A (IN REF. 1). FT CONFLICT 193 193 G -> A (IN REF. 1). FT CONFLICT 332 343 MISSING (IN REF. 1). FT CONFLICT 465 465 L -> P (IN REF. 1). SQ SEQUENCE 506 AA; 58117 MW; A0B2A49DA3B99173 CRC64; MALTYILFQV AVALLAILTY YIHRKLTYFK RRGIPFVAPH LIRGNMEELQ KTKNIHEIFQ DHYNKFRESK APFVGFFFFQ SPAAFVIDLE LAKQILIKDF SNFSNKGIFY NEKDDPISAH LFNLDGAQWR LLRNKLSSTF TSGKMKLMYP TVVSVANEFM TVMHEKVPKN SVLEIRDLVA RFTVDVIGTC AFGIQCNSLR DEKAEFLYFG KRSLVDKRHG TLLNGFMRSY PKLARKLGMV RTAPHIQEFY SRIVTETVAV REKEHIKRND FMDMLIELKN QKEMTLENGD VVRGLTMEEV LAQAFVFFIA GFETSSSTMG FALYELAKNP DIQDKVRAEV EEVIEQHDQN FTYECTKDLK YLNQVLDETL RLYTIVPNLD RMAAKRYVVP GHPNFVIEAG QSVIIPSSAI HHDPSIYPEP FEFRPERFSP EESAGRPSVA WLPFGDGPRN CIGLRFGQMQ ARIGLALLIR NFKFSTCSKT PNPLVYDPKS FVLGVKDGIY LKVETV // ID C6A9_DROME STANDARD; PRT; 504 AA. AC Q27594; Q9V772; DT 15-DEC-1998 (Rel. 37, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 6a9 (EC 1.14.-.-) (CYPVIA9). GN CYP6A9 OR CG10246. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC STRAIN=91-R; RX MEDLINE=97128822; PubMed=8973362; RA Maitra S., Dombrowski S.M., Waters L.C., Ganguly R.; RT "Three second chromosome-linked clustered Cyp6 genes show RT differential constitutive and barbital-induced expression in RT DDT-resistant and susceptible strains of Drosophila melanogaster."; RL Gene 180:165-171(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN THE METABOLISM OF INSECT HORMONES AND IN THE CC BREAKDOWN OF SYNTHETIC INSECTICIDES. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L46860; AAB46609.1; ALT_SEQ. DR EMBL; AE003813; AAF58188.1; ALT_SEQ. DR PIR; JC5321; JC5321. DR FlyBase; FBgn0013771; Cyp6a9. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 449 449 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 137 137 Y -> S (IN REF. 1). FT CONFLICT 376 376 V -> D (IN REF. 1). FT CONFLICT 424 434 DNFSPERVKER -> IFFARTSEGS (IN REF. 1). FT CONFLICT 448 448 N -> L (IN REF. 1). SQ SEQUENCE 504 AA; 58005 MW; 3B0C875DAC3D4290 CRC64; MGVYSVLLAI VVVLVGYLLL KWRRALHYWQ NLDIPCEEPH ILMGSLTGVQ TSRSFSAIWM DYYNKFRGTG PFAGFYWFQR PGILVLDISL AKLILIKEFN KFTDRGFYHN TEDDPLSGQL FLLDGQKWKS MRSKLSYTFT SGKMKYMFPT VVKVGHEFIE VFGQAMEKSP IVEVRDILAR FTTDVIGTCA FGIECSSLKD PEAEFRVMGR RAIFEQRHGP IGIAFINSFQ NLARRLHMKI TLEEAEHFFL RIVRETVAFR EKNNIRRNDF MDQLIDLKNS PLTKSESGES VNLTIEEMAA QAFVFFGAGF ETSSTTMGFA LYELAQHQDI QDRVRKECQE VIGKYNGEIT YESMKDMVYL DQVISETLRL YTVLPVLNRE CLEDYEVPGH PKYVIKKGMP VLIPCGAMHR DEKLYANPNT FNPDNFSPER VKERDSVEWL PFGDGPRNCI GMRFGQMQAR SGLALLINRF KFSVCEQTTI PIVYSKKTFL ISSETGIFLK VERV // ID C6AD_DROME STANDARD; PRT; 493 AA. AC Q9V4U9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6a13 (EC 1.14.-.-) (CYPVIA13). GN CYP6A13 OR CG2397. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003836; AAF59076.1; -. DR EMBL; AY051723; AAK93147.1; -. DR FlyBase; FBgn0033304; Cyp6a13. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 435 435 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 493 AA; 57643 MW; 0B091E7D227BA642 CRC64; MLTLLVLVFT VGLLLYVKLR WHYSYWSRRG VAGERPVYFR GNMSGLGRDL HWTDINLRIY RKFRGVERYC GYFTFMTKSL FIMDLELIRD IMIRDFSSFA DRGLFHNVRD DPLTGNLLFL DGPEWRWLRQ NLTQVFTSGK MKFMFPNMVE VGEKLTQACR LQVGEIEAKD LCARFTTDVI GSCAFGLECN SLQDPESQFR RMGRSVTQEP LHSVLVQAFM FAQPELARKL RFRLFRPEVS EFFLDTVRQT LDYRRRENIH RNDLIQLLME LGEEGVKDAL SFEQIAAQAL VFFLAGFDTS STTMSFCLYE LALNPDVQER LRVEVLAVLK RNNQKLTYDS VQEMPYLDQV VAETLRKYPI LPHLLRRSTK EYQIPNSNLI LEPGSKIIIP VHSIHHDPEL YPDPEKFDPS RFEPEEIKAR HPFAYLPFGE GPRNCIGERF GKLQVKVGLV YLLRDFKFSR SEKTQIPLKF SSRNFLISTQ EGVHLRMEGL ERP // ID C6AE_DROME STANDARD; PRT; 509 AA. AC Q9V4U7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6a14 (EC 1.14.-.-) (CYPVIA14). GN CYP6A14 OR CG8687. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Nelson B.; RL Unpublished observations (SEP-2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003836; AAF59078.1; ALT_SEQ. DR FlyBase; FBgn0033302; Cyp6a14. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 454 454 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 509 AA; 58202 MW; 5A2563C549A0CA69 CRC64; MLFTIALVGV VLGLAYSLHI KIFSYWKRKG VPHETPLPIV GNMRGIVKKY HFRDINQRIY KKFKGQGPIA GMYTFFKRTA LITDLDFIKQ VMIKDFSYFQ DRGAFTNPRD DPLTGHLFAL EGEEWRAMRH KLTPVFTSGK IKQMSKVIVD VGLRLGDAMD KAVKEAKVEE GNVEIKDLCA RFTTDVIGSC AFGLECNSLQ DPSAEFRQKG REIFTRRRHS TLVQSFIFTN ARLARKLRIK VLPDDLTQFF MSTVKNTVDY RLKNGIKRND FIEQMIELRA EDQEAAKKGQ GIDLSHGLTL EQMAAQAFVF FVAGFETSSS TMSLCLYELA LQPDIQQRLR EEIESVLANV DGGELNYDVL AQMTYLDQVL SETLRKHPLL PHLIRETTKD YQIPNSDIVL DKGILALIPV HNIHHDPEIY PEPEKFDPSR FDPEEVKNRH PMAYLPFGDG PRNCIGLRFG KIQAKIGLVS LLRRFKFSVS NRTDVPLIFS KKSFLLTTND GIYLKVERV // ID C6AH_DROME STANDARD; PRT; 501 AA. AC Q9V770; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable cytochrome P450 6a17 (EC 1.14.-.-) (CYPVIA17). GN CYP6A17 OR CG10241. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003813; AAF58190.1; -. DR EMBL; AY069090; AAL39235.1; -. DR FlyBase; FBgn0015714; Cyp6a17. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 444 444 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 501 AA; 58208 MW; 00E0E85B4AE40D41 CRC64; MLLLALIVVI LSLLVFAARR RHGYWQRRGI PHDEVHPLFG NIKDWPNKRH IAEIFRDYYF KYKNSDYPFA GFFFFFTRTA VVTDMELLKR VLIKDFNHFE NRGVFYNEID DPLSATLFSI EGQKWRHLRH KLTPTFTSGK MKNMFPIVVK VGEEMDKVFR SKTAADRGQV LEVVDLVARY TADVIGNCAF GLNCNSLYDP KAEFVSIGKR AITEHRYGNM LDIFLFGFPK LSRRLRLKLN IQEAEDFYTK IVRETIDYRL RTKEKRNDFM DSLIEMYKNE QSGNSEDGLT FNELLAQAFI FFVAGFETSS TTMGFALYEL ARNQDVQDKL REEIGNVFGK HNKEFTYEGI KEMKYLEQVV METLRKYPVL AHLTRMTDTD FSPEDPKYFI AKGTIVVIPA LGIHYDPDIY PEPEIFKPER FTDEEIAARP SCTWLPFGEG PRNCIGLRFG MMQTCVGLAY LIRGYKFSVS PETQIPMKIV VKNILISAEN GIHLKVEKLA K // ID C6AI_DROME STANDARD; PRT; 507 AA. AC Q9VB31; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6a18 (EC 1.14.-.-) (CYPVIA18). GN CYP6A18 OR CG13977. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003761; AAF56712.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0039519; Cyp6a18. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 451 451 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 507 AA; 57956 MW; 5CCFC44101BBC17B CRC64; MQLTYFLFQV AVALLAIVTY ILHRKLTYFK RRGIPYDKPH PLRGNMEGYK KTRTVHEIHQ EYYNKYRNSK APFVGFYLFQ KPAAFVIDLE LAKQILIKNF SNFTDKGIYY NEKDDPMSAH LFNLDGPQWR LLRSKLSSTF TSGKMKFMYP TVVSVAEEFM AVMHEKVSEN SILDVRDLVA RFTVDVIGTC AFGIKCNSLR DEKAEFLHFG RRALLDSRHG NLVSGLMRSY PNLARRLGLC RNTAQIQEFY QRIVKETVTL REKENIKRND FMDMLIGLKN QKNMTLENGE VVKGLTMDEI VAQAFVFFIA GFDTSSSTMG FALYELAKNP SIQDKVRAEL GQVLEQHDQK FTYECIKDLK YLDQVINETL RHYTIVPNVD RVAAKRFVVP GNPKFVIEAG QSVIIPSSAI HHDPSIYPEP NEFRPERFSP EESAKRPSVA WLPFGEGPRN CIGLRFGQMQ ARIGLAMLIK NFTFSPCSAT PDPLTFDPHS AILLGIKGGI QLKVEAI // ID C6AJ_DROME STANDARD; PRT; 503 AA. AC P82711; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6a19 (EC 1.14.-.-) (CYPVIA19). GN CYP6A19 OR CG10243. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003813; AAG22266.1; -. DR FlyBase; FBgn0033979; Cyp6a19. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 445 445 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 503 AA; 57758 MW; 0A24CDDB5C2CF2C6 CRC64; MAILLGLVVG VLTLVAWWVL QNYTYWKRRG IPHDPPNIPL GNTGELWRTM PLAGILKRTY LKFRKQTDGP FAGFYLYAMK YIVITDVDFV KTVLIRDFDK FHDRGVYHNE KDDPLTNNLA TIEGQKWKNL RQKLTHTFTS AKMKSMFSTV LNVGDEMIRV VDEKISSSSQ TLEVTDIVSR FTSDVIGICA FGLKCNSLRD PKAEFVQMGY SALRERRHGW LVDLLIFGMP KLAVKLGFQF LLPSVQKFYM KIVQDTIDYR MKRKVTRNDF MDTLIDMKQQ YDKGDKENGL AFNEVAAQAF VFFLAGFEAG STTMGFTLYE LACNQDVQDK LRAEIDSVLE RYNGKLEYDS MQDLFYMEKV INESLRKHPV VAHLARIATK PYQHSNPKYF IEAGTGVLVS TLGIHHDPEF YPEPEKFIPE RFDEEQVKKR PTCAFLPFGA GPRNCIGLRF GRMQVIIGLA LLIHNFRFEL HPKTPVPMKY TINNLLLGSE GGIHLNITKV VRD // ID C6AK_DROME STANDARD; PRT; 501 AA. AC Q9V773; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6a20 (EC 1.14.-.-) (CYPVIA20). GN CYP6A20 OR CG10245. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Nelson B.; RL Unpublished observations (SEP-2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003813; AAF58187.1; ALT_SEQ. DR FlyBase; FBgn0033980; Cyp6a20. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 445 445 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 501 AA; 57728 MW; 14090AF782ABE824 CRC64; MAVMIVLLIG VITFVAWYVH QHFNYWKRRG IPHDEPKIPY GNTSELMKTV HFADIFKRTY NKLRNKTDGP FVGFYMYFKR MVVVTDIDFA KTVLIREFDK FHDRGVFHNE RDDPLSANLV NIDGQKWKTL RQKLTPTFTS GKMKTMFPTI LTVGDELIRV FGETASADSD SMEITNVVAR FTADVIGSCA FGLDCHSLSD PKAKFVQMGT TAITERRHGK SMDLLLFGAP ELAAKLRMKA TVQEVEDFYM NIIRDTVDYR VKNNVKRHDF VDMLIEMKLK FDNGDKENGL TFNEIAAQAF IFFLAGFETS STTMGFALYE LACHQDIQDK LRTEINTVLK QHNGKLDYDS MREMTYLEKV IDETMRKRPV VGHLIRVATQ HYQHTNPKYN IEKGTGVIVP TLAIHHDPEF YPEPEKFIPE RFDEDQVQQR PACTFLPFGD GPRNCIGLRF GRMQVIVGMA LLIHNFKFEF HPTKTVVPLE YRTDDFLLSS KGGIHLKVTR V // ID C6AL_DROME STANDARD; PRT; 504 AA. AC Q9V774; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6a21 (EC 1.14.-.-) (CYPVIA21). GN CYP6A21 OR CG10247. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003813; AAF58186.1; -. DR FlyBase; FBgn0033981; Cyp6a21. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 449 449 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 504 AA; 57841 MW; 1633B8FC4B5BB793 CRC64; MSVGTVLLTA LLALVGYLLM KWRSTMRHWQ DLGIPCEEPH ILMGSMKGVR TARSFNEIWT SYYNKFRGSG PFAGFYWFRR PAVFVLETSL AKQILIKEFN KFTDRGFFHN PEDDPLSGQL FLLDGQKWRT MRNKLSSTFT SGKMKYMFPT VVKVANEFTD VFGQNVAKSP VVEVRELLAR FTTDVIGTCA FGIECSSLKD PDAEFREMGR RSLTEQRLGP VGIGFVNSFP NLARRLHMKM TAEPIERFFM RIVRETVAFR EQNNIRRNDF MDQLIDLKNK PLMVSQSGES VNLTIEEIAA QAFVFFAAGF ETSSTTMGFA LYELAQNQDI QNRVRKECQE VIEKCNGELN YESMKDLVYL DQVVSETLRL YTVLPVLNRE CLEDYEVPGH PKYVIKKGMP VLIPCGAMHR DEKLYANPNT FNPDNFSPER VKERDSVEWL PFGDGPRNCI GMRFGQMQAR IGLALLIKDF KFSVCEKTTI PMTYNKEMFL IASNSGIYLK AERV // ID C6AM_DROME STANDARD; PRT; 499 AA. AC Q9V769; Q27592; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 6a22 (EC 1.14.-.-) (CYPVIA22). GN CYP6A22 OR CYT-P450-RBF6-2 OR CG10240. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 338-499 FROM N.A. RC STRAIN=91-R; RX MEDLINE=97128822; PubMed=8973362; RA Maitra S., Dombrowski S.M., Waters L.C., Ganguly R.; RT "Three second chromosome-linked clustered Cyp6 genes show differential RT constitutive and barbital-induced expression in DDT-resistant and RT susceptible strains of Drosophila melanogaster."; RL Gene 180:165-171(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003813; AAF58191.1; -. DR EMBL; L46858; AAB41549.1; -. DR PIR; PC4262; PC4262. DR FlyBase; FBgn0013773; Cyp6a22. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 439 439 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 485 485 N -> H (IN REF. 2). SQ SEQUENCE 499 AA; 57277 MW; F12EA2E04CEB3A7B CRC64; MLDVVALLLI ALAVGFWFVR TRYSYWTRRG IGSEPARFPV GNMEGFRKNK HFIDIVTPIY EKFKGNGAPF AGFFMMLRPV VLVTDLELAK QILIQDFANF EDRGMYHNER DDPLTGHLFR IDGPKWRPLR QKMSPTFTSA KMKYMFPTVC EVGEELTQVC GELADNAMCG ILEIGDLMAR YTSDVIGRCA FGVECNGLRN PEAEFAIMGR RAFSERRHCK LVDGFIESFP EVARFLRMRQ IHQDITDFYV GIVRETVKQR EEQGIVRSDF MNLLIEMKQR GELTIEEMAA QAFIFFAAGF DTSASTLGFA LYELAKQPAL QAKLREEIDQ ALRLHNGEFT YDSMQELRYM ELVIAETLRK YPILPQLTRI SRHLYAAKGD RHFYIEPGQM LLIPVYGIHH DPALYPEPHK FIPERFLADQ LAQRPTAAWL PFGDGPRNCI GMRFGKMQTT IGLVSLLRNF HFSVCPRTDP KIEFLKSNIL LCPANGIYLK VQQLSQMSS // ID C6AN_DROME STANDARD; PRT; 502 AA. AC Q9V771; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6a23 (EC 1.14.-.-) (CYPVIA23). GN CYP6A23 OR CG10242. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003813; AAF58189.2; -. DR FlyBase; FBgn0033978; Cyp6a23. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 445 445 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 502 AA; 58089 MW; 14A13976A629849C CRC64; MSLLLTLIAL LVSLLLFMAR RRHGYWQRRG IPHDVPHPIY GNMKDWPKKR HIAMIFRDYY TKYKRSVYPF AGFYFFFTRS AVITDLELVK RVLIKDFNHF ENRGIFYNEI DDPLSATLFS IEGQKWRHLR HKLTPTFTSG KMKNMFPIIV KVGEEMEKIF SAKTTTGEGQ VLEIVDLVAR YTADVIGNCA FGLNCNSLQN PNAEFVTIGK RAIIERRYGG LLDFLIFGFP KLSRRLRLKL NVQDVEDFYT SIVRNTIDYR LRTNEKRHDF MDSLIEMYEK EQAGNTEDGL SFNEILAQAF IFFVAGFETS STTMGFALYE LALDQDIQDQ LRAEINNVLS KHNNEFTYEG IKEMKYLEQV VMETLRKYPV LAHLTRMTQT DFSPEDPKYF IAKGTTVVIP ALGIHYDPEI YPEPEKFKPE RFTDEAIAAR PSCTWLPFGE GPRNCIGLRF GLMQACVGLA YLIRGYKFSV STETQIPMKF VVKSILLSAE NGIHLKVEKL SK // ID C6D2_DROME STANDARD; PRT; 512 AA. AC Q9W223; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable cytochrome P450 6d2 (EC 1.14.-.-) (CYPVID2). GN CYP6D2 OR CG4373. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003458; AAF46877.1; -. DR EMBL; BT009998; AAQ22467.1; -. DR FlyBase; FBgn0034756; Cyp6d2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 457 457 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 512 AA; 58678 MW; 83F4A67622883876 CRC64; MWTILLTILI AGLLYRYVKR HYTHWQRLGV DEEPAKIPFG VMDTVMKQER SLGMALADIY ARHEGKIVGI YMLNKRSILI RDAQLARQIM TSDFASFHDR GVYVDEDKDP LSANLFNLRG ASWRNLRQKL TPSFSSGKIK GMFGTIDDVG DKLVQHLEGA LDQSDEVEIK DVMTTYAVDI IGSVIFGLEI DSFRNPKNEF REISSSTSRD ESLLLKIHNM SMFICPPIAK LMNRLGYESR ILTSLRDMMK RTIEFREEHN VVRKDMLQLL IRLRNTGKIG EDDDQVWDME TAQEQLKSMS IEKIAAQAFL FYVAGSESTA AASAFTLYEL SMYPELLKEA QEEVDAVLMK HNLKPKDRFT YEAVQDLKFL DICIMETIRK YPGLPFLNRE CTEDYPVPGT NHIIAKGTPI LISLFGMQRD PVYFPNPNGY DPHRFDSNNM NYDQAAYMPF GEGPRHCIAL RMGKVNSKVA VAKILANFDL VQSPRKEVEF RFDAAPVLVT KEPLKLRLTK RK // ID C6D4_DROME STANDARD; PRT; 515 AA. AC Q9VCW1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6d4 (EC 1.14.-.-) (CYPVID4). GN CYP6D4 OR CG12800. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003740; AAF56044.1; -. DR EMBL; AY051606; AAK93030.1; -. DR FlyBase; FBgn0039006; Cyp6d4. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 457 457 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 515 AA; 59182 MW; E1A55FA2C1BAAE4F CRC64; MFSLILLAVT LLTLAWFYLK RHYEYWERRG FPFEKHSGIP FGCLDSVWRQ EKSMGLAIYD VYVKSKERVL GIYLLFRPAV LIRDADLARR VLAQDFASFH DRGVYVDEER DPLSANIFSL RGQSWRSMRH MLSPCFTSGK LKSMFSTSED IGDKMVAHLQ KELPEEGFKE VDIKKVMQNY AIDIIASTIF GLDVNSFENP DNKFRKLVSL ARANNRFNAM FGMMIFLVPS IAQFLFRIGF KNPVGLAMLQ IVKETVEYRE KHGIVRKDLL QLLIQLRNTG KIDENDEKSF SIQKTPDGHI KTISLEAITA QAFIFYIAGQ ETTGSTAAFT IYELAQYPEL LKRLQDEVDE TLAKNDGKIT YDSLNKMEFL DLCVQETIRK YPGLPILNRE CTQDYTVPDT NHVIPKGTPV VISLYGIHHD AEYFPDPETY DPERFSEESR NYNPTAFMPF GEGPRICIAQ RMGRINSKLA IIKILQNFNV EVMSRSEIEF ENSGIALIPK HGVRVRLSKR VPKLS // ID C6D5_DROME STANDARD; PRT; 508 AA. AC Q9VFP1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6d5 (EC 1.14.-.-) (CYPVID5). GN CYP6D5 OR CG3050. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003702; AAF55009.1; -. DR FlyBase; FBgn0038194; Cyp6d5. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 453 453 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 508 AA; 57384 MW; CEDE963953000205 CRC64; MIGIYLLIAA VTLLYVYLKW TFSYWDRKGF PSTGVSIPFG ALESVTKGKR SFGMAIYDMY KSTKEPVIGL YLTLRPALLV RDAQLAHDVL VKDFASFHDR GVYVDEKNDP MSASLFQMEG ASWRALRNKL TPSFTSGKLK AMFETSDSVG DKLVDSIRKQ LPANGAKELE LKKLMATYAI DIIATTIFGL DVDSFADPNN EFQIISKKVN RNNIEDIIRG TSSFLYPGLE KFFVKIGWKQ EATERMRELS NRTVDLREQN NIVRKDLLQL LLQLRNQGKI NTDDNIWSAE STKNGVKSMS KDLIAGQLFL FYVAGYETTA STTSFTLYEL TQNPEVMEKA KEDVRSAIEK HGGKLTYDAI SDMKYLEACI LETARKYPAL PLLNRICTKD YPVPDSKLVI QKGTPIIISL IGMHRDEEYF PDPLAYKPER YLENGKDYTQ AAYLPFGEGP RMCIGARMGK VNVKIAIAKV LSNFDLEIRK EKCEIEFGVY GIPLMPKSGV PVRLSLKK // ID C6G1_DROME STANDARD; PRT; 524 AA. AC Q9V674; O76800; Q95SI8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 6g1 (EC 1.14.-.-) (CYPVIG1) (Cyp6-like protein). GN CYP6G1 OR CYP6-LIKE OR RST(2)DDT OR DDT-R OR CG8453. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Larva; RA Danielson P.B., Al-Zahrani A., Fogleman J.C.; RT "Isolation of a novel CYP6-like cytochrome P450 from Drosophila RT melanogaster."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND POLYMORPHISM. RC STRAIN=Canton-S, Hikone-R, and WC2; RX MEDLINE=22240273; PubMed=12351787; RA Daborn P.J., Yen J.L., Bogwitz M.R., Le Goff G., Feil E., Jeffers S., RA Tijet N., Perry T., Heckel D., Batterham P., Feyereisen R., RA Wilson T.G., ffrench-Constant R.H.; RT "A single P450 allele associated with insecticide resistance in RT Drosophila."; RL Science 297:2253-2256(2002). RN [3] RP SEQUENCE FROM N.A. RA Buzeli R.A., Pedra J.H.F., Scharf M., Pittendrigh B.R.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 216-524 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP FUNCTION. RC STRAIN=Canton-S, Hikone-R, and Wisconsin-1; RX MEDLINE=21669003; PubMed=11810226; RA Daborn P., Boundy S., Yen J., Pittendrigh B., ffrench-Constant R.H.; RT "DDT resistance in Drosophila correlates with Cyp6g1 over-expression RT and confers cross-resistance to the neonicotinoid imidacloprid."; RL Mol. Genet. Genomics 266:556-563(2001). CC -!- FUNCTION: NECESSARY AND SUFFICIENT FOR RESISTANCE TO INSECTICIDES CC DDT AND IMIDACLOPRID. MAY BE INVOLVED IN THE METABOLISM OF INSECT CC HORMONES. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- POLYMORPHISM: HIKONE-R AND WC2 ARE INSECTICIDE RESISTANT STRAINS, CC CANTON-S AND OREGON-RC ARE INSECTICIDE SUSCEPTIBLE. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF083946; AAC33298.1; -. DR EMBL; AY081960; AAL89788.1; -. DR EMBL; AE003823; AAF58557.1; -. DR EMBL; AY060770; AAL28318.1; ALT_INIT. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0025454; Cyp6g1. DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS. DR GO; GO:0008163; P:DDT resistance; IMP. DR GO; GO:0017085; P:response to insecticide; IMP. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 458 458 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 31 34 KGIP -> RHT (IN REF. 1). FT CONFLICT 39 43 TPIIG -> RDHCNTKVVFKWTLGDLC (IN REF. 1). FT CONFLICT 59 59 L -> P (IN REF. 1). FT CONFLICT 108 120 ARCDPHGDPLGYN -> GRLRIPWRSIGLY (IN REF. FT 1). FT CONFLICT 129 133 HWKGI -> IGREF (IN REF. 1). FT CONFLICT 153 153 M -> L (IN REF. 1). FT CONFLICT 274 274 D -> S (IN REF. 1). FT CONFLICT 304 305 AQ -> VS (IN REF. 1). FT CONFLICT 500 500 L -> H (IN REF. 1). SQ SEQUENCE 524 AA; 59866 MW; 35F41CCCA866756F CRC64; MVLTEVLFVV VAALVALYTW FQRNHSYWQR KGIPYIPPTP IIGNTKVVFK MENSFGMHLS EIYNDPRLKD EAVVGIYSMN KPGLIIRDIE LIKSILIKDF NRFHNRYARC DPHGDPLGYN NLFFVRDAHW KGIRTKLTPV FTSGKVKQMY TLMQEIGKDL ELALQRRGEK NSGSFITEIK EICAQFSTDS IATIAFGIRA NSLENPNAEF RNYGRKMFTF TVARAKDFFV AFFLPKLVSL MRIQFFTADF SHFMRSTIGH VMEERERSGL LRNDLIDVLV SLRKEAAAEP SKPHYAKNQD FLVAQAGVFF TAGFETSSST MSFALYEMAK HPEMQKRLRD EINEALVEGG GSLSYEKIQS LEYLAMVVDE VLRMYPVLPF LDREYESVEG QPDLSLKPFY DYTLENGTPV FIPIYALHHD PKYWTNPSQF DPERFSPANR KNIVAMAYQP FGSGPHNCIG SRIGLLQSKL GLVSLLKNHS VRNCEATMKD MKFDPKGFVL QADGGIHLEI VNDRLYDQSA PSLQ // ID C6G2_DROME STANDARD; PRT; 519 AA. AC Q9V675; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6g2 (EC 1.14.-.-) (CYPVIG2). GN CYP6G2 OR CG8859. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003823; AAF58556.1; -. DR FlyBase; FBgn0033696; Cyp6g2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 460 460 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 519 AA; 59607 MW; 8C1770B4264CF8FB CRC64; MELVLLILVA SLIGIAFLAL QQHYSYWRRM GVREIRPKWI VGNLMGLLNM RMSPAEFISQ LYNHPDAENE PFVGIHVFHK PALLLRDPEM VRNILVKDFA GFSNRYSSSD PKGDPLGSQN IFFLKNPAWK EVRLKLSPFF TGNRLKQMFP LIEEVGASLD AHLRQQPLHN ERMRCFDLEA KELCALYTTD VIATVAYGVS ANSFTDPKCE FRRHGRSVFE FNLLRAAEFT LVFFLPHLVP FVRFKVVPAE ATRFLRKTIN YVMSEREKSG QKRNDLIDIL IEFRRSTQLA KASGIKDQFV FEGDILVAQA VLFFTAGFES SSSTMAFAMY ELAKDTDVQQ RLREEIKDAL VESGGQVTLK MIESLEFMQM ILLEVLRMYP PLPFLDRECT SGRDYSLAPF HKKFVVPKGM PVYIPCYALH MDPQYFPQPR KFLPERFSPE NRKLHTPYTY MPFGLGPHGC IGERFGYLQA KVGLVNLLRN HMITTSERTP HRMQLDPKAI ITQAKGGIHL RLVRDALGV // ID C6T1_DROME STANDARD; PRT; 529 AA. AC Q9VRI9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6t1 (EC 1.14.-.-) (CYPVIT1). GN CYP6T1 OR CG1644. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003568; AAF50807.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0031182; Cyp6t1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 472 472 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 529 AA; 60518 MW; 2BAD7875F3BD9C10 CRC64; MIAVFSLIAA ALAVGSLVLL PVVLRGGCLL VVTIVWLWQI LHFWHWRRLG VPFVPAAPFV GNVWNLLRGA CCFGDQFREL YESKEAAGRA FVGIDVLHNH ALLLRDPALI KRIMVEDFAQ FSSRFETTDP TCDTMGSQNL FFSKYETWRE THKIFAPFFA AGKVRNMYGL LENIGQKLEE HMEQKLSGRD SMELEVKQLC ALFTTDIIAS LAFGIEAHSL QNPEAEFRRM CIEVNDPRPK RLLHLFTMFF FPRLSHRVGT HLYSEEYERF MRKSMDYVLS QRAESGENRH DLIDIFLQLK RTEPAESIIH RPDFFAAQAA FLLLAGFDTS SSTITFALYE LAKNTTIQDR LRTELRAALQ SSQDRQLSCD TVTGLVYLRQ VVDEVLRLYP PTAFLDRCCN SRTGYDLSPW NGGSPFKLRA GTPVYISVLG IHRDAQYWPN PEVFDPERFS AEQRQQHHPM TYLPFGAGPR GCIGTLLGQL EIKVGLLHIL NHFRVEVCER TLPEMRFDPK AFVLTAHNGT YLRFVKNSL // ID C6T3_DROME STANDARD; PRT; 501 AA. AC Q9V676; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6t3 (EC 1.14.-.-) (CYPVIT3). GN CYP6T3 OR CG8457. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003823; AAF58555.1; -. DR FlyBase; FBgn0033697; Cyp6t3. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 444 444 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 501 AA; 57844 MW; 84692FA41419C333 CRC64; MLLIWLLLLT IVTLNFWLRH KYDYFRSRGI PHLPPSSWSP MGNLGQLLFL RISFGDLFRQ LYADPRNGQA KIVGFFIFQT PALMVRDPEL IRQVLIKNFN NFLNRFESAD AGDPMGALTL PLAKYHHWKE SRQCMSQLFT SGRMRDVMYS QMLDVASDLE QYLNRKLGDR LERVLPLGRM CQLYTTDVTG NLFYSLNVGG LRRGRSELIT KTKELFNTNP RKVLDFMSVF FLPKWTGVLK PKVFTEDYAR YMRHLVDDHH EPTKGDLINQ LQHFQLSRSS NHYSQHPDFV ASQAGIILLA GFETSSALMG FTLYELAKAP DIQERLRSEL REAFISTATL SYDTLMTLPY LKMVCLEALR LYPAAAFVNR ECTSSASEGF SLQPHVDFIV PPGMPAYISI LGLHRDERFW PEPCVFDPER FGPERSRHIH PMTYIPFGAG PHGCIGSRLG VLQLKLGIVH ILKQYWVETC ERTVSEIRFN PKSFMLESEN EIYLRFCRSS L // ID C6U1_DROME STANDARD; PRT; 485 AA. AC Q9V979; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6u1 (EC 1.14.-.-) (CYPVIU1). GN CYP6U1 OR CG3567. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Nelson B.; RL Unpublished observations (SEP-2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003790; AAF57417.1; ALT_SEQ. DR FlyBase; FBgn0033121; Cyp6u1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 427 427 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 485 AA; 55206 MW; 3EC4D83BE3676AB3 CRC64; MHRTLLTALG ELSVVYALVK FSLGYWKRRG ILHEKPKFLW GNIKGVVSGK RHAQDALQDI YTAYKGRAPF VGFYACLKPF ILALDLKLVH QIIFTDAGHF TSRGLYSNPS GEPLSHNLLQ LDGHKWRSLH AKSAEVFTPA NMQKLLVRLS QISSRIQRDL GEKSLQTINI SELVGAYNTD VMASMAFGLV GQDNVEFAKW TRNYWADFRM WQAYLALEFP LIARLLQYKS YAEPATAYFQ KVALSQLQLH RRRDRQPLQT FLQLYSNAEK PLTDIEIAGQ AFGFVLAGLG PLNATLAFCL YELARQPEVQ DRTRLEINKA LEEHGGQVTP ECLRELRYTK QVLNETLRLH TPHPFLLRRA TKEFEVPGSV FVIAKGNNVL IPTAAIHMDP GIYENPQRFY PERFEEQARR SRPAAAFLPF GDGLRGCIAA RFAEQQLLVG LVALLRQHRY APSAETSIPV EYDNRRLLLM PKSDIKLSVE RVDKL // ID C6V1_DROME STANDARD; PRT; 520 AA. AC Q9VRB3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 6v1 (EC 1.14.-.-) (CYPVIV1). GN CYP6V1 OR CG1829. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003570; AAF50889.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0031126; Cyp6v1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 465 465 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 520 AA; 60762 MW; 36D1F9E4308A974B CRC64; MVYSTNILLA IVTILTGVFI WSRRTYVYWQ RRRVKFVQPT HLLGNLSRVL RLEESFALQL RRFYFDERFR NEPVVGIYLF HQPALLIRDL QLVRTVLVED FVSFSNRFAK CDGRSDKMGA LSLFLAKQPE WREIRTRLAP AFAGAKLKQM FSLMEEIGCD LEWYLKRLTR DLRRGDAERG AIVSIKDVCD LYNTDMIASI AFGLRSYSLR NTQSEIGSHC QDLFRPNVRR IIDLFVIFYL PKLVPLLRPK LFTEPHAEFL RRVIQLVIEE RERGGDLRND LIEMLLTLKK EADLQQDKSH FTHHRDFLAA QAASFEVAGI ETCSASMSFA LYELAKQPLM QSRLRREIRE AFASNPNGRL TYEAVARMEF LDMVVEETLR KYPIVPLLER ECTPINKKRF YSLRPHAECY TRRGMPVFIS NLAIHHDPKY WPDPDRFDPE RFSAANKALQ APMSYMPFGA GPRNCIGMQI GLLQIKLGLV YFLHQHRVEI CDRTVERIQF DAKFALLASE QRIYLKVDCL // ID C6W1_DROME STANDARD; PRT; 514 AA. AC Q9V9L1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable cytochrome P450 6w1 (EC 1.14.-.-) (CYPVIW1). GN CYP6W1 OR CG8345. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003784; AAF57277.1; -. DR EMBL; AY069121; AAL39266.1; -. DR FlyBase; FBgn0033065; Cyp6w1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 450 450 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 514 AA; 59320 MW; 1CA0E9F2692825E5 CRC64; MLLLLLLGSL TIVFYIWQRR TLSFWERHGV KYIRPFPVVG CTREFLTAKV PFFEQIQKFH EAPGFENEPF VGVYMTHRPA LVIRDLELIK TVMIKKFQYF NNRVLQTDPH NDALGYKNLF FARSPGWREL RTKISPVFTS GKIKQMYPLM VKIGKNLQDS AERLGSGTEV QVKDLCSRFT TDLIATIAFG VEANALQDAK SEFFYHNRAI FSLTLSRGID FAIIFMIPAL ASLARVKLFS RETTKFIRSS VNYVLKERER TGEKRNDLID ILLALKREAA ANPGKMSKEV DLDYLVAQAA VFQTAGFETS ASTMTMTLYE LAKNEALQDR LRQEIVDFFG DEDHISYERI QEMPYLSQVV NETLRKYPIV GYIERECSQP AEGERFTLEP FHNMELPHGM SIYMSTVAVH RDPQYWPDPE KYDPERFNSS NRDNLNMDAY MPFGVGPRNC IGMRLGLLQS KLGLVHILRN HRFHTCDKTI KKIEWAPTSP VMASKRDIIL RVEKVSGKKD FGQK // ID C9B1_DROME STANDARD; PRT; 505 AA. AC Q9V4I0; Q24122; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 9b1 (EC 1.14.-.-) (CYPIXB1). GN CYP9B1 OR CG4485. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 326-444 FROM N.A. RC STRAIN=Haag-79, and Hikone-R; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003842; AAF59291.1; -. DR EMBL; U34324; AAA80658.1; -. DR PIR; S70620; S70620. DR FlyBase; FBgn0015038; Cyp9b1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 449 449 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 345 345 P -> L (IN REF. 1). SQ SEQUENCE 505 AA; 58735 MW; 0C628FAC35174E05 CRC64; MSFVEICLVL ATIGLLLFKW STGTFKAFEG RNLYFEKPYP FLGNMAASAL QKASFQKQIS EFYNRTRHHK LVGLFNLRTP MIQINDPQLI KKICVKDFDH FPNHQTLNIP NERLVNDMLN VMRDQHWRNM RSVLTPVFTS AKMRNMFTLM NESFAQCLEH LKSSQPIAAG ENAFELDMKV LCNKLSNDVI ATTAFGLKVN SFDDPENEFH TIGKTLAFSR GLPFLKFMMC LLAPKVFNFF KLTIFDSTNV EYFVRLVVDA MQYREKHNIT RPDMIQLLME AKKESKDNWT DDEIVAQCFI FFFAAFENNS NLICTTAYEL LRNLDIQERL YEEVKETQEA LKGAPLTYDA AQEMTYMDMV ISESLRKWTL SAAADRLCAK DYTLTDDEGT KLFEFKAGDN INIPICGLHW DERFFPQPQR FDPERFSERR KKDLIPYTYL PFGVGPRSCI GNRYAVMQAK GMLYNLMLNY KIEASPRTTR DMWESARGFN IIPTTGFWMQ LVSRK // ID C9B2_DROME STANDARD; PRT; 505 AA. AC Q9V4I1; Q24123; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 9b2 (EC 1.14.-.-) (CYPIXB2). GN CYP9B2 OR CG4486. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 326-444 FROM N.A. RC STRAIN=Hikone-R; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003842; AAF59290.1; -. DR EMBL; AY059439; AAL13345.1; -. DR EMBL; U34325; AAA80659.1; -. DR FlyBase; FBgn0015039; Cyp9b2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 449 449 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 505 AA; 58911 MW; 570AA37FEBC1A8CC CRC64; MALIEICLAL VVIGYLIYKW STATFKTFEE RKLYFEKPYP FVGNMAAAAL QKSSFQRQLT EFYERTRQHK LVGFFNMRTP MITLNDPELI KKVCVKDFDH FPNHQPFITS NDRLFNDMLS VMRDQRWKHM RNTLTPVFTA AKMRNMFTLM NESFAECLQH LDSSSKTLPG RKGFEVDMKV MCNKLSNDII ATTAFGLKVN SYDNPKNEFY EIGQSLVFSR GLQFFKFMLS TLVPKLFSLL KLTIFDSAKV DYFARLVVEA MQYREKHNIT RPDMIQLLME AKNESEDKWT DDEIVAQCFI FFFAAFENNS NLICTTTYEL LYNPDVQERL YEEIVETKKA LNGAPLTYDA VQKMTYMDMV ISESLRKWTL AAATDRLCSK DYTLTDDDGT KLFDFKVGDR INIPISGLHL DDRYFPEPRK FDPDRFSEER KGDMVPYTYL PFGVGPRNCI GNRYALMQVK GMLFNLLLHY KIEASPRTIK DLWGSASGFN FTPRSGFWMH LVPRK // ID C9C1_DROME STANDARD; PRT; 522 AA. AC Q9W130; Q24124; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 9c1 (EC 1.14.-.-) (CYPIXC1). GN CYP9C1 OR CG3616. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 341-459 FROM N.A. RC STRAIN=Haag-79; RX MEDLINE=96262181; PubMed=8676871; RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., RA ffrench-Constant R.H., Feyereisen R.; RT "Cytochrome P450 gene clusters in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:290-297(1996). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003464; AAF47247.1; -. DR EMBL; U34326; AAA80660.1; -. DR PIR; S70621; S70621. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0015040; Cyp9c1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 464 464 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 522 AA; 60538 MW; D80559A6BF84FF31 CRC64; MVFVELSIFV AFIGLLLYKW SVYTFGYFSK RGVAHEKPIP LLGNIPWSVL MGKESYIKHS IDLHLRLKQH KVYGVFNLRD PLYYLSDPEL IRQVGIKNFD TFTNHRKGIT EGFNDTSVIS KSLLSLRDRR WKQMRSTLTP TFTSLKIRQM FELIHFCNVE AVDFVQRQLD AGTSELELKD FFTRYTNDVI ATAAFGIQVN SFKDPNNEFF SIGQRISEFT FWGGLKVMLY ILMPKLMKAL RVPVMDMNNV DYFKKLVFGA MKYRKEQSIV RPDMIHLLME AQRQFKAEQE GSAESAAQQD KAEFNDDDLL AQCLLFFSAG FETVATCLSF TSYELMMNPE VQEKLLAEIL AVKEQLGEKP LDYDTLMGMK YLNCVVSESL RKWPPAFIVD RMCGSDFQLK DEEGEVVVNL REDDLVHINV GALHHDPDNF PEPEQFRPER FDEEHKHEIR QFTYLPFGVG QRSCIGNRLA LMEVKSLIFQ LVLRYHLKPT DRTPADMMSS ISGFRLLPRE LFWCKLESRG PA // ID C9F2_DROME STANDARD; PRT; 516 AA. AC Q9VG82; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 9f2 (EC 1.14.-.-) (CYPIXF2). GN CYP9F2 OR CG11466. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003695; AAF54803.1; ALT_SEQ. DR EMBL; AY058466; AAL13695.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0038037; Cyp9f2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 460 460 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 516 AA; 60278 MW; 3666745A8BDC9D15 CRC64; MLWEFFALFA IAAALFYRWA SANNDFFKDR GIAYEKPVLY FGNMAGMFLR KRAMFDIVCD LYTKGGSKKF FGIFEQRQPL LMVRDPDLIK QITIKDFDHF INHRNVFATS SDDDPHDMSN LFGSSLFSMR DARWKDMRST LSPAFTGSKM RQMFQLMNQV AKEAVDCLKQ DDSRVQENEL DMKDYCTRFT NDVIASTAFG LQVNSFKDRE NTFYQMGKKL TTFTFLQSMK FMLFFALKGL NKILKVELFD RKSTQYFVRL VLDAMKYRQE HNIVRPDMIN MLMEARGIIQ TEKTKASAVR EWSDRDIVAQ CFVFFFAGFE TSAVLMCFTA HELMENQDVQ QRLYEEVQQV DQDLEGKELT YEAIMGMKYL DQVVNEVLRK WPAAIAVDRE CNKDITFDVD GQKVEVKKGD VIWLPTCGFH RDPKYFENPM KFDPERFSDE NKESIQPFTY FPFGLGQRNC IGSRFALLEA KAVIYYLLKD YRFAPAKKSC IPLELITSGF QLSPKGGFWI KLVQRN // ID C9H1_DROME STANDARD; PRT; 518 AA. AC Q9V6H1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 9h1 (EC 1.14.-.-) (CYPIXH1). GN CYP9H1 OR CG17577. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003820; AAF58453.1; -. DR HSSP; P14779; 1JPZ. DR FlyBase; FBgn0033775; Cyp9h1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 462 462 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 518 AA; 60044 MW; A3585251AA179421 CRC64; MDQSMIALAL FIILLVLLYK WSVAKYDVFS ERGVSHEKPW PLIGNIPLKA MIGGMPVLKK MIELHTKHTG SPVYGIYALR DAVFFVRDPE LIKLIGIKEF DHFVNHNSMH NNIQESILSK SLISLRDGRW KEMRNILTPA FTGSKMRIMY DLIQSCSEEG VIHIQEQLEL SQDASIELEM KDYFTRFAND VIATVAFGIS INSFRRKDNE FFRIGQAMSR ISAWSVVKAM LYALFPRLMK VLRIQVLDTK NIDYFSSLVT AAMRYRQEHK VVRPDMIHLL MEAKQQRLAD LSDKSKDELY YSEFTADDLL AQCLLFFFAG FEIISSSLCF LTHELCLNPT VQDRLYEEII SVHEELKGQP LTYDKLTKMK YLDMVVLEAL RKWPPSISTD RECRQDIDLF DENGQKLFSA RKGDVLQIPI FSLHHDPENF EDPEFFNPER FADGHALESR VYMPFGVGPR NCIGNRMALM ELKSIVYQLL LNFKLLPAKR TSRDLLNDIR GHGLKPKNGF WLKFEARQ // ID CA14_DROME STANDARD; PRT; 1775 AA. AC P08120; DT 01-AUG-1988 (Rel. 08, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Collagen alpha 1(IV) chain precursor. GN CG25C OR DCG1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89054012; PubMed=3142875; RA Blumberg B., Mackrell A.J., Fessler J.H.; RT "Drosophila basement membrane procollagen alpha 1(IV). II. Complete RT cDNA sequence, genomic structure, and general implications for RT supramolecular assemblies."; RL J. Biol. Chem. 263:18328-18337(1988). RN [2] RP SEQUENCE FROM N.A. RA Blumberg B.; RL Thesis (1987), University of California / Los Angeles, U.S.A. RN [3] RP SEQUENCE FROM N.A. RA Mackrell A.J.; RL Thesis (1992), University of California / Los Angeles, U.S.A. RN [4] RP SEQUENCE OF 1065-1775 FROM N.A. RX MEDLINE=87194801; PubMed=3106346; RA Blumberg B., Mackrell A.J., Olson P.F., Kurkinen M., Monson J.M., RA Natzle J.E., Fessler J.H.; RT "Basement membrane procollagen IV and its specialized carboxyl domain RT are conserved in Drosophila, mouse, and human."; RL J. Biol. Chem. 262:5947-5950(1987). RN [5] RP SEQUENCE OF 1355-1775 FROM N.A. RX MEDLINE=87246644; PubMed=3109906; RA Cecchini J.P., Knibiehler B., Mirre C., le Parco Y.; RT "Evidence for a type-IV-related collagen in Drosophila melanogaster. RT Evolutionary constancy of the carboxyl-terminal noncollagenous RT domain."; RL Eur. J. Biochem. 165:587-593(1987). RN [6] RP SEQUENCE OF 762-1230 FROM N.A. RX MEDLINE=82197577; PubMed=6210912; RA Monson J.M., Natzle J., Friedman J., McCarthy B.J.; RT "Expression and novel structure of a collagen gene in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 79:1761-1765(1982). CC -!- FUNCTION: COLLAGEN TYPE IV IS SPECIFIC FOR BASEMENT MEMBRANES. CC -!- SUBUNIT: TRIMERS OF TWO ALPHA 1(IV) AND ONE ALPHA 2(IV) CHAIN. CC TYPE IV COLLAGEN FORMS A MESH-LIKE NETWORK LINKED THROUGH CC INTERMOLECULAR INTERACTIONS BETWEEN 7S DOMAINS AND BETWEEN NC1 CC DOMAINS. CC -!- DOMAIN: ALPHA CHAINS OF TYPE IV COLLAGEN HAVE A NONCOLLAGENOUS CC DOMAIN (NC1) AT THEIR C-TERMINUS, FREQUENT INTERRUPTIONS OF THE CC G-X-Y REPEATS IN THE LONG CENTRAL TRIPLE-HELICAL DOMAIN (WHICH MAY CC CAUSE FLEXIBILITY IN THE TRIPLE HELIX), AND A SHORT N-TERMINAL CC TRIPLE-HELICAL 7S DOMAIN. CC -!- PTM: PROLINES AT THE THIRD POSITION OF THE TRIPEPTIDE REPEATING CC UNIT (G-X-Y) ARE HYDROXYLATED IN SOME OR ALL OF THE CHAINS. CC -!- PTM: TYPE IV COLLAGENS CONTAIN NUMEROUS CYSTEINE RESIDUES WHICH CC ARE INVOLVED IN INTER- AND INTRAMOLECULAR DISULFIDE BONDING. 12 OF CC THESE, LOCATED IN THE NC1 DOMAIN, ARE CONSERVED IN ALL KNOWN TYPE CC IV COLLAGENS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23704; AAA28404.1; -. DR EMBL; M96575; AAB59184.1; -. DR EMBL; J02727; AAA28423.1; -. DR EMBL; M28334; AAA28422.1; -. DR EMBL; V00200; CAA23486.2; -. DR PIR; A31893; A31893. DR FlyBase; FBgn0000299; Cg25C. DR GO; GO:0005587; C:collagen type IV; NAS. DR InterPro; IPR008161; Clg_helix. DR InterPro; IPR008160; Collagen. DR InterPro; IPR001442; Procollagn4_C. DR Pfam; PF01413; C4; 2. DR Pfam; PF01391; Collagen; 25. DR ProDom; PD000007; Clg_helix; 9. DR ProDom; PD003923; ProcollagnC4; 1. DR SMART; SM00111; C4; 2. KW Extracellular matrix; Connective tissue; Basement membrane; KW Repeat; Hydroxylation; Glycoprotein; Collagen; Signal. FT SIGNAL 1 23 FT PROPEP 24 ? AMINO-TERMINAL PROPEPTIDE (7S DOMAIN). FT CHAIN ? 1775 COLLAGEN ALPHA 1(IV) CHAIN. FT DOMAIN ? 1544 TRIPLE-HELICAL REGION. FT DOMAIN 1545 1775 NONHELICAL REGION (NC1). FT DISULFID 1569 1655 OR 1652 (BY SIMILARITY). FT DISULFID 1599 1652 OR 1655 (BY SIMILARITY). FT DISULFID 1611 1617 BY SIMILARITY. FT DISULFID 1674 1770 OR 1767 (BY SIMILARITY). FT DISULFID 1708 1767 OR 1770 (BY SIMILARITY). FT DISULFID 1720 1727 BY SIMILARITY. FT CARBOHYD 72 72 N-LINKED (GLCNAC...) (PROBABLE). FT CONFLICT 948 948 L -> S (IN REF. 6). FT CONFLICT 997 997 S -> T (IN REF. 6). FT CONFLICT 1357 1357 Q -> K (IN REF. 5). FT CONFLICT 1360 1360 Q -> K (IN REF. 5). FT CONFLICT 1373 1373 T -> I (IN REF. 5). FT CONFLICT 1496 1496 L -> R (IN REF. 5). FT CONFLICT 1507 1511 ETGNV -> RAGQR (IN REF. 5). FT CONFLICT 1529 1529 E -> K (IN REF. 5). FT CONFLICT 1733 1733 M -> I (IN REF. 5). SQ SEQUENCE 1775 AA; 174119 MW; 2DE5AB23149525CD CRC64; MLPFWKRLLY AAVIAGALVG ADAQFWKTAG TAGSIQDSVK HYNRNEPKFP IDDSYDIVDS AGVARGDLPP KNCTAGYAGC VPKCIAEKGN RGLPGPLGPT GLKGEMGFPG MEGPSGDKGQ KGDPGPYGQR GDKGERGSPG LHGQAGVPGV QGPAGNPGAP GINGKDGCDG QDGIPGLEGL SGMPGPRGYA GQLGSKGEKG EPAKENGDYA KGEKGEPGWR GTAGLAGPQG FPGEKGERGD SGPYGAKGPR GEHGLKGEKG ASCYGPMKPG APGIKGEKGE PASSFPVKPT HTVMGPRGDM GQKGEPGLVG RKGEPGPEGD TGLDGQKGEK GLPGGPGDRG RQGNFGPPGS TGQKGDRGEP GLNGLPGNPG QKGEPGRAGA TGEPGLLGPP GPPGGGRGTP GPPGPKGPRG YVGAPGPQGL NGVDGLPGPQ GYNGQKDGAG LPGRPGNEGP PGKKGEKGTA GLNGPKGSIG PIGHPGPPGP EGQKGDAGLP GYGIQGSKGD AGIPGYPGLK GSKGERGFKG NAGAPGDSKL GRPGTPGAAG APGQKGDAGR PGTPGQKGDM GIKGDVGGKC SSCRAGPKGD KGTSGLPGIP GKDGARGPPG ERGYPGERGH DGINGQTGPP GEKGEDGRTG LPGATGEPGK PALCDLSLIE PLKGDKGYPG APGAKGVQGF KGAEGLPGIP GPKGEFGFKG EKGLSGAPGN DGTPGRAGRD GYPGIPGQSI KGEPGFHGRD GAKGDKGSFG RSGEKGEPGS CALDEIKMPA KGNKGEPGQT GMPGPPGEDG SPGERGYTGL KGNTGPQGPP GVEGPRGLNG PRGEKGNQGA VGVPGNPGKD GLRGIPGRNG QPGPRGEPGI SRPGPMGPPG LNGLQGEKGD RGPTGPIGFP GADGSVGYPG DRGDAGLPGV SGRPGIVGEK GDVGPIGPAG VAGPPGVPGI DGVRGRDGAK GEPGSPGLVG MPGNKGDRGA PGNDGPKGFA GVTGAPGKRG PAGIPGVSGA KGDKGASGLT GNDGPVGGRG PPGAPGLMGI KGDQGLAGAP GQQGLDGMPG EKGNQGFPGL DGPPGLPGDA SEKGQKGEPG PSGLRGDTGP AGTPGWPGEK GLPGLAVHGR AGPPGEKGDQ GRSGIDGRDG INGEKGEQGL QGVWGQPGEK GSVGAPGIPG APGMDGLPGA AGAPGAVGYP GDRGDKGEPG LSGLPGLKGE TGPVGLQGFT GAPGPKGERG IRGQPGLPAT VPDIRGDKGS QGERGYTGEK GEQGERGLTG PAGVAGAKGD RGLQGPPGAS GLNGIPGAKG DIGPRGEIGY PGVTIKGEKG LPGRPGRNGR QGLIGAPGLI GERGLPGLPE SRLVGLPGPI GPAGSKGERG LAGSPGQPGQ DGFPGAPGLK GDTGPQGFKG ERGLNGFEGQ KGDKGDRGLQ GPSGLPGLVG QKGDTGYPGL NGNDGPVGAP GERGFTGPKG RDGRDGTPGL PGQKGEPGML PPPGPKGEPG QPGRNGPKGE PGRPGERGLI GIQGELGEKG ERGLIGETGN VGRPGPKGDR GEPGERGYEG AIGLIGQKGE PGAPAPAALD YLTGILITRH SQSETVPACS AGHTELWTGY SLLYVDGNDY AHNQDLGSCV PRFSTLPVLS CGQNNVCNYA SRNDKTFWLT TNAAIPMMPV ENIEIRQYIS RCVVCEAPAN VIAVHSQTIE VPDCPNGWEG LWIGYSFLMH TAVGNGGGGQ ALQSPGSCLE DFRATPFIEC NGAKGTCHFY ETMTSFWMYN LESSQPFERP QQQTIKAGER QSHVSRCQVC MKNSS // ID CACT_DROME STANDARD; PRT; 500 AA. AC Q03017; Q9V3M6; DT 01-OCT-1993 (Rel. 27, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Developmental protein cactus. GN CACT OR BG:DS02740.15 OR CG5848. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RX MEDLINE=93046660; PubMed=1423618; RA Geisler R., Bergmann A., Hiromi Y., Nuesslein-Volhard C.; RT "Cactus, a gene involved in dorsoventral pattern formation of RT Drosophila, is related to the I kappa B gene family of vertebrates."; RL Cell 71:613-621(1992). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=93046661; PubMed=1423619; RA Kidd S.; RT "Characterization of the Drosophila cactus locus and analysis of RT interactions between cactus and dorsal proteins."; RL Cell 71:623-635(1992). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [4] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN THE FORMATION OF THE DORSOVENTRAL PATTERN. CC IT INHIBITS NUCLEAR TRANSLOCATION OF THE DORSAL MORPHOGEN IN THE CC DORSAL REGION OF THE EMBRYO. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q03017-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q03017-2; Sequence=VSP_000286; CC -!- DEVELOPMENTAL STAGE: IT IS EXPRESSED IN OVARIES AND 0-1 HR CC EMBRYOS. AFTER 2-3 HR UNPHOSPHORYLATED ZYGOTIC PROTEIN IS CC EXPRESSED. BETWEEN 4-8 HR PHOSPHORYLATED ZYGOTIC PROTEIN IS CC EXPRESSED. AFTER 12 HR THE AMOUNT OF UNPHOSPHORYLATED ZYGOTIC CC PROTEIN INCREASES UNTIL BY THE END OF EMBRYOGENESIS IT IS THE MOST CC ABUNDANT FORM OF CACTUS. CC -!- SIMILARITY: TO THE I KAPPA B FAMILY OF VERTEBRATES. CC -!- SIMILARITY: CONTAINS 5 ANK REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L04964; AAA85908.1; -. DR EMBL; L03367; AAA28407.1; -. DR EMBL; L03368; AAA28408.1; -. DR EMBL; AE003415; AAF45005.1; -. DR EMBL; AE003650; AAF53524.1; -. DR PIR; A44269; A44269. DR PIR; B44268; B44268. DR HSSP; P25963; 1IKN. DR FlyBase; FBgn0000250; cact. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0006966; P:antifungal humoral response (sensu Inverteb...; IMP. DR GO; GO:0006967; P:antifungal polypeptide induction; IMP. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR InterPro; IPR002110; ANK. DR Pfam; PF00023; ank; 5. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 5. DR PROSITE; PS50088; ANK_REPEAT; 4. DR PROSITE; PS50297; ANK_REP_REGION; 1. KW Developmental protein; Alternative splicing; ANK repeat; Repeat; KW Phosphorylation. FT DOMAIN 120 136 ASP/GLU-RICH (ACIDIC). FT REPEAT 229 261 ANK 1. FT REPEAT 265 294 ANK 2. FT REPEAT 298 327 ANK 3. FT REPEAT 361 390 ANK 4. FT REPEAT 395 424 ANK 5. FT DOMAIN 469 475 ASP/GLU-RICH (ACIDIC). FT MOD_RES 45 45 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 144 144 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 183 183 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 293 293 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 319 319 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 395 395 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT VARSPLIC 478 500 MYDRFGDPRYFVSYNGGNPMTVA -> VSVTA (in FT isoform Short). FT /FTId=VSP_000286. FT CONFLICT 196 196 A -> G (IN REF. 1 AND 2; AAA28407). FT CONFLICT 222 222 Q -> R (IN REF. 2; AAA28407). SQ SEQUENCE 500 AA; 53818 MW; 9E9711B97CDB499F CRC64; MPSPTKAAEA ATKATATSDC SCSAASVEQR APSNAANPSS SLATSGKIGG KTQDQTAAIN KQKEFAVPNE TSDSGFISGP QSSQIFSEEI VPDSEEQDKD QQESAPQKEQ PVVLDSGIID EEEDQEEQEK EEEHQDTTTA TADSMRLKHS ADTGIPQWTV ESHLVSRGEQ LNNLGQSSST QITGRSKVQS STASTANANP SGSGATSSAP PSSINIMNAW EQFYQQNDDG DTPLHLACIS GSVDVVAALI RMAPHPCLLN IQNDVAQTPL HLAALTAQPN IMRILLLAGA EPTVRDRHGN TALHLSCIAG EKQCVRALTE KFGATEIHEA HRQYGHRSND KAVSSLSYAC LPADLEIRNY DGERCVHLAA EAGHIDILRI LVSHGADINA REGKSGRTPL HIAIEGCNED LANFLLDECE KLNLETATYA GLTAYQFACI MNKSRMQNIL EKRGAETVTP PDSDYDSSDI EDLDDTKMYD RFGDPRYFVS YNGGNPMTVA // ID CADE_DROME STANDARD; PRT; 1507 AA. AC Q24298; Q9W2N1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DE-cadherin precursor (Shotgun protein). GN SHG OR GP150 OR CG3722. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=95046887; PubMed=7958432; RA Oda H., Uemura T., Harada Y., Iwai Y., Takeichi M.; RT "A Drosophila homolog of cadherin associated with armadillo and RT essential for embryonic cell-cell adhesion."; RL Dev. Biol. 165:716-726(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CADHERINS ARE CALCIUM DEPENDENT CELL ADHESION PROTEINS. CC THEY PREFERENTIALLY INTERACT WITH THEMSELVES IN A HOMOPHILIC CC MANNER IN CONNECTING CELLS; CADHERINS MAY THUS CONTRIBUTE TO THE CC SORTING OF HETEROGENEOUS CELL TYPES. N-CADHERIN MAY BE INVOLVED IN CC NEURONAL RECOGNITION MECHANISM. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: STAGE 10 EMBRYOS EXHIBIT INTENSE EXPRESSION IN CC EPITHELIAL CELLS. STAGE 14 EMBRYOS SHOW EXPRESSION IN THE HINDGUT CC (AT THE APICAL POLES OF CELL-CELL BOUNDARIES), AT THE APICAL CC JUNCTIONS OF TRACHEAL CELLS AND IN THE DORSAL LONGITUDINAL TRUNK. CC IN STAGE 16 EMBRYOS THE GLIAL MIDLINE CELLS OF THE CENTRAL NERVOUS CC SYSTEM SHOW STRONG EXPRESSION. CC -!- SIMILARITY: CONTAINS 7 CADHERIN DOMAINS. CC -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN. CC -!- SIMILARITY: CONTAINS 1 LAMININ G-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D28749; BAA05942.1; -. DR EMBL; AE003452; AAF46659.1; -. DR HSSP; P09803; 1EDH. DR FlyBase; FBgn0003391; shg. DR GO; GO:0005912; C:adherens junction; NAS. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0008356; P:asymmetric cytokinesis; IMP. DR GO; GO:0007156; P:homophilic cell adhesion; IDA. DR GO; GO:0007314; P:oocyte anterior/posterior axis determination; NAS. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR000233; Cadherin_C_term. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006210; IEGF. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF00028; cadherin; 7. DR Pfam; PF01049; Cadherin_C_term; 1. DR Pfam; PF00054; laminin_G; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 7. DR SMART; SM00181; EGF; 1. DR SMART; SM00282; LamG; 1. DR PROSITE; PS00232; CADHERIN_1; 5. DR PROSITE; PS50268; CADHERIN_2; 7. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50025; LAM_G_DOMAIN; 1. KW Cell adhesion; Glycoprotein; Transmembrane; Calcium-binding; Repeat; KW Signal; EGF-like domain. FT SIGNAL 1 69 POTENTIAL. FT PROPEP 70 261 POTENTIAL. FT CHAIN 262 1507 DE-CADHERIN. FT DOMAIN 262 1328 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1329 1349 POTENTIAL. FT DOMAIN 1350 1507 CYTOPLASMIC (POTENTIAL). FT DOMAIN 97 195 CADHERIN 1. FT DOMAIN 204 301 CADHERIN 2. FT DOMAIN 311 412 CADHERIN 3. FT DOMAIN 420 522 CADHERIN 4. FT DOMAIN 532 633 CADHERIN 5. FT DOMAIN 631 733 CADHERIN 6. FT DOMAIN 741 835 CADHERIN 7. FT DOMAIN 1084 1123 EGF-LIKE. FT DOMAIN 1125 1313 LAMININ G-LIKE. FT DISULFID 1088 1098 POTENTIAL. FT DISULFID 1090 1112 POTENTIAL. FT DISULFID 1114 1123 POTENTIAL. FT CARBOHYD 317 317 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 466 466 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 552 552 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 766 766 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 949 949 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 983 983 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 999 999 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1073 1073 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1145 1145 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1274 1274 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1290 1290 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 974 974 L -> F (IN REF. 1). SQ SEQUENCE 1507 AA; 169819 MW; DF2B5CAAA29D8EE5 CRC64; MSTSVQRMSR SYHCINMSAT PQAGHLNPAQ QQTHQQHKRK CRDLGRRLIP ARLLLGVIVA ISLLSPALAL HSPPDKNFSG DNRKPAFKNC AGYAPKVKEE QPENTYVLTV EAVDPDPDQV IRYSIVQSPF ERPKFFINPS TGVIFTTHTF DRDEPIHEKF VFVTVQATDN GLPPLDDVCT FNVTIEDIND NAPAFNKARY DESMSENAQP DAVVMTISAS DFDDGNNSLV EYEILRERDF QYFKIDKESG IIYLKRPIDK RPGQSYAIIV RAYNVVPDPP QDAQIEVRIR VVESSIKPPS FVNPIDTPIY LKENLKNFTH PIATLRAVSN MPDKPEVIFE LNTGRTEQTN SKNTFVFNQI GNEVTISLGK TLDYEAITDY TLTMIVRNTH ELGTEHQIKI QVEDVNDNIP YYTEVKSGTI LENEPPGTPV MQVRAFDMDG TSANNIVSFE LADNREYFTI DPNTGNITAL TTFDREERDF YNVKVIASDN SPSSLFDNGE PNRGHQVFRI SIGDKNDHKP HFQQDKYLAE RLLEDANTNT EVIEVKAEDE DNASQILYSI ESGNVGDAFK IGLKTGKITV NQKLDYETIT EYELKVRAFD GIYDDYTTVV IKIEDVNDNP PVFKQDYSVT ILEETTYDDC ILTVEAYDPD IKDRNADQHI VYSIHQNDGN RWTIDNSGCL RLVKTLDRDP PNGHKNWQVL IKANDEDGVG TTVSTVKEVT VTLKDINDNA PFLINEMPVY WQENRNPGHV VQLQANDYDD TPGAGNFTFG IDSEATPDIK TKFSMDGDYL HANVQFDREA QKEYFIPIRI SDSGVPRQSA VSILHLVIGD VNDNAMSEGS SRIFIYNYKG EAPETDIGRV FVDDLDDWDL EDKYFEWKDL PHDQFRLNPS TGMITMLVHT AEGEYDLSFV VTEDSMFVPR HSVDAYVTVV VRELPEEAVD KSGSIRFINV TKEEFISVPR DFQSPDALSL KDRLQLSLAK LFNTSVSNVD VFTVLQNENH TLDVRFSAHG SPYYAPEKLN GIVAQNQQRL ENELDLQMLM VNIDECLIEK FKCEESCTNE LHKSSVPYMI YSNTTSFVGV NAFVQAQCVC EAPLMRRCLN GGSPRYGEND VCDCIDGFTG PHCELVSVAF YGSGYAFYEP IAACNNTKIS LEITPQIDQG LIMYLGPLNF NPLLAISDFL ALELDNGYPV LTVDYGSGAI RIRHQHIKMV ADRTYQLDII LQRTSIEMTV DNCRLSTCQT LGAPIGPNEF LNVNAPLQLG GTPVDLEQLG RQLNWTHVPN QKGFFGCIRN LTINEQTYNL GMPSVFRNID SGCQQSVAVA FSFGIDRNFI IAIIVCLALL LIILLAVVVQ KKQKNGWHEK DIDDIRETII NYEDEGGGER DTDYDLNVLR TQPFYEEKLY KDPHALQGNM RDPNDIPDIA DFLGDKKENC DRDVGATTVD DVRHYAYEGD GNSDGSLSSL ASCTDDGDLN FDYLSNFGPR FRKLADMYGE EPSDTDSNVD DDQGWRI // ID CADF_DROME STANDARD; PRT; 148 AA. AC P45594; Q9W1C4; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cofilin/actin depolymerizing factor homolog (D61 protein) (Twinstar DE protein). GN TSR OR CADF OR CG4254. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94240181; PubMed=8183953; RA Edwards K.A., Montague R.A., Shepard S., Edgar B.A., Erikson R.L., RA Kiehart D.P.; RT "Identification of Drosophila cytoskeletal proteins by induction of RT abnormal cell shape in fission yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 91:4589-4593(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96095784; PubMed=8522587; RA Gunsalus K.C., Bonaccorsi S., Williams E., Verni F., Gatti M., RA Goldberg M.L.; RT "Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF RT homologue, result in defects in centrosome migration and RT cytokinesis."; RL J. Cell Biol. 131:1243-1259(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE ACTIN-BINDING PROTEINS ADF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U08217; AAA19856.1; -. DR EMBL; U24490; AAC46962.1; -. DR EMBL; U24676; AAC46963.1; -. DR EMBL; AE003462; AAF47146.1; -. DR PIR; A57569; A57569. DR HSSP; Q39250; 1F7S. DR FlyBase; FBgn0011726; tsr. DR GO; GO:0003779; F:actin binding; IMP. DR InterPro; IPR002108; Actbind_cofln. DR Pfam; PF00241; cofilin_ADF; 1. DR ProDom; PD002129; Actbind_cofln; 1. DR SMART; SM00102; ADF; 1. DR PROSITE; PS00325; ACTIN_DEPOLYMERIZING; 1. KW Actin-binding; Cytoskeleton; Nuclear protein. FT DOMAIN 19 23 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 96 115 ACTIN-BINDING (POTENTIAL). SQ SEQUENCE 148 AA; 17153 MW; 24F7216033859620 CRC64; MASGVTVSDV CKTTYEEIKK DKKHRYVIFY IRDEKQIDVE TVADRNAEYD QFLEDIQKCG PGECRYGLFD FEYMHQCQGT SESSKKQKLF LMSWCPDTAK VKKKMLYSSS FDALKKSLVG VQKYIQATDL SEASREAVEE KLRATDRQ // ID CADN_DROME STANDARD; PRT; 3097 AA. AC O15943; Q9VJB7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Neural-cadherin precursor (Cadherin-N protein) (DN-cadherin). GN CADN OR CG7100. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM D). RC TISSUE=Embryo, and Head; RX MEDLINE=97388431; PubMed=9247265; RA Iwai Y., Usui T., Hirano S., Steward R., Takeichi M., Uemura T.; RT "Axon patterning requires DN-cadherin, a novel neuronal adhesion RT receptor, in the Drosophila embryonic CNS."; RL Neuron 19:77-89(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP INTERACTION WITH ARM. RX MEDLINE=98298928; PubMed=9635189; RA Loureiro J., Peifer M.; RT "Roles of Armadillo, a Drosophila catenin, during central nervous RT system development."; RL Curr. Biol. 8:622-632(1998). CC -!- FUNCTION: CADHERINS ARE CALCIUM DEPENDENT CELL ADHESION PROTEINS. CC THEY PREFERENTIALLY INTERACT WITH THEMSELVES IN A HOMOPHILIC CC MANNER IN CONNECTING CELLS; CADHERINS MAY THUS CONTRIBUTE TO THE CC SORTING OF HETEROGENEOUS CELL TYPES. MAY ASSOCIATE WITH ARM NEURAL CC ISOFORM AND PARTICIPATE IN THE TRANSMISSION OF DEVELOPMENTAL CC INFORMATION. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=D; CC IsoId=O15943-1; Sequence=Displayed; CC Name=A; CC IsoId=O15943-2; Sequence=VSP_000667, VSP_000668; CC Name=B; CC IsoId=O15943-3; Sequence=VSP_000668; CC Name=C; CC IsoId=O15943-4; Sequence=VSP_000667, VSP_000668, VSP_000669; CC Name=E; CC IsoId=O15943-5; Sequence=VSP_000667; CC Name=F; CC IsoId=O15943-6; Sequence=VSP_000669; CC Name=G; CC IsoId=O15943-7; Sequence=VSP_000667, VSP_000669; CC Name=H; CC IsoId=O15943-8; Sequence=VSP_000668, VSP_000669; CC -!- TISSUE SPECIFICITY: IN THE EMBRYO, THE PROTEIN FIRST APPEARS IN CC THE MESODERM AT STAGE 9 AND IS PRESENT IN THE MYOBLASTS AND MUSCLE CC FIBERS BY STAGE 12 AND STAGE 14, RESPECTIVELY. AT STAGE 12 THE CC PROTEIN IS ALSO LOCATED IN THE AXONS OF THE ENTIRE CNS, BUT NOT IN CC THE GLIAL CELLS. IN THIRD INSTAR LARVAE PROTEIN IS EXPRESSED IN CC THE CNS NEUROPILE, PHOTORECEPTOR AXONS AND PRECURSORS OF ADULT CC MUSCLES. CC -!- SIMILARITY: CONTAINS 16 CADHERIN DOMAINS. CC -!- SIMILARITY: CONTAINS 3 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 2 LAMININ G-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB002397; BAA22151.1; -. DR EMBL; AE003656; AAF53635.1; -. DR EMBL; AE003656; AAN10992.1; -. DR EMBL; AE003656; AAN10993.1; -. DR EMBL; AE003656; AAN10994.1; -. DR EMBL; AE003656; AAN10995.1; -. DR EMBL; AE003656; AAN10996.1; -. DR EMBL; AE003656; AAN10997.1; -. DR EMBL; AE003656; AAN10998.1; -. DR PIR; T00021; T00021. DR HSSP; P00740; 1EDM. DR FlyBase; FBgn0015609; CadN. DR GO; GO:0005911; C:intercellular junction; IDA. DR GO; GO:0008014; F:calcium-dependent cell adhesion molecule ac...; IPI. DR GO; GO:0007412; P:axon target recognition; IMP. DR GO; GO:0007156; P:homophilic cell adhesion; IDA. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR000233; Cadherin_C_term. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF00028; cadherin; 14. DR Pfam; PF01049; Cadherin_C_term; 1. DR Pfam; PF00008; EGF; 2. DR Pfam; PF00054; laminin_G; 2. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 16. DR SMART; SM00179; EGF_CA; 1. DR SMART; SM00282; LamG; 2. DR PROSITE; PS00232; CADHERIN_1; 9. DR PROSITE; PS50268; CADHERIN_2; 16. DR PROSITE; PS00022; EGF_1; 3. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS50026; EGF_3; 3. DR PROSITE; PS50025; LAM_G_DOMAIN; 2. KW Cell adhesion; Glycoprotein; Transmembrane; Calcium-binding; Repeat; KW Signal; EGF-like domain; Alternative splicing. FT SIGNAL 1 36 POTENTIAL. FT PROPEP 37 ? FT CHAIN ? 3097 NEURAL-CADHERIN. FT DOMAIN ? 1454 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1455 1475 POTENTIAL. FT DOMAIN 1476 3097 CYTOPLASMIC (POTENTIAL). FT DOMAIN 181 305 CADHERIN 1. FT DOMAIN 430 543 CADHERIN 2. FT DOMAIN 554 651 CADHERIN 3. FT DOMAIN 660 756 CADHERIN 4. FT DOMAIN 766 858 CADHERIN 5. FT DOMAIN 867 968 CADHERIN 6. FT DOMAIN 978 1078 CADHERIN 7. FT DOMAIN 1087 1183 CADHERIN 8. FT DOMAIN 1193 1299 CADHERIN 9. FT DOMAIN 1307 1414 CADHERIN 10. FT DOMAIN 1423 1514 CADHERIN 11. FT DOMAIN 1523 1630 CADHERIN 12. FT DOMAIN 1639 1742 CADHERIN 13. FT DOMAIN 1749 1861 CADHERIN 14. FT DOMAIN 1870 1966 CADHERIN 15. FT DOMAIN 1974 2085 CADHERIN 16. FT DOMAIN 2346 2377 EGF-LIKE 1. FT DOMAIN 2379 2585 LAMININ G-LIKE 1. FT DOMAIN 2592 2627 EGF-LIKE 2. FT DOMAIN 2631 2822 LAMININ G-LIKE 2. FT DOMAIN 2869 2902 EGF-LIKE 3. FT DISULFID 2346 2357 POTENTIAL. FT DISULFID 2351 2366 POTENTIAL. FT DISULFID 2368 2377 POTENTIAL. FT DISULFID 2592 2607 POTENTIAL. FT DISULFID 2601 2616 POTENTIAL. FT DISULFID 2618 2627 POTENTIAL. FT DISULFID 2869 2880 POTENTIAL. FT DISULFID 2874 2891 POTENTIAL. FT DISULFID 2893 2902 POTENTIAL. FT CARBOHYD 97 97 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 150 150 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 325 325 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 426 426 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 930 930 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1266 1266 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1147 1206 ETYKLEAMAQDKGYPPLSRTVEVQIDVVDRANNPPVWDHTV FT YGPIYVKENMPVGGKVVSI -> DRYRLRVSASDKGTPASA FT ADVDVELDVVDRNNKPPIWDKSIYGPIHIRENVTVGTVVTS FT V (in isoform A, isoform C, isoform E and FT isoform G). FT /FTId=VSP_000667. FT VARSPLIC 1486 1536 RLAASDNLKENYTTVIIHVKDVNDNPPVFERPTYRTQITEE FT DDRNLPKRVL -> KLVASDSLNENQTTIVINVRDVNDLPP FT QFPQTSYERTLDEGMTNTPFTIM (in isoform A, FT isoform B, isoform C and isoform H). FT /FTId=VSP_000668. FT VARSPLIC 2851 2930 GEGRIMSPDSKGCMDRNECLDMPCMNGATCINLEPRLRYRC FT ICPDGFWGENCELVQEGQTLKLSMGALAAILVCLLIILI FT -> PAGYKSSGSTCVNDNECLLFPCRNGGRCRDHHPPKKYE FT CHCPMGFTGMHCELELLASGVLTPSRDFIVALALCLGTLIL FT (in isoform C, isoform F, isoform G and FT isoform H). FT /FTId=VSP_000669. FT VARIANT 1425 1425 E -> K (IN ALLELE CADN-M12; MUSCLE FT DEFECTS). FT CONFLICT 1342 1342 P -> A (IN REF. 1). FT CONFLICT 2786 2786 S -> T (IN REF. 1). SQ SEQUENCE 3097 AA; 347201 MW; 082242F28D9B5CC3 CRC64; MAARRCLNQL RQRYITNRFN ICTCAIFLIS LPFILAIEET TFAGLSAENA ARMLAGSPGD VEKSSLSHHS EMSLVLPHDT YPGFSIKKFK THPVKINGSS HSGAAAYHML DTDYSKYFTV LEDGVVMTTA DISPLVNRPV QLVVVEQTPN ATNTHNLQLF VMHRNDMLRF SGSLLDASGE VRENQPAGTR VRGVPLMQAF SGSILDEELA TPKKVRYTII DGNVDDAFAL QERKANKNIQ ISAKSLVING DDESGVWLVT NRPLDREERA HYDLSVEASD VDGLDRTVSK IQITVLDEND NRPIFKSLDY KFAIAGQKSA SMESNSSVTY QRFAIMGKVE ATDADGDKIA YRLKSPSNVV IIVPQTGEIM LAGEPTSNEL LIEVIAHDLR YPSLVSAKPA KVLLEFLAAE PVSFIMQHLE HDDINNHSHH REKRRVTRAV RPTKRIEFTE ADGDTEGKSV FQLEKETDKE TFKIRDDNPW VTVETNGAVR VKKKWDYEEL GPEKTIDFWV IITNMGHNAG IKYTDNQRVI ILVKDVNDEP PYFINRPLPM QAVVQLNAPP NTPVFTLQAR DPDTDHNIHY FIVRDRTGGR FEVDERSGVV RTRGTDLFQL DMEYVLYVKA EDQNGKVDDR RFQSTPEERL SIVGGKRAPQ FYMPSYEAEI PENQKKDSDI ISIKAKSFAD REIRYTLKAQ GQGAGTFNIG PTSGIVKLAK ELDFEDLRQP HVYSLIVTAT EDSGGFSTSV DLTIRVTDVN DNAPKFELPD YQAHNVDEDI PLGTSILRVK AMDSDSGSNA EIEYLVSDDH FAVDSNGIIV NNKQLDADNN NAYYEFIVTA KDKGEPPKSG VATVRVYTKN KNDEEPKFSQ QVYTPNVDEN AGPNTLVTTV VASDKDGDNV RFGFVGGGTS SGQFVIEDIT GVIRLHNKAI SLDKDKYELN VTAMDDGSCC VNGDQTIHTS TAVVVVFITD VNDNKPVFKD CSTYYPKVEE GAPNGSPVIK VVATDEDKGV NGQVKYSIVQ QPNQKGTKFT VDEETGEVST NKVFDREGDD GKFVSVTVKA TDQGDPSLEG VCSFTVEITD VNDNPPLFDR QKYVENVKQD ASIGTNILRV SASDEDADNN GAIVYSLTAP FNPNDLEYFE IQAESGWIVL KKPLDRETYK LEAMAQDKGY PPLSRTVEVQ IDVVDRANNP PVWDHTVYGP IYVKENMPVG GKVVSIKASS GIEGNPTVFY RLMPGSTAQT NKFHTFYLQQ RPDNGDTWAD IKVNHPLDYE SIKEYNLTIR VENNGAQQLA SEATVYIMLE DVNDEIPLFT EREQETVLEG EPIGTKVTQV NAIDKDGTFP NNQVYYYIVD SPRNEGKEFF EINLQSGEIF TKTVFDREKK GAYALEVEAR DGAPSARPNS NGPNSVTKFI RIGIADKNDN PPYFDKSLYE AEVDENEDIQ HTVLTVTAKD HDESSRIRYE ITSGNIGGAF AVKNMTGAIY VAGALDYETR RRYELRLAAS DNLKENYTTV IIHVKDVNDN PPVFERPTYR TQITEEDDRN LPKRVLQVTA TDGDKDRPQN IVYFLTGQGI DPDNPANSKF DINRTTGEIF VLKPLDRDQP NGRPQWRFTV FAQDEGGEGL VGYADVQVNL KDINDNAPIF PQGVYFGNVT ENGTAGMVVM TMTAVDYDDP NEGSNARLVY SIEKNVIEEE TGSPIFEIEP DTGVIKTAVC CLDRERTPDY SIQVVAMDGG GLKGTGTASI RVKDINDMPP QFTKDEWFTE VDETDGTALP EMPILTVTVH DEDETNKFQY KVIDNSGYGA DKFTMVRNND GTGSLKIVQP LDYEDQLQSN GFRFRIQVND KGEDNDNDKY HVAYSWVVVK LRDINDNKPH FERANVEVSV FEDTKVGTEL EKFKATDPDQ GGKSKVSYSI DRSSDRQRQF AINQNGSVTI QRSLDREVVP RHQVKILAID DGSPPKTATA TLTVIVQDIN DNAPKFLKDY RPVLPEHVPP RKVVEILATD DDDRSKSNGP PFQFRLDPSA DDIIRASFKV EQDQKGANGD GMAVISSLRS FDREQQKEYM IPIVIKDHGS PAMTGTSTLT VIIGDVNDNK MQPGSKDIFV YNYQGQSPDT PIGRVYVYDL DDWDLPDKKF YWEAMEHPRF KLDEDSGMVT MRAGTREGRY HLRFKVYDRK HTQTDIPANV TVTVREIPHE AVVNSGSVRL SGISDEDFIR VWNYRTQSMS RSKMDRFRDK LADLLNTERE NVDIFSVQLK RKHPPLTDVR FSAHGSPYYK PVRLNGIVLM HREEIEKDVG INITMVGIDE CLYENQMCEG SCTNSLEISP LPYMVNANKT ALVGVRVDTI ADCTCGARNF TKPESCRTTP CHNGGRCVDT RFGPHCSCPV GYTGPRCQQT TRSFRGNGWA WYPPLEMCDE SHLSLEFITR KPDGLIIYNG PIVPPERDET LISDFIALEL ERGYPRLLID FGSGTLELRV KTKKTLDDGE WHRIDLFWDT ESIRMVVDFC KSAEIAEMED GTPPEFDDMS CQARGQIPPF NEYLNVNAPL QVGGLYREQF DQSLYFWHYM PTAKGFDGCI RNLVHNSKLY DLAHPGLSRN SVAGCPQTEE VCAQTETTAR CWEHGNCVGS LSEARCHCRP GWTGPACNIP TIPTTFKAQS YVKYALSFEP DRFSTQVQLR FRTREEYGEL FRVSDQHNRE YGILEIKDGH LHFRYNLNSL RTEEKDLWLN AIVVNDGQWH VVKVNRYGSA ATLELDGGEG RRYNETFEFV GHQWLLVDKQ EGVYAGGKAE YTGVRTFEVY ADYQKSCLDD IRLEGKHLPL PPAMNGTQWG QATMARNLEK GCPSNKPCSN VICPDPFECV DLWNVYECTC GEGRIMSPDS KGCMDRNECL DMPCMNGATC INLEPRLRYR CICPDGFWGE NCELVQEGQT LKLSMGALAA ILVCLLIILI LVLVFVVYNR RREAHIKYPG PDDDVRENII NYDDEGGGED DMTAFDITPL QIPIGGPMPP ELAPMKMPIM YPVMTLMPGQ EPNVGMFIEE HKKRADGDPN APPFDDLRNY AYEGGGSTAG SLSSLASGTD DEQQEYDYLG AWGPRFDKLA NMYGPEAPNP HNTELEL // ID CAF1_DROME STANDARD; PRT; 430 AA. AC Q24572; Q9VFB4; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Chromatin assembly factor 1 P55 subunit (CAF-1 P55 subunit) (dCAF-1) DE (Nucleosome remodeling factor 55 kDa subunit) (NURF-55). GN CAF1 OR CG4236. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 256-268; 301-313; 322-334 AND RP 354-376. RC STRAIN=Canton-S; RX MEDLINE=97042445; PubMed=8887645; RA Tyler J.K., Bulger M., Kamakaka R.T., Kobayashi R., Kadonaga J.T.; RT "The p55 subunit of Drosophila chromatin assembly factor 1 is RT homologous to a histone deacetylase-associated protein."; RL Mol. Cell. Biol. 16:6149-6159(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPLEX THAT ASSEMBLES HISTONE OCTAMERS ONTO REPLICATING CC DNA IN VITRO. CAF-1 PERFORMS THE FIRST STEP OF THE NUCLEOSOME CC ASSEMBLY PROCESS, BRINGING NEWLY SYNTHESIZED HISTONES H3 AND H4 TO CC REPLICATING DNA; HISTONES H2A/H2B CAN BIND TO THIS CHROMATIN CC PRECURSOR SUBSEQUENT TO DNA REPLICATION TO COMPLETE THE HISTONE CC OCTAMER. P150 AND P60 FORM COMPLEXES WITH NEWLY SYNTHESIZED CC HISTONES H3 AND ACETYLATED H4 IN CELL EXTRACTS (BY SIMILARITY). CC P55 ASSOCIATES WITH ACETYLTRANSFERASES AND DEACETYLASES IN CELL CC EXTRACTS AND IS ALSO A COMPONENT OF THE NUCLEOSOME REMODELING CC FACTOR COMPLEX (NURF), A PROTEIN COMPLEX CONSISTING OF FOUR CC POLYPEPTIDES THAT FACILITATES THE PERTURBATION OF CHROMATIN CC STRUCTURE IN VITRO IN AN ATP-DEPENDENT MANNER. THIS SUBUNIT MAY CC ASSIST TARGETING OF PROTEIN COMPLEXES TO CHROMATIN. CC -!- SUBUNIT: CAF IS COMPOSED OF FOUR SUBUNITS (P180, P105, P75, AND CC P55). NURF IS COMPOSED OF FOUR SUBUNITS; A 215 KDA PROTEIN, CC IMITATION SWITCH (ISWI), NURF-55, AND NURF-38. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: HIGHEST LEVEL DURING EARLY EMBRYOGENESIS AND CC THEN DECREASES IN LARVAE, PUPAE AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE WD-REPEAT RBAP46/RBAP48/MSI1 FAMILY. CC -!- SIMILARITY: CONTAINS 6 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U62388; AAB37257.1; -. DR EMBL; AE003708; AAF55146.1; -. DR EMBL; AY061408; AAL28956.1; -. DR FlyBase; FBgn0015610; Caf1. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0006340; P:negative regulation of transcription of hom...; IPI. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 5. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Nuclear protein; Repeat; WD repeat. FT REPEAT 126 159 WD 1. FT REPEAT 179 210 WD 2. FT REPEAT 229 260 WD 3. FT REPEAT 275 306 WD 4. FT REPEAT 319 350 WD 5. FT REPEAT 376 407 WD 6. SQ SEQUENCE 430 AA; 48634 MW; 90C5FB959F1660D5 CRC64; MVDRSDNAAE SFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTKQ DGKDYSVHRL ILGTHTSDEQ NHLLIASVQL PSEDAQFDGS HYDNEKGEFG GFGSVCGKIE IEIKINHEGE VNRARYMPQN ACVIATKTPS SDVLVFDYTK HPSKPEPSGE CQPDLRLRGH QKEGYGLSWN PNLNGYLLSA SDDHTICLWD INATPKEHRV IDAKNIFTGH TAVVEDVAWH LLHESLFGSV ADDQKLMIWD TRNNNTSKPS HTVDAHTAEV NCLSFNPYSE FILATGSADK TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLHVWD LSKIGEEQST EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWIICSVSED NIMQVWQMAE NVYNDEEPEI PASELETNTA // ID CAKI_DROME STANDARD; PRT; 898 AA. AC Q24210; Q24272; Q86P03; Q86P17; Q8SX09; Q9VD77; Q9VD78; Q9VD79; DT 15-JUL-1999 (Rel. 38, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calcium/calmodulin-dependent protein kinase (EC 2.7.1.123) (CAKI) DE (Peripheral plasma membrane protein CaMGUK). GN CAKI OR CMG OR CG6703/CG13412. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Oregon-R; RX MEDLINE=97321552; PubMed=9178262; RA Dimitratos S.D., Woods D.F., Bryant P.J.; RT "Camguk, Lin-2, and CASK: novel membrane-associated guanylate kinase RT homologs that also contain CaM kinase domains."; RL Mech. Dev. 63:127-130(1997). RN [2] RP SEQUENCE FROM N.A. (ISOFORM B), AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=96203108; PubMed=8617233; RA Martin J.-R., Ollo R.; RT "A new Drosophila Ca2+/calmodulin-dependent protein kinase (Caki) is RT localized in the central nervous system and implicated in walking RT speed."; RL EMBO J. 15:1865-1876(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS A; B AND C). RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY REGULATE TRANSMEMBRANE PROTEINS THAT BIND CALCIUM, CC CALMODULIN, OR NUCLEOTIDES. CC -!- CATALYTIC ACTIVITY: ATP + PROTEIN = ADP + O-PHOSPHOPROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=B; CC IsoId=Q24210-3; Sequence=Displayed; CC Name=A; CC IsoId=Q24210-2; Sequence=VSP_008088, VSP_008089, VSP_008090; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q24210-1; Sequence=VSP_008086, VSP_008087; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: DURING EMBRYOGENESIS, LARVAL AND PUPAL LIFE, CC FOUND ALMOST EXCLUSIVELY IN THE CENTRAL NERVOUS SYSTEM. IN THE CC ADULT HEAD FOUND IN THE LAMINA, THE NEUROPIL OF THE MEDULLA, CC LOBULA, LOBULA PLATE AND IN THE CENTRAL BRAIN. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE SER/THR CC FAMILY OF PROTEIN KINASES. CAMK SUBFAMILY. CC -!- SIMILARITY: BELONGS TO THE MAGUK FAMILY. CC LIN-27/CASK SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 PDZ/DHR DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 GUANYLATE KINASE-LIKE DOMAIN. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS DUE TO FRAMESHIFTS IN POSITION 537 CC AND 667. CC -!- CAUTION: REF.5 (AAO39536) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC A FRAMESHIFT IN POSITION 114. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U53190; AAC80169.1; -. DR EMBL; X94264; CAA63940.1; ALT_FRAME. DR EMBL; AE003736; AAF55920.2; -. DR EMBL; AE003736; AAF55921.2; -. DR EMBL; AE003736; AAF55922.2; -. DR EMBL; AY094916; AAM11269.1; -. DR EMBL; BT003532; AAO39536.1; ALT_FRAME. DR EMBL; BT003550; AAO39554.1; -. DR HSSP; O14936; 1KWA. DR FlyBase; FBgn0013759; Caki. DR GO; GO:0004685; F:calcium/calmodulin-dependent protein kinase...; IDA. DR GO; GO:0007628; P:adult walking behavior; IMP. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016081; P:synaptic vesicle docking; NAS. DR GO; GO:0016080; P:synaptic vesicle targeting; NAS. DR InterPro; IPR008144; Guanylate_kin. DR InterPro; IPR008145; Guanylt/Ca. DR InterPro; IPR004172; L27. DR InterPro; IPR001478; PDZ. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001452; SH3. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00018; SH3; 1. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00569; L27; 2. DR SMART; SM00228; PDZ; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. DR PROSITE; PS50002; SH3; 1. KW SH3 domain; Membrane; Calmodulin-binding; Transferase; KW Phosphorylation; ATP-binding; Serine/threonine-protein kinase; KW Alternative splicing. FT DOMAIN 12 278 PROTEIN KINASE. FT DOMAIN 306 316 CALMODULIN-BINDING. FT DOMAIN 495 576 PDZ. FT DOMAIN 582 651 SH3. FT DOMAIN 711 883 GUANYLATE KINASE. FT NP_BIND 18 26 ATP (BY SIMILARITY). FT BINDING 41 41 ATP (BY SIMILARITY). FT ACT_SITE 141 141 BY SIMILARITY. FT MOD_RES 292 292 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT VARSPLIC 1 583 Missing (in isoform C). FT /FTId=VSP_008086. FT VARSPLIC 584 584 E -> M (in isoform C). FT /FTId=VSP_008087. FT VARSPLIC 1 317 Missing (in isoform A). FT /FTId=VSP_008088. FT VARSPLIC 318 443 MDPLYATDADMPITGATDEWADEEAGIEAVQRILDCLDDIY FT SLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTSNGR FT APAAEAVGRCRDVLEQLSSTSGGNSLGGKYAKEELMRLLAA FT PHM -> MCQHHGLTSQSLMSGGSHISLLGSSGSSGMSGSG FT VGSSGQSVPQCPAAVAAADAAMMGSNAGGHCRSLSGLSSIS FT IPPPPPALFNPCSSALSLQQAAVTRWGPRTSCPVHSPFRVR FT VPNGSICSGH (in isoform A). FT /FTId=VSP_008089. FT VARSPLIC 584 584 E -> ELFRIRPAPVL (in isoform A). FT /FTId=VSP_008090. FT CONFLICT 7 7 L -> V (IN REF. 1). FT CONFLICT 136 136 D -> E (IN REF. 1). FT CONFLICT 463 463 L -> A (IN REF. 1). FT CONFLICT 465 477 VTPPPMVPYLNGD -> HPAPDGALPQWR (IN REF. FT 1). FT CONFLICT 497 497 Q -> H (IN REF. 1). FT CONFLICT 523 523 I -> L (IN REF. 1). FT CONFLICT 632 632 D -> G (IN REF. 1). FT CONFLICT 740 740 A -> V (IN REF. 1). FT CONFLICT 759 759 S -> N (IN REF. 5; AAO39554). FT CONFLICT 864 878 LTIVNNDISETIATL -> PTMQIHATSPHHTHH (IN FT REF. 5; AAM11269). FT CONFLICT 879 898 MISSING (IN REF. 5; AAM11269). FT CONFLICT 886 892 HTTPQWV -> DIPPRSGC (IN REF. 2). SQ SEQUENCE 898 AA; 100910 MW; 5B16014EC66E0E9B CRC64; MTEDEILFDD VYELCEVIGK GPFSIVRRCI HRESNQQFAV KIVDVAKFTA SPGLSTADLK REATICHMLK HPHIVELLET YSSEGMLYMV FEFMEGSDLC FEVVRRAVAG FVYSEAVACH YMRQILEALR YCHENDILHR DVRPACALLA TVDNSAPVKL GGFGSAIQLP GTRETIETHG RVGCPHYMAP EVVTRRLYGK GCDVWGAGVM LHVLLSGRLP FLGSGVRLQQ SVARGRLSFE APEWKSISAN AKDLVMKMLA ANPHHRLSIT EVLDHPWIRD RDKLQRTHLA DTVEELKRYN ARRKLKGAVQ AIAGGTNMDP LYATDADMPI TGATDEWADE EAGIEAVQRI LDCLDDIYSL QDAHVDADVL RDMLRDNRLH QFLQLFDRIA ATVVTSNGRA PAAEAVGRCR DVLEQLSSTS GGNSLGGKYA KEELMRLLAA PHMQALLHSH DVVARDVYGE EALRVTPPPM VPYLNGDELD NVEGGELQHV TRVRLVQFQK NTDEPMGITL KMTEDGRCIV ARIMHGGMIH RQATLHVGDE IREINGQPVQ HQSVGQLQRM LREARGSVTF KIVPSYRSAP PPCEIFVRAQ FDYNPLDDEL IPCAQAGISF QVGDILQIIS KDDHHWWQAR LDTVGGSAGL IPSPELQEWR IACQTVDKTK QEQVNCSIFG RKKKQCRDKY LAKHNAIFDT LDVVTYEEVV KVPVGDPNFQ RKTLVLLGAH GVGRRHIKNT LISKYPDKYA YPIPHTTRPA KPEEENGRSY YFVSHDEMMA DIGANEYLEY GTHEDAMYGT KLDTIRRIHT EGKMAILDVE PQALKILRTA EFTPYVVFIA APSLQNIADY DGSLERLAKE SEMLRQLYGH FFDLTIVNND ISETIATLET AIDRVHTTPQ WVPVSWLY // ID CALB_DROME STANDARD; PRT; 170 AA. AC P48451; Q9W4D0; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calcineurin B subunit, isoform 1 (Protein phosphatase 2B regulatory DE subunit). GN CANB OR CANB1 OR CNB1 OR CNB OR CG4209. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93054551; PubMed=1331060; RA Guerini D., Montell C., Klee C.B.; RT "Molecular cloning and characterization of the genes encoding the two RT subunits of Drosophila melanogaster calcineurin."; RL J. Biol. Chem. 267:22542-22549(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CALCINEURIN IS A CALCIUM BINDING AND CALMODULIN BINDING CC PROTEIN FOUND IN ALL CELLS FROM YEAST TO MAMMALS, IT IS A CALCIUM CC DEPENDENT, CALMODULIN STIMULATED PROTEIN PHOSPHATASE (BY CC SIMILARITY). CC -!- SUBUNIT: COMPOSED OF TWO COMPONENTS (A AND B), THE A COMPONENT IS CC THE CATALYTIC SUBUNIT AND THE B COMPONENT CONFERS CALCIUM CC SENSITIVITY (BY SIMILARITY). CC -!- MISCELLANEOUS: THIS PROTEIN HAS FOUR FUNCTIONAL CALCIUM-BINDING CC SITES. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97215; AAA28411.1; -. DR EMBL; AE003434; AAF46026.1; -. DR PIR; A44307; A44307. DR HSSP; P06705; 1TCO. DR FlyBase; FBgn0010014; CanB. DR GO; GO:0008021; C:synaptic vesicle; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016083; P:synaptic vesicle fusion; NAS. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR008080; Parvalbumin. DR InterPro; IPR001125; Recoverin. DR Pfam; PF00036; efhand; 4. DR PRINTS; PR01697; PARVALBUMIN. DR PRINTS; PR00450; RECOVERIN. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND; 4. KW Calcium-binding; Repeat. FT CA_BIND 31 42 EF-HAND 1 (POTENTIAL). FT CA_BIND 63 74 EF-HAND 2 (POTENTIAL). FT CA_BIND 100 111 EF-HAND 3 (POTENTIAL). FT CA_BIND 141 152 EF-HAND 4 (POTENTIAL). SQ SEQUENCE 170 AA; 19341 MW; 77D89BE9BD961900 CRC64; MGNETSLPMD MCSNFDADEI RRLGKRFRKL DLDNSGALSI DEFMSLPELQ QNPLVQRVID IFDADGNGEV DFKEFIQGVS QFSVRGDKLS KLRFAFRIYD MDNDGYISNG ELFQVLKMMV GNNLKDTQLQ QIVDKTICFA DKDEDGKISF DEFCSVVGNT DIHKKMVVDV // ID CALC_DROME STANDARD; PRT; 170 AA. AC Q24214; Q9V315; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calcineurin B subunit, isoform 2 (Protein phosphatase 2B regulatory DE subunit). GN CANB2 OR CNB2 OR CG11217. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97080515; PubMed=8921860; RA Warren W.D., Phillips A.M., Howells A.J.; RT "Drosophila melanogaster contains both X-linked and autosomal RT homologues of the gene encoding calcineurin B."; RL Gene 177:149-153(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CALCINEURIN IS A CALCIUM BINDING AND CALMODULIN BINDING CC PROTEIN FOUND IN ALL CELLS FROM YEAST TO MAMMALS, IT IS A CALCIUM CC DEPENDENT, CALMODULIN STIMULATED PROTEIN PHOSPHATASE (BY CC SIMILARITY). CC -!- SUBUNIT: COMPOSED OF A CATALYTIC SUBUNIT (A) AND A REGULATORY CC SUBUNIT (B) (BY SIMILARITY). CC -!- MISCELLANEOUS: THIS PROTEIN HAS FOUR FUNCTIONAL CALCIUM-BINDING CC SITES. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U56245; AAC47350.1; -. DR EMBL; AE003840; AAF59195.2; -. DR EMBL; AY070642; AAL48113.1; -. DR EMBL; AY089602; AAL90340.1; -. DR EMBL; BT003768; AAO41447.1; -. DR PIR; JC5174; JC5174. DR HSSP; P06705; 1TCO. DR FlyBase; FBgn0015614; CanB2. DR GO; GO:0008021; C:synaptic vesicle; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016083; P:synaptic vesicle fusion; NAS. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR008080; Parvalbumin. DR InterPro; IPR001125; Recoverin. DR Pfam; PF00036; efhand; 4. DR PRINTS; PR01697; PARVALBUMIN. DR PRINTS; PR00450; RECOVERIN. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND; 4. KW Calcium-binding; Repeat. FT CA_BIND 31 42 EF-HAND 1 (POTENTIAL). FT CA_BIND 63 74 EF-HAND 2 (POTENTIAL). FT CA_BIND 100 111 EF-HAND 3 (POTENTIAL). FT CA_BIND 141 152 EF-HAND 4 (POTENTIAL). FT CONFLICT 10 10 E -> D (IN REF. 4; AAL48113). FT CONFLICT 40 40 V -> I (IN REF. 4; AAL48113). FT CONFLICT 85 85 K -> R (IN REF. 4; AAL48113). FT CONFLICT 138 138 G -> C (IN REF. 4; AAL48113). SQ SEQUENCE 170 AA; 19267 MW; FDB1BD9DB5A4BDEC CRC64; MGNETSLPME MCSNFDADEI RRLGKRFRKL DLDNSGALSV DEFMSLPELQ QNPLVQRVID IFDADGNGEV DFKEFIQGVS QFSVKGDKLS KLRFAFRIYD MDNDGYISNG ELFQVLKMMV GNNLKDTQLQ QIVDKTIGFA DKDEDGKISF DEFCSVVGNT DIHKKMVVDV // ID CALL_DROME STANDARD; PRT; 148 AA. AC P49258; Q9VBL9; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calmodulin related protein 97A (Androcam protein). GN AND OR CAMR97A OR CG17769. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95071221; PubMed=7980384; RA Fyrberg C., Parker H., Hutchison B., Fyrberg E.A.; RT "Drosophila melanogaster genes encoding three troponin-C isoforms and RT a calmodulin-related protein."; RL Biochem. Genet. 32:119-135(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN CALCIUM-MEDIATED SIGNAL TRANSDUCTION. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76045; CAA53630.1; -. DR EMBL; AE003753; AAF56511.1; -. DR HSSP; P02593; 1FW4. DR FlyBase; FBgn0011273; And. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 4. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND; 2. KW Calcium-binding; Repeat. FT CA_BIND 20 31 EF-HAND 1. FT CA_BIND 56 67 EF-HAND 2 (POTENTIAL). FT CA_BIND 93 104 EF-HAND 3. FT CA_BIND 129 140 EF-HAND 4. FT CONFLICT 105 105 L -> I (IN REF. 1). SQ SEQUENCE 148 AA; 17015 MW; 32DB8DC4B35C6CB8 CRC64; MSELTEEQIA EFKDAFVQFD KEGTGKIATR ELGTLMRTLG QNPTEAELQD LIAEAENNNN GQLNFTEFCG IMAKQMRETD TEEEMREAFK IFDRDGDGFI SPAELRFVMI NLGEKVTDEE IDEMIREADF DGDGMINYEE FVWMISQK // ID CALM_DROME STANDARD; PRT; 148 AA. AC P07181; Q9V3T4; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calmodulin. GN CAM OR CAL OR CG8472. OS Drosophila melanogaster (Fruit fly), OS Locusta migratoria (Migratory locust), OS Aplysia californica (California sea hare), OS Halocynthia roretzi (Sea squirt), OS Branchiostoma floridae (Florida lancelet) (Amphioxus), and OS Branchiostoma lanceolatum (Common lancelet) (Amphioxus). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7004, 6500, 7729, 7739, 7740; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Canton-S, and Oregon-R; RX MEDLINE=87203365; PubMed=3106931; RA Yamanaka M.K., Saugstad J.A., Hanson-Painton O., McCarthy B.J., RA Tobin S.L.; RT "Structure and expression of the Drosophila calmodulin gene."; RL Nucleic Acids Res. 15:3335-3348(1987). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=88062687; PubMed=3119855; RA Smith V.L., Doyle K.E., Maune J.F., Munjaal R.P., Beckingham K.; RT "Structure and sequence of the Drosophila melanogaster calmodulin RT gene."; RL J. Mol. Biol. 196:471-485(1987). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=90294277; PubMed=2113585; RA Doyle K.E., Kovalick G.E., Lee E., Beckingham K.; RT "Drosophila melanogaster contains a single calmodulin gene. Further RT structure and expression studies."; RL J. Mol. Biol. 213:599-605(1990). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 1-140 FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=87228266; PubMed=3035324; RA Beckingham K., Doyle K.E., Maune J.F.; RT "The calmodulin gene of Drosophila melanogaster."; RL Meth. Enzymol. 139:230-247(1987). RN [6] RP SEQUENCE. RC SPECIES=L.migratoria; RA Toda H.; RL Submitted (MAY-1988) to the PIR data bank. RN [7] RP SEQUENCE FROM N.A. RC SPECIES=A.californica; TISSUE=Ganglion; RX MEDLINE=91080147; PubMed=2258931; RA Swanson M.E., Sturner S.F., Schwartz J.H.; RT "Structure and expression of the Aplysia californica calmodulin RT gene."; RL J. Mol. Biol. 216:545-553(1990). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=B.floridae; RA Karabinos A., Riemer D., Weber K.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [9] RP SEQUENCE FROM N.A. RC SPECIES=H.roretzi; RX MEDLINE=99196995; PubMed=10095116; RA Yuasa H.J., Yamamoto H., Takagi T.; RT "The structural organization of the ascidian, Halocynthia roretzi, RT calmodulin genes. The vicissitude of introns during the evolution of RT calmodulin genes."; RL Gene 229:163-169(1999). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=H.roretzi, B.floridae, and B.lanceolatum; RA Yuasa H.J., Takagi T.; RT "Primary structure of Protochordate calmodulin."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [11] RP STRUCTURE BY NMR. RC SPECIES=D.melanogaster; RX MEDLINE=91369934; PubMed=1909892; RA Ikura M., Spera S., Barbato G., Kay L.E., Krinks M., Bax A.; RT "Secondary structure and side-chain 1H and 13C resonance assignments RT of calmodulin in solution by heteronuclear multidimensional NMR RT spectroscopy."; RL Biochemistry 30:9216-9228(1991). RN [12] RP STRUCTURE BY NMR. RC SPECIES=D.melanogaster; RX MEDLINE=92263094; PubMed=1585175; RA Ikura M., Clore G.M., Gronenborn A.M., Zhu G., Klee C.B., Bax A.; RT "Solution structure of a calmodulin-target peptide complex by RT multidimensional NMR."; RL Science 256:632-638(1992). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RC SPECIES=D.melanogaster; RX MEDLINE=92042027; PubMed=1939171; RA Taylor D.A., Sack J.S., Maune J.F., Beckingham K., Quiocho F.A.; RT "Structure of a recombinant calmodulin from Drosophila melanogaster RT refined at 2.2-A resolution."; RL J. Biol. Chem. 266:21375-21380(1991). CC -!- FUNCTION: CALMODULIN MEDIATES THE CONTROL OF A LARGE NUMBER OF CC ENZYMES BY CA(++). AMONG THE ENZYMES TO BE STIMULATED BY THE CC CALMODULIN-CA(++) COMPLEX ARE A NUMBER OF PROTEIN KINASES AND CC PHOSPHATASES. CC -!- MISCELLANEOUS: THIS PROTEIN HAS FOUR FUNCTIONAL CALCIUM-BINDING CC SITES. CC -!- SIMILARITY: CONTAINS 4 EF-HAND CALCIUM-BINDING DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00133; CAA68327.1; -. DR EMBL; X05948; CAA29380.1; -. DR EMBL; X05949; CAA29381.1; -. DR EMBL; X05950; CAB51566.1; -. DR EMBL; X05951; CAA29383.1; -. DR EMBL; AE003823; AAF58542.1; -. DR EMBL; AE003823; AAF58543.1; -. DR EMBL; X56888; CAA40207.1; -. DR EMBL; X64653; -; NOT_ANNOTATED_CDS. DR EMBL; X64655; -; NOT_ANNOTATED_CDS. DR EMBL; Y09863; CAA70990.1; -. DR EMBL; Y09880; CAA71006.1; -. DR EMBL; AB018796; BAA33967.1; -. DR EMBL; AB003081; BAA19786.1; -. DR EMBL; AB003082; BAA19787.1; -. DR EMBL; AB003083; BAA19788.1; -. DR PIR; JK0010; MCLQ. DR PIR; S01173; MCFF. DR PIR; S13248; MCGAC. DR PDB; 4CLN; 15-JUL-92. DR PDB; 2BBM; 31-JAN-94. DR PDB; 2BBN; 31-JAN-94. DR PDB; 1MXE; 07-JAN-03. DR FlyBase; FBgn0000253; Cam. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0016060; P:metarhodopsin inactivation; IGI. DR GO; GO:0016061; P:regulation of light-activated channel activity; IMP. DR GO; GO:0016056; P:rhodopsin mediated signaling; IMP. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 4. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND; 4. KW Calcium-binding; Repeat; Methylation; 3D-structure. FT INIT_MET 0 0 FT MOD_RES 1 1 BLOCKED (IN LOCUST). FT MOD_RES 115 115 METHYLATION (IN LOCUST). FT CA_BIND 20 31 EF-HAND 1. FT CA_BIND 56 67 EF-HAND 2. FT CA_BIND 93 104 EF-HAND 3. FT CA_BIND 129 140 EF-HAND 4. FT HELIX 6 19 FT TURN 21 22 FT STRAND 26 27 FT HELIX 29 38 FT TURN 39 39 FT HELIX 45 55 FT STRAND 63 64 FT HELIX 65 92 FT TURN 93 95 FT HELIX 102 112 FT TURN 113 113 FT HELIX 118 126 FT TURN 127 128 FT HELIX 138 144 FT TURN 145 148 SQ SEQUENCE 148 AA; 16679 MW; 4644E145D5A2D1CA CRC64; ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGFI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVTMMTSK // ID CAN_DROME STANDARD; PRT; 828 AA. AC Q11002; Q9V8U7; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calpain (EC 3.4.22.-) (Calcium-activated neutral proteinase) (CANP). GN CALPA OR CG7563. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95014293; PubMed=7929201; RA Emori Y., Saigo K.; RT "Calpain localization changes in coordination with actin-related RT cytoskeletal changes during early embryonic development of RT Drosophila."; RL J. Biol. Chem. 269:25137-25142(1994). RN [2] RP SEQUENCE FROM N.A., CHARACTERIZATION, AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; RX MEDLINE=95124340; PubMed=7823949; RA Theopold U., Pinter M., Daffre S., Tryselius Y., Friedrich P., RA Nassel D.R., Hultmark D.; RT "CalpA, a Drosophila calpain homolog specifically expressed in a RT small set of nerve, midgut, and blood cells."; RL Mol. Cell. Biol. 15:824-834(1995). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CALPAINS ARE CALCIUM-ACTIVATED NON-LYSOSOMAL THIOL- CC PROTEASES. INVOLVED IN THE ORGANIZATION OF THE ACTIN-RELATED CC CYTOSKELETON DURING EMBRYOGENESIS. CC -!- CATALYTIC ACTIVITY: BROAD ENDOPEPTIDASE SPECIFICITY. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=Long; CC IsoId=Q11002-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q11002-2; Sequence=VSP_005244, VSP_005245; CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED. HIGHEST IN THE CENTRAL CC NERVOUS SYSTEM, BLOOD CELLS AND MIDGUT. CC -!- MISCELLANEOUS: THIS PROTEIN BINDS CALCIUM. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C2. CC -!- SIMILARITY: CONTAINS 2 EF-HAND CALCIUM-BINDING DOMAINS. CC -!- SIMILARITY: CONTAINS 1 CALPAIN CATALYTIC DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78555; CAA55298.1; -. DR EMBL; X78555; CAA55297.1; ALT_INIT. DR EMBL; Z46891; CAA86993.1; -. DR EMBL; Z46892; CAA86994.1; -. DR EMBL; AE003796; AAF57563.1; -. DR EMBL; AY051678; AAK93102.1; -. DR HSSP; Q07009; 1DF0. DR MEROPS; C02.014; -. DR FlyBase; FBgn0012051; CalpA. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR001300; Peptidase_C2. DR InterPro; IPR000169; SHprot_acsite. DR Pfam; PF01067; Calpain_III; 1. DR Pfam; PF00036; efhand; 2. DR Pfam; PF00648; Peptidase_C2; 1. DR PRINTS; PR00704; CALPAIN. DR SMART; SM00720; calpain_III; 1. DR SMART; SM00230; CysPc; 1. DR SMART; SM00054; EFh; 2. DR PROSITE; PS50203; CALPAIN_CAT; 1. DR PROSITE; PS00018; EF_HAND; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; FALSE_NEG. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; FALSE_NEG. KW Hydrolase; Thiol protease; Calcium-binding; Multigene family; KW Alternative splicing. FT DOMAIN 88 387 CALPAIN CATALYTIC. FT DOMAIN 388 557 DOMAIN III. FT DOMAIN 558 577 LINKER. FT DOMAIN 578 827 DOMAIN IV. FT CA_BIND 712 723 EF-HAND 1 (PROBABLE). FT CA_BIND 742 753 EF-HAND 2 (PROBABLE). FT DOMAIN 777 789 ANCESTRAL CALCIUM SITE 3 (POTENTIAL). FT DOMAIN 807 819 ANCESTRAL CALCIUM SITE 4 (POTENTIAL). FT ACT_SITE 143 143 BY SIMILARITY. FT ACT_SITE 299 299 BY SIMILARITY. FT ACT_SITE 327 327 BY SIMILARITY. FT VARSPLIC 554 558 ENDDH -> RTSRQ (in isoform Short). FT /FTId=VSP_005244. FT VARSPLIC 559 828 Missing (in isoform Short). FT /FTId=VSP_005245. FT CONFLICT 35 35 I -> Y (IN REF. 2). FT CONFLICT 306 306 V -> I (IN REF. 2). FT CONFLICT 397 397 N -> H (IN REF. 1). SQ SEQUENCE 828 AA; 93962 MW; 09576D1268BD569C CRC64; MDDLRGFLRQ AGQEFLNAAG EAAMGAAKDV VGSVINEIFI KKEADTKRVL PSIKNMRVLG EKSSSLGPYS EVQDYETILN SCLASGSLFE DPLFPASNES LQFSRRPDRH IEWLRPHEIA ENPQFFVEGY SRFDVQQGEL GDCWLLAATA NLTQESNLFF RVIPAEQSFE ENYAGIFHFR FWQYGKWVDV IIDDRLPTYN GELMYMHSTE KNEFWSALLE KAYAKLHGSY EALKGGSTCE AMEDFTGGVS EWYDLKEAPG NLFTILQKAA ERNSMMGCSI EPDPNVTEAE TPQGLIRGHA YSITKVCLID IVTPNRQGKI PMIRMRNPWG NEAEWNGPWS DSSPEWRYIP EEQKAEIGLT FDRDGEFWMS FQDFLNHFDR VEICNLSPDS LTEDQQNSGK RKWEMSMYEG EWTPGVTAGG CRNFLDTFWH NPQYIITLVD PDEEDEEGQC TVIVALMQKN RRSKRNMGME CLTIGFAIYS LNDRELENRP QGLNFFRYKS SVGRSPHFIN TREVCARFKL PPGHYLIVPS TFDPNEEGEF IIRVFSETQN NMEENDDHVG YGGKADTITP GFPTPKPIDP QKEGLRRLFD SIAGKDMEVD WMELKRILDH SMRDDLPKPV VFNRFSNNMA FETQAAGPGD DGAGACGLLS LICGPFLKGT PFEEQLGMND QSNKRLIGDN PADGGPVTAN AIVDETHGFS KDVCRSMVAM LDADKSGKLG FEEFETLLSE IAKWKAIFKV YDVENTGRVS GFQLREALNS AGYHLNNRVL NVLGHRYGSR DGKIAFDDFI MCAVKIKTYI DIFKERDTEK NETATFTLEE WIERTIYS // ID CAPB_DROME STANDARD; PRT; 276 AA. AC P48603; Q9VQ33; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE F-actin capping protein beta subunit. GN CPB OR ANCP-BETA OR CG17158. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96281970; PubMed=8682865; RA Hopmann R., Cooper J.A., Miller K.G.; RT "Actin organization, bristle morphology, and viability are affected RT by actin capping protein mutations in Drosophila."; RL J. Cell Biol. 133:1293-1305(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: F-ACTIN CAPPING PROTEINS BIND IN A CA(2+)-INDEPENDENT CC MANNER TO THE FAST GROWING ENDS OF ACTIN FILAMENTS (BARBED END) CC THEREBY BLOCKING THE EXCHANGE OF SUBUNITS AT THESE ENDS. UNLIKE CC OTHER CAPPING PROTEINS (SUCH AS GELSOLIN AND SEVERIN), THESE CC PROTEINS DO NOT SEVER ACTIN FILAMENTS. CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. CC -!- SIMILARITY: BELONGS TO THE F-ACTIN CAPPING PROTEIN BETA SUBUNIT CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U35240; AAB38521.1; -. DR EMBL; AE003585; AAF51349.1; -. DR FlyBase; FBgn0011570; cpb. DR GO; GO:0003782; F:F-actin capping activity; IDA. DR InterPro; IPR001698; Factin_cap_beta. DR Pfam; PF01115; F_actin_cap_B; 1. DR PRINTS; PR00192; FACTINCAPB. DR ProDom; PD008617; Factin_cap_beta; 1. DR PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1. KW Cytoskeleton; Actin-binding; Actin capping. SQ SEQUENCE 276 AA; 31363 MW; 512952A1A49629D3 CRC64; MSEMQMDCAL DLMRRLPPQQ IEKNLIDLID LAPDLCEDLL SSVDQPLKIA KDKEHGKDYL LCDYNRDGDS YRSPWSNSYY PPLEDGQMPS ERLRKLEIEA NYAFDQYREM YYEGGVSSVY LWDLDHGFAA VILIKKAGDG SKMIRGCWDS IHVVEVQEKT TGRTAHYKLT STAMLWLQTN KQGSGTMNLG GSLTRQQEQD ANVSESSPHI ANIGKMVEEM ENKIRNTLNE IYFGKTKDIV NGLRSTQSLA DQRQQAAMKQ DLAAAILRRN VKPESN // ID CAPR_DROME STANDARD; PRT; 477 AA. AC Q8ITC7; Q9VP15; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Neuropeptides capa receptor (Cap2b receptor). GN CAPAR OR CG14575. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC STRAIN=Canton-S; RX MEDLINE=22177201; PubMed=12177421; RA Park Y., Kim Y.J., Adams M.E.; RT "Identification of G protein-coupled receptors for Drosophila PRXamide RT peptides, CCAP, corazonin, and AKH supports a theory of RT ligand-receptor coevolution."; RL Proc. Natl. Acad. Sci. U.S.A. 99:11423-11428(2002). RN [2] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=22347021; PubMed=12459185; RA Iversen A., Cazzamali G., Williamson M., Hauser F., RA Grimmelikhuijzen C.J.P.; RT "Molecular cloning and functional expression of a Drosophila receptor RT for the neuropeptides capa-1 and -2."; RL Biochem. Biophys. Res. Commun. 299:628-633(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: ACTS AS A RECEPTOR FOR THE NEUROPEPTIDES CAP-1 AND CAP- CC 2, BUT NOT CAP-3. PROBABLY A COMPONENT OF SIGNAL TRANSDUCTION CC PATHWAY THAT LEADS TO MALPIGHIAN TUBULE FLUID SECRETION IN CC RESPONSE TO THESE LIGANDS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: IN ADULTS, EXPRESSION IN THORAX AND/OR CC ABDOMEN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED WEAKLY IN 16-24 HOUR EMBRYOS AND CC SECOND INSTAR LARVAE AND STRONGLY IN FIRST AND THIRD INSTAR LARVAE CC AND ADULTS. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF522193; AAN10046.1; -. DR EMBL; AF505865; AAO20968.1; -. DR EMBL; AE003594; AAF51746.2; ALT_SEQ. DR FlyBase; FBgn0037100; capaR. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004930; F:G-protein coupled receptor activity; IDA. DR GO; GO:0008188; F:neuropeptide receptor activity; IDA. DR GO; GO:0007589; P:fluid secretion; TAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein. FT DOMAIN 1 72 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 73 93 1 (POTENTIAL). FT DOMAIN 94 109 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 110 130 2 (POTENTIAL). FT DOMAIN 131 145 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 146 166 3 (POTENTIAL). FT DOMAIN 167 189 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 190 210 4 (POTENTIAL). FT DOMAIN 211 237 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 238 258 5 (POTENTIAL). FT DOMAIN 259 295 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 296 316 6 (POTENTIAL). FT DOMAIN 317 335 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 336 356 7 (POTENTIAL). FT DOMAIN 357 477 CYTOPLASMIC (POTENTIAL). FT DISULFID 142 228 BY SIMILARITY. FT CARBOHYD 2 2 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 13 13 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 477 AA; 54004 MW; 34FFB13F301A9F4D CRC64; MNSSTDPTFS ELNASFTNTP DTLFATSVSS DPSHGFGEED YACGTFNCSP KEFVAFVLGP QTLPLYKAVL ITIIFGGIFI TGVVGNLLVC IVIIRHSAMH TATNYYLFSL AVSDLLYLLF GLPTEVFLYW HQYPDLFGMP FCKIRAFISE ACTYVSVFTI VAFSMERFLA ICHPLHLYAM VGFKRAIRII TALWIVSFIS AIPFGLLSDI QYLNYPLDHS RIEESAFCSM SPKIVNEIPV FEVSFCIFFV IPMILIILLY GRMGAKIRSR TNQKLGVQQG TNNRETRNSQ MRKKTVIRML AAVVITFFVC WFPFHLQRLI FLYAKNMDNY LDINEALFSI AGFAYYVSCT VNPIVYSVMS RRYRVAFREL LCGKAVGAYY NSGFARDHSS FRESSAYDRV HSVHVRASQH PNKFETDSSS ANRVLIKKTY SLPLPKNADS TVLSTTDIVI VLENSHTVCE EPKVENDIWI ENEETCI // ID CAPU_DROME STANDARD; PRT; 1059 AA. AC Q24120; Q9VQV8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cappuccino protein. GN CAPU OR CG3399. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=96033799; PubMed=7590229; RA Emmons S., Phan H., Calley J., Chen W., James B., Manseau L.; RT "Cappuccino, a Drosophila maternal effect gene required for polarity RT of the egg and embryo, is related to the vertebrate limb deformity RT locus."; RL Genes Dev. 9:2482-2494(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: CONTAINS 1 FORMIN HOMOLOGY 1 (FH1) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 FORMIN HOMOLOGY 2 (FH2) DOMAIN. CC -!- SIMILARITY: BELONGS TO THE FORMIN HOMOLOGY FAMILY. CAPPUCCINO CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U34258; AAC46925.1; -. DR EMBL; AE003578; AAF51054.1; -. DR PIR; T13286; T13286. DR FlyBase; FBgn0000256; capu. DR GO; GO:0007304; P:eggshell formation (sensu Insecta); IMP. DR GO; GO:0007316; P:pole plasm RNA localization; IMP. DR InterPro; IPR000269; CuNH_oxidase. DR InterPro; IPR003104; FH2. DR InterPro; IPR001265; Formin. DR Pfam; PF02181; FH2; 1. DR PRINTS; PR00828; FORMIN. DR SMART; SM00498; FH2; 1. KW Developmental protein. FT DOMAIN 480 560 FH1 (PRO-RICH). FT DOMAIN 585 1021 FH2. FT CONFLICT 260 260 S -> C (IN REF. 1). FT CONFLICT 364 364 S -> T (IN REF. 1). FT CONFLICT 386 386 T -> S (IN REF. 1). FT CONFLICT 471 471 E -> K (IN REF. 1). FT CONFLICT 495 495 H -> P (IN REF. 1). FT CONFLICT 513 513 MISSING (IN REF. 1). SQ SEQUENCE 1059 AA; 113863 MW; 009B0E24F61B6EA5 CRC64; MALQLGKKLA QVLGSGAGSP LTPGTMEPCA AGSGSPLANG ELFNVSKAKK VELQNLSSRF TAAVTQTPPG VTSSTPNESG VTGPAGPLGA TTSSPSLETQ STVIISFKSS QTPVQSQTNS AASENVEDDT APLPLPPPPP GFGTPTTPLL SSNVLKKVAS FTVEKSSAGN NSSNPPNLCP TSDETTLLAT PCSSSLTVAT LPPEIAVGAA AGGVAGGAGS RRGSSYVPEK LSFAAYEKFE GQMLIKWLIS TMQSNPKSSS GDANQELFNT LALQFCNNLK YVGVLKQISN EHLDCGFSPY EMYQWTHTEQ PTTSLPLTPG KLDKVAAWPF SSTPSGIRAL ESASLASLGA GGVAGSLATI ATASTASSDN QKTLQQILKK RLLNCTTLAE VHAVVNELLS SVDEPPRRPS KRCVNLTELL NASEATVYEY NKTGAEGCVK SFTDAETQTE SEDCEGTCKC GQSSTKVSDN ESAKEDGEKP HAVAPPPPPP PPPLHAFVAP PPPPPPPPPP PPPLANYGAP PPPPPPPPGS GSAPPPPPPA PIEGGGGIPP PPPPMSASPS KTTISPAPLP DPAEGNWFHR TNTMRKSAVN PPKPMRPLYW TRIVTSAPPA PRPPSVANST DSTENSGSSP DEPPAANGAD APPTAPPATK EIWTEIEETP LDNIDEFTEL FSRQAIAPVS KPKELKVKRA KSIKVLDPER SRNVGIIWRS LHVPSSEIEH AIYHIDTSVV SLEALQHMSN IQATEDELQR IKEAAGGDIP LDHPEQFLLD ISLISMASER ISCIVFQAEF EESVTLLFRK LETVSQLSQQ LIESEDLKLV FSIILTLGNY MNGGNRQRGQ ADGFNLDILG KLKDVKSKES HTTLLHFIVR TYIAQRRKEG VHPLEIRLPI PEPADVERAA QMDFEEVQQQ IFDLNKKFLG CKRTTAKVLA ASRPEIMEPF KSKMEEFVEG ADKSMAKLHQ SLDECRDLFL ETMRFYHFSP KACTLTLAQC TPDQFFEYWT NFTNDFKDIW KKEITSLLNE LMKKSKQAQI ESRRNVSTKV EKSGRISLKE RMLMRRSKN // ID CATA_DROME STANDARD; PRT; 506 AA. AC P17336; Q9VVT1; DT 01-AUG-1990 (Rel. 15, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Catalase (EC 1.11.1.6). GN CAT OR CG6871. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96239139; PubMed=8660653; RA Orr W.C., Orr E.C., Legan S.K., Sohal R.S.; RT "Molecular analysis of the Drosophila catalase gene."; RL Arch. Biochem. Biophys. 330:251-258(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90301508; PubMed=2362827; RA Orr E.C., Bewley G.C., Orr W.C.; RT "cDNA and deduced amino acid sequence of Drosophila catalase."; RL Nucleic Acids Res. 18:3663-3663(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 76-92. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- FUNCTION: OCCURS IN ALMOST ALL AEROBICALLY RESPIRING ORGANISMS AND CC SERVES TO PROTECT CELLS FROM THE TOXIC EFFECTS OF HYDROGEN CC PEROXIDE. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: HEME GROUP. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE CATALASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U00145; AAC13738.1; -. DR EMBL; X52286; CAA36529.1; ALT_SEQ. DR EMBL; AE003519; AAF49228.1; -. DR PIR; S12725; CSFF. DR HSSP; P04040; 1F4J. DR FlyBase; FBgn0000261; Cat. DR GO; GO:0004096; F:catalase activity; IDA. DR GO; GO:0042542; P:response to hydrogen peroxide; IMP. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Peroxisome. FT ACT_SITE 73 73 BY SIMILARITY. FT ACT_SITE 146 146 BY SIMILARITY. FT METAL 356 356 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT SITE 504 506 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 5 5 D -> Y (IN REF. 1). FT CONFLICT 12 12 I -> N (IN REF. 1). SQ SEQUENCE 506 AA; 57149 MW; 396377DC5F784ECE CRC64; MAGRDAASNQ LIDYKNSQTV SPGAITTGNG APIGIKDASQ TVGPRGPILL QDVNFLDEMS HFDRERIPER VVHAKGAGAF GYFEVTHDIT QYCAAKIFDK VKKRTPLAVR FSTVGGESGS ADTARDPRGF AVKFYTEDGV WDLVGNNTPV FFIRDPILFP SFIHTQKRNP QTHLKDPDMF WDFLTLRPES AHQVCILFSD RGTPDGYCHM NGYGSHTFKL INAKGEPIYA KFHFKTDQGI KNLDVKTADQ LASTDPDYSI RDLYNRIKTC KFPSWTMYIQ VMTYEQAKKF KYNPFDVTKV WSQKEYPLIP VGKMVLDRNP KNYFAEVEQI AFSPAHLVPG VEPSPDKMLH GRLFSYSDTH RHRLGPNYLQ IPVNCPYKVK IENFQRDGAM NVTDNQDGAP NYFPNSFNGP QECPRARALS SCCPVTGDVY RYSSGDTEDN FGQVTDFWVH VLDKCAKKRL VQNIAGHLSN ASQFLQERAV KNFTQVHADF GRMLTEELNL AKSSKF // ID CATL_DROME STANDARD; PRT; 341 AA. AC Q95029; O97431; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cathepsin L precursor (EC 3.4.22.15) (Cysteine proteinase 1). GN CP1 OR FS(2)50CA OR CG6692. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Hemocyte; RX MEDLINE=97254346; PubMed=9099581; RA Tryselius Y., Hultmark D.; RT "Cysteine proteinase 1 (CP1), a cathepsin L-like enzyme expressed in RT the Drosophila melanogaster haemocyte cell line mbn-2."; RL Insect Mol. Biol. 6:173-181(1997). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=98324856; PubMed=9662479; RA Gray Y.H.M., Sved J.A., Preston C.R., Engels W.R.; RT "Structure and associated mutational effects of the cysteine RT proteinase (CP1) gene of Drosophila melanogaster."; RL Insect Mol. Biol. 7:291-293(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 34-341 FROM N.A., AND CHARACTERIZATION. RC STRAIN=Canton-S; RX MEDLINE=95154345; PubMed=7851441; RA Matsumoto I., Watanabe H., Abe K., Arai S., Emori Y.; RT "A putative digestive cysteine proteinase from Drosophila melanogaster RT is predominantly expressed in the embryonic and larval midgut."; RL Eur. J. Biochem. 227:582-587(1995). CC -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN CC LYSOSOMES. ESSENTIAL FOR ADULT MALE AND FEMALE FERTILITY. MAY PLAY CC A ROLE IN DIGESTION. CC -!- CATALYTIC ACTIVITY: SPECIFICITY CLOSE TO THAT OF PAPAIN. AS CC COMPARED TO CATHEPSIN B, CATHEPSIN L EXHIBITS HIGHER ACTIVITY CC TOWARDS PROTEIN SUBSTRATES, BUT HAS LITTLE ACTIVITY ON Z-ARG-ARG- CC NHMEC, AND NO PEPTIDYL-DIPEPTIDASE ACTIVITY. CC -!- SUBUNIT: DIMER OF A HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE CC BONDS. CC -!- SUBCELLULAR LOCATION: LYSOSOMAL. CC -!- TISSUE SPECIFICITY: IN THE EMBRYO, PREDOMINANTLY EXPRESSED IN THE CC MIDGUT. ALSO EXPRESSED IN LARVAL ALIMENTARY ORGANS SUCH AS CC SALIVARY GLAND AND MIDGUT INCLUDING GASTRIC CAECA. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN EMBRYO, LARVA, PUPA AND ADULT. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U75652; AAB18345.1; -. DR EMBL; AF012089; AAB65749.1; -. DR EMBL; AE003816; AAM68566.1; -. DR EMBL; D31970; BAA06738.1; ALT_SEQ. DR HSSP; O60911; 1FH0. DR MEROPS; C01.092; -. DR FlyBase; FBgn0013770; Cp1. DR InterPro; IPR000668; Peptidase_C1. DR InterPro; IPR000169; SHprot_acsite. DR Pfam; PF00112; Peptidase_C1; 1. DR PRINTS; PR00705; PAPAIN. DR ProDom; PD000158; Peptidase_C1; 1. DR SMART; SM00645; Pept_C1; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. KW Hydrolase; Thiol protease; Glycoprotein; Lysosome; Zymogen; Signal; KW Digestion; Developmental protein. FT SIGNAL 1 18 POTENTIAL. FT PROPEP 19 123 ACTIVATION PEPTIDE. FT CHAIN 124 296 CATHEPSIN L HEAVY CHAIN. FT PROPEP 297 299 FT CHAIN 300 341 CATHEPSIN L LIGHT CHAIN. FT ACT_SITE 148 148 BY SIMILARITY. FT ACT_SITE 287 287 BY SIMILARITY. FT ACT_SITE 308 308 BY SIMILARITY. FT DISULFID 145 188 BY SIMILARITY. FT DISULFID 179 221 BY SIMILARITY. FT DISULFID 280 330 INTERCHAIN (BY SIMILARITY). FT CARBOHYD 97 97 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 198 198 R -> P (IN REF. 4). FT CONFLICT 225 227 KGT -> RAQ (IN REF. 4). FT CONFLICT 247 251 AEAVA -> PEPVP (IN REF. 4). FT CONFLICT 335 335 A -> P (IN REF. 4). SQ SEQUENCE 341 AA; 37970 MW; D18382396ACE1D59 CRC64; MRTAVLLPLL ALLAVAQAVS FADVVMEEWH TFKLEHRKNY QDETEERFRL KIFNENKHKI AKHNQRFAEG KVSFKLAVNK YADLLHHEFR QLMNGFNYTL HKQLRAADES FKGVTFISPA HVTLPKSVDW RTKGAVTAVK DQGHCGSCWA FSSTGALEGQ HFRKSGVLVS LSEQNLVDCS TKYGNNGCNG GLMDNAFRYI KDNGGIDTEK SYPYEAIDDS CHFNKGTVGA TDRGFTDIPQ GDEKKMAEAV ATVGPVSVAI DASHESFQFY SEGVYNEPQC DAQNLDHGVL VVGFGTDESG EDYWLVKNSW GTTWGDKGFI KMLRNKENQC GIASASSYPL V // ID CAUP_DROME STANDARD; PRT; 693 AA. AC P54269; Q9VU00; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein caupolican. GN CAUP OR CG10605. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96180722; PubMed=8620542; RA Gomez-Skarmeta J.-L., del Corral R.D., de la Calle-Mustienes E., RA Ferres-Marco D., Modolell J.; RT "Araucan and caupolican, two members of the novel iroquois complex, RT encode homeoproteins that control proneural and vein-forming genes."; RL Cell 85:95-110(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONTROLS PRONEURAL AND VEIN FORMING GENES. POSITIVE CC TRANSCRIPTIONAL CONTROLER OF AC-SC (ACHAETE-SCUTE). MAY ACT AS AN CC ACTIVATOR THAT INTERACTS WITH THE TRANSCRIPTIONAL COMPLEX CC ASSEMBLED ON THE AC AND SC PROMOTERS AND PARTICIPATES IN CC TRANSCRIPTION INITIATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- MISCELLANEOUS: 'CAUPOLICAN' IS NAMED AFTER THE ARAUCANIAN CC AMERICAN-INDIAN TRIBE, ALSO CALLED MOHAWKS, WHO SHAVED ALL BUT A CC MEDIAL STRIPE OF HAIRS ON THE HEAD. CC -!- SIMILARITY: BELONGS TO THE TALE/IRO HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95178; CAA64485.1; -. DR EMBL; AE003540; AAF49895.1; -. DR HSSP; P41778; 1DU6. DR FlyBase; FBgn0015919; caup. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR003893; Iroquois_homeo. DR Pfam; PF00046; homeobox; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00548; IRO; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Activator; DNA-binding; Homeobox; KW Nuclear protein; Developmental protein. FT DNA_BIND 226 288 HOMEOBOX (TALE-TYPE). FT DOMAIN 300 303 POLY-ASP. FT DOMAIN 405 418 POLY-GLN. FT DOMAIN 501 516 POLY-GLN. FT DOMAIN 517 528 POLY-HIS. FT DOMAIN 565 572 POLY-SER. FT DOMAIN 613 624 POLY-SER. FT CONFLICT 106 106 C -> R (IN REF. 1). FT CONFLICT 316 316 G -> A (IN REF. 1). FT CONFLICT 678 678 G -> A (IN REF. 1). SQ SEQUENCE 693 AA; 73667 MW; FBEB1616493F7EC9 CRC64; MAAYAQFGYA GYPTANQLTT ANTDSQSGHG GGSPLSGTNE ASLSPSGGST ATGLTAGPLS PGAVSQSSHH AGHKGLSTSP AEDVVGGDVP VGLSSAAQDL PSRGSCCENG RPIITDPVSG QTVCSCQYDP ARLAIGGYSR MALPSGGVGV GVYGGPYPSN EQNPYPSIGV DNSAFYAPLS NPYGIKDTSP STEMSAWTSA SLQSTTGYYS YDPTLAAYGY GPNYDLAARR KNATRESTAT LKAWLSEHKK NPYPTKGEKI MLAIITKMTL TQVSTWFANA RRRLKKENKM TWEPKNKTED DDDGMMSDDE KEKDAGDGGK LSTEAFDPGN QLIKSELGKA EKEVDSSGDQ KLDLDREPHN LVAMRGLAPY ATPPGAHPMH AAYSSYAQSH NTHTHPHPQQ MQHHQQQQQQ QQNQQQLQHH QMDQPYYHPG GYGQEESGEF AAQKNPLSRD CGIPVPASKP KIWSVADTAA CKTPPPTAAY LGQNFYPPSS ADQQLPHQPL QQHQQQQLQQ LQQQQQHHHH PHHHHPHHSM ELGSPLSMMS SYAGGSPYSR IPTAYTEAMG MHLPSSSSSS SSTGKLPPTH IHPAPQRVGF PEIQPDTPPQ TPPTMKLNSS GGSSSSSGSS HSSSMHSVTP VTVASMVNIL YSNTDSGYGH GHSHGHGHGH GHGLGHGHGL GHGHGHMGVT SNAYLTEGGR SGS // ID CAZ_DROME STANDARD; PRT; 404 AA. AC Q27294; Q24445; Q9VXI4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE RNA-binding protein cabeza (Sarcoma-associated RNA-binding fly DE homolog) (P19). GN CAZ OR SARFH OR CG3606. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Canton-S; RX MEDLINE=95349623; PubMed=7623847; RA Immanuel D., Zinszner H., Ron D.; RT "Association of SARFH (sarcoma-associated RNA-binding fly homolog) RT with regions of chromatin transcribed by RNA polymerase II."; RL Mol. Cell. Biol. 15:4562-4571(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Canton-S; RX MEDLINE=95223793; PubMed=7708500; RA Stolow D.T., Haynes S.R.; RT "Cabeza, a Drosophila gene encoding a novel RNA binding protein, RT shares homology with EWS and TLS, two genes involved in human sarcoma RT formation."; RL Nucleic Acids Res. 23:835-843(1995). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 39-404 FROM N.A. RC STRAIN=Oregon-R; RA Haynes S.R.; RL Submitted (APR-1988) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 212-261 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=87175568; PubMed=3031652; RA Haynes S.R., Rebbert M.L., Mozer B.A., Forquignon F., Dawid I.B.; RT "Pen repeat sequences are GGN clusters and encode a glycine-rich RT domain in a Drosophila cDNA homologous to the rat helix destabilizing RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 84:1819-1823(1987). CC -!- FUNCTION: MAY PARTICIPATE IN A FUNCTION COMMON TO THE EXPRESSION CC OF MOST GENES TRANSCRIBED BY RNA POLYMERASE II. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=2; CC IsoId=Q27294-1; Sequence=Displayed; CC Name=1; CC IsoId=Q27294-2; Sequence=VSP_005778; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: UBIQUITOUS. ENRICHED IN THE BRAIN AND CENTRAL CC NERVOUS SYSTEM DURING EMBRYOGENESIS. ENRICHED IN THE ADULT HEAD. CC EMBRYOS CONTAIN BOTH TYPE 1 AND TYPE 2 ISOFORMS, WHEREAS LATER IN CC DEVELOPMENT (HEADS AND TORSOS) ONLY THE TYPE 2 ISOFORM IS CC DETECTED. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE DEVELOPING EMBRYO FROM THE CC EARLIEST STAGES OF CELLULARIZATION AND IS SUBSEQUENTLY FOUND IN CC MANY CELL TYPES. CC -!- MISCELLANEOUS: 'CABEZA' MEANS 'HEAD' IN SPANISH. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RANBP2-TYPE ZINC FINGER. CC -!- SIMILARITY: BELONGS TO THE TET FAMILY OF RNP PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13178; AAA86955.1; -. DR EMBL; L37083; AAC41563.1; -. DR EMBL; AE003501; AAF48578.1; -. DR EMBL; M15765; AAA70425.1; -. DR PIR; S54729; S54729. DR FlyBase; FBgn0011571; caz. DR InterPro; IPR000504; RNA_rec_mot. DR InterPro; IPR001876; Znf_RanGDP. DR Pfam; PF00076; rrm; 1. DR Pfam; PF00641; zf-RanBP; 1. DR SMART; SM00360; RRM; 1. DR SMART; SM00547; ZnF_RBZ; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. DR PROSITE; PS01358; ZF_RANBP2_1; 1. DR PROSITE; PS50199; ZF_RANBP2_2; 1. KW Nuclear protein; Zinc-finger; Metal-binding; RNA-binding; KW Alternative splicing. FT DOMAIN 42 111 GLY-RICH. FT DOMAIN 119 205 RNA-BINDING (RRM). FT DOMAIN 212 275 GLY-RICH. FT ZN_FING 280 309 RANBP2-TYPE. FT DOMAIN 312 391 GLY-RICH. FT VARSPLIC 4 47 Missing (in isoform 1). FT /FTId=VSP_005778. FT CONFLICT 39 41 PNY -> LFI (IN REF. 4). FT CONFLICT 92 92 P -> H (IN REF. 3). FT CONFLICT 108 108 G -> GG (IN REF. 3). FT CONFLICT 253 258 MISSING (IN REF. 3). FT CONFLICT 283 283 D -> E (IN REF. 4 AND 5). FT CONFLICT 389 398 DGGPMRNDGG -> MVDQEKRWS (IN REF. 4). SQ SEQUENCE 404 AA; 39141 MW; 7062A0446BEA5984 CRC64; MERGGYGGGS GQGYNNFAVP PPNYQQMPNK TGNYNEPPPN YGKQGGGYDS GSGHRGSGGS GNGGGGGGSW NDRGGNSYGN GGASKDSYNK GPGGYSGGGG GGGGGGGGSG GNDMITQEDT IFVSGMDPST TEQDIETHFG AIGIIKKDKR TMKPKIWLYK NKETGASKGE ATVTYDDTNA AQSAIEWFDG RDFNGNAIKV SLAQRQNNWN KGGGGGGGGG GRGGFGGRRG GGGGGGGGGG GGGRFDRGGG GGGNGGGGGG RYDRGGGGGG GGGGGNVQPR DGDWKCNSCN NTNFAWRNEC NRCKTPKGDD EGSSGGGGGG GYGGGGGGGG YDRGNDRGSG GGGYHNRDRG GNSQGGGGGG GGGGGYSRFN DNNGGGRGGR GGGGGNRRDG GPMRNDGGMR SRPY // ID CB32_DROME STANDARD; PRT; 310 AA. AC P41044; Q9V7W4; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calbindin-32. GN CBP53E OR CBN OR CG6702. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berlin; TISSUE=Brain; RX MEDLINE=93240238; PubMed=8478695; RA Reifegerste R., Grimm S., Albert S., Lipski N., Heimbeck G., RA Hofbauer A., Pflugfelder G.O., Quack D., Reichmuth C., Schug B., RA Zinsmaier K.E., Buchner S., Buchner E.; RT "An invertebrate calcium-binding protein of the calbindin subfamily: RT protein structure, genomic organization, and expression pattern of RT the calbindin-32 gene of Drosophila."; RL J. Neurosci. 13:2186-2198(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- TISSUE SPECIFICITY: EXPRESSED IN A LARGE NUMBER OF NEURON OF THE CC BRAIN AND THE THORACIC GANGLION AS WELL AS IN TWO SMALL MUSCLES OF CC THE THORAX. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. BELONGS TO CC THE CALBINDIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X68566; CAA48566.1; -. DR EMBL; S59242; AAA15214.1; -. DR EMBL; S59190; AAA15214.1; JOINED. DR EMBL; S59191; AAA15214.1; JOINED. DR EMBL; AE003805; AAF57925.1; -. DR EMBL; AY058340; AAL13569.1; -. DR PIR; S37695; S37695. DR HSSP; P02631; 1RRO. DR FlyBase; FBgn0004580; Cbp53E. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 6. DR SMART; SM00054; EFh; 5. DR PROSITE; PS00018; EF_HAND; 5. KW Calcium-binding; Repeat. FT DOMAIN 4 9 POLY-ALA. FT CA_BIND 48 59 EF-HAND 1 (POTENTIAL). FT CA_BIND 98 109 EF-HAND 2 (POTENTIAL). FT CA_BIND 144 155 EF-HAND 3 (POTENTIAL). FT CA_BIND 190 201 EF-HAND 4 (POTENTIAL). FT CA_BIND 237 248 EF-HAND 5 (POTENTIAL). FT DOMAIN 282 293 ANCESTRAL CALCIUM SITE 6. SQ SEQUENCE 310 AA; 35717 MW; F5B53A15816E0F02 CRC64; MDSAAAAAAK RVQIEKAHNF MRQYRDPESR ELKKLSANQF MDVWAHYDKD GNGYIEGTEL DGFLREFVSS ANATDISPEA VTDTMLEELK SCFMEAYDDN QDGKIDIREL AQLLPMEENF LLLFRFDNPL ESSVEFMKIW REYDTDNSGY IEADELKNFL RDLLKEAKKI NDVSEDKLIE YTDTMLQVFD ANKDGRLQLS EMAKLLPVKE NFLCRQVFKG ATKLTKEDIE KVFSLYDRDN SGTIENEELK GFLKDLLELV KKDDYDAQDL AAFEETIMRG VGTDKHGKIS RKELTMILLT LAKISPDDEE // ID CBPD_DROME STANDARD; PRT; 1406 AA. AC P42787; O46058; Q24094; Q24095; Q9W5F3; Q9W5F4; Q9W5F5; DT 01-NOV-1995 (Rel. 32, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Carboxypeptidase D precursor (EC 3.4.17.-) (Silver protein). GN SVR OR CPEPE OR EG:171D11.3 OR CG32818/CG18503/CG4122. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 2 AND 6). RC TISSUE=Embryo; RX MEDLINE=96003800; PubMed=7568156; RA Settle S.H. Jr., Green M.M., Burtis K.C.; RT "The silver gene of Drosophila melanogaster encodes multiple RT carboxypeptidases similar to mammalian prohormone-processing RT enzymes."; RL Proc. Natl. Acad. Sci. U.S.A. 92:9470-9474(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1; 3; 5; 6 AND 7). RC TISSUE=Embryo; RX MEDLINE=22371038; PubMed=12393882; RA Sidyelyeva G., Fricker L.D.; RT "Characterization of Drosophila carboxypeptidase D."; RL J. Biol. Chem. 277:49613-49620(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 3). RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE OF 425-688 FROM N.A., AND FUNCTION. RC STRAIN=Canton-S; RX MEDLINE=95093109; PubMed=8000074; RA Bernasconi P.; RT "Molecular cloning of a Drosophila melanogaster gene coding for an RT homologue of human carboxypeptidase E."; RL Arch. Insect Biochem. Physiol. 27:169-178(1994). CC -!- FUNCTION: REQUIRED FOR THE PROPER MELANIZATION AND SCLEROTIZATION CC OF THE CUTICLE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; Synonyms=B, 1B long tail-1; CC IsoId=P42787-1; Sequence=Displayed; CC Name=2; CC IsoId=P42787-2; Sequence=VSP_000777, VSP_000778; CC Name=3; Synonyms=1A long tail-1; CC IsoId=P42787-3; Sequence=VSP_000773; CC Name=4; Synonyms=A; CC IsoId=P42787-4; Sequence=VSP_000774; CC Name=5; Synonyms=1B long tail-2; CC IsoId=P42787-5; Sequence=VSP_000779; CC Name=6; Synonyms=1A short; CC IsoId=P42787-6; Sequence=VSP_000773, VSP_000775, VSP_000776; CC Name=7; Synonyms=1B short; CC IsoId=P42787-7; Sequence=VSP_000775, VSP_000776; CC -!- DEVELOPMENTAL STAGE: EMBRYONIC AND ADULT STAGES. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M14. CC -!- CAUTION: REF.4 (AAO41630) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U29591; AAA91650.1; -. DR EMBL; U29592; AAA91651.1; -. DR EMBL; AL009147; CAA15634.1; -. DR EMBL; AL009147; CAA15635.1; -. DR EMBL; AF545816; AAN73045.1; -. DR EMBL; AF545817; AAN73046.1; -. DR EMBL; AF545818; AAN73047.1; -. DR EMBL; AF545819; AAN73048.1; -. DR EMBL; AF545820; AAN73049.1; -. DR EMBL; AE003417; AAF45514.2; -. DR EMBL; AE003417; AAF45515.3; -. DR EMBL; AE003417; AAO41630.1; ALT_SEQ. DR EMBL; U03883; AAC46486.1; ALT_SEQ. DR PIR; T13420; T13420. DR PIR; T13421; T13421. DR MEROPS; M14.011; -. DR MEROPS; M14.016; -. DR FlyBase; FBgn0004648; svr. DR InterPro; IPR008969; CarboxypepD_reg. DR InterPro; IPR000834; Peptidase_M14. DR InterPro; IPR008575; Peptidase_M14B. DR Pfam; PF05885; DUF857; 2. DR Pfam; PF00246; Zn_carbOpept; 2. DR PRINTS; PR00765; CRBOXYPTASEA. DR SMART; SM00631; Zn_pept; 2. DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2. DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2. KW Hydrolase; Carboxypeptidase; Metalloprotease; Metal-binding; Zinc; KW Cuticle; Repeat; Signal; Transmembrane; Alternative splicing. FT SIGNAL 1 25 POTENTIAL. FT CHAIN 26 1406 CARBOXYPEPTIDASE D. FT DOMAIN 26 1312 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1313 1333 POTENTIAL. FT DOMAIN 1334 1406 CYTOPLASMIC (POTENTIAL). FT DOMAIN 26 446 DOMAIN 1. FT DOMAIN 447 865 DOMAIN 2. FT DOMAIN 866 1313 DOMAIN 3. FT SITE 1343 1345 CELL ATTACHMENT SITE (POTENTIAL). FT METAL 101 101 ZINC 1 (BY SIMILARITY). FT METAL 104 104 ZINC 1 (BY SIMILARITY). FT METAL 217 217 ZINC 1 (BY SIMILARITY). FT ACT_SITE 305 305 NUCLEOPHILE 1 (BY SIMILARITY). FT METAL 517 517 ZINC 2 (BY SIMILARITY). FT METAL 520 520 ZINC 2 (BY SIMILARITY). FT METAL 626 626 ZINC 2 (BY SIMILARITY). FT ACT_SITE 708 708 PROTON DONOR (BY SIMILARITY). FT ACT_SITE 730 730 NUCLEOPHILE 2 (BY SIMILARITY). FT CARBOHYD 133 133 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 269 269 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 458 458 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 549 549 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 612 612 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 652 652 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 787 787 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 808 808 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 981 981 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1152 1152 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1251 1251 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 152 MPTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYA FT SQEQLEDLFAGLEKAYPNQAKVHFLGRSLEGRNLLALQISR FT NTRSRNLLTPPVKYIANMHGDETVGRQLLVYMAQYLLGNHE FT RISDLGQLVNSTDIYLVPTMNPDGYALSQ -> MLFFCLAL FT IIGCAVGEYSEVRVIQEEDNFLESPHYLKNEEIGDLFSQLA FT KDYPDLAQTYTIGKSLEDRPIYALALSAPTGESKNGDLLRP FT MVKLVANIQGDEAVGRQMVLYMAEYLATHYDGDPKVQALLN FT LTEIHFLPTCNPDGFAKAK (in isoform 3 and FT isoform 6). FT /FTId=VSP_000773. FT VARSPLIC 1 152 MPTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYA FT SQEQLEDLFAGLEKAYPNQAKVHFLGRSLEGRNLLALQISR FT NTRSRNLLTPPVKYIANMHGDETVGRQLLVYMAQYLLGNHE FT RISDLGQLVNSTDIYLVPTMNPDGYALSQ -> MNTCL FT (in isoform 4). FT /FTId=VSP_000774. FT VARSPLIC 426 435 NFRKVKVERS -> ISSFYSPYYF (in isoform 6 FT and isoform 7). FT /FTId=VSP_000775. FT VARSPLIC 436 1406 Missing (in isoform 6 and isoform 7). FT /FTId=VSP_000776. FT VARSPLIC 1106 1119 VWRKNIDKIKNFLA -> FGAKTSIRLRTFWL (in FT isoform 2). FT /FTId=VSP_000777. FT VARSPLIC 1120 1406 Missing (in isoform 2). FT /FTId=VSP_000778. FT VARSPLIC 1385 1406 ELSQRAHLVNNQTNYSFIIQAA -> GMTIQPYFDEEQLER FT ILHTDDDDDDGPHMEPELDVADDSEDDIVMLHNNGNKRRH FT (in isoform 5). FT /FTId=VSP_000779. FT CONFLICT 733 733 C -> Y (IN REF. 1). FT CONFLICT 1041 1041 V -> E (IN REF. 1). SQ SEQUENCE 1406 AA; 158789 MW; E7CF31AEC21363BD CRC64; MPTLGLLFAS IGIAVLAMGV PHCRGYTIKE DESFLQQPHY ASQEQLEDLF AGLEKAYPNQ AKVHFLGRSL EGRNLLALQI SRNTRSRNLL TPPVKYIANM HGDETVGRQL LVYMAQYLLG NHERISDLGQ LVNSTDIYLV PTMNPDGYAL SQEGNCESLP NYVGRGNAAN IDLNRDFPDR LEQSHVHQLR AQSRQPETAA LVNWIVSKPF VLSANFHGGA VVASYPYDNS LAHNECCEES LTPDDRVFKQ LAHTYSDNHP IMRKGNNCND SFSGGITNGA HWYELSGGMQ DFNYAFSNCF ELTIELSCCK YPAASTLPQE WQRNKASLLQ LLRQAHIGIK GLVTDASGFP IADANVYVAG LEEKPMRTSK RGEYWRLLTP GLYSVHASAF GYQTSAPQQV RVTNDNQEAL RLDFKLAPVE TNFDGNFRKV KVERSEPPQK LKKQFNGFLT PTKYEHHNFT AMESYLRAIS SSYPSLTRLY SIGKSVQGRD LWVLEIFATP GSHVPGVPEF KYVANMHGNE VVGKELLLIL TKYMLERYGN DDRITKLVNG TRMHFLYSMN PDGYEISIEG DRTGGVGRAN AHGIDLNRNF PDQYGTDRFN KVTEPEVAAV MNWTLSLPFV LSANLHGGSL VANYPFDDNE NDFNDPFMRL RNSSINGRKP NPTEDNALFK HLAGIYSNAH PTMYLGQPCE LFQNEFFPDG ITNGAQWYSV TGGMQDWNYV RAGCLELTIE MGCDKFPKAA ELSRYWEDHR EPLLQFIEQV HCGIHGFVHS TIGTPIAGAV VRLDGANHST YSQVFGDYWK LALPGRHNLT VLGDNYAPLR MEVEVPDVHP FEMRMDITLM PDDPQHWASA NDFRIIENVV NTRYHTNPQV RARLAELENQ NGQIASFGYA DSEFGTIFNY LKMTSDIGEP EEHKYKLLVV SSLYDTTAPL GREILLNLIR HLVEGFKLQD TSVVELLKRS VIYFLPQTSK FQNVFDMYNS NTSICDPVLG DELAERILGP ETDQAKDVFL QFLRSERFDL MLTFGAGNSD LNYPKGDSVL VKFAHRMQRT EFNYSPLQCP PSATRQLHRE TTERLTNMMY RIYNLPVYTL GISCCRMPHQ KKIASVWRKN IDKIKNFLAL VKTGVSGLVQ NDKGQPLREA YVRLLEHDRI INVTKNVARF QLMLPHGLYG LEVTAPNYES QMIKVDVEDG RVTELGIIRM HPFTLIRGVV LELPNNDNRA TTSIAGVVLD ESNHPVRNAK VSVVGQTQLR NFTGSMGQYR ISAVPLGTIT LKVEAPRHLE ATRQMHLIQG GLATENVVFH LKVNEHVFGL PRFLFILCAS VLIIVGVIVC VLCAQFWFYR RHRGDKPYYN FSLLPQRGKE QFGLEDDDGG DDGETELFRS PIKRELSQRA HLVNNQTNYS FIIQAA // ID CC2C_DROME STANDARD; PRT; 314 AA. AC P23573; Q9TXB2; Q9VDJ4; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cell division control protein 2 cognate (EC 2.7.1.-). GN CDC2C OR CG10498. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=91006057; PubMed=2120045; RA Lehner C.F., O'Farrell P.H.; RT "Drosophila cdc2 homologs: a functional homolog is coexpressed with a RT cognate variant."; RL EMBO J. 9:3573-3581(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 21-167 FROM N.A. RC TISSUE=Imaginal disks; RX MEDLINE=92335284; PubMed=1378625; RA Biggs W.H. III, Zipursky S.L.; RT "Primary structure, expression, and signal-dependent tyrosine RT phosphorylation of a Drosophila homolog of extracellular signal- RT regulated kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992). CC -!- FUNCTION: LIKE CDC2, COULD PLAY A KEY ROLE IN THE CONTROL OF THE CC EUKARYOTIC CELL CYCLE. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CDC2/CDKX SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57486; CAA40724.1; -. DR EMBL; AE003731; AAF55799.1; -. DR EMBL; AY051671; AAK93095.1; -. DR PIR; E46036; E46036. DR HSSP; Q00534; 1BI8. DR FlyBase; FBgn0004107; cdc2c. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Cell cycle; Cell division; Mitosis; Phosphorylation. FT DOMAIN 8 287 PROTEIN KINASE. FT NP_BIND 14 22 ATP (BY SIMILARITY). FT BINDING 37 37 ATP (BY SIMILARITY). FT ACT_SITE 130 130 BY SIMILARITY. FT MOD_RES 18 18 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 19 19 PHOSPHORYLATION (BY SIMILARITY). FT CONFLICT 27 27 S -> T (IN REF. 4). FT CONFLICT 119 119 G -> A (IN REF. 4). SQ SEQUENCE 314 AA; 35888 MW; 576A88767F9D35C0 CRC64; MTTILDNFQR AEKIGEGTYG IVYKARSNST GQDVALKKIR LEGETEGVPS TAIREISLLK NLKHPNVVQL FDVVISGNNL YMIFEYLNMD LKKLMDKKKD VFTPQLIKSY MHQILDAVGF CHTNRILHRD LKPQNLLVDT AGKIKLADFG LARAFNVPMR AYTHEVVTLW YRAPEILLGT KFYSTGVDIW SLGCIFSEMI MRRSLFPGDS EIDQLYRIFR TLSTPDETNW PGVTQLPDFK TKFPRWEGTN MPQPITEHEA HELIMSMLCY DPNLRISAKD ALQHAYFRNV QHVDHVALPV DPNAGSASRL TRLV // ID CC37_DROME STANDARD; PRT; 389 AA. AC Q24276; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Hsp90 co-chaperone Cdc37 (Hsp90 chaperone protein kinase-targeting DE subunit) (Enhancer of sevenless 3B). GN CDC37 OR E(SEV)3B OR CG12019. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND SUBUNIT. RX MEDLINE=94291193; PubMed=8020093; RA Cutforth T., Rubin G.M.; RT "Mutations in Hsp83 and cdc37 impair signaling by the sevenless RT receptor tyrosine kinase in Drosophila."; RL Cell 77:1027-1036(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CO-CHAPERONE THAT BINDS TO NUMEROUS KINASES CC AND PROMOTES THEIR INTERACTION WITH THE HSP90 COMPLEX, CC RESULTING IN STABILIZATION AND PROMOTION OF THEIR ACTIVITY. CC -!- SUBUNIT: FORMS A COMPLEX WITH HSP90. INTERACTS WITH A NUMBER OF CC KINASES SUCH AS CDC2 AND SEVENLESS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CDC37 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L32839; AAA28414.1; -. DR EMBL; AE003472; AAF47571.1; -. DR FlyBase; FBgn0011573; Cdc37. DR GO; GO:0005737; C:cytoplasm; ISS. DR GO; GO:0003767; F:co-chaperone activity; NAS. DR GO; GO:0030296; F:protein tyrosine kinase activator activity; NAS. DR GO; GO:0007243; P:protein kinase cascade; NAS. DR InterPro; IPR004918; Cdc37. DR Pfam; PF03234; Cdc37; 1. KW Chaperone. SQ SEQUENCE 389 AA; 45149 MW; 33490D24D4B60BFD CRC64; MVDYSKWKNI EISDDEDDTH PNIDTPSLFR WRHQARVERM AEMDHEKDEL KKKRQSYQAR LMDVKERISK KDGDEEALKK ELEKIEAEGK ELDRIESEMI KKEKKTPWNV DTISKPGFEK TVINKKAGRK PDENLSEEER EQRMKQFVKE NEKLCQQYGM LRKYDDSKRF LQEHLHLVGE ETANYLVIWS INLEMEEKHE LMAHVAHQCI CMQYILELAK QLDVDPRACV SSFFSKIQHC HPEYRAQFDS EIEGFKGRIQ KRAQEKIQEA IAQAEEEERK ERLGPGGLDP ADVFESLPDE LKACFESRDV ELLQKTIAAM PVDVAKLHMK RCVDSGLWVP NAADLEGDKK EEDDSDDVAG GEEKTDDAKS ESAAKEEPIY TGVSTEDVD // ID CC42_DROME STANDARD; PRT; 191 AA. AC P40793; Q9V465; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cdc42 homolog. GN CDC42 OR CG12530. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95047333; PubMed=7958857; RA Luo L., Liao Y.J., Jan L.Y., Jan Y.; RT "Distinct morphogenetic functions of similar small GTPases: RT Drosophila Drac1 is involved in axonal outgrowth and myoblast RT fusion."; RL Genes Dev. 8:1787-1802(1994). RN [2] RP SEQUENCE FROM N.A. RA Genova J.L., Jong S., Camp T., Fehon R.G.; RT "Functional analysis of Cdc42 in actin filament assembly, epithelial RT morphogenesis, and cell signaling during Drosophila development."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RHO FAMILY. CC CDC42 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11824; AAA62871.1; -. DR EMBL; AF153423; AAD43787.1; -. DR EMBL; AF153425; AAD43789.1; -. DR EMBL; AF153427; AAD43791.1; -. DR EMBL; AE003512; AAF49007.1; -. DR PIR; I45716; I45716. DR HSSP; P21181; 1AM4. DR FlyBase; FBgn0010341; Cdc42. DR GO; GO:0003924; F:GTPase activity; NAS. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; NAS. DR GO; GO:0016358; P:dendrite morphogenesis; IMP. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR GO; GO:0007391; P:dorsal closure; IMP. DR InterPro; IPR003578; GTPase_Rho. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00174; RHO; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Lipoprotein; Prenylation. FT NP_BIND 10 17 GTP (BY SIMILARITY). FT NP_BIND 57 61 GTP (BY SIMILARITY). FT NP_BIND 115 118 GTP (BY SIMILARITY). FT DOMAIN 32 40 EFFECTOR REGION (POTENTIAL). FT LIPID 188 188 S-geranylgeranyl cysteine FT (By similarity). SQ SEQUENCE 191 AA; 21403 MW; 0AB96574ADC8E0E3 CRC64; MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCQKTPF LLVGTQIDLR DENSTLEKLA KNKQKPITME QGEKLAKELK AVKYVECSAL TQKGLKNVFD EAILAALEPP EPTKKRKCKF L // ID CCA4_DROME STANDARD; PRT; 536 AA. AC Q9VE00; Q8SZL9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 12a4, mitochondrial precursor (EC 1.14.-.-) DE (CYPXIIA4). GN CYP12A4 OR CG6042. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003725; AAF55636.2; -. DR EMBL; AY070663; AAL48134.1; -. DR FlyBase; FBgn0038681; Cyp12a4. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Mitochondrion; KW Transit peptide; Hypothetical protein. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 536 PROBABLE CYTOCHROME P450 12A4. FT METAL 482 482 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 203 203 D -> H (IN REF. 3). SQ SEQUENCE 536 AA; 61776 MW; DDE51C7726A8805E CRC64; MLKVRSALSL IQSQKATLSL ATQKRWQTNV ATAEAREDSE WLQAKPFEQI PRLNMWALSM KMSMPGGKYK NMELMEMFEA MRQDYGDIFF MPGIMGNPPF LSTHNPQDFE VVFRNEGVWP NRPGNYTLLY HREEYRKDFY QGVMGVIPTQ GKPWGDFRTV VNPVLMQPKN VRLYYKKMSQ VNQEFVQRIL ELRDPDTLEA PDDFIDTINR WTLESVSVVA LDKQLGLLKN SNKESEALKL FHYLDEFFIV SIDLEMKPSP WRYIKTPKLK RLMRALDGIQ EVTLAYVDEA IERLDKEAKE GVVRPENEQS VLEKLLKVDR KVATVMAMDM LMAGVDTTSS TFTALLLCLA KNPEKQARLR EEVMKVLPNK NSEFTEASMK NVPYLRACIK ESQRLHPLIV GNARVLARDA VLSGYRVPAG TYVNIVPLNA LTRDEYFPQA SEFLPERWLR SPKDSESKCP ANELKSTNPF VFLPFGFGPR MCVGKRIVEM ELELGTARLI RNFNVEFNYP TENAFRSALI NLPNIPLKFK FIDLPN // ID CCA5_DROME STANDARD; PRT; 536 AA. AC Q9VE01; Q8MQI5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 12a5, mitochondrial precursor (EC 1.14.-.-) DE (CYPXIIA5). GN CYP12A5 OR CG11821. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003725; AAF55635.1; -. DR EMBL; AY129460; AAM76202.1; -. DR FlyBase; FBgn0038680; Cyp12a5. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Mitochondrion; KW Transit peptide; Hypothetical protein. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 536 PROBABLE CYTOCHROME P450 12A5. FT METAL 482 482 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 66 66 G -> S (IN REF. 2). SQ SEQUENCE 536 AA; 61355 MW; 231BFD7E6284A1F6 CRC64; MLKGRIALNI LQSQKPIVFS ASQQRWQTNV PTAEIRNDPE WLQAKPFEEI PKANILSLFA KSALPGGKYK NLEMMEMIDA LRQDYGNIIF LPGMMGRDGL VMTHNPKDFE VVFRNEGVWP FRPGSDILRY HRTVYRKDFF DGVQGIIPSQ GKSWGDFRSI VNPVLMQPKN VRLYFKKMSQ VNQEFVELIK EIRDASTQEV PGNFLETINR WTLESVSVVA LDKQLGLLRE SGKNSEATKL FKYLDEFFLH SADLEMKPSL WRYFKTPLLK KMLRTMDSVQ EVTLKYVDEA IERLEKEAKE GVVRPEHEQS VLEKLLKVDK KVATVMAMDM LMAGVDTTSS TFTALLLCLA KNPEKQARLR EEVMKVLPNK DSEFTEASMK NVPYLRACIK ESQRVYPLVI GNARGLTRDS VISGYRVPAG TIVSMIPINS LYSEEYFPKP TEFLPERWLR NASDSAGKCP ANDLKTKNPF VFLPFGFGPR MCVGKRIVEM ELELGTARLI RNFNVEFNHS TKNAFRSALI NLPNIPLKFK FTDVPN // ID CCAA_DROME STANDARD; PRT; 1848 AA. AC P91645; O01713; O01714; Q9VYR8; DT 15-JUL-1998 (Rel. 36, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Voltage-dependent calcium channel type A alpha-1 subunit (Cacophony DE protein) (Nightblind A protein) (No-on-transient B protein) (DmCA1A). GN CAC OR NBA OR NONB OR CG1522. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97141514; PubMed=8987815; RA Smith L.A., Wang X.J., Peixoto A.A., Neumann E.K., Hall L.M., RA Hall J.C.; RT "A Drosophila calcium channel alpha1 subunit gene maps to a genetic RT locus associated with behavioral and visual defects."; RL J. Neurosci. 16:7868-7879(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP PARTIAL SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=97247730; PubMed=9093853; RA Peixoto A.A., Smith L.A., Hall J.C.; RT "Genomic organization and evolution of alternative exons in a RT Drosophila calcium channel gene."; RL Genetics 145:1003-1013(1997). RN [4] RP VARIANT CAC-S. RX MEDLINE=98315104; PubMed=9649530; RA Smith L.A., Peixoto A.A., Kramer E.M., Villella A., Hall J.C.; RT "Courtship and visual defects of cacophony mutants reveal functional RT complexity of a calcium-channel alpha1 subunit in Drosophila."; RL Genetics 149:1407-1426(1998). CC -!- FUNCTION: VOLTAGE-SENSITIVE CALCIUM CHANNELS (VSCC) MEDIATE THE CC ENTRY OF CALCIUM IONS INTO EXCITABLE CELLS AND ARE ALSO INVOLVED CC IN A VARIETY OF CALCIUM-DEPENDENT PROCESSES, INCLUDING MUSCLE CC CONTRACTION, NEUROTRANSMITTER RELEASE, GENE EXPRESSION, CELL CC MOTILITY, CELL DIVISION AND CELL DEATH (BY SIMILARITY). PROBABLY CC ENCODES A DIHYDROPYRIDINE-INSENSITIVE CURRENT. VITAL FOR SURVIVAL CC TO ADULTHOOD. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=At least 2 regions (Exon IS4 and Exon I/II) undergo CC alternative splicing. The total number of isoforms is CC currently not known; CC Name=1; CC IsoId=P91645-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: EXPRESSED WIDELY IN THE EMBRYONIC NERVOUS CC SYSTEM. CC -!- DEVELOPMENTAL STAGE: EXPRESSION PEAKS IN THE FIRST LARVAL INSTAR, CC MIDPUPAL, AND LATE PUPAL STAGES. IN LATE-STAGE EMBRYOS, IT IS CC EXPRESSED PREFERENTIALLY IN THE NERVOUS SYSTEM. CC -!- DOMAIN: EACH OF THE FOUR INTERNAL REPEATS CONTAINS FIVE CC HYDROPHOBIC TRANSMEMBRANE SEGMENTS (S1, S2, S3, S5, S6) AND ONE CC POSITIVELY CHARGED TRANSMEMBRANE SEGMENT (S4). S4 SEGMENTS CC PROBABLY REPRESENT THE VOLTAGE-SENSOR AND ARE CHARACTERIZED BY A CC SERIE OF POSITIVELY CHARGED AMINO ACIDS AT EVERY THIRD POSITION. CC -!- SIMILARITY: BELONGS TO THE CALCIUM CHANNEL ALPHA-1 SUBUNITS CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U55776; AAC47406.1; -. DR EMBL; AE003487; AAF48120.1; -. DR EMBL; U88664; AAB53271.1; -. DR EMBL; U88665; AAB53272.1; -. DR PIR; T13980; T13980. DR FlyBase; FBgn0005563; cac. DR GO; GO:0016324; C:apical plasma membrane; IDA. DR GO; GO:0016323; C:basolateral plasma membrane; IDA. DR GO; GO:0005891; C:voltage-gated calcium channel complex; NAS. DR GO; GO:0005245; F:voltage-gated calcium channel activity; NAS. DR GO; GO:0006816; P:calcium ion transport; NAS. DR GO; GO:0007619; P:courtship behavior; NAS. DR GO; GO:0042045; P:epithelial fluid transport; IDA. DR GO; GO:0045433; P:male courtship behavior (sensu Insecta), so...; NAS. DR GO; GO:0007602; P:phototransduction; NAS. DR GO; GO:0007632; P:visual behavior; NAS. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR002077; Ca_channel_alpha. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR003915; PKD_2. DR Pfam; PF00036; efhand; 1. DR Pfam; PF00520; ion_trans; 4. DR PRINTS; PR00167; CACHANNEL. DR PRINTS; PR01433; POLYCYSTIN2. KW Ionic channel; Transmembrane; Ion transport; Voltage-gated channel; KW Calcium channel; Glycoprotein; Repeat; Multigene family; KW Calcium-binding; Phosphorylation; Alternative splicing; KW Developmental protein. FT REPEAT 25 316 I. FT REPEAT 427 670 II. FT REPEAT 762 1049 III. FT REPEAT 1086 1344 IV. FT DOMAIN 1 38 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 39 57 S1 OF REPEAT I (POTENTIAL). FT DOMAIN 58 75 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 76 95 S2 OF REPEAT I (POTENTIAL). FT DOMAIN 96 107 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 108 128 S3 OF REPEAT I (POTENTIAL). FT DOMAIN 129 133 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 134 152 S4 OF REPEAT I (POTENTIAL). FT DOMAIN 153 171 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 172 191 S5 OF REPEAT I (POTENTIAL). FT DOMAIN 192 288 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 289 313 S6 OF REPEAT I (POTENTIAL). FT DOMAIN 314 441 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 442 460 S1 OF REPEAT II (POTENTIAL). FT DOMAIN 461 475 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 476 495 S2 OF REPEAT II (POTENTIAL). FT DOMAIN 496 503 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 504 522 S3 OF REPEAT II (POTENTIAL). FT DOMAIN 523 531 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 532 550 S4 OF REPEAT II (POTENTIAL). FT DOMAIN 551 569 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 570 589 S5 OF REPEAT II (POTENTIAL). FT DOMAIN 590 642 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 643 667 S6 OF REPEAT II (POTENTIAL). FT DOMAIN 668 767 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 768 786 S1 OF REPEAT III (POTENTIAL). FT DOMAIN 787 802 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 803 822 S2 OF REPEAT III (POTENTIAL). FT DOMAIN 823 834 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 835 853 S3 OF REPEAT III (POTENTIAL). FT DOMAIN 854 866 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 867 885 S4 OF REPEAT III (POTENTIAL). FT DOMAIN 886 904 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 905 924 S5 OF REPEAT III (POTENTIAL). FT DOMAIN 925 1013 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1014 1038 S6 OF REPEAT III (POTENTIAL). FT DOMAIN 1039 1093 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1094 1122 S1 OF REPEAT IV (POTENTIAL). FT DOMAIN 1123 1127 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1128 1147 S2 OF REPEAT IV (POTENTIAL). FT DOMAIN 1148 1155 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1156 1174 S3 OF REPEAT IV (POTENTIAL). FT DOMAIN 1175 1181 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1182 1200 S4 OF REPEAT IV (POTENTIAL). FT DOMAIN 1201 1219 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1220 1239 S5 OF REPEAT IV (POTENTIAL). FT DOMAIN 1240 1305 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1306 1330 S6 OF REPEAT IV (POTENTIAL). FT DOMAIN 1331 1848 CYTOPLASMIC (POTENTIAL). FT DOMAIN 396 402 POLY-GLU. FT DOMAIN 732 735 POLY-GLU. FT DOMAIN 1733 1799 ARG-RICH. FT SITE 271 271 CALCIUM ION SELECTIVITY AND PERMEABILITY. FT SITE 621 621 CALCIUM ION SELECTIVITY AND PERMEABILITY. FT SITE 989 989 CALCIUM ION SELECTIVITY AND PERMEABILITY. FT SITE 1278 1278 CALCIUM ION SELECTIVITY AND PERMEABILITY. FT BINDING 1303 1345 PHENYLALKYLAMINES (BY SIMILARITY). FT MOD_RES 1345 1345 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT CA_BIND 1363 1374 BY SIMILARITY. FT CARBOHYD 234 234 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 235 235 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 865 865 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 121 153 FMTQYPQIGPEVDLRTLRAIRVLRPLKLVSGIP -> AMTI FT FAEANIDVDLRMLRSFRVLRPLKLVSRIP (in FT isoforms with exon IS4A). FT /FTId=VSP_000952. FT VARSPLIC 315 352 EFSNERNRVERRMEFQKCRFRAMFQTAMVSYLDWITQA -> FT EFAKEREKVENRQEFLKLRRQQQLERELNGYVEWICKA FT (in isoforms with exon I/IIB). FT /FTId=VSP_000953. FT VARIANT 1029 1029 F -> I (IN CAC-S; EXHIBITS DEFECTS IN THE FT PATTERNING OF COURTSHIP LOVESONG AND A FT SUBTLE ABNORMALITY IN VISUAL PHYSIOLOGY). FT CONFLICT 514 514 S -> G (IN REF. 1). FT CONFLICT 815 815 I -> M (IN REF. 1). FT CONFLICT 839 839 N -> S (IN REF. 1). FT CONFLICT 906 906 N -> S (IN REF. 1). FT CONFLICT 937 937 S -> G (IN REF. 1). FT CONFLICT 1016 1016 M -> V (IN REF. 1). FT CONFLICT 1181 1182 SN -> HDDSS (IN REF. 1). FT CONFLICT 1266 1266 Q -> H (IN REF. 1). FT CONFLICT 1365 1365 N -> G (IN REF. 1). FT CONFLICT 1577 1577 N -> D (IN REF. 1). FT CONFLICT 1599 1599 R -> G (IN REF. 1). SQ SEQUENCE 1848 AA; 212102 MW; 4060158ECCA1E71D CRC64; MGGPKKEENP PGGGPTSLFI LTEDNPIRKY TRFIIEWPPF EYAVLLTIIA NCVVLALEEH LPGGDKTVLA QKLEKTEAYF LCIFCVEASL KILALGLVLH KHSYLRNIWN IMDFFVVVTG FMTQYPQIGP EVDLRTLRAI RVLRPLKLVS GIPSLQVVLK SIIKAMAPLL QIGLLVLFAI VIFAIIGLEF YSGALHKTCY SLEDPNKLVK EGESETPCNT DNILEKATGS FVCNNTTSMC LEKWEGPNSG ITSFDNIGFA MLTVFQCITM EGWTAILYWT NDALGSAFNW IYFVPLIVIG SFFMLNLVLG VLSGEFSNER NRVERRMEFQ KCRFRAMFQT AMVSYLDWIT QAEEVILAEE RTTEEEKMHI MEARRRNAAK RKKLKSLGKS KSTDTEEEEA EEDYGDDGYL KTRSKPQGSC TGFWRAEKRF RFWIRHTVKT QWFYWFVIVL VFLNTVCVAV EHYGQPSFLT EFLYYAEFIF LGLFMSEMFI KMYALGPRIY FESSFNRFDC VVISGSIFEV IWSEVKGGSF GLSVLRALRL LRIFKVTKYW SSLRNLVISL LNSMRSIISL LFLLFLFILI FALLGMQLFG GQFNLPGGTP ETNFNTFPIA LLTVFQILTG EDWNEVMYQG IISQGGAQKG MIYSIYFIVL VLFGNYTLLN VFLAIAVDNL ANAQELTAAE EEQVEEDKEK QLQELEKEME ALQADGVHVE NGDGAVAPSK SKGKKKEEEK KEEEEVTEGP KPMLPYSSMF ILSPTNPIRR GAHWVVNLPY FDFFIMVVIS MSSIALAAED PVRENSRRNK ILNYFDYAFT GVFTIEMLLK IVDLGVILHP GSYLREFWNI MDAVVVICAA VSFGFDMSGS SAGQNLSTIK SLRVLRVLRP LKTIKRVPKL KAVFDCVVNS LKNVVNILIV YILFQFIFSV IGVQLFNGKF FYCTDESKHT SAECQGSYFK YEEDELLPKQ ELRVWKPRAF HYDNVAAAML TLFAVQTGEG WPQVLQHSMA ATYEDRGPIQ NFRIEMSIFY IVYFIVFPFF FVNIFVALII ITFQEQGEAE LQDGEIDKNQ KSCIDFTIGA RPLERYMPKN RNTFKYKVWR IVVSTPFEYF IMMLIVFNTL LLMMKYHNQG DMYEKSLKYI NMGFTGMFSV ETVLKIIGFG VKNFFKDPWN IFDLITVLGS IVDALWMEFG SNSINVGFLR LFRAARLIKL LRQGYTIRIL LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIKLGT VENSITRHNN FQSFIQGVML LFRCATGEAW PNIMLACLKG KACDDDAEKA PGEYCGSTLA YAYFVSFIFF CSFLMLNLFV AVIMDNFDYL TRDSSILGAH HLDEFVRIWA EYDPNATGKI HYTEMYDMLK NMDPPLGFGN KCPNRLAYKK LIRMNMPLDD ELRVQFTTTL FALIRENLSI KMRAPEEMDQ ADMELRETIT NIWPLQAKKM LNLLVPPSDQ LNKGKLSVGK IYAGFLILES WRSTRFGQLD SGMPMLELQD ASRHPSQESL TGADAGHLHP GHSYMNGHRR SPSLRHNGSP LARSPSPRRR GHQYIHHDIG FSDTVSNVVE MVKETRHPRH GNSHPRYPRG SWSASTSPAR SPSPSRYGGH LSRSKRTQLP YPTYGTTSLC QRSRSPSPAR LQEMRERDRL GYGIDMGVTH VQHSYPTLAS RRAGIGRRLP PTPSKPSTLQ LKPTNINFPK LNASPTHTHH STPHSVHSLP HHRDLLRDPR DMYYSSRERE RDRERLRDRD RDRDRDRLHE YDLRYEYRDR ERELYERERD REREVERERL EYIAPLSFEQ ALAMGRTGRV LPSPVLNGFK PKSGLNPRHS DSDEEDWC // ID CCAD_DROME STANDARD; PRT; 2516 AA. AC Q24270; Q8IP23; Q95U73; Q9V3P7; DT 15-JUL-1999 (Rel. 38, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Voltage-dependent calcium channel type D alpha-1 subunit (DmCA1D). GN CA-ALPHA-1D OR L(2)35FA OR DROCA1 OR CG4894. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), FUNCTION, AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=95173658; PubMed=7869089; RA Zheng W., Feng G., Ren D., Eberl D.F., Hannan F., Dubald M., RA Hall L.M.; RT "Cloning and characterization of a calcium channel alpha 1 subunit RT from Drosophila melanogaster with similarity to the rat brain type D RT isoform."; RL J. Neurosci. 15:1132-1143(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 1895-2300 FROM N.A. (ISOFORM D). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP VARIANT AR66. RX MEDLINE=98171540; PubMed=9502794; RA Ren D., Xu H., Eberl D.F., Chopra M., Hall L.M.; RT "A mutation affecting dihydropyridine-sensitive current levels and RT activation kinetics in Drosophila muscle and mammalian heart calcium RT channels."; RL J. Neurosci. 18:2335-2341(1998). RN [7] RP VARIANT AR66. RX MEDLINE=98198839; PubMed=9539432; RA Eberl D.F., Ren D., Feng G., Lorenz L.J., van Vactor D., Hall L.M.; RT "Genetic and developmental characterization of Dmca1D, a calcium RT channel alpha-1 subunit gene in Drosophila melanogaster."; RL Genetics 148:1159-1169(1998). CC -!- FUNCTION: VOLTAGE-SENSITIVE CALCIUM CHANNELS (VSCC) MEDIATE THE CC ENTRY OF CALCIUM IONS INTO EXCITABLE CELLS AND ARE ALSO INVOLVED CC IN A VARIETY OF CALCIUM-DEPENDENT PROCESSES, INCLUDING MUSCLE CC CONTRACTION, HORMONE OR NEUROTRANSMITTER RELEASE, GENE EXPRESSION, CC CELL MOTILITY, CELL DIVISION AND CELL DEATH. ENCODES A CC DIHYDROPYRIDINE-AND DILTIAZEM-SENSITIVE CURRENT IN LARVAL BODY CC WALL MUSCLE. VITAL FOR EMBRYONIC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=A number of isoforms may be produced; CC Name=A; CC IsoId=Q24270-1; Sequence=Displayed; CC Name=D; CC IsoId=Q24270-2; Sequence=VSP_007604, VSP_007605; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT BODY, HEAD AND LEG. CC HIGHLY EXPRESSED IN THE EMBRYONIC NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: FAINTLY EXPRESSED IN EMBRYOS AT 9-12 HOURS. CC EXPRESSION INCREASES RAPIDLY AS THE NERVOUS SYSTEM MATURES, CC PEAKING JUST PRIOR TO HATCHING. A SECOND PEAK IS OBSERVED IN LATE CC PUPAL STAGES AROUND 73-108 HOURS POSTPUPARIUM. CC -!- DOMAIN: EACH OF THE FOUR INTERNAL REPEATS CONTAINS FIVE CC HYDROPHOBIC TRANSMEMBRANE SEGMENTS (S1, S2, S3, S5, S6) AND ONE CC POSITIVELY CHARGED TRANSMEMBRANE SEGMENT (S4). S4 SEGMENTS CC PROBABLY REPRESENT THE VOLTAGE-SENSOR AND ARE CHARACTERIZED BY A CC SERIE OF POSITIVELY CHARGED AMINO ACIDS AT EVERY THIRD POSITION. CC -!- SIMILARITY: BELONGS TO THE CALCIUM CHANNEL ALPHA-1 SUBUNITS CC FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1, MET-494, MET-539, MET-544 CC OR MET-553 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U00690; AAA81883.1; -. DR EMBL; AE003415; AAF44986.1; -. DR EMBL; AE003650; AAF53504.1; -. DR EMBL; AE003650; AAN10931.1; -. DR EMBL; AY058268; AAL13497.1; ALT_INIT. DR FlyBase; FBgn0001991; Ca-alpha-1D. DR GO; GO:0016324; C:apical plasma membrane; IDA. DR GO; GO:0016323; C:basolateral plasma membrane; IDA. DR GO; GO:0005891; C:voltage-gated calcium channel complex; NAS. DR GO; GO:0005245; F:voltage-gated calcium channel activity; NAS. DR GO; GO:0006816; P:calcium ion transport; NAS. DR GO; GO:0042045; P:epithelial fluid transport; IDA. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR002077; Ca_channel_alpha. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR005446; LVDCCAlpha1. DR InterPro; IPR005820; M+channel_nlg. DR Pfam; PF00520; ion_trans; 4. DR PRINTS; PR00167; CACHANNEL. DR PRINTS; PR01630; LVDCCALPHA1. KW Ionic channel; Transmembrane; Ion transport; Voltage-gated channel; KW Calcium channel; Glycoprotein; Repeat; Multigene family; KW Calcium-binding; Phosphorylation; Alternative splicing. FT REPEAT 602 883 I. FT REPEAT 971 1217 II. FT REPEAT 1331 1613 III. FT REPEAT 1648 1929 IV. FT DOMAIN 1 615 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 616 634 S1 OF REPEAT I (POTENTIAL). FT DOMAIN 635 653 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 654 671 S2 OF REPEAT I (POTENTIAL). FT DOMAIN 672 684 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 685 699 S3 OF REPEAT I (POTENTIAL). FT DOMAIN 700 711 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 712 730 S4 OF REPEAT I (POTENTIAL). FT DOMAIN 731 750 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 751 770 S5 OF REPEAT I (POTENTIAL). FT DOMAIN 771 853 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 854 878 S6 OF REPEAT I (POTENTIAL). FT DOMAIN 879 985 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 986 1005 S1 OF REPEAT II (POTENTIAL). FT DOMAIN 1006 1018 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1019 1038 S2 OF REPEAT II (POTENTIAL). FT DOMAIN 1039 1047 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1048 1066 S3 OF REPEAT II (POTENTIAL). FT DOMAIN 1067 1076 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1077 1095 S4 OF REPEAT II (POTENTIAL). FT DOMAIN 1096 1114 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1115 1134 S5 OF REPEAT II (POTENTIAL). FT DOMAIN 1135 1190 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1191 1215 S6 OF REPEAT II (POTENTIAL). FT DOMAIN 1216 1339 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1340 1363 S1 OF REPEAT III (POTENTIAL). FT DOMAIN 1364 1380 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1381 1400 S2 OF REPEAT III (POTENTIAL). FT DOMAIN 1401 1408 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1409 1431 S3 OF REPEAT III (POTENTIAL). FT DOMAIN 1432 1439 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1440 1454 S4 OF REPEAT III (POTENTIAL). FT DOMAIN 1455 1475 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1476 1495 S5 OF REPEAT III (POTENTIAL). FT DOMAIN 1496 1584 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1585 1609 S6 OF REPEAT III (POTENTIAL). FT DOMAIN 1610 1664 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1665 1683 S1 OF REPEAT IV (POTENTIAL). FT DOMAIN 1684 1697 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1698 1717 S2 OF REPEAT IV (POTENTIAL). FT DOMAIN 1718 1726 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1727 1745 S3 OF REPEAT IV (POTENTIAL). FT DOMAIN 1746 1777 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1778 1796 S4 OF REPEAT IV (POTENTIAL). FT DOMAIN 1797 1815 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1816 1835 S5 OF REPEAT IV (POTENTIAL). FT DOMAIN 1836 1902 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1903 1921 S6 OF REPEAT IV (POTENTIAL). FT DOMAIN 1922 2516 CYTOPLASMIC (POTENTIAL). FT DOMAIN 59 62 POLY-VAL. FT DOMAIN 208 211 POLY-GLY. FT DOMAIN 262 267 POLY-SER. FT DOMAIN 322 328 POLY-ALA. FT DOMAIN 460 463 POLY-GLU. FT DOMAIN 1115 1121 POLY-LEU. FT DOMAIN 1288 1292 POLY-GLU. FT DOMAIN 1591 1597 POLY-ILE. FT DOMAIN 2466 2469 POLY-ASN. FT SITE 836 836 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1168 1168 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1559 1559 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1869 1869 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT BINDING 1533 1622 DIHYDROPYRIDINES (BY SIMILARITY). FT BINDING 1885 1948 DIHYDROPYRIDINES (BY SIMILARITY). FT BINDING 1896 1937 PHENYLALKYLAMINES (BY SIMILARITY). FT MOD_RES 1937 1937 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT CA_BIND 1957 1968 BY SIMILARITY. FT CARBOHYD 644 644 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 647 647 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 2282 2300 NRNRGILLHPYNNVYAPNG -> LRTQWCSSWPRTHDPIDT FT S (in isoform D). FT /FTId=VSP_007604. FT VARSPLIC 2301 2516 Missing (in isoform D). FT /FTId=VSP_007605. FT VARIANT 629 629 C -> Y (IN AR66; SLOWER CHANNEL FT ACTIVATION AND REDUCTION OF PEAK FT CURRENT). FT CONFLICT 134 134 P -> A (IN REF. 1). FT CONFLICT 282 282 F -> L (IN REF. 1). FT CONFLICT 678 678 N -> D (IN REF. 1). FT CONFLICT 683 683 R -> G (IN REF. 1). FT CONFLICT 696 696 I -> M (IN REF. 1). FT CONFLICT 1390 1390 I -> M (IN REF. 1). FT CONFLICT 1433 1433 N -> D (IN REF. 1). FT CONFLICT 2479 2479 N -> S (IN REF. 1). SQ SEQUENCE 2516 AA; 276698 MW; 8CFC07499E750901 CRC64; MGGGELVNCI AYDDNTLVIE RKPSPSSPST SRRYLKAETP TRGSRKYNRK SSAKSDLEVV VVKPEHHHQH RSPTITLPVP ANPLTTSASA GSSPTGAGLA AGLGTASGTV LQQSCSALDP PEDSNQPSGT RRRPTSTELA LSNVTSQIVN NATYKLDFKQ RRHKSNNGGS ESGSLTGIAT GPATSPAGPT GPTSSSGKRR KSSCTSCGGG GISAPPPRLT PEEAWQLQPQ NSVTSAGSTN SSFSSGGGRD DNSSYSAVGG DSSSSNSCNC DITGDNSTLH GFGVGDVCSF IADCDDNSED DDGDPNNQDL SSQTLRTAAI VAAVAAAAKE QAQEQSLADC ESFSDRRQDA DEDVRIIQDC CGGNNDSLED VGEVDDNADV VVRKNSRNRP SIRRTCRITE EDDDEDENAD YGDFDREDQE LDDEEPEGTT IDIDEQEQQH DQGDSAEEED DDEDVDEYFE EEEDDTQAFS PFYSSSAELI DNFGGGAGKF FNIMDFERGA SGEGGFSPNG NGGPGSGDVS RTARYDSGEG DLGGGNNIMG IDSMGIANIP ETMNGTTIGP SGAGGQKGGA AAGAAGQKRQ QRRGKPQPDR PQRALFCLSV KNPLRALCIR IVEWKPFEFL ILLTIFANCI ALAVYTPYPG SDSNVTNQTL EKVEYVFLVI FTAECVMKIL AYGFVLHNGA YLRNGWNLLD FTIVVIGAIS TALSQLMKDA FDVKALRAFR VLRPLRLVSG VPSLQVVLNS ILKAMVPLFH IALLVLFVII IYAIIGLELF SGKLHKACRD EITGEYEENI RPCGVGYQCP PGYKCYGGWD GPNDGITNFD NFGLAMLTVF QCVTLEGWTD VLYSIQDAMG SDWQWMYFIS MVILGAFFVM NLILGVLSGE FSKERNKAKN RGDFQKLREK QQIEEDLRGY LDWITQAEDI EPDAVGGLIS DGKGKQPNEM DSTENLGEEM PEVQMTESRW RKMKKDFDRV NRRMRRACRK AVKSQAFYWL IIVLVFLNTG VLATEHYGQL DWLDNFQEYT NVFFIGLFTC EMLLKMYSLG FQGYFVSLFN RFDCFVVIGS ITETLLTNTG MMPPLGVSVL RCVRLLRVFK VTKYWRSLSN LVASLLNSIQ SIASLLLLLF LFIVIFALLG MQVFGGKFNF DGKEEKYRMN FDCFWQALLT VFQIMTGEDW NAVMYVGINA YGGVSSYGAL ACIYFIILFI CGNYILLNVF LAIAVDNLAD ADSLSEVEKE EEPHDESAQK KSHSPTPTID GMDDHLSIDI DMEQQELDDE DKMDHETLSD EEVREMCEEE EEVDEEGMIT ARPRRMSEVN TATKILPIPP GTSFFLFSQT NRFRVFCHWL CNHSNFGNII LCCIMFSSAM LAAENPLRAN DDLNKVLNKF DYFFTAVFTI ELILKLISYG FVLHDGAFCR SAFNLLDLLV VCVSLISLVS SSNAISVVKI LRVLRVLRPL RAINRAKGLK HVVQCVIVAV KTIGNIVLVT CLLQFMFAVI GVQLFKGKFF KCTDGSKMTQ DECYGTYLVY DDGDVHKPRL REREWSNNRF HFDDVAKGML TLFTVSTFEG WPGLLYVSID SNKENGGPIH NFRPIVAAYY IIYIIIIAFF MVNIFVGFVI VTFQNEGEQE YKNCDLDKNQ RNCIEFALKA KPVRRYIPKH GIQYKVWWFV TSSSFEYTIF ILIMINTVTL AMKFYNQPLW YTELLDALNM IFTAVFALEF VFKLAAFRFK NYFGDAWNVF DFIIVLGSFI DIVYSEIKSK DTSQIAECDI VEGCKSTKKS AGSNLISINF FRLFRVMRLV KLLSKGEGIR TLLWTFIKSF QALPYVALLI VLLFFIYAVV GMQVFGKIAL DGGNAITANN NFQTFQQAVL VLFRSATGEA WQEIMMSCSA QPDVKCDMNS DTPGEPCGSS IAYPYFISFY VLCSFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFIRL WSEYDPDAKG RIKHLDVVTL LRKISPPLGF GKLCPHRMAC KRLVSMNMPL NSDGTVLFNA TLFAVVRTSL SIKTDGNIDD ANSELRATIK QIWKRTNPKL LDQVVPPPGN DDEVTVGKFY ATYLIQDYFR RFKKRKEQEG KEGHPDSNTV TLQAGLRTLH EVSPALKRAI SGNLDELDQE PEPMHRRHHT LFGSVWSSIR RHGNGTFRRS AKATASQSNG ALAIGGSASA ALGVGGSSLV LGSSDPAGGD YLYDTLNRSV ADGVNNITRN IMQARLAAAG KLQDELQGAG SGGELRTFGE SISMRPLAKN GGGAATVAGT LPPEANAINY DNRNRGILLH PYNNVYAPNG ALPGHERMIQ STPASPYDQR RLPTSSDMNG LAESLIGGVL AAEGLGKYCD SEFVGTAARE MREALDMTPE EMNLAAHQIL SNEHSLSLIG SSNGSIFGGS AGGLGGAGSG GVGGLGGSSS IRNAFGGSGS GPSSLSPQHQ PYSGTLNSPP IPDNRLRRVA TVTTTNNNNK SQVSQNNSNS LNVRANANSQ MNMSPTGQPV QQQSPLRGQG NQTYSS // ID CCB2_DROME STANDARD; PRT; 561 AA. AC Q9V8M2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 12b2, mitochondrial precursor (EC 1.14.-.-) DE (CYPXIIB2). GN CYP12B2 OR CG15077. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003798; AAF57642.1; -. DR FlyBase; FBgn0034387; Cyp12b2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Mitochondrion; KW Transit peptide; Hypothetical protein. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 561 PROBABLE CYTOCHROME P450 12B2. FT METAL 505 505 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 561 AA; 64601 MW; 4135ABB3D331E565 CRC64; MWKYSNKIIY RNVSGNQLWF NRNSSVGGTL SQQVRSWQKE QELLKSRNLF TNNGYICSQT QLELADSRID EKWQQARSFG EIPGPSLLRM LSFFMPGGAL RNTNLIQMNR LMREMYGDIY CIPGMMGKPN AVFTYNPDDF EMTYRNEGVW PIRIGLESLN YYRKIHRPDV FKGVGGLASD QGQEWADIRN KVNPVLMKVQ NVRQNLPQLD QISKEFIDKL ETQRNPETHT LTTDFHNQLK MWAFESISFV ALNTRMGLLS DNPDPNADRL AKHMRDFFNY SFQFDVQPSI WTFYKTAGFK KFLKTYDNIT DITSNYIETA MRGFGKNDDG KTKCVLEQLL EHNKKVAVTM VMDMLMAGID TTSSACLTIL YHLARNPSKQ EKLRRELLRI LPTTKDSLTD QNTKNMPYLR ACIKEGLRIT SITPGNFRIT PKDLVLSGYQ VPRGTGVLMG VLELSNDDKY FAQSSEFIPE RWLKSDLAPD IQACPAARTR NPFVYLPFGF GPRTCIGKRI AELEIETLLV RLLRSYKVSW LPETPIEYES TIILSPCGDI RFKLEPVGDL M // ID CCC1_DROME STANDARD; PRT; 524 AA. AC Q9VVR9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 12c1, mitochondrial precursor (EC 1.14.-.-) DE (CYPXIIC1). GN CYP12C1 OR CG4120. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003519; AAF49240.2; -. DR EMBL; AY058426; AAL13655.1; -. DR FlyBase; FBgn0036806; Cyp12c1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Mitochondrion; KW Transit peptide; Hypothetical protein. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 524 PROBABLE CYTOCHROME P450 12C1. FT METAL 470 470 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 524 AA; 60598 MW; 2D60672D40DDB9FB CRC64; MLRLTVKHGL RANSQLAATR NPDASSYVQQ LESEWEGAKP FTELPGPTRW QLFRGFQKGG EYHQLGMDDV MRLYKKQFGD ICLIPGLFGM PSTVFTFNVE TFEKVYRTEG QWPVRGGAEP VIHYRNKRKD EFFKNCMGLF GNGAEWGKNR SAVNPVLMQH RNVAIYLKPM QRVNRQFVNR IREIRDKESQ EVPGDFMNTI NHLTFESVAT VALDRELGLL REANPPPEAS KLFKNIEVLM DSFFDLGVRP SLYRYIPTPT YKKFSRAMDE IFDTCSMYVN QAIERIDRKS SQGDSNDHKS VLEQLLQIDR KLAVVMAMDM LMGGVDTTST AISGILLNLA KNPEKQQRLR EEVLSKLTSL HSEFTVEDMK SLPYLRAVIK ESLRLYPVTF GNARSAGADV VLDGYRIPKG TKLLMTNSFL LKDDRLYPRA KEFIPERWLR RKDDDKSDVL MNKDLNAFIY LPFGFGPRMC VGKRIVDLEM ELTVANLVRN FHIEYNYSTE KPYKCRFLYK PNIPLKFKFT DLKY // ID CCD1_DROME STANDARD; PRT; 521 AA. AC P82712; Q8IH46; Q8T4K3; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 12d1, mitochondrial precursor (EC 1.14.-.-) DE (CYPXIID1). GN CYP12D1 OR CG30489/CG18239/CG18240. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Buzeli R.A., Pedra J.H.F., Scharf M., Pittendrigh B.R.; RT "Drosophila melanogaster CYP12D1 complete cDNA."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 3-521 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY081961; AAL89789.1; -. DR EMBL; AE003827; AAM68745.1; -. DR EMBL; BT001433; AAN71188.1; -. DR FlyBase; FBgn0041339; Cyp12d1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Mitochondrion; KW Transit peptide; Hypothetical protein. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 521 PROBABLE CYTOCHROME P450 12D1. FT METAL 467 467 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 94 94 W -> S (IN REF. 4). FT CONFLICT 277 277 S -> A (IN REF. 2). FT CONFLICT 392 392 F -> L (IN REF. 2). FT CONFLICT 505 505 V -> L (IN REF. 4). SQ SEQUENCE 521 AA; 60260 MW; 97AB143CDE8AC4EB CRC64; MNTLSSARSV AIYVGPVRSS RSASVLAHEQ AKSSITEEHK TYDEIPRPNK FKFMRAFMPG GEFQNASITE YTSAMRKRYG DIYVMPGMFG RKDWVTTFNT KDIEMVFRNE GIWPRRDGLD SIVYFREHVR PDVYGEVQGL VASQNEAWGK LRSAINPIFM QPRGLRMYYE PLSNINNEFI ERIKEIRDPK TLEVPEDFTD EISRLVFESL GLVAFDRQMG LIRKNRDNSD ALTLFQTSRD IFRLTFKLDI QPSMWKIIST PTYRKMKRTL NDSLNVSQKM LKENQDALEK RRQAGEKINS NSMLERLMEI DPKVAVIMSL DILFAGVDAT ATLLSAVLLC LSKHPDKQAK LREELLSIMP TKDSLLNEEN MKDMPYLRAV IKETLRYYPN GFGTMRTCQN DVILSGYRVP KGTTVLLGSN VLMKEATYYP RPDEFLPERW LRDPETGKKM QVSPFTFLPF GFGPRMCIGK RVVDLEMETT VAKLIRNFHV EFNRDASRPF KTMFVMEPAI TFPFKFTDIE Q // ID CCE1_DROME STANDARD; PRT; 514 AA. AC Q9VGZ0; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 12e1, mitochondrial precursor (EC 1.14.-.-) DE (CYPXIIE1). GN CYP12E1 OR CG14680. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003687; AAF54532.3; -. DR FlyBase; FBgn0037817; Cyp12e1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Mitochondrion; KW Transit peptide; Hypothetical protein. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 514 PROBABLE CYTOCHROME P450 12E1. FT METAL 460 460 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 514 AA; 58943 MW; C9381850A54625D0 CRC64; MLSTQWNANK QISRQIYQLC RVNLEEAKPY ADIPGPSKLQ LIRAFLPGGL YKNLPVHEMF LDMNRQYGSI FRMPSVAGTD LVLTMNPQDY EVIFRNEGQY PYRRSFEVMD YFKRVHRREV FDGYDGLTSG NGPAWGKMRT AVNPILLQPR NAKLYMTNLV QVSDEFLERI RIIRDPVTQE MPDDFAVDIR HLVIESICSV ALNTHLGLLG EQRNNKDIQK LVLALQDVVE LGFQLDIMPA FWKYLPMPNF KKLMRSLDTI TDFCYFHIGN ALKRIEEDAK AGTLNEIGLE TSLLEKLARF DRQTAVIIAM DLLFAGADPT LVTLGGILFS LSKSPDKQAR LLEEIRGILP NKDSSLTIEN MRNLPYLRAC IKEGIRMYPI GPGTLRRMPH DVVLSGYRVV AGTDVGIAAN YQMANMEQFV PKVREFIPER WLRDESNSHL VGETATPFMY LPFGFGPRSC AGKRIVDMML EIAISRLVRN FKIGFDYPIE NAFKAQFFVQ PNIPFKFKFI ERNE // ID CCF_DROME STANDARD; PRT; 550 AA. AC P41046; Q24271; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Centrosomal and chromosomal factor (CCF) (Chromocentrosomin). GN CORTO. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=98130597; PubMed=9463384; RA Kodjabachian L., Delaage M., Maurel C., Miassod R., Jacq B., RA Rosset R.; RT "Mutations in ccf, a novel Drosophila gene encoding a chromosomal RT factor, affect progression through mitosis and interact with Pc-G RT mutations."; RL EMBO J. 17:1063-1075(1998). RN [2] RP SEQUENCE FROM N.A. RA Takamura C., Imamura Y., Taira T., Iguchi-Ariga S., Ariga H.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR PROPER CONDENSATION OF MITOTIC CHROMOSOMES CC AND PROGRESSION THROUGH MITOSIS. IS AN ESSENTIAL GENE. BINDS TO CC SPECIFIC POLYTENE CHROMOSOME SITES, MANY OF WHICH ARE SHARED WITH CC THE POSTERIOR SEX COMBS PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CENTROSOMAL. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING OOGENESIS, EMBRYONIC AND CC LARVAL STAGES. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO NUMEROUS CC FRAMESHIFTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U35074; AAC13917.1; -. DR EMBL; D43795; BAA07853.1; ALT_FRAME. DR FlyBase; FBgn0010313; corto. KW DNA-binding; Nuclear protein; Mitosis; Coiled coil. FT DOMAIN 26 35 POLY-GLN. FT DOMAIN 46 50 POLY-GLN. FT DOMAIN 66 72 POLY-GLN. FT DOMAIN 84 89 POLY-SER. FT DOMAIN 110 126 POLY-GLN. FT DOMAIN 204 210 POLY-SER. FT DOMAIN 215 220 POLY-GLY. FT DOMAIN 236 275 COILED COIL (POTENTIAL). FT DOMAIN 243 250 POLY-GLN. FT DOMAIN 253 258 POLY-GLN. FT DOMAIN 285 297 POLY-GLN. FT DOMAIN 322 329 POLY-ALA. FT DOMAIN 332 336 POLY-ALA. FT DOMAIN 396 410 POLY-GLN. FT DOMAIN 414 417 POLY-PRO. FT DOMAIN 466 469 POLY-GLY. FT DOMAIN 504 507 POLY-ALA. FT DOMAIN 512 518 POLY-ALA. SQ SEQUENCE 550 AA; 58930 MW; 05DBE3BE5E107964 CRC64; MTMAACYANY DMSSLSHGMS ALSALQQQQQ QQQQQHSQTQ QQHHHQQQQQ HMYHAAVAAH QQQLLQQQQQ QQHHRHHHQP ANTSSSSNSR HSHAAATQTQ VAAAVANSRQ QQQQQQQQQQ QQQQQQTASS NSNTAPAPSP QKDYSIPLHV DCSVEYELPN QPKPPAGQRV EPLLMIHPCY FRKMESQRRS PFVNNMHATA RAVSSSSLSS GAALGGGGSG AAVATAPSSS AARRGARAAT SAQQQQQQQQ RYQQQQQQLR QQHQQMSQMS QQAHYPQQQS SLVRQHQQQQ QQQQQQQRAS SNQSQRQSQS QSQSQSHAAN SAAAAAAQAS IAAAAAGQWD QLAALAARTA LTPHHMLHPH SHYAAKGSGG EQGGGKRDAM ISGSYGQTAV ASGKLQQSQV QQQQPQQQQQ HCLPPPPWDA TSMLMDRSPM ATVPSNYQAG PDTNPMRLYS ATPTAGAASG GSASVGGGGA VSGAGATGAV NTATDKLSGK YRQYLRSQRM HPYAAAASLN LAAAAAAAGQ TSFVPFSSAA TAVAATPTFQ HLPQISCYNV // ID CCT_DROME STANDARD; PRT; 1097 AA. AC O96433; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Cyclin T. GN CYCT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98256315; PubMed=9593731; RA Peng J.-M., Marshall N.F., Price D.H.; RT "Identification of a cyclin subunit required for the function of RT Drosophila P-TEFb."; RL J. Biol. Chem. 273:13855-13860(1998). CC -!- FUNCTION: REGULATORY SUBUNIT OF THE CYCLIN-DEPENDENT KINASE PAIR CC (CDK9/CYCLIN T) COMPLEX, ALSO CALLED POSITIVE TRANSCRIPTION CC ELONGATION FACTOR B (P-TEFB), WHICH IS PROPOSED TO FACILITATE THE CC TRANSITION FROM ABORTIVE TO PRODUCTION ELONGATION BY CC PHOSPHORYLATING THE CTD (CARBOXY-TERMINAL DOMAIN) OF THE LARGE CC SUBUNIT OF RNA POLYMERASE II (RNAP II). CC -!- SUBUNIT: ASSOCIATES WITH CDK9 TO FORM P-TEFB. CC -!- SIMILARITY: BELONGS TO THE CYCLIN FAMILY. CYCLIN C SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF051933; AAC73052.1; -. DR PIR; T13033; T13033. DR FlyBase; FBgn0025455; CycT. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0005703; C:polytene chromosome puff; IDA. DR GO; GO:0008024; C:transcription elongation factor complex b; IPI. DR GO; GO:0003711; F:transcriptional elongation regulator activity; IDA. DR GO; GO:0009408; P:response to heat; IDA. DR GO; GO:0006350; P:transcription; IDA. DR InterPro; IPR006670; Cyclin. DR InterPro; IPR006671; Cyclin_N. DR Pfam; PF00134; cyclin; 1. DR SMART; SM00385; CYCLIN; 2. KW Cyclin; Transcription regulation. FT DOMAIN 15 21 POLY-SER. FT DOMAIN 382 390 POLY-SER. FT DOMAIN 426 429 POLY-SER. FT DOMAIN 441 449 POLY-SER. FT DOMAIN 553 556 POLY-PRO. FT DOMAIN 598 603 POLY-GLN. FT DOMAIN 872 880 POLY-LYS. FT DOMAIN 993 998 POLY-GLY. SQ SEQUENCE 1097 AA; 118401 MW; AD55F3F57BCD3D6B CRC64; MSLLATPMPQ AATASSSSSA SAAASASGIP ITANNNLPFE KDKIWYFSND QLANLPSRRC GIKGDDELQY RQMTAYLIQE MGQRLQVSQL CINTAIVYMH RFYAFHSFTH FHRNSMASAS LFLAAKVEEQ PRKLEHVIRA ANKCLPPTTE QNYAELAQEL VFNENVLLQT LGFDVAIDHP HTHVVRTCQL VKACKDLAQT SYFLASNSLH LTSMCLQYRP TVVACFCIYL ACKWSRWEIP QSTEGKHWFY YVDKTVSLDL LKQLTDEFIA IYEKSPARLK SKLNSIKAIA QGASNRTANS KDKPKEDWKI TEMMKGYHSN ITTPPELLNG NDSRDRDRDR ERERERERDP SSLLPPPAMV PQQRRQDGGH QRSSSVSGVP GSSSSSSSSS HKMPNYPGGM PPEAHPDHKS KQPGYNNRMP SSHQRSSSSG LGSSGSGSQH SSSSSSSSSQ QPGRPSMPVD YHKSSRGMPP VGVGMPPHGS HKMTSGSKPQ QPQQQPVPHP SASNSSASGM SSKDKSQSNK MYPNAPPPYS NSAPQNPLMS RGGYPGASNG SQPPPPAGYG GHRSKSGSTV HGMPHFEQQL PYSQSQSYGH MQQQPVPQSQ QQQMPPEASQ HSLQSKNSLF SPEWPDIKKE PMSQSQPQLF NGLLPPPAPP GHDYKLNSHP RDKESPKKER LTPTKKDKHR PVMPPMGSGN SSSGSGSSKP MLPPHKKQIP HGGDLLTNPG ESGSLKRPNE ISGSQYGLNK LDEIDNSNMP REKLRKLDTT TGLPTYPNYE EKHTPLNMSN GIETTPDLVR SLLKESLCPS NASLLKPDAL TMPGLKPPAE LLEPMPAPAT IKKEQGITPM TSLASGPAPM DLEVPTKQAG EIKEESSSKS EKKKKKDKHK HKEKDKSKDK TEKEERKKHK RDKQKDRSGS GGSKDSSLPN EPLKMVIKNP NGSLQAGASA PIKLKISKNK VEPNNYSAAA GLPGAIGYGL PPTTATTTSA SIGAAAPVLP PYGAGGGGYS SSGGSSSGGS SKKKHSDRDR DKESKKNKSQ DYAKYNGAGG GIFNPLGGAG AAPNMSGGMG APMSTAVPPS MLLAPTGAVP PSAAGLAPPP MPVYNKK // ID CD87_DROME STANDARD; PRT; 1967 AA. AC Q9VGG5; Q8MQL5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cadherin 87A precursor. GN CAD87A OR CG6977. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE OF 435-1967 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CADHERINS ARE CALCIUM DEPENDENT CELL ADHESION PROTEINS. CC THEY PREFERENTIALLY INTERACT WITH THEMSELVES IN A HOMOPHILIC CC MANNER IN CONNECTING CELLS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: CONTAINS 14 CADHERIN DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003693; AAF54717.3; -. DR EMBL; AY128505; AAM75098.1; -. DR HSSP; P15116; 1NCJ. DR FlyBase; FBgn0037963; Cad87A. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008014; F:calcium-dependent cell adhesion molecule ac...; NAS. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion; NAS. DR InterPro; IPR002126; Cadherin. DR Pfam; PF00028; cadherin; 13. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 14. DR PROSITE; PS00232; CADHERIN_1; 3. DR PROSITE; PS50268; CADHERIN_2; 14. KW Hypothetical protein; Cell adhesion; Glycoprotein; Transmembrane; KW Calcium; Calcium-binding; Repeat; Signal; Multigene family. FT SIGNAL 1 ? POTENTIAL. FT CHAIN ? 1967 CADHERIN 87A. FT DOMAIN ? 1767 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1768 1788 POTENTIAL. FT DOMAIN 1789 1967 CYTOPLASMIC (POTENTIAL). FT DOMAIN 20 124 CADHERIN 1. FT DOMAIN 125 237 CADHERIN 2. FT DOMAIN 238 350 CADHERIN 3. FT DOMAIN 351 464 CADHERIN 4. FT DOMAIN 465 661 CADHERIN 5. FT DOMAIN 662 766 CADHERIN 6. FT DOMAIN 767 870 CADHERIN 7. FT DOMAIN 871 990 CADHERIN 8. FT DOMAIN 991 1095 CADHERIN 9. FT DOMAIN 1096 1203 CADHERIN 10. FT DOMAIN 1204 1310 CADHERIN 11. FT DOMAIN 1311 1423 CADHERIN 12. FT DOMAIN 1424 1545 CADHERIN 13. FT DOMAIN 1546 1669 CADHERIN 14. FT CARBOHYD 31 31 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 69 69 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 195 195 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 416 416 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 722 722 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 753 753 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1031 1031 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1041 1041 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1103 1103 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1155 1155 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1209 1209 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1317 1317 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1341 1341 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1484 1484 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1568 1568 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1683 1683 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 763 763 V -> M (IN REF. 3). FT CONFLICT 1102 1102 F -> S (IN REF. 3). FT CONFLICT 1642 1642 S -> R (IN REF. 3). FT CONFLICT 1682 1682 R -> C (IN REF. 3). SQ SEQUENCE 1967 AA; 216689 MW; 7164EE6E5E80CF41 CRC64; MICLGLTLAK GETNLPPVFT QTLNNIILYE NVTVGTVVFR LEAYDPEGSP VTYGAIGADH FSVDPVSGNI TLIKPLDREE KDTLKFLVSI RDRVDPEGES ERDNVVEVPI TFIILDLNDN PPEFQNTPYE ADVNEDAAVG TTIFDKITVK DRDIVGESLD LKCLPQQQSP EACRKFRLHI IKRDATILEA AVVLNDTLNY NQRMVYHFQI EATDGPHKTQ TTFEARVKDV QDKPPVFQGS LSTVIDEDSP INTLVLTVHA RDGDTGEPRK IVYDLRTNPN DYFLLDAQTG ELRTAKPLDR EALEDSTGII SLVIRARELV NGVPSDDPLT SATAKATVTI RDVNDSPPVF NHKEYSVSLL ENTLPGTPLA LDMSVSDADV GINSKFALRL DDVSGVFDVE PKLVTGYSQV NIRVANGTLD YENPNQRKFI VLVVAEETDT NPRLSSTATI TVSVLDANDN KPVFEQESYS ASVSEAALPG QYIATITARD VDSGSYGDSG IRYSLSGTGA ELFHVNEQTG VISLANCHDN GESNRRERRD LNEDEHVEED DGEGHLEMLS MEAATREIGT EPTVQYTLIT QAPEEQASSV PLPAPVPHAA PSGVPAATAN DDKAPQTCLD YESETTYFLS YKATDDNGRG SASVVSLRIS VTDANDSPPV CESPLYRASV DEGAVVFDSP LIVKARDADT MSRISYRIRG SEQVESIFDI DRETGQIIIR PNATLDVTNL NSDQLIFAVE ANDGLFTAHC GVNITVRDVN NHVPNFEQQS YSAVVEENSE IGTSVERVHA TDLDTGKNAE LRYRIQQGSF DDFGIVETTG EVFVSRKLDF DRRNTYQLQI QASDQGTPSL TGTATLTINV QNSNDKDPYF VPATQHAEVR ADAPPGQLVY TLIALDPDVA NHNALEFAGT DDITAIDKEG KELPHYDQFK EYFKISRNGK VSVNKQLDRN LFAVMRINVL VTDSTAPNVQ QGRGLLIIQI IDVNKNPPRF NAPWSVEQPQ IKLQMVEEQP VGTVLTTLQA NDEDSSIGEF NISDNDYFAI NQTSGMIYTI ARLDYEVVKE VKFQVTVSDT GVPALTATAD VVVDIINLND NDPKFSQSDY YFNVTENSPR GTVAGKVEAH DGDVGVFGEI TYTLIGENNK YFSIDAYTGN VMVANSSILD REQIKELTLS VVAQDKAPAA VQKSATATIH INILDVNDNA PVFTRDVYNS TVAENAAYQP PAALLQVQAI DQDEGLYGDV RYIITAGNEM GLFKLDAQSG IVYPAQSLSG KHGAYELTIS ARDTQGSGTM ESTTKAIITV LRVNRHKPEF VIPALSNATI EIPGDIVQPD YLLLTVRAMD NDTEENGKVS YHLQVNNRNE QQTGEFKIDE VTGELRAKTQ LNRKNRANYD IILVARDAGN PPFESLRLLS VSIVDANENR PEFPDASNPY KVSINENSGR DVKIGHIQAA SRSKHNRDIF YYMLLGNEDG AFYVDKLTGD IYTNKSLDRE ETDVYTLYIL ASIKADLHIS EEERASFSIK TLNRDNTVAK VAITVLDVND NPPVFEKPIY YAGVNANAKM GAAITLVNAT DADQGKNAKI EFMIVASNLY KFGATKSTGS IVPSPFAISQ DGRISANTIM AEYNQDRFEL EIVARELEQP QSSASTKVNI WVFDGTQLVR VILSRPPEEV YQEQEEIIAE LRNATQHRII VDEIRFHLDS IGRIRMDWCD LYFHAVDPQT QQIAPVDEIL KDIDRNYDYL KDYYAGFAIE NVVPAYIAIV QDEFDLAVAG LVALVIVLFV GVISFIVLCC CLKHWNLSVP VETRRKEALI KKQIIEDLNT TENPLWIEQK LKLYEEQELT MQVFSEPDHI SNSEAPGHLD HRSSLEQVHH VGQTVDNTYA TIQPRNNQNR LTGGGGAGGG SMRSGGGASA GGVGGAGLLL ARVDPHMNEF ADYATLRNNR APSLYEFTGS TFQAPIRDGD DAVAELI // ID CD89_DROME STANDARD; PRT; 2240 AA. AC Q9VEU1; Q9GR86; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cadherin 89D precursor. GN CAD89D OR CG14900. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Hirano S., Kimura H., Takeichi M., Uemura T.; RT "A novel member of the Drosophila cadherin superfamily, Cad89D."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: CADHERINS ARE CALCIUM DEPENDENT CELL ADHESION PROTEINS. CC THEY PREFERENTIALLY INTERACT WITH THEMSELVES IN A HOMOPHILIC CC MANNER IN CONNECTING CELLS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: CONTAINS 12 CADHERIN DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB053260; BAB20634.1; -. DR EMBL; AE003713; AAF55327.2; -. DR HSSP; P15116; 1NCJ. DR FlyBase; FBgn0038439; Cad89D. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008014; F:calcium-dependent cell adhesion molecule ac...; NAS. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion; NAS. DR InterPro; IPR002126; Cadherin. DR Pfam; PF00028; cadherin; 9. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 12. DR PROSITE; PS00232; CADHERIN_1; 7. DR PROSITE; PS50268; CADHERIN_2; 12. KW Cell adhesion; Glycoprotein; Transmembrane; Calcium; Calcium-binding; KW Repeat; Signal; Multigene family. FT SIGNAL 1 ? POTENTIAL. FT CHAIN ? 2240 CADHERIN 89D. FT DOMAIN ? 1883 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1884 1904 POTENTIAL. FT DOMAIN 1905 2240 CYTOPLASMIC (POTENTIAL). FT DOMAIN 70 179 CADHERIN 1. FT DOMAIN 180 295 CADHERIN 2. FT DOMAIN 296 411 CADHERIN 3. FT DOMAIN 412 528 CADHERIN 4. FT DOMAIN 529 643 CADHERIN 5. FT DOMAIN 824 927 CADHERIN 6. FT DOMAIN 928 1087 CADHERIN 7. FT DOMAIN 1171 1284 CADHERIN 8. FT DOMAIN 1285 1389 CADHERIN 9. FT DOMAIN 1411 1520 CADHERIN 10. FT DOMAIN 1534 1660 CADHERIN 11. FT DOMAIN 1661 1774 CADHERIN 12. FT CARBOHYD 114 114 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 119 119 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 191 191 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 278 278 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 334 334 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 417 417 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 585 585 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 720 720 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 752 752 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 822 822 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 833 833 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 983 983 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 989 989 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1006 1006 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1255 1255 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1318 1318 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1486 1486 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1529 1529 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1556 1556 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 8 8 M -> R (IN REF. 1). FT CONFLICT 53 54 GN -> AS (IN REF. 1). FT CONFLICT 208 208 D -> E (IN REF. 1). FT CONFLICT 305 305 N -> Y (IN REF. 1). FT CONFLICT 310 310 M -> I (IN REF. 1). FT CONFLICT 702 702 E -> D (IN REF. 1). FT CONFLICT 823 823 I -> L (IN REF. 1). FT CONFLICT 997 997 S -> P (IN REF. 1). FT CONFLICT 1187 1187 T -> A (IN REF. 1). FT CONFLICT 1258 1258 V -> G (IN REF. 1). FT CONFLICT 1319 1319 I -> M (IN REF. 1). FT CONFLICT 1330 1330 F -> S (IN REF. 1). FT CONFLICT 1342 1342 G -> S (IN REF. 1). FT CONFLICT 1497 1497 P -> A (IN REF. 1). FT CONFLICT 1504 1504 I -> V (IN REF. 1). FT CONFLICT 1606 1606 S -> C (IN REF. 1). FT CONFLICT 1633 1633 D -> G (IN REF. 1). FT CONFLICT 1660 1660 F -> Y (IN REF. 1). FT CONFLICT 1745 1745 D -> V (IN REF. 1). FT CONFLICT 1801 1801 P -> R (IN REF. 1). FT CONFLICT 1892 1892 L -> R (IN REF. 1). SQ SEQUENCE 2240 AA; 250647 MW; A561CAD634C28E53 CRC64; MDSEAYPMKS SVKISQKKKA SQDMAVICVW VMPLAVFGLI AIGQAAKTGQ VQGNSGSCAF HTLDGVAAES EGVRFIRLRE DAQVGKEILR LQAYPRSTAA LKGADASGDH KYFNLTEHNA TTLVVSLARS LERLVDRDVP RNLLKFRILC AGKQEKLEEG SYLSITVYIE DVNDNAPEFL NVPYVVDVDE NTSIESIIFE GVQAFDRDKP NTPNSEVHFS MSTVPEQLSA DGSPYFALKS PHRPLLILKR ELDFDNGIRQ FKLPIFAWDR GTPANQANTT ITINVRDVDD LPPKFTEGVY RTRINEFYPM TGVPIRIPLY FAPPIMAFDQ DSLNASLVYD IISGNERQLF RVNPHNGVMY LQKEIDLEEE SLPGNTFVLQ LEARQKDNPL KKALARIEVE VLDLNDNVPE FEADYYNISI VENLPTGFSV LQVNAVDRDQ GENSEFLYNL VETKDAAGAF RIDSRTGWIT VRDDRLLDRE QRRSIQLNVE ALERNPSYLD DKHLKKPGPS KVQVEITLLD TNDNTPKFEH GNLYEFKVPI NAPTGYVIGQ VVAHDPDEGP NGHLLYELQR PKGSGYIPFR LDNKNGTIYV GGPLRRGRIA VFVEATDQPT NPSERRFSLA VITIEVYATI DDQAIDFVGA PYEFWVGANT PLGTSVGQVR TTLIYEGGDE IMYDLLHTYS EGVPFAIEER SGIITVIREL SEFKRKVYQF EAVANYLFAN SSQSLVMSRS SSPLTTIASP AELSDEGVLI TNLTIHIVNK PEQKVPLRPV IEEINMNVIH FHVEENVVGG IIGQLLYKNG INLVNNELGT YREMPSEPTS RNITMGSRFR SRNRSRSSKS KRRLPRRLVG DANIKLRYII ANQQEVVNKI SITEDGTLLT LTGLDREQQP SYELTVIVEY STGLVSGAGI YQVNIKVDDV NDNAPKFNAL TYVGLINENC VVGTELSMNH AILIQDADEG PNAEFRVQLQ GDYSDEFSIE YVNGTSSENS THHKMPSTTG AFNIFNLTDQ WNDEFKYQEL HTTFMQTNFK LSSGPYFRIS YTGKRGLDRE KQQLYNLKII AADTGGLSGY AHLTVLVADV NDNAPMFERI SVFKDSRLEI REYTTDMEIY FVESSSGMTA PQATAAMMLA PPPYHIPGSP RFNVDRERSV GAGLGVVARA KSRRRMVRAL TTKCPLFAIY EDTPVGTKVL QLSASDEDFG KNALLHYELQ GEQVERTPGM PMLRVHGVKY FAIDKLSGEL SVNYPLSANI EIMLNLTVTD IDGLKDSTCL RFTVMDVNNH APTFKKSWYS FDTPEGEYKD SVLGQLTAID MDFGENANIT YTLSDSHLPF TIKPASGVLK IGGQLDRELK DKYSFQVIAT DNAPVMQRMS SSVDVEVNVL DINDNRPEFI GYDDQTKAVK FIPSVADRTL MLPVYKAYLD RSTQPGTFVR QLTAIDKDNV GNGNGLVLYS IRHQEMQAPL FQIDSRDGTI STISRINGYN DYEHLNVSVI ASDVGSPALS ATAIVIVNLQ GQAVTDPPKS TPKPEPPANV TVFQHAYYEV KLTENNEAPI EVMRLNLSAG LNPENYRWSL WLEEGLDETD AHPPFEYDAK NMLLYALKPF DREHISRYQL RIRADRLSRE ARNYARVSYP VVDERIEGLS LNECRILVHI ADENDNAPKF RGNGQPIVAV LPQSASFGYP VTRVEANDLD EGLNAEIRYR LLNEPARLFG IDELSGNIRL LGELSRTEHI YGFDVKATDR MGADDGRSGI VNVFVYIINE AKQVRLVVAG MPVEVERRIE GLMEALSDAI GKDVRVRLLE PYSGGLEPAT NAYIYAVDPH TNSIMEMEQL QDALAGLQLD ALQLQQQKLD GGKPMPRILE LAEFGQLARP AHASASSFMG GLEFVTVVLL ALISLGALIA ACCYVCMRQK RRLWSQRDFS ASDAGLTYTI AGIGSPRGQK QRRQRQQRHT QRCSKGSTGS QRPTSAFMPE SVCSSAQTQS TATATEKLEQ QLHHHHQQQA MATQQQHHQY LNEQQRQQKR EYIDVPLPKS IAKAAAVTSG GDGAVGVGST PFVLKYNACQ PVNNLNNYET SLFSLHSTGQ DSGVEFLSSR ELYETSPDSF QHGGSKRGNN TEVLCPRHAK AHLELRQPNT DSSDTYEDSL KTDEPLVAHN CRSANCEHRQ HQQHPSHHPH YQNTRFEKRS CVRHSFSGVK DDLMQQSPQI SLRPRGHALR NSMNDLEQRL HNLEQSFRRP LEFSKSNSLF // ID CD96_DROME STANDARD; PRT; 773 AA. AC Q9VBW3; O18368; Q8SZC9; Q9VBW2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine kinase receptor Cad96Ca precursor (EC 2.7.1.112) (Cadherin DE 96Ca) (Tyrosine kinase receptor HD-14). GN CAD96CA OR HD-14 OR CG10239/CG10244. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 616-668 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE FIBROBLAST GROWTH FACTOR RECEPTOR CC FAMILY. CC -!- SIMILARITY: CONTAINS 1 CADHERIN DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003751; AAF56414.2; -. DR EMBL; AY070958; AAL48580.1; -. DR EMBL; BT001586; AAN71341.1; -. DR EMBL; BT001657; AAN71412.1; -. DR EMBL; AJ002910; CAA05745.1; -. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0022800; Cad96Ca. DR GO; GO:0004713; F:protein-tyrosine kinase activity; NAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; NAS. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00112; CA; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00232; CADHERIN_1; FALSE_NEG. DR PROSITE; PS50268; CADHERIN_2; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. KW Receptor; Glycoprotein; Kinase; Tyrosine-protein kinase; ATP-binding; KW Transferase; Transmembrane; Signal. FT SIGNAL 1 48 POTENTIAL. FT CHAIN 49 773 TYROSINE KINASE RECEPTOR CAD96CA. FT DOMAIN 49 315 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 316 336 POTENTIAL. FT DOMAIN 337 773 CYTOPLASMIC (POTENTIAL). FT DOMAIN 58 172 CADHERIN. FT DOMAIN 470 749 PROTEIN KINASE. FT DOMAIN 202 236 PRO-RICH. FT NP_BIND 476 484 ATP (BY SIMILARITY). FT BINDING 504 504 ATP (BY SIMILARITY). FT ACT_SITE 610 610 BY SIMILARITY. SQ SEQUENCE 773 AA; 86220 MW; CFD6B8F27EAC46E4 CRC64; MVYHHHNHES RIIHCRKQLT SWRRRSLLLT IIVVTATVVS LISQEAEAHN QNAPPILYVR ERNWRISETE KVGQIIDRVR AEDPDGDDLI FGIEPRFSLP GGENDASPPE KIPFQIDRET GVVTLNESLA GRAGQNFLIY ITVTDGSYTA KNEVFINILG ERENSSGYRP QTSISNVVHN ISQFLPRFDQ LPGVQSIRNG LPNSRPGGWY PPVPQNNIFG PPPFGNNYPP PPPNIPGVRG EQSGEEEQPD EEVTPTTPVR ISSTTPKSRT KLTPITANNS TRVESAIPAE TTTPSGGHHN NSSSPITIFS LKSGTIPIVV TVGGFFVAIA VLLAYLCRRR LCAISRTLKK TKEKEELAKK SNQSQLSSTL TDDSRNSMVM QQWQGPVAFA NRYVPWERDQ QMGIATSQLS TGVTNGGVSS PGVPSPGTGE PGSNLGPGCL TGGAGSSGAP ENAFAGEANC DRWEFPRYRL KFFNILGEGA FGQVWRCEAT NINGNEGITT VAVKTLKESA TEVDRKDLLS ELEVMKSLEP HINVVHLLGC CTDKDPTFVI LEYVNRGKLQ TYLRSSRAER HYGNTHGKSN VLTSCDLTSF MYQVAKGMDY LTSRGIIHRD LAARNILITD DHTCKVADFG FARDVITSKI YERKSEGKLP IRWMATESLY DNIFSVKSDI WSFGILMWEI VTLGSTPYPG ISAADVMRKV RDGYRLEKPE HCRRELYNIM YYCWSHDPQE RPLFAEIIQM LDKLLHTEMD YIELERFPDH NYYNIVSLSG EKL // ID CDC2_DROME STANDARD; PRT; 297 AA. AC P23572; Q9TX68; Q9TX69; Q9TX70; Q9TX71; Q9TX72; Q9TX73; Q9TX74; AC Q9VKX5; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cell division control protein 2 homolog (EC 2.7.1.-) (p34 protein DE kinase). GN CDC2 OR CG5363. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91006057; PubMed=2120045; RA Lehner C.F., O'Farrell P.H.; RT "Drosophila cdc2 homologs: a functional homolog is coexpressed with a RT cognate variant."; RL EMBO J. 9:3573-3581(1990). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RX MEDLINE=91006056; PubMed=2120044; RA Jimenez J., Alphey L., Nurse P., Glover D.M.; RT "Complementation of fission yeast cdc2ts and cdc25ts mutants RT identifies two cell cycle genes from Drosophila: a cdc2 homologue and RT string."; RL EMBO J. 9:3565-3571(1990). RN [3] RP SEQUENCE FROM N.A., AND MUTAGENESIS OF ALA-145; GLY-148; GLU-196; RP GLY-206 AND PRO-242. RX MEDLINE=94038657; PubMed=8223248; RA Stern B., Ried G., Clegg N.J., Grigliatti T.A., Lehner C.F.; RT "Genetic analysis of the Drosophila cdc2 homolog."; RL Development 117:219-232(1993). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP MUTAGENESIS OF GLY-43; ALA-145; GLY-148; LEU-176; GLU-196; GLY-206 RP AND PRO-242, AND DEVELOPMENTAL STAGE. RX MEDLINE=94010270; PubMed=8405984; RA Clegg N.J., Whitehead I.P., Williams J.A., Spiegelman G.B., RA Grigliatti T.A.; RT "A developmental and molecular analysis of cdc2 mutations in RT Drosophila melanogaster."; RL Genome 36:676-685(1993). CC -!- FUNCTION: PLAYS A KEY ROLE IN THE CONTROL OF THE EUKARYOTIC CC CELL CYCLE. IT IS REQUIRED IN HIGHER CELLS FOR ENTRY INTO S-PHASE CC AND MITOSIS. P34 IS A COMPONENT OF THE KINASE COMPLEX THAT CC PHOSPHORYLATES THE REPETITIVE CARBOXYL-TERMINUS OF RNA CC POLYMERASE II. CC -!- ENZYME REGULATION: PHOSPHORYLATION AT THR-14 OR TYR-15 INACTIVATES CC THE ENZYME, WHILE PHOSPHORYLATION AT THR-161 ACTIVATES IT (BY CC SIMILARITY). CC -!- SUBUNIT: FORMS A STABLE BUT NON-COVALENT COMPLEX WITH A REGULATORY CC SUBUNIT AND WITH A CYCLIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CDC2/CDKX SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57485; CAA40723.1; -. DR EMBL; X57496; CAA40733.1; -. DR EMBL; S66801; -; NOT_ANNOTATED_CDS. DR EMBL; S66804; -; NOT_ANNOTATED_CDS. DR EMBL; S66805; -; NOT_ANNOTATED_CDS. DR EMBL; S66807; -; NOT_ANNOTATED_CDS. DR EMBL; S66810; -; NOT_ANNOTATED_CDS. DR EMBL; AE003628; AAF52932.1; -. DR EMBL; AY061450; AAL28998.1; -. DR HSSP; P24941; 1HCL. DR FlyBase; FBgn0004106; cdc2. DR GO; GO:0004693; F:cyclin-dependent protein kinase activity; IGI. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Cell cycle; Cell division; Mitosis; Phosphorylation. FT DOMAIN 4 287 PROTEIN KINASE. FT NP_BIND 10 18 ATP (BY SIMILARITY). FT BINDING 33 33 ATP (BY SIMILARITY). FT ACT_SITE 128 128 BY SIMILARITY. FT MOD_RES 14 14 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 15 15 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 161 161 PHOSPHORYLATION (BY CAK) (BY SIMILARITY). FT MUTAGEN 43 43 G->D: IN CDC2-E1-4; LARVAL-PUPAL LETHAL FT WITH SOME ADULT ESCAPERS. FT MUTAGEN 145 145 A->V: IN CDC2-216A; LARVAL-PUPAL LETHAL. FT MUTAGEN 148 148 G->R: IN CDC2-D57; EMBRYONIC OR LARVAL- FT PUPAL LETHAL. FT MUTAGEN 176 176 L->Q: IN CDC2-E10; LARVAL-PUPAL LETHAL. FT MUTAGEN 196 196 E->K: IN CDC2-E1-24; LARVAL-PUPAL LETHAL FT WITH SOME ADULT ESCAPERS. FT MUTAGEN 206 206 G->D: IN CDC2-E1-23; LARVAL-PUPAL LETHAL. FT MUTAGEN 242 242 P->S: IN CDC2-E1-9; LARVAL-PUPAL LETHAL. SQ SEQUENCE 297 AA; 34439 MW; 952CF136D8AB64C0 CRC64; MEDFEKIEKI GEGTYGVVYK GRNRLTGQIV AMKKIRLESD DEGVPSTAIR EISLLKELKH ENIVCLEDVL MEENRIYLIF EFLSMDLKKY MDSLPVDKHM ESELVRSYLY QITSAILFCH RRRVLHRDLK PQNLLIDKSG LIKVADFGLG RSFGIPVRIY THEIVTLWYR APEVLLGSPR YSCPVDIWSI GCIFAEMATR KPLFQGDSEI DQLFRMFRIL KTPTEDIWPG VTSLPDYKNT FPCWSTNQLT NQLKNLDANG IDLIQKMLIY DPVHRISAKD ILEHPYFNGF QSGLVRN // ID CDK5_DROME STANDARD; PRT; 294 AA. AC P48609; Q94878; Q9V7D8; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cell division protein kinase 5 homolog (EC 2.7.1.-). GN CDK5 OR CG8203. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95104441; PubMed=7805863; RA Hellmich M.R., Kennison J.A., Hampton L.L., Battey J.F.; RT "Cloning and characterization of the Drosophila melanogaster CDK5 RT homolog."; RL FEBS Lett. 356:317-321(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=97084555; PubMed=8930898; RA Sauer K., Weigmann K., Sigrist S., Lehner C.F.; RT "Novel members of the cdc2-related kinase family in Drosophila: RT cdk4/6, cdk5, PFTAIRE, and PITSLRE kinase."; RL Mol. Biol. Cell 7:1759-1769(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLY INVOLVED IN THE CONTROL OF THE CELL CYCLE. CC INTERACTS WITH D1 AND D3-TYPE G1 CYCLINS. POSSIBLE REGULATOR OF CC NEURONAL DIFFERENTIATION AND/OR DEVELOPMENT. CC -!- TISSUE SPECIFICITY: ABUNDANTLY EXPRESSED IN ALL ADULT TISSUES. CC LOWER LEVELS FOUND IN LARVAE AND EARLY EMBRYOS. BARELY DETECTABLE CC IN LATE EMBRYOS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CDC2/CDKX SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U21552; AAA63754.1; -. DR EMBL; X99511; CAA67861.1; -. DR EMBL; AE003810; AAF58119.1; -. DR EMBL; AY061049; AAL28597.1; -. DR PIR; S51008; S51008. DR HSSP; P24941; 1CKP. DR FlyBase; FBgn0013762; Cdk5. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Cell cycle; Cell division; Phosphorylation. FT DOMAIN 4 286 PROTEIN KINASE. FT NP_BIND 10 18 ATP (BY SIMILARITY). FT BINDING 33 33 ATP (BY SIMILARITY). FT ACT_SITE 126 126 BY SIMILARITY. FT MOD_RES 14 14 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 15 15 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 159 159 PHOSPHORYLATION (BY SIMILARITY). FT CONFLICT 25 25 D -> A (IN REF. 1). FT CONFLICT 166 166 W -> L (IN REF. 1). SQ SEQUENCE 294 AA; 33180 MW; E6B7B37B2410AA23 CRC64; MQKYDKMEKI GEGTYGTVFK GRNRDTMEIV ALKRVRLDED DEGVPSSALR EICLLKELKH KNIVRLIDVL HSDKKLTLVF EHCDQDLKKY FDSLNGEIDM AVCRSFMLQL LRGLAFCHSH NVLHRDLKPQ NLLINKNGEL KLADFGLARA FGIPVKCYSA EVVTLWYRPP DVLFGAKLYT TSIDMWSAGC ILAELADAGR PLFPGSDVLD QLMKIFRVLG TPNEDSWPGV SHLSDYVALP SFPAITSWSQ LVPRLNSKGR DLLQKLLICR PNQRISAEAA MQHPYFTDSS SSGH // ID CDN2_DROME STANDARD; PRT; 2215 AA. AC Q9VJB6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative neural-cadherin 2 precursor (Cadherin-N2 protein) (DN2- DE cadherin). GN CADN2 OR CG7527. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: CADHERINS ARE CALCIUM DEPENDENT CELL ADHESION PROTEINS. CC THEY PREFERENTIALLY INTERACT WITH THEMSELVES IN A HOMOPHILIC CC MANNER IN CONNECTING CELLS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: CONTAINS 7 CADHERIN DOMAINS. CC -!- SIMILARITY: CONTAINS 3 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 2 LAMININ G-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003656; AAF53636.2; -. DR HSSP; P00740; 1EDM. DR FlyBase; FBgn0032655; CadN2. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008014; F:calcium-dependent cell adhesion molecule ac...; NAS. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion; NAS. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR000233; Cadherin_C_term. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006210; IEGF. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF00028; cadherin; 4. DR Pfam; PF01049; Cadherin_C_term; 1. DR Pfam; PF00008; EGF; 2. DR Pfam; PF00054; laminin_G; 2. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 6. DR SMART; SM00181; EGF; 3. DR SMART; SM00179; EGF_CA; 3. DR SMART; SM00282; LamG; 2. DR PROSITE; PS00232; CADHERIN_1; 4. DR PROSITE; PS50268; CADHERIN_2; 7. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 3. DR PROSITE; PS01187; EGF_CA; FALSE_NEG. DR PROSITE; PS50025; LAM_G_DOMAIN; 2. KW Hypothetical protein; Cell adhesion; Glycoprotein; Transmembrane; KW Calcium; Calcium-binding; Repeat; Signal; EGF-like domain; KW Multigene family. FT SIGNAL 1 ? POTENTIAL. FT CHAIN ? 2215 PUTATIVE NEURAL-CADHERIN 2. FT DOMAIN ? 1743 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1744 1764 POTENTIAL. FT DOMAIN 1765 2215 CYTOPLASMIC (POTENTIAL). FT DOMAIN 146 249 CADHERIN 1. FT DOMAIN 250 422 CADHERIN 2. FT DOMAIN 423 534 CADHERIN 3. FT DOMAIN 535 655 CADHERIN 4. FT DOMAIN 656 760 CADHERIN 5. FT DOMAIN 761 879 CADHERIN 6. FT DOMAIN 880 982 CADHERIN 7. FT DOMAIN 1143 1180 EGF-LIKE 1. FT DOMAIN 1181 1387 LAMININ G-LIKE 1. FT DOMAIN 1390 1430 EGF-LIKE 2. FT DOMAIN 1433 1625 LAMININ G-LIKE 2. FT DOMAIN 1693 1731 EGF-LIKE 3. FT DISULFID 1147 1158 POTENTIAL. FT DISULFID 1152 1167 POTENTIAL. FT DISULFID 1170 1179 POTENTIAL. FT DISULFID 1394 1409 POTENTIAL. FT DISULFID 1403 1418 POTENTIAL. FT DISULFID 1420 1429 POTENTIAL. FT DISULFID 1697 1708 POTENTIAL. FT DISULFID 1702 1719 POTENTIAL. FT DISULFID 1721 1730 POTENTIAL. FT CARBOHYD 20 20 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 199 199 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 231 231 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 308 308 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 430 430 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 434 434 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 453 453 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 547 547 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 771 771 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 963 963 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1080 1080 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1118 1118 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1139 1139 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1546 1546 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1628 1628 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 2215 AA; 248062 MW; B9F6B2FA25D77423 CRC64; MSHITRKRLL TLDEESQHIN STKRCGSNCI EKMLTKWSRQ SIPGVNSISR KRSFPWEDNS PDIFPAKHSR KHIIKKKSKT IHEPEVPIDF LMGLPVLLDS DFSDSEECRP KSEIHVAKPE TEDNRDLFTY QQLKLMCCEM MKQCEDRVVL EYEIALTQKM AEQYDTFIKF NHDQLQREST NIRYQITGGN IGNAFAVQNT TGVIYVASPL DYETRPRYEL RLEATRNRKN NYTTVVINVR DVNDNPPVFD RQTYRTQITE EDDRNLPKRI LQVTATDGDV DRPINIVYFL TGQGIDPDNP ANSKFDINRT TGDIFVLKAK TKRLTGPKHS HTQATHNKRM LKGIFIEWMA FISSLAMQFR VDNSFNEKSN NRLLCPLDRD QPNGRPQWRF TVFAQDEGGE GLVGYADIQV NLKDINDNAP QFPQGIYFGN VTENGTAGSS VMTMSAVDYD DPNESTNAKL IYSIEKNVIE EETGAPIFEI EPETGLIKTA VCCLDRERTP DYSIQVVAMD GGGLKGTGTA SIRVKDLNDM PPQFTKDEWV TEVDETNGTY IPETPILTVT VQDEDETNTF QYKVVPNSGF GADKFAMVRN GDGTGSLKII QPLDYEDPLQ SSGFRFRIQV NDKGDDGPGG SDKYHVAYSW VVVKLRDIND NVPKFDREHI EVSIYEDTKV GTILEQFKAT DADQGGHSKV AYKIVRSTNR KRQFAISDRG AVSIQRPLDR ETQDRHHIQI LAIDDGSPAR TATATLTVIV KDVNDNAPTF AQDYKPTLPE NVSGKKILEV AAKDPDDRLR GNGGPFTFRL DPLASDEIKA GFKVEYDRRG DNENGVAIIS SLRPFDREAQ KSYAIPIEIK DNGAPAMTGT STLTVTIGDV NDNKMQPGSK SVLVYNYQGQ SQDTPIGRVY VNDPDDWDVP DKKYYWEVQE HQRFKLDTDT GILTMRAGTR RGRYQLRFKV YDREHGQEDI PANLSVTVRD ITAEAVQQAG SMRLSHITDE DFVRTWNPVK NQVEPSKLER FRNKLAELLY TDRDNVDVFS VQLKEGSPYP LTDVHFAARS ATQQPYFKAV RLNGVVQMHR EEIEKDVGLN ITMVNINECL HEGKGKCGSN SCTSKVELGK KPYTVSVNRT ALVGVRLDIS AQCVCRARNF THQDHNCRTH LCYNGGRCVE TRNGPKCVAC PVGYNGPRCQ QSTRSFRGNG WAWYPPLQLC QESHLSLEFI TRVADGLILY NGPIVPPKPE ETVISDFIAL ELEQGYPRLL IDFGSGTLEL RVKTKKTLDD GVWHRLDIFW DTENVRMVVD FCRTALVSEM EDGTPPEFDD NACQARGQIP PFAESLNLNQ PLQLGGLYRQ HFDQTLYNWQ YAFSSKGFDG CIRNVIHNSE HYDLAFPALA RNSFPACPQT DEVCLKTEHT ARCWEHGNCV ASLVQAKCHC QPGWMGPGCN VPTIPTTFKA QSYVKFALSF EPDRFSTQLQ LRFRTREQGG ELFRVSDQHH REYAILELRR GHLQFRYNLN SMRNEEQLLT LTAIAVNDGQ WHVIRISRYG SAALMELDGG ESRRYNESFH FTGHQWLTID KQEGVYAGGK AEYTGIKTFE VQSDFQRSCL DDIRRRWPAT WSATAPRTGR ARMSSVPIPL TASTCGTNTS ALVGSSSRSA LLEFVSLTQD TKMSDKELSS IGIRNDFNLN VHNVCEGCSE GRIMSSDTKG CVDRNECLDL PCLNGATCIN LEPRLRYRCI CPEGYWGENC ELVQEGQRLK LSMGALGAIF VCLIIILSQC KCVFSYAMHD NLFSFRQLVW DLKGFSISAT LWALFRMAFI YTYISVNSGK RLLALIFVLY SRKRKTTKKK KRSGPEKDVR ETVISYEDEG GGEDDMTAFD ITPLQIPISA QGGPPDIAAC KMPIIYPVMT LLPPGQELNV AYLMEERKQR IDKDNNAPPF DDLRNFTFEG SGSIAESLSS LASGTDDENQ DFNYLQNWGP RFNALAAMYV HDKAKASSQL PSDGGGGSGD GPGPGASSSS PLGGGGTGGG SGIPGNVLAV VATGSGAGPG GGGGSTRKLN QTKPEFGQLP ENVEQCNICV PPTGERARLP TGARSQVASE NRESRAGKAA LKAATEPTQP QKLAERGGNL IKDFWMPANP AIRLLTLPND AWCLHFRPRH CGIWCPKRAA KSRQRCPNGS RRKEATLGAS SERQSSTERL TGQHALPLTE NQKLSANWMN LRQFWGQSLL GRKKC // ID CDSA_DROME STANDARD; PRT; 447 AA. AC P56079; Q9VSE0; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Phosphatidate cytidylyltransferase, photoreceptor-specific DE (EC 2.7.7.41) (CDP-diglyceride synthetase) (CDP-diglyceride DE pyrophosphorylase) (CDP-diacylglycerol synthase) (CDS) DE (CTP:phosphatidate cytidylyltransferase) (CDP-DAG synthase) (CDP-DG DE synthetase). GN CDSA OR CG7962. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Retina; RX MEDLINE=95115794; PubMed=7816135; RA Wu L., Niemeyer B., Colley N., Socolich M., Zuker C.S.; RT "Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol RT synthase."; RL Nature 373:216-222(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE REGENERATION OF THE SIGNALING MOLECULE CC PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE (PTDINSP2) FROM PHOSPHATIDIC CC ACID AND MAINTENANCE OF ITS STEADY SUPPLY DURING SIGNALING CC THUS PLAYS AN ESSENTIAL ROLE DURING PHOSPHOLIPASE C-MEDIATED CC TRANSDUCTION. CC -!- CATALYTIC ACTIVITY: CTP + PHOSPHATIDATE = DIPHOSPHATE + CDP- CC DIACYLGLYCEROL. CC -!- PATHWAY: PHOSPHOLIPID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: RETINA. LOCALIZED TO THE PHOTORECEPTOR CC NEURONS, BOTH IN THE COMPOUND EYES AND OCELLI. CC -!- SIMILARITY: BELONGS TO THE CDS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003556; AAF50483.1; -. DR FlyBase; FBgn0010350; CdsA. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthesis; NAS. DR GO; GO:0007602; P:phototransduction; IGI. DR GO; GO:0016056; P:rhodopsin mediated signaling; IMP. DR InterPro; IPR000374; PC_trans. DR Pfam; PF01148; CTP_transf_1; 1. DR PROSITE; PS01315; CDS; 1. KW Transferase; Nucleotidyltransferase; Phospholipid biosynthesis; KW Transmembrane; Vision. FT TRANSMEM 88 108 POTENTIAL. FT TRANSMEM 147 167 POTENTIAL. FT TRANSMEM 180 200 POTENTIAL. FT TRANSMEM 203 223 POTENTIAL. FT TRANSMEM 227 247 POTENTIAL. FT TRANSMEM 276 296 POTENTIAL. FT TRANSMEM 350 370 POTENTIAL. FT CONFLICT 444 444 D -> H (IN REF. 1). SQ SEQUENCE 447 AA; 51511 MW; 2E690CD02D3F4187 CRC64; MAEVRRRKGE DEPLEDTAIS GSDAANKRNS AADSSDHVDS EEEKIPEEKF VDELAKNLPQ GTDKTPEILD SALKDLPDRW KNWVIRGIFT WIMICGFALI IYGGPLALMI TTLLVQVKCF QEIISIGYQV YRIHGLPWFR SLSWYFLLTS NYFFYGENLV DYFGVVINRV EYLKFLVTYH RFLSFALYII GFVWFVLSLV KKYYIKQFSL FAWTHVSLLI VVTQSYLIIQ NIFEGLIWFI VPVSMIVCND VMAYVFGFFF GRTPLIKLSP KKTWEGFIGG GFATVLFGIL FSYVLCNYQY FICPIQYSEE QGRMTMSCVP SYLFTPQEYS LKLFGIGKTL NLYPFIWHSI SLSLFSSIIG PFGGFFASGF KRAFKIKDFG DMIPGHGGIM DRFDCQFLMA TFVNVYISSF IRTPSPAKLL TQIYNLKPDQ QYQIYQSLKD NLGDMLT // ID CEB_DROME STANDARD; PRT; 444 AA. AC Q02637; DT 01-JUN-1994 (Rel. 29, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE CCAAT/enhancer binding protein (C/EBP) (Slow border cell protein). GN SLBO. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93008243; PubMed=1394432; RA Montell D.J., Rorth P., Spradling A.C.; RT "Slow border cells, a locus required for a developmentally regulated RT cell migration during oogenesis, encodes Drosophila C/EBP."; RL Cell 71:51-62(1992). RN [2] RP CHARACTERIZATION. RX MEDLINE=93093465; PubMed=1459454; RA Rorth P., Montell D.J.; RT "Drosophila C/EBP: a tissue-specific DNA-binding protein required for RT embryonic development."; RL Genes Dev. 6:2299-2311(1992). CC -!- FUNCTION: MAY BE REQUIRED FOR THE EXPRESSION OF GENE PRODUCTS CC MEDIATING BORDER CELL MIGRATION. AMONG THE DNA SEQUENCES THAT CC THIS PROTEIN BIND WITH HIGH AFFINITY IS A CONSERVED SITE WITHIN CC THE PROMOTER OF ITS GENE. CC -!- SUBUNIT: BINDS DNA AS A DIMER AND CAN FORM STABLE HETERODIMERS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE BZIP FAMILY. C/EBP SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L00632; AAA28415.1; -. DR TRANSFAC; T00106; -. DR FlyBase; FBgn0005638; slbo. DR GO; GO:0007298; P:border cell migration (sensu Insecta); IMP. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF00170; bZIP; 1. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; FALSE_NEG. KW Transcription regulation; Activator; DNA-binding; Nuclear protein. FT DOMAIN 45 68 POLY-GLN. FT DNA_BIND 364 380 BASIC MOTIF (BY SIMILARITY). FT DOMAIN 386 422 LEUCINE-ZIPPER (BY SIMILARITY). SQ SEQUENCE 444 AA; 48892 MW; 2D980C4BF1C2CC78 CRC64; MLNMESPQMY ADAVQTLAQL DLKKEPPLQQ ATIGQITLTA MSTAQQQQQQ QQQQQQQQQQ QQQQPQQQTT DANNNTSQDA ALLVKQHAMH QMQQVAALGS NNNLLQKQML QQYSTQTDLD ELTTQEITLD LQHLIDDQFR DTETLGIFSD MVTSPGGLSA TLRRANGLGG AKVLQQQTLR NQHGYGGRGG GGGAGGALAY MPQPVHATYN NSSDENSSVG SDSSTIKEEP IDPEYRRHLQ EAASQQAAFM GNGAGLYNGY GSGANGLTGG GNPLNGGNTT PSSNGSNGST GSSNGSQFTN LTTANVLAHH NLPHLAAAAG AHNLLKQHSK LHAQQQHQQH QQQQQHRKHS NKHVDKGTDE YRRRRERNNI AVRKSREKAK VRSREVEERV KSLLKEKDAL IRQLGEMTNE LQLHKQIYMQ LMNHANPEVS RVCRSFLNTN EHSL // ID CECA_DROME STANDARD; PRT; 63 AA. AC P14954; O16815; O16816; O16817; O16818; O16819; O16820; O16821; AC O61275; O61276; O61277; O61279; O62590; P82449; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cecropin A1/A2 precursor. GN (CECA1 OR CG1365) AND (CECA2 OR CG1367). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND INDUCTION. RC STRAIN=Canton-S; RX MEDLINE=90107946; PubMed=2104802; RA Kylsten P., Samakovlis C., Hultmark D.; RT "The cecropin locus in Drosophila; a compact gene cluster involved in RT the response to infection."; RL EMBO J. 9:217-224(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=B115, B137, B141, B205, B208, B222, B225, B226, B316, M13, Z5, RC Z10, Z18, Z22, and Z24; RX MEDLINE=97476321; PubMed=9335607; RA Clark A.G., Wang L.; RT "Molecular population genetics of Drosophila immune system genes."; RL Genetics 147:713-724(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=MA1, MA2, MA3, MJ1, MJ2, MJ3, and 3RC; RX MEDLINE=98221115; PubMed=9553148; RA Date A., Satta Y., Takahata N., Chigusa S.I.; RT "Evolutionary history and mechanism of the Drosophila cecropin gene RT family."; RL Immunogenetics 47:417-429(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=M2, M11, M26, M36, M40, M47, M54, M55, and M66; RX MEDLINE=98393576; PubMed=9725836; RA Ramos-Onsins S., Aguade M.; RT "Molecular evolution of the Cecropin multigene family in Drosophila: RT functional genes vs pseudogenes."; RL Genetics 150:157-171(1998). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP INDUCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; RX MEDLINE=90361012; PubMed=2390977; RA Samakovlis C., Kimbrell D.A., Kylsten P., Engstrom A., Hultmark D.; RT "The immune response in Drosophila: pattern of cecropin expression RT and biological activity."; RL EMBO J. 9:2969-2976(1990). CC -!- FUNCTION: CECROPINS HAVE LYTIC AND ANTIBACTERIAL ACTIVITY AGAINST CC SEVERAL GRAM-POSITIVE AND GRAM-NEGATIVE BACTERIA. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: STRONGLY EXPRESSED IN LARVAL, PUPAL AND ADULT CC FAT BODY AND HEMOCYTES AFTER INJECTION OF BACTERIA. MAXIMAL CC EXPRESSION IN THE ADULT INVOLVES FAT BODY CELLS OF THE HEAD, CC THORAX AND ABDOMEN. CC -!- INDUCTION: INDUCED AS PART OF THE HUMORAL RESPONSE TO A BACTERIAL CC INVASION. TRANSCRIPTS APPEAR WITHIN ONE HOUR AFTER INJECTION OF CC BACTERIA INTO THE HEMOCOEL, REACH A MAXIMUM AFTER 2-6 HOURS AND CC HAVE ALMOST DISAPPEARED AFTER 24 HOURS. SIMILAR RESPONSE IS SEEN CC WHEN FLIES INGEST BACTERIA PRESENT IN THEIR FOOD. CC -!- SIMILARITY: BELONGS TO THE CECROPIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16972; CAA34843.1; -. DR EMBL; X16972; CAA34844.1; -. DR EMBL; AF018964; AAB82461.1; -. DR EMBL; AF018965; AAB82462.1; -. DR EMBL; AF018966; AAB82463.1; -. DR EMBL; AF018967; AAB82464.1; -. DR EMBL; AF018968; AAB82465.1; -. DR EMBL; AF018969; AAB82466.1; -. DR EMBL; AF018970; AAB82467.1; -. DR EMBL; AF018971; AAB82468.1; -. DR EMBL; AF018972; AAB82469.1; -. DR EMBL; AF018973; AAB82470.1; -. DR EMBL; AF018974; AAB82471.1; -. DR EMBL; AF018975; AAB82472.1; -. DR EMBL; AF018976; AAB82473.1; -. DR EMBL; AF018977; AAB82474.1; -. DR EMBL; AF018978; AAB82475.1; -. DR EMBL; AF018979; AAB82476.1; -. DR EMBL; AF018980; AAB82477.1; -. DR EMBL; AF018981; AAB82478.1; -. DR EMBL; AF018982; AAB82479.1; -. DR EMBL; AF018983; AAB82480.1; -. DR EMBL; AF018984; AAB82481.1; -. DR EMBL; AB010791; BAA28719.1; -. DR EMBL; AB010791; BAA28721.1; -. DR EMBL; AB010792; BAA28723.1; -. DR EMBL; AB010792; BAA28725.1; -. DR EMBL; AB010793; BAA28727.1; -. DR EMBL; AB010793; BAA28728.1; -. DR EMBL; AB010794; BAA28730.1; -. DR EMBL; AB010794; BAA28732.1; -. DR EMBL; AB010795; BAA28734.1; -. DR EMBL; AB010796; BAA28736.1; -. DR EMBL; AB010796; BAA28738.1; -. DR EMBL; AB010797; BAA28740.1; -. DR EMBL; AB010797; BAA28742.1; -. DR EMBL; Y16852; CAA76425.1; -. DR EMBL; Y16852; CAA76427.1; -. DR EMBL; Y16853; CAA76431.1; -. DR EMBL; Y16853; CAA76433.1; -. DR EMBL; Y16854; CAA76437.1; -. DR EMBL; Y16854; CAA76439.1; -. DR EMBL; Y16855; CAA76443.1; -. DR EMBL; Y16855; CAA76445.1; -. DR EMBL; Y16856; CAA76449.1; -. DR EMBL; Y16856; CAA76451.1; -. DR EMBL; Y16857; CAA76455.1; -. DR EMBL; Y16857; CAA76457.1; -. DR EMBL; Y16858; CAA76463.1; -. DR EMBL; Y16859; CAA76467.1; -. DR EMBL; Y16859; CAA76469.1; -. DR EMBL; Y16861; CAA76477.1; -. DR EMBL; Y16861; CAA76479.1; -. DR EMBL; AE003773; AAF57025.1; -. DR EMBL; AE003773; AAF57026.1; -. DR FlyBase; FBgn0000276; CecA1. DR FlyBase; FBgn0000277; CecA2. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0008225; F:Gram-negative antibacterial peptide activity; IDA. DR GO; GO:0008224; F:Gram-positive antibacterial peptide activity; IDA. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IDA. DR InterPro; IPR000875; Cecropin. DR InterPro; IPR003253; Sarctxn_cecrpn. DR Pfam; PF00272; cecropin; 1. DR ProDom; PD001670; Sarctxn_cecrpn; 1. DR PROSITE; PS00268; CECROPIN; 1. KW Insect immunity; Antibiotic; Hemolymph; Amidation; Multigene family; KW Signal; Polymorphism. FT SIGNAL 1 23 FT CHAIN 24 62 CECROPIN A1/A2. FT MOD_RES 62 62 AMIDATION (G-63 PROVIDE AMIDE GROUP). FT VARIANT 2 2 N -> K (IN CECA2; STRAIN Z24). FT VARIANT 2 2 N -> D (IN CECA2; STRAIN Z5). FT VARIANT 3 3 F -> L (IN CECA2; STRAINS M2, MJ1 AND FT MJ3). FT VARIANT 7 7 F -> L (IN CECA2; STRAIN B226). FT VARIANT 8 8 V -> A (IN CECA1; STRAIN M26). FT VARIANT 8 8 V -> G (IN CECA2; STRAIN Z5). FT VARIANT 11 11 A -> P (IN CECA1; STRAINS B226 AND B316). FT VARIANT 11 11 A -> T (IN CECA2; STRAINS B115, M11 AND FT M47). FT VARIANT 14 14 L -> V (IN CECA1; STRAIN MJ3). FT VARIANT 20 20 Q -> E (IN CECA1; STRAIN B316). FT VARIANT 36 36 V -> A (IN CECA2; STRAIN MJ2). FT VARIANT 45 45 I -> V (IN CECA1; STRAIN MJ1). FT VARIANT 45 45 I -> IFT (IN CECA1; STRAIN M40). FT VARIANT 56 56 N -> D (IN CECA1; STRAIN MJ1). FT VARIANT 61 61 A -> G (IN CECA1; STRAIN Z24). SQ SEQUENCE 63 AA; 6771 MW; F709070C5BEC7D74 CRC64; MNFYNIFVFV ALILAITIGQ SEAGWLKKIG KKIERVGQHT RDATIQGLGI AQQAANVAAT ARG // ID CECB_DROME STANDARD; PRT; 63 AA. AC P14956; Q9V425; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cecropin B precursor. GN CECB OR CG1878. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90107946; PubMed=2104802; RA Kylsten P., Samakovlis C., Hultmark D.; RT "The cecropin locus in Drosophila; a compact gene cluster involved in RT the response to infection."; RL EMBO J. 9:217-224(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=M31, B115, B137, B202, and B225; RX MEDLINE=97476321; PubMed=9335607; RA Clark A.G., Wang L.; RT "Molecular population genetics of Drosophila immune system genes."; RL Genetics 147:713-724(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=MA2, MA3, MJ1, and MJ3; RX MEDLINE=98221115; PubMed=9553148; RA Date A., Satta Y., Takahata N., Chigusa S.I.; RT "Evolutionary history and mechanism of the Drosophila cecropin gene RT family."; RL Immunogenetics 47:417-429(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Montemayor; RX MEDLINE=98393576; PubMed=9725836; RA Ramos-Onsins S., Aguade M.; RT "Molecular evolution of the Cecropin multigene family in Drosophila: RT functional genes vs pseudogenes."; RL Genetics 150:157-171(1998). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP INDUCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; RX MEDLINE=90361012; PubMed=2390977; RA Samakovlis C., Kimbrell D.A., Kylsten P., Engstrom A., Hultmark D.; RT "The immune response in Drosophila: pattern of cecropin expression RT and biological activity."; RL EMBO J. 9:2969-2976(1990). CC -!- FUNCTION: CECROPINS HAVE LYTIC AND ANTIBACTERIAL ACTIVITY AGAINST CC SEVERAL GRAM-POSITIVE AND GRAM-NEGATIVE BACTERIA. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: STRONGLY EXPRESSED IN LARVAL, PUPAL AND ADULT CC FAT BODY AND HEMOCYTES AFTER INJECTION OF BACTERIA. MAXIMAL CC EXPRESSION IS SEEN IN PUPAE. CC -!- INDUCTION: INDUCED AS PART OF THE HUMORAL RESPONSE TO A BACTERIAL CC INVASION. TRANSCRIPTS APPEAR WITHIN ONE HOUR AFTER INJECTION OF CC BACTERIA INTO THE HEMOCOEL, REACH A MAXIMUM AFTER 2-6 HOURS AND CC HAVE ALMOST DISAPPEARED AFTER 24 HOURS. SIMILAR RESPONSE IS SEEN CC WHEN FLIES INGEST BACTERIA PRESENT IN THEIR FOOD. CC -!- SIMILARITY: BELONGS TO THE CECROPIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16972; CAA34845.1; -. DR EMBL; AF018994; AAB82491.1; -. DR EMBL; AF018995; AAB82492.1; -. DR EMBL; AF018997; AAB82494.1; -. DR EMBL; AF019000; AAB82497.1; -. DR EMBL; AB010792; BAA28726.1; -. DR EMBL; AB010793; BAA28729.1; -. DR EMBL; AB010794; BAA28733.1; -. DR EMBL; AB010796; BAA28739.1; -. DR EMBL; Y16852; CAA76429.1; -. DR EMBL; Y16853; CAA76435.1; -. DR EMBL; Y16854; CAA76441.1; -. DR EMBL; Y16855; CAA76447.1; -. DR EMBL; Y16858; CAA76465.1; -. DR EMBL; Y16859; CAA76471.1; -. DR EMBL; AE003773; AAF57027.1; -. DR PIR; S07666; S07666. DR FlyBase; FBgn0000278; CecB. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0008225; F:Gram-negative antibacterial peptide activity; IDA. DR GO; GO:0008224; F:Gram-positive antibacterial peptide activity; IDA. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IDA. DR InterPro; IPR000875; Cecropin. DR InterPro; IPR003253; Sarctxn_cecrpn. DR Pfam; PF00272; cecropin; 1. DR ProDom; PD001670; Sarctxn_cecrpn; 1. DR PROSITE; PS00268; CECROPIN; 1. KW Insect immunity; Antibiotic; Hemolymph; Amidation; Multigene family; KW Signal. FT SIGNAL 1 23 FT CHAIN 24 62 CECROPIN B. FT MOD_RES 62 62 AMIDATION (G-63 PROVIDE AMIDE GROUP). SQ SEQUENCE 63 AA; 6778 MW; 26D0251BF3C28AB4 CRC64; MNFNKIFVFV ALILAISLGN SEAGWLRKLG KKIERIGQHT RDASIQVLGI AQQAANVAAT ARG // ID CECC_DROME STANDARD; PRT; 63 AA. AC P29561; O16837; Q9VA89; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cecropin C precursor. GN CECC OR CG1373. OS Drosophila melanogaster (Fruit fly), OS Drosophila mauritiana (Fruit fly), OS Drosophila sechellia (Fruit fly), and OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7226, 7238, 7240; RN [1] RP SEQUENCE FROM N.A., INDUCTION, AND TISSUE SPECIFICITY. RC SPECIES=D.melanogaster; STRAIN=Canton-S; RX MEDLINE=92155231; PubMed=1740152; RA Tryselius Y., Samakovlis C., Kimbrell D.A., Hultmark D.; RT "CecC, a cecropin gene expressed during metamorphosis in Drosophila RT pupae."; RL Eur. J. Biochem. 204:395-399(1992). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=B009, B101, B115, M31, and Z5; RX MEDLINE=97476321; PubMed=9335607; RA Clark A.G., Wang L.; RT "Molecular population genetics of Drosophila immune system genes."; RL Genetics 147:713-724(1997). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=D.mauritiana, D.sechellia, and D.simulans; RC STRAIN=Mauritius, Seychelles, S1, and S2; RX MEDLINE=21962106; PubMed=11965438; RA Date-Ito A., Kasahara K., Sawai H., Chigusa S.I.; RT "Rapid evolution of the male-specific antibacterial protein andropin RT gene in Drosophila."; RL J. Mol. Evol. 54:665-670(2002). CC -!- FUNCTION: CECROPINS HAVE LYTIC AND ANTIBACTERIAL ACTIVITY AGAINST CC SEVERAL GRAM-POSITIVE AND GRAM-NEGATIVE BACTERIA. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: IN THE ANTERIOR END OF THE LARVAL HINDGUT AND CC IN OTHER LARVAL TISSUES THAT ARE UNDERGOING HISTOLYSIS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING METAMORPHOSIS IN PUPAE. CC -!- INDUCTION: INDUCED AS PART OF THE HUMORAL RESPONSE TO A BACTERIAL CC INVASION. CC -!- SIMILARITY: BELONGS TO THE CECROPIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11167; CAA77559.1; -. DR EMBL; AF019007; AAB82504.1; -. DR EMBL; AF019008; AAB82505.1; -. DR EMBL; AF019009; AAB82506.1; -. DR EMBL; AF019014; AAB82511.1; -. DR EMBL; AF019019; AAB82516.1; -. DR EMBL; AE003773; AAF57028.1; -. DR EMBL; AB047055; BAB78560.1; -. DR EMBL; AB047056; BAB78561.1; -. DR EMBL; AB047057; BAB78562.1; -. DR EMBL; AB047058; BAB78563.1; -. DR PIR; S23501; S23501. DR FlyBase; FBgn0000279; CecC. DR FlyBase; FBgn0023317; Dmau\CecC. DR FlyBase; FBgn0046928; Dsec\CecC. DR FlyBase; FBgn0046915; Dsim\CecC. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0008225; F:Gram-negative antibacterial peptide activity; IDA. DR GO; GO:0008224; F:Gram-positive antibacterial peptide activity; IDA. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IDA. DR InterPro; IPR000875; Cecropin. DR InterPro; IPR003253; Sarctxn_cecrpn. DR Pfam; PF00272; cecropin; 1. DR ProDom; PD001670; Sarctxn_cecrpn; 1. DR PROSITE; PS00268; CECROPIN; 1. KW Insect immunity; Antibiotic; Hemolymph; Amidation; Multigene family; KW Signal. FT SIGNAL 1 23 FT CHAIN 24 62 CECROPIN C. FT MOD_RES 62 62 AMIDATION (G-63 PROVIDE AMIDE GROUP). SQ SEQUENCE 63 AA; 6813 MW; 95686510DA767EDA CRC64; MNFYKIFVFV ALILAISIGQ SEAGWLKKLG KRIERIGQHT RDATIQGLGI AQQAANVAAT ARG // ID CF1A_DROME STANDARD; PRT; 427 AA. AC P16241; Q24460; Q9VRY9; DT 01-APR-1990 (Rel. 14, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE POU-domain protein CF1A (Chorion factor 1A) (CF1-A) (Ventral veins DE lacking protein) (Drifter protein). GN VVL OR CF1A OR CG10037. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91204052; PubMed=1673230; RA Treacy M.N., He X., Rosenfeld M.G.; RT "I-POU: a POU-domain protein that inhibits neuron-specific gene RT activation."; RL Nature 350:577-584(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=92001544; PubMed=1680380; RA Billin A.N., Cockerill K.A., Poole S.J.; RT "Isolation of a family of Drosophila POU domain genes expressed in RT early development."; RL Mech. Dev. 34:75-84(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 83-427 FROM N.A. RX MEDLINE=90136944; PubMed=1967821; RA Johnson W.A., Hirsh J.; RT "Binding of a Drosophila POU-domain protein to a sequence element RT regulating gene expression in specific dopaminergic neurons."; RL Nature 343:467-470(1990). RN [6] RP SHOWS THAT CF1A DOES NOT ASSOCIATE WITH I-POU. RX MEDLINE=97140288; PubMed=8986770; RA Turner E.E.; RT "Similar DNA recognition properties of alternatively spliced RT Drosophila POU factors."; RL Proc. Natl. Acad. Sci. U.S.A. 93:15097-15101(1996). CC -!- FUNCTION: BINDS TO A DNA SEQUENCE ELEMENT REQUIRED FOR THE CC EXPRESSION OF THE DOPA DECARBOXYLASE GENE (DDC) IN SPECIFIC CC DOPAMINERGIC NEURONS. COULD ALSO PLAY AN EARLY ROLE IN SPECIFIC CC ECTODERMAL CELLS, AND A SUBSEQUENT ROLE IN THE EMBRYONIC NERVOUS CC SYSTEM. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE EPIDERMIS AND CENTRAL NERVOUS CC SYSTEM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT MAXIMAL LEVELS IN EARLY EMBRYOS CC (6-12 HRS). FIRST DETECTED IN THE PRECURSOR OF THE TRACHEAL PITS CC AND THE STOMODEAL INVAGINATION AND LATER IN THE PERIPHERAL NERVOUS CC SYSTEM. CC -!- SIMILARITY: BELONGS TO THE POU TRANSCRIPTION FACTOR FAMILY. CC CLASS-3 SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT TO INTERACT WITH I-POU. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS CC IN POSITIONS 9, 52, 102 AND 420. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58435; CAA41341.1; ALT_FRAME. DR EMBL; M81959; AAA28831.1; -. DR EMBL; AE003561; AAF50641.3; -. DR EMBL; X52252; CAA36496.1; -. DR HSSP; P14859; 1OCT. DR TRANSFAC; T01897; -. DR FlyBase; FBgn0003995; vvl. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000327; POU_domain. DR InterPro; IPR007103; POU_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00157; pou; 1. DR PRINTS; PR00028; POUDOMAIN. DR ProDom; PD000010; Homeobox; 1. DR ProDom; PD000583; POU_domain; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00352; POU; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00035; POU_1; 1. DR PROSITE; PS00465; POU_2; 1. KW Homeobox; DNA-binding; Transcription regulation; Activator; KW Nuclear protein. FT DOMAIN 216 286 POU. FT DNA_BIND 302 362 HOMEOBOX. FT DOMAIN 19 22 POLY-GLY. FT DOMAIN 42 198 HIS-RICH. FT DOMAIN 48 54 POLY-ALA. FT DOMAIN 103 111 POLY-ALA. FT DOMAIN 380 404 HIS-RICH. FT CONFLICT 83 102 SWSALHPDPWMQTHHTHHLP -> LMECPPSGSVDANPSYA FT PSA (IN REF. 5). FT CONFLICT 130 140 GMASPHAAWHA -> ACLAPCRLAC (IN REF. 5). FT CONFLICT 147 147 A -> G (IN REF. 5). FT CONFLICT 364 375 PPNTLGGDMMDG -> AKYARRRHDGR (IN REF. 5). SQ SEQUENCE 427 AA; 45927 MW; 161F40CF3DBB8BF7 CRC64; MAATSYMTPP SGDLDMALGG GGYHTSSPRS AADAGEMKYM QHHHHHHAAA AAAAHHQLPS SPSPNGQGNG GGLGLGSGSG LGSWSALHPD PWMQTHHTHH LPAAAAVASA ADTVKQEMSH LSQQTRIQQG MASPHAAWHA PHAGHYAPTG GSPLQYHHAM NGMLHHPAHA VAAAHHQSVA PLHHTLRGES PQLHIHHHMG GGDRDAISGG EEDTPTSDDL EAFAKQFKQR RIKLGFTQAD VGLALGTLYG NVFSQTTICR FEALQLSFKN MCKLKPLLQK WLEEADSTTG SPTSIDKIAA QGRKRKKRTS IEVSVKGALE QHFHKQPKPS AQEITSLADS LQLEKEVVRV WFCNRRQKEK RMTPPNTLGG DMMDGMPPGH MHHGGYHPHH DMHGSPMGTH SHSHSPPMLS PQNMQSSAVA AHQLAAH // ID CF23_DROME STANDARD; PRT; 514 AA. AC Q01522; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chorion transcription factor Cf2, isoform III. GN CF2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93030711; PubMed=1411512; RA Hsu T., Gogos J.A., Kirsh S.A., Kafatos F.C.; RT "Multiple zinc finger forms resulting from developmentally regulated RT alternative splicing of a transcription factor gene."; RL Science 257:1946-1950(1992). CC -!- FUNCTION: TRANSCRIPTIONAL REGULATOR. THE EXACT FUNCTION OF THIS CC ISOFORM IS NOT YET KNOWN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=III; CC IsoId=Q01522-1; Sequence=Displayed; CC Name=I; CC IsoId=P20385-1; Sequence=External; CC Name=II; CC IsoId=P20385-2; Sequence=External; CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: CONTAINS 3 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97196; AAA28394.1; -. DR TRANSFAC; T00121; -. DR FlyBase; FBgn0000286; Cf2. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IDA. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 3. DR SMART; SM00355; ZnF_C2H2; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. KW Nuclear protein; DNA-binding; Zinc-finger; Trans-acting factor; KW Transcription regulation; Alternative splicing; Metal-binding; Repeat. FT ZN_FING 76 97 C2H2-TYPE 1. FT ZN_FING 127 138 C2H2-TYPE 2. FT ZN_FING 366 388 C2H2-TYPE 3. FT DOMAIN 21 28 POLY-PRO. FT DOMAIN 238 252 POLY-GLN. FT DOMAIN 263 270 POLY-GLN. FT DOMAIN 466 477 POLY-SER. SQ SEQUENCE 514 AA; 56270 MW; C7DE6725EAF70B16 CRC64; MIKSTTNPQE QRLPRPEDQS PAPPPPPPSS ATTSTAAPAT PTHQVATVIA NMDTLKTAFL PNLSMDPNVH VSPHYCPMCH QQFERPQHVA DHMQLCHGIT LNAQGAIATL DGGHPQAQQH PKLSHPCFNC DEKFGNAVDL DEHHRLAHQT PAFLSRCLMC SIYGIHSATQ QPNEYKCTQC GSICTTAMLA AGQQGFMEQQ EAAVTPDDQL PAMAPRDMRL TPEEQHHQQQ LQAEHHHQQQ HQQQQQQQQQ QQESLEQQQR EMQEQAQQQQ VHHHQQDQDL AGDQVALKVP PLTVKLNKNA NGGAIVSHPQ VIIKEEPLSL SDSGDVVNSV PVYAIQANPG VPAPASSGVL VGTQTVPADL AHKIRHKCPD CPKTFKTPGT LAMHRKIHTG EAEREAVPLR LLREVLQREG LSDQAHTDAH RREAVHLSVL RQALHAAQRP HCAHDQAASA LGKAGRWPPV TRSCPSRSSS SYSSSKSFWS WCAAAVVRRH GYRSQEAICG GCGIGLGRTA AETG // ID CF2_DROME STANDARD; PRT; 510 AA. AC P20385; Q24263; Q9VR41; DT 01-FEB-1991 (Rel. 17, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chorion transcription factor Cf2, isoforms I and II. GN CF2 OR CG11924. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS I AND II). RC STRAIN=Oregon-R; TISSUE=Embryo, and Ovary; RX MEDLINE=93030711; PubMed=1411512; RA Hsu T., Gogos J.A., Kirsh S.A., Kafatos F.C.; RT "Multiple zinc finger forms resulting from developmentally regulated RT alternative splicing of a transcription factor gene."; RL Science 257:1946-1950(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 248-510 FROM N.A. (ISOFORM II). RC TISSUE=Embryo; RX MEDLINE=91007257; PubMed=2120114; RA Shea M.J., King D.L., Conboy M.J., Mariani B.D., Kafatos F.C.; RT "Proteins that bind to Drosophila chorion cis-regulatory elements: a RT new C2H2 zinc finger protein and a C2C2 steroid receptor-like RT component."; RL Genes Dev. 4:1128-1140(1990). CC -!- FUNCTION: TRANSCRIPTIONAL REGULATOR. ISOFORM II BINDS TO THE CC PROMOTER REGION OF S15 CHORION GENE, WHEREAS ISOFORM II BINDS TO CC CF2 PROMOTER, THUS HAVING A PROBABLE AUTOREGULATORY ROLE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=I; CC IsoId=P20385-1; Sequence=Displayed; CC Name=II; CC IsoId=P20385-2; Sequence=VSP_006824; CC Name=III; CC IsoId=Q01522-1; Sequence=External; CC -!- TISSUE SPECIFICITY: ISOFORM I IS FOUND IN EMBRYOS, PUPAE AND ADULT CC SOMATIC TISSUE; ISOFORM II OCCURS IN EMBRYOS, PUPAE, OVARIES AND CC TO A LESSER EXTENT IN ADULT SOMATIC TISSUE. CC -!- SIMILARITY: CONTAINS 7 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97196; AAA28395.1; -. DR EMBL; M97196; AAA28396.1; -. DR EMBL; AE003575; AAF50966.2; -. DR EMBL; X53380; CAA37460.1; -. DR PIR; B36901; B36901. DR HSSP; P08047; 1SP2. DR TRANSFAC; T00119; -. DR TRANSFAC; T00120; -. DR FlyBase; FBgn0000286; Cf2. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IDA. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR007086; Znf_C2H2_sub. DR Pfam; PF00096; zf-C2H2; 7. DR PRINTS; PR00048; ZINCFINGER. DR ProDom; PD000003; Znf_C2H2; 3. DR SMART; SM00355; ZnF_C2H2; 7. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. KW Nuclear protein; DNA-binding; Zinc-finger; Trans-acting factor; KW Transcription regulation; Alternative splicing; Metal-binding; Repeat. FT ZN_FING 76 97 C2H2-TYPE 1. FT ZN_FING 127 138 C2H2-TYPE 2. FT ZN_FING 366 388 C2H2-TYPE 3. FT ZN_FING 403 423 C2H2-TYPE 4. FT ZN_FING 431 451 C2H2-TYPE 5. FT ZN_FING 459 479 C2H2-TYPE 6. FT ZN_FING 487 508 C2H2-TYPE 7. FT DOMAIN 21 28 POLY-PRO. FT DOMAIN 238 252 POLY-GLN. FT DOMAIN 263 270 POLY-GLN. FT VARSPLIC 430 457 Missing (in isoform II). FT /FTId=VSP_006824. FT CONFLICT 254 254 S -> L (IN REF. 2). SQ SEQUENCE 510 AA; 56724 MW; 4895FB851F4EE0AB CRC64; MIKSTTNPQE QRLPRPEDQS PAPPPPPPSS ATTSTAAPAT PTHQVATVIA NMDTLKTAFL PNLSMDPNVH VSPHYCPMCH QQFERPQHVA DHMQLCHGIT LNAQGAIATL DGGHPQAQQH PKLSHPCFNC DEKFGNAVDL DEHHRLAHQT PAFLSRCLMC SIYGIHSATQ QPNEYKCTQC GSICTTAMLA AGQQGFMEQQ EAAVTPDDQL PAMAPRDMRL TPEEQHHQQQ LQAEHHHQQQ HQQQQQQQQQ QQESLEQQQR EMQEQAQQQQ VHHHQQDQDL AGDQVALKVP PLTVKLNKNA NGGAIVSHPQ VIIKEEPLSL SDSGDVVNSV PVYAIQANPG VPAPASSGVL VGTQTVPADL AHKIRHKCPD CPKTFKTPGT LAMHRKIHTG EADATPKERP YTCSYCGKSF TQSNTLKQHT RIHTGEKPFR CGYCGRAFTV KDYLNKHLTT HTGEKPFHCG YCEKSFSVKD YLTKHIRTHT GEKPYTCPYC DKRFTQRSAL TVHTTKLHPL // ID CG1A_DROME STANDARD; PRT; 995 AA. AC Q9NGC3; Q8MR30; Q95SF3; Q9NKE5; Q9VJV4; Q9VJV5; Q9VJV7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Centaurin gamma 1A protein. GN CENG1A OR BG:DS08220.1 OR CG31811/CG7982/CG16866/CG16867. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RA Hendrick A.G., Harrington L.S.; RT "Identification of novel ARF-GTPase activating protein (GAP)-like RT proteins in the Drosophila genome."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: GTPASE-ACTIVATING PROTEIN FOR THE ADP RIBOSYLATION CC FACTOR FAMILY (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=B; CC IsoId=Q9NGC3-1; Sequence=Displayed; CC Name=A; CC IsoId=Q9NGC3-2; Sequence=VSP_000312, VSP_000313; CC Name=C; CC IsoId=Q9NGC3-3; Sequence=VSP_000314; CC -!- SIMILARITY: CONTAINS 1 ANK REPEAT. CC -!- SIMILARITY: CONTAINS 1 ARF-GAP DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC DUPLICATION OF 79 RESIDUES INSERTED IN POSITION 130 OF ISOFORM A. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF254741; AAF66064.1; ALT_SEQ. DR EMBL; AE003408; AAF44832.1; ALT_SEQ. DR EMBL; AE003641; AAF53343.2; -. DR EMBL; AE003641; AAF53349.2; -. DR EMBL; AE003641; AAF53350.2; -. DR EMBL; AY122158; AAM52670.1; -. DR EMBL; AY060821; AAL28369.1; ALT_SEQ. DR FlyBase; FBgn0028509; cenG1A. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0007264; P:small GTPase mediated signal transduction; NAS. DR InterPro; IPR002110; ANK. DR InterPro; IPR003579; GTPase_Rab. DR InterPro; IPR003577; GTPase_Ras. DR InterPro; IPR003578; GTPase_Rho. DR InterPro; IPR001164; hRIP_like. DR InterPro; IPR001849; PH. DR InterPro; IPR001806; Ras_trnsfrmng. DR Pfam; PF00023; ank; 1. DR Pfam; PF01412; ArfGap; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00405; REVINTRACTNG. DR SMART; SM00105; ArfGap; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS50115; ARFGAP; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. KW GTPase activation; ANK repeat; Zinc-finger; GTP-binding; KW Alternative splicing. FT DOMAIN 453 682 PH. FT DOMAIN 679 822 ARF-GAP. FT ZN_FING 717 740 C4-TYPE. FT REPEAT 866 898 ANK. FT VARSPLIC 1 68 Missing (in isoform A). FT /FTId=VSP_000312. FT VARSPLIC 69 125 AHPPQPLISNSLAIRQEIQRFESVHPSIYAIYELIDLLPMA FT DAQIAQSIRDHVVCIE -> MLAVKNFFLPERAKAPETPQR FT FSRMPEAFLRSIRRRSLRVKRAKSLVVPDRSEKRKS (in FT isoform A). FT /FTId=VSP_000313. FT VARSPLIC 1 232 Missing (in isoform C). FT /FTId=VSP_000314. SQ SEQUENCE 995 AA; 108043 MW; E2376662937C328F CRC64; MSNYHPHSHP HALSHPHPQQ VHNQLQNPHQ NQLPPPQRHN HAAPTAAASA SGAPSSSASA SASASILVAH PPQPLISNSL AIRQEIQRFE SVHPSIYAIY ELIDLLPMAD AQIAQSIRDH VVCIEDSFVN SQEWTISRSV PDLRLGIVGS LNSGKSALVH RYLTGSYMQE ESPEGGRFKK EVFIDGQSYL LLIRDEGGAP EMQFAGWVDA VIFVFSLENE GSFNTVYNYY TKMAHFRNGQ EIPMILVGTQ DAISERNPRV IDDTRARKLA SDLKRCSYYE TCATYGLNVE RVFQDACQKI LSQRLPLPPQ VQPARPTTPQ GNRLGLAPYQ APTNGQRGQQ QLPLRMSADF AQAEQKLWSL QAASSSTINE NNNITKYNPG AANSLQGDCS QVQLRDPRDL APPPGKELPT PTSTPTTSRK SRRRSNLFIP SSSKKADKEK EPKSSELGSG RSIPIKQGYL YKRSSKSLNK EWKKKYVTLC DDGRLTYHPS LHDYMDDVHG KEIPLQYVTV KVPGQKPRGS KSIITNSALT SSLMANGQRA QNTLSDGIGC LTLAKDNQRK LSEKLSLLGA GSIAAGAGGE PLKSNSSQQT SGDEGIAMSN SNSQTFIAGE VANAGNKLEA QTPNVKKRHR RMKSSSVKAN EADDNDGYEF YIVSLDSKQW HFEAANSEER DEWVAAVEQE IFKSLQSIES SKTKQATSTD LAAMLAIRQR VPGNGFCVDC GAPNPEWASL NLGVLMCIEC SGVHRNLGSH ISKVRSLGLD DWPSPHLSVM LAIGNSLANS VWESNTRQRV KPTSQASRED KERWVRSKYE AKEFLTPLGN GSSAHPSPSP GQQLIEAVIR ADIKSIVSIL ANCPSEVTNA NVSARDVRTP LLLACAIGNL AIAQLLIWNG ANIKHTDHEG RTCLAYARAA QSLATAKSIK AAAAAQAGTT IPAPAPPTNG GIPAPQYNVE DTTALVELLE GLGCPEAAPL TASGTLPRRR DTLGTPYEKS VSGVI // ID CG1C_DROME STANDARD; PRT; 267 AA. AC P25008; Q9VFF1; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE G1/S-specific cyclin C. GN CYCC OR CLND OR CG7281. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92084091; PubMed=1836192; RA Lahue E.E., Smith A.V., Orr-Weaver T.L.; RT "A novel cyclin gene from Drosophila complements CLN function in RT yeast."; RL Genes Dev. 5:2166-2175(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92005672; PubMed=1833067; RA Leopold P., O'Farrell P.H.; RT "An evolutionarily conserved cyclin homolog from Drosophila rescues RT yeast deficient in G1 cyclins."; RL Cell 66:1207-1216(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ESSENTIAL FOR THE CONTROL OF THE CELL CYCLE AT THE G1/S CC (START) TRANSITION. INTERACTS WITH THE CDC2 PROTEIN KINASE TO CC FORM MPF. CC -!- SIMILARITY: BELONGS TO THE CYCLIN FAMILY. CYCLIN C SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62948; CAA44720.1; -. DR EMBL; M74906; -; NOT_ANNOTATED_CDS. DR EMBL; AE003706; AAF55109.1; -. DR PIR; A40269; A40269. DR FlyBase; FBgn0004597; CycC. DR GO; GO:0016538; F:cyclin-dependent protein kinase, intrinsic ...; IDA. DR InterPro; IPR006670; Cyclin. DR InterPro; IPR004367; Cyclin_Cterm. DR InterPro; IPR006671; Cyclin_N. DR Pfam; PF00134; cyclin; 1. DR Pfam; PF02984; cyclin_C; 1. DR SMART; SM00385; CYCLIN; 2. DR PROSITE; PS00292; CYCLINS; FALSE_NEG. KW Cyclin; Cell cycle; Cell division. SQ SEQUENCE 267 AA; 31292 MW; DA73CB7EA89149FE CRC64; MAGNFWQSSH SQQWILDKPD LLRERQHDLL ALNEDEYQKV FIFFANVIQV LGEQLKLRQQ VIATATVYFK RFYARNSLKN IDPLLLAPTC ILLASKVEEF GVISNSRLIS ICQSAIKTKF SYAYAQEFPY RTNHILECEF YLLENLDCCL IVYQPYRPLL QLVQDMGQED QLLTLSWRIV NDSLRTDVCL LYPPYQIAIA CLQIACVILQ KDATKQWFAE LNVDLDKVQE IVRAIVNLYE LWKDWKEKDE IQMLLSKIPK PKPPPQR // ID CG1E_DROME STANDARD; PRT; 709 AA. AC P54733; Q24479; Q95RP5; Q9V3B3; Q9V456; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE G1/S-specific cyclin E (DmCycE). GN CYCE OR CG3938. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS I AND II), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=94244469; PubMed=8187637; RA Richardson H.E., O'Keefe L.V., Reed S.I., Saint R.; RT "A Drosophila G1-specific cyclin E homolog exhibits different modes RT of expression during embryogenesis."; RL Development 119:673-690(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS I AND II). RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM II). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ESSENTIAL FOR THE CONTROL OF THE CELL CYCLE AT THE G1/S CC (START) TRANSITION. CC -!- SUBUNIT: INTERACTS WITH A MEMBER OF THE CDK2/CDK PROTEIN KINASES CC TO FORM A SERINE/THREONINE KINASE HOLOENZYME COMPLEX. THE CYCLIN CC SUBUNIT IMPARTS SUBSTRATE SPECIFICITY TO THE COMPLEX. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=II; Synonyms=A, C; CC IsoId=P54733-1; Sequence=Displayed; CC Name=I; Synonyms=B; CC IsoId=P54733-2; Sequence=VSP_001254, VSP_001255; CC -!- TISSUE SPECIFICITY: ISOFORM II IS UBIQUITOUS IN EARLY EMBRYOS AND, CC PRIOR TO MITOSIS 14, IS RAPIDLY DEGRADED IN ALL CELLS EXCEPT THE CC POLE (GERM) CELLS. EXPRESSED DURING G1 PHASE IN PROLIFERATING CC PERIPHERAL NERVOUS SYSTEM CELLS. CONSTITUTIVE EXPRESSION IN CC EMBRYONIC CYCLES LACKING A G1 PHASE. CC -!- DEVELOPMENTAL STAGE: ISOFORM II IS EXPRESSED MATERNALLY AND CC ISOFORM I ZYGOTICALLY IN LARVAE. CC -!- SIMILARITY: BELONGS TO THE CYCLIN FAMILY. CYCLIN E SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75026; CAA52934.1; -. DR EMBL; X75027; CAA52935.1; -. DR EMBL; AE003414; AAF44960.1; -. DR EMBL; AE003414; AAF44961.1; -. DR EMBL; AE003648; AAF53477.1; -. DR EMBL; AE003648; AAF53479.1; -. DR EMBL; AY069507; AAL39652.1; -. DR EMBL; AY061233; AAL28781.1; -. DR HSSP; P30274; 1VIN. DR FlyBase; FBgn0010382; CycE. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0016538; F:cyclin-dependent protein kinase, intrinsic ...; IDA. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA. DR GO; GO:0007422; P:peripheral nervous system development; IEP. DR GO; GO:0007277; P:pole cell development; IEP. DR InterPro; IPR006670; Cyclin. DR InterPro; IPR004367; Cyclin_Cterm. DR InterPro; IPR006671; Cyclin_N. DR Pfam; PF00134; cyclin; 1. DR Pfam; PF02984; cyclin_C; 1. DR SMART; SM00385; CYCLIN; 1. DR PROSITE; PS00292; CYCLINS; 1. KW Cyclin; Cell cycle; Cell division; Alternative splicing; KW Phosphorylation; Nuclear protein. FT MOD_RES 651 651 PHOSPHORYLATION (BY SIMILARITY). FT VARSPLIC 1 107 Missing (in isoform I). FT /FTId=VSP_001254. FT VARSPLIC 108 119 KRKRRLSSDSNE -> MKLEQKRKFIEM (in isoform FT I). FT /FTId=VSP_001255. FT CONFLICT 633 633 A -> S (IN REF. 1). FT CONFLICT 644 645 RA -> P (IN REF. 1). FT CONFLICT 691 691 G -> V (IN REF. 1). SQ SEQUENCE 709 AA; 77220 MW; F4E6CE53C6E30170 CRC64; MGLNAKSVCS TSSTEPNGSI VTTAPSNGEV SSSIVVVVSS SSISSSSDSP IAILPHPDPI PSTSFSSASQ RSEEELPGTS AASRTDEMCS CDSQNLAAST AATSNGNKRK RRLSSDSNED PELGFEPPSA KRQQRLPALY GSEQGNLSSV ASSVYTSPVV SVDGQSTQEL LSIRSSPAED LSEAPHSPLP DSPDSPPSPD RGSKQTPVVV RYAAEQVVTS TVVTQKTEDD DLLDDSCEDY SYDEDDEDDV EEEDDDVEIY SSTISPASSG CSQQQAVNGE RTPGLPKHQE QIHHPVSDLM INMRTPMSPA VENGLRQCPL PALAWANAAD VWRLMCHRDE QDSRLRSISM LEQHPGLQPR MRAILLDWLI EVCEVYKLHR ETFYLAVDYL DRYLHVAHKV QKTHLQLIGI TCLFVAAKVE EIYPPKIGEF AYVTDGACTE RDILNHEKIL LQALDWDISP ITITGWLGVY MQLNVNNRTP ASFSQIGRQK SAEADDAFIY PQFSGFEFVQ TSQLLDLCTL DVGMANYSYS VLAAAAISHT FSREMALRCS GLDWQVIQPC ARWMEPFFRV ISQKAPYLQL NEQNEQVSNK FGLGLICPNI VTDDSHIIQT HTTTMDMYDE VLMAQDAAHA MRARIQASPA TALRAPESLL TPPASSHKPD EYLGDEGDET GARSGISSTT TCCNTAASNK GGKSSSNNSV TSCSSRSNP // ID CG2A_DROME STANDARD; PRT; 491 AA. AC P14785; Q8IGR7; Q9VTP6; Q9VTP7; DT 01-APR-1990 (Rel. 14, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE G2/mitotic-specific cyclin A. GN CYCA OR CG5940. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Canton-S; RX MEDLINE=93077051; PubMed=1332913; RA Takahisa M., Togashi S., Ueda R., Mikuni M., Tsurumura S., Kondo K., RA Miyake T.; RT "Structure of the Drosophila melanogaster gene encoding cyclin A."; RL Gene 121:343-346(1992). RN [2] RP SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=89168447; PubMed=2564316; RA Lehner C.F., O'Farrell P.H.; RT "Expression and function of Drosophila cyclin A during embryonic cell RT cycle progression."; RL Cell 56:957-968(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 235-247 AND 288-300 FROM N.A. RX MEDLINE=89159430; PubMed=2564167; RA Whitfield W.G.F., Gonzalez C., Sanchez-Herrero E., Glover D.M.; RT "Transcripts of one of two Drosophila cyclin genes become localized RT in pole cells during embryogenesis."; RL Nature 338:337-340(1989). CC -!- FUNCTION: ESSENTIAL FOR THE CONTROL OF THE CELL CYCLE AT THE G2/M CC (MITOSIS) TRANSITION. INTERACTS WITH THE CDC2 AND CDK2 PROTEIN CC KINASES TO FORM MPF. G2/M CYCLINS ACCUMULATE STEADILY DURING G2 CC AND ARE ABRUPTLY DESTROYED AT MITOSIS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=Long; CC IsoId=P14785-1; Sequence=Displayed; CC Name=B; Synonyms=Short; CC IsoId=P14785-2; Sequence=VSP_001249; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE CYCLIN FAMILY. CYCLIN AB SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D10857; BAA01628.1; -. DR EMBL; D10856; BAA01628.1; JOINED. DR EMBL; D10858; BAA01629.1; -. DR EMBL; M24841; AAA28435.1; -. DR EMBL; AE003543; AAF49999.2; -. DR EMBL; AE003543; AAF50000.3; -. DR EMBL; AY058712; AAL13941.1; -. DR EMBL; BT001635; AAN71390.1; -. DR PIR; JC1390; JC1390. DR HSSP; P20248; 1FIN. DR FlyBase; FBgn0000404; CycA. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0016538; F:cyclin-dependent protein kinase, intrinsic ...; NAS. DR GO; GO:0016359; P:mitotic sister chromatid separation; IMP. DR GO; GO:0007088; P:regulation of mitosis; IEP. DR InterPro; IPR006670; Cyclin. DR InterPro; IPR004367; Cyclin_Cterm. DR InterPro; IPR006671; Cyclin_N. DR Pfam; PF00134; cyclin; 1. DR Pfam; PF02984; cyclin_C; 1. DR SMART; SM00385; CYCLIN; 2. DR PROSITE; PS00292; CYCLINS; 1. KW Cyclin; Cell cycle; Cell division; Mitosis; Alternative splicing. FT VARSPLIC 1 146 Missing (in isoform B). FT /FTId=VSP_001249. FT CONFLICT 147 147 M -> I (IN REF. 1; BAA01629). FT CONFLICT 179 179 V -> A (IN REF. 1). FT CONFLICT 200 200 V -> M (IN REF. 1; BAA01629). FT CONFLICT 220 220 P -> A (IN REF. 5; AAN71390). FT CONFLICT 223 223 L -> R (IN REF. 2). FT CONFLICT 474 474 H -> Q (IN REF. 1; BAA01629). SQ SEQUENCE 491 AA; 56152 MW; 6B700EB48A18ED99 CRC64; MASFQIHQDM SNKENPGIKI PAGVKNTKQP LAVIGGKAEK NALAPRANFA VLNGNNNVPR PAGKVQVFRD VRNLNVDENV EYGAKKSNVV PVVEQFKTFS VYEDNNDTQV APSGKSLASL VDKENHDVKF GAGQKELVDY DLDSTPMSVT DVQSPMSVDR SILGVIQSSD ISVGTETGVS PTGRVKELPP RNDRQRFLEV VQYQMDILEY FRESEKKHRP KPLYMRRQKD ISHNMRSILI DWLVEVSEEY KLDTETLYLS VFYLDRFLSQ MAVVRSKLQL VGTAAMYIAA KYEEIYPPEV GEFVFLTDDS YTKAQVLRME QVILKILSFD LCTPTAYVFI NTYAVLCDMP EKLKYMTLYI SELSLMEGET YLQYLPSLMS SASVALARHI LGMEMWTPRL EEITTYKLED LKTVVLHLCH THKTAKELNT QAMREKYNRD TYKKVAMMES VEMSKDDFDQ LCEAYNCKQK EDEHQQPDIN TKSNVNLFYK F // ID CG2B_DROME STANDARD; PRT; 530 AA. AC P20439; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE G2/mitotic-specific cyclin B. GN CYCB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90242399; PubMed=2139805; RA Lehner C.F., O'Farrell P.H.; RT "The roles of Drosophila cyclins A and B in mitotic control."; RL Cell 61:535-547(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90316115; PubMed=2142452; RA Whitfield W.G.F., Gonzalez C., Maldonado-Codina G., Glover D.M.; RT "The A- and B-type cyclins of Drosophila are accumulated and RT destroyed in temporally distinct events that define separable phases RT of the G2-M transition."; RL EMBO J. 9:2563-2572(1990). RN [3] RP SEQUENCE OF 289-301 AND 343-355 FROM N.A. RX MEDLINE=89159430; PubMed=2564167; RA Whitfield W.G.F., Gonzalez C., Sanchez-Herrero E., Glover D.M.; RT "Transcripts of one of two Drosophila cyclin genes become localized RT in pole cells during embryogenesis."; RL Nature 338:337-340(1989). CC -!- FUNCTION: ESSENTIAL FOR THE CONTROL OF THE CELL CYCLE AT THE G2/M CC (MITOSIS) TRANSITION. CC -!- SUBUNIT: INTERACTS WITH THE CDC2 PROTEIN KINASE TO FORM A CC SERINE/THREONINE KINASE HOLOENZYME COMPLEX ALSO KNOWN AS CC MATURATION PROMOTING FACTOR (MPF). THE CYCLIN SUBUNIT IMPARTS CC SUBSTRATE SPECIFICITY TO THE COMPLEX. CC -!- DEVELOPMENTAL STAGE: ACCUMULATES STEADILY DURING G2 AND IS CC ABRUPTLY DESTROYED AT MITOSIS. CC -!- SIMILARITY: BELONGS TO THE CYCLIN FAMILY. CYCLIN AB SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33192; AAA28436.1; -. DR EMBL; X55542; CAA39148.1; -. DR PIR; A35144; A35144. DR HSSP; P30274; 1VIN. DR FlyBase; FBgn0000405; CycB. DR GO; GO:0016538; F:cyclin-dependent protein kinase, intrinsic ...; IDA. DR GO; GO:0016288; P:cytokinesis; IMP. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; NAS. DR GO; GO:0000092; P:mitotic anaphase B; IMP. DR GO; GO:0007079; P:mitotic chromosome movement; IMP. DR InterPro; IPR006670; Cyclin. DR InterPro; IPR004367; Cyclin_Cterm. DR InterPro; IPR006671; Cyclin_N. DR Pfam; PF00134; cyclin; 1. DR Pfam; PF02984; cyclin_C; 1. DR SMART; SM00385; CYCLIN; 2. DR PROSITE; PS00292; CYCLINS; 1. KW Cyclin; Cell cycle; Cell division; Mitosis. FT CONFLICT 162 162 G -> R (IN REF. 2). FT CONFLICT 383 383 D -> N (IN REF. 2). FT CONFLICT 515 515 L -> P (IN REF. 2). SQ SEQUENCE 530 AA; 59156 MW; 34911BE0CEDCCE90 CRC64; MVGTTLKMRG DENASENFKQ VQLKKLTVPS MEATTKRAAL GDLQNRGISR PIAAKDAAQK DSKDLKLTDA LRNAKARVDS HWKKQPLGST NGNGNGAVPP KVNEGGVSAF LRSNSVRNRV PTKTTVEPTK VTVKSSSSEN VNEPTLKRED SNLSKKSLTK LGAALAKPVM GVSGIRREPV AVSRKEAETK KELPETKKDS LEVKKDATRM PLIRGNSAVT TTTSTMPTTM SLSSKRLAGI EDIDANDKEN LVLVSEYVND IYDYLYQVEL EQPIHKDHLA GQKEVSHKMR AVLIDWINEV HLQFHLAAET FQLAVAIIDR YLQVVKDTKR TYLQLVGVTA LFIATKYEEL FPPAIGDFVF ITDDTYTARQ IRQMELQIFK AIDCNLSRPL PIHFLRRYSK AAGAEDEHHT MSKYFIELAS VDYEMATYRP SEIAAASLFL SLHLLNGNHR AGTGFNDRHW TPTLTFYSRY SAAHLRPITR LIAKLARDAP QAKLKAIYNK YQGSKFQKIA LRTELTGALM DSIVGQSQRK // ID CH15_DROME STANDARD; PRT; 115 AA. AC P07185; Q9VSP2; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chorion protein S15. GN CP15 OR S15 OR CG6519. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85229804; PubMed=2988878; RA Wong Y.-C., Pustell J., Spoerel N., Kafatos F.C.; RT "Coding and potential regulatory sequences of a cluster of chorion RT genes in Drosophila melanogaster."; RL Chromosoma 92:124-135(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85229805; PubMed=3924529; RA Levine J., Spradling A.; RT "DNA sequence of a 3.8 kilobase pair region controlling Drosophila RT chorion gene amplification."; RL Chromosoma 92:136-142(1985). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02497; CAA26329.1; -. DR EMBL; X06257; CAA29603.1; -. DR EMBL; AE003554; AAF50374.1; -. DR FlyBase; FBgn0000355; Cp15. DR InterPro; IPR005649; Chorion_2. DR Pfam; PF03964; Chorion_2; 1. KW Chorion. SQ SEQUENCE 115 AA; 11981 MW; 4E386EB446DE30A1 CRC64; MKYLIVCVTL ALFAYINASP AYGNRGGYGG GYGGGYGPVQ RVVYEEVPAY GPSRGYNSYP RSLRSEGNGG SAAAAAAASA AAVNPGTYKQ YAIPSYELDG ARGYEIGHGY GQRAY // ID CH16_DROME STANDARD; PRT; 138 AA. AC P22977; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 01-AUG-1991 (Rel. 19, Last annotation update) DE Chorion protein S16. GN CP16 OR S16. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90040741; PubMed=2509714; RA Fenerjian M.G., Martinez-Cruzado J.C., Swimmer C., King D., RA Kafatos F.C.; RT "Evolution of the autosomal chorion cluster in Drosophila. II. RT Chorion gene expression and sequence comparisons of the s16 and s19 RT genes in evolutionarily distant species."; RL J. Mol. Evol. 29:108-125(1989). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16715; CAA34686.1; -. DR PIR; A32998; A32998. DR FlyBase; FBgn0000356; Cp16. DR InterPro; IPR008450; Chorion_S16. DR Pfam; PF05836; Chorion_S16; 1. KW Chorion. SQ SEQUENCE 138 AA; 14321 MW; 7B5B26BE208BDADD CRC64; MSATLRLLCL MACCVALAVA NRPHYGGSGY GASYGDVVKA AETAEAQASA LTNAAGAAAS AAKLDGADWY ALNRYGWEQG RPLLAKPYGP LDPLYAAALP PRSFVAEVDP VFKKSQYGGS YGENAYLKTD AKLGVVAI // ID CH18_DROME STANDARD; PRT; 172 AA. AC P07184; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Chorion protein S18. GN CP18 OR S18. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85229804; PubMed=2988878; RA Wong Y.-C., Pustell J., Spoerel N., Kafatos F.C.; RT "Coding and potential regulatory sequences of a cluster of chorion RT genes in Drosophila melanogaster."; RL Chromosoma 92:124-135(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85229805; PubMed=3924529; RA Levine J., Spradling A.; RT "DNA sequence of a 3.8 kilobase pair region controlling Drosophila RT chorion gene amplification."; RL Chromosoma 92:136-142(1985). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02497; CAA26328.1; -. DR EMBL; X06257; CAA29602.1; -. DR FlyBase; FBgn0000357; Cp18. DR InterPro; IPR005649; Chorion_2. DR Pfam; PF03964; Chorion_2; 1. KW Chorion. SQ SEQUENCE 172 AA; 17269 MW; 928405D34360D0CE CRC64; MMKFMCICLC AISAVSANSY GRPRGGYGGA PVGGYAYQVQ PALTVKAIVP SYGGGYGGNH GGYGGAYESV PVPVSSVYSG ANVGSQYSGS GYGGAPPVDA QAIALAKLAL AAPSAGAPLV WKEAPRYAQP VYPPTSYVNQ EYGHSEKVKG GSAAAAASSV AAGKKGYKRP SY // ID CH19_DROME STANDARD; PRT; 173 AA. AC P07186; Q9VSP3; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chorion protein S19. GN CP19 OR S19 OR CG6524. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85229804; PubMed=2988878; RA Wong Y.-C., Pustell J., Spoerel N., Kafatos F.C.; RT "Coding and potential regulatory sequences of a cluster of chorion RT genes in Drosophila melanogaster."; RL Chromosoma 92:124-135(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02497; CAA26330.1; -. DR EMBL; AE003554; AAF50373.1; -. DR FlyBase; FBgn0000358; Cp19. DR InterPro; IPR005649; Chorion_2. DR Pfam; PF03964; Chorion_2; 1. KW Chorion. SQ SEQUENCE 173 AA; 18524 MW; 209D7BDCBE27569A CRC64; MNKFATLAVI FCACIVGSCY ANYGGQQSYG QRSYGQDSSA ASAASSAAAA GAEGQQRYER PVEIIAGGYR GSYAPEILRP IQVSGGYGGE RRGYNGGNYR RAGYGPRWTV QPAGATLLYP GQNNYKAYVS PPEYSKVILP IRPAAPVAKL FVPENQYGNQ YVSQYSAPRS SGY // ID CH36_DROME STANDARD; PRT; 286 AA. AC P07182; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 01-NOV-1990 (Rel. 16, Last annotation update) DE Chorion protein S36. GN CP36 OR S36. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87246506; PubMed=3036489; RA Spradling A.C., de Cicco D.V., Wakimoto B.T., Levine J.F., RA Kalfayan L.J., Cooley L.; RT "Amplification of the X-linked Drosophila chorion gene cluster RT requires a region upstream from the s38 chorion gene."; RL EMBO J. 6:1045-1053(1987). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05245; CAA28870.1; -. DR PIR; S07193; S07193. DR FlyBase; FBgn0000359; Cp36. DR GO; GO:0005213; F:structural constituent of chorion (sensu In...; NAS. DR InterPro; IPR008449; Chorion_3. DR Pfam; PF05387; Chorion_3; 1. KW Chorion. SQ SEQUENCE 286 AA; 30080 MW; 29B7CC12E11F1833 CRC64; MQLGLWFGIL AIAAAPLVSA NYGPAGGHGH GHGHGHGQYL SGPNAGLEEY VNVASGGNQQ AANQIASQAE IQPTPEEARR LGRVQAQLQA LNADPNYQKL KNSEDIAESL AETNLASNIR QGKIKVVSPQ FVDQHLFRSL LVPSGHNNHQ VIATQPLPPI IVHQPGAPPA HVNSGPPTVV RGNPVIYKIK PSVIYQQEVI NKVPTPLSLN PVYVKVYKPG KKIEAPLAPV VAPVYSQPRE YSQPQGYGSA GAASSAAGAA SSADGNAYGN EAPLYNSPAP YGQPNY // ID CH38_DROME STANDARD; PRT; 306 AA. AC P07183; Q9W3E5; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chorion protein S38. GN CP38 OR S38 OR CG1121. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87246506; PubMed=3036489; RA Spradling A.C., de Cicco D.V., Wakimoto B.T., Levine J.F., RA Kalfayan L.J., Cooley L.; RT "Amplification of the X-linked Drosophila chorion gene cluster RT requires a region upstream from the s38 chorion gene."; RL EMBO J. 6:1045-1053(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05245; CAA28871.1; -. DR EMBL; AE003444; AAF46383.1; -. DR PIR; S08607; S08607. DR FlyBase; FBgn0000360; Cp38. DR InterPro; IPR008449; Chorion_3. DR Pfam; PF05387; Chorion_3; 1. KW Chorion. SQ SEQUENCE 306 AA; 30448 MW; 2F51C96F9F82DF83 CRC64; MTRSTYIWAL AACLIACASA NYGSSQGYGP ESGSGASDGG ADAASAAAAA AGGAGGAGGE YGGANAGAGA LESGADAAGV AQAGQSSYGS DQNIPYKPVN TKGNTLTSSI TYPQNKGEIL IHRPAPIIVK RPPTKVLVNH PPLVVKPAPV VLHKPPAIVL RKVYVKHHPR RVKVEPVFVN VVKPPAEKYF VNENKQGYGQ GSQSHGHGHG HGGHGHGHSG HGHGGHGAGP HGPGPHDGGR ALPAYASGAD SAAASAGYQL LQSGNQGLSA LANIAGEREG PYGPAPSHQH YSAGPAGHGG YAAPAY // ID CH60_DROME STANDARD; PRT; 573 AA. AC O02649; P35380; Q95026; Q9VZ31; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60 kDa heat shock protein, mitochondrial precursor (Hsp60) (60 kDa DE chaperonin) (CPN60) (Heat shock protein 60) (HSP-60) (Mitochondrial DE matrix protein P1). GN HSP60 OR MMP-P1 OR CG12101. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Kozlova T., Reynaud E., Perezgasga L., Zurita M.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 318-573 FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [4] RP SEQUENCE OF 58-68. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- FUNCTION: PREVENTS MISFOLDING AND PROMOTES THE REFOLDING AND CC PROPER ASSEMBLY OF UNFOLDED POLYPEPTIDES GENERATED UNDER STRESS CC CONDITIONS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CHAPERONIN (HSP60) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99341; CAA67720.1; -. DR EMBL; AE003485; AAF47999.1; -. DR EMBL; Y09066; CAA70287.1; -. DR HSSP; P06139; 1GRL. DR FlyBase; FBgn0015245; Hsp60. DR GO; GO:0005739; C:mitochondrion; IDA. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR008950; GroEL-ATPase. DR Pfam; PF00118; cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR PRINTS; PR00304; TCOMPLEXTCP1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. KW Chaperone; ATP-binding; Mitochondrion; Transit peptide. FT TRANSIT 1 57 MITOCHONDRION. FT CHAIN 58 573 60 KDA HEAT SHOCK PROTEIN. FT CONFLICT 261 262 NA -> KS (IN REF. 1). FT CONFLICT 318 321 GIVF -> ARVG (IN REF. 3). FT CONFLICT 371 373 KDQ -> RTK (IN REF. 1). FT CONFLICT 414 414 K -> E (IN REF. 1). FT CONFLICT 439 443 ALLRC -> RLVRL (IN REF. 1). FT CONFLICT 468 468 L -> S (IN REF. 1). FT CONFLICT 492 492 N -> T (IN REF. 3). SQ SEQUENCE 573 AA; 60809 MW; 7A3792C1D2F3BE4C CRC64; MFRLPVSLAR SSISRQLAMR GYAKDVRFGP EVRAMMLQGV DVLADAVAVT MGPKGRNVII EQSWGSPKIT KDGVTVAKSI ELKDKFQNIG AKLVQDVANN TNEEAGDGTT TATVLARAIA KEGFEKISKG ANPVEIRRGV MLAVETVKDN LKTMSRPVST PEEIAQVATI SANGDQAIGN LISEAMKKVG RDGVITVKDG KTLTDELEVI EGMKFDRGYI SPYFINSSKG AKVEFQDALL LLSEKKISSV QSIIPALELA NAQRKPLVII AEDIDGEALS TLVVNRLKIG LQVAAVKAPG FGDNRKSTLT DMAIASGGIV FGDDADLVKL EDVKVSDLGQ VGEVVITKDD TLLLKGKGKK DDVLRRANQI KDQIEDTTSE YEKEKLQERL ARLASGVALL RVGGSSEVEV NEKKDRVHDA LNATRAAVEE GIVPGGGTAL LRCIEKLEGV ETTNEDQKLG VEIVRRALRM PCMTIAKNAG VDGAMVVAKV ENQAGDYGYD ALKGEYGNLI EKGIIDPTKV VRTAITDASG VASLLTTAEA VVTEIPKEDG APAMPGMGGM GGMGGMGGMG GMM // ID CH6B_DROME STANDARD; PRT; 648 AA. AC Q9VPS5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable 60 kDa heat shock protein homolog 1, mitochondrial precursor DE (Hsp60) (60 kDa chaperonin) (CPN60) (Heat shock protein 60) (HSP-60). GN HSP60B OR CG2830. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PREVENTS MISFOLDING AND PROMOTES THE REFOLDING AND CC PROPER ASSEMBLY OF UNFOLDED POLYPEPTIDES GENERATED UNDER STRESS CC CONDITIONS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CHAPERONIN (HSP60) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003588; AAF51467.1; -. DR HSSP; P06139; 1GRL. DR FlyBase; FBgn0011244; Hsp60B. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR008950; GroEL-ATPase. DR Pfam; PF00118; cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR PRINTS; PR00304; TCOMPLEXTCP1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. KW Hypothetical protein; Chaperone; ATP-binding; Mitochondrion; KW Transit peptide. FT TRANSIT 1 55 MITOCHONDRION (BY SIMILARITY). FT CHAIN 56 648 PROBABLE 60 KDA HEAT SHOCK PROTEIN FT HOMOLOG 1. SQ SEQUENCE 648 AA; 68636 MW; E45D44A166C78455 CRC64; MFRSCVPKAI TSSRCFARMY SKDVRFGSGV RAMMIRGVDI LADAVAVTMG PKGRSVIVER PWTSPKITKD GFTVARSIAL KDQHMNLGAK LVQDVADNTN ESAGDGTTTA TVLARAIAKE GFNQITMGAN PVEIRRGVML AVDVVKDKLK EMSKAVETRE EIQQVATLSA NGDTEIGRLI GEATDKVGPR GTITVKDGKR LKDELNIIQG LRFDNGYVSP FFVNSSKGSK VEFANALVMI SLKKITGLSQ IVKGLEQSLR QRRPLIIIAE DISGEALNAL VLNKLRLGLQ VCAVKSPSYG HHRKELIGDI SAATGATIFG DDINYSKMEE AKLEDLGQVG EAVISKDSTM LLQGKPKTGL LEMRIQQIQD ELAEKQIKPE QRDRLRQRLS ALTKGVAVLH IGGGSEVEVN EKKDRVVDAL NATRAAIEEG IVPGGGTAFL RCIPYLQELK TESADLQKGV DIVCNALRMP CQTIAQNAGV DGPMVVAKVL NGSEDYGYDA MGDEYCRLVE KGIIDPTKVL RTAITDAAGV ASLLSTTEVV ITDSRNDDLL SKLSGAGGGM DDGLDMNMGG LEELAALSGL GGMGGMGGMG GMGGMGGMGG GFGGMGAGGG MSASASNDGP TAEEMNEMVK AIPGMEQVEV RDIDSGMM // ID CHAO_DROME STANDARD; PRT; 1315 AA. AC P12024; Q9VA01; DT 01-OCT-1989 (Rel. 12, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chaoptin precursor (Photoreceptor cell-specific membrane protein). GN CHP OR CHT OR CG1744. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=88135762; PubMed=3124963; RA Reinke R., Krantz D.E., Yen D., Zipursky S.L.; RT "Chaoptin, a cell surface glycoprotein required for Drosophila RT photoreceptor cell morphogenesis, contains a repeat motif found in RT yeast and human."; RL Cell 52:291-301(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 30-50 FROM N.A. RC TISSUE=Head; RX MEDLINE=85166231; PubMed=3920657; RA Zipursky S.L., Venkatesh T.R., Benzer S.; RT "From monoclonal antibody to gene for a neuron-specific glycoprotein RT in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 82:1855-1859(1985). RN [4] RP SEQUENCE OF 30-50, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=84106810; PubMed=6420071; RA Zipursky S.L., Venkatesh T.R., Teplow D.B., Benzer S.; RT "Neuronal development in the Drosophila retina: monoclonal antibodies RT as molecular probes."; RL Cell 36:15-26(1984). CC -!- FUNCTION: REQUIRED FOR PHOTORECEPTOR CELL MORPHOGENESIS. MEDIATES CC HOMOPHILIC CELLULAR ADHESION. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR SURFACE OF R-CELL PLASMA CC MEMBRANE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN PHOTORECEPTOR CELLS AND THEIR CC AXONS IN THE ADULT RETINA, THE OCELLUS AND LARVAL PHOTORECEPTOR CC ORGAN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED 24 HOURS AFTER INITIATION OF CC PHOTORECEPTOR CELL DIFFERENTIATION, PERSISTS THROUGH DEVELOPMENT CC TO ADULTHOOD. CC -!- SIMILARITY: BELONGS TO THE CHAOPTIN FAMILY. CC -!- SIMILARITY: CONTAINS 38 LEUCINE-RICH (LRR) REPEATS. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 1123. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19017; AAA28425.1; ALT_FRAME. DR EMBL; M19008; AAA28425.1; JOINED. DR EMBL; M19009; AAA28425.1; JOINED. DR EMBL; M19010; AAA28425.1; JOINED. DR EMBL; M19011; AAA28425.1; JOINED. DR EMBL; M19012; AAA28425.1; JOINED. DR EMBL; M19013; AAA28425.1; JOINED. DR EMBL; M19014; AAA28425.1; JOINED. DR EMBL; M19016; AAA28425.1; JOINED. DR EMBL; AE003777; AAF57127.1; -. DR EMBL; K03274; AAA28851.1; -. DR PIR; A29944; A29944. DR FlyBase; FBgn0000313; chp. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0007156; P:homophilic cell adhesion; IDA. DR InterPro; IPR001611; LRR. DR InterPro; IPR003591; LRR_typ. DR Pfam; PF00560; LRR; 29. DR PRINTS; PR00019; LEURICHRPT. DR SMART; SM00369; LRR_TYP; 7. KW Vision; Cell adhesion; Membrane; Repeat; Signal; Leucine-rich repeat; KW Glycoprotein. FT SIGNAL 1 29 FT CHAIN 30 1315 CHAOPTIN. FT REPEAT 101 124 LRR 1. FT REPEAT 126 149 LRR 2. FT REPEAT 150 173 LRR 3. FT REPEAT 175 198 LRR 4. FT REPEAT 199 222 LRR 5. FT REPEAT 224 247 LRR 6. FT REPEAT 249 272 LRR 7. FT REPEAT 277 300 LRR 8. FT REPEAT 302 324 LRR 9. FT REPEAT 326 347 LRR 10. FT REPEAT 349 372 LRR 11. FT REPEAT 374 397 LRR 12. FT REPEAT 451 474 LRR 13. FT REPEAT 475 498 LRR 14. FT REPEAT 525 548 LRR 15. FT REPEAT 550 572 LRR 16. FT REPEAT 575 598 LRR 17. FT REPEAT 599 622 LRR 18. FT REPEAT 624 646 LRR 19. FT REPEAT 648 670 LRR 20. FT REPEAT 674 697 LRR 21. FT REPEAT 706 729 LRR 22. FT REPEAT 731 754 LRR 23. FT REPEAT 755 778 LRR 24. FT REPEAT 779 802 LRR 25. FT REPEAT 803 826 LRR 26. FT REPEAT 828 849 LRR 27. FT REPEAT 852 875 LRR 28. FT REPEAT 877 900 LRR 29. FT REPEAT 902 924 LRR 30. FT REPEAT 926 947 LRR 31. FT REPEAT 948 970 LRR 32. FT REPEAT 971 994 LRR 33. FT REPEAT 995 1017 LRR 34. FT REPEAT 1043 1068 LRR 35. FT REPEAT 1117 1140 LRR 36. FT REPEAT 1142 1165 LRR 37. FT REPEAT 1169 1193 LRR 38. FT CARBOHYD 77 77 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 267 267 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 305 305 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 339 339 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 361 361 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 422 422 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 680 680 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 692 692 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 718 718 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 746 746 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 936 936 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 970 970 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1012 1012 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1104 1104 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1122 1122 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1152 1152 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1171 1171 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 12 12 A -> V (IN REF. 1). FT CONFLICT 44 44 C -> H (IN REF. 4). FT CONFLICT 50 50 C -> H (IN REF. 4). FT CONFLICT 937 937 I -> V (IN REF. 1). SQ SEQUENCE 1315 AA; 151982 MW; D2D89A64EB46FCE5 CRC64; MGLEFFFKFG YAFLTITLMI MIWMSLARAS MFDREMEETH YPPCTYNVMC TCSKSSTDLG IVHCKNVPFP ALPRMVNQSK VFMLHMENTG LREIEPYFLQ STGMYRLKIS GNHLTEIPDD AFTGLERSLW ELILPQNDLV EIPSKSLRHL QKLRHLDLGY NHITHIQHDS FRGLEDSLQT LILRENCISQ LMSHSFSGLL ILETLDLSGN NLFEIDPNVF VDGMPRLTRL LLTDNILSEI PYDALGPLKS LRTLDISHNV IWSLSGNETY EIKASTKLNL DNLHLEYNHI EVLPPNSFKY FDTVNRTFFD GNPIHTLRED AFKPARIREI YMRYCGLTNI SPVAFDSLVN SLQILDLSGN NLTKLHHKLF NNFDVLRVIS MRDNKIKIQK PTETFNAVHY TLLKLDLSGD RNDPTNLQTL RNMTRMRNMR SLSISRLGSS SVGPEDFKDF GVELEDLQIT RASLSGIQSH AFKHVRGLKR LDFSENGISS IENDAFHEIG HSLISLKMSH GYSGSALPAE PLRHLTSLQE LDFSNNHISS MSDTSFHFLK NLRLLELHDN RIEQVLKGTF QGDIHSKLEE ISLRFNHLTS ISQHTFFDLE ALRKLHLDDN KIDKIERRAF MNLDELEYLS LRGNKINNLA DESFQNLPKL EILDMAFNQL PNFNFDYFDQ VGTLSNLNVN VSHNQIRQLM YNSSWSGRNE HGGMYHSNIK ILDLSHNNIS IIHPGYFRPA EISLTHLHLG YNSLMNTTRD VFGNMPHLQW LDLSYNWIHE LDFDAFKNTK QLQLVFFGHN YLSDIPQDIF KPVQGLRIVD FSHNHLRGLP DNLFYNGGME KLDVSHNMML KIPSSSLSSL AALTLCELHL SNNFISTIHS MDLSNKFRSL RYLDISYNYL LRIDDAVFAT MPKLAVLDLS HNRDLKVMDK SFMGLENSLI KLGLENISLS TVPEIRLKYL REFRLGYNEL PSIPQELAHN MSNLRMLDLS NNDLTNVPLM TQALPHLRRL MLSGNPITSL NNNSFDGVNE DLEMLDISNF RLHYFEYGCL DSLPHLRSLK LTAYSHLEHF NIPHLLRHHY NIRQLWIEAP QPFTRIVKKG SGPTQEMQTL QLGNPTDLQR EMEGHLPSKL TNITFSGPQF TNLNERILRG MRSPYLYMQL FNTSLQALPP NFFKYMGRVR NISLDIRYHN RNLKKIPNPN TGAVPYLPNS VFLTDLKMSH TDLNCDCDLG WVEFWQRKRR QYICSSQTWT DTVFRTFMNS PCQVYGRHNC DEHDDDLRET RCENKGGQQL MEALKFDLEC GWDNANCREA AFVVVMVCVA MVFWM // ID CHD3_DROME STANDARD; PRT; 892 AA. AC O16102; Q8SYJ8; Q9VVZ3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chromodomain helicase-DNA-binding protein 3. GN CHD3 OR CG9594. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 1-812 FROM N.A. RX MEDLINE=97470991; PubMed=9326634; RA Woodage T., Basrai M.A., Baxevanis A.D., Hieter P., Collins F.S.; RT "Characterization of the CHD family of proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 94:11472-11477(1997). CC -!- FUNCTION: POSSIBLE TRANSCRIPTION ACTIVATOR (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SNF2/RAD54 HELICASE FAMILY. CC -!- SIMILARITY: CONTAINS 2 CHROMO DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PHD-TYPE ZINC FINGER. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A STOP CC CODON IN POSITION 628 AND A FRAMESHIFT IN POSITION 720. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CLONING CC ARTEFACTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003517; AAF49162.2; -. DR EMBL; AY071503; AAL49125.1; ALT_FRAME. DR EMBL; AF007780; AAB87384.1; ALT_SEQ. DR FlyBase; FBgn0023395; Chd3. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0003682; F:chromatin binding; ISS. DR GO; GO:0004386; F:helicase activity; ISS. DR GO; GO:0006333; P:chromatin assembly/disassembly; NAS. DR InterPro; IPR000953; Chromo. DR InterPro; IPR001410; DEAD. DR InterPro; IPR002464; DEAH_box. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR000330; SNF2_N. DR InterPro; IPR001965; Znf_PHD. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF00176; SNF2_N; 1. DR SMART; SM00298; CHROMO; 2. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00249; PHD; 1. DR PROSITE; PS00598; CHROMO_1; FALSE_NEG. DR PROSITE; PS50013; CHROMO_2; 2. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. KW DNA-binding; ATP-binding; Helicase; Nuclear protein; Repeat; KW Transcription regulation; Activator; Antigen; Zinc-finger. FT ZN_FING 35 82 PHD-TYPE. FT DOMAIN 84 156 CHROMO 1. FT DOMAIN 179 240 CHROMO 2. FT NP_BIND 292 299 ATP (POTENTIAL). FT SITE 409 412 DEAH BOX. FT CONFLICT 617 617 V -> I (IN REF. 4). SQ SEQUENCE 892 AA; 103021 MW; E11DF7F65A1F6D6D CRC64; MSSKRGADPD WKTPGKASKD KRPKTNAKKQ KFRDEEYCKV CSDGGDLLCC DSCPSVYHRT CLSPPLKSIP KGDWICPRCI PLPGKAEKIL SWRWALDRSV ELRTSKGEKR REYFIKWHGM SYWHCEWIPE GQMLLHHASM VASFQRRSDM EEPSLEELDD QDGNLHERFY RYGIKPEWLL VQRVINHSEE PNGGTMYLVK WRELSYNDSS WERESDSIPG LNQAIALYKK LRSSNKGRQR DRPAPTIDLN KKYEDQPVFL KEAGLKLHPF QIEGVSWLRY SWGQGIPTIL ADEMGLGKTI QTVVFLYSLF KEGHCRGPFL ISVPLSTLTN WERELELWAP ELYCVTYVGG KTARAVIRKH EISFEEVTTK TMRENQTQYK FNVMLTSYEF ISVDAAFLGC IDWAALVVDE AHRLRSNQSK FFRILSKYRI GYKLLLTGTP LQNNLEELFH LLNFLSSGKF NDLQTFQAEF TDVSKEEQVK RLHEILEPHM LRRLKADVLK SMPPKSEFIV RVELSSMQKK FYKHILTKNF KALNQKGGGR VCSLLNIMMD LRKCCNHPYL FPSAAEEATI SPSGLYEMSS LTKASGKLDL LSKMLKQLKA DNHRVLLFSQ MTKMLNVLEH FLEGEGYQYD RIDGSIKGDL RQKAIDRFND PVSEHFVFLL STRAGGLGIN LATADTVIIF DSDWNPHNDV QAFSRAHRMG QKKKVMIYRF VTHNSVEERI MQVAKHKMML THLVVRPGMG GMTTNFSKDE LEDILRFGTE DLFKDGKSEA IHYDDKAVAD LLDRTNRGIE EKESWANEYL SSFKVASYAT KEDHEEHDDY NNDAENTDPF YWENLMGKSQ PKLPKKQKKQ SQQSQVDVES IMGKGKRIRK EIDYSNQYPS PNRATPSSIV LM // ID CHDM_DROME STANDARD; PRT; 1982 AA. AC O97159; Q8MZ43; Q9VW50; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chromodomain helicase-DNA-binding protein Mi-2 homolog (dMi-2). GN MI-2 OR CG8103. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND MUTAGENESIS OF GLY-737. RX MEDLINE=99055400; PubMed=9836641; RA Kehle J., Beuchle D., Treuheit S., Christen B., Kennison J.A., RA Bienz M., Muller J.; RT "dMi-2, a hunchback-interacting protein that functions in Polycomb RT repression."; RL Science 282:1897-1900(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 1191-1982 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: VITAL ROLE IN DEVELOPMENT. PROTEIN BINDS TO A PORTION OF CC HUNCHBACK (HB) PROTEIN THAT IS CRITICAL FOR REPRESSION OF BITHORAX CC COMPLEX (BXC) GENES. MAY ALSO FUNCTION IN POLYCOMB GROUP (PCG) CC REPRESSION OF HOX GENES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE SNF2/RAD54 HELICASE FAMILY. CC -!- SIMILARITY: CONTAINS 2 CHROMO DOMAINS. CC -!- SIMILARITY: CONTAINS 2 PHD-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF119716; AAD17276.1; -. DR EMBL; AE003515; AAF49099.2; -. DR EMBL; AY113368; AAM29373.1; ALT_INIT. DR FlyBase; FBgn0013591; Mi-2. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0005700; C:polytene chromosome; IDA. DR GO; GO:0003682; F:chromatin binding; ISS. DR GO; GO:0004386; F:helicase activity; ISS. DR GO; GO:0016564; F:transcriptional repressor activity; IGI. DR GO; GO:0006333; P:chromatin assembly/disassembly; ISS. DR InterPro; IPR000953; Chromo. DR InterPro; IPR001410; DEAD. DR InterPro; IPR002464; DEAH_box. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR000330; SNF2_N. DR InterPro; IPR001965; Znf_PHD. DR Pfam; PF00385; chromo; 1. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00628; PHD; 2. DR Pfam; PF00176; SNF2_N; 1. DR SMART; SM00298; CHROMO; 2. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00249; PHD; 2. DR PROSITE; PS00598; CHROMO_1; FALSE_NEG. DR PROSITE; PS50013; CHROMO_2; 2. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS01359; ZF_PHD_1; 2. DR PROSITE; PS50016; ZF_PHD_2; 2. KW DNA-binding; ATP-binding; Helicase; Nuclear protein; Repeat; KW Transcription regulation; Repressor; Zinc-finger. FT ZN_FING 377 424 PHD-TYPE 1. FT ZN_FING 437 484 PHD-TYPE 2. FT DOMAIN 488 566 CHROMO 1. FT DOMAIN 612 673 CHROMO 2. FT NP_BIND 755 762 ATP (POTENTIAL). FT SITE 875 878 DEAH BOX. FT DOMAIN 13 16 POLY-GLU. FT DOMAIN 70 76 POLY-LYS. FT DOMAIN 239 248 POLY-GLU. FT DOMAIN 1279 1287 POLY-GLU. FT DOMAIN 1672 1677 POLY-ASP. FT MUTAGEN 737 737 G->D: IN ALLELE MI-2-5; LARVAL LETHAL. FT CONFLICT 101 101 G -> A (IN REF. 1). SQ SEQUENCE 1982 AA; 224199 MW; ED8E256D1AD0AC2F CRC64; MASEEENDDN FQEEEEAQED NAPAAELSND SDAPLKPNND EDDDYDPEDS RRKKKGKKRK TRKGEEKGRK KKKRKKNESE EDSDFVQHDE EVEYPSTSKR GRKRKEEKQA AKEKESASSG MPSVEDVCSA FSVCNVEIEY SEEELQSLTT YKAFMHHVRP ILQKENPKIA APKLVMLVAA KWREFCESNP HIQQEGGAAG SGGSAGQARS VTGDEPEEPR SSRSSRNEKP DDIYEEAVEE EEEEEEEEKK PRRKRSGRGK KGRRPSGKVP TLKIKLLGKR KRDSSDEEQD ASGASERDSD LEFERMLQKS DDSADEKEAP VSSKADNSAP AAQDDGSGAP VVRKKAKTKI GNKFKKKNKL KKTKNFPEGE DGEHEHQDYC EVCQQGGEII LCDTCPRAYH LVCLEPELDE PPEGKWSCPH CEADGGAAEE EDDDEHQEFC RVCKDGGELL CCDSCPSAYH TFCLNPPLDT IPDGDWRCPR CSCPPLTGKA EKIITWRWAQ RSNDDGPSTS KGSKNSNSRV REYFIKWHNM SYWHCEWVPE VQLDVHHPLM IRSFQRKYDM EEPPKFEESL DEADTRYKRI QRHKDKVGMK ANDDAEVLEE RFYKNGVKPE WLIVQRVINH RTARDGSTMY LVKWRELPYD KSTWEEEGDD IQGLRQAIDY YQDLRAVCTS ETTQSRSKKS KKGRKSKLKV EDDEDRPVKH YTPPPEKPTT DLKKKYEDQP AFLEGTGMQL HPYQIEGINW LRYSWGQGID TILADEMGLG KTIQTVTFLY SLYKEGHCRG PFLVAVPLST LVNWEREFEL WAPDFYCITY IGDKDSRAVI RENELSFEEG AIRGSKVSRL RTTQYKFNVL LTSYELISMD AACLGSIDWA VLVVDEAHRL KSNQSKFFRI LNSYTIAYKL LLTGTPLQNN LEELFHLLNF LSRDKFNDLQ AFQGEFADVS KEEQVKRLHE MLGPHMLRRL KTDVLKNMPS KSEFIVRVEL SAMQKKFYKF ILTKNYEALN SKSGGGSCSL INIMMDLKKC CNHPYLFPSA AEEATTAAGG LYEINSLTKA AGKLVLLSKM LKQLKAQNHR VLIFSQMTKM LDILEDFLEG EQYKYERIDG GITGTLRQEA IDRFNAPGAQ QFVFLLSTRA GGLGINLATA DTVIIYDSDW NPHNDIQAFS RAHRIGQANK VMIYRFVTRN SVEERVTQVA KRKMMLTHLV VRPGMGGKGA NFTKQELDDI LRFGTEDLFK EDDKEEAIHY DDKAVAELLD RTNRGIEEKE SWANEYLSSF KVASYATKEE EEEEETEIIK QDAENSDPAY WVKLLRHHYE QHQEDVGRSL GKGKRVRKQV NYTDGGVVAA DTTRDDSNWQ DNGSEYNSEY SAGSDEDGGD DDFDDQNGAE RKAKRRLERR DDRPLPPLLA RVGGNIEVLG FNARQRKSFL NAIMRYGMPP QDAFNSQWLV RDLRGKSERN FKAYVSLFMR HLCEPGADNA ETFADGVPRE GLSRQHVLTR IGVMSLIRKK VQEFEHINGY YSMPELILKP CEPVRSALKQ DVAALEAPPT GGNVDKSATT SNSVTPATSA APSPAPASEK GEDKDKDSEK EKDKTSAEKS EVKQEQEAEE DKKPGDVKQE NPVEEAAGDT KPSDAEVKTE VAKTEPKEET KDPEVKEEPK TEEKEKEKVD DKKPIPPTTV IDDDDDDVMI VKEDGELEKP SASSPKDQKA VAAATSAATG ATGKGAEDSL EVLKRKFMFN IADGGFTELH TLWLNEEKAA VPGREYEIWH RRHDYWLLAG IVTHGYGRWQ DIQNDIRFAI INEPFKMDVG KGNFLEIKNK FLARRFKLLE QALVIEEQLR RAAYLNLAQD PSHPAMSLNA RFAEVECLAE SHQHLSKESL AGNKPANAVL HKVLNQLEEL LSDMKSDVSR LPATLARIPP VAQRLQMSER SILSRLAATA GNASNAAQLM AQFPAGFQGT TLPAFTSGPA GNFANFRPQF SVPGQLSNNS GV // ID CHI1_DROME STANDARD; PRT; 508 AA. AC Q9W5U3; O17420; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable chitinase 1 (EC 3.2.1.14). GN CHT1 OR CG17682. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). RN [2] RP SEQUENCE OF 151-263 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98324849; PubMed=9662472; RA de la Vega H., Specht C.A., Liu Y., Robbins P.W.; RT "Chitinases are a multi-gene family in Aedes, Anopheles and RT Drosophila."; RL Insect Mol. Biol. 7:233-239(1998). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 1,4-BETA-LINKAGES OF N- CC ACETYL-D-GLUCOSAMINE POLYMERS OF CHITIN. CC -!- SIMILARITY: BELONGS TO CHITINASE CLASS II (FAMILY 18 OF GLYCOSYL CC HYDROLASES). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF026500; AAB81858.1; -. DR FlyBase; FBgn0022703; Cht1. DR InterPro; IPR001223; Glyco_hydro_18. DR InterPro; IPR001579; Glyco_hydro_18AS. DR Pfam; PF00704; Glyco_hydro_18; 2. DR ProDom; PD000471; Glyco_hydro_18; 2. DR SMART; SM00636; Glyco_18; 1. DR PROSITE; PS01095; CHITINASE_18; 1. KW Hydrolase; Glycosidase; Chitin degradation; Multigene family. FT ACT_SITE 264 264 PROTON DONOR (BY SIMILARITY). SQ SEQUENCE 508 AA; 57751 MW; 26CA23B02EFDEE97 CRC64; MGPYAYKGTQ WVSYDSPDMV RKKSLLVRSL KLGGGMVWAL DLDDFKNRCG NGVHPLLTEI HNVLKDPPSL MEIPGPIETT PTEYPGMEEE IHESNGEGPE VQPIEAVMQT CENEGEEHEG ILDPNHVLEE ENIEATEMAT EFKIICYFTN WAWYRQGGGK FLPEDIDSDL CTHIIYGFAV LSRDNLTIQP HDSWADLDNK FYERIVAYRK KGAKVTVAIG GWNDSAGDKY SRLVRNPEAR SRFIRNVLDF IEEYNFDGLD LDWEYPVCWQ VDCKKGTAEE KIGFSALVRE LFYAFQPRGL ILSAAVSPNK KVIDAGYEVA ELSHYFSWIS VMAYDYHGQW DKKTGHVAPM YSHPEGTANF NANFSMNYWI SMGADRRKLV MGIPLYGQSF SLAETTKHQL NAPTYGGGEA GEATRARGFL AYYEICLKIR HHRWNVVRDT KGRIGPFAYH GDQWVSFDDV PMIRHKSEYI KAMGLGGAMI WALDLDDFKN VAKHQTAFQA NNKCPIWT // ID CHI3_DROME STANDARD; PRT; 458 AA. AC Q9W5U2; O17422; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable chitinase 3 (EC 3.2.1.14). GN CHT3 OR CG18140. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). RN [2] RP SEQUENCE OF 182-294 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98324849; PubMed=9662472; RA de la Vega H., Specht C.A., Liu Y., Robbins P.W.; RT "Chitinases are a multi-gene family in Aedes, Anopheles and RT Drosophila."; RL Insect Mol. Biol. 7:233-239(1998). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 1,4-BETA-LINKAGES OF N- CC ACETYL-D-GLUCOSAMINE POLYMERS OF CHITIN. CC -!- SIMILARITY: BELONGS TO CHITINASE CLASS II (FAMILY 18 OF GLYCOSYL CC HYDROLASES). CC -!- SIMILARITY: CONTAINS 2 CHITIN-BINDING TYPE-2 DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF026502; AAB81860.1; -. DR FlyBase; FBgn0022701; Cht3. DR InterPro; IPR002557; Chitin_bind_PerA. DR InterPro; IPR001223; Glyco_hydro_18. DR InterPro; IPR001579; Glyco_hydro_18AS. DR Pfam; PF01607; CBM_14; 2. DR Pfam; PF00704; Glyco_hydro_18; 1. DR ProDom; PD000471; Glyco_hydro_18; 1. DR SMART; SM00494; ChtBD2; 2. DR SMART; SM00636; Glyco_18; 1. DR PROSITE; PS50940; CHIT_BIND_II; 2. DR PROSITE; PS01095; CHITINASE_18; FALSE_NEG. KW Hydrolase; Glycosidase; Chitin degradation; Chitin-binding; KW Multigene family; Repeat. FT DOMAIN 5 58 CHITIN-BINDING TYPE-2 1. FT DOMAIN 74 128 CHITIN-BINDING TYPE-2 2. FT ACT_SITE 295 295 PROTON DONOR (BY SIMILARITY). SQ SEQUENCE 458 AA; 52330 MW; 4A063190B7E96248 CRC64; MRPTILECTE GDYYPHRNCR KYYICVNKAL VPSECGGDLH WDGIKKLCDW PENVQCVTSK KYLKIIKSSS ANEEDPCKGE KRVPYPGNCS KYLFCLWNRL QASDCPPGLH YNERIGNCDW PAAAKCNPKG SESSEEAELN AMPKPPTPQT PSSHLRPTYP TEKPVPKPRD SHYKVICYFT NWAWYRKGIG RFTPDDINTE LCTHVIYGFA VLDYSELVLR THDSWADVEN NFYTRVTSLK SKGIKVSLAL GGWNDSQGDK YSRLVRSPMA RSRFVRHALE FIEKYGFEGL DLDWEYPVCW QTECNKGSTE EKDGFTAWVQ ELSEAFRPRG LMLSTAVSPS RKIIDAGYDI PQLSRYFDWI AVMTYDFHGH WDKKTGHVAP LYHHPDDDFE YFNVNYSINY WMEKGAPSQK LVMGIPLYGQ SFTLENTNSS GLNAKAPAPG EAGEFTRAAG FLAYYEVN // ID CIC_DROME STANDARD; PRT; 1403 AA. AC Q9U1H0; Q9VDN9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative transcription factor capicua. GN CIC OR CG5067. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Embryo; RX MEDLINE=20119182; PubMed=10652276; RA Jimenez G., Guichet A., Ephrussi A., Casanova J.; RT "Relief of gene repression by torso RTK signaling: role of capicua in RT Drosophila terminal and dorsoventral patterning."; RL Genes Dev. 14:224-231(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: REQUIRED FOR TERMINAL AND DORSOVENTRAL PATTERNING OF CC EARLY EMBRYOS. MAY ASSOCIATE WITH GRO TO REPRESS TLL AND HKB, CC RESTRICTING THEIR EXPRESSION TO EMBRYONIC TERMINAL POLES WHERE CC THEY INITIATE CORRECT DEVELOPMENT OF HEAD AND TAIL STRUCTURES. CC ALSO MEDIATES VENTRAL REPRESSION OF ZEN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN CENTRAL REGION OF EMBRYOS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MATERNALLY IN STAGE 1-3 CC BLASTODERM EMBRYOS. CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ252268; CAB66144.1; -. DR EMBL; AE003729; AAF55751.3; -. DR HSSP; P48436; 1SX9. DR FlyBase; FBgn0028386; cic. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW Transcription regulation; Developmental protein; DNA-binding; KW Nuclear protein. FT DNA_BIND 490 558 HMG BOX. FT DOMAIN 68 76 POLY-GLN. FT DOMAIN 110 116 POLY-ASN. FT DOMAIN 167 170 POLY-HIS. FT DOMAIN 172 177 POLY-PRO. FT DOMAIN 189 194 POLY-SER. FT DOMAIN 211 223 POLY-GLN. FT DOMAIN 323 342 POLY-GLN. FT DOMAIN 379 388 POLY-ALA. FT DOMAIN 466 474 POLY-GLN. FT DOMAIN 677 680 POLY-GLN. SQ SEQUENCE 1403 AA; 150128 MW; 068209695B4C18AC CRC64; MNAFQDFELG AKLYLQCLLS LSSSRSATPS YTSPVNHAGA SPLNAIAHSP VNVSATHRQN FFTPIANQSQ QQQQQQPVAV PLDSKWKTTP SPVLYNANNN SSNNNTSSSN NNNNSNWEVG SNSNTHVAAT AAATSTVGAQ PLPPQTTPVS LVMHAPPPQQ QPLQQQHHHH QPPPPPPASL PAPSAPPTSG SSSSHNSVGH ATSVIRISSS QQQHQQQQQH QQQAHPHVVV SGGQTFHPVI VDATQLSVPL PPTTVSFHQP NTPTSTAASV ASMSQDKMLA KNGYNAPWFK LLPHMTPMSK ASPAPVTPTL TTSASSYNVV MMQQQQQHQQ LQQQQQLQQQ QQSPPQMPLN HNNNHLIVSA PLSSPGKPLN CSMNDAKVAA AAAAAAVANQ RQKQQQEEPD DQLDDDVFET TTPGISANSK KQTAAMRLPT HNSNIRKLEE CHDDGAAGAP ATSAAKRRSQ SLSALQQQQQ QQQQAGAAGT AAGQPANKKI RRPMNAFMIF SKKHRKMVHK KHPNQDNRTV SKILGEWWYA LKPEQKAQYH ELASSVKDAH FKLHPEWKWC SKDRRKSSTS TATPGGKASG AAGTGDAKQR LVSVDGSDSL EHDMCPSTPG GSGSCGGQGI SSDLQGDIIP LTIDNYNSTC DEAPTTISMK GNGNGKLMKN ELPSDEDEQM LVVEEEQQQQ TVKKIDLHCR ERVNDSDMDD TPFDYRKQQP EANQRSAEEH STSGANGQAI NAPPLSGGER EITLKPKAIK AHPVLESNML PYTQMSIYTQ YTSPKNPIGV TPFQPTGGAF KSMPISPKGS GGKPEDAGSL QAHIKQEDIK QEPPSPYKLN NGSGSASGGG VVSAPPPNSG SVGAIFNFNV PTATALSQKQ FHYPMHHPHR SPTDLRAAHQ ACVPSSPAGM GLGHAANIAT PPASAPAQIM GGGPASQKMF FAMTHPYTLL QRSHQPGTPS LEHLQLDAFA PGGYTLRNHN GLSSLPPPVS AQPTMLLHGY PPSHGVEPPA RSPSYKSMPS TPKSATYLMS APPERGMDGG MSGCASAAAS GGDESDIDAD GQQFILAPTP AQLGRAPLQR RKNLSQSKSE SNVSFGANLG ASNGQHISRK LHSPTMMESS SPIIGHVNSS NLSSALPTPT SSTTTPNSDE QLPLTPTTSS SNSNLNQQQP KSPMKGAPGS TAAALKKKND EMNNSVLKQV DFEKKYKALP QFQPEDCQSP SAIAVPSSPR VYGTNYRKKN TAPPPVQKLM CEDDSIDEPA SAPPTTTQRF FGPDFNNELK ELESSDQTGR SPRTPKTPLQ SARSDASEKG HRKVLETRRS LVLQLFAEHG NFPTAQATMA FQSKHSDVFP RKQDLQLKIR EVRQKLLGQA SCTPHSAGPN TPSDSNSSST TLSASSTSLN MQTTSAADVF QYY // ID CID_DROME STANDARD; PRT; 1397 AA. AC P19538; O18525; Q8T6T1; Q9V4A8; DT 01-NOV-1990 (Rel. 16, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cubitus interruptus protein. GN CI OR CI-D OR CG2125. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=90346286; PubMed=2166702; RA Orenic T.V., Slusarski D.C., Kroll K.L., Holmgren R.A.; RT "Cloning and characterization of the segment polarity gene cubitus RT interruptus Dominant of Drosophila."; RL Genes Dev. 4:1053-1067(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=92146935; PubMed=1686006; RA Berry A.J., Ajioka J.W., Kreitman M.; RT "Lack of polymorphism on the Drosophila fourth chromosome resulting RT from selection."; RL Genetics 129:1111-1117(1991). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=97473533; PubMed=9332387; RA Ahmed A., Podemski L.; RT "Use of ordered deletions in genome sequencing."; RL Gene 197:367-373(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 1-5 FROM N.A., AND INTERACTION WITH ENGRAILED. RX MEDLINE=95324390; PubMed=7600980; RA Schwartz C., Locke J., Nishida C., Kornberg T.B.; RT "Analysis of cubitus interruptus regulation in Drosophila embryos and RT imaginal disks."; RL Development 121:1625-1635(1995). RN [6] RP SEQUENCE OF 521-769 FROM N.A. RC STRAIN=253.27; RX MEDLINE=21636764; PubMed=11778050; RA Wang W., Thornton K., Berry A., Long M.; RT "Nucleotide variation along the Drosophila melanogaster fourth RT chromosome."; RL Science 295:134-137(2002). CC -!- FUNCTION: INVOLVED IN SEGMENT POLARITY. REQUIRED FOR THE NORMAL CC DEVELOPMENT OF THE POSTERIOR HALF OF EACH EMBRYONIC SEGMENT. CC ENGRAILED PROTEIN DIRECTLY REPRESSES CI EXPRESSION IN POSTERIOR CC COMPARTMENT CELLS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: IN EMBRYOS, EXPRESSED UNIFORMLY THROUGHOUT CC THE BLASTODERM STAGE AND GASTRULATION (FROM STAGE 5). DURING STAGE CC 10, CI IS ELIMINATED FROM THE POSTERIOR COMPARTMENT OF EACH CC SEGMENT FORMING 15 SEGMENTALLY REPEATING STRIPES AT THE END OF THE CC SHORT PHASE OF GERM-BAND EXTENSION. CC -!- SIMILARITY: TO THE GLI-RELATED GROUP OF C2H2-TYPE ZINC-FINGERS CC PROTEINS. CC -!- SIMILARITY: CONTAINS 5 C2H2-TYPE ZINC FINGERS. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54360; CAA38244.1; -. DR EMBL; U66884; AAC47752.1; -. DR EMBL; AE003845; AAF59373.1; ALT_SEQ. DR EMBL; U21390; AAG15271.1; -. DR EMBL; AF433680; AAM17953.1; -. DR PIR; A38926; A38926. DR HSSP; P08151; 2GLI. DR FlyBase; FBgn0004859; ci. DR GO; GO:0005634; C:nucleus; IEP. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR GO; GO:0007367; P:segment polarity determination; IMP. DR GO; GO:0007224; P:smoothened signaling pathway; NAS. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 5. DR SMART; SM00355; ZnF_C2H2; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. KW Developmental protein; Segmentation polarity protein; Zinc-finger; KW Metal-binding; DNA-binding; Repeat; Nuclear protein. FT ZN_FING 451 476 C2H2-TYPE 1. FT ZN_FING 484 511 C2H2-TYPE 2. FT ZN_FING 517 541 C2H2-TYPE 3. FT ZN_FING 547 572 C2H2-TYPE 4. FT ZN_FING 578 603 C2H2-TYPE 5. FT CONFLICT 403 403 T -> K (IN REF. 3). FT CONFLICT 457 457 S -> R (IN REF. 1 AND 2). FT CONFLICT 804 805 YT -> IS (IN REF. 1 AND 2). FT CONFLICT 968 968 T -> S (IN REF. 1 AND 2). FT CONFLICT 1043 1043 S -> L (IN REF. 1 AND 2). FT CONFLICT 1152 1152 MISSING (IN REF. 1 AND 2). FT CONFLICT 1155 1155 V -> L (IN REF. 3). FT CONFLICT 1378 1397 DMTTSLTSLLEENRYLQMMQ -> V (IN REF. 1 AND FT 2). SQ SEQUENCE 1397 AA; 153280 MW; C3232A71EF9B8004 CRC64; MDAYALPTYF PLAYSELQFL ASRRAAAVAA AATVLPGSPC INQHHPTDVS SSVTVPSIIP TGGTSDSIKT SIQPQICNEN TLLGNAGHQH NHQPQHVHNI NVTGQPHDFH PAYRIPGYME QLYSLQRTNS ASSFHDPYVN CASAFHLAGL GLGSADFLGS RGLSSLGELH NAAVAAAAAG SLASTDFHFS VDGNRRLGSP RPPGGSIRAS ISRKRALSSS PYSDSFDINS MIRFSPNSLA TIMNGSRGSS AASGSYGHIS ATALNPMSHV HSTRLQQIQA HLLRASAGLL NPMTPQQVAA SGFSIGHMPT SASLRVNDVH PNLSDSHIQI TTSPTVTKDV SQVPAAAFSL KNLDDAREKK GPFKDVVPEQ PSSTSGGVAQ VEADSASSQL SDRCYNNVVN NITGIPGDVK VNSRLDEYIN CGSISIPSNE YDCANADTTD IKDEPGDFIE TNCHWRSCRI EFITQDELVK HINNDHIQTN KKAFVCRWED CTRGEKPFKA QYMLVVHMRR HTGEKPHKCT FEGCFKAYSR LENLKTHLRS HTGEKPYTCE YPGCSKAFSN ASDRAKHQNR THSNEKPYIC KAPGCTKRYT DPSSLRKHVK TVHGAEFYAN KKHKGLPLND ANSRLQQNNS RHNLQEHNID SSPCSEDSHL GKMLGTSSPS IKSESDISSS NHHLVNGVRA SDSLLTYSPD DLAENLNLDD GWNCDDDVDV ADLPIVLRAM VNIGNGNASA STIGGSVLAR QRFRGRLQTK GINSSTIMLC NIPESNRTFG ISELNQRITE LKMEPGTDAE IKIPKLPNTT IGGYTEDPLQ NQTSFRNTVS NKQGTVSGSI QGQFRRDSQN STASTYYGSM QSRRSSQSSQ VSSIPTMRPN PSCNSTASFY DPISPGCSRR SSQMSNGANC NSFTSTSGLP VLNKESNKSL NACINKPNIG VQGVGIYNSS LPPPPSSHLI ATNLKRLQRK DSEYHNFTSG RFSVPSYMHS LHIKNNKPVG ENEFDKAIAS NARRQTDPVP NINLDPLTNI SRFSTTPHSF DINVGKTNNI ASSINKDNLR KDLFTVSIKA DMAMTSDQHP NERINLDEVE ELILPDEMLQ YLNLVKDDTN HLEKEHQAVP VGSNVSETIA SNHYREQSNI YYTNKQILTP PSNVDIQPNT TKFTVQDKFA MTAVGGSFSQ RELSTLAVPN EHGHAKCESF HHQSQKYMNT DIGSKQQSAL PSAHQRQTEK SNYNQIIDSS MTSLPELNVD SIYPRNETEN IFKVHGDHDN EIQCGIISQS QMSPSTNLNN DGQFSTVNMQ PITTSKLFPP EPQKIVCDTQ ASNTSVMHLD TYQRTLEYVQ SCQNWMETNN TSTNQIQSLP GMPVNNTLFP DVSSSTHPYH GTNMVINDMT TSLTSLLEEN RYLQMMQ // ID CIKB_DROME STANDARD; PRT; 985 AA. AC P17970; O76805; Q9I7T9; Q9I7U0; DT 01-NOV-1990 (Rel. 16, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Potassium voltage-gated channel protein Shab. GN SHAB OR CG1066. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; RX MEDLINE=89146139; PubMed=2493160; RA Butler A., Wei A.G., Baker K., Salkoff L.; RT "A family of putative potassium channel genes in Drosophila."; RL Science 243:943-947(1989). RN [2] RP SEQUENCE FROM N.A. (ISOFORM LONG). RX MEDLINE=90239553; PubMed=2333511; RA Wei A.G., Covarrubias M., Butler A., Baker K., Pak M., Salkoff L.; RT "K+ current diversity is produced by an extended gene family RT conserved in Drosophila and mouse."; RL Science 248:599-603(1990). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG). RX MEDLINE=90245668; PubMed=2336395; RA Butler A., Wei A.G., Salkoff L.; RT "Shal, Shab, and Shaw: three genes encoding potassium channels in RT Drosophila."; RL Nucleic Acids Res. 18:2173-2174(1990). RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT), AND MUTAGENESIS. RC STRAIN=Canton-S; RX MEDLINE=99348357; PubMed=10419540; RA Hegde P., Gu G.G., Chen D., Free S.J., Singh S.; RT "Mutational analysis of the Shab-encoded delayed rectifier K(+) RT channels in Drosophila."; RL J. Biol. Chem. 274:22109-22113(1999). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS PROTEIN MEDIATES THE VOLTAGE-DEPENDENT POTASSIUM CC ION PERMEABILITY OF EXCITABLE MEMBRANES. ASSUMING OPENED OR CLOSED CC CONFORMATIONS IN RESPONSE TO THE VOLTAGE DIFFERENCE ACROSS THE CC MEMBRANE, THE PROTEIN FORMS A POTASSIUM-SELECTIVE CHANNEL THROUGH CC WHICH K+ IONS MAY PASS IN ACCORDANCE WITH THEIR ELECTROCHEMICAL CC GRADIENT. CC -!- SUBUNIT: HETEROTETRAMER OF POTASSIUM CHANNEL PROTEINS (PROBABLE). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P17970-1; Sequence=Displayed; CC Name=Short; CC IsoId=P17970-2; Sequence=VSP_000960; CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN LATE EMBRYOS AND PUPAE. CC -!- DOMAIN: THE AMINO TERMINUS MAY BE IMPORTANT IN DETERMINING THE CC RATE OF INACTIVATION OF THE CHANNEL WHILE THE TAIL MAY PLAY A ROLE CC IN MODULATION OF CHANNEL ACTIVITY AND/OR TARGETING OF THE CHANNEL CC TO SPECIFIC SUBCELLULAR COMPARTMENTS. CC -!- MISCELLANEOUS: THE SEGMENT S4 IS PROBABLY THE VOLTAGE-SENSOR AND CC IS CHARACTERIZED BY A SERIES OF POSITIVELY CHARGED AMINO ACIDS AT CC EVERY THIRD POSITION. CC -!- SIMILARITY: BELONGS TO THE POTASSIUM CHANNEL FAMILY. B (SHAB) CC SUBFAMILY. CC -!- CAUTION: REF.5 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32659; AAA28896.1; -. DR EMBL; AF084525; AAC33365.1; -. DR EMBL; AE003476; AAG22232.1; ALT_SEQ. DR EMBL; AE003476; AAG22233.1; ALT_INIT. DR PIR; S12746; S12746. DR HSSP; Q54397; 1BL8. DR FlyBase; FBgn0003383; Shab. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR001622; K+channel_pore. DR InterPro; IPR003091; K_channel. DR InterPro; IPR003131; K_tetra. DR InterPro; IPR003971; Kv9_channel. DR InterPro; IPR003968; Kv_channel. DR InterPro; IPR005820; M+channel_nlg. DR Pfam; PF00520; ion_trans; 1. DR Pfam; PF02214; K_tetra; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01494; KV9CHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR SMART; SM00225; BTB; 1. KW Transport; Ion transport; Ionic channel; Voltage-gated channel; KW Potassium channel; Potassium transport; Potassium; Transmembrane; KW Glycoprotein; Phosphorylation; Multigene family; Alternative splicing. FT TRANSMEM 436 454 SEGMENT S1. FT TRANSMEM 474 495 SEGMENT S2. FT TRANSMEM 506 527 SEGMENT S3. FT TRANSMEM 536 561 SEGMENT S4. FT TRANSMEM 577 598 SEGMENT S5. FT TRANSMEM 638 659 SEGMENT S6. FT CARBOHYD 245 245 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 429 429 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 530 530 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 749 749 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 756 756 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 885 885 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 888 888 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 914 914 N-LINKED (GLCNAC...) (POTENTIAL). FT MOD_RES 690 690 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT MOD_RES 731 731 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT MOD_RES 796 796 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT VARSPLIC 717 746 Missing (in isoform Short). FT /FTId=VSP_000960. FT MUTAGEN 435 435 R->Q: IN ALLELE SHAB-1; TEMPERATURE- FT SENSITIVE PARALYTIC. FT MUTAGEN 608 608 V->D: IN ALLELE SHAB-1; TEMPERATURE- FT SENSITIVE PARALYTIC. FT CONFLICT 31 31 Q -> L (IN REF. 1, 2 AND 3). FT CONFLICT 220 220 S -> G (IN REF. 1, 2 AND 3). FT CONFLICT 307 307 R -> G (IN REF. 1, 2 AND 3). FT CONFLICT 362 362 S -> G (IN REF. 1, 2 AND 3). FT CONFLICT 414 415 FS -> CA (IN REF. 5). FT CONFLICT 495 495 A -> S (IN REF. 1, 2 AND 3). FT CONFLICT 553 553 V -> I (IN REF. 5). FT CONFLICT 613 613 A -> T (IN REF. 5). FT CONFLICT 630 630 C -> Y (IN REF. 5). FT CONFLICT 651 651 V -> I (IN REF. 5). FT CONFLICT 827 828 EQ -> DE (IN REF. 1, 2 AND 3). FT CONFLICT 877 877 A -> G (IN REF. 1, 2 AND 3). FT CONFLICT 903 985 GDGDGGGVDDDNLSQAKGLPIQMMITPGEVAELRRQVALEN FT LQNQRMDNLEQDVPVEFECCFCTTKGLPGCHGECIPLRANS FT V -> VMEMGAVSMTTTFPRPRDCPSR (IN REF. 1, 2 FT AND 3). FT CONFLICT 911 913 DDD -> NDN (IN REF. 4). SQ SEQUENCE 985 AA; 106359 MW; 59E38AD35F064AC8 CRC64; MVGQLQGGQA AGQQQQQQQA TQQQQHSKQQ QQQQQQQQQQ LQLKQHQQQQ QDILYQQHNE AIAIARGLQA ATPADIGDNQ PYYDTSGNVD WERAMGAGGA GAYGGIGIGS LPAAGGAAYH LGPANPAGLV SRHLDYGDGG HLAGPSAGLP AGAVGSGAGA GAGAGASVTG SGSGAGTGTG TGAGSGSGSG AAGKEVRYAP FPVASPTHSI PTTSQQIVGS VGGVGVGGAS SQSISGGVPT HSQSNTTGAL QRTHSRSMSS IPPPEPFMIA QSKAVNSRVS INVGGVRHEV LWRTLERLPH TRLGRLRECT THEAIVELCD DYSLADNEYF FDRHPKSFSS ILNFYRTGKL HIVDEMCVLA FSDDLEYWGV DELYLESCCQ HKYHQRKENV HEEMRKEAES LRQRDEEEFG EGKFSEYQKY LWELLEKPNT SFAARVIAVI SILFIVLSTI ALTLNTLPQL QHIDNGTPQD NPQLAMVEAV CITWFTLEYI LRFSASPDKW KFFKGGLNII DLLAILPYFV SLFLLETNKN ATDQFQDVRR VVQVFRIMRI LRVLKLARHS TGLQSLGFTL RNSYKELGLL MLFLAMGVLI FSSLAYFAEK DEKDTKFVSI PEAFWWAGIT MTTVGYGDIC PTTALGKVIG TVCCICGVLV VALPIPIIVN NFAEFYKNQM RREKALKRRE ALDRAKREGS IVSFHHINLK DAFAKSMDLI DVIVDTGKQT NVVHPKGKRQ STPNIGRQTL DVQSAPGHNL SQTDGNSTEG ESTSGRNPAT TGTGCYKNYD HVANLRNSNL HNRRGSSSEQ DAVPPYSFDN PNARQTSMMA MESYRREQQA LLQQQQQQQQ QMLQMQQIQQ KAPNGNGGAT GGGVANNLAM VAASSAATAV ATATNASNAS NTAPGSEGAE GGGDGDGGGV DDDNLSQAKG LPIQMMITPG EVAELRRQVA LENLQNQRMD NLEQDVPVEF ECCFCTTKGL PGCHGECIPL RANSV // ID CIKE_DROME STANDARD; PRT; 1174 AA. AC Q02280; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Potassium voltage-gated channel protein eag (Ether-a-go-go protein). GN EAG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91262635; PubMed=1840699; RA Warmke J., Drysdale R., Ganetzky B.; RT "A distinct potassium channel polypeptide encoded by the Drosophila RT eag locus."; RL Science 252:1560-1562(1991). CC -!- FUNCTION: PROTEIN EAG IS MOST PROBABLY A STRUCTURAL COMPONENT OF CC THE POTASSIUM CHANNEL AND MEDIATES THE POTASSIUM PERMEABILITY OF CC MEMBRANES. CC -!- SUBUNIT: DIMER (POTENTIAL). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- MISCELLANEOUS: THE SEGMENT S4 IS PROBABLY THE VOLTAGE-SENSOR AND CC IS CHARACTERIZED BY A SERIES OF POSITIVELY CHARGED AMINO ACIDS AT CC EVERY THIRD POSITION. CC -!- MISCELLANEOUS: THE SEGMENT H5 IS THOUGHT TO LINE THE CHANNEL PORE. CC -!- SIMILARITY: BELONGS TO THE POTASSIUM CHANNEL FAMILY. H (EAG) CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 CYCLIC NUCLEOTIDE-BINDING DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PAS (PER-ARNT-SIM) DIMERIZATION DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PAS-ASSOCIATED C-TERMINAL (PAC) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M61157; AAA28495.1; -. DR PIR; A40853; A40853. DR FlyBase; FBgn0000535; eag. DR GO; GO:0007619; P:courtship behavior; NAS. DR GO; GO:0007611; P:learning and/or memory; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR GO; GO:0008016; P:regulation of heart rate; NAS. DR GO; GO:0045474; P:response to ether (sensu Insecta); NAS. DR InterPro; IPR000595; cNMP_binding. DR InterPro; IPR003967; Erg_channel. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR001622; K+channel_pore. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR001610; PAC. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR000014; PAS_domain. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF00520; ion_trans; 1. DR Pfam; PF00785; PAC; 1. DR PRINTS; PR01470; ERGCHANNEL. DR SMART; SM00100; cNMP; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 1. DR PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG. DR PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR PROSITE; PS50113; PAC; 1. DR PROSITE; PS50112; PAS; 1. KW Transport; Ion transport; Ionic channel; Voltage-gated channel; KW Potassium channel; Potassium; Potassium transport; Transmembrane; KW Glycoprotein; Phosphorylation; Repeat; Multigene family. FT DOMAIN 1 226 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 227 246 SEGMENT S1 (POTENTIAL). FT TRANSMEM 269 291 SEGMENT S2 (POTENTIAL). FT DOMAIN 292 313 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 314 335 SEGMENT S3 (POTENTIAL). FT TRANSMEM 343 369 SEGMENT S4 (POTENTIAL). FT DOMAIN 370 371 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 372 393 SEGMENT S5 (POTENTIAL). FT DOMAIN 442 467 SEGMENT H5 (PORE-FORMING) (POTENTIAL). FT TRANSMEM 471 493 SEGMENT S6 (POTENTIAL). FT DOMAIN 494 1174 CYTOPLASMIC (POTENTIAL). FT DOMAIN 43 97 PAS. FT DOMAIN 113 165 PAC. FT NP_BIND 571 688 CNMP. FT CARBOHYD 262 262 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 412 412 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 424 424 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1174 AA; 126236 MW; 344C80DC06E4340E CRC64; MPGGRRGLVA PQNTFLENII RRSNSQPDSS FLLANAQIVD FPIVYCNESF CKISGYNRAE VMQKSCRYVC GFMYGELTDK ETVGRLEYTL ENQQQDQFEI LLYKKNNLQC GCALSQFGKA QTQETPLWLL LQVAPIRNER DLVVLFLLTF RDITALKQPI DSEDTKGVLG LSKFAKLARS VTRSRQFSAH LPTLKDPTKQ SNLAHMMSLS ADIMPQYRQE APKTPPHILL HYCAFKAIWD WVILCLTFYT AIMVPYNVAF KNKTSEDVSL LVVDSIVDVI FFIDIVLNFH TTFVGPGGEV VSDPKVIRMN YLKSWFIIDL LSCLPYDVFN AFDRDEDGIG SLFSALKVVR LLRLGRVVRK LDRYLEYGAA MLILLLCFYM LVAHWLACIW YSIGRSDADN GIQYSWLWKL ANVTQSPYSY IWSNDTGPEL VNGPSRKSMY VTALYFTMTC MTSVGFGNVA AETDNEKVFT ICMMIIAALL YATIFGHVTT IIQQMTSATA KYHDMLNNVR EFMKLHEVPK ALSERVMDYV VSTWAMTKGL DTEKVLNCCP KDMKADICVH LNRKVFDEHP TFRLASDGCL RALAMHFMMS HSAPGDLLYH TGESIDSLCF IVTGSLEVIQ DDEVVAILGK GDVFGDQFWK DSAVGQSAAN VRALTYCDLH AIKRDKLLEV LDFYSAFANS FARNLVLTYN LRHRLIFRRV ADVKREKELA ERRKNEPQLP QNQDHLVRKI FSKFRRTPQV QAGSKELVGG SGQSDVEKGD GEVERTKVLP KAPKLQASQA TLARQDTIDE GGEVDSSPPS RDSRVVIEGA AVSSATVGPS PPVATTSSAA AGAGVSGGPG SGGTVVAIVT KADRNLALER ERQIEMASSR ATTSDTYDTG LRETPPTLAQ RDLVATVLDM KVDVRLELQR MQQRIGRIED LLGELVKRLA PGASSGGNAP DNSSGQTTPG DEICAGCGAG GGGTPTTQAP PTSAVTSPVD TVITISSPGA SGSGSGTGAG AGSAVAGAGG AGLLDPGATV VSSAGGNGLG PLMLKKRRSK SGKAPAPPEQ TLASTAGTAT AAPAGVAGSG MTSSAPASAD QQQQHQSAAD QSPTTPGAEL LHLRLLEEDF TAAQLPSTSS GGAGGGGGSG SGATPTTPPP TIAGGSGSGT PTSTTATTTP TGSGTATRGK LDFL // ID CIKL_DROME STANDARD; PRT; 490 AA. AC P17971; Q9VW11; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Potassium voltage-gated channel protein Shal (Shal2). GN SHAL OR SHAL2 OR CG9262. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90239553; PubMed=2333511; RA Wei A., Covarrubias M., Butler A., Baker K., Pak M., Salkoff L.; RT "K+ current diversity is produced by an extended gene family RT conserved in Drosophila and mouse."; RL Science 248:599-603(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90245668; PubMed=2336395; RA Wei A., Covarrubias M., Butler A., Baker K., Pak M., Salkoff L.; RT "Shal, Shab, and Shaw: three genes encoding potassium channels in RT Drosophila."; RL Nucleic Acids Res. 18:2173-2174(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MEDIATES THE VOLTAGE-DEPENDENT POTASSIUM ION CC PERMEABILITY OF EXCITABLE MEMBRANES. ASSUMING OPENED OR CLOSED CC CONFORMATIONS IN RESPONSE TO THE VOLTAGE DIFFERENCE ACROSS THE CC MEMBRANE, THE PROTEIN FORMS A POTASSIUM-SELECTIVE CHANNEL THROUGH CC WHICH K+ IONS MAY PASS IN ACCORDANCE WITH THEIR ELECTROCHEMICAL CC GRADIENT. MAY PLAY A ROLE IN THE NERVOUS SYSTEM AND IN THE CC REGULATION OF BEATING FREQUENCY IN PACEMAKER CELLS. CC -!- SUBUNIT: HETEROTETRAMER OF POTASSIUM CHANNEL PROTEINS (PROBABLE). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P17971-1; Sequence=Displayed; CC Name=2; CC IsoId=P17971-2; Sequence=Not described; CC -!- DOMAIN: THE AMINO TERMINUS MAY BE IMPORTANT IN DETERMINING THE CC RATE OF INACTIVATION OF THE CHANNEL WHILE THE TAIL MAY PLAY A ROLE CC IN MODULATION OF CHANNEL ACTIVITY AND/OR TARGETING OF THE CHANNEL CC TO SPECIFIC SUBCELLULAR COMPARTMENTS. CC -!- MISCELLANEOUS: THE SEGMENT S4 IS PROBABLY THE VOLTAGE-SENSOR AND CC IS CHARACTERIZED BY A SERIES OF POSITIVELY CHARGED AMINO ACIDS AT CC EVERY THIRD POSITION. CC -!- SIMILARITY: BELONGS TO THE POTASSIUM CHANNEL FAMILY. SHAL CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32660; AAA28895.1; -. DR EMBL; AE003516; AAF49144.2; -. DR PIR; A35312; A35312. DR FlyBase; FBgn0005564; Shal. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR001622; K+channel_pore. DR InterPro; IPR003091; K_channel. DR InterPro; IPR003131; K_tetra. DR InterPro; IPR003968; Kv_channel. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR003975; Shal_channel. DR Pfam; PF00520; ion_trans; 1. DR Pfam; PF02214; K_tetra; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR PRINTS; PR01497; SHALCHANNEL. DR SMART; SM00225; BTB; 1. KW Transport; Ion transport; Ionic channel; Voltage-gated channel; KW Potassium channel; Potassium transport; Potassium; Transmembrane; KW Multigene family; Alternative splicing. FT TRANSMEM 186 204 SEGMENT S1. FT TRANSMEM 229 250 SEGMENT S2. FT TRANSMEM 261 282 SEGMENT S3. FT TRANSMEM 290 308 SEGMENT S4. FT TRANSMEM 324 345 SEGMENT S5. FT TRANSMEM 385 406 SEGMENT S6. FT CARBOHYD 46 46 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 350 350 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 353 353 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 408 408 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 490 AA; 55918 MW; E178E1C89B07DA74 CRC64; MASVAAWLPF ARAAAIGWVP IATHPLPPPP MPKDRRKTDD EKLLINVSGR RFETWRNTLE KYPDTLLGSN EREFFYDEDC KEYFFDRDPD IFRHILNYYR TGKLHYPKHE CLTSYDEELA FFGIMPDVIG DCCYEDYRDR KRENAERLMD DKLSENGDQN LQQLTNMRQK MWRAFENPHT STSALVFYYV TGFFIAVSVM ANVVETVPCG HRPGRAGTLP CGERYKIVFF CLDTACVMIF TAEYLLRLFA APDRCKFVRS VMSIIDVVAI MPYYIGLGIT DNDDVSGAFV TLRVFRVFRI FKFSRHSQGL RILGYTLKSC ASELGFLVFS LAMAIIIFAT VMFYAEKNVN GTNFTSIPAA FWYTIVTMTT LGYGDMVPET IAGKIVGGVC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD KRKAQRKARL ARIRIAKASS GAAFVSKKKA AEARWAAQES GIELDDNYRD EDIFELQHHH LLRCLEKTTM // ID CIKS_DROME STANDARD; PRT; 656 AA. AC P08510; P08511; P08512; P08513; Q24277; Q24521; Q9VWZ9; DT 01-AUG-1988 (Rel. 08, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Potassium voltage-gated channel protein Shaker. GN SH OR CG12348. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM ALPHA). RX MEDLINE=87292096; PubMed=2441471; RA Tempel B.L., Papazian D.M., Schwarz T.L., Jan Y.N., Jan L.Y.; RT "Sequence of a probable potassium channel component encoded at Shaker RT locus of Drosophila."; RL Science 237:770-775(1987). RN [2] RP SEQUENCE OF 1-257 FROM N.A. (ISOFORM BETA). RX MEDLINE=87273502; PubMed=2440582; RA Kamb A., Iverson L.E., Tanouye M.A.; RT "Molecular characterization of Shaker, a Drosophila gene that encodes RT a potassium channel."; RL Cell 50:405-413(1987). RN [3] RP SEQUENCE FROM N.A. (ISOFORM DELTA). RC STRAIN=Canton-S, and Oregon-R; RA Baumann A., Krah-Jentgens I., Mueller R., Mueller-Holtkamp F., RA Seidel R., Kecskemethy N., Casal J., Ferrus A., Pongs O.; RT "Molecular organization of the maternal effect region of the Shaker RT complex of Drosophila: characterization of an I(A) channel transcript RT with homology to vertebrate Na(+) channel."; RL EMBO J. 6:3419-3429(1987). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS ALPHA; BETA; DELTA; GAMMA AND EPSILON). RC STRAIN=Canton-S; RX MEDLINE=88296413; PubMed=2456921; RA Pongs O., Kecskemethy N., Mueller R., Krah-Jentgens I., RA Baumann A., Kiltz H.H., Canal I., Llamazares S., Ferrus A.; RT "Shaker encodes a family of putative potassium channel proteins in RT the nervous system of Drosophila."; RL EMBO J. 7:1087-1096(1988). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS ALPHA; BETA; GAMMA AND B). RX MEDLINE=88122563; PubMed=2448635; RA Schwarz T.L., Tempel B.L., Papazian D.M., Jan Y.N., Jan L.Y.; RT "Multiple potassium-channel components are produced by alternative RT splicing at the Shaker locus in Drosophila."; RL Nature 331:137-142(1988). RN [6] RP ERRATUM. RA Schwarz T.L., Tempel B.L., Papazian D.M., Jan Y.N., Jan L.Y.; RL Nature 332:740-740(1988). RN [7] RP SEQUENCE OF 450-534 FROM N.A. RC STRAIN=H4; RX MEDLINE=90166523; PubMed=3272175; RA Kamb A., Tseng-Crank J., Tanouye M.A.; RT "Multiple products of the Drosophila Shaker gene may contribute to RT potassium channel diversity."; RL Neuron 1:421-430(1988). RN [8] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [9] RP RNA EDITING. RX MEDLINE=22789647; PubMed=12907802; RA Hoopengardner B., Bhalla T., Staber C., Reenan R.; RT "Nervous system targets of RNA editing identified by comparative RT genomics."; RL Science 301:832-836(2003). CC -!- FUNCTION: MEDIATES THE VOLTAGE-DEPENDENT POTASSIUM ION CC PERMEABILITY OF EXCITABLE MEMBRANES. ASSUMING OPENED OR CLOSED CC CONFORMATIONS IN RESPONSE TO THE VOLTAGE DIFFERENCE ACROSS THE CC MEMBRANE, THE PROTEIN FORMS A POTASSIUM-SELECTIVE CHANNEL THROUGH CC WHICH K(+) IONS MAY PASS IN ACCORDANCE WITH THEIR ELECTROCHEMICAL CC GRADIENT. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=B; CC IsoId=P08510-1; Sequence=Displayed; CC Name=Alpha; Synonyms=A, Adult; CC IsoId=P08510-2; Sequence=VSP_000959; CC Name=Beta; Synonyms=D, Late population; CC IsoId=P08510-3; Sequence=VSP_000954; CC Name=Gamma; Synonyms=C; CC IsoId=P08510-4; Sequence=VSP_000955, VSP_000959; CC Name=Delta; Synonyms=Larval; CC IsoId=P08510-5; Sequence=VSP_000956, VSP_000957, VSP_000958; CC Name=Epsilon; Synonyms=Larval; CC IsoId=P08510-6; Sequence=VSP_000957, VSP_000958; CC -!- DOMAIN: THE SEGMENT S4 IS PROBABLY THE VOLTAGE-SENSOR AND IS CC CHARACTERIZED BY A SERIES OF POSITIVELY CHARGED AMINO ACIDS AT CC EVERY THIRD POSITION. CC -!- SIMILARITY: BELONGS TO THE POTASSIUM CHANNEL FAMILY. A (SHAKER) CC SUBFAMILY. CC -!- CAUTION: REF.2 AND REF.8 SEQUENCES DIFFER FROM THAT SHOWN DUE TO CC FRAMESHIFTS. CC -!- CAUTION: REF.8 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17211; AAA28417.1; -. DR EMBL; M17155; AAA70217.1; ALT_FRAME. DR EMBL; X06184; CAA29549.1; -. DR EMBL; X07131; CAA30143.1; -. DR EMBL; X07132; CAA30144.1; -. DR EMBL; X07133; CAA30145.1; -. DR EMBL; X07134; CAA30146.1; -. DR EMBL; X78908; CAA55519.1; -. DR EMBL; X06742; CAA29917.1; -. DR EMBL; AE003507; AAF48786.2; ALT_SEQ. DR PIR; JH0193; JH0193. DR PIR; S02284; S02284. DR PDB; 1HO2; 05-JUN-02. DR PDB; 1HO7; 05-JUN-02. DR FlyBase; FBgn0003380; Sh. DR GO; GO:0008076; C:voltage-gated potassium channel complex; NAS. DR GO; GO:0005249; F:voltage-gated potassium channel activity; NAS. DR GO; GO:0007619; P:courtship behavior; NAS. DR GO; GO:0007611; P:learning and/or memory; NAS. DR GO; GO:0045474; P:response to ether (sensu Insecta); NAS. DR GO; GO:0007607; P:taste; NAS. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR001622; K+channel_pore. DR InterPro; IPR003091; K_channel. DR InterPro; IPR003131; K_tetra. DR InterPro; IPR003968; Kv_channel. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR003972; Shaker_channel. DR Pfam; PF00520; ion_trans; 1. DR Pfam; PF02214; K_tetra; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR PRINTS; PR01496; SHAKERCHANEL. DR SMART; SM00225; BTB; 1. KW Transport; Ion transport; Ionic channel; Voltage-gated channel; KW Potassium channel; Potassium transport; Potassium; Transmembrane; KW Glycoprotein; Alternative splicing; Multigene family; 3D-structure; KW RNA editing. FT DOMAIN 1 227 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 228 246 SEGMENT S1. FT TRANSMEM 279 300 SEGMENT S2. FT DOMAIN 301 311 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 312 332 SEGMENT S3. FT TRANSMEM 361 380 SEGMENT S4. FT DOMAIN 381 395 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 396 415 SEGMENT S5. FT TRANSMEM 457 478 SEGMENT S6. FT DOMAIN 479 616 CYTOPLASMIC (POTENTIAL). FT DOMAIN 20 27 POLY-GLN. FT DOMAIN 558 564 POLY-GLN. FT DOMAIN 592 602 POLY-GLN. FT DOMAIN 607 620 POLY-GLN. FT DOMAIN 626 631 POLY-ALA. FT CARBOHYD 259 259 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 263 263 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 61 MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIA FT ERKLQLREQQLQRNSLDGYG -> MTMWQSGGMGGHGSQNN FT PWMKLMGIVHKERRHTENVQSQSGSNERNLNQ (in FT isoform Beta). FT /FTId=VSP_000954. FT VARSPLIC 1 61 MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIA FT ERKLQLREQQLQRNSLDGYG -> MQMILVAGG (in FT isoform Gamma). FT /FTId=VSP_000955. FT VARSPLIC 1 61 MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIA FT ERKLQLREQQLQRNSLDGYG -> MAHITTTHGSLSQATR FT (in isoform Delta). FT /FTId=VSP_000956. FT VARSPLIC 349 349 D -> V (in isoform Delta and isoform FT Epsilon). FT /FTId=VSP_000957. FT VARSPLIC 350 656 Missing (in isoform Delta and isoform FT Epsilon). FT /FTId=VSP_000958. FT VARSPLIC 535 656 VESTPGLTETHPGRSAVAPFLGAQQQQQQQPVASSLSMSID FT KQLQHPLQHVTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQL FT QQQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV FT -> IDATTPGLTDHTGRHMVPFLRTQQSFEKQQLQLQLQLQ FT QQSQSPHGQQMTQQQQLGQNGLRSTNSLQLRHNNAMAVSIE FT TDV (in isoform Alpha and isoform Gamma). FT /FTId=VSP_000959. FT VARIANT 178 178 K -> E (partial, due to RNA editing). FT VARIANT 178 178 K -> G (partial, due to RNA editing). FT VARIANT 178 178 K -> R (partial, due to RNA editing). FT VARIANT 360 360 I -> M (partial, due to RNA editing). FT VARIANT 464 464 I -> V (partial, due to RNA editing). FT VARIANT 489 489 T -> A (partial, due to RNA editing). FT VARIANT 491 491 Q -> R (partial, due to RNA editing). FT CONFLICT 93 93 H -> D (IN REF. 2). FT CONFLICT 102 102 N -> NIN (IN REF. 2). FT CONFLICT 216 216 L -> S (IN REF. 2). FT CONFLICT 453 453 V -> F (IN REF. 1 AND 4; CAA30143). FT CONFLICT 463 463 A -> V (IN REF. 1 AND 4; CAA30143). FT CONFLICT 506 506 P -> S (IN REF. 1 AND 4; CAA30143). FT CONFLICT 511 511 T -> A (IN REF. 1 AND 4; CAA30143). FT CONFLICT 513 513 G -> VG (IN REF. 7). FT CONFLICT 516 516 M -> L (IN REF. 1 AND 4; CAA30143). FT CONFLICT 528 528 M -> I (IN REF. 1 AND 4; CAA30143). FT CONFLICT 564 564 MISSING (IN REF. 4; CAA30144). FT CONFLICT 584 585 HV -> QL (IN REF. 4; CAA30144). SQ SEQUENCE 656 AA; 74316 MW; 8F09B69BB6793FEE CRC64; MAAVAGLYGL GEDRQHRKKQ QQQQQHQKEQ LEQKEEQKKI AERKLQLREQ QLQRNSLDGY GSLPKLSSQD EEGGAGHGFG GGPQHFEPIP HDHDFCERVV INVSGLRFET QLRTLNQFPD TLLGDPARRL RYFDPLRNEY FFDRSRPSFD AILYYYQSGG RLRRPVNVPL DVFSEEIKFY ELGDQAINKF REDEGFIKEE ERPLPDNEKQ RKVWLLFEYP ESSQAARVVA IISVFVILLS IVIFCLETLP EFKHYKVFNT TTNGTKIEED EVPDITDPFF LIETLCIIWF TFELTVRFLA CPNKLNFCRD VMNVIDIIAI IPYFITLATV VAEEEDTLNL PKAPVSPQDK SSNQAMSLAI LRVIRLVRVF RIFKLSRHSK GLQILGRTLK ASMRELGLLI FFLFIGVVLF SSAVYFAEAG SENSFFKSIP DAFWWAVVTM TTVGYGDMTP VGVWGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETD QEEMQSQNFN HVTSCPYLPG TLGQHMKKSS LSESSSDMMD LDDGVESTPG LTETHPGRSA VAPFLGAQQQ QQQQPVASSL SMSIDKQLQH PLQHVTQTQL YQQQQQQQQQ QQNGFKQQQQ QTQQQLQQQQ SHTINASAAA ATSGSGSSGL TMRHNNALAV SIETDV // ID CIKW_DROME STANDARD; PRT; 498 AA. AC P17972; Q9VQU5; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Potassium voltage-gated channel protein Shaw (Shaw2). GN SHAW OR SHAW2 OR CG2822. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90239553; PubMed=2333511; RA Wei A., Covarrubias M., Butler A., Baker K., Pak M., Salkoff L.; RT "K+ current diversity is produced by an extended gene family RT conserved in Drosophila and mouse."; RL Science 248:599-603(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90245668; PubMed=2336395; RA Wei A., Covarrubias M., Butler A., Baker K., Pak M., Salkoff L.; RT "Shal, Shab, and Shaw: three genes encoding potassium channels in RT Drosophila."; RL Nucleic Acids Res. 18:2173-2174(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MEDIATES THE VOLTAGE-DEPENDENT POTASSIUM ION CC PERMEABILITY OF EXCITABLE MEMBRANES. ASSUMING OPENED OR CLOSED CC CONFORMATIONS IN RESPONSE TO THE VOLTAGE DIFFERENCE ACROSS THE CC MEMBRANE, THE PROTEIN FORMS A POTASSIUM-SELECTIVE CHANNEL THROUGH CC WHICH K(+) IONS MAY PASS IN ACCORDANCE WITH THEIR ELECTROCHEMICAL CC GRADIENT. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- MISCELLANEOUS: THE SEGMENT S4 IS PROBABLY THE VOLTAGE-SENSOR AND CC IS CHARACTERIZED BY A SERIES OF POSITIVELY CHARGED AMINO ACIDS AT CC EVERY THIRD POSITION. CC -!- MISCELLANEOUS: THIS CHANNEL PROTEIN BELONGS TO THE DELAYED CC RECTIFIER CLASS. CC -!- SIMILARITY: BELONGS TO THE POTASSIUM CHANNEL FAMILY. C (SHAW) CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32661; AAA28897.1; -. DR EMBL; AE003579; AAF51069.1; -. DR PIR; A41359; A41359. DR HSSP; Q54397; 1BL8. DR FlyBase; FBgn0003386; Shaw. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR001622; K+channel_pore. DR InterPro; IPR003091; K_channel. DR InterPro; IPR003131; K_tetra. DR InterPro; IPR003968; Kv_channel. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR003974; Shaw_channel. DR Pfam; PF00520; ion_trans; 1. DR Pfam; PF02214; K_tetra; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR PRINTS; PR01498; SHAWCHANNEL. DR SMART; SM00225; BTB; 1. KW Transport; Ion transport; Ionic channel; Voltage-gated channel; KW Potassium channel; Potassium transport; Potassium; Transmembrane; KW Multigene family. FT TRANSMEM 175 193 SEGMENT S1. FT TRANSMEM 230 252 SEGMENT S2. FT TRANSMEM 263 284 SEGMENT S3. FT TRANSMEM 292 313 SEGMENT S4. FT TRANSMEM 329 350 SEGMENT S5. FT TRANSMEM 392 413 SEGMENT S6. FT CARBOHYD 206 206 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 213 213 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 481 481 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 498 AA; 56509 MW; 977E3B7F22F098E2 CRC64; MNLINMDSEN RVVLNVGGIR HETYKATLKK IPATRLSRLT EALANYDPIL NEYFFDRHPG VFAQVLNYYR TGKLHYPTDV CGPLFEEELE FWGLDSNQVE PCCWMTYTQH RDTQETLAVL DRLDLDTEKP SEEELARKFG FEEDYYKGTI SWWQEMKPRI WSLFDEPYSS NAAKTIGVVS VFFICISILS FCLKTHPDMR VPIVRNITVK TANGSNGWFL DKTQTNAHIA FFYIECVCNA WFTFEILVRF ISSPNKWEFI KSSVNIIDYI ATLSFYIDLV LQRFASHLEN ADILEFFSII RIMRLFKLTR HSSGLKILIQ TFRASAKELT LLVFFLVLGI VIFASLVYYA ERIQPNPHND FNSIPLGLWW ALVTMTTVGY GDMAPKTYIG MFVGALCALA GVLTIALPVP VIVSNFAMYY SHTQARAKLP KKRRRVLPVE QPRQPRLPGA PGGVSGCGTP GSGPHSGPMG SGGTGPRRMN NKTKDLVSPK SDMAFSFD // ID CINA_DROME STANDARD; PRT; 2131 AA. AC P35500; O15994; P92137; Q24082; Q24083; Q24084; Q24528; Q24529; AC Q24530; Q24531; Q24532; Q9VXF7; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sodium channel protein para (Paralytic protein). GN PARA OR CG9907. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; RX MEDLINE=94238327; PubMed=8182428; RA Thackeray J.R., Ganetzky B.; RT "Developmentally regulated alternative splicing generates a complex RT array of Drosophila para sodium channel isoforms."; RL J. Neurosci. 14:2569-2578(1994). RN [2] RP SEQUENCE FROM N.A. (ISOFORM D). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-1862 FROM N.A., FUNCTION, AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=89376565; PubMed=2550145; RA Loughney K., Kreber R., Ganetzky B.; RT "Molecular analysis of the para locus, a sodium channel gene in RT Drosophila."; RL Cell 58:1143-1154(1989). RN [4] RP SEQUENCE OF 1683-1895 FROM N.A. RX MEDLINE=89184571; PubMed=2538830; RA Ramaswami M., Tanouye M.A.; RT "Two sodium-channel genes in Drosophila: implications for channel RT diversity."; RL Proc. Natl. Acad. Sci. U.S.A. 86:2079-2082(1989). RN [5] RP SEQUENCE OF 51-61 FROM N.A. RA Tanaka Y.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE OF 51-61 FROM N.A. RA Tanaka Y., Yagi Y., Gamo S.; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE. RX MEDLINE=96042905; PubMed=8536968; RA Thackeray J.R., Ganetzky B.; RT "Conserved alternative splicing patterns and splicing signals in the RT Drosophila sodium channel gene para."; RL Genetics 141:203-214(1995). CC -!- FUNCTION: MEDIATES THE VOLTAGE-DEPENDENT SODIUM ION PERMEABILITY CC OF EXCITABLE MEMBRANES. ASSUMING OPENED OR CLOSED CONFORMATIONS IN CC RESPONSE TO THE VOLTAGE DIFFERENCE ACROSS THE MEMBRANE, THE CC PROTEIN FORMS A SODIUM-SELECTIVE CHANNEL THROUGH WHICH NA(+) IONS CC MAY PASS IN ACCORDANCE WITH THEIR ELECTROCHEMICAL GRADIENT. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Further isoforms have been identified but not yet CC sequenced. These have different combinations of the optional CC exons A, B, C, D, E and F. Isoforms always have either exon C CC or D as these encode segment S4. Sequence identity to para CC from D.virilis suggests there may also be optional exons H and CC I; CC Name=D; CC IsoId=P35500-1; Sequence=Displayed; CC Name=A; CC IsoId=P35500-2; Sequence=VSP_001035; CC Name=B; CC IsoId=P35500-3; Sequence=VSP_001036; CC Name=C; CC IsoId=P35500-4; Sequence=VSP_001037; CC Name=E; CC IsoId=P35500-5; Sequence=VSP_001038; CC Name=F24; CC IsoId=P35500-6; Sequence=VSP_001039; CC Name=F30; CC IsoId=P35500-7; Sequence=VSP_001040; CC -!- DEVELOPMENTAL STAGE: ISOFORMS A AND B ARE SEEN IN EMBRYOS AND CC ADULTS. ISOFORMS D, F24 AND F30 ARE PREDOMINANT IN EMBRYOS AND CC ISOFORMS C AND E PREDOMINANT IN ADULTS. CC -!- DOMAIN: THE SEQUENCE CONTAINS 4 INTERNAL REPEATS, EACH WITH 5 CC HYDROPHOBIC SEGMENTS (S1,S2,S3,S5,S6) AND ONE POSITIVELY CHARGED CC SEGMENT (S4). SEGMENTS S4 ARE PROBABLY THE VOLTAGE-SENSORS AND ARE CC CHARACTERIZED BY A SERIES OF POSITIVELY CHARGED AMINO ACIDS AT CC EVERY THIRD POSITION. CC -!- SIMILARITY: BELONGS TO THE SODIUM CHANNEL FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U26713; AAA98541.1; -. DR EMBL; U26714; AAA98542.1; -. DR EMBL; U26715; AAA98543.1; -. DR EMBL; U26716; AAA98544.1; -. DR EMBL; U26716; AAA98545.1; -. DR EMBL; U26716; AAA98546.1; -. DR EMBL; U26716; AAA98547.1; -. DR EMBL; U26716; AAA98548.1; -. DR EMBL; U26717; AAA98549.1; -. DR EMBL; AE003502; AAF48617.1; ALT_SEQ. DR EMBL; M32078; AAB59190.1; -. DR EMBL; M32078; AAB59191.1; -. DR EMBL; M32078; AAB59192.1; -. DR EMBL; M32078; AAB59193.1; -. DR EMBL; M32078; AAB59194.1; -. DR EMBL; M32078; AAB59195.1; -. DR EMBL; AB008113; BAA22890.1; -. DR EMBL; AB035812; BAA88526.1; -. DR FlyBase; FBgn0003036; para. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0005248; F:voltage-gated sodium channel activity; NAS. DR GO; GO:0045433; P:male courtship behavior (sensu Insecta), so...; NAS. DR GO; GO:0046680; P:response to DDT; IMP. DR GO; GO:0046684; P:response to pyrethroid; IMP. DR GO; GO:0006814; P:sodium ion transport; NAS. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR001696; Na_channel. DR InterPro; IPR003915; PKD_2. DR Pfam; PF00520; ion_trans; 4. DR PRINTS; PR00170; NACHANNEL. DR PRINTS; PR01433; POLYCYSTIN2. KW Ionic channel; Transmembrane; Ion transport; Voltage-gated channel; KW Glycoprotein; Repeat; Alternative splicing; Phosphorylation. FT REPEAT 134 467 I. FT REPEAT 799 1069 II. FT REPEAT 1284 1591 III. FT REPEAT 1601 1862 IV. FT TRANSMEM 149 172 S1 OF REPEAT I. FT TRANSMEM 181 199 S2 OF REPEAT I. FT TRANSMEM 213 231 S3 OF REPEAT I. FT TRANSMEM 238 257 S4 OF REPEAT I. FT TRANSMEM 274 297 S5 OF REPEAT I. FT TRANSMEM 406 427 S6 OF REPEAT I. FT TRANSMEM 813 837 S1 OF REPEAT II. FT TRANSMEM 849 873 S2 OF REPEAT II. FT TRANSMEM 881 900 S3 OF REPEAT II. FT TRANSMEM 907 926 S4 OF REPEAT II. FT TRANSMEM 942 963 S5 OF REPEAT II. FT TRANSMEM 1014 1041 S6 OF REPEAT II. FT TRANSMEM 1297 1320 S1 OF REPEAT III. FT TRANSMEM 1335 1359 S2 OF REPEAT III. FT TRANSMEM 1366 1387 S3 OF REPEAT III. FT TRANSMEM 1392 1413 S4 OF REPEAT III. FT TRANSMEM 1433 1454 S5 OF REPEAT III. FT TRANSMEM 1534 1560 S6 OF REPEAT III. FT TRANSMEM 1615 1638 S1 OF REPEAT IV. FT TRANSMEM 1650 1673 S2 OF REPEAT IV. FT TRANSMEM 1680 1703 S3 OF REPEAT IV. FT TRANSMEM 1714 1735 S4 OF REPEAT IV. FT TRANSMEM 1751 1773 S5 OF REPEAT IV. FT TRANSMEM 1836 1860 S6 OF REPEAT IV. FT MOD_RES 553 553 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT MOD_RES 570 570 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT CARBOHYD 313 313 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 325 325 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 343 343 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 682 682 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 982 982 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1055 1055 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1180 1180 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1463 1463 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1482 1482 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1862 1862 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2047 2047 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 555 575 Missing (in isoform A). FT /FTId=VSP_001035. FT VARSPLIC 763 770 Missing (in isoform B). FT /FTId=VSP_001036. FT VARSPLIC 914 967 LRVFKLAKSWPTLNLLISIMGRTMGALGNLTFVLCIIIFIF FT AVMGMQLFGKNYH -> LRVFKLAKSWPTLNLLISIMGRTV FT GALGNLTFVLCIIIFIFAVMGMQLFGKNYT (in FT isoform C). FT /FTId=VSP_001037. FT VARSPLIC 1099 1112 Missing (in isoform E). FT /FTId=VSP_001038. FT VARSPLIC 1113 1122 Missing (in isoform F24). FT /FTId=VSP_001039. FT VARSPLIC 1115 1122 Missing (in isoform F30). FT /FTId=VSP_001040. FT CONFLICT 52 52 R -> Q (IN REF. 2, 5 AND 6). FT CONFLICT 189 189 Y -> C (IN CDNA ZS20.2). FT CONFLICT 198 198 M -> V (IN CDNA ZS20.2). FT CONFLICT 205 205 C -> R (IN CDNA ZS20.2). FT CONFLICT 299 299 E -> Q (IN REF. 1; AAA98542 AND 5). FT CONFLICT 304 304 K -> E (IN REF. 1; AAA98542). FT CONFLICT 437 437 R -> K (IN REF. 2). FT CONFLICT 1110 1111 SE -> TK (IN REF. 1; AAA98543). FT CONFLICT 1296 1296 R -> Q (IN REF. 1; AAA98543 AND 2). FT CONFLICT 1300 1300 D -> N (IN REF. 1; AAA98543 AND 2). FT CONFLICT 1363 1363 L -> F (IN REF. 2). FT CONFLICT 1587 1587 S -> N (IN REF. 2). SQ SEQUENCE 2131 AA; 239385 MW; D1ECE68845A90F16 CRC64; MTEDSDSISE EERSLFRPFT RESLVQIEQR IAAEHEKQKE LERKRAEGEV PRYGRKKKQK EIRYDDEDED EGPQPDPTLE QGVPIPVRLQ GSFPPELAST PLEDIDPYYS NVLTFVVVSK GKDIFRFSAS KAMWMLDPFN PIRRVAIYIL VHPLFSLFII TTILVNCILM IMPTTPTVES TEVIFTGIYT FESAVKVMAR GFILCPFTYL RDAWNWLDFV VIALAYVTMG IDLGNLAALR TFRVLRALKT VAIVPGLKTI VGAVIESVKN LRDVIILTMF SLSVFALMGL QIYMGVLTEK CIKKFPLDGS WGNLTDENWD YHNRNSSNWY SEDEGISFPL CGNISGAGQC DDDYVCLQGF GPNPNYGYTS FDSFGWAFLS AFRLMTQDFW EDLYQLVLRA AGPWHMLFFI VIIFLGSFYL VNLILAIVAM SYDELQRKAE EEEAAEEEAI REAEEAAAAK AAKLEERANA QAQAAADAAA AEEAALHPEM AKSPTYSCIS YELFVGGEKG NDDNNKEKMS IRSVEVESES VSVIQRQPAP TTAHQATKVR KVSTTSLSLP GSPFNIRRGS RSSHKYTIRN GRGRFGIPGS DRKPLVLSTY QDAQQHLPYA DDSNAVTPMS EENGAIIVPV YYGNLGSRHS SYTSHQSRIS YTSHGDLLGG MAVMGVSTMT KESKLRNRNT RNQSVGATNG GTTCLDTNHK LDHRDYEIGL ECTDEAGKIK HHDNPFIEPV QTQTVVDMKD VMVLNDIIEQ AAGRHSRASD RGVSVYYFPT EDDDEDGPTF KDKALEVILK GIDVFCVWDC CWVWLKFQEW VSLIVFDPFV ELFITLCIVV NTMFMAMDHH DMNKEMERVL KSGNYFFTAT FAIEATMKLM AMSPKYYFQE GWNIFDFIIV ALSLLELGLE GVQGLSVLRS FRLLRVFKLA KSWPTLNLLI SIMGRTMGAL GNLTFVLCII IFIFAVMGMQ LFGKNYHDHK DRFPDGDLPR WNFTDFMHSF MIVFRVLCGE WIESMWDCMY VGDVSCIPFF LATVVIGNLV VLNLFLALLL SNFGSSSLSA PTADNDTNKI AEAFNRIGRF KSWVKRNIAD CFKLIRNKLT NQISDQPSGE RTNQISWIWS EGKGVCRCIS AEHGDNELEL GHDEILADGL IKKGIKEQTQ LEVAIGDGME FTIHGDMKNN KPKKSKYLNN ATDDDTASIN SYGSHKNRPF KDESHKGSAE TMEGEEKRDA SKEDLGLDEE LDEEGECEEG PLDGDIIIHA HDEDILDEYP ADCCPDSYYK KFPILAGDDD SPFWQGWGNL RLKTFRLIED KYFETAVITM ILMSSLALAL EDVHLPQRPI LQDILYYMDR IFTVIFFLEM LIKWLALGFK VYLTNAWCWL DFVIVMVSLI NFVASLVGAG GIQAFKTMRT LRALRPLRAM SRMQGMRVVV NALVQAIPSI FNVLLVCLIF WLIFAIMGVQ LFAGKYFKCE DMNGTKLSHE IIPNRNACES ENYTWVNSAM NFDHVGNAYL CLFQVATFKG WIQIMNDAID SREVDKQPIR ETNIYMYLYF VFFIIFGSFF TLNLFIGVII DNFNEQKKKA GGSLEMFMTE DQKKYYSAMK KMGSKKPLKA IPRPRWRPQA IVFEIVTDKK FDIIIMLFIG LNMFTMTLDR YDASDTYNAV LDYLNAIFVV IFSSECLLKI FALRYHYFIE PWNLFDVVVV ILSILGLVLS DIIEKYFVSP TLLRVVRVAK VGRVLRLVKG AKGIRTLLFA LAMSLPALFN ICLLLFLVMF IFAIFGMSFF MHVKEKSGIN DVYNFKTFGQ SMILLFQMST SAGWDGVLDA IINEEACDPP DNDKGYPGNC GSATVGITFL LSYLVISFLI VINMYIAVIL ENYSQATEDV QEGLTDDDYD MYYEIWQQFD PEGTQYIRYD QLSEFLDVLE PPLQIHKPNK YKIISMDIPI CRGDLMYCVD ILDALTKDFF ARKGNPIEET GEIGEIAARP DTEGYEPVSS TLWRQREEYC ARLIQHAWRK HKARGEGGGS FEPDTDHGDG GDPDAGDPAP DEATDGDAPA GGDGSVNGTA EGAADADESN VNSPGEDAAA AAAAAAAAAA AGTTTAGSPG AGSAGRQTAV LVESDGFVTK NGHKVVIHSR SPSITSRTAD V // ID CIN_DROME STANDARD; PRT; 674 AA. AC P39205; Q9U1M0; Q9V3E2; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Molybdenum cofactor synthesis protein cinnamon. GN CIN OR EG:BACR37P7.3 OR CG2945. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 2). RX MEDLINE=94374679; PubMed=8088525; RA Kamdar K.P., Shelton M.E., Finnerty V.; RT "The Drosophila molybdenum cofactor gene cinnamon is homologous to RT three Escherichia coli cofactor proteins and to the rat protein RT gephyrin."; RL Genetics 137:791-801(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN MOLYBDENUM COFACTOR BIOSYNTHESIS. CC -!- PATHWAY: MOLYBDENUM COFACTOR BIOSYNTHESIS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P39205-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; Synonyms=A, B; CC IsoId=P39205-2; Sequence=VSP_003236, VSP_003237; CC -!- SIMILARITY: STRONG, TO RAT GEPHYRIN. CC -!- SIMILARITY: IN THE N-TERMINAL HALF, TO E.COLI MOAB AND MOG AND IN CC THE C-TERMINAL END TO E.COLI MOEA. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19876; AAA65877.1; -. DR EMBL; AE003417; AAF45488.1; -. DR EMBL; AL050231; CAB65851.1; -. DR EMBL; AL050231; CAB65852.1; -. DR EMBL; AY069078; AAL39223.1; -. DR HSSP; P28694; 1DI6. DR FlyBase; FBgn0000316; cin. DR InterPro; IPR001453; MoCF_biosynth. DR InterPro; IPR008285; MoCF_bios_C. DR InterPro; IPR008284; MoCF_bios_N. DR InterPro; IPR005111; MoeA_C. DR InterPro; IPR005110; MoeA_N. DR Pfam; PF00994; MoCF_biosynth; 2. DR Pfam; PF03454; MoeA_C; 1. DR Pfam; PF03453; MoeA_N; 1. DR ProDom; PD002460; MoCF_biosynth; 2. DR TIGRFAMs; TIGR00177; molyb_syn; 2. DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1. DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1. KW Molybdenum cofactor biosynthesis; Multifunctional enzyme; KW Alternative splicing. FT DOMAIN 76 226 G-DOMAIN. FT DOMAIN 257 669 E-DOMAIN. FT VARSPLIC 1 73 Missing (in isoform 2). FT /FTId=VSP_003236. FT VARSPLIC 74 84 MAQGYDPLEDL -> MESITFGVLTI (in isoform FT 2). FT /FTId=VSP_003237. FT CONFLICT 487 487 S -> T (IN REF. 1). SQ SEQUENCE 674 AA; 74577 MW; 939C39D457E02E59 CRC64; MSFPDKAERK KCWNNRDEYW KCLEEHAPKH SSTSGEKVPT PCQSLRKSFE QSCPGQWVKH FDRKRTYDQF KEKMAQGYDP LEDLSDTCWQ EPEKDTSGPI LRQLIGETFA NTQVIGNIVP DEKDIIQQEL RKWIDREELR VILTTGGTGF APRDVTPEAT RQLLEKECPQ LSMYITLESI KQTQYAALSR GLCGIAGNTL ILNLPGSEKA VKECFQTISA LLPHAVHLIG DDVSLVRKTH AEVQGSAQKS HICPHKTGTG TDSDRNSPYP MLPVQEVLSI IFNTVQKTAN LNKILLEMNA PVNIPPFRAS IKDGYAMKST GFSGTKRVLG CIAAGDSPNS LPLAEDECYK INTGAPLPLE ADCVVQVEDT KLLQLDKNGQ ESLVDILVEP QAGLDVRPVG YDLSTNDRIF PALDPSPVVV KSLLASVGNR LILSKPKVAI VSTGSELCSP RNQLTPGKIF DSNTTMLTEL LVYFGFNCMH TCVLSDSFQR TKESLLELFE VVDFVICSGG VSMGDKDFVK SVLEDLQFRI HCGRVNIKPG KPMTFASRKD KYFFGLPGNP VSAFVTFHLF ALPAIRFAAG WDRCKCSLSV LNVKLLNDFS LDSRPEFVRA SVISKSGELY ASVNGNQISS RLQSIVGADV LINLPARTSD RPLAKAGEIF PASVLRFDFI SKYE // ID CKS1_DROME STANDARD; PRT; 74 AA. AC Q24152; Q9VLD0; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cyclin-dependent kinases regulatory subunit. GN CKS OR CKS1 OR CDI2 OR CG3738. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95108082; PubMed=7809159; RA Finley R.L., Brent R.; RT "Interaction mating reveals binary and ternary connections between RT Drosophila cell cycle regulators."; RL Proc. Natl. Acad. Sci. U.S.A. 91:12980-12984(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: BINDS TO THE CATALYTIC SUBUNIT OF THE CYCLIN DEPENDENT CC KINASES (CDC2 AND CDC2C) AND IS ESSENTIAL FOR THEIR BIOLOGICAL CC FUNCTION. CC -!- SUBUNIT: FORMS AN HOMOHEXAMER THAT CAN PROBABLY BIND SIX KINASE CC SUBUNITS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CKS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U40077; AAB02189.1; -. DR EMBL; AE003624; AAF52763.1; -. DR EMBL; AY061285; AAL28833.1; -. DR HSSP; P33552; 1CKS. DR FlyBase; FBgn0010314; Cks. DR InterPro; IPR000789; Cyc_dep_kin_rsub. DR Pfam; PF01111; CKS; 1. DR PIRSF; PIRSF000659; Cdcp_CKS1; 1. DR PRINTS; PR00296; CYCLINKINASE. DR ProDom; PD005152; Cyc_dep_kin_rsub; 1. DR PROSITE; PS00944; CKS_1; 1. DR PROSITE; PS00945; CKS_2; 1. KW Cell division. SQ SEQUENCE 74 AA; 9122 MW; 1AAF5486960FE8AD CRC64; MSKDIYYSDK YYDEQFEYRH VVLPKELVKM VPKTHLMTEA EWRSIGVQQS RGWIHYMIHK PEPHILLFRR PKTD // ID CLAT_DROME STANDARD; PRT; 721 AA. AC P07668; Q8MQR2; Q9VE41; DT 01-APR-1988 (Rel. 07, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Choline O-acetyltransferase (EC 2.3.1.6) (CHOACTase) (Choline DE acetylase) (ChAT). GN CHA OR CG12345. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=86233376; PubMed=3086876; RA Itoh N., Slemmon J.R., Hawke D.H., Williamson R., Morita E., RA Itakura K., Roberts E., Shively J.E., Crawford G.D., Salvaterra P.M.; RT "Cloning of Drosophila choline acetyltransferase cDNA."; RL Proc. Natl. Acad. Sci. U.S.A. 83:4081-4085(1986). RN [2] RP REVISIONS, AND SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=91072373; PubMed=2123874; RA Sugihara H., Andrisani V., Salvaterra P.M.; RT "Drosophila choline acetyltransferase uses a non-AUG initiation codon RT and full length RNA is inefficiently translated."; RL J. Biol. Chem. 265:21714-21719(1990). RN [3] RP REVISIONS. RA Salvaterra P.; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CATALYZES THE REVERSIBLE SYNTHESIS OF ACETYLCHOLINE CC (ACH) FROM ACETYL COA AND CHOLINE AT CHOLINERGIC SYNAPSES. CC -!- CATALYTIC ACTIVITY: ACETYL-COA + CHOLINE = COA + O-ACETYLCHOLINE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=P07668-1; Sequence=Displayed; CC Name=B; CC IsoId=P07668-2; Sequence=VSP_008316; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -!- CAUTION: REF.6 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 310. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63724; AAA28406.2; -. DR EMBL; AE003723; AAF55588.3; -. DR EMBL; AY128433; AAM75026.1; ALT_FRAME. DR PIR; A24889; A24889. DR FlyBase; FBgn0000303; Cha. DR InterPro; IPR000542; Carn_acyl_trans. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. KW Transferase; Acyltransferase; Neurotransmitter biosynthesis; KW Alternative splicing. FT ACT_SITE 419 419 POTENTIAL. FT VARSPLIC 583 589 Missing (in isoform B). FT /FTId=VSP_008316. FT CONFLICT 1 1 M -> V (IN REF. 6). SQ SEQUENCE 721 AA; 81327 MW; 1867F3B8421F994E CRC64; MASNEASTSA AGSGPESAAL FSKLRSFSIG SGPNSPQRVV SNLRGFLTHR LSNITPSDTG WKDSILSIPK KWLSTAESVD EFGFPDTLPK VPVPALDETM ADYIRALEPI TTPAQLERTK ELIRQFSAPQ GIGARLHQYL LDKREAEDNW AYYYWLNEMY MDIRIPLPIN SNPGMVFPPR RFKTVHDVAH FAARLLDGIL SHREMLDSGE LPLERAASRE KNQPLCMAQY YRLLGSCRRP GVKQDSQFLP SRERLNDEDR HVVVICRNQM YCVVLQASDR GKLSESEIAS QILYVLSDAP CLPAKPVPVG LLTAEPRSTW ARDREMLQED ERNQRNLELI ETAQVVLCLD EPLAGNFNAR GFTGATPTVH RAGDRDETNM AHEMIHGGGS EYNSGNRWFD KTMQLIICTD GTWGLCYEHS CSEGIAVVQL LEKIYKKIEE HPDEDNGLPQ HHLPPPERLE WHVGPQLQLR FAQASKSVDK CIDDLDFYVY RYQSYGKTFI KSCQVSPDVY IQLALQLAHY KLYGRLVATY ESASTRRFLH GRVDCIRAAS TEALEWAKAM CQGEGANVPL ESDREDEEES RKVKFSIYSK DHLRELFRCA VARQTEVMVK NILGNGIDIP LLGLREASIE VTGEMHELFK DESYIISQCF LLSTSQVACS TDSFMGYGPV TPRGYGCSYN PHPEQIVFCV SAFYSCEDTS ASRYAKSLQD SLDIMRDLLQ N // ID CLC_DROME STANDARD; PRT; 219 AA. AC Q9VWA1; O61647; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Clathrin light chain (dClc). GN CLC OR CG6948. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RX MEDLINE=99196241; PubMed=10098605; RA Vasyukevich K., Bazinet C.; RT "A Drosophila clathrin light-chain gene: sequence, mapping, and RT absence of neuronal specialization."; RL DNA Cell Biol. 18:235-241(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CLATHRIN IS THE MAJOR PROTEIN OF THE POLYHEDRAL COAT OF CC COATED PITS AND VESICLES. CC -!- SUBUNIT: CLATHRIN COATS ARE FORMED FROM MOLECULES CONTAINING 3 CC HEAVY CHAINS AND 3 LIGHT CHAINS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC FACE OF COATED PITS AND CC VESICLES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. CC -!- MISCELLANEOUS: THERE IS NO EVIDENCE OF THE NEURONAL SPLICE VARIANT CC FOUND IN VERTEBRATES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF055900; AAC14276.1; -. DR EMBL; AE003514; AAF49047.1; -. DR EMBL; AY121633; AAM51960.1; -. DR FlyBase; FBgn0024814; Clc. DR GO; GO:0030132; C:clathrin coat of coated pit; ISS. DR GO; GO:0030125; C:clathrin vesicle coat; ISS. DR GO; GO:0005326; F:neurotransmitter transporter activity; ISS. DR GO; GO:0007269; P:neurotransmitter secretion; ISS. DR GO; GO:0006836; P:neurotransmitter transport; ISS. DR GO; GO:0016183; P:synaptic vesicle coating; ISS. DR InterPro; IPR000996; Clathrin_lg_ch. DR InterPro; IPR008939; Muramidase_bact. DR Pfam; PF01086; Clathrin_lg_ch; 1. DR PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; FALSE_NEG. DR PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; FALSE_NEG. KW Coated pits; Calcium-binding. FT DOMAIN 68 79 GLY/SER/THR-RICH. FT DOMAIN 96 158 INVOLVED IN BINDING CLATHRIN HEAVY FT CHAIN (BY SIMILARITY). FT CONFLICT 218 219 ST -> RHLGSFNYALA (IN REF. 1). SQ SEQUENCE 219 AA; 23840 MW; 8B764209C2D0CCA4 CRC64; MDFGDDFAAK EDVDPAAEFL AREQSALGDL EAEITGGSAS APPAASTDEG LGELLGGTAS EGDLLSAGGT GGLESSTGSF EVIGGESNEP VGISGPPPSR EEPEKIRKWR EEQKQRLEEK DIEEERKKEE LRQQSKKELD DWLRQIGESI SKTKLASRNA EKQAATLENG TIEPGTEWER IAKLCDFNPK VNKAGKDVSR MRSIYLHLKQ NPIQVQKST // ID CLH_DROME STANDARD; PRT; 1678 AA. AC P29742; Q9VXN6; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Clathrin heavy chain. GN CHC OR CG9012. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93387666; PubMed=8375651; RA Bazinet C., Katzen A.L., Morgan M., Mahowald A.P., Lemmon S.K.; RT "The Drosophila clathrin heavy chain gene: clathrin function is RT essential in a multicellular organism."; RL Genetics 134:1119-1134(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CLATHRIN IS THE MAJOR PROTEIN OF THE POLYHEDRAL COAT OF CC COATED PITS AND VESICLES. CC -!- SUBUNIT: CLATHRIN TRISKELIONS, COMPOSED OF 3 HEAVY CHAINS AND 3 CC LIGHT CHAINS, ARE THE BASIC SUBUNITS OF THE CLATHRIN COAT. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC FACE OF COATED PITS AND CC VESICLES. CC -!- DOMAIN: THE C-TERMINAL THIRD OF THE HEAVY CHAINS FORMS THE HUB OF CC THE TRISKELION. THIS REGION CONTAINS THE TRIMERIZATION DOMAIN AND CC THE LIGHT-CHAIN BINDING DOMAIN INVOLVED IN THE ASSEMBLY OF THE CC CLATHRIN LATTICE. CC -!- SIMILARITY: BELONGS TO THE CLATHRIN HEAVY CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z14133; CAA78507.1; -. DR EMBL; AE003500; AAF48522.1; -. DR PIR; S52588; S52588. DR HSSP; P11442; 1BPO. DR FlyBase; FBgn0000319; Chc. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR InterPro; IPR008938; ARM. DR InterPro; IPR001473; Clathrin_propel. DR InterPro; IPR000547; Clathrin_repeat. DR InterPro; IPR008941; TPR-like. DR Pfam; PF00637; Clathrin; 7. DR Pfam; PF01394; Clathrin_propel; 7. DR SMART; SM00299; CLH; 7. KW Coated pits. FT BINDING 1334 1643 LIGHT CHAIN (BY SIMILARITY). FT DOMAIN 1552 1677 TRIMERIZATION (BY SIMILARITY). SQ SEQUENCE 1678 AA; 191176 MW; 73CAF8631BEE9BA3 CRC64; MTQPLPIRFQ EHLQLTNVGI NANSFSFSTL TMESDKFICV REKVNDTAQV VIIDMNDATN PTRRPISADS AIMNPASKVI ALKAQKTLQI FNIEMKSKMK AHTMNEDVVF WKWISLNTLA LVTETSVFHW SMEGDSMPQK MFDRHSSLNG CQIINYRCNA SQQWLLLVGI SALPSRVAGA MQLYSVERKV SQAIEGHAAS FATFKIDANK EPTTLFCFAV RTATGGKLHI IEVGAPPNGN QPFAKKAVDV FFPPEAQNDF PVAMQVSAKY DTIYLITKYG YIHLYDMETA TCIYMNRISA DTIFVTAPHE ASGGIIGVNR KGQVLSVTVD EEQIIPYINT VLQNPDLALR MAVRNNLAGA EDLFVRKFNK LFTAGQYAEA AKVAALAPKA ILRTPQTIQR FQQVQTPAGS TTPPLLQYFG ILLDQGKLNK FESLELCRPV LLQGKKQLCE KWLKEEKLEC SEELGDLVKA SDLTLALSIY LRANVPNKVI QCFAETGQFQ KIVLYAKKVN YTPDYVFLLR SVMRSNPEQG AGFASMLVAE EEPLADINQI VDIFMEHSMV QQCTAFLLDA LKHNRPAEGA LQTRLLEMNL MSAPQVADAI LGNAMFTHYD RAHIAQLCEK AGLLQRALEH YTDLYDIKRA VVHTHMLNAE WLVSFFGTLS VEDSLECLKA MLTANLRQNL QICVQIATKY HEQLTNKALI DLFEGFKSYD GLFYFLSSIV NFSQDPEVHF KYIQAACKTN QIKEVERICR ESNCYNPERV KNFLKEAKLT DQLPLIIVCD RFDFVHDLVL YLYRNNLQKY IEIYVQKVNP SRLPVVVGGL LDVDCSEDII KNLILVVKGQ FSTDELVEEV EKRNRLKLLL PWLESRVHEG CVEPATHNAL AKIYIDSNNN PERYLKENQY YDSRVVGRYC EKRDPHLACV AYERGLCDRE LIAVCNENSL FKSEARYLVG RRDAELWAEV LSESNPYKRQ LIDQVVQTAL SETQDPDDIS VTVKAFMTAD LPNELIELLE KIILDSSVFS DHRNLQNLLI LTAIKADRTR VMDYINRLEN YDAPDIANIA ISNQLYEEAF AIFKKFDVNT SAIQVLIDQV NNLERANEFA ERCNEPAVWS QLAKAQLQQG LVKEAIDSYI KADDPSAYVD VVDVASKVES WDDLVRYLQM ARKKARESYI ESELIYAYAR TGRLADLEEF ISGPNHADIQ KIGNRCFSDG MYDAAKLLYN NVSNFARLAI TLVYLKEFQG AVDSARKANS TRTWKEVCFA CVDAEEFRLA QMCGLHIVVH ADELEDLINY YQNRGYFDEL IALLESALGL ERAHMGMFTE LAILYSKFKP SKMREHLELF WSRVNIPKVL RAAESAHLWS ELVFLYDKYE EYDNAVLAMM AHPTEAWREG HFKDIITKVA NIELYYKAIE FYLDFKPLLL NDMLLVLAPR MDHTRAVSYF SKTGYLPLVK PYLRSVQSLN NKAINEALNG LLIDEEDYQG LRNSIDGFDN FDNIALAQKL EKHELTEFRR IAAYLYKGNN RWKQSVELCK KDKLYKDAME YAAESCKQDI AEELLGWFLE RDAYDCFAAC LYQCYDLLRP DVILELAWKH KIVDFAMPYL IQVLREYTTK VDKLELNEAQ REKEDDSTEH KNIIQMEPQL MITAGPAMGI PPQYAQNYPP GAATVTAAGG RNMGYPYL // ID CLOC_DROME STANDARD; PRT; 1023 AA. AC O61735; O76342; O77137; Q9VSB0; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Circadian locomoter output cycles Kaput protein (dCLOCK) (dPAS1). GN CLK OR JRK OR CLOCK OR PAS1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=98279147; PubMed=9616122; RA Darlington T.K., Wager-Smith K., Ceriani M.F., Staknis D., Gekakis N., RA Steeves T.D.L., Weitz C.J., Takahashi J.S., Kay S.A.; RT "Closing the circadian loop: CLOCK-induced transcription of its own RT inhibitors per and tim."; RL Science 280:1599-1603(1998). RN [2] RP SEQUENCE FROM N.A., AND MUTAGENESIS. RC TISSUE=Head; RX MEDLINE=98292177; PubMed=9630223; RA Allada R., White N.E., So W.V., Hall J.C., Rosbash M.; RT "A mutant Drosophila homolog of mammalian Clock disrupts circadian RT rhythms and transcription of period and timeless."; RL Cell 93:791-804(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98414630; PubMed=9742131; RA Bae K., Lee C., Sidote D., Chuang K.-Y., Edery I.; RT "Circadian regulation of a Drosophila homolog of the mammalian clock RT gene: PER and TIM function as positive regulators."; RL Mol. Cell. Biol. 18:6142-6151(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CIRCADIAN REGULATOR THAT ACTS AS A TRANSCRIPTION FACTOR CC AND GENERATES A RYTHMIC OUTPUT WITH A PERIOD OF ABOUT 24 HOURS. CC OSCILLATES IN ANTIPHASE TO THE CYCLING OBSERVED FOR PERIOD (PER) CC AND TIMELESS (TIM). ACCORDING TO REF.3, REACHES PEAK ABUNDANCE CC WITHIN SEVERAL HOURS OF THE DARK-LIGHT TRANSITION AT ZT0 CC (ZEITGEBER 0), WHEREAS REF.1 DESCRIBES BIMODAL OSCILLATING CC EXPRESSION WITH MAXIMUM AT ZT5 AND ZT23. CLOCK-CYCLE HETERODIMERS CC ACTIVATE CYCLING TRANSCRIPTION OF PER AND TIM BY BINDING TO THE E- CC BOX (3'-CACGTG-5') PRESENT IN THEIR PROMOTERS. ONCE INDUCED, CC PERIOD AND TIMELESS BLOCK CLOCK'S ABILITY TO TRANSACTIVATE THEIR CC PROMOTERS. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. FORMS A HETERODIMER WITH CYCLE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED. FOUND IN HEAD, BODY, AND CC APPENDAGE FRACTIONS. CC -!- DOMAIN: CONTAINS THREE POLYGLUTAMINE REPEATS WHICH COULD CC CORRESPOND TO THE TRANSACTIVATION DOMAIN. THE LENGTH OF THE CC REPEATS IS POLYMORPHIC. IN THE ARRYTHMIC MUTANT JRK, DELETION OF CC THIS REGION LEADS TO THE LOSS OF CIRCADIAN RHYTHMICITY AND ALTERED CC LIGHT RESPONSE. CC -!- POLYMORPHISM: THE VARIABILITY IN LENGTH OF THE POLYGLUTAMINE CC STRETCH IS DUE TO POLYMORPHISM OF THIS REGION. VARIANT B ENCODES CC TWO CONCEPTUAL PROTEINS, THE FIRST CONSISTS ONLY OF THE BHLH CC DOMAIN, THE OTHER CONSISTS OF THE PAS-1 AND ALL C-TERMINAL CC DOMAINS. VARIANT B IS EXPRESSED WEAKLY AT ALL THE TIMES OF THE CC DAY, AND IT CYCLES IN PHASE WITH THE FULL-LENGTH FORM. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PAS (PER-ARNT-SIM) DIMERIZATION DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PAS-ASSOCIATED C-TERMINAL (PAC) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF067207; AAD10630.1; -. DR EMBL; AF065133; AAC39101.1; -. DR EMBL; AF069997; AAC62234.1; -. DR EMBL; AE003557; AAF50516.1; -. DR PIR; T13068; T13068. DR PIR; T13071; T13071. DR FlyBase; FBgn0023076; Clk. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0008062; P:eclosion rhythm; NAS. DR GO; GO:0045475; P:locomotor rhythm; NAS. DR GO; GO:0045893; P:positive regulation of transcription, DNA-d...; IGI. DR GO; GO:0045187; P:regulation of sleep; IMP. DR GO; GO:0008341; P:response to cocaine (sensu Insecta); NAS. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR001067; Nuc_translocat. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS_domain. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00785; PAC; 1. DR Pfam; PF00989; PAS; 1. DR PRINTS; PR00785; NCTRNSLOCATR. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR PROSITE; PS50888; HLH; 1. DR PROSITE; PS50112; PAS; 1. KW Transcription regulation; Nuclear protein; Repeat; Biological rhythms; KW DNA-binding; Polymorphism. FT DNA_BIND 12 24 BASIC DOMAIN. FT DOMAIN 25 62 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 84 154 PAS 1. FT DOMAIN 251 317 PAS 2. FT DOMAIN 548 559 POLY-GLN. FT DOMAIN 766 769 POLY-GLN. FT DOMAIN 794 836 POLY-GLN. FT DOMAIN 874 877 POLY-ASN. FT DOMAIN 887 895 POLY-ASN. FT DOMAIN 953 963 POLY-GLN. FT DOMAIN 776 1023 IMPLICATED IN THE CIRCADIAN RHYTHMICITY. FT VARIANT 816 823 MISSING (IN VARIANT B). FT CONFLICT 12 12 K -> KSFLC (IN REF. 3). FT CONFLICT 32 32 N -> D (IN REF. 3). FT CONFLICT 128 128 N -> K (IN REF. 2). FT CONFLICT 555 555 N -> S (IN REF. 1). FT CONFLICT 605 605 I -> L (IN REF. 3 AND 4). FT CONFLICT 912 912 Y -> C (IN REF. 3 AND 4). SQ SEQUENCE 1023 AA; 115751 MW; 514374CBC050DAFB CRC64; MDDESDDKDD TKRKSRNLSE KKRRDQFNSL VNDLSALIST SSRKMDKSTV LKSTIAFLKN HNEATDRSKV FEIQQDWKPA FLSNDEYTHL MLESLDGFMM VFSSMGSIFY ASESITSQLG YLPQDLYNMT IYDLAYEMDH EALLNIFMNP TPVIEPRQTD ISSSNQITFY THLRRGGMEK VDANAYELVK FVGYFRNDTN TSTGSSSEVS NGSNGQPAVL PRIFQQNPNA EVDKKLVFVG TGRVQNPQLI REMSIIDPTS NEFTSKHSME WKFLFLDHRA PPIIGYMPFE VLGTSGYDYY HFDDLDSIVA CHEELRQTGE GKSCYYRFLT KGQQWIWLQT DYYVSYHQFN SKPDYVVCTH KVVSYAEVLK DSRKEGQKSG NSNSITNNGS SKVIASTGTS SKSASATTTL RDFELSSQNL DSTLLGNSLA SLGTETAATS PAVDSSPMWS ASAVQPSGSC QINPLKTSRP ASSYGNISST GISPKAKRKC YFYNNRGNDS DSTSMSTDSV TSRQSMMTHV SSQSQRQRSH HREHHRENHH NQSHHHMQQQ QQHQNQQQQH QQHQQLQQQL QHTVGTPKMV PLLPIASTQI MAGNACQFPQ PAYPIASPQL VAPTFLEPPQ YLTAIPMQPV IAPFPVAPVL SPLPVQSQTD MLPDTVVMTP TQSQLQDQLQ RKHDELQKLI LQQQNELRIV SEQLLLSRYT YLQPMMSMGF APGNMTAAAV GNLGASGQRG LNFTGSNAVQ PQFNQYGFAL NSEQMLNQQD QQMMMQQQQN LHTQHQHNLQ QQHQSHSQLQ QHTQQQHQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ LQLQQQNDIL LREDIDDIDA FLNLSPLHSL GSQSTINPFN SSSNNNNQSY NGGSNLNNGN QNNNNRSSNP PQNNNEDSLL SYMQMATESS PSINFHMGIS DDGSETQSED NKMMHTSGSN LVQQQQQQQQ QQQILQQHQQ QSNSFFSSNP FLNSQNQNQN QLPNDLEILP YQMSQEQSQN LFNSPHTAPG SSQ // ID CLP1_DROME STANDARD; PRT; 130 AA. AC P02839; Q24290; Q9V4S9; DT 21-JUL-1986 (Rel. 01, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval cuticle protein I precursor. GN LCP1 OR CG11650. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=Oregon-R, and Canton-S; TISSUE=Larva; RX MEDLINE=83103095; PubMed=6817923; RA Snyder M., Hunkapiller M., Yuen D., Silvert D., Fristrom J., RA Davidson N.; RT "Cuticle protein genes of Drosophila: structure, organization and RT evolution of four clustered genes."; RL Cell 29:1027-1040(1982). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE LARVAL CUTICLE. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00202; CAA23487.1; -. DR EMBL; AE003837; AAF59096.1; -. DR PIR; A03328; UCFF1L. DR PIR; A25299; A25299. DR FlyBase; FBgn0002531; Lcp1. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 16 FT CHAIN 17 130 LARVAL CUTICLE PROTEIN I. FT DOMAIN 102 108 PRO-RICH. FT CONFLICT 37 37 Q -> R (IN REF. 1). SQ SEQUENCE 130 AA; 13921 MW; 0A20F5B9D2DC3F4B CRC64; MFKFVMICAV LGLAVANPPV PHSLGRSEDV HADVLSQSDD VRADGFDSSL HTSNGIEQAA SGDAHGNIHG NFGWISPEGE HVEVKYVANE NGYQPSGAWI PTPPPIPEAI ARAVAWLESH PPAPEHPRHH // ID CLP2_DROME STANDARD; PRT; 126 AA. AC P07187; Q9V4T0; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval cuticle protein II precursor. GN LCP2 OR CG8697. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=Oregon-R, and Canton-S; TISSUE=Larva; RX MEDLINE=83103095; PubMed=6817923; RA Snyder M., Hunkapiller M., Yuen D., Silvert D., Fristrom J., RA Davidson N.; RT "Cuticle protein genes of Drosophila: structure, organization and RT evolution of four clustered genes."; RL Cell 29:1027-1040(1982). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE LARVAL CUTICLE. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00203; CAA23488.1; -. DR EMBL; AE003837; AAF59095.2; -. DR PIR; B25299; B25299. DR FlyBase; FBgn0002533; Lcp2. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 16 FT CHAIN 17 126 LARVAL CUTICLE PROTEIN II. FT DOMAIN 97 103 PRO-RICH. SQ SEQUENCE 126 AA; 13488 MW; 0246143E069CCE1E CRC64; MFKFVMILAV VGVATALAPV SRSDDVHADV LSRSDDVRAD GFDSSLHTSN GIEQAASGDA HGNIHGNFGW ISPEGEHVEV KYVANENGYQ PSGAWIPTPP PIPEAIARAV AWLESHPPAP EHPRHH // ID CLP3_DROME STANDARD; PRT; 112 AA. AC P07188; Q9V4T1; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval cuticle protein III precursor. GN LCP3 OR CG2043. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=Oregon-R, and Canton-S; TISSUE=Larva; RX MEDLINE=83103095; PubMed=6817923; RA Snyder M., Hunkapiller M., Yuen D., Silvert D., Fristrom J., RA Davidson N.; RT "Cuticle protein genes of Drosophila: structure, organization and RT evolution of four clustered genes."; RL Cell 29:1027-1040(1982). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE LARVAL CUTICLE. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00203; CAA23489.1; -. DR EMBL; AE003837; AAF59094.1; -. DR PIR; C25299; C25299. DR FlyBase; FBgn0002534; Lcp3. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 16 FT CHAIN 17 112 LARVAL CUTICLE PROTEIN III. FT DOMAIN 89 95 PRO-RICH. SQ SEQUENCE 112 AA; 11857 MW; 2C6AC731B77291A6 CRC64; MFKILLVCSL AALVAANANV EVKELVNDVQ PDGFVSKLVL DDGSASSATG DIHGNIDGVF EWISPEGVHV RVSYKADENG YQPQSDLLPT PPPIPAAILK AIAYIEANPS KN // ID CLP4_DROME STANDARD; PRT; 112 AA. AC P07189; Q9V4T2; DT 01-APR-1988 (Rel. 07, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval cuticle protein IV precursor. GN LCP4 OR CG2044. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=Oregon-R, and Canton-S; TISSUE=Larva; RX MEDLINE=83103095; PubMed=6817923; RA Snyder M., Hunkapiller M., Yuen D., Silvert D., Fristrom J., RA Davidson N.; RT "Cuticle protein genes of Drosophila: structure, organization and RT evolution of four clustered genes."; RL Cell 29:1027-1040(1982). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE LARVAL CUTICLE. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00203; CAA23490.1; -. DR EMBL; AE003837; AAF59093.1; -. DR PIR; D25299; D25299. DR FlyBase; FBgn0002535; Lcp4. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 16 FT CHAIN 17 112 LARVAL CUTICLE PROTEIN IV. FT DOMAIN 89 95 PRO-RICH. SQ SEQUENCE 112 AA; 11979 MW; FE2AC596EC8BFEDB CRC64; MFKILLVCAL VALVAANENP EVKELVNDVQ ADGFVSKLVL DNGSAASATG DVHGNIDGVF EWVSPEGEHV RVSYKADENG YQPQSDLLPT PPPIPEAILK AIAYIQAHPS KE // ID CLP8_DROME STANDARD; PRT; 105 AA. AC P92201; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval cuticle protein VIII precursor. GN (LCP65AG1 OR LCP8 OR DCP8-ALPHA OR CG10530) AND GN (LCP65AG2 OR LCP8 OR DCP8-BETA OR CG10534). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1; RX MEDLINE=98043412; PubMed=9383064; RA Charles J.-P., Chihara C., Nejad S., Riddiford L.M.; RT "A cluster of cuticle genes of Drosophila at 65A: sequence, structure RT and evolution."; RL Genetics 147:1213-1224(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 19-28. RC STRAIN=Oregon-R; TISSUE=Larva; RX MEDLINE=98318806; PubMed=9654737; RA Charles J.-P., Chihara C., Nejad S., Riddiford L.M.; RT "Identification of proteins and developmental expression of RNAs RT encoded by the 65A cuticle protein gene cluster in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 28:131-138(1998). CC -!- FUNCTION: COMPONENT OF THE CUTICLE OF THE LARVA. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003563; AAF50692.1; -. DR EMBL; AE003563; AAF50693.1; -. DR EMBL; U84753; AAB88071.1; -. DR EMBL; U84754; AAB88072.1; -. DR EMBL; AY061536; AAL29084.1; -. DR FlyBase; FBgn0020638; Lcp65Ag1. DR FlyBase; FBgn0020637; Lcp65Ag2. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PRINTS; PR00947; CUTICLE. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 18 FT CHAIN 19 105 LARVAL CUTICLE PROTEIN VIII. SQ SEQUENCE 105 AA; 11194 MW; F23DA9A5BAB21D2F CRC64; MKFLIVFVAL FAVALAAPAA EEPTIVRSES DVGPESFKYD WETSDGQAAQ AVGQLNDIGT ENEAISVSGS YRFIADDGQT YQVNYIADKN GFQPQGAHLP VAPVA // ID CLP9_DROME STANDARD; PRT; 92 AA. AC P82384; Q9W109; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval cuticle protein IX precursor. GN LCP9 OR CG16914. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 17-26. RC STRAIN=Oregon-R; TISSUE=Larva; RX MEDLINE=98318806; PubMed=9654737; RA Charles J.-P., Chihara C., Nejad S., Riddiford L.M.; RT "Identification of proteins and developmental expression of RNAs RT encoded by the 65A cuticle protein gene cluster in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 28:131-138(1998). CC -!- FUNCTION: COMPONENT OF THE CUTICLE OF THE LARVA. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003465; AAF47269.1; -. DR FlyBase; FBgn0025578; Lcp9. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 16 FT CHAIN 17 92 LARVAL CUTICLE PROTEIN IX. SQ SEQUENCE 92 AA; 10237 MW; D661B07B7387DDC8 CRC64; MKFVIVLACL LAVVFANEEA DVVKSDSEVN LLDFNYAYEL SNHIRAVQTG ALKEHDNWVV SGEYEYVAPN GKTVKVVYTA DETGYHPKVV EA // ID CLS1_DROME STANDARD; PRT; 978 AA. AC Q9V498; Q9GP64; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calsyntenin-1 precursor. GN CALS OR CLSTN1 OR CG11059. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=21109376; PubMed=11161476; RA Vogt L., Schrimpf S.P., Meskenaite V., Frischknecht R., Kinter J., RA Leone D.P., Ziegler U., Sonderegger P.; RT "Calsyntenin-1, a proteolytically processed postsynaptic membrane RT protein with a cytoplasmic calcium-binding domain."; RL Mol. Cell. Neurosci. 17:151-166(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY MODULATE CALCIUM-MEDIATED POSTSYNAPTIC SIGNALS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- DOMAIN: BINDS SYNAPTIC CA(2+) WITH ITS CYTOPLASMIC DOMAIN (BY CC SIMILARITY). CC -!- SIMILARITY: CONTAINS 2 CADHERIN DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ289018; CAC17749.1; -. DR EMBL; AE003846; AAF59384.2; -. DR EMBL; AY121644; AAM51971.1; -. DR FlyBase; FBgn0039928; cals. DR GO; GO:0005576; C:extracellular; ISS. DR GO; GO:0045211; C:postsynaptic membrane; ISS. DR GO; GO:0005509; F:calcium ion binding; ISS. DR GO; GO:0007268; P:synaptic transmission; ISS. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR008985; ConA_like_lec_gl. DR Pfam; PF00028; cadherin; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 2. DR PROSITE; PS00232; CADHERIN_1; FALSE_NEG. DR PROSITE; PS50268; CADHERIN_2; 2. KW Cell adhesion; Glycoprotein; Transmembrane; Calcium; Calcium-binding; KW Repeat; Signal. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 978 CALSYNTENIN-1. FT DOMAIN 27 876 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 877 897 POTENTIAL. FT DOMAIN 898 978 CYTOPLASMIC (POTENTIAL). FT DOMAIN 37 143 CADHERIN 1. FT DOMAIN 144 249 CADHERIN 2. FT CARBOHYD 53 53 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 304 304 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 486 486 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 608 608 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 823 823 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 978 AA; 110492 MW; 0FED6AE787A4299C CRC64; MTFHKTFGYG CIVLICFELL FAGVETSSEN DDEYLTQKEI ILEKSYHGLI RENETLVEIT PLIKVNEEKI CNFHILKKPY HEIPFKIELV NNLGILKARR TLNCENRKSY HFEICAIYCD GTPSNTANVH ITVIDVNEYA PTFLEPSYVI EVDEGRLYNE ILRVEASDKD CTPLFGDVCK YEILNNDEPF SIDNEGSIKN TEPLSHKASH NHILSVVAYD CAMKESAPIM VSIKVRRVCE TKFVGMPERI DYTSGSTESL QLFPNARLDL CDISCKNEED LRIHSSIALK TKHISFGCDR DISNCTSGQK VKDLLPHGAE WTKELSYDEG LEPIFHFDGS TGVVVPATVI DHYDFSSQPF SILTLFRHNS QVEINKHVKE HIVCSADDHK MNRHHMALFV RNCRLIFLLR KNFNEGDLNI FSPAEWRWKI PEVCDNEWHH YVLNVEDSSK VDLFIDGVRF ENSIENRHSN PEVIDDWPLH AAHGVNTSLA IGACYQSLEN RLKHGFNGDI SEVKVSLNSV LTAEDIKCGT TCAEHLLAPK PLQSNNEKSY SDNSQIKENI EMNEIYISAK NKHDIEQFMR KVQYINTKQK PTVGRRNIEV LTTLNCKNES SLRLPPIETY IMVNEPIAPL GIDIDVVSAS LETSDLTPPS YSPKIAISGT SNKLVSYQEI KLGVHILEKT CIDSVSKNNG KLEEKNHIDS CSVVVFPSLN PDHEDIKIDG DESLSSSMDI KTNINKDGVE MIGKDTISNY INVLRSLVYS NKKPAYYLNR VFKLSCAQQS SQYKSGEYTL TLTVLHPKQT LFKSTNVLPS SLSKVNFIGN TDNETSFHRN SGSVNGNDNN QPTESKVYSY SLLHTNNVQE PKSHIHSFIH KAEGSHVTML IILVSVFLAV LLCGVSIARL KNNQKYIEHH QPCPKISDDG LIWDDSALTI TINPMQADVT SDASSESENS ESEDEEALKD GFTHINQLEW DNSNIFQQ // ID CMC1_DROME STANDARD; PRT; 695 AA. AC Q9VA73; Q95TN5; Q9U5V8; Q9VA72; Q9VA74; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calcium-binding mitochondrial carrier Aralar1. GN ARALAR1 OR CG2139. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Ovary; RX MEDLINE=20115110; PubMed=10642534; RA Del Arco A., Agudo M., Satrustegui J.; RT "Characterization of a second member of the subfamily of calcium- RT binding mitochondrial carriers expressed in human non-excitable RT tissues."; RL Biochem. J. 345:725-732(2000). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CALCIUM-DEPENDENT MITOCHONDRIAL SOLUTE CARRIER (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; CC IsoId=Q9VA73-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9VA73-2; Sequence=VSP_003266; CC Name=3; CC IsoId=Q9VA73-3; Sequence=VSP_003265; CC -!- SIMILARITY: BELONGS TO THE MITOCHONDRIAL CARRIER FAMILY. CC -!- SIMILARITY: CONTAINS 4 EF-HAND CALCIUM-BINDING DOMAINS. CC -!- SIMILARITY: CONTAINS 3 SOLCAR REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y18197; CAB62169.1; -. DR EMBL; AE003774; AAF57048.1; -. DR EMBL; AE003774; AAF57049.1; -. DR EMBL; AE003774; AAF57050.2; -. DR EMBL; AY058654; AAL13883.1; -. DR HSSP; P02593; 1CDM. DR FlyBase; FBgn0028646; aralar1. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR002067; Mit_carrier. DR InterPro; IPR001993; Mitoch_carrier. DR Pfam; PF00036; efhand; 3. DR Pfam; PF00153; mito_carr; 3. DR PRINTS; PR00926; MITOCARRIER. DR SMART; SM00054; EFh; 3. DR PROSITE; PS00018; EF_HAND; 1. DR PROSITE; PS50920; SOLCAR; 3. KW Mitochondrion; Inner membrane; Repeat; Transmembrane; Transport; KW Calcium-binding; Alternative splicing. FT TRANSMEM 346 363 1 (POTENTIAL). FT TRANSMEM 406 425 2 (POTENTIAL). FT TRANSMEM 449 462 3 (POTENTIAL). FT TRANSMEM 498 517 4 (POTENTIAL). FT TRANSMEM 537 554 5 (POTENTIAL). FT TRANSMEM 594 613 6 (POTENTIAL). FT CA_BIND 84 95 EF-HAND 1. FT CA_BIND 118 129 EF-HAND 2. FT DOMAIN 157 168 ANCESTRAL CALCIUM SITE 3. FT CA_BIND 189 200 EF-HAND 4. FT REPEAT 340 431 SOLCAR 1. FT REPEAT 439 523 SOLCAR 2. FT REPEAT 531 619 SOLCAR 3. FT VARSPLIC 1 52 Missing (in isoform 3). FT /FTId=VSP_003265. FT VARSPLIC 3 22 MHIPFPFNWIPTLPVARCQE -> LTKSLPN (in FT isoform 2). FT /FTId=VSP_003266. FT CONFLICT 356 357 GA -> AP (IN REF. 1). FT CONFLICT 556 556 V -> A (IN REF. 1). FT CONFLICT 653 653 V -> L (IN REF. 1). SQ SEQUENCE 695 AA; 76753 MW; 8EC93D92031F5B77 CRC64; MPMHIPFPFN WIPTLPVARC QESPSLLKRA GTEKLREVFL KYASIQKNGE HYMTSEDFVR KFLGLFSESA FNDESVRLLA NIADTSKDGL ISFSEFQAFE GLLCTPDALY RTAFQLFDRK GNGTVSYADF ADVVQKTELH SKIPFSLDGP FIKRYFGDKK QRLINYAEFT QLLHDFHEEH AMEAFRSKDP AGTGFISPLD FQDIIVNVKR HLLTPGVRDN LVSVTEGHKV SFPYFIAFTS LLNNMELIKQ VYLHATEGSR TDMITKDQIL LAAQTMSQIT PLEIDILFHL AGAVHQAGRI DYSDLSNIAP EHYTKHMTHR LAEIKAVESP ADRSAFIQVL ESSYRFTLGS FAGAVGATVV YPIDLVKTRM QNQRAGSYIG EVAYRNSWDC FKKVVRHEGF MGLYRGLLPQ LMGVAPEKAI KLTVNDLVRD KLTDKKGNIP TWAEVLAGGC AGASQVVFTN PLEIVKIRLQ VAGEIASGSK IRAWSVVREL GLFGLYKGAR ACLLRDVPFS AIYFPTYAHT KAMMADKDGY NHPLTLLAAG AIAGVPAASL VTPADVIKTR LQVVARSGQT TYTGVWDATK KIMAEEGPRA FWKGTAARVF RSSPQFGVTL VTYELLQRLF YVDFGGTQPK GSEAHKITTP LEQAAASVTT ENVDHIGGYR AAVPLLAGVE SKFGLYLPRF GRGVTAASPS TATGS // ID CNA1_DROME STANDARD; PRT; 777 AA. AC P12252; DT 01-OCT-1989 (Rel. 12, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE cAMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Learning/ DE memory process protein) (Dunce protein). GN DNC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., REVISIONS, CATALYTIC ACTIVITY, AND ALTERNATIVE RP SPLICING. RC STRAIN=Canton-S; RX MEDLINE=92085274; PubMed=1660926; RA Qiu Y.H., Chen C.-N., Malone T., Richter L., Beckendorf S.K., RA Davis R.L.; RT "Characterization of the memory gene dunce of Drosophila RT melanogaster."; RL J. Mol. Biol. 222:553-565(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORM VII). RX MEDLINE=87092243; PubMed=3025834; RA Chen C.-N., Denome S., Davis R.L.; RT "Molecular analysis of cDNA clones and the corresponding genomic RT coding sequences of the Drosophila dunce+ gene, the structural gene RT for cAMP phosphodiesterase."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9313-9317(1986). CC -!- FUNCTION: VITAL FOR FEMALE FERTILITY. CC -!- CATALYTIC ACTIVITY: ADENOSINE 3',5'-CYCLIC PHOSPHATE + H(2)O = CC ADENOSINE 5'-PHOSPHATE. CC -!- PATHWAY: CYCLIC NUCLEOTIDE METABOLISM. CC -!- SUBUNIT: MONOMER. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Comment=Additional isoforms seem to exist; CC Name=II; CC IsoId=P12252-1; Sequence=Displayed; CC Note=Isoform III is produced by alternative initiation at CC Met-137 of isoform II; CC Name=I; CC IsoId=P12252-2; Sequence=VSP_004583, VSP_004584; CC Name=IV; CC IsoId=P12252-3; Sequence=VSP_004585, VSP_004586; CC Name=V; CC IsoId=P12252-4; Sequence=VSP_004588; CC Name=VI; CC IsoId=P12252-5; Sequence=VSP_004589; CC Name=VII; CC IsoId=P12252-6; Sequence=VSP_004587; CC Event=Alternative initiation; CC Comment=2 isoforms, II (shown here) and III, are produced by CC alternative initiation at Met-1 and Met-137; CC -!- SIMILARITY: BELONGS TO THE CYCLIC NUCLEOTIDE PHOSPHODIESTERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55167; CAA38960.1; ALT_SEQ. DR EMBL; X55168; CAA38960.1; JOINED. DR EMBL; X55169; CAA38960.1; JOINED. DR EMBL; X55170; CAA38960.1; JOINED. DR EMBL; X55171; CAA38960.1; JOINED. DR EMBL; X55172; CAA38960.1; JOINED. DR EMBL; X55173; CAA38960.1; JOINED. DR EMBL; X55174; CAA38960.1; JOINED. DR EMBL; X55175; CAA38960.1; JOINED. DR EMBL; M14982; AAC34201.1; -. DR EMBL; M14978; AAC34201.1; JOINED. DR EMBL; M14979; AAC34201.1; JOINED. DR EMBL; M14980; AAC34201.1; JOINED. DR EMBL; M14981; AAC34201.1; JOINED. DR PIR; S65543; S65543. DR FlyBase; FBgn0000479; dnc. DR GO; GO:0019933; P:cAMP-mediated signaling; NAS. DR GO; GO:0007612; P:learning; NAS. DR GO; GO:0045475; P:locomotor rhythm; NAS. DR GO; GO:0000003; P:reproduction; NAS. DR GO; GO:0045473; P:response to ethanol (sensu Insecta); NAS. DR InterPro; IPR003607; Met_phsphohydro. DR InterPro; IPR002073; PDEase. DR Pfam; PF00233; PDEase; 1. DR PRINTS; PR00387; PDIESTERASE1. DR SMART; SM00471; HDc; 1. DR PROSITE; PS00126; PDEASE_I; 1. KW Hydrolase; cAMP; Alternative splicing; Alternative initiation. FT CHAIN 1 777 CAMP-DEPENDENT 3',5'-CYCLIC FT PHOSPHODIESTERASE, ISOFORM II. FT CHAIN 137 777 CAMP-DEPENDENT 3',5'-CYCLIC FT PHOSPHODIESTERASE, ISOFORM III. FT INIT_MET 137 137 FOR ISOFORM III. FT DOMAIN 498 503 PART OF CAMP BINDING SITE (BY SIMILARITY FT TO MAMMALIAN REGULATORY SUBUNIT OF TYPE 2 FT CAMP DEPENDENT PROTEIN KINASE). FT DOMAIN 728 776 GLY/THR-RICH. FT VARSPLIC 1 63 Missing (in isoform I). FT /FTId=VSP_004583. FT VARSPLIC 64 93 GLHDMLKRAQGRSPLSPRISFPGSDSDLFG -> MQAEQGS FT IGDLQKYHSRYLKNRRHTLANVR (in isoform I). FT /FTId=VSP_004584. FT VARSPLIC 1 75 Missing (in isoform IV). FT /FTId=VSP_004585. FT VARSPLIC 76 93 SPLSPRISFPGSDSDLFG -> MVCSFCCCCYNFRNSPSR FT (in isoform IV). FT /FTId=VSP_004586. FT VARSPLIC 1 415 Missing (in isoform VII). FT /FTId=VSP_004587. FT VARSPLIC 152 164 Missing (in isoform V). FT /FTId=VSP_004588. FT VARSPLIC 201 202 Missing (in isoform VI). FT /FTId=VSP_004589. SQ SEQUENCE 777 AA; 85164 MW; 95129B23C2CFD916 CRC64; MQLSMSKLGL QQSSSILISK SAETIEMKSS SAGMRTQLTL SGGFLAPPGN RKITILSPIH APPGLHDMLK RAQGRSPLSP RISFPGSDSD LFGFDVENGQ GARSPLEGGS PSAGLVLQNL PQRRESFLYR SDSDFEMSPK SMSRNSSIAS ERFKEQEASI LVDRSHGEDL IVTPFAQILA SLRSVRNNLL SLTNVPASNK SRRPNQSSSA SRSGNPPGAP LSQGEEAYTR LATDTIEELD WCLDQLETIQ THRSVSDMAS LKFKRMLNKE LSHFSESSRS GNQISEYICS TFLDKQQEFD LPSLRVEDNP ELVAANAAAG QQSAGQYARS RSPRGPPMSQ ISGVKRPLSH TNSFTGERLP TFGVETPREN ELGTLLGELD TWGIQIFSIG EFSVNRPLTC VAYTIFQSRE LLTSLMIPPK TFLNFMSTLE DHYVKDNPFH NSLHAADVTQ STNVLLNTPA LEGVFTPLEV GGALFAACIH DVDHPGLTNQ FLVNSSSELA LMYNDESVLE NHHLAVAFKL LQNQGCDIFC NMQKKQRQTL RKMVIDIVLS TDMSKHMSLL ADLKTMVETK KVAGSGVLLL DNYTDRIQVL ENLVHCADLS NPTKPLPLYK RWVALLMEEF FLQGDKERES GMDISPMCDR HNATIEKSQV GFIDYIVHPL WETWASLVHP DAQDILDTLE ENRDYYQSMI PPSPPPSGVD ENPQEDRIRF QVTLEESDQE NLAELEEGDE SGGETTTTGT TGTTAASALR AGGGGGGGGG MAPRTGGCQN QPQHGGM // ID CNC_DROME STANDARD; PRT; 533 AA. AC P20482; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Segmentation protein cap'n'collar. GN CNC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92001535; PubMed=1911393; RA Mohler J., Vani K., Leung S., Epstein A.; RT "Segmentally restricted, cephalic expression of a leucine zipper gene RT during Drosophila embryogenesis."; RL Mech. Dev. 34:3-9(1991). CC -!- FUNCTION: PLAYS A ROLE IN CEPHALIC PATTERNING. PROBABLE SUBUNIT CC OF A HETERODIMERIC REGULATORY PROTEIN INVOLVED IN THE CONTROL OF CC HEAD MORPHOGENESIS. CC -!- DEVELOPMENTAL STAGE: LOCALIZED TO THE MANDIBULAR SEGMENT AND THE CC HYPOPHARYNGEAL AND LABRAL PRIMORDIA FIRST DETECTABLE IN LATE CC BLASTODERM STAGES. CC -!- SIMILARITY: BELONGS TO THE BZIP FAMILY. CNC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37495; AAB59246.1; -. DR HSSP; P34707; 1SKN. DR TRANSFAC; T01998; -. DR FlyBase; FBgn0000338; cnc. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IMP. DR GO; GO:0007350; P:blastoderm segmentation; IMP. DR GO; GO:0007310; P:oocyte dorsal/ventral axis determination; IMP. DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP. DR GO; GO:0042070; P:oocyte nucleus anchoring; IMP. DR GO; GO:0008359; P:regulation of bicoid mRNA localization; IMP. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localiz...; IMP. DR InterPro; IPR008917; Euk_transcr_DNA. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF00170; bZIP; 1. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW Transcription regulation; Activator; DNA-binding; Nuclear protein; KW Developmental protein. FT DNA_BIND 351 369 BASIC MOTIF. FT DOMAIN 387 408 LEUCINE-ZIPPER. FT DOMAIN 497 529 GLN-RICH. FT CONFLICT 349 349 I -> L (IN REF. 1; AAB59246). SQ SEQUENCE 533 AA; 56948 MW; EADFF9A5D6CA5C5F CRC64; MVDNSTSNNS SVLGLPSSGH VSNGSGSSAQ LGAGNPHGNQ ANGASGGVGS MSGSAVGAGA TGMTADLLAS GGAGAQGRAD RLDATSDSAV SSMGSERVPS LSDGEWGEGS DSAQDYHQGK YGGPYDFSYK NNSRLSTATR QPPVAQKKHQ LYGKRDPHKQ TPSALPPTAP PAAATAVQSQ RIKYEYDAGY ASSGMASGGI SEPGAMGPAL SKDYHHHQPY GMGASRSAFS GDYTVRPSPR TSQDLVQLNH TYSLPQGSGS LPRPQARHKK PLVATKTASK GASAGNSSSV GGNSSNLEEE HLTRDEKRAR SLNIPISVPD IINLPMDEFN ERLSKYDLSE NQLSLIRDIR RRGKNKVAAQ NCRKRKLDQI LTLEDEVNAV VKRKTQLNQD RDHLESERKR ISNKFAMLHR HVFQYLRDPE GNPCWPADYS LQQAADGSVY LLPREKSEGN NTATAASNAV SSASGGSLNG HVPTQAPMHS HQSHGMQAQH VVGGMSQQQQ QQSRLPPHLQ QQHHLQSQQQ QPGGQQQQQH RKE // ID CNG_DROME STANDARD; PRT; 665 AA. AC Q24278; Q9V7L5; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cyclic-nucleotide-gated cation channel (CNG channel). GN CNG OR CG7779. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95045396; PubMed=7957070; RA Baumann A., Frings S., Godde M., Seifert R., Kaupp U.B.; RT "Primary structure and functional expression of a Drosophila cyclic RT nucleotide-gated channel present in eyes and antennae."; RL EMBO J. 13:5040-5050(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: APPROXIMATELY 50-FOLD MORE SENSITIVE TO CGMP THAN TO CC CAMP. MAY BE INVOLVED IN TRANSDUCTION CASCADES OF BOTH CC INVERTEBRATE PHOTORECEPTORS AND OLFACTORY SENSILLAE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN ANTENNAE AND THE VISUAL SYSTEM. CC -!- SIMILARITY: BELONGS TO THE CYCLIC NUCLEOTIDE-GATED CATION CHANNEL CC (TC 1.A.1.5) FAMILY. CC -!- SIMILARITY: CONTAINS 1 CYCLIC NUCLEOTIDE-BINDING DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X89601; CAA61760.1; -. DR EMBL; AE003807; AAF58033.1; -. DR FlyBase; FBgn0014462; Cng. DR GO; GO:0017071; C:intracellular cyclic nucleotide activated c...; NAS. DR InterPro; IPR000595; cNMP_binding. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR001622; K+channel_pore. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF00520; ion_trans; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 1. DR PROSITE; PS00889; CNMP_BINDING_2; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. KW Ionic channel; Ion transport; cGMP-binding; Transmembrane. FT DOMAIN 1 110 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 111 131 H1 (POTENTIAL). FT DOMAIN 132 138 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 139 159 H2 (POTENTIAL). FT DOMAIN 160 186 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 187 207 H3 (POTENTIAL). FT DOMAIN 208 253 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 254 274 H4 (POTENTIAL). FT DOMAIN 275 325 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 326 346 H5 (POTENTIAL). FT DOMAIN 347 481 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 482 502 H6 (POTENTIAL). FT DOMAIN 503 665 CYTOPLASMIC (POTENTIAL). FT NP_BIND 437 559 CGMP (BY SIMILARITY). FT BINDING 496 496 CGMP (POTENTIAL). FT BINDING 511 511 CGMP (POTENTIAL). FT CARBOHYD 135 135 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 73 73 G -> R (IN REF. 1). SQ SEQUENCE 665 AA; 75823 MW; 6EFFC9A7CA243660 CRC64; MRHFKVKAMV QSLDISAITG QQTDAEPSKR SKPSALRRTL QALRQRLTKR NRPKPPDWFL EKFSNTTNTD KIGKGCPAME DAALSSEIRG SSVLCNRLSV DPTLQSHYRW LAIVSLAVLY NIIFVVGRAV FWEINKSAPA FWYTLDYLCD FIYLLDTLVH MHEGFLDQGL LVRDAFRLRR HYFHTKGWYL DVLSMLPTDL AYIWWPPETC SSLYLPCPVI VRLNRLLRIN RLWEWFDRTE TATGYPNAFR ICKVVLAILV LIHWNACMYF AISYEIGFSS DSWVYNLNGT RNNTLQRQYI YSFYWSTLTL TTIGETPTPE NDVEYLFVVA DFLAGVLIFA TIVGNIGSMI SNMNVARVEF QNRMDGVKQY MAFRRVGHEL EARVIRWFAY TWSQSGALDE ERVLAALPDK LKAEIAIQVH MDTLKQVRIF HDTEPGLLEA LVLKLKLQVF SPGDYICRKG DVGKEMYIVK RGKLSVVGDD GITVLATLGA GSVFGEVSVL EIAGNRTGNR RTANVRSLGY SDLFCLAKRD LWETLSDYPE ARSTLTQRGC QLLRKDGLLD EQIFADSQRV HDSIEGGIEK LELSVENLNM RLARLLAEYT ASQAKIKQRL AKLEMNGGPG TWRLECEPQS RARSGRLYSL QPKRRPRSRP DATAKSSDAA KQNTL // ID CNI_DROME STANDARD; PRT; 144 AA. AC P49858; Q9V423; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cornichon protein. GN CNI OR CG5855. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=95300228; PubMed=7540118; RA Roth S., Neuman-Silberberg F.S., Barcelo G., Schuepbach T.; RT "Cornichon and the EGF receptor signaling process are necessary for RT both anterior-posterior and dorsal-ventral pattern formation in RT Drosophila."; RL Cell 81:967-978(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ASSOCIATED WITH GURKEN, PRODUCES A SIGNAL RECEIVED BY CC TORPEDO RESULTING IN A SIGNALING PATHWAY THAT FIRST ESTABLISHES CC POSTERIOR FOLLICLE CELL FATES AND NORMAL LOCALIZATION OF THE CC ANTERIOR AND POSTERIOR DETERMINANTS, LATER THEY ACT IN A SIGNALING CC EVENT INDUCING DORSAL FOLLICLE CELL FATES AND REGULATING THE CC DORSAL-VENTRAL PATTERN OF EGG AND EMBRYO. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: IN EARLY STAGES, IT IS PRESENT IN THE NURSE CC CELL OOCYTE CLUSTER. IT IS HIGHLY EXPRESSED IN STAGE 1-6 EGG CC CHAMBERS, EXPRESSION CEASES DURING STAGE 7 AND CANNOT BE DETECTED CC IN STAGES 8 AND 9. DURING STAGE 10, IT IS REEXPRESSED IN THE NURSE CC CELLS. CC -!- SIMILARITY: BELONGS TO THE CORNICHON FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U28069; AAA86527.1; -. DR EMBL; AE003415; AAF45003.1; -. DR EMBL; AE003650; AAF53521.1; -. DR PIR; A56724; A56724. DR FlyBase; FBgn0000339; cni. DR InterPro; IPR003377; Cornichon. DR Pfam; PF03311; Cornichon; 1. DR PROSITE; PS01340; CORNICHON; 1. KW Developmental protein; Transmembrane. FT TRANSMEM 11 31 POTENTIAL. FT TRANSMEM 57 77 POTENTIAL. FT TRANSMEM 123 143 POTENTIAL. SQ SEQUENCE 144 AA; 16931 MW; 27692A3F68ECE1A9 CRC64; MAFNFTAFTY IVALIGDAFL IFFAIFHVIA FDELKTDYKN PIDQCNSLNP LVLPEYLLHI FLNLLFLFCG EWFSLCINIP LIAYHIWRYK NRPVMSGPGL YDPTTVLKTD TLYRNMREGW IKLAVYLISF FYYIYGMVYS LIST // ID CNN_DROME STANDARD; PRT; 1148 AA. AC P54623; DT 01-OCT-1996 (Rel. 34, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Centrosomin (Arrow protein). GN CNN OR ARR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96102828; PubMed=8582295; RA Heuer J.G., Li K., Kaufman T.C.; RT "The Drosophila homeotic target gene centrosomin (cnn) encodes a RT novel centrosomal protein with leucine zippers and maps to a genomic RT region required for midgut morphogenesis."; RL Development 121:3861-3876(1995). RN [2] RP REVISIONS. RC STRAIN=Oregon-R; RA Li K., Kaufman T.C.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP CHARACTERIZATION. RX MEDLINE=96222300; PubMed=8653793; RA Li K., Kaufman T.C.; RT "The homeotic target gene centrosomin encodes an essential centrosomal RT component."; RL Cell 85:585-596(1996). CC -!- FUNCTION: MAY PARTICIPATE IN MITOTIC SPINDLE ASSEMBLY AND THE CC MECHANICS OF MORPHOGENESIS THROUGH AN INTERACTION WITH CC MICROTUBULES, EITHER DIRECTLY OR INDIRECTLY. CNN IS A TARGET OF CC SEVERAL HOMEOTIC GENES. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: LOCALIZED TO THE CENTROSOMES THROUGH CC COMPLETE NUCLEAR CYCLES IN MITOTIC CELLS. REDISTRIBUTED INTO THE CC CYTOPLASM IN G2 PHASE CELLS. CC -!- TISSUE SPECIFICITY: DEVELOPING VISCERAL MESODERM OF THE MIDGUT, CC THE CENTRAL AND PERIPHERAL NERVOUS SYSTEM, AND DEVELOPING GONADS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U35621; AAB82065.1; -. DR PIR; T13347; T13347. DR FlyBase; FBgn0013765; cnn. DR GO; GO:0005813; C:centrosome; IDA. DR GO; GO:0007417; P:central nervous system development; IMP. DR GO; GO:0007098; P:centrosome cycle; IMP. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR GO; GO:0007494; P:midgut development; IMP. DR GO; GO:0007422; P:peripheral nervous system development; IMP. KW Phosphorylation; Developmental protein; Coiled coil. FT DOMAIN 97 516 COILED COIL (POTENTIAL). FT DOMAIN 626 654 COILED COIL (POTENTIAL). FT DOMAIN 644 656 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 712 983 COILED COIL (POTENTIAL). SQ SEQUENCE 1148 AA; 129907 MW; 6C178AF7ABEC89C6 CRC64; MDQSKQVLRD YCGDGNGTCA SSLKEITLIE TVTSFLEENG AAEIDRRVLR KLAEALSKSI DDTSPGALQD VTMENSYASF DVPRPPGGGN SPLPSQGRSV RELEEQMSAL RKENFNLKLR IYFLEEGQPG ARADSSTESL SKQLIDAKIE IATLRKTVDV KMELLKDAAR AISHHEELQR KADIDSQAII DELQEQIHAY QMAESGGQPV ENIAKTRKML RLESEVQRLE EELVNIEARN VAARNELEFM LAERLESLTA CEGKIQELAI KNSELVERLE KETASAESSN ANRDLGAQLA DKICELQEAQ EKLKERERIH EQACRTIQKL MQKLSSQEKE IKKLNQENEQ SANKENDCAK TVISPSSSGR SMSDNEASSQ EMSTNLRVRY ELKINEQEEK IKQLQTEVKK KTANLQNLVN KELWEKNREV ERLTKLLANQ QKTLPQISEE SAGEADLQQS FTEAEYMRAL ERNKLLQRKV DVLFQRLADD QQNSAVIGQL RLELQQARTE VETADKWRLE CVDVCSVLTN RLEELAGFLN SLLKHKDVLG VLAADRRNAM RKAVDRSLDL SKSLNMTLNI TATSLADQSL AQLCNLSEIL YTEGDASHKT FNSHEELHAA TSMAPTVENL KAENKALKKE LEKRRSSEGQ RKERRSLPLP SQQFDNQSES EAWSEPDRKV SLARIGLDET SNSLAAPEQA ISESESEGRT CATRQDRNRN SERIAQLEEQ IAQKDERMLN VQCQMVELDN RYKQEQLRCL DITQQLEQLR AINEALTADL QAIGSHEEER MVELQRQLEL KNQQIDQLKL AHSTLTADSQ ITEMELQALQ QQMQEIEQQH ADSVETLQSQ LQKLKLDAVQ QLEEHERLHR EALERDWVAL TTYQEQAQQL LELQRSLDYH QENEKELKQT LVENELATRA LKKQLDESTL QASKAVMERT KAYNDKLQLE KRSEELRLQL EALKEEHQKL LQKRSNSSDV SQSGYTSEEV AVPMGPPSGQ ATTCKQAAAA VLGQRVNTSS PDLGIESDAG RISSVEVSNA QRAMLKTVEM KTEGSASPKA KSEESTSPDS KSNVATGAAT VHDCAKVDLE NAELRRKLIR TKRAFEDTYE KLRMANKAKA QVEKDIKNQI LKTHNVLRNV RSNMENEL // ID COG2_DROME STANDARD; PRT; 710 AA. AC Q9VF78; Q8SZC5; Q9XZ52; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Conserved oligomeric Golgi complex component 2 (LdlCp-related DE protein). GN LDLCP OR CG6177. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Fyrberg E.A., Fyrberg C.C.; RT "Drosophila melanogaster gene for ldlCp-related protein."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR NORMAL GOLGI MORPHOLOGY AND FUNCTION (BY CC SIMILARITY). CC -!- SUBUNIT: COMPONENT OF THE CONSERVED OLIGOMERIC GOLGI COMPLEX WHICH CC IS COMPOSED OF EIGHT DIFFERENT SUBUNITS AND IS REQUIRED FOR NORMAL CC GOLGI MORPHOLOGY AND LOCALIZATION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: ASSOCIATED WITH THE CYTOSOLIC FACE OF CC THE GOLGI APPARATUS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE COG2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF132535; AAD31443.1; -. DR EMBL; AF132532; AAD31443.1; JOINED. DR EMBL; AF132533; AAD31443.1; JOINED. DR EMBL; AF132534; AAD31443.1; JOINED. DR EMBL; AE003708; AAF55182.1; -. DR EMBL; AY070962; AAL48584.1; -. DR FlyBase; FBgn0026634; ldlCp. DR GO; GO:0017119; C:Golgi transport complex; ISS. DR GO; GO:0008565; F:protein transporter activity; ISS. DR GO; GO:0007030; P:Golgi organization and biogenesis; ISS. DR GO; GO:0006891; P:intra-Golgi transport; ISS. KW Transport; Protein transport; Golgi stack; Membrane. FT CONFLICT 50 53 EQLR -> DDVL (IN REF. 1). FT CONFLICT 129 130 QL -> HV (IN REF. 1). FT CONFLICT 184 184 K -> R (IN REF. 3). FT CONFLICT 193 193 D -> E (IN REF. 1). FT CONFLICT 291 292 LL -> FV (IN REF. 1). FT CONFLICT 324 325 NS -> EF (IN REF. 1). FT CONFLICT 401 401 V -> E (IN REF. 1). FT CONFLICT 512 512 C -> R (IN REF. 1). FT CONFLICT 548 548 G -> A (IN REF. 1). FT CONFLICT 647 648 AA -> PR (IN REF. 1). FT CONFLICT 698 698 M -> V (IN REF. 3). SQ SEQUENCE 710 AA; 81135 MW; E6B420B6244B214F CRC64; MHDPVKKSAH LTAGSTSTAE KLCFDKNEFM KANFSVDEFL HKNRNAPSLE QLRDNLGLYL KGLRAAMIDL INEDYADFVN LSANLVGLDQ NIKTIQQPLE QFRSDIESIH GLIDENVTEL RAQLEEKRQL REFKRGLQSL KKVYETINKL QDLIDRKLSG EQPIKAVDLE RAALDLIQLK FHEKHCFKHL SPDHQGKIQQ LEEQLHQHLR RFFNDALSQA RNSAPESLER CLRIYITLNA CDQAECAFRE DVVAPYMTGV IGEQQLQNSP QGLAGIYSKI LNFISLHMTD LLRLTLYSDK FPGFNFVVNS YWSDVETRLE LHMNSIFAPG NSEVFYVKYK CTRDFLGKIE ELLTCSGEQA VTFYRQHKQT KSFEARWNLP VYFQICFQEI AGKFEAQLEP VLQEDSLKDN LTDSDYKISA FNAAKEAMTR CWAEGVYLPE VFPKFYKLNV QVVLRLSRWI TDAITQSKGS NFSKPYTRNQ LLIALHADIR KLDAHLPELQ QLIIKSVPVE QCTKIFSDVL AKSMSCLADT LGAHLTNIQK TLVELLIGEC ETENVRQVND LPRLYRKTNR EVPTRCSSYV EQMLRPLKAF AQQNESQLGT LVVEQILAEV ASHITKAYFN VVSDVLTSVQ KTEESLRRLR NVKSGGAATV STGSSAVMSD DDKIRVQLRV DVTSWRQELC KLNFQATQID KLVELTNMVE DSIKLKDNSA // ID COG5_DROME STANDARD; PRT; 751 AA. AC Q9VJD3; Q8T0G3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative conserved oligomeric Golgi complex subunit 5 (Four way stop DE protein). GN FWS OR CG6549. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 406-751 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR NORMAL GOLGI FUNCTION (BY SIMILARITY). CC -!- SUBUNIT: COMPONENT OF THE CONSERVED OLIGOMERIC GOLGI COMPLEX WHICH CC IS COMPOSED OF EIGHT DIFFERENT SUBUNITS AND IS REQUIRED FOR NORMAL CC GOLGI MORPHOLOGY AND LOCALIZATION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GOLGI (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE COG5 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003655; AAF53619.1; -. DR EMBL; AY069335; AAL39480.1; ALT_INIT. DR FlyBase; FBgn0024689; fws. KW Hypothetical protein; Transport; Protein transport; Golgi stack; KW Membrane. SQ SEQUENCE 751 AA; 84953 MW; E32B1D05BEEF6EBA CRC64; MVTGDPVATK TPNAADSDDN DFTASMSHLT IGQQIQELSK QLQNTKEELH QQVRDKHGAL LQQATHAGRF DAALNALAED VQRVRETGHR LKNQVDTQYQ QVENQTQVLG RLHDVSHLLR SAGTLLSLTA KLKATKDVLR LAEIHFELGQ LIEDKELKDI DFIQQERAYV ISSAQKIRNL TQMQLVTGLQ ERNENQVVNA LKIFMNFNTL EKSLDNLLAT FIADMEQSLK ECFAGNDISV LNKSPTHNVS KPAPSRGPGK TPQLTTTQNF RAKFWKSLHW LLYDELFETC TQIKLLKTAL EQINQFGYTS ESSDQCIPQR FWQQVQQLLR KSFDECPQHV TQTLQEGLSK LLTSARGLEQ RLHGEFQFDN ELFAPLEVGY VSKCAANFKA CLAGVDLPGN ETVDNFIRVA STELSAALID SRLTNAIANV FAACGKELCT KLEAQIKLGA DSKQVVDLPN LQQQQNTQLA NVLFYYKDSV RRMLSDLHVH FEKTPGTARE IISRSLEQAD LLIGTILQQI MESIITTISI IVLSMHREPG LNSERMSTTG PSMYMKELQE FVNRSWSHHI ALFDDKQMTK KCGHELAKRC IELFLHNVCI LRPLSSCGRQ RLKQDCQHME QALKPLCPNL AELGKPSRLL RAMSLLIVQT AEELVKQTIG EDSLVPSYIV LLLLFGHAGA DLQSPHTTAN WSNERLIEWL DGHTAEREKL ELISGALQRY RDNARRKNIQ QYDEVYPMMV DYFEQALKAL P // ID COLL_DROME STANDARD; PRT; 575 AA. AC P56721; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Transcription factor collier (Transcription factor knot). GN KN OR COL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=96385439; PubMed=8793297; RA Crozatier M., Valle D., Dubois L., Ibnsouda S., Vincent A.; RT "Collier, a novel regulator of Drosophila head development, is RT expressed in a single mitotic domain."; RL Curr. Biol. 6:707-718(1996). RN [2] RP FUNCTION. RX MEDLINE=99307499; PubMed=10375526; RA Vervoort M., Crozatier M., Valle D., Vincent A.; RT "The COE transcription factor Collier is a mediator of short-range RT Hedgehog-induced patterning of the Drosophila wing."; RL Curr. Biol. 9:632-639(1999). RN [3] RP FUNCTION. RX MEDLINE=99169092; PubMed=10068642; RA Crozatier M., Vincent A.; RT "Requirement for the Drosophila COE transcription factor Collier in RT formation of an embryonic muscle: transcriptional response to notch RT signalling."; RL Development 126:1495-1504(1999). RN [4] RP FUNCTION. RX MEDLINE=99406633; PubMed=10477305; RA Crozatier M., Valle D., Dubois L., Ibnsouda S., Vincent A.; RT "Head versus trunk patterning in the Drosophila embryo; collier RT requirement for formation of the intercalary segment."; RL Development 126:4385-4394(1999). CC -!- FUNCTION: MAY ACT AS A 'SECOND-LEVEL REGULATOR' OF HEAD CC PATTERNING. REQUIRED FOR ESTABLISHMENT OF THE PS(-1)/PS0 CC PARASEGMENTAL BORDER AND FORMATION OF THE INTERCALARY SEGMENT. CC REQUIRED FOR EXPRESSION OF THE SEGMENT POLARITY GENES HEDGEHOG, CC ENGRAILED AND WINGLESS, AND THE SEGMENT-IDENTITY GENES CAP AND CC COLLAR IN THE INTERCALARY SEGMENT. REQUIRED AT THE ONSET OF THE CC GASTRULATION FOR THE CORRECT FORMATION OF THE MANDIBULAR SEGMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=COL1; CC IsoId=P56721-1; Sequence=Displayed; CC Name=COL2; CC IsoId=P56721-2; Sequence=VSP_001111; CC -!- TISSUE SPECIFICITY: ITS EXPRESSION AT THE BLASTODERM STAGE IS CC RESTRICTED TO A SINGLE STRIPE OF CELLS CORRESPONDING TO PART OF CC THE INTERCALARY AND MANDIBULAR SEGMENT PRIMORDIA, POSSIBLY CC PARASEGMENT O. CC -!- DEVELOPMENTAL STAGE: BLASTODERM. CC -!- SIMILARITY: BELONGS TO THE COE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X97803; -; NOT_ANNOTATED_CDS. DR TRANSFAC; T05041; -. DR TRANSFAC; T05055; -. DR FlyBase; FBgn0001319; kn. DR GO; GO:0007474; P:wing vein specification; IMP. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR002909; IPT_TIG. DR InterPro; IPR003523; TF_COE. DR Pfam; PF01833; TIG; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00429; IPT; 1. DR PROSITE; PS01345; COE; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW Developmental protein; Alternative splicing; Zinc-finger. FT ZN_FING 167 186 C5-TYPE (POTENTIAL). FT VARSPLIC 529 575 MSAVSSTWHQAFVQHHHAATAHPHHHYPHPHQPWHNPAVSA FT ATAAAV -> RVSSLSFNPFALPTCNTQGYSTQLVTSTK FT (in isoform COL2). FT /FTId=VSP_001111. SQ SEQUENCE 575 AA; 62461 MW; 1D5FD65DC7E2186B CRC64; MEWGRKLYPS AVSGPRSAGG LMFGLPPTAA VDMNQPRGPM TSLKEEPLGS RWAMQPVVDQ SNLGIGRAHF EKQPPSNLRK SNFFHFVIAL YDRAGQPIEI ERTAFIGFIE KDSESDATKT NNGIQYRLQL LYANGARQEQ DIFVRLIDSV TKQAIIYEGQ DKNPEMCRVL LTHEVMCSRC CDKKSCGNRN ETPSDPVIID RFFLKFFLKC NQNCLKNAGN PRDMRRFQVV ISTQVAVDGP LLAISDNMFV HNNSKHGRRA KRLDTTEGTG NTSLSISGHP LAPDSTYDGL YPPLPVATPC IKAISPSEGW TTGGATVIIV GDNFFDGLQV VFGTMLVWSE LITSHAIRVQ TPPSDIPGVV EVTLSYKSKQ FCKGSPGRFV YVSALNEPTI DYGFQRLQKL IPRHPGDPEK LQKEIILKRA ADLVEALYSM PRSPDGSTGF NSYAGQLAVS VQDGSGQWTE DDYQRAQSSS VSPRGGYCSS ASTPHSSGGS YGATAASAAV AATANGYAPA PNMGTLSSSP GSVFNSTSMS AVSSTWHQAF VQHHHAATAH PHHHYPHPHQ PWHNPAVSAA TAAAV // ID COMM_DROME STANDARD; PRT; 370 AA. AC Q24139; Q9VUT9; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Commissureless protein. GN COMM OR CG17943. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96207804; PubMed=8785048; RA Tear G., Harris R., Sutaria S., Kilomanski K., Goodman C.S., RA Seeger M.A.; RT "Commissureless controls growth cone guidance across the CNS midline RT in Drosophila and encodes a novel membrane protein."; RL Neuron 16:501-514(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONTROLS GROWTH CONE GUIDANCE ACROSS THE CNS MIDLINE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U35854; AAC47019.1; -. DR EMBL; AE003530; AAF49584.1; -. DR FlyBase; FBgn0010105; comm. DR GO; GO:0005794; C:Golgi apparatus; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. KW Developmental protein; Transmembrane. FT TRANSMEM 137 157 POTENTIAL. FT DOMAIN 12 15 POLY-THR. FT DOMAIN 258 262 POLY-HIS. FT DOMAIN 283 286 POLY-ALA. FT DOMAIN 294 301 POLY-SER. FT DOMAIN 365 368 POLY-VAL. SQ SEQUENCE 370 AA; 40310 MW; EB298EA415D4FBDA CRC64; MISTTDYPTV ETTTTAEELY AEYISAPASS MSPAAIAEHL QQNQITFEIP SAHDLRHIDA LNSFNALLQR IGNAAVSYDP APPSGWSPDG SISTEQLSKS VVLDLADLRD RSEESGESSW WSQIFGDADM HVIINYLWIG VVSSLVILSL VFILFSCYFY RKFRTWKKCN KDIRAQIHAA SDSYSSHLVG CDASRLLLHQ QMQHPHHRSS EAGFYQIESP PCYTIATGLP SYDEALHHQP RHFAYGMKFV YPSLAAVHHH HHCISNWEKQ EPLNKLQKCK LSAAAAVEED KADSSSSTSA SASPSSSESS NLATATPAIC INMPSGRQDE EVDNSDSDSA IAVAVAVAQS LQPAAPADDD CASLVVVVAA // ID CONN_DROME STANDARD; PRT; 682 AA. AC Q01819; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Connectin precursor. GN CON. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92370678; PubMed=1505024; RA Nose A., Mahajan V.B., Goodman C.S.; RT "Connectin: a homophilic cell adhesion molecule expressed on a subset RT of muscles and the motoneurons that innervate them in Drosophila."; RL Cell 70:553-567(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93202002; PubMed=1363542; RA Gould A.P., White R.A.H.; RT "Connectin, a target of homeotic gene control in Drosophila."; RL Development 116:1163-1174(1992). CC -!- FUNCTION: CELL ADHESION PROTEIN INVOLVED IN TARGET RECOGNITION CC DURING NEUROMUSCULAR DEVELOPMENT. MEDIATES HOMOPHILIC CELLULAR CC ADHESION. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN ABDOMINAL AND CC THORACIC SEGMENT MUSCLE AND MOTORNEURON CELLS. CC -!- DEVELOPMENTAL STAGE: EMBRYO. CC -!- SIMILARITY: CONTAINS 10 LEUCINE-RICH (LRR) REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96647; AAA28424.1; -. DR EMBL; X68701; CAA48652.1; -. DR PIR; A43318; A43318. DR PIR; A49121; A49121. DR HSSP; P01233; 1XUL. DR FlyBase; FBgn0005775; Con. DR InterPro; IPR001611; LRR. DR InterPro; IPR000483; LRR_Cterm. DR InterPro; IPR003591; LRR_typ. DR Pfam; PF00560; LRR; 7. DR Pfam; PF01463; LRRCT; 1. DR SMART; SM00369; LRR_TYP; 2. DR SMART; SM00082; LRRCT; 1. KW Cell adhesion; Developmental protein; Embryo; Signal; GPI-anchor; KW Leucine-rich repeat; Repeat; Lipoprotein. FT SIGNAL 1 24 FT CHAIN 25 658 CONNECTIN. FT PROPEP 659 682 REMOVED IN MATURE FORM (POTENTIAL). FT REPEAT 149 172 LRR 1. FT REPEAT 173 196 LRR 2. FT REPEAT 197 220 LRR 3. FT REPEAT 222 244 LRR 4. FT REPEAT 245 268 LRR 5. FT REPEAT 269 292 LRR 6. FT REPEAT 294 316 LRR 7. FT REPEAT 317 340 LRR 8. FT REPEAT 341 364 LRR 9. FT REPEAT 366 388 LRR 10. FT LIPID 658 658 GPI-anchor amidated alanine (Potential). FT CONFLICT 631 631 E -> G (IN REF. 2). FT CONFLICT 674 677 QVAL -> VALM (IN REF. 2). SQ SEQUENCE 682 AA; 75992 MW; FA296353438F6A80 CRC64; MATLADSAIC FLLLSLLLIG ACLVTPTEGR AKDDRRTRGR GSSSGVLSSS SSSSNNMNNG YYSGSSSTAG SSSGYVFTSS SAVNSGSTGY SGPMDSTGFC TRRRDMKLMC YCTPDENHVP VQKAECWVFS EGLHQNDTTW TRFYQQKRLR ELKFVIQNNA RLDYIPTMII EPLKNLSSIV IEYSQVEIVK SYAFANLPFL ERIILNNNHI MALDQDAFAN HIRLRELNLE HNQIFEMDRY AFRNLPLCER LFLNNNNIST LHEGLFADMA RLTFLNLAHN QINVLTSEIF RGLGNLNVLK LTRNNLNFIG DTVFAELWSL SELELDDNRI ERISERALDG LNTLKTLNLR NNLLKKIDNG LLRGTPALLS INVQANKLET LTFYTFQPIM DNLVNSTSEL LVSDNKFICD CRLQWIFELK NRTRHLQLRD SLEDLHCTLQ EPKLSHFVDP VPPTILDVLN IGGFTAIGSN SASMGGVGNS VVGSSYSGLT MDDSRKHLGS RSRQALRGQR QFASSAENVV ESKMRRRRKR QEEVKEKDLA AVAPAHKRYD YYDDNNGGMS LGHGLDLDDN LSLHKQGFYG AGSPVVGHND VDVLMTSHSA SGDALDILTT KNAIYIKLFL LKPEMLPCHD ELSDPTELPL SRDLMDVRSN VGQDMSTAGA NSLAQGMTII VSLQVALMIS RG // ID COPB_DROME STANDARD; PRT; 964 AA. AC P45437; Q9VWV7; Q9Y116; DT 01-NOV-1995 (Rel. 32, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Coatomer beta subunit (Beta-coat protein) (Beta-COP). GN BETA-COP OR BCDNA:GH09317 OR CG6223. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=94173932; PubMed=8127899; RA Ripoche J., Link B., Yucel J.K., Tokuyasu K., Malhotra V.; RT "Location of Golgi membranes with reference to dividing nuclei in RT syncytial Drosophila embryos."; RL Proc. Natl. Acad. Sci. U.S.A. 91:1878-1882(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE COATOMER IS A CYTOSOLIC PROTEIN COMPLEX THAT BINDS CC TO DILYSINE MOTIFS AND REVERSIBLY ASSOCIATES WITH GOLGI NON- CC CLATHRIN-COATED VESICLES, WHICH FURTHER MEDIATE BIOSYNTHETIC CC PROTEIN TRANSPORT FROM THE ER, VIA THE GOLGI UP TO THE TRANS GOLGI CC NETWORK. COATOMER COMPLEX IS REQUIRED FOR BUDDING FROM GOLGI CC MEMBRANES, AND IS ESSENTIAL FOR THE RETROGRADE GOLGI-TO-ER CC TRANSPORT OF DILYSINE-TAGGED PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: OLIGOMERIC COMPLEX THAT CONSISTS OF AT LEAST THE ALPHA, CC BETA, BETA', GAMMA, DELTA, EPSILON AND ZETA SUBUNITS. CC -!- SUBCELLULAR LOCATION: THE COATOMER IS CYTOPLASMIC OR POLYMERIZED CC ON THE CYTOPLASMIC SIDE OF THE GOLGI, AS WELL AS ON THE CC VESICLES/BUDS ORIGINATING FROM IT (BY SIMILARITY). CC -!- MISCELLANEOUS: BREFELDIN A INDUCES DISSOCIATION FROM THE GOLGI OF CC THE BETA-COP AND PRESUMABLY THE OTHER COATOMER SUBUNITS (BY CC SIMILARITY). CC -!- SIMILARITY: SIGNIFICANT, OF THE N-TERMINAL HALF OF BETA-COP WITH CC THOSE OF BETA-ADAPTINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L31852; AAA21090.1; -. DR EMBL; AE003508; AAF48830.2; -. DR EMBL; AF145656; AAD38631.1; -. DR FlyBase; FBgn0008635; beta-Cop. DR GO; GO:0005794; C:Golgi apparatus; IDA. DR InterPro; IPR002553; Adaptin_N. DR InterPro; IPR008938; ARM. DR Pfam; PF01602; Adaptin_N; 1. KW Transport; Protein transport; Golgi stack; Membrane; Phosphorylation. FT CONFLICT 68 68 Q -> E (IN REF. 1). FT CONFLICT 168 168 V -> A (IN REF. 1). FT CONFLICT 239 240 ER -> DG (IN REF. 1). FT CONFLICT 325 325 R -> P (IN REF. 1). FT CONFLICT 507 515 AGGNAAGSA -> EAAMQLDR (IN REF. 1). FT CONFLICT 543 543 A -> P (IN REF. 1). FT CONFLICT 938 943 IRAKSQ -> LRQES (IN REF. 1). SQ SEQUENCE 964 AA; 107406 MW; 08AB7F17F04F361D CRC64; MTSQVPCYTI INSPDLEVTN EMQLKRDLEK GDTNVKIETL KRVIKLLLNG ERYPGLIMTI IRFVLPVQNH TIKKLLLIFW EIVPKTSADG KLLQEMILVC DAYRKDLQHP NEFLRGSTLR FLCKLKEPEL LEPLMPAIRA CLDHRHSYVR RNAVLAIFTI YKNFDWLVPD GPELIASFLD TQQDMSCKRN AFLMLLHADQ ERALNYLASC IDQVHTFGDI LQLVIVELIY KVCHANPAER SRFIRCIYNL LNSSSNAVRY ESAGTLITLS LAPTAIKAAA SCYIELVVKE SDNNVKLIVL DRLVAMKEHE GMEKVMQDLV MDVLRVLAAP DIEVRRKTLA LALDLVYSRN IGEMVLVLKK EVAKTHNVEH EDTGKYRQLL VRTLHTCSIK FPDVAANVIP VLVEFLSDTN ELAAADVLIF IREAIQKFPA LRALIIEHLI EAFPQIKSSK IHRAAVWILG EYVEGSQILE VIAVIQQTLG EVPMVEAEQR RLAGDQTEEQ KQQQGSAGGN AAGSAAEGSG SGNASNKVTS DGTYATQSAY SLAPVAKAEK RPPLRQYLMD GDFFIGAALS ATLTKLALRY AELETEARAQ NRLTTQVMLI MSSILHLGKS GFPSKPITND DTDRIFVCLR TLSERTPEAI SVFTLYCREA LGKMLDAQHD EDQRMLKEKQ KATAKVQPDD PVLFAQLSNG RDNQLGENVF ESSLNQALAG SKNAQLSDVA SPNSKLNKVT QLTGFSDPVY AEAYVNVNQY DIVLDVLIVN QTNDTLQNCT LELATLGDLK LVERPHPVVL APHDFCNIKA NVKVSSTENG IIFGNIVYET ALNTNVVVLN TIHIDIMDYI IPASCTDTEF RQMWQDFEWE NKVTVNTSFT DLHEYLKHLL KSTNMKCLTP EKALSGQCGF MAANMYAKSI FGENALANLS IEKPVDDPDS KVTGHIRIRA KSQGMALSLG DKISSSQKQS VQAA // ID COPI_DROME STANDARD; PRT; 1409 AA. AC P04146; Q03728; Q24280; Q24555; Q24585; Q24586; Q24587; DT 01-NOV-1986 (Rel. 03, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Copia protein [Contains: Copia VLP protein; Copia protease DE (EC 3.4.23.-)]. GN COPIA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RX MEDLINE=85267679; PubMed=2410772; RA Mount S.M., Rubin G.M.; RT "Complete nucleotide sequence of the Drosophila transposable element RT copia: homology between copia and retroviral proteins."; RL Mol. Cell. Biol. 5:1630-1638(1985). RN [2] RP SEQUENCE FROM N.A., SEQUENCE OF 2-10, AND ALTERNATIVE SPLICING. RX MEDLINE=85240569; PubMed=2409449; RA Emori Y., Shiba T., Kanaya S., Inouye S., Yuki S., Saigo K.; RT "The nucleotide sequences of copia and copia-related RNA in Drosophila RT virus-like particles."; RL Nature 315:773-776(1985). RN [3] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RX MEDLINE=89183629; PubMed=2538806; RA Miller K., Rosenbaum J., Zbrzezna V., Pogo A.O.; RT "The nucleotide sequence of Drosophila melanogaster copia-specific RT 2.1-kb mRNA."; RL Nucleic Acids Res. 17:2134-2134(1989). RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT), AND MUTAGENESIS OF ASP-292. RC TISSUE=Larva; RX MEDLINE=90151630; PubMed=1689241; RA Yoshioka K., Honma H., Zushi M., Kondo S., Togashi S., Miyake T., RA Shiba T.; RT "Virus-like particle formation of Drosophila copia through RT autocatalytic processing."; RL EMBO J. 9:535-541(1990). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P04146-1; Sequence=Displayed; CC Name=Short; CC IsoId=P04146-2; Sequence=VSP_005226; CC -!- SIMILARITY: THE PROTEASE BELONGS TO PEPTIDASE FAMILY A11. CC -!- SIMILARITY: CONTAINS 1 CCHC-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04456; CAA28054.2; -. DR EMBL; X02599; CAA26444.1; -. DR EMBL; X02599; CAA26445.1; -. DR EMBL; X02600; CAA26446.1; -. DR EMBL; X02600; CAA26447.1; -. DR EMBL; X13719; CAA31997.1; -. DR EMBL; X54147; CAA38086.1; -. DR PIR; A03324; OFFFCP. DR MEROPS; A11.001; -. DR FlyBase; FBgn0013437; copia\GIP. DR InterPro; IPR001969; Aspprotease_AS. DR InterPro; IPR001584; Rve. DR InterPro; IPR001878; Znf_CCHC. DR Pfam; PF00665; rve; 1. DR Pfam; PF00098; zf-CCHC; 1. DR PRINTS; PR00939; C2HCZNFINGER. DR SMART; SM00343; ZnF_C2HC; 1. DR PROSITE; PS00141; ASP_PROTEASE; FALSE_NEG. DR PROSITE; PS50158; ZF_CCHC; 1. KW Transposable element; Hydrolase; Aspartyl protease; ATP-binding; KW Polyprotein; Alternative splicing; Polymorphism; Zinc-finger. FT CHAIN 1 270 COPIA VLP PROTEIN (POTENTIAL). FT CHAIN 271 1409 COPIA PROTEASE (POTENTIAL). FT ZN_FING 230 247 CCHC-TYPE. FT ACT_SITE 292 292 PROTEASE (BY SIMILARITY). FT VARSPLIC 392 1374 Missing (in isoform Short). FT /FTId=VSP_005226. FT VARIANT 1265 1288 STTGYLFKMFDFNLICWNTKRQNS -> VQQGIYSKCLILI FT SFVGIQRDRTQ (IN VARIANT COPIA-RELATED). FT VARIANT 1289 1409 MISSING (IN VARIANT COPIA-RELATED). FT MUTAGEN 292 292 D->A: LOSS OF ACTIVITY. FT CONFLICT 191 191 S -> N (IN REF. 2; CAA26447). FT CONFLICT 300 300 I -> V (IN REF. 2; CAA26447). FT CONFLICT 866 866 Q -> E (IN REF. 2; CAA26447). SQ SEQUENCE 1409 AA; 162817 MW; BE89440763A47691 CRC64; MDKAKRNIKP FDGEKYAIWK FRIRALLAEQ DVLKVVDGLM PNEVDDSWKK AERCAKSTII EYLSDSFLNF ATSDITARQI LENLDAVYER KSLASQLALR KRLLSLKLSS EMSLLSHFHI FDELISELLA AGAKIEEMDK ISHLLITLPS CYDGIITAIE TLSEENLTLA FVKNRLLDQE IKIKNDHNDT SKKVMNAIVH NNNNTYKNNL FKNRVTKPKK IFKGNSKYKV KCHHCGREGH IKKDCFHYKR ILNNKNKENE KQVQTATSHG IAFMVKEVNN TSVMDNCGFV LDSGASDHLI NDESLYTDSV EVVPPLKIAV AKQGEFIYAT KRGIVRLRND HEITLEDVLF CKEAAGNLMS VKRLQEAGMS IEFDKSGVTI SKNGLMVVKN SGMLNNVPVI NFQAYSINAK HKNNFRLWHE RFGHISDGKL LEIKRKNMFS DQSLLNNLEL SCEICEPCLN GKQARLPFKQ LKDKTHIKRP LFVVHSDVCG PITPVTLDDK NYFVIFVDQF THYCVTYLIK YKSDVFSMFQ DFVAKSEAHF NLKVVYLYID NGREYLSNEM RQFCVKKGIS YHLTVPHTPQ LNGVSERMIR TITEKARTMV SGAKLDKSFW GEAVLTATYL INRIPSRALV DSSKTPYEMW HNKKPYLKHL RVFGATVYVH IKNKQGKFDD KSFKSIFVGY EPNGFKLWDA VNEKFIVARD VVVDETNMVN SRAVKFETVF LKDSKESENK NFPNDSRKII QTEFPNESKE CDNIQFLKDS KESENKNFPN DSRKIIQTEF PNESKECDNI QFLKDSKESN KYFLNESKKR KRDDHLNESK GSGNPNESRE SETAEHLKEI GIDNPTKNDG IEIINRRSER LKTKPQISYN EEDNSLNKVV LNAHTIFNDV PNSFDEIQYR DDKSSWEEAI NTELNAHKIN NTWTITKRPE NKNIVDSRWV FSVKYNELGN PIRYKARLVA RGFTQKYQID YEETFAPVAR ISSFRFILSL VIQYNLKVHQ MDVKTAFLNG TLKEEIYMRL PQGISCNSDN VCKLNKAIYG LKQAARCWFE VFEQALKECE FVNSSVDRCI YILDKGNINE NIYVLLYVDD VVIATGDMTR MNNFKRYLME KFRMTDLNEI KHFIGIRIEM QEDKIYLSQS AYVKKILSKF NMENCNAVST PLPSKINYEL LNSDEDCNTP CRSLIGCLMY IMLCTRPDLT TAVNILSRYS SKNNSELWQN LKRVLRYLKG TIDMKLIFKK NLAFENKIIG YVDSDWAGSE IDRKSTTGYL FKMFDFNLIC WNTKRQNSVA ASSTEAEYMA LFEAVREALW LKFLLTSINI KLENPIKIYE DNQGCISIAN NPSCHKRAKH IDIKYHFARE QVQNNVICLE YIPTENQLAD IFTKPLPAAR FVELRDKLGL LQDDQSNAE // ID COPP_DROME STANDARD; PRT; 914 AA. AC O62621; Q8MRM3; Q9VJZ0; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Coatomer beta' subunit (Beta'-coat protein) (Beta'-COP). GN BETA'-COP OR CG6699. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Merdes G., Heid H.W., Mechler B.M.; RT "Cloning and characterization of the Drosophila coatomer subunit RT beta'."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 613-914 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE COATOMER IS A CYTOSOLIC PROTEIN COMPLEX THAT BINDS CC TO DILYSINE MOTIFS AND REVERSIBLY ASSOCIATES WITH GOLGI NON- CC CLATHRIN-COATED VESICLES, WHICH FURTHER MEDIATE BIOSYNTHETIC CC PROTEIN TRANSPORT FROM THE ER, VIA THE GOLGI UP TO THE TRANS GOLGI CC NETWORK. COATOMER COMPLEX IS REQUIRED FOR BUDDING FROM GOLGI CC MEMBRANES, AND IS ESSENTIAL FOR THE RETROGRADE GOLGI-TO-ER CC TRANSPORT OF DILYSINE-TAGGED PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: OLIGOMERIC COMPLEX THAT CONSIST OF AT LEAST THE ALPHA, CC BETA, BETA', GAMMA, DELTA, EPSILON AND ZETA SUBUNITS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: THE COATOMER IS CYTOPLASMIC OR POLYMERIZED CC ON THE CYTOPLASMIC SIDE OF THE GOLGI, AS WELL AS ON THE CC VESICLES/BUDS ORIGINATING FROM IT (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 6 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ006524; CAA07085.1; -. DR EMBL; AJ006523; CAA07084.1; -. DR EMBL; AE003639; AAF53294.2; -. DR EMBL; AY119527; AAM50181.1; ALT_INIT. DR FlyBase; FBgn0025724; beta'-Cop. DR GO; GO:0030126; C:COPI vesicle coat; NAS. DR GO; GO:0006888; P:ER to Golgi transport; NAS. DR GO; GO:0006890; P:retrograde (Golgi to ER) transport; NAS. DR InterPro; IPR006692; Coatomer_WDAD. DR InterPro; IPR001680; WD40. DR Pfam; PF04053; Coatomer_WDAD; 1. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 4. DR SMART; SM00320; WD40; 6. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; 4. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Transport; Protein transport; Golgi stack; Membrane; Repeat; KW WD repeat; Endoplasmic reticulum. FT REPEAT 13 43 WD 1. FT REPEAT 55 85 WD 2. FT REPEAT 97 127 WD 3. FT REPEAT 140 171 WD 4. FT REPEAT 183 215 WD 5. FT REPEAT 227 257 WD 6. FT CONFLICT 254 254 R -> C (IN REF. 1). FT CONFLICT 343 345 LPV -> CPF (IN REF. 1). SQ SEQUENCE 914 AA; 102713 MW; 15E862E1944F5C4B CRC64; MPLKLDIKRR LTSRSDRVKC VDLHPAEPWM LCALYNGHVH IMNYENQQMV KDFEVCDVPV RSARFVARKN WILTGSDDMQ IRVFNYNTLE KVHSFEAHSD YLRCIAVHPT QPLVLTSSDD MLIKLWNWEK MWACQRVFEG HTHYVMQIVF NPKDNNTFAS ASLDRTVKVW QLGSNFANFT LEGHEKGVNC VDYYHGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NISAVCFHPE LPIVLTGSED GTVRIWHSGT YRLETCLNYG FERVWTISSM RGTNNVALGY DEGSIIIKVG REEPAMSMDV VGSKIIWAKH SEMQQVNLKT IADGTEIKDG ERLPVATKDM GACEIYPQTI AHNPNGRFVV VCGDGEYIIY TSMALRNKAF GSAQEFVWAL ESNEYAIREN NGTVRLFRNF KERKSFTPEY GAESIYGGYY FGVKTSSGLA FYDWETLQLV RRIEVQPKNV FWNESGSLVC LATDDSYFVL GVDTAQVANA VETKEGLEDD GVESAFNVLG EVSECVKTGL WVGDCFIYTN SVNRINYYVG GEIVTVSHLD RTMYLLGYVP KDNRIYLGDK ELNVISFCLQ LSVLEYQTAV MRRDFERADV VLPTIPKEHR TRVAHFLEKQ GFKSQALQVS TDADHKFDLA LQIGDLEIAL KLARESENSQ KWSQLADVAS SKNNMSLVKE CMQKANDLSG LLLLSTASGD AQLLEVVGAA GSAQGHHNLA FLSAFLRSDV ERCLEILIET NRLPEAAFFA RTYLPSQMSR IVELWREKLG KVNEKAGQSL ADPAQYTNLF PGLGDALRVE QHLQEERARK APARLAANLP LNSERHPLQE LFAAEQGAAG QHLEEKVKPA YVPAQAVVSS SQVAEPTSAA DDDDDLDLEI DGITLDDNID TTDVNLDDDF LSDD // ID CORT_DROME STANDARD; PRT; 483 AA. AC Q960N3; Q9VMA1; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein cortex. GN CORT OR CG11330. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND MUTANTS QW55 AND RH65. RX MEDLINE=21150807; PubMed=11252055; RA Chu T., Henrion G., Haegeli V., Strickland S.; RT "Cortex, a Drosophila gene required to complete oocyte meiosis, is a RT member of the Cdc20/fizzy protein family."; RL Genesis 29:141-152(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 10-483 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP INDUCTION. RX MEDLINE=20384592; PubMed=10924478; RA Harms E., Chu T., Henrion G., Strickland S.; RT "The only function of Grauzone required for Drosophila oocyte meiosis RT is transcriptional activation of the cortex gene."; RL Genetics 155:1831-1839(2000). CC -!- FUNCTION: ESSENTIAL FOR FEMALE MEIOSIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN OVARIES. EXPRESSED IN CC NURSE CELLS FROM STAGE 6 TO STAGE 12 EGG CHAMBERS. AS OOCYTE CC MATURES, IT IS TRANSFERRED FROM THE NURSE CELLS TO THE OOCYTE. CC -!- DEVELOPMENTAL STAGE: ZYGOTICALLY EXPRESSED DURING OOGENESIS AND CC MATERNALLY DEPOSITED IN OOCYTES. MATERNAL EXPRESSION RAPIDLY DROPS CC OFF AFTER 1HR. CC -!- INDUCTION: EXPRESSION IS TRANSCRIPTIONALLY ACTIVATED BY GRAU. CC -!- SIMILARITY: CONTAINS 5 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY033478; AAK54464.1; -. DR EMBL; AE003614; AAF52421.1; -. DR EMBL; AY051966; AAK93390.1; ALT_INIT. DR GermOnline; 209841; -. DR FlyBase; FBgn0000351; cort. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0007143; P:female meiosis; IMP. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 3. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Meiosis; Repeat; Developmental protein; WD repeat. FT REPEAT 158 195 WD 1. FT REPEAT 196 237 WD 2. FT REPEAT 245 284 WD 3. FT REPEAT 287 326 WD 4. FT REPEAT 421 460 WD 5. FT MUTAGEN 303 303 Y->C: IN QW55; ABNORMAL ARREST IN FEMALE FT MEIOSIS. FT MUTAGEN 431 483 MISSING: IN RH65; ABNORMAL ARREST IN FT FEMALE MEIOSIS. SQ SEQUENCE 483 AA; 55574 MW; 007DD0190DE06735 CRC64; MFVEMSVCDS PNKNSKLDKK SLTPFKKVRR KNWKQEAAYK SDTSKGQEVS YVGERFIPNR FERENIEFNL KYIGKRKERD ILETGVTLTA SYWRQSGFIS NINRTFGIGE RRLFQFSSQQ GTRSRVVDND SADSDWPCNP RARPYAIQNA THEMPGICSP VDYNMMDWSS GGMVAMSSGQ DVMLWRNLDE STMVFSVESP TSLKYSPDGK HLAIGCMDRN YPVLDLWEVR SPTEFLVSYR KLFFKSMGYI SCIEWSHDGK EVICGTQCGV IIVLAMPTLN TLMQLREHRH TVKKMKFAPT HKYFASSDTD GKIFIFDAVL KVRLLKLDGR SIVFDWHPWT GEDLAVAERS PASIFIFNIP RRQFVASYRR RDDRIVIKTL TYSKITGELL VNVIRRDDAD LAVCEILVLA SLNRVVDLMS HQDRGTLFLM WNPDGTKIAT GGLDDTFSLW NFFPTYKREA ILRKQEQKAK DKCSSLSLYK GIR // ID CORZ_DROME STANDARD; PRT; 154 AA. AC Q26377; Q9VFK7; DT 15-JUL-1998 (Rel. 36, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Crz precursor [Contains: Corazonin; Corazonin-precursor-related DE peptide (CPRP)]. GN CRZ OR CG3302. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-82 FROM N.A. RX MEDLINE=95032110; PubMed=7945373; RA Veenstra J.A.; RT "Isolation and structure of the Drosophila corazonin gene."; RL Biochem. Biophys. Res. Commun. 204:292-296(1994). RN [3] RP SEQUENCE OF 20-30, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- FUNCTION: CARDIOACTIVE PEPTIDE. CORAZONIN IS PROBABLY INVOLVED CC IN THE PHYSIOLOGICAL REGULATION OF THE HEART BEAT. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003704; AAF55046.1; -. DR EMBL; S74038; AAB32283.1; ALT_SEQ. DR FlyBase; FBgn0013767; Crz. KW Neuropeptide; Amidation; Cleavage on pair of basic residues; Signal; KW Pyrrolidone carboxylic acid. FT SIGNAL 1 19 FT PEPTIDE 20 30 CORAZONIN. FT PEPTIDE 34 67 CORAZONIN-PRECURSOR-RELATED PEPTIDE. FT PROPEP 68 154 FT MOD_RES 20 20 PYRROLIDONE CARBOXYLIC ACID. FT MOD_RES 30 30 AMIDATION (G-31 PROVIDE AMIDE GROUP). FT CONFLICT 81 81 L -> Q (IN REF. 2). SQ SEQUENCE 154 AA; 17154 MW; 06046282A1C61A2F CRC64; MLRLLLLPLF LFTLSMCMGQ TFQYSRGWTN GKRSFNAASP LLANGHLHRA SELGLTDLYD LQDWSSDRRL ERCLSQLQRS LIARNCVPGS DFNANRVDPD PENSAHPRLS NSNGENVLYS SANIPNRHRQ SNELLEELSA AGGASAEPNV FGKH // ID COX1_DROME STANDARD; PRT; 512 AA. AC P00399; Q9MGN6; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome c oxidase polypeptide I (EC 1.9.3.1). GN MT:COI OR COI. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83245048; PubMed=6408489; RA de Bruijn M.H.L.; RT "Drosophila melanogaster mitochondrial DNA, a novel organization and RT genetic code."; RL Nature 304:234-241(1983). RN [2] RP SEQUENCE FROM N.A., AND VARIANT PHE-128. RC STRAIN=Oregon-R, and Zimbabwe 53; RX MEDLINE=20363871; PubMed=10903372; RA Ballard J.W.O.; RT "Comparative genomics of mitochondrial DNA in members of the RT Drosophila melanogaster subgroup."; RL J. Mol. Evol. 51:48-63(2000). CC -!- FUNCTION: CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CC CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- CC 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CC CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CC CYTOCHROME C ARE TRANSFERRED VIA THE COPPER A CENTER OF SUBUNIT 2 CC AND HEME A OF SUBUNIT 1 TO THE BIMETALLIC CENTER FORMED BY HEME A3 CC AND COPPER B. CC -!- CATALYTIC ACTIVITY: 4 FERROCYTOCHROME C + O(2) = 4 FERRICYTOCHROME CC C + 2 H(2)O. CC -!- PATHWAY: RESPIRATORY CHAIN; TERMINAL STEP. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE. CONTAINS 12 POTENTIAL TRANSMEMBRANE DOMAINS. CC -!- SIMILARITY: BELONGS TO THE HEME-COPPER RESPIRATORY OXIDASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01404; AAB59239.1; ALT_INIT. DR EMBL; U37541; AAC47812.2; -. DR EMBL; AF200828; AAF77227.1; -. DR EMBL; AF200829; AAF77245.1; -. DR PIR; A93307; ODFF1. DR HSSP; P00396; 2OCC. DR FlyBase; FBgn0013674; mt:CoI. DR InterPro; IPR000883; COX1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR PROSITE; PS00077; COX1; 1. KW Oxidoreductase; Heme; Copper; Mitochondrion; Transmembrane; KW Respiratory chain; Inner membrane; Polymorphism. FT METAL 60 60 IRON (HEME A AXIAL LIGAND) (PROBABLE). FT METAL 239 239 COPPER B (PROBABLE). FT METAL 243 243 COPPER B (PROBABLE). FT METAL 289 289 COPPER B (PROBABLE). FT METAL 290 290 COPPER B (PROBABLE). FT METAL 375 375 IRON (HEME A3 AXIAL LIGAND) (PROBABLE). FT METAL 377 377 IRON (HEME A AXIAL LIGAND) (PROBABLE). FT CROSSLNK 239 243 1'-histidyl-3'-tyrosine (His-Tyr) FT (By similarity). FT VARIANT 128 128 Y -> F (IN STRAIN ZIMBABWE 53). SQ SEQUENCE 512 AA; 56503 MW; F7B95FF298EBBA0F CRC64; MSRQWLFSTN HKDIGTLYFI FGAWAGMVGT SLSILIRAEL GHPGALIGDD QIYNVIVTAH AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWLLPPALSL LLVSSMVENG AGTGWTVYPP LSAGIAHGGA SVDLAIFSLH LAGISSILGA VNFITTVINM RSTGISLDRM PLFVWSVVIT ALLLLLSLPV LAGAITMLLT DRNLNTSFFD PAGGGDPILY QHLFWFFGHP EVYILILPGF GMISHIISQE SGKKETFGSL GMIYAMLAIG LLGFIVWAHH MFTVGMDVDT RAYFTSATMI IAVPTGIKIF SWLATLHGTQ LSYSPAILWA LGFVFLFTVG GLTGVVLANS SVDIILHDTY YVVAHFHYVL SMGAVFAIMA GFIHWYPLFT GLTLNNKWLK SHFIIMFIGV NLTFFPQHFL GLAGMPRRYS DYPDAYTTWN IVSTIGSTIS LLGILFFFFI IWESLVSQRQ VIYPIQLNSS IEWYQNTPPA EHSYSELPLL TN // ID COX2_DROME STANDARD; PRT; 228 AA. AC P00408; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Cytochrome c oxidase polypeptide II (EC 1.9.3.1). GN MT:COII OR COII. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=83245048; PubMed=6408489; RA de Bruijn M.H.L.; RT "Drosophila melanogaster mitochondrial DNA, a novel organization and RT genetic code."; RL Nature 304:234-241(1983). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Zimbabwe 53; RX MEDLINE=20363871; PubMed=10903372; RA Ballard J.W.O.; RT "Comparative genomics of mitochondrial DNA in members of the RT Drosophila melanogaster subgroup."; RL J. Mol. Evol. 51:48-63(2000). CC -!- FUNCTION: CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CC CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- CC 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. SUBUNIT 2 CC TRANSFERS THE ELECTRONS FROM CYTOCHROME C VIA ITS BINUCLEAR COPPER CC A CENTER TO THE BIMETALLIC CENTER OF THE CATALYTIC SUBUNIT 1. CC -!- CATALYTIC ACTIVITY: 4 FERROCYTOCHROME C + O(2) = 4 FERRICYTOCHROME CC C + 2 H(2)O. CC -!- COFACTOR: COPPER A. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME C OXIDASE SUBUNIT 2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01404; AAB59240.1; -. DR EMBL; U37541; AAC47813.1; -. DR EMBL; AF200828; AAF77228.1; -. DR EMBL; AF200829; AAF77240.1; -. DR PIR; A00476; OBFF2. DR FlyBase; FBgn0013675; mt:CoII. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR002429; Cyt_c_ox_2. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR ProDom; PD000131; Copper_CuA; 1. DR PROSITE; PS00078; COX2; 1. KW Oxidoreductase; Copper; Mitochondrion; Transmembrane; Inner membrane; KW Electron transport; Respiratory chain. FT DOMAIN 1 26 MITOCHONDRIAL INTERMEMBRANE (POTENTIAL). FT TRANSMEM 27 48 POTENTIAL. FT DOMAIN 49 62 MITOCHONDRIAL MATRIX (POTENTIAL). FT TRANSMEM 63 82 POTENTIAL. FT DOMAIN 83 228 MITOCHONDRIAL INTERMEMBRANE (POTENTIAL). FT METAL 161 161 COPPER A (PROBABLE). FT METAL 196 196 COPPER A (PROBABLE). FT METAL 200 200 COPPER A (PROBABLE). FT METAL 204 204 COPPER A (PROBABLE). SQ SEQUENCE 228 AA; 26190 MW; 65FF4502C543335D CRC64; MSTWANLGLQ DSASPLMEQL IFFHDHALLI LVMITVLVGY LMFMLFFNNY VNRFLLHGQL IEMIWTILPA IILLFIALPS LRLLYLLDEI NEPSVTLKSI GHQWYWSYEY SDFNNIEFDS YMIPTNELMT DGFRLLDVDN RVVLPMNSQI RILVTAADVI HSWTVPALGV KVDGTPGRLN QTNFFINRPG LFYGQCSEIC GANHSFMPIV IESVPVNYFI KWISSNNS // ID COX3_DROME STANDARD; PRT; 262 AA. AC P00417; Q9MGN4; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Cytochrome c oxidase polypeptide III (EC 1.9.3.1). GN MT:COIII OR COIII. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND VARIANT MET-170. RC STRAIN=Oregon-R, and Zimbabwe 53; RX MEDLINE=20363871; PubMed=10903372; RA Ballard J.W.O.; RT "Comparative genomics of mitochondrial DNA in members of the RT Drosophila melanogaster subgroup."; RL J. Mol. Evol. 51:48-63(2000). RN [2] RP SEQUENCE OF 1-179 FROM N.A. RX MEDLINE=83245048; PubMed=6408489; RA de Bruijn M.H.L.; RT "Drosophila melanogaster mitochondrial DNA, a novel organization and RT genetic code."; RL Nature 304:234-241(1983). RN [3] RP SEQUENCE OF 179-262 FROM N.A. RX MEDLINE=83220794; PubMed=6304652; RA Clary D.O., Wahleithner J.A., Wolstenholme D.R.; RT "Transfer RNA genes in Drosophila mitochondrial DNA: related 5' RT flanking sequences and comparisons to mammalian mitochondrial tRNA RT genes."; RL Nucleic Acids Res. 11:2411-2425(1983). RN [4] RP SEQUENCE OF 179-262 FROM N.A. RC STRAIN=Bretagne; RX MEDLINE=88212147; PubMed=3130291; RA Garesse R.; RT "Drosophila melanogaster mitochondrial DNA: gene organization and RT evolutionary considerations."; RL Genetics 118:649-663(1988). CC -!- FUNCTION: SUBUNITS I, II AND III FORM THE FUNCTIONAL CORE OF CC THE ENZYME COMPLEX. CC -!- CATALYTIC ACTIVITY: 4 FERROCYTOCHROME C + O(2) = 4 FERRICYTOCHROME CC C + 2 H(2)O. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME C OXIDASE SUBUNIT 3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF200828; AAF77231.1; -. DR EMBL; AF200829; AAF77243.1; -. DR EMBL; J01404; AAB59243.1; -. DR EMBL; M37275; AAA69708.1; -. DR EMBL; U37541; AAC47816.1; -. DR PIR; A00485; OTFF3. DR FlyBase; FBgn0013676; mt:CoIII. DR InterPro; IPR000298; CytC_oxdse_III. DR Pfam; PF00510; COX3; 1. DR ProDom; PD000382; CytC_oxdse_III; 1. DR PROSITE; PS50253; COX3; 1. KW Oxidoreductase; Mitochondrion; Transmembrane; Polymorphism. FT VARIANT 170 170 L -> M (IN STRAIN ZIMBABWE 53). SQ SEQUENCE 262 AA; 30064 MW; 68D5AEFC2297C130 CRC64; MSTHSNHPFH LVDYSPWPLT GAIGAMTTVS GMVKWFHQYD ISLFVLGNII TILTVYQWWR DVSREGTYQG LHTYAVTIGL RWGMILFILS EVLFFVSFFW AFFHSSLSPA IELGASWPPM GIISFNPFQI PLLNTAILLA SGVTVTWAHH SLMENNHSQT TQGLFFTVLL GIYFTILQAY EYIEAPFTIA DSIYGSTFFM ATGFHGIHVL IGTTFLLVCL LRHLNNHFSK NHHFGFEAAA WYWHFVDVVW LFLYITIYWW GG // ID COXA_DROME STANDARD; PRT; 149 AA. AC Q94514; Q9VGH4; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome c oxidase polypeptide Va, mitochondrial precursor DE (EC 1.9.3.1). GN COVA OR CG14724. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS IS THE HEME A-CONTAINING CHAIN OF CYTOCHROME C CC OXIDASE, THE TERMINAL OXIDASE IN MITOCHONDRIAL ELECTRON TRANSPORT. CC -!- CATALYTIC ACTIVITY: 4 FERROCYTOCHROME C + O(2) = 4 FERRICYTOCHROME CC C + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME C OXIDASE VA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y09065; CAA70286.1; -. DR EMBL; AE003693; AAF54706.1; -. DR FlyBase; FBgn0019624; CoVa. DR InterPro; IPR003204; Cyt_c_ox5A. DR Pfam; PF02284; COX5A; 1. KW Oxidoreductase; Heme; Mitochondrion; Inner membrane; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 149 CYTOCHROME C OXIDASE POLYPEPTIDE VA. FT CONFLICT 73 73 S -> N (IN REF. 1). SQ SEQUENCE 149 AA; 16622 MW; 82E1A198D5D8F55A CRC64; MLSITARNLA SALRSSLVGT SSRVAAVRCL HGTEESAEEF DKRYEKYFSR EGIDGWEIRK GMNDLLGMDL VPSPKIIEAG LRASRRVNDI ALAIRWLEGC KDKCGDQKAT LYPYLLEKIT PTLQELGIPT IEELGYDKPE LALKSVYDA // ID CP18_DROME STANDARD; PRT; 538 AA. AC Q95078; Q27767; Q9VWR4; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome P450 18a1 (EC 1.14.-.-) (CYPXVIIIA1). GN CYP18A1 OR CYP18 OR EIG17-1 OR CG6816. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, INDUCTION, AND TISSUE SPECIFICITY. RC TISSUE=Larva; RX MEDLINE=97398464; PubMed=9256362; RA Bassett M.H., McCarthy J.L., Waterman M.R., Sliter T.J.; RT "Sequence and developmental expression of Cyp18, a member of a new RT cytochrome P450 family from Drosophila."; RL Mol. Cell. Endocrinol. 131:39-49(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 459-479 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94019381; PubMed=8413299; RA Hurban P., Thummel C.S.; RT "Isolation and characterization of fifteen ecdysone-inducible RT Drosophila genes reveal unexpected complexities in ecdysone RT regulation."; RL Mol. Cell. Biol. 13:7101-7111(1993). CC -!- FUNCTION: PROBABLY INVOLVED IN STEROID HORMONES BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN BODY WALL (EPIDERMAL AND MUSCLE CC CELLS) AND MID-AND HIND-GUT. CC -!- DEVELOPMENTAL STAGE: LOW LEVELS THROUGHOUT POSTEMBRYONIC CC DEVELOPMENT. CC -!- INDUCTION: BY 20-HYDROXYECDYSONE DURING THE THREE LARVAL STAGES, CC AT PUPARIATION AND IN PUPAE. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U44753; AAB69750.1; -. DR EMBL; AE003509; AAF48874.1; -. DR EMBL; S66112; AAB28524.1; -. DR HSSP; P00179; 1DT6. DR FlyBase; FBgn0010383; Cyp18a1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Transmembrane; Heme; Microsome; KW Endoplasmic reticulum; Developmental protein. FT TRANSMEM 24 44 POTENTIAL. FT METAL 466 466 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CONFLICT 19 19 Q -> E (IN REF. 1). FT CONFLICT 478 479 LF -> PV (IN REF. 3). FT CONFLICT 520 520 R -> S (IN REF. 1). SQ SEQUENCE 538 AA; 61948 MW; A1C95E74505C28CE CRC64; MLADSYLIKF VLRQLQVQQD GDAQHLLMVF LGLLALVTLL QWLVRNYREL RKLPPGPWGL PVIGYLLFMG SEKHTRFMEL AKQYGSLFST RLGSQLTVVM SDYKMIRECF RREEFTGRPD TPFMQTLNGY GIINSTGKLW KDQRRFLHDK LRQFGMTYMG NGKQQMQKRI MTEVHEFIGH LHASDGQPVD MSPVISVAVS NVICSLMMST RFSIDDPKFR RFNFLIEEGM RLFGEIHTVD YIPTMQCFPS ISTAKNKIAQ NRAEMQRFYQ DVIDDHKRSF DPNNIRDLVD FYLCEIEKAK AEGTDAELFD GKNHEEQLVQ VIIDLFSAGM ETIKTTLLWI NVFMLRNPKE MRRVQDELDQ VVGRHRLPTI EDLQYLPITE STILESMRRS SIVPLATTHS PTRDVELNGY TIPAGSHVIP LINSVHMDPN LWEKPEEFRP SRFIDTEGKV RKPEYFIPFG VGRRMCLGDV LARMELFLFF ASFMHCFDIA LPEGQPLPSL KGNVGATITP ESFKVCLKRR PLGPTAADPH HMRNVGAN // ID CP2B_DROME STANDARD; PRT; 151 AA. AC Q9NIP6; Q9VAE2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cardio acceleratory peptide 2b precursor (Myotropin-CAP2b-like DE protein) [Contains: CAP-1 (Capa-1) (CAP2b-1); CAP-2 (Capa-2) DE (CAP2b-2); CAP-3 (Capa-3) (CAP2b-3) (Myotropin) (Pyrokinin)]. GN CAPA OR MT-CAP2B OR CG15520. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=21955908; PubMed=11959669; RA Kean L., Cazenave W., Costes L., Broderick K.E., Graham S., RA Pollock V.P., Davies S.A., Veenstra J.A., Dow J.A.; RT "Two nitridergic peptides are encoded by the gene capability in RT Drosophila melanogaster."; RL Am. J. Physiol. 282:R1297-R1307(2002). RN [2] RP SEQUENCE FROM N.A. RA Vanden Broeck J.J.M.; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 31-42 AND 83-92, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). RN [7] RP FUNCTION. RC STRAIN=Canton-S; RX MEDLINE=22177201; PubMed=12177421; RA Park Y., Kim Y.J., Adams M.E.; RT "Identification of G protein-coupled receptors for Drosophila PRXamide RT peptides, CCAP, corazonin, and AKH supports a theory of RT ligand-receptor coevolution."; RL Proc. Natl. Acad. Sci. U.S.A. 99:11423-11428(2002). RN [8] RP FUNCTION. RX MEDLINE=22347021; PubMed=12459185; RA Iversen A., Cazzamali G., Williamson M., Hauser F., RA Grimmelikhuijzen C.J.P.; RT "Molecular cloning and functional expression of a Drosophila receptor RT for the neuropeptides capa-1 and -2."; RL Biochem. Biophys. Res. Commun. 299:628-633(2002). RN [9] RP REVIEW. RX MEDLINE=21107400; PubMed=11179818; RA Vanden Broeck J.J.M.; RT "Neuropeptides and their precursors in the fruitfly, Drosophila RT melanogaster."; RL Peptides 22:241-254(2001). CC -!- FUNCTION: CAP-1 AND CAP-2, BUT NOT CAP-3 ARE LIGANDS FOR THE CAPA CC RECEPTOR. CAP-1 AND CAP-2 ARE PROBABLY COMPONENTS OF THE SIGNAL CC TRANSDUCTION PATHWAY THAT LEADS TO MALPIGHIAN TUBULE FLUID CC SECRETION VIA THE SECOND MESSENGER NITRIC OXIDE. CAP-3 MAY BE A CC LIGAND FOR THE CG8795 G PROTEIN COUPLED RECEPTORS. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: IN LARVAE, THE PRECURSOR PEPTIDE IS CC EXCLUSIVELY PRESENT IN A SINGLE PAIR OF NEUROENDOCRINE CELLS IN CC THE LABIAL NEUROMERE AND THREE PAIRS OF CELLS IN THE VENTRAL CC GANGLION ABDOMINAL NEUROMERES. CC -!- SIMILARITY: BELONGS TO THE PYROKININ FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF203878; AAF62876.1; -. DR EMBL; AJ291724; CAC17603.1; -. DR EMBL; AE003771; AAF56969.2; -. DR EMBL; AY069234; AAL39379.1; -. DR FlyBase; FBgn0039722; capa. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0016084; F:myostimulatory hormone activity; NAS. DR GO; GO:0005184; F:neuropeptide hormone activity; NAS. DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS. DR InterPro; IPR001484; Pyrokinin. DR PROSITE; PS00539; PYROKININ; 1. KW Neuropeptide; Signal; Cleavage on pair of basic residues; Amidation. FT SIGNAL 1 21 POTENTIAL. FT PROPEP 22 28 FT PEPTIDE 31 42 CAP-1. FT PROPEP 45 80 FT PEPTIDE 83 92 CAP-2. FT PROPEP 95 113 FT PEPTIDE 116 130 CAP-3. FT PROPEP 134 151 FT MOD_RES 42 42 AMIDATION (G-43 PROVIDE AMIDE GROUP). FT MOD_RES 92 92 AMIDATION (G-93 PROVIDE AMIDE GROUP). FT MOD_RES 130 130 AMIDATION (G-131 PROVIDE AMIDE GROUP). SQ SEQUENCE 151 AA; 16507 MW; F9E97535665B37E5 CRC64; MKSMLVHIVL VIFIIAEFST AETDHDKNRR GANMGLYAFP RVGRSDPSLA NSLRDGLEAG VLDGIYGDAS QEDYNEADFQ KKASGLVAFP RVGRGDAELR KWAHLLALQQ VLDKRTGPSA SSGLWFGPRL GKRSVDAKSF ADISKGQKEL N // ID CPD1_DROME STANDARD; PRT; 355 AA. AC P22058; Q24215; Q9VHH3; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chromosomal protein D1. GN D1 OR CG9745. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-33. RX MEDLINE=89255282; PubMed=2542275; RA Ashley C.T., Pendleton C.G., Jennings W.W., Saxena A., Glover C.V.C.; RT "Isolation and sequencing of cDNA clones encoding Drosophila RT chromosomal protein D1. A repeating motif in proteins which recognize RT at DNA."; RL J. Biol. Chem. 264:8394-8401(1989). RN [2] RP SEQUENCE FROM N.A. RA Kleven D.T., Murdock D.G., Crawford M.J., Glover C.V.C.; RT "Structure of the gene encoding Drosophila chromosomal protein D1."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS SATELLITE DNA-ASSOCIATED PROTEIN IS A DOUBLE- CC STRANDED DNA BINDING PROTEIN SPECIFIC FOR TRACTS OF PURE AT DNA. CC IT MAY PLAY A ROLE IN ORGANIZING THE HIGHER ORDER STRUCTURE OF CC EUCHROMATIN AS WELL AS HETEROCHROMATIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: D1 MAY BE THE MOST ABUNDANT MEMBER OF A SMALL CC FAMILY OF D1-LIKE PROTEINS. CC -!- SIMILARITY: CONTAINS 11 A.T HOOK DNA-BINDING REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04725; AAA28440.1; -. DR EMBL; U56393; AAB01211.1; -. DR EMBL; AE003682; AAF54341.1; -. DR PIR; A33821; A33821. DR FlyBase; FBgn0000412; D1. DR InterPro; IPR000637; AT_hook. DR Pfam; PF02178; AT_hook; 10. DR PRINTS; PR00929; ATHOOK. DR SMART; SM00384; AT_hook; 9. KW Nuclear protein; DNA-binding; Chromosomal protein; Phosphorylation; KW Repeat; Acetylation. FT MOD_RES 1 1 ACETYLATION (PROBABLE). FT DNA_BIND 7 14 A.T HOOK 1. FT DNA_BIND 34 41 A.T HOOK 2. FT DNA_BIND 60 67 A.T HOOK 3. FT DNA_BIND 94 101 A.T HOOK 4. FT DNA_BIND 122 129 A.T HOOK 5. FT DNA_BIND 155 162 A.T HOOK 6. FT DNA_BIND 174 181 A.T HOOK 7. FT DNA_BIND 196 203 A.T HOOK 8. FT DNA_BIND 219 226 A.T HOOK 9. FT DNA_BIND 262 269 A.T HOOK 10. FT DNA_BIND 281 288 A.T HOOK 11. FT MOD_RES 133 133 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 135 135 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 186 186 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 246 246 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 311 311 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 332 332 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT CONFLICT 291 291 D -> E (IN REF. 2). SQ SEQUENCE 355 AA; 37000 MW; 516744AF0D048969 CRC64; MEEVAVKKRG RPSKASVGGK SSTAAVAAIS PGIKKRGRPA KNKGSSGGGG QRGRPPKASK IQNDEDPEDE GEEDGDGDGS GAELANNSSP SPTKGRGRPK SSGGAGSGSG DSVKTPGSAK KRKAGRPKKH QPSDSENEDD QDEDDDGNSS IEERRPVGRP SAGSVNLNIS RTGRGLGRPK KRAVESNGDG EPQVPKKRGR PPQNKSGSGG STGYVPTGRP RGRPKANAAP VEKHEDNDDD QDDENSGEEE HSSPEKTVVA PKKRGRPSLA AGKVSKEETT KPRSRPAKNI DDDADDADSA DQGQHNSKKE SNDEDRAVDG TPTKGDGLKW NSDGENDAND GYVSDNYNDS ESVAA // ID CPN_DROME STANDARD; PRT; 865 AA. AC Q02910; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calphotin. GN CPN OR CAP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93165729; PubMed=8094559; RA Martin J.H., Benzer S., Rudnicka M., Miller C.A.; RT "Calphotin: a Drosophila photoreceptor cell calcium-binding protein."; RL Proc. Natl. Acad. Sci. U.S.A. 90:1531-1535(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93165730; PubMed=8434015; RA Ballinger D.G., Xue N., Harshman K.D.; RT "A Drosophila photoreceptor cell-specific protein, calphotin, binds RT calcium and contains a leucine zipper."; RL Proc. Natl. Acad. Sci. U.S.A. 90:1536-1540(1993). CC -!- FUNCTION: MIGHT FUNCTION AS A CALCIUM-SEQUESTERING "SPONGE" TO CC REGULATE THE AMOUNT OF FREE CYTOPLASMIC CALCIUM. IT BINDS 0.3 MOLE CC OF CA(2+) PER MOLE OF PROTEIN. CC -!- SUBUNIT: HOMODIMER (PROBABLE). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC; HYPODENSE COMPARTMENT. CC -!- TISSUE SPECIFICITY: SOMA AND AXONS OF PHOTORECEPTOR CELLS OF CC COMPOUND EYES AND OCELLI. CC -!- DEVELOPMENTAL STAGE: EXPRESSED EARLY IN PHOTORECEPTOR CELL CC DEVELOPMENT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L02111; AAA28405.1; -. DR EMBL; L05080; AAA28420.1; -. DR PIR; A47282; A47282. DR PIR; A47283; A47283. DR FlyBase; FBgn0010218; Cpn. DR GO; GO:0005509; F:calcium ion binding; IDA. KW Calcium-binding. FT CONFLICT 36 36 A -> AVAPAVVA (IN REF. 2). FT CONFLICT 43 43 I -> T (IN REF. 2). FT CONFLICT 64 64 I -> V (IN REF. 2). FT CONFLICT 76 76 T -> A (IN REF. 2). FT CONFLICT 100 100 P -> PP (IN REF. 2). FT CONFLICT 126 127 VQ -> AP (IN REF. 2). FT CONFLICT 154 154 I -> V (IN REF. 2). FT CONFLICT 160 160 S -> T (IN REF. 2). FT CONFLICT 534 534 A -> E (IN REF. 2). FT CONFLICT 699 699 I -> T (IN REF. 2). FT CONFLICT 703 703 V -> L (IN REF. 2). FT CONFLICT 721 721 D -> E (IN REF. 2). SQ SEQUENCE 865 AA; 84781 MW; 2110417E0B0E7CFE CRC64; MEPGTIPSPV SAPVAAPVTP SAVAAPVQVV SPAAVAPAPA APIAVTPVAP PPTLASVQPA TVTIPAPAPI AAASVTPVAS VAPPVVAAPT PPAASPVSTP VAVAQIPVAV SAPVAPPVAA TPTPVVQIPV AAPVIATPPV AASAPTPAAV TPVISPVIAS PPVVPANTTV PVAAPVAAVP AAVPVVAPVL APAVAPAVAP VVAETPAPPP VAEIPVATIP ECVAPLIPEV SVVATKPLAA AEPVVVAPPA TETPVVAPAA ASPHVSVAPA VETAVVAPVS ASTEPPVAAA TLTTAPETPA LAPVVAESQV AANTVVATPP TPAPEPETIA PPVVAETPEV ASVAVAETTP PVVPPVAAES IPAPVVATTP VPATLAVTDP DVTASAVPEL PPVIAPSPVP SAVAETPVDL APPVLPPVAA EPVPAVVAEE TPETPAPASA PVTIAALDIP EVAPVIAAPS DAPAEAPSAA APIVSTPPTT ASVPETTAPP AAVPTEPIDV SVLSEAAIET PVAPPVEVTT EVAVADVAPP EAAADLIIEP VEPPAPIPDL LEQTTSVPAV EAAESTSSPI PETSLPPPNE AVASPEVAVA PITAPEPIPE PEPSLATPTE PIPVEAPVVI QEAVDAVEVP VTETSTSIPE TTVEFPEAVA EKVLDPAITE APVTTQEPDV ANINDGAPAT EITTPAVEIV TAAAEVSDIA IPVIDPPVPQ EIAVAEIPET DTKPAEVIVE QSTIPIEAPV PEVSKYAEPV ISEAPAAEVP ITAGDNPDNT SVGISEVVPT IAEKPVEEVP TSEIPEQSSS PSDSVPVAKI TPLLRDLQTT DVSLLAIAAT LDAIGEKLKD QKARNQQVMD RLCEIEKILG PPKSN // ID CPO_DROME STANDARD; PRT; 615 AA. AC Q01617; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Putative couch potato protein. GN CPO. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS CPO 17; CPO 61.1 AND CPO 61.2). RX MEDLINE=93051332; PubMed=1427076; RA Bellen H.J., Kooyer S., D'Evelyn D., Pearlman J.; RT "The Drosophila couch potato protein is expressed in nuclei of RT peripheral neuronal precursors and shows homology to RNA-binding RT proteins."; RL Genes Dev. 6:2125-2136(1992). CC -!- FUNCTION: MAY PLAY A ROLE IN THE DEVELOPMENT OR FUNCTION OF THE CC PERIPHERAL NERVOUS SYSTEM BY REGULATING THE PROCESSING OF NERVOUS CC SYSTEM-SPECIFIC TRANSCRIPTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Cpo 61.1; CC IsoId=Q01617-1; Sequence=Displayed; CC Name=Cpo 17; CC IsoId=Q01617-2; Sequence=VSP_005780, VSP_005781; CC Name=Cpo 61.2; CC IsoId=Q01617-3; Sequence=VSP_005779, VSP_005782, VSP_005783; CC -!- TISSUE SPECIFICITY: EXPRESSED IN NEURAL PRECURSORS AND THEIR CC DAUGHTER CELLS IN THE EMBRYONIC PERIPHERAL NERVOUS SYSTEM. LESS CC ABUNDANT IN A NUMBER OF GLIAL CELLS IN THE PERIPHERAL AND CENTRAL CC NERVOUS SYSTEMS AND ALSO PRESENT AT LOW LEVELS IN THE DEVELOPING CC GUT. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -!- CAUTION: THE AUTHORS PROPOSE THAT THE INITIATOR IS A LEUCINE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z14974; CAA78696.1; -. DR EMBL; Z14311; CAA78663.1; -. DR EMBL; Z14312; CAA78664.1; -. DR FlyBase; FBgn0000363; cpo. DR GO; GO:0005634; C:nucleus; IDA. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Nuclear protein; Alternative splicing; Repeat; RNA-binding. FT DOMAIN 24 31 POLY-ALA. FT DOMAIN 65 68 POLY-SER. FT DOMAIN 90 114 NUCLEAR LOCALIZATION SIGNAL. FT DOMAIN 100 173 7 X 5 AA APPROXIMATE REPEATS OF P-V-S-V- FT P. FT REPEAT 100 104 1. FT REPEAT 118 122 2. FT REPEAT 123 127 3. FT REPEAT 131 135 4. FT REPEAT 137 141 5. FT REPEAT 143 147 6. FT REPEAT 168 172 7. FT DOMAIN 194 206 POLY-GLN. FT DOMAIN 209 214 POLY-GLN. FT DOMAIN 217 220 POLY-GLN. FT DOMAIN 230 239 POLY-GLN. FT DOMAIN 248 252 POLY-ALA. FT DOMAIN 259 274 POLY-GLN. FT DOMAIN 290 294 POLY-GLN. FT DOMAIN 297 426 ALA/SER-RICH. FT DOMAIN 299 305 POLY-SER. FT DOMAIN 377 384 POLY-ALA. FT DOMAIN 411 419 POLY-SER. FT DOMAIN 451 533 RNA-BINDING (RRM). FT DOMAIN 583 587 POLY-ALA. FT VARSPLIC 294 294 Q -> QQ (in isoform Cpo 61.2). FT /FTId=VSP_005779. FT VARSPLIC 451 490 RTLFVSGLPMDAKPRELYLLFRAYEGYEGSLLKVTSKNGK FT -> SHSFHSAIPKDKRNKKLQIKIALGGQKRKGSGPSSEMR FT QK (in isoform Cpo 17). FT /FTId=VSP_005780. FT VARSPLIC 491 615 Missing (in isoform Cpo 17). FT /FTId=VSP_005781. FT VARSPLIC 515 535 GVRFDPDMPQTIRLEFAKSNT -> VNMHITYTYISVPFII FT ERTLK (in isoform Cpo 61.2). FT /FTId=VSP_005782. FT VARSPLIC 536 615 Missing (in isoform Cpo 61.2). FT /FTId=VSP_005783. SQ SEQUENCE 615 AA; 64313 MW; C5D8D15C373F2645 CRC64; LVKIANYQDL LGSHHQLLIA ATDAAAAAAA AEPQLQLQHL LPAAPTTPAV ISNPINSIGP INQISSSSHP SNNNQQAVFE KAITISSIAI KRRPTLPQTP ASAPQVLSPS PKRQCAAAVS VLPVTVPVPV PVSVPLPVSV PVPVSVKGHP ISHTHQIAHT HQISHSHPIS HPHHHQLTFA HPTQFAAAVA AHHQQQQQQQ AQQQQQAVQQ QQQQAVQQQQ VAYAVAASPQ LQQQQQQQQH RLAQFNQAAA AALLNQHLQQ QHQAQQQQHQ AQQQSLAHYG GYQLHRYAPQ QQQQHILLSS GSSSSKHNSN TNSNTSAGGA SAAVPIATSV AAVPTTGGSL PDSPAHESHS HESNSATASA PTTPSPAGSV TSAAPTATAT AAAAGSAAAT AAATGTPATS AVSDSNNNLN SSSSSNSNSN AIMENQMALA PLGLSQSMDS VNTASNEEEV RTLFVSGLPM DAKPRELYLL FRAYEGYEGS LLKVTSKNGK TASPVGFVTF HTRAGAEAAK QDLQGVRFDP DMPQTIRLEF AKSNTKVSKP KPQPNTATTA SHPALMHPLT GHLGGPFFPG GPELWHHPLA YSAAAAAELP GAAALHSATL VHPALHPQVP VRSYL // ID CPSA_DROME STANDARD; PRT; 1455 AA. AC Q9V726; Q960R9; Q9GV83; Q9GV84; Q9GV85; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cleavage and polyadenylation specificity factor, 160 kDa subunit (CPSF DE 160 kDa subunit) (CPSF-160) (dCPSF). GN CPSF OR DCPSF160 OR CG10110. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RC TISSUE=Eye imaginal disk; RX MEDLINE=98265927; PubMed=9604891; RA Salinas C.A., Sinclair D.A., O'Hare K., Brock H.W.; RT "Characterization of a Drosophila homologue of the 160-kDa subunit of RT the cleavage and polyadenylation specificity factor CPSF."; RL Mol. Gen. Genet. 257:672-680(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CPSF PLAYS A KEY ROLE IN PRE-MRNA 3'-END FORMATION, CC RECOGNIZING THE AAUAAA SIGNAL SEQUENCE AND INTERACTING WITH CC POLY(A)POLYMERASE AND OTHER FACTORS TO BRING ABOUT CLEAVAGE AND CC POLY(A) ADDITION. THIS SUBUNIT IS INVOLVED IN THE RNA RECOGNITION CC STEP OF THE POLYADENYLATION REACTION (BY SIMILARITY). CC -!- SUBUNIT: CPSF IS A HETEROTETRAMER COMPOSED OF FOUR DISTINCT CC SUBUNITS 160, 100, 70 AND 30 KDA (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q9V726-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9V726-2; Sequence=VSP_001216; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE CPSF160 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF241364; AAF98386.1; -. DR EMBL; AF241365; AAF98387.1; -. DR EMBL; AF241366; AAF98388.1; -. DR EMBL; AE003814; AAM68553.1; -. DR EMBL; AY051896; AAK93320.1; -. DR FlyBase; FBgn0024698; cpsf. DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specifici...; ISS. DR GO; GO:0003730; F:mRNA 3' UTR binding; ISS. DR GO; GO:0006379; P:mRNA cleavage; ISS. DR GO; GO:0006378; P:mRNA polyadenylation; ISS. DR InterPro; IPR004871; CPSF_A_C. DR Pfam; PF03178; CPSF_A; 1. KW mRNA processing; Nuclear protein; RNA-binding; Alternative splicing. FT VARSPLIC 244 278 Missing (in isoform B). FT /FTId=VSP_001216. FT CONFLICT 907 907 M -> L (IN REF. 1). FT CONFLICT 921 921 D -> E (IN REF. 1). FT CONFLICT 1076 1076 G -> D (IN REF. 1). SQ SEQUENCE 1455 AA; 164680 MW; B939D522310F479F CRC64; MFSMCKQTHS ATAVEFSIAC RFFNNLDENL VVAGANVLKV YRIAPNVEAS QRQKLNPSEM RLAPKMRLEC LATYTLYGNV MSLQCVSLAG AMRDALLISF KDAKLSVLQH DPDTFALKTL SLHYFEEDDI RGGWTGRYFV PTVRVDPDSR CAVMLVYGKR LVVLPFRKDN SLDEIELADV KPIKKAPTAM VSRTPIMASY LIALRDLDEK IDNVLDIQFL HGYYEPTLLI LYEPVRTCPG RIKVRSDTCV LVAISLNIQQ RVHPIIWTVN SLPFDCLQVY PIQKPIGGCL VMTVNAVIYL NQSVPPYGVS LNSSADNSTA FPLKPQDGVR ISLDCANFAF IDVDKLVISL RTGDLYVLTL CVDSMRTVRN FHFHKAAASV LTSCICVLHS EYIFLGSRLG NSLLLHFTEE DQSTVITLDE VEQQSEQQQR NLQDEDQNLE EIFDVDQLEM APTQAKSRRI EDEELEVYGS GAKASVLQLR KFIFEVCDSL MNVAPINYMC AGERVEFEED GVTLRPHAES LQDLKIELVA ATGHSKNGAL SVFVNCINPQ IITSFELDGC LDVWTVFDDA TKKSSRNDQH DFMLLSQRNS TLVLQTGQEI NEIENTGFTV NQPTIFVGNL GQQRFIVQVT TRHVRLLQGT RLIQNVPIDV GSPVVQVSIA DPYVCLRVLN GQVITLALRE TRGTPRLAIN KHTISSSPAV VAISAYKDLS GLFTVKGDDI NLTGSSNSAF GHSFGGYMKA EPNMKVEDEE DLLYGDAGSA FKMNSMADLA KQSKQKNSDW WRRLLVQAKP SYWLVVARQS GTLEIYSMPD MKLVYLVNDV GNGSMVLTDA MEFVPISLTT QENSKAGIVQ ACMPQHANSP LPLELSVIGL GLNGERPLLL VRTRVELLIY QVFRYPKGHL KIRFRKMDQL NLLDQQPTHI DLDENDEQEE IESYQMQPKY VQKLRPFANV GGLSGVMVCG VNPCFVFLTF RGELRIHRLL GNGDVRSFAA FNNVNIPNGF LYFDTTYELK ISVLPSYLSY DSVWPVRKVP LRCTPRQLVY HRENRVYCLI TQTEEPMTKY YRFNGEDKEL SEESRGERFI YPIGSQFEMV LISPETWEIV PDASITFEPW EHVTAFKIVK LSYEGTRSGL KEYLCIGTNF NYSEDITSRG NIHIYDIIEV VPEPGKPMTK FKIKEIFKKE QKGPVSAISD VLGFLVTGLG QKIYIWQLRD GDLIGVAFID TNIYVHQIIT VKSLIFIADV YKSISLLRFQ EEYRTLSLAS RDFNPLEVYG IEFMVDNSNL GFLVTDAERN IIVYMYQPEA RESLGGQKLL RKADYHLGQV VNTMFRVQCH QKGLHQRQPF LYENKHFVVY GTLDGALGYC LPLPEKVYRR FLMLQNVLLS YQEHLCGLNP KEYRTLKSSK KQGINPSRCI IDGDLIWSYR LMANSERNEV AKKIGTRTEE ILGDLLEIER LASVF // ID CRBA_DROME STANDARD; PRT; 515 AA. AC P29747; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Cyclic-AMP response element binding protein A (Box B binding factor-2) DE (BBF-2). GN CREBA OR BBBF2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92192458; PubMed=1532159; RA Abel T., Bhatt R., Maniatis T.; RT "A Drosophila CREB/ATF transcriptional activator binds to both fat RT body- and liver-specific regulatory elements."; RL Genes Dev. 6:466-480(1992). CC -!- FUNCTION: TRANSCRIPTIONAL ACTIVATOR. BINDS TO FAT BODY-SPECIFIC CC ENHANCERS OF ALCOHOL DEHYDROGENASE (ADH) AND YOLK PROTEIN GENES. CC BBF-2 MAY PLAY A ROLE IN FAT BODY GENE EXPRESSION. IT BINDS THE CC CONSENSUS SEQUENCE 5'T(A/C)NACGTAN(T/G)C-3'. CC -!- SUBUNIT: MAY BIND DNA AS HETERODIMERS WHIT OTHER BZIP PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: IN ALL CELL TYPES EXAMINED. CC -!- DEVELOPMENTAL STAGE: PRESENT THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE BZIP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64429; CAA45771.1; -. DR PIR; A42140; A42140. DR TRANSFAC; T01603; -. DR FlyBase; FBgn0004396; CrebA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IDA. DR GO; GO:0007435; P:salivary gland morphogenesis; NAS. DR InterPro; IPR008917; Euk_transcr_DNA. DR InterPro; IPR001630; Leuzip_CREB. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF00170; bZIP; 1. DR PRINTS; PR00041; LEUZIPPRCREB. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW Transcription regulation; Activator; DNA-binding; Nuclear protein. FT DNA_BIND 442 462 BASIC MOTIF. FT DOMAIN 468 503 LEUCINE-ZIPPER. SQ SEQUENCE 515 AA; 56528 MW; 0E08FB9655200223 CRC64; MEFYDGDLKD IWDSDLDPES LKISPDHDMH DWLFDRDVKD PTVILNDKLI SDALLNGTQP IKTEHSYSLS SDVDSLPDSP KSLQAKIEDM DDECFPAISP KTATNGRVTI DPKCLTFHVP PTHATPISRL SSNPALNTSV ADLTRSSGLQ SLQAHQPHHG SGSSHVVVAN LEHFQLPQHL YDNDCSSSVS SLRDGSMSPD ICSDIEIDES AIKDEPMSPD SSCPASPTSQ ASSSQHQLSL NLAHLQSEML FEPKHCGLLL TASSNSNNSL IKSQQRHEQI LGQDNLLMAK MEIKSEKQST SNSSGKSHAH GYGIPTTPPS SLPSDDSEGN LSPEHLFRHC RPTQPFPSLW PIQPAVSHPY GSATAASITR SSSGSASASG SSTSSTVTTT RQPIHTPLIS SQPKGSTGTL LLTEEEKRTL LAEGYPIPQK LPLTKAEEKS LKKIRRKIKN KISAQESRRK KKEYMDQLER RVEILVTENH DYKKRLEGLE ETNANLLSQL HKLQALVSKH NVKKS // ID CRB_DROME STANDARD; PRT; 2139 AA. AC P10040; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Crumbs protein precursor (95F). GN CRB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=90263104; PubMed=2344615; RA Tepass U., Theres C., Knust E.; RT "Crumbs encodes an EGF-like protein expressed on apical membranes of RT Drosophila epithelial cells and required for organization of RT epithelia."; RL Cell 61:787-799(1990). RN [2] RP SEQUENCE OF 1663-1955 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=87218537; PubMed=3107986; RA Knust E., Dietrich U., Tepass U., Bremer K.A., Weigel D., RA Vaessin H., Campos-Ortega J.A.; RT "EGF homologous sequences encoded in the genome of Drosophila RT melanogaster, and their relation to neurogenic genes."; RL EMBO J. 6:761-766(1987). CC -!- FUNCTION: MAY PLAY A ROLE IN THE DEVELOPMENT OF EPITHELIA, CC POSSIBLY FOR THE ESTABLISHMENT AND/OR MAINTENANCE OF CELL CC POLARITY. IT MAY ACT AS A SIGNAL. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- PTM: PHOSPHORYLATED IN THE CYTOPLASMIC DOMAIN (POTENTIAL). CC -!- SIMILARITY: CONTAINS 29 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 3 LAMININ G-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33753; AAA28428.1; ALT_SEQ. DR EMBL; X05144; CAA28793.1; -. DR PIR; A35672; A35672. DR PIR; B26637; B26637. DR HSSP; P00740; 1EDM. DR FlyBase; FBgn0000368; crb. DR GO; GO:0016324; C:apical plasma membrane; NAS. DR GO; GO:0016327; C:apicolateral plasma membrane; IDA. DR GO; GO:0007163; P:establishment and/or maintenance of cell po...; IMP. DR GO; GO:0016332; P:establishment and/or maintenance of polarit...; IMP. DR GO; GO:0016334; P:establishment and/or maintenance of polarit...; IMP. DR GO; GO:0045494; P:photoreceptor maintenance; IMP. DR GO; GO:0042052; P:rhabdomere development; NAS. DR GO; GO:0045186; P:zonula adherens assembly; IMP. DR GO; GO:0045218; P:zonula adherens maintenance; IMP. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR001438; EGF_II. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF00008; EGF; 26. DR Pfam; PF00054; laminin_G; 3. DR PRINTS; PR00010; EGFBLOOD. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00179; EGF_CA; 11. DR SMART; SM00282; LamG; 3. DR PROSITE; PS00010; ASX_HYDROXYL; 15. DR PROSITE; PS00022; EGF_1; 26. DR PROSITE; PS01186; EGF_2; 17. DR PROSITE; PS50026; EGF_3; 27. DR PROSITE; PS01187; EGF_CA; 12. DR PROSITE; PS50025; LAM_G_DOMAIN; 3. KW Differentiation; Repeat; EGF-like domain; Transmembrane; KW Glycoprotein; Signal; Phosphorylation. FT SIGNAL 1 90 FT CHAIN 91 2139 CRUMBS PROTEIN. FT DOMAIN 91 2084 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2085 2111 POTENTIAL. FT DOMAIN 2112 2139 CYTOPLASMIC (POTENTIAL). FT DOMAIN 267 303 EGF-LIKE 1. FT DOMAIN 306 343 EGF-LIKE 2. FT DOMAIN 348 386 EGF-LIKE 3. FT DOMAIN 388 425 EGF-LIKE 4, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 427 463 EGF-LIKE 5. FT DOMAIN 464 500 EGF-LIKE 6. FT DOMAIN 501 532 EGF-LIKE 7. FT DOMAIN 545 581 EGF-LIKE 8. FT DOMAIN 582 611 EGF-LIKE 9. FT DOMAIN 609 646 EGF-LIKE 10. FT DOMAIN 648 685 EGF-LIKE 11, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 687 723 EGF-LIKE 12, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 725 761 EGF-LIKE 13, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 763 800 EGF-LIKE 14, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 802 838 EGF-LIKE 15, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 840 902 EGF-LIKE 16. FT DOMAIN 904 940 EGF-LIKE 17, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 942 978 EGF-LIKE 18, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 980 1021 EGF-LIKE 19. FT DOMAIN 1023 1205 LAMININ G-LIKE 1. FT DOMAIN 1207 1243 EGF-LIKE 20. FT DOMAIN 1250 1480 LAMININ G-LIKE 2. FT DOMAIN 1481 1517 EGF-LIKE 21. FT DOMAIN 1558 1758 LAMININ G-LIKE 3. FT DOMAIN 1759 1795 EGF-LIKE 22. FT DOMAIN 1797 1833 EGF-LIKE 23, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1835 1871 EGF-LIKE 24, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1874 1915 EGF-LIKE 25. FT DOMAIN 1915 1951 EGF-LIKE 26. FT DOMAIN 1953 1989 EGF-LIKE 27, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1991 2029 EGF-LIKE 28, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 2030 2070 EGF-LIKE 29. FT DISULFID 271 282 BY SIMILARITY. FT DISULFID 276 291 BY SIMILARITY. FT DISULFID 293 302 BY SIMILARITY. FT DISULFID 310 321 BY SIMILARITY. FT DISULFID 315 331 BY SIMILARITY. FT DISULFID 333 342 BY SIMILARITY. FT DISULFID 352 363 BY SIMILARITY. FT DISULFID 357 374 BY SIMILARITY. FT DISULFID 376 385 BY SIMILARITY. FT DISULFID 392 403 BY SIMILARITY. FT DISULFID 397 412 BY SIMILARITY. FT DISULFID 414 424 BY SIMILARITY. FT DISULFID 431 442 BY SIMILARITY. FT DISULFID 436 451 BY SIMILARITY. FT DISULFID 453 462 BY SIMILARITY. FT DISULFID 468 479 BY SIMILARITY. FT DISULFID 473 488 BY SIMILARITY. FT DISULFID 490 499 BY SIMILARITY. FT DISULFID 505 515 BY SIMILARITY. FT DISULFID 509 520 BY SIMILARITY. FT DISULFID 522 531 BY SIMILARITY. FT DISULFID 549 562 BY SIMILARITY. FT DISULFID 556 569 BY SIMILARITY. FT DISULFID 571 580 BY SIMILARITY. FT DISULFID 586 597 BY SIMILARITY. FT DISULFID 591 602 BY SIMILARITY. FT DISULFID 604 610 BY SIMILARITY. FT DISULFID 613 624 BY SIMILARITY. FT DISULFID 618 634 BY SIMILARITY. FT DISULFID 636 645 BY SIMILARITY. FT DISULFID 652 664 BY SIMILARITY. FT DISULFID 659 673 BY SIMILARITY. FT DISULFID 675 684 BY SIMILARITY. FT DISULFID 691 702 BY SIMILARITY. FT DISULFID 696 711 BY SIMILARITY. FT DISULFID 713 722 BY SIMILARITY. FT DISULFID 729 740 BY SIMILARITY. FT DISULFID 734 749 BY SIMILARITY. FT DISULFID 751 760 BY SIMILARITY. FT DISULFID 767 778 BY SIMILARITY. FT DISULFID 772 787 BY SIMILARITY. FT DISULFID 789 799 BY SIMILARITY. FT DISULFID 806 817 BY SIMILARITY. FT DISULFID 811 826 BY SIMILARITY. FT DISULFID 828 837 BY SIMILARITY. FT DISULFID 844 855 BY SIMILARITY. FT DISULFID 849 890 BY SIMILARITY. FT DISULFID 892 901 BY SIMILARITY. FT DISULFID 908 919 BY SIMILARITY. FT DISULFID 913 928 BY SIMILARITY. FT DISULFID 930 939 BY SIMILARITY. FT DISULFID 946 957 BY SIMILARITY. FT DISULFID 952 966 BY SIMILARITY. FT DISULFID 968 977 BY SIMILARITY. FT DISULFID 984 995 BY SIMILARITY. FT DISULFID 989 1009 BY SIMILARITY. FT DISULFID 1011 1020 BY SIMILARITY. FT DISULFID 1211 1222 BY SIMILARITY. FT DISULFID 1216 1231 BY SIMILARITY. FT DISULFID 1233 1242 BY SIMILARITY. FT DISULFID 1485 1496 BY SIMILARITY. FT DISULFID 1490 1505 BY SIMILARITY. FT DISULFID 1507 1516 BY SIMILARITY. FT DISULFID 1763 1774 BY SIMILARITY. FT DISULFID 1768 1783 BY SIMILARITY. FT DISULFID 1785 1794 BY SIMILARITY. FT DISULFID 1801 1812 BY SIMILARITY. FT DISULFID 1806 1821 BY SIMILARITY. FT DISULFID 1823 1832 BY SIMILARITY. FT DISULFID 1839 1850 BY SIMILARITY. FT DISULFID 1844 1859 BY SIMILARITY. FT DISULFID 1861 1870 BY SIMILARITY. FT DISULFID 1878 1889 BY SIMILARITY. FT DISULFID 1883 1903 BY SIMILARITY. FT DISULFID 1905 1914 BY SIMILARITY. FT DISULFID 1919 1930 BY SIMILARITY. FT DISULFID 1924 1939 BY SIMILARITY. FT DISULFID 1941 1950 BY SIMILARITY. FT DISULFID 1957 1968 BY SIMILARITY. FT DISULFID 1962 1977 BY SIMILARITY. FT DISULFID 1979 1988 BY SIMILARITY. FT DISULFID 1995 2008 BY SIMILARITY. FT DISULFID 2002 2017 BY SIMILARITY. FT DISULFID 2019 2028 BY SIMILARITY. FT CARBOHYD 37 37 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 96 96 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 198 198 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 238 238 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 239 239 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 336 336 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 400 400 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 550 550 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 565 565 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 736 736 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 746 746 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 860 860 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 884 884 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 976 976 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1102 1102 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1114 1114 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1138 1138 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1192 1192 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1245 1245 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1255 1255 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1354 1354 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1363 1363 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1441 1441 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1454 1454 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1546 1546 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1740 1740 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1752 1752 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1809 1809 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1849 1849 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1885 1885 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1894 1894 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1900 1900 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2029 2029 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2035 2035 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2068 2068 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 1663 1676 MVDPTPAFSTDIDQ -> WWIRRQLFPRTSTK (IN FT REF. 2). FT CONFLICT 1722 1722 L -> V (IN REF. 2). FT CONFLICT 1955 1955 N -> K (IN REF. 2). SQ SEQUENCE 2139 AA; 233619 MW; E37E190F452986A3 CRC64; MAKIANASLS QQQKQRQAET ATTTTTTVAA SGRNSNNNSK KSRPHEKRHV KLRSHLLKRR PFQFIRRPQW IPLFILIYLA TDVASVAVPT KEAYFNGSTY LRLTTPMPIW DHSAISFRSC RGGEILAQQY NKNSIVISVL NDFLQISLAG PAVHGPNNRL DVKLPYQLLD NRWHTLQFKY EYGNLYLHVD RAASIFANST YNSQFLTNQD IGYKDAILIL GNSFSGCLLD GPGLQFVNNS TVQNVVFGHC PLTPGPCSDH DLFTRLPDNF CLNDPCMGHG TCSSSPEGYE CRCTARYSGK NCQKDNGSPC AKNPCENGGS CLENSEGNYQ CFCDPNHSGQ HCETEVNIHP LCQTNPCLNN GACVVIGGSG ALTCECPKGY AGARCEVDTD ECASQPCQNN GSCIDRINGF SCDCSGTGYT GAFCQTNVDE CDKNPCLNGG RCLHTYGWYT CQCLDGWGGE ICDRPMTCQT QQCFNGGTCL DKPIGFQCLC PPEYTGELCQ IAPSCAQQCP IDSECVGGKC VCKPGSSGYN CQTSTGDGAS ALALTPINCN ATNGKCLNGG TCSMNGTHCY CAVGYSGDRC EKAENCSPLN CQEPMVCVQN QCLCPENKVC NQCATQPCQN GGECVDLPNG DYECKCTRGW TGRTCGNDVD ECTLHPKICG NGICKNEKGS YKCYCTPGFT GVHCDSDVDE CLSFPCLNGA TCHNKINAYE CVCQPGYEGE NCEVDIDECG SNPCSNGSTC IDRINNFTCN CIPGMRGRIC DIDIDDCVGD PCLNGGQCID QLGGFRCDCS GTGYEGENCE LNIDECLSNP CTNGAKCLDR VKDYFCDCHN GYKGKNCEQD INECESNPCQ YNGNCLERSN ITLYQMSRIT DLPKVFSQPF SFENASGYEC VCVPGIIGKN CEININECDS NPCSKHGNCN DGIGTYTCEC EPGFEGTHCE INIDECDRYN PCQRGTCYDQ IDDYDCDCDA NYGGKNCSVL LKGCDQNPCL NGGACLPYLI NEVTHLYTCT CENGFQGDKC EKTTTLSMVA TSLISVTTER EEGYDINLQF RTTLPNGVLA FGTTGEKNEP VSYILELING RLNLHSSLLN KWEGVFIGSK LNDSNWHKVF VAINTSHLVL SANDEQAIFP VGSYETANNS QPSFPRTYLG GTIPNLKSYL RHLTHQPSAF VGCMQDIMVN GKWIFPDEQD ANISYTKLEN VQSGCPRTEQ CKPNPCHSNV ECTDLWHTFA CHCPRPFFGH TCQHNMTAAT FGHENTTHSA VIVETTDVAR RAIRSILDIS MFIRTREPTG QVFYLGTDPR KAPTKNIGDS YVAAKLHGGE LLVKMQFSGT PEAYTVGGQK LDNGYNHLIE VVRNQTLVQV KLNGTEYFRK TLSTTGLLDA QLLYLGGPAP TRESLLGATT EPGIIPVPGA GIPIEDTTVP KEADDSRDYF KGIIQDVKVS NGSLNLIVEM YSLNVTDVQV NAKPLGAVTI DRASVLPGEV SDDLCRKNAC LHNAECRNTW NDYTCKCPNG YKGKKCARRS EFCQHVTCPG QSLCQNLDDG YECVTNTTFT GQERSPLAFF YFQEQQSDDI VSEASPKQTL KPVIDIAFRL VLEVLCLYID NVDGFFEIGV NGGRVTITWK LSALHFGESA RFEKENTDGE WSRIYLRAHN SKLEGGWKGW ESMVDPTPAF STDIDQAAFQ SLIATSTQVY LGGMPESRQA RGSTLSAQQG SQFKGCVGEA RLGDLLLPYF SMAELYSRTN VSVQQKAQFR LNATRPEEGC ILCFQSDCKN DGFCQSPSDE YACTCQPGFE GDDCGTDIDE CLNTECLNNG TCINQVAAFF CQCQPGFEGQ HCEQNIDECA DQPCHNGGNC TDLIASYVCD CPEDYMGPQC DVLKQMTCEN EPCRNGSTCQ NGFNASTGNN FTCTCVPGFE GPLCDIPFCE ITPCDNGGLC LTTGAVPMCK CSLGYTGRLC EQDINECESN PCQNGGQCKD LVGRYECDCR ARIRGIRCEN DIDECNMEGD YCGGLGRCFN KPGSFQCICQ KPYCGAYCNF TDPCNATDLC LNGGRCVESC GAKPDYYCEC PEGFAGKNCT APITAKEDGP STTDIAIIVI PVVVVLLLIA GALLGTFLVM ARNKRATRGT YSPSVVKSTA THGWKWTTY // ID CRK_DROME STANDARD; PRT; 271 AA. AC Q9XYM0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Adapter molecule Crk. GN CRK OR CG1587. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Embryo; RX MEDLINE=99173888; PubMed=10072777; RA Galletta B.J., Niu X.-P., Erickson M.R., Abmayr S.M.; RT "Identification of a Drosophila homologue to vertebrate Crk by RT interaction with MBC."; RL Gene 228:243-252(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ADAPTER PROTEIN WHICH INTERACTS WITH C-TERMINAL PORTION CC OF MBC, HOMOLOG OF HUMAN DOCK180. MAY PLAY A ROLE IN CELLULAR CC PROCESSES THROUGHOUT DEVELOPMENT. CC -!- TISSUE SPECIFICITY: EMBRYONIC ZYGOTIC EXPRESSION IS SEEN IN CC INVAGINATING PRESUMPTIVE MESODERM AND ECTODERMALLY DERIVED TISSUES CC DURING GASTRULATION. AT STAGE 8, EXPRESSION IS ALSO SEEN IN CC ANTERIOR AND POSTERIOR MIDGUT AND CEPHALIC FURROW. BY STAGE 9, CC EXPRESSION IS HIGHEST IN VISCERAL MESODERM OF ANTERIOR AND CC POSTERIOR MIDGUT, VENTRAL NERVE CORD AND SOMATIC MESODERM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT EMBRYOGENESIS, DECLINES DURING LARVAL STAGES AND CC REAPPEARS DURING PUPATION. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 2 SH3 DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003844; AAF59362.1; -. DR EMBL; AF112976; AAD28428.1; -. DR HSSP; Q64010; 1CKA. DR FlyBase; FBgn0024811; Crk. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 2. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW SH2 domain; SH3 domain; Repeat; Developmental protein. FT DOMAIN 12 114 SH2. FT DOMAIN 117 165 SH3 1. FT DOMAIN 220 259 SH3 2. SQ SEQUENCE 271 AA; 31205 MW; D1B4FE43150932DC CRC64; MDTFDVSDRN SWYFGPMSRQ DATEVLMNER ERGVFLVRDS NSIAGDYVLC VREDTKVSNY IINKVQQQDQ IVYRIGDQSF DNLPKLLTFY TLHYLDTTPL KRPACRRVEK VIGKFDFVGS DQDDLPFQRG EVLTIVRKDE DQWWTARNSS GKIGQIPVPY IQQYDDYMDE DAIDKNEPSI SGSSNVFEST LKRTDLNRKL PAYARVKQSR VPNAYDKTAL KLEIGDIIKV TKTNINGQWE GELNGKNGHF PFTHVEFVDD CDLSKNSTEI C // ID CRM_DROME STANDARD; PRT; 982 AA. AC O76906; Q8MM10; Q8MM41; Q8MM71; Q8MX89; Q8MX90; Q8MX91; Q8MX92; AC Q8MX93; Q8MX94; Q8MX95; Q9W4V7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cramped protein. GN CRM OR EG:95B7.2 OR CG2714. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=97454258; PubMed=9310333; RA Yamamoto Y., Girard F., Bello B., Affolter M., Gehring W.J.; RT "The cramped gene of Drosophila is a member of the Polycomb-group, and RT interacts with mus209, the gene encoding Proliferating Cell Nuclear RT Antigen."; RL Development 124:3385-3394(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=k1, k2, k3, k5, k8, k9, k11, pe1, pe2, pe4, pe4, pe7, pe9, RC pe10, pe12, pe29, pe33, pe45, pe46, wi1, wi2, wi4, wi5, wi7, wi8, RC wi10, wi12, wi13, wi14, wi16, wi18, wi19, wi27, and wi28; RX MEDLINE=22247773; PubMed=12351680; RA Harr B., Kauer M., Schloetterer C.; RT "Hitchhiking mapping: A population-based fine-mapping strategy for RT adaptive mutations in Drosophilamelanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 99:12949-12954(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: POLYCOMB GROUP (PC-G) GENES ARE NEEDED TO MAINTAIN CC EXPRESSION PATTERNS OF THE HOMEOTIC SELECTOR GENES OF THE CC ANTENNAPEDIA (ANTP-C) AND BITHORAX (BX-C) COMPLEXES, AND HENCE FOR CC THE MAINTENANCE OF SEGMENTAL DETERMINATION. CAN ACT AS A MODIFIER CC OF POSITION EFFECT VARIEGATION (PEV). CC -!- SUBCELLULAR LOCATION: NUCLEAR, DURING S-PHASE IN EARLY CC EMBRYOGENESIS. CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED THROUGHOUT EMBRYONIC CC DEVELOPMENT. HIGH EXPRESSION IS DETECTED IN CNS AND GONADS. CO- CC LOCALIZED WITH MUS209 (PCNA) IN POLYTENE NUCLEI DURING CC EMBRYOGENESIS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: CONTAINS 1 MYB-LIKE DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 676. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y13674; CAB55550.1; ALT_FRAME. DR EMBL; AF365364; AAN04260.1; -. DR EMBL; AF365365; AAN04261.1; -. DR EMBL; AF365366; AAN04262.1; -. DR EMBL; AF365367; AAN04263.1; -. DR EMBL; AF365368; AAN04264.1; -. DR EMBL; AF365369; AAN04265.1; -. DR EMBL; AF365370; AAN04266.1; -. DR EMBL; AF365371; AAN04267.1; -. DR EMBL; AF365372; AAN04268.1; -. DR EMBL; AF365373; AAN04269.1; -. DR EMBL; AF365374; AAN04270.1; -. DR EMBL; AF365375; AAN04271.1; -. DR EMBL; AF365376; AAN04272.1; -. DR EMBL; AF365377; AAN04273.1; -. DR EMBL; AF365378; AAN04274.1; -. DR EMBL; AF365379; AAN04275.1; -. DR EMBL; AF365380; AAN04276.1; -. DR EMBL; AF365381; AAN04277.1; -. DR EMBL; AF365382; AAN04278.1; -. DR EMBL; AF365383; AAN04279.1; -. DR EMBL; AF365384; AAN04280.1; -. DR EMBL; AF365385; AAN04281.1; -. DR EMBL; AF365386; AAN04282.1; -. DR EMBL; AF365387; AAN04283.1; -. DR EMBL; AF365388; AAN04284.1; -. DR EMBL; AF365389; AAN04285.1; -. DR EMBL; AF365390; AAN04286.1; -. DR EMBL; AF365391; AAN04287.1; -. DR EMBL; AF365392; AAN04288.1; -. DR EMBL; AF365393; AAN04289.1; -. DR EMBL; AF365394; AAN04290.1; -. DR EMBL; AF365396; AAN04291.1; -. DR EMBL; AF365397; AAN04292.1; -. DR EMBL; AF365398; AAN04293.1; -. DR EMBL; AL021728; CAA16818.1; -. DR EMBL; AE003425; AAF45822.1; -. DR EMBL; AY051767; AAK93191.1; -. DR FlyBase; FBgn0000376; crm. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0045449; P:regulation of transcription; NAS. DR GO; GO:0007379; P:segment specification; IMP. DR InterPro; IPR001005; Myb_DNA_binding. DR Pfam; PF00249; myb_DNA-binding; 1. DR PROSITE; PS50090; MYB_3; FALSE_NEG. KW DNA-binding; Nuclear protein; Transcription regulation; KW Developmental protein; Polymorphism. FT DNA_BIND 111 169 MYB. FT DOMAIN 412 437 GLU/PRO/SER/THR-RICH. FT DOMAIN 529 564 ALA-RICH. FT VARIANT 322 322 S -> N (IN STRAINS K3 AND K5). FT VARIANT 402 402 M -> I (IN STRAIN K5). FT VARIANT 493 493 N -> T (IN STRAINS BERKELEY, K1, K8, FT OREGON-R, PE7 AND PE10). FT VARIANT 527 527 S -> T (IN STRAIN K2). FT VARIANT 639 639 G -> A (IN STRAINS BERKELEY, K1, K2, K3, FT K5, K8, K9 AND K11). FT VARIANT 747 747 M -> I (IN STRAIN K5). FT VARIANT 823 823 T -> I (IN STRAINS BERKELEY, K9, WI10 AND FT WI19). FT VARIANT 830 830 T -> S (IN STRAIN K1). FT VARIANT 837 837 C -> S (IN STRAINS BERKELEY, K3, K8, K9, FT WI10 AND WI19). FT VARIANT 842 842 M -> T (IN STRAINS BERKELEY, K1, K2, K3, FT K5, K8, K9, K11, PE1, PE4, PE45, PE5, FT WI4, WI7, WI10, WI13, WI18 AND WI19). FT VARIANT 845 845 S -> P (IN STRAIN K8). FT CONFLICT 645 645 S -> A (IN REF. 4 AND 5). FT CONFLICT 653 653 S -> G (IN REF. 4 AND 5). FT CONFLICT 965 965 F -> L (IN REF. 1). SQ SEQUENCE 982 AA; 107461 MW; 70E79DB1F2BCCA45 CRC64; MEELSKQPPP PPLTQPPPPS SSVSIEEPLP NGKGGGAVVV NSIAKLPEEE LLGSVTMHNC PGTRASARVI QKMKQDQTRP MTPPPSEREP NKKEEKAAQK TPSQLKTGSG KTTWTNVERN CFFDALNEFG KDFEAVANCI NAKLKRRNAN SDYSFKTKDQ VRQHYYQTHH KICKYVRFSE ELKKPAQELY TLINYGEMRR KLQFLTEKHF MKLKQLVYQG QITVRCKGKN IRIKTPSCKA LRRLNQLDDS LEDIRLPSKV EVLVTPANME AFGRVQSLAQ NPRGRIIVPL HKKLISFIKT FEYKWRSANQ RLHEEKSAYF SSSLPSAASN NNNNNNETEP LQPSVASLDP SMCFQPRPGV AIHRPLLSIT AYLSSISICL TAYEERMGFK VRSETLGNLA GMSVAANKRL RTESGSEKRS PETKKPKSSA SPPLEKSLDD GPLEGNLMKM ENSSGDELGE EIHEFLGDIL EAMQHPQAAT IPALSATTGD TTNVAVALET SHDPVQQAYP ANADLSNAMA TSVLQTSCAA APAPSTPVTG SLAAPSVARS KRKEAKEAAA AAQARNFKPL LSDDILKRIR KGWTQANAAD ITIGDLYVVF GQDSKLELEY YWCEVDSSTA MASSILTINT VTPSSSSVGT QTGSSASNAN QTSASSNCYV SASSNSSTSS TSLPYNPNDC DSVERVRAVT TSSVSNKLKH LLLVANLSER VRKRQCNCGH TCDRKRDLMT KAQQLAEATA TGGVGGMVEG NFRTPMLPVR RPISNIDPVR QLSALTRQKI SRQVLVQRRL LPPTSAGDRP YDLLSVRQLH SGLFEPIDRV DGTSSAGIST SGSKPDCSMN AMTASQDQEP GDQGALEFLN DEATQVSARD MPNLDICVAT NRTDVSSSLN EAAQDGSTTQ SFFQGSMSPM HLLRDSTSNA RWLEDNINDF SLTSLLGHLD EIDATRDILD PSSSMSVISE SSVDFRHKFQ EIAALLQQQE KD // ID CRN_DROME STANDARD; PRT; 702 AA. AC P17886; O46071; Q24283; DT 01-MAR-1992 (Rel. 21, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Crooked neck protein. GN CRN OR EG:30B8.1 OR CG3193. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91257574; PubMed=2044955; RA Zhang K., Smouse D., Perrimon N.; RT "The crooked neck gene of Drosophila contains a motif found in a RT family of yeast cell cycle genes."; RL Genes Dev. 5:1080-1091(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION. RX MEDLINE=22152880; PubMed=12163015; RA Raisin-Tani S., Leopold P.; RT "Drosophila crooked-neck protein co-fractionates in a multiprotein RT complex with splicing factors."; RL Biochem. Biophys. Res. Commun. 296:288-288(2002). CC -!- FUNCTION: MAY BE INVOLVED IN PRE-MRNA SPLICING PROCESS. INVOLVED CC IN NEUROGENESIS. LOSS OF ZYGOTIC EXPRESSION OF CRN CAUSES DEFECTS CC IN THE PROLIFERATION OF BRAIN NEUROBLASTS AND RESULTS IN THE CC ABSENCE OF IDENTIFIED NEURONAL LINEAGES IN THE CENTRAL AND CC PERIPHERAL NERVOUS SYSTEMS. CC -!- SUBUNIT: COLOCALIZES WITH A COMPLEX CONTAINING SNRNP PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR; CONCENTRATED IN NUCLEAR SPECKLES. CC -!- TISSUE SPECIFICITY: TRANSCRIBED IN ALL CELLS DURING EMBRYONIC CC DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: IS EXPRESSED THROUGHOUT EMBRYONIC, LARVAL, CC PUPAL AND ADULT STAGES AT RELATIVELY CONSTANT LEVELS. CC -!- SIMILARITY: CONTAINS 13 HAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58374; CAA41263.1; -. DR EMBL; AE003423; AAF45760.1; -. DR EMBL; AL009195; CAA15705.1; -. DR EMBL; AY051666; AAK93090.1; -. DR PIR; T13427; T13427. DR FlyBase; FBgn0000377; crn. DR GO; GO:0016607; C:nuclear speck; IDA. DR InterPro; IPR003107; HAT. DR InterPro; IPR008940; Prenyl_trans. DR InterPro; IPR008941; TPR-like. DR InterPro; IPR001440; TPR. DR Pfam; PF02184; HAT; 10. DR SMART; SM00386; HAT; 14. KW Nuclear protein; mRNA processing; mRNA splicing; Neurogenesis; KW Repeat. FT REPEAT 56 88 HAT 1. FT REPEAT 90 122 HAT 2. FT REPEAT 124 156 HAT 3. FT REPEAT 158 189 HAT 4. FT REPEAT 191 222 HAT 5. FT REPEAT 224 259 HAT 6. FT REPEAT 261 295 HAT 7. FT REPEAT 305 337 HAT 8. FT REPEAT 339 373 HAT 9. FT REPEAT 383 419 HAT 10. FT REPEAT 454 486 HAT 11. FT REPEAT 488 522 HAT 12. FT REPEAT 524 555 HAT 13. FT DOMAIN 620 628 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT CONFLICT 94 94 R -> P (IN REF. 1). SQ SEQUENCE 702 AA; 84261 MW; 8E03A869B84E4A12 CRC64; MERPQKMPKV AKVKNKAPAE VQITAEQLLR EAKERDLEIL PPPPKQKISD PAELADYQQR KRKTFEDNLR KNRMVVSHWI KYAQWEEQQQ EIQRARSIWE RALDNEHRNV TLWLKYAEME MKNKQVNHAR NLWDRAVTIM PRVNQFWYKY TYMEEMLENV AGARQVFERW MEWQPEEQAW QTYVNFELRY KEIDRAREIY ERFVYVHPDV KNWIKFARFE ESHGFIHGSR RVFERAVEFF GDDYIEERLF IAFARFEEGQ KEHDRARIIY KYALDHLPKD RTQELFKAYT KHEKKYGDRA GIEDVIVSKR KYQYEQEVAA NPTNYDAWFD YLRLIEAEGD RDQIRETYER AISNVPPANE KNFWRRYIYL WINYALYEEL EAEDAERTRQ IYKTCLELIP HKQFTFSKLW LLYAQFEIRC KELQRARKAL GLAIGMCPRD KLFRGYIDLE IQLREFERCR MLYEKFLEFG PENCVTWMKF AELENLLGDT DRARAIFELA VQQPRLDMPE LLWKAYIDFE VALGETELAR QLYERLLERT QHVKVWMSFA KFEMGLSHGD SGPDAELNVQ LARRIYERAN EMLRQLGDKE SRVLLLEAWR DFERDASDSQ EMQKVMDKMP RRIKKRQKIV SDNGVEEGWE EVFDYIFPED EMARPNLKLL AAAKMWKTQK DNTVDDPPAT AIASEPEPAA DAAPADTTDS GD // ID CROC_DROME STANDARD; PRT; 508 AA. AC P32027; Q9VP32; DT 01-JUL-1993 (Rel. 26, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fork head domain protein crocodile (FKH protein FD1). GN CROC OR FD78E OR FD1 OR CG5069. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96080166; PubMed=7489720; RA Haecker U., Kaufmann E., Hartmann C., Juergens G., Knoechel W., RA Jaeckle H.; RT "The Drosophila fork head domain protein crocodile is required for RT the establishment of head structures."; RL EMBO J. 14:5306-5317(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 55-182 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=92409595; PubMed=1356269; RA Haecker U., Grossniklaus U., Gehring W.J., Jaeckle H.; RT "Developmentally regulated Drosophila gene family encoding the fork RT head domain."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8754-8758(1992). CC -!- FUNCTION: REQUIRED FOR THE ESTABLISHMENT OF HEAD STRUCTURES. CC REQUIRED TO FUNCTION AS AN EARLY PATTERNING GENE IN THE ANTERIOR- CC MOST BLASTODERM HEAD SEGMENT ANLAGE AND FOR THE ESTABLISHMENT OF A CC SPECIFIC HEAD SKELETAL STRUCTURE THAT DERIVES FROM THE NON- CC ADJACENT INTERCALARY SEGMENT AT A LATER STAGE OF EMBRYOGENESIS. CC BINDS THE CONSENSUS DNA SEQUENCE 5'-[AG]TAAA[TC]A-3'. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN EARLY BLASTODERM EMBRYOS IN CC ANTERIOR AND POSTERIOR GUT PRECURSORS, AND, LATER IN A SUBSET OF CC CELLS IN CENTRAL NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYOGENESIS, MAXIMALLY CC DURING THE 5-12 HOUR PERIOD. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S80254; AAB35643.1; -. DR EMBL; AE003594; AAF51727.1; -. DR EMBL; M96440; AAF02177.1; -. DR PIR; S59870; S59870. DR HSSP; Q63245; 2HFH. DR TRANSFAC; T02291; -. DR FlyBase; FBgn0014143; croc. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR InterPro; IPR001766; TF_Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR ProDom; PD000425; TF_Fork_head; 1. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 34 40 POLY-ALA. FT DNA_BIND 69 160 FORK-HEAD. FT DOMAIN 161 165 POLY-ARG. FT DOMAIN 301 304 POLY-ALA. FT DOMAIN 377 380 POLY-ASN. FT DOMAIN 389 403 POLY-GLY. FT DOMAIN 452 461 POLY-ALA. FT DOMAIN 466 473 POLY-HIS. FT VARIANT 122 122 L -> F (IN ALLELE CROC-75-3). FT VARIANT 453 453 A -> V (IN ALLELE CROC-75-3). SQ SEQUENCE 508 AA; 54516 MW; 2EFED1D8F63016D6 CRC64; MHTLFSDQNS FTRHYAQTAA GYGSASAVAA ASSASAAAAA HYAYDQYSRY PYSASAYGLG APHQNKEIVK PPYSYIALIA MAIQNAADKK VTLNGIYQYI MERFPYYRDN KQGWQNSIRH NLSLNECFVK VARDDKKPGK GSYWTLDPDS YNMFDNGSFL RRRRRFKKKD VMREKEEAIK RQAMMNEKLA EMKPLKLMTN GILEAKHMAA HAAHFKKEPL MDLGCLSGKE VSHAAMLNSC HDSLAQMNHL AGGGVEHPGF TVDSLMNVYN PRIHHSAYPY HLNEDNLATV ASSQMHHVHH AAAAHHAQQL QRHVAHVAHP LTPGGQGAGG QSSGHSPTTI STPHGPAHGG WYTPETPPSE PVPHNGQQGT PTHPGHNNNN SSSVLNHNGV GNGGGGGGGG GGGSSSVLTS SPTSALGFRD MIFEQNQSCQ LDTGSPTGSL QSASPPASAS VAAASAAAAA AVISSHHHHH HHHAALSGNL GQLGQLSNLS HYRPHVGHYQ EYGIKYGV // ID CRQ_DROME STANDARD; PRT; 457 AA. AC Q27367; Q9VPQ1; DT 15-JUL-1999 (Rel. 38, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Croquemort protein (d-CD36). GN CRQ OR CG31655/CG4280. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96222807; PubMed=8630729; RA Franc N.C., Dimarcq J.-L., Lagueux M., Hoffmann J., Ezekowitz R.A.B.; RT "Croquemort, a novel Drosophila hemocyte/macrophage receptor that RT recognizes apoptotic cells."; RL Immunity 4:431-443(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MACROPHAGE RECEPTOR FOR APOPTOTIC CELLS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: FOUND ON HEMOCYTES FROM HEMOLYMPH, AND LATER CC IN THE DEVELOPMENT, ON MACROPHAGES THAT CONTAIN APOPTOTIC CELL CC CORPSES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED ON HEMOCYTES/MACROPHAGES IN CC EMBRYOGENESIS. FIRST DETECTED IN LATE STAGE 11 EMBRYOS, WHICH CC CORRESPONDS TO THE FIRST WAVE OF APOPTOSIS. EXPRESSED IN CELLS CC THAT BY STAGE 12 SPREAD THROUGHOUT THE EMBRYO AND BY STAGE 13/14 CC HAVE MIGRATED FROM BOTH ENDS TOWARDS THE MIDDLE UNTIL THEY ARE CC EVENLY DISTRIBUTED BY STAGE 15. CC -!- PTM: N-GLYCOSYLATED AND/OR O-GLYCOSYLATED (PROBABLE). CC -!- MISCELLANEOUS: 'CROQUEMORT' MEANS LITERALLY 'THE ONE WHO BITES CC DEAD PERSONS' IN FRENCH AND IS COLLOQUIAL FOR UNDERTAKER. CC -!- SIMILARITY: BELONGS TO THE CD36 FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z31583; CAA83455.1; -. DR EMBL; Z31582; CAA83454.1; -. DR EMBL; AE003589; AAF51494.1; ALT_SEQ. DR PIR; S43137; S43137. DR FlyBase; FBgn0015924; crq. DR InterPro; IPR002159; CD36. DR Pfam; PF01130; CD36; 1. DR PRINTS; PR01609; CD36FAMILY. KW Glycoprotein; Transmembrane; Apoptosis; Palmitate; Lipoprotein; KW Receptor. FT DOMAIN 1 12 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 13 33 POTENTIAL. FT DOMAIN 34 457 EXTRACELLULAR (POTENTIAL). FT LIPID 2 2 S-palmitoyl cysteine (Potential). FT LIPID 3 3 S-palmitoyl cysteine (Potential). FT LIPID 5 5 S-palmitoyl cysteine (Potential). FT LIPID 6 6 S-palmitoyl cysteine (Potential). FT DISULFID 256 324 BY SIMILARITY. FT DISULFID 285 345 BY SIMILARITY. FT DISULFID 326 334 BY SIMILARITY. FT CARBOHYD 72 72 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 104 104 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 129 129 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 189 189 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 198 198 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 216 216 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 260 260 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 247 247 S -> A (IN REF. 1). SQ SEQUENCE 457 AA; 52334 MW; CD6FA6CD21A18D61 CRC64; MCCKCCGETQ RKVWVFGLGS VFLLLGILIV VFWPGIADNL VEDGLTLKPG TDAYESWLEA PIPIYLSFYM FNWTNPEDIR NPDIKPNFVE MGPYTFLEKH KKENYTFYDN ATVAYYERRT WFFDPERSNG TLDDMVTAAH AITATVADEM RDQRKIVKKI INFMLNHEGG KLYVTKPVGE WIFEGYQDNI TDFLNLFNTT KIDIPYKRFG WLADRNESLT YDGLFTIHTG TDDISNLGRL THWNGKSETG FYEMPCGIVN GTTGDMFPPK MNVNDEITIF ATDACRFMNL RPRGTYENHG LTATKWVGTE ETLDSGENYP NQACFCDEAR FDECPKTGVV ECKACRDKAP IYSSFPHFYL ADQSYVDAVS GMKPEKEKHE FFLAVEPITG VPVQVHGRIQ INMMIEPDDD FDIYRGVQKV LMPMFWFDQY AELSSELASK PSWPLICPVT ESYSAIP // ID CRTC_DROME STANDARD; PRT; 406 AA. AC P29413; Q9VHA3; DT 01-APR-1993 (Rel. 25, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calreticulin precursor (CRP55) (Calregulin) (HACBP). GN CRC OR CG9429. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93208374; PubMed=1296819; RA Smith M.J.; RT "Nucleotide sequence of a Drosophila melanogaster gene encoding a RT calreticulin homologue."; RL DNA Seq. 3:247-250(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 91-124 AND 182-220. RX MEDLINE=90307981; PubMed=2365822; RA McCauliffe D.P., Zappi E., Lieu T.S., Michalak M., Sontheimer R.D., RA Capra J.D.; RT "A human Ro/SS-A autoantigen is the homologue of calreticulin and is RT highly homologous with onchocercal RAL-1 antigen and an aplysia RT 'memory molecule'."; RL J. Clin. Invest. 86:332-335(1990). CC -!- FUNCTION: THIS PROTEIN BINDS CALCIUM. THERE ARE BOTH HIGH AND LOW CC AFFINITY CALCIUM-BINDING SITES. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN. CC -!- SIMILARITY: BELONGS TO THE CALRETICULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64461; CAA45791.1; -. DR EMBL; AE003683; AAF54416.1; -. DR PIR; A56637; A56637. DR FlyBase; FBgn0005585; Crc. DR GO; GO:0007417; P:central nervous system development; IMP. DR InterPro; IPR009033; Calret_calnex_P. DR InterPro; IPR001580; Calreticulin. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR000886; ER_target_S. DR Pfam; PF00262; calreticulin; 1. DR PIRSF; PIRSF002356; Calreticulin; 1. DR PRINTS; PR00626; CALRETICULIN. DR ProDom; PD001866; Calreticulin; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00803; CALRETICULIN_1; 1. DR PROSITE; PS00804; CALRETICULIN_2; 1. DR PROSITE; PS00805; CALRETICULIN_REPEAT; 3. KW Endoplasmic reticulum; Calcium-binding; Repeat; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 406 CALRETICULIN. FT CONFLICT 107 107 G -> A (IN REF. 3). FT CONFLICT 184 184 V -> L (IN REF. 3). SQ SEQUENCE 406 AA; 46808 MW; 65D72C69D0BEC427 CRC64; MMWCKTVIVL LATVGFISAE VYLKENFDNE NWEDTWIYSK HPGKEFGKFV LTPGTFYNDA EADKGIQTSQ DARFYAASRK FDGFSNEDKP LVVQFSVKHE QNIDCGGGYV KLFDCSLDQT DMHGESPYEI MFGPDICGPG TKKVHVIFSY KGKNHLISKD IRCKDDVYTH FYTLIVRPDN TYEVLIDNEK VESGNLEDDW DFLAPKKIKD PTATKPEDWD DRATIPDPDD KKPEDWDKPE HIPDPDATKP EDWDDEMDGE WEPPMIDNPE FKGEWQPKQL DNPNYKGAWE HPEIANPEYV PDDKLYLRKE ICTLGFDLWQ VKSGTIFDNV LITDDVELAA KAAAEVKNTQ AGEKKMKEAQ DEVQRKKDEE EAKKASDKDD EDEDDDDEEK DDESKQDKDQ SEHDEL // ID CSA5_DROME STANDARD; PRT; 505 AA. AC Q9V419; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 28a5 (EC 1.14.-.-) (CYPXXVIIIA5). GN CYP28A5 OR BG:DS00180.11 OR CG8864. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003408; AAF44844.1; -. DR EMBL; AE003642; AAF53365.1; -. DR EMBL; AY051533; AAK92957.1; -. DR FlyBase; FBgn0028940; Cyp28a5. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum. FT METAL 450 450 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 505 AA; 57704 MW; 292421C5D319BCDB CRC64; MVLITLTLVS LVVGLLYAVL VWNYDYWRKR GVPGPKPKLL CGNYPNMFTM KRHAIYDLDD IYRQYKNKYD AVGIFGSRSP QLLVINPALA RRVFVSNFKN FHDNEIAKNI DEKTDFIFAN NPFSLTGEKW KTRRADVTPG LTMGRIKTVY PVTNKVCQKL TEWVEKQLRL GSKDGIDAKH MSLCFTTEMV TDCVLGLGAE SFSDKPTPIM SKINDLFNQP WTFVLFFILT SSFPSLSHLI KLRFVPVDVE RFFVDLMGSA VETRRAQLAA GKQFERSDFL DYILQLGEKR NLDNRQLLAY SMTFLLDGFE TTATVLAHIL LNLGRNKEAQ NLLREEIRSH LQDGTIAFEK LSDLPYLDAC VQETIRLFPP GFMSNKLCTE SIEIPNKEGP NFVVEKGTTV VVPHYCFMLD EEFFPNPQSF QPERFLEPDA AKTFRERGVF MGFGDGPRVC IGMRFATVQI KAAIVELISK FNVKINDKTR KDNDYEPGQI ITGLRGGIWL DLEKL // ID CSC1_DROME STANDARD; PRT; 505 AA. AC Q9VYT8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 28c1 (EC 1.14.-.-) (CYPXXVIIIC1). GN CYP28C1 OR CG1895. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003487; AAF48100.1; -. DR FlyBase; FBgn0030339; Cyp28c1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 444 444 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 505 AA; 57410 MW; 8BF581609401A2C8 CRC64; MFGSLLLGIA TLLGAIYAFL VSNFGHWRRR GVTEPRALPL FGSFPNMIWP RQHFTMDMRD IYMHYRNTHS YVGCYLLRAP KLLVLEPRLV YEIYVSAFSH FENNDASKMV DIAKDRLVAL NPFVLEGEEW RHQRAVFSTL LTNGRIRTTH AIMQRVCLDL CQFIAIKSAG GKDLDCIDLG LRFTGESLFD CVLGIQARTF TDNPLPVVRQ NHEMSAENRG LAIAGAVHGL FPNLPRWLRP KVFPRSHDRF YGQMISEALR LRRSKHQERN DFINHLLEMQ RELDLSEEDM ASHAMTFMFD GLDTTSNSIA HCLLLLGRNP DCQRRLYEEL QLVNPGGYLP DLDALIDLPY LSACFNESLR IYPAGGWASK TCTKEYELRG SHHSEPLKLR PGDHVMVPIY ALHNDPDLYP EPDVFRPERF LDGGLKNCKQ QGIFLGFGNG PRQCVGMRLG LAMAKAALAA IVQRFEVVVS PRTLNGTELD PLIFVGVHKG GIWLQFVPRK NVTTK // ID CSD1_DROME STANDARD; PRT; 502 AA. AC Q9VMT5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable cytochrome P450 28d1 (EC 1.14.-.-) (CYPXXVIIID1). GN CYP28D1 OR CG10833. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003609; AAF52226.1; -. DR EMBL; AY069176; AAL39321.1; -. DR FlyBase; FBgn0031689; Cyp28d1. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 446 446 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 502 AA; 57271 MW; 99B71BAA074D1DB4 CRC64; MCPISTALFV IAAILALIYV FLTWNFSYWK KRGIPTAKSW PFVGSFPSVF TQKRNVVYDI DEIYEQYKNT DSIVGVFQTR IPQLMVTTPE YAHKIYVSDF RSFHDNEMAK FTDSKTDPIL ANNPFVLTGE AWKERRAEVT PGLSANRVKA AYPVSLRVCK KFVEYIRRQS LMAPAQGLNA KDLCLCYTTE VISDCVLGIS AQSFTDNPTP MVGMTKRVFE QSFGFIFYTV VANLWPPITK FYSVSLFAKD VAAFFYDLMQ KCIQVRRESP AAQQRDDFLN YMLQLQEKKG LNAAELTSHT MTFLTDGFET TAQVLTHTLL FLARNPKEQM KLREEIGTAE LTFEQISELP FTEACIHETL RIFSPVLAAR KVVTEPCELT NKNGVSVKLR PGDVVIIPVN ALHHDPQYYE EPQSFKPERF LNINGGAKKY RDQGLFFGFG DGPRICPGMR FSLTQIKAAL VEIVRNFDIK VNPKTRKDNE IDDTYFMPAL KGGVWLDFVE RN // ID CSD2_DROME STANDARD; PRT; 501 AA. AC Q9VMT6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable cytochrome P450 28d2 (EC 1.14.-.-) (CYPXXVIIID2). GN CYP28D2 OR CG6081. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Nelson B.; RL Unpublished observations (SEP-2000). CC -!- FUNCTION: MAY BE INVOLVED IN THE METABOLISM OF INSECT HORMONES AND CC IN THE BREAKDOWN OF SYNTHETIC INSECTICIDES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003609; AAF52225.1; ALT_SEQ. DR FlyBase; FBgn0031688; Cyp28d2. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Membrane; Heme; Microsome; KW Endoplasmic reticulum; Hypothetical protein. FT METAL 446 446 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). SQ SEQUENCE 501 AA; 58222 MW; 9AD85F249390A655 CRC64; MCPVTTFLVL VLTLLVLVYV FLTWNFNYWR KRGIKTAPTW PFVGSFPSIF TRKRNIAYDI DDIYEKYKDT DNMVGVFTTR VPQLLVMCPE YIHKIYATDF RSFHNNEWRN FVNKKTDMIL GNNPFVLTGD EWKERRSEIM PALSPNRVKA VYPVSQSVCK KFVEYIRRQQ QMATSEGLDA MDLSLCYTTE VVSDCGLGVS AQSFTDTPTP LLKMIKRVFN TSFEFIFYSV VTNLWQKVRK FYSVPFFNKE TEVFFLDIIR RCITLRLEKP EQQRDDFLNY MLQLQEKKGL HTDNILINTM TFILDGFETT ALVLAHIMLM LGRNPEEQDK VRKEIGSADL TFDQMSELPH LDACIYETLR LFSPQVAARK LVTEPFEFAN KNGRTVHLKP GDVVTIPVKA LHHDPQYYED PLTFKPERFL ESNGGGMKSY RDRGVYLAFG DGPRHCPGMR FALTQLKAAL VEILRNFEIK VNPKTRSDNQ IDDTFFMATL KGGIYLDFKD L // ID CSE1_DROME STANDARD; PRT; 975 AA. AC Q9XZU1; Q9UB14; Q9VJH4; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Importin-alpha re-exporter (Cellular apoptosis susceptibility protein DE homolog). GN CAS OR BCDNA:LD14270 OR CG13281. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21942515; PubMed=11944946; RA Tekotte H., Berdnik D., Toeroek T., Buszczak M., Jones L.M., RA Cooley L., Knoblich J.A., Davis I.; RT "Dcas is required for importin-alpha3 nuclear export and RT mechano-sensory organ cell fate specification in Drosophila."; RL Dev. Biol. 244:396-406(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: EXPORT RECEPTOR FOR IMPORTIN ALPHA. MEDIATES IMPORTIN- CC ALPHA REEXPORT FROM THE NUCLEUS TO THE CYTOPLASM AFTER IMPORT CC SUBSTRATES HAVE BEEN RELEASED INTO THE NUCLEOPLASM (BY CC SIMILARITY). CC -!- SUBUNIT: BINDS WITH HIGH AFFINITY TO IMPORTIN-ALPHA ONLY IN THE CC PRESENCE OF RANGTP (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CSE1 FAMILY. CC -!- SIMILARITY: CONTAINS 1 IMPORTIN N-TERMINAL DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ238857; CAB42967.1; -. DR EMBL; AE003652; AAF53575.1; -. DR EMBL; AF132562; AAD27861.1; -. DR FlyBase; FBgn0022213; Cas. DR GO; GO:0006611; P:protein-nucleus export; IMP. DR InterPro; IPR008938; ARM. DR InterPro; IPR005043; CAS_CSE1_C. DR InterPro; IPR001494; Importinb_N. DR Pfam; PF03378; CAS_CSE1; 1. DR Pfam; PF03810; IBN_NT; 1. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. KW Transport; Protein transport; Nuclear protein. FT DOMAIN 29 105 IMPORTIN N-TERMINAL. FT CONFLICT 194 194 K -> T (IN REF. 2). FT CONFLICT 331 331 Q -> P (IN REF. 1). FT CONFLICT 589 590 AA -> GR (IN REF. 1). SQ SEQUENCE 975 AA; 110168 MW; 5C9BA11C08D49C11 CRC64; MEVTEANLQL LAGYLQQTLS ADPNVRRPAE KLLESTELQQ NYPILLLNLI DKAQMDMTTR VAGAIAFKNY IKRNWAAHLD SDGPDRIHES DRNTIKTLIV TLMLHSPVAL QKQLSDAVSI IGKYDFPKKW PQLIDEMVER FASGDFNVIN GVLQTAHSLF KRYRYEFKSQ ALWEEIKFVL DRMAKPLTDL LQAKMQLTKV HENNAGALKV IYGSLVLVNK VFFSLNSQDL PEFFEDNINT WMGAFIQQLA ADVPSLRTAD DEDAGVLEHL RAQVCENICL YAKKYDEEFK PFMEQFVTAV WELLVKTSLH TKYDSLVSHA LQFLSVVADR QHYQSIFENP EILAQICDKV VIPNLDIRPS DEEIFEDSPE EYIRRDIEGS DIDTRRRAAC DLVKTLSINF EQKIFGIFGQ YLERLLTKYK ENPATNWRSK DTAIYLVTSW ASRGGTQKHG ITQTSELVPL PEFCAQQIIP ELERPNINEF PVLKAAAIKY VMVFRSILGP QVLASCLPQL IRHLPAESSV VHSYAACSVE KILSMRDASN AIVFGPQILA PYTTELISGL FATLSLPGSG ENEYVMKAIM RSFSVLQSAA MPFMGVALPR LTEILTQVAK NPSRPQFNHY LFETLALCIK IVCHADSSAV SSFEEALFPV FQGILQQDIV EFMPYVFQML SVLLEMREGT GTIPEPYWAL FPCLLSPALW DRTGNVTPLI RLISAFIKQG SAQIQALGKL SGILGIFQKM IASKANDHEG FYLLQNLLSY YPPAEIQTNL RQIFGLLFQR LSLSKTPKYL SGIIIFFSFY VIKFSGSQMA QLIDEIQPNL FGMLLDRVFI TEMGKIPKEQ DRKMVAVGVT KLLTETPEIL QQQYATFWPR LLHSLIDLFE RPPEKLMGLE IGETAGVAED PDAGYQVAFA QLTHAQPNQQ DHLAEIKDAR QFLATSLSKF AQARAGEFST LLSPLEPEYK QVLQKYCDQA GVRIA // ID CSN2_DROME STANDARD; PRT; 444 AA. AC Q94899; Q9V3Z0; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE COP9 signalosome complex subunit 2 (SGN2) (Alien protein) (Dch2). GN ALIEN OR CG9556. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=20003063; PubMed=10531038; RA Freilich S., Oron E., Kapp Y., Nevo-Caspi Y., Orgad S., Segal D., RA Chamovitz D.A.; RT "The COP9 signalosome is essential for development of Drosophila RT melanogaster."; RL Curr. Biol. 9:1187-1190(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 1-363 FROM N.A., DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=96414432; PubMed=8817453; RA Goubeaud A., Knirr S., Renkawitz-Pohl R., Paululat A.; RT "The Drosophila gene alien is expressed in the muscle attachment sites RT during embryogenesis and encodes a protein highly conserved between RT plants, Drosophila and vertebrates."; RL Mech. Dev. 57:59-68(1996). CC -!- FUNCTION: SUBUNIT OF THE COP9 SIGNALOSOME COMPLEX (OR COP9 CC COMPLEX). THE SIGNALOSOME COMPLEX MAY PLAY A ROLE IN SIGNAL CC TRANSDUCTION. ESSENTIAL FOR DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: EXPRESSED DURING EMBRYONIC STAGES 11-14 IN THE CC MUSCLE ATTACHMENT SITES (APODEMES); PHARYNX ATTACHMENT TO THE ROOF CC OF THE MOUTH AND IN THE EPIDERMIS OF THE HEAD FOR THE DORSAL AND CC VENTRAL PROTHORACIC PHARYNGEAL MUSCLE ATTACHMENT. FROM STAGE 16 CC ONWARDS EXPRESSION IS SEEN IN ALL THORACIC AND ABDOMINAL APODEMES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY WITH HIGH LEVELS CC DURING OOGENESIS, AND ZYGOTICALLY. CC -!- SIMILARITY: CONTAINS 1 PCI DOMAIN. CC -!- CAUTION: REF.5 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 356. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF129079; AAD28604.1; -. DR EMBL; AE003623; AAN10685.1; -. DR EMBL; AY069836; AAL39981.1; -. DR EMBL; U57758; AAB49932.1; ALT_FRAME. DR FlyBase; FBgn0013746; alien. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0008180; C:signalosome complex; IDA. DR GO; GO:0004871; F:signal transducer activity; ISS. DR GO; GO:0007275; P:development; IMP. DR GO; GO:0007165; P:signal transduction; ISS. DR InterPro; IPR000717; PCI. DR InterPro; IPR008941; TPR-like. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. KW Signalosome; Nuclear protein; Developmental protein. FT DOMAIN 249 414 PCI. SQ SEQUENCE 444 AA; 51526 MW; 3E471578DD495B57 CRC64; MSDNDDDFMC DDDEDYGLEY SEDSNSEPDV DLENQYYNSK ALKEEEPKAA LASFQKVLDL ENGEKGEWGF KALKQMIKIN FRLCNYDEMM VRYKQLLTYI KSAVTRNHSE KSINSILDYI STSKNMALLQ NFYETTLDAL RDAKNDRLWF KTNTKLGKLY FDRSDFTKLQ KILKQLHQSC QTDDGEDDLK KGTQLLEIYA LEIQMYTVQK NNKKLKALYE QSLHIKSAIP HPLIMGVIRE CGGKMHLREG EFEKAHTDFF EAFKNYDESG SPRRTTCLKY LVLANMLMKS GINPFDSQEA KPYKNDPEIL AMTNLVNSYQ NNDINEFETI LRQHRSNIMA DQFIREHIED LLRNIRTQVL IKLIRPYKNI AIPFIANALN IEPAEVESLL VSCILDDTIK GRIDQVNQVL QLDKINSSAS RYNALEKWSN QIQSLQFAVV QKMA // ID CSP_DROME STANDARD; PRT; 249 AA. AC Q03751; O61664; O61665; Q9VNV1; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cysteine string protein. GN CSP OR CG6395. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS CSP1 AND CSP3). RX MEDLINE=91286850; PubMed=2129171; RA Zinsmaier K.E., Hofbauer A., Heimbeck G., Pflugfelder G.O., RA Buchner S., Buchner E.; RT "A cysteine-string protein is expressed in retina and brain of RT Drosophila."; RL J. Neurogenet. 7:15-29(1990). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS CSP1; CSP2 AND CSP3). RC STRAIN=Berlin; RX MEDLINE=99015937; PubMed=9799436; RA Eberle K.K., Zinsmaier K.E., Buchner S., Gruhn M., Jenni M., RA Arnold C., Leibold C., Reisch D., Walter N., Hafen E., Hofbauer A., RA Pflugfelder G.O., Buchner E.; RT "Wide distribution of the cysteine string proteins in Drosophila RT tissues revealed by targeted mutagenesis."; RL Cell Tissue Res. 294:203-217(1998). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS CSP1 AND CSP3). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Berlin; RX MEDLINE=94143742; PubMed=8310297; RA Zinsmaier K.E., Eberle K.K., Buchner E., Walter N., Benzer S.; RT "Paralysis and early death in cysteine string protein mutants of RT Drosophila."; RL Science 263:977-980(1994). RN [5] RP FATTY ACYLATION. RX MEDLINE=96186935; PubMed=8601435; RA van de Goor J., Kelly R.B.; RT "Association of Drosophila cysteine string proteins with membranes."; RL FEBS Lett. 380:251-256(1996). CC -!- FUNCTION: MAY HAVE AN IMPORTANT ROLE IN PRESYNAPTIC FUNCTION. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=CSP1; Synonyms=CSP32; CC IsoId=Q03751-1; Sequence=Displayed; CC Name=CSP2; CC IsoId=Q03751-2; Sequence=VSP_001293; CC Name=CSP3; Synonyms=CSP29; CC IsoId=Q03751-3; Sequence=VSP_001293, VSP_001294; CC -!- TISSUE SPECIFICITY: EXPRESSED IN WIDE RANGE OF SYNAPTIC TERMINALS: CC EMBRYONIC NERVOUS SYSTEM, LARVAL NEUROMUSCULAR JUNCTIONS, ADULT CC VISUAL SYSTEM (NEUROPIL OF OPTIC GANGLIA AND TERMINAL OF R1-8 CC PHOTORECEPTORS) AND THORACIC NEUROMUSCULAR JUNCTIONS. ALSO CC EXPRESSED IN NON-NEURONAL CELLS: FOLLICLE CELLS, SPERMATHECA, CC TESTIS AND EJACULATORY BULB. LOW LEVEL OF EXPRESSION IS FOUND IN CC MANY NEURONAL AND NON-NEURONAL TISSUES. CC -!- PTM: FATTY ACYLATED. HEAVILY PALMITOYLATED IN THE CYSTEINE STRING CC MOTIF. CC -!- SIMILARITY: CONTAINS 1 J DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63421; AAA28432.1; -. DR EMBL; M63008; AAA28431.1; -. DR EMBL; AF057167; AAD09428.1; -. DR EMBL; AF057167; AAD09430.1; -. DR EMBL; AF057167; AAD09431.1; -. DR EMBL; AE003597; AAF51816.1; -. DR EMBL; AE003597; AAF51817.1; -. DR HSSP; P25685; 1HDJ. DR FlyBase; FBgn0004179; Csp. DR GO; GO:0003754; F:chaperone activity; NAS. DR GO; GO:0006887; P:exocytosis; IMP. DR InterPro; IPR001623; DnaJ_N. DR InterPro; IPR003095; Hsp_DnaJ. DR Pfam; PF00226; DnaJ; 1. DR PRINTS; PR00625; DNAJPROTEIN. DR SMART; SM00271; DnaJ; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. KW Chaperone; Membrane; Lipoprotein; Palmitate; Alternative splicing. FT DOMAIN 15 84 J-DOMAIN. FT DOMAIN 121 131 POLY-CYS. FT VARSPLIC 154 174 Missing (in isoform CSP3 and isoform FT CSP2). FT /FTId=VSP_001293. FT VARSPLIC 243 249 DMVNQKY -> GI (in isoform CSP3). FT /FTId=VSP_001294. FT VARIANT 71 71 N -> D (IN STRAIN BERKELEY). SQ SEQUENCE 249 AA; 26896 MW; 3EF97C3BF2553EB8 CRC64; MSAPGMDKRK LSTSGDSLYE ILGLPKTATG DDIKKTYRKL ALKYHPDKNP DNVDAADKFK EVNRAHSILS NQTKRNIYDN YGSLGLYIAE QFGEENVNAY FVVTSPAVKA VVICCAVITG CCCCCCCCCC CNFCCGKFKP PVNESHDQYS HLNRPDGNRE GNDMPTHLGQ PPRLEDVDLD DVNLGAGGAP VTSQPREQAG GQPVFAMPPP SGAVGVNPFT GAPVAANENT SLNTTEQTTY TPDMVNQKY // ID CSUP_DROME STANDARD; PRT; 449 AA. AC Q9V3A4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Catecholamines up protein. GN CATSUP OR CG10449. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99403013; PubMed=10471719; RA Stathakis D.G., Burton D.Y., McIvor W.E., Krishnakumar S., RA Wright T.R., O'Donnell J.M.; RT "The catecholamines up (Catsup) protein of Drosophila melanogaster RT functions as a negative regulator of tyrosine hydroxylase activity."; RL Genetics 153:361-382(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: NEGATIVELY REGULATES TYROSINE HYDROXYLASE ACTIVITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE ZIP TRANSPORTER (TC 2.A.5) FAMILY. CC KE4/CATSUP SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF216584; AAF37226.1; -. DR EMBL; AE003661; AAF53744.1; -. DR EMBL; AY058528; AAL13757.1; -. DR FlyBase; FBgn0002022; Catsup. DR GO; GO:0007300; P:nurse cell/oocyte transport (sensu Insecta); IMP. DR InterPro; IPR003689; Zn_transpt_Zip. DR Pfam; PF02535; Zip; 1. KW Transport; Transmembrane. FT TRANSMEM 19 39 POTENTIAL. FT TRANSMEM 135 155 POTENTIAL. FT TRANSMEM 167 187 POTENTIAL. FT TRANSMEM 222 242 POTENTIAL. FT TRANSMEM 371 391 POTENTIAL. FT TRANSMEM 395 415 POTENTIAL. FT CARBOHYD 316 316 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 449 AA; 48658 MW; F7111A254C07AB4C CRC64; MAKQVADYQC SKLQLYQKLA LVVILGAVLF SLPALCAGQG NPSFKYSREA NENFDPQKAP RAEHHHHHDH DHDHGHHHHG HDHDHDHDHG HDHGHHHHGH DHDHDHDHGH HHHGHDERHT KAKPDLDMST IWLHSIGSTL LISAAPFVLL YIIPLDNSEA MKPRLKVLLA FASGGLLGDA FLHLIPHATH PHSHGEHGHD HGHDHHHHHD GEEHEHGHSH DMSIGLWVLG GIIAFLSVEK LVRILKGGHG GHGHSHGAPK PKPVPAKKKS SDKEDSGDGD KPAKPAKIKS KKPEAEPEGE VEISGYLNLA ADFAHNFTDG LAIGASYLAG NSIGIVTTIT ILLHEVPHEI GDFAILIKSG CSRRKAMLLQ LVTALGALAG TALALLGAGG GDGSAPWVLP FTAGGFIYIA TVSVLPELLE ESTKLKQSLK EIFALLTGVA LMIVIAKFE // ID CSW_DROME STANDARD; PRT; 845 AA. AC P29349; Q24032; Q24033; Q8I074; Q8I0H8; Q8I0S4; Q8ISD5; Q8ISD6; AC Q9V3H1; Q9W524; DT 01-DEC-1992 (Rel. 24, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein-tyrosine phosphatase corkscrew (EC 3.1.3.48). GN CSW OR EG:BACN25G24.2 OR CG3954. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=92346711; PubMed=1638629; RA Perkins L.A., Larsen I., Perrimon N.; RT "Corkscrew encodes a putative protein tyrosine phosphatase that RT functions to transduce the terminal signal from the receptor tyrosine RT kinase torso."; RL Cell 70:225-236(1992). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 4). RC STRAIN=DP CN BW; RA Melnick M.B., Melnick C.B., Larsen I., Perrimon N., Perkins L.A.; RT "The role of the Drosophila corkscrew protein as a transducer RT downstream of receptor tyrosine kinases is functionally conserved."; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 2 AND 4), AND VARIANTS THR-119 AND RP SER-749. RC STRAIN=10A, Ann Arbor1, Ann Arbor3, Ann Arbor6, Ann Arbor20, RC Kakamega-b1, Kakamega-b3, Kakamega-b4, Kenya-HLa3, Kenya-HLa6, RC Kenya-HLb1, M2, Makindu-b1, Makindu-b5, Nairobi-a, PYR2, Reids2, and RC Sapporo; RA Riley R.M., Jin W., Gibson G.; RT "Contrasting selection pressures on components of the Ras-mediated RT signal transduction pathway in Drosophila."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 4). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 4). RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [7] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [8] RP FUNCTION. RX MEDLINE=97105827; PubMed=8948575; RA Perkins L.A., Johnson M.R., Melnick M.B., Perrimon N.; RT "The nonreceptor protein tyrosine phosphatase corkscrew functions in RT multiple receptor tyrosine kinase pathways in Drosophila."; RL Dev. Biol. 180:63-81(1996). CC -!- FUNCTION: REQUIRED IN ALL RECEPTOR TYROSINE KINASE SIGNALING CC PATHWAYS. FUNCTIONS DOWNSTREAM OF THE RECEPTOR TYROSINE KINASE CC TORSO, ACTING IN CONCERT WITH D-RAF VIA TAILLESS. ALSO FUNCTIONS CC DOWNSTREAM OF EGFR (EPIDERMAL GROWTH FACTOR RECEPTOR) AND BTL CC (FIBROBLAST GROWTH FACTOR RECEPTOR). THE SH2 DOMAIN SUGGESTS THAT CC CSW EFFECTS ITS ROLE BY MEDIATING HETEROMERIC PROTEIN CC INTERACTIONS. MATERNALLY REQUIRED FOR NORMAL DETERMINATION OF CELL CC FATES AT THE TERMINI OF THE EMBRYO. REQUIRED FOR CELL FATE CC SPECIFICATION OF THE VENTRAL ECTODERM, IN THE DEVELOPING EMBRYONIC CC CNS AND FOR EMBRYONIC TRACHEAL CELL MIGRATION. FUNCTIONS DURING CC IMAGINAL DEVELOPMENT FOR PROPER FORMATION OF ADULT STRUCTURES SUCH CC AS EYES, ARISTAE, L5 WING VEIN AND THE TARSAL CLAW. CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=2; CC IsoId=P29349-1; Sequence=Displayed; CC Name=1; Synonyms=Y1229, A; CC IsoId=P29349-2; Sequence=VSP_005141; CC Name=3; Synonyms=C; CC IsoId=P29349-3; Sequence=VSP_005139, VSP_005141; CC Name=4; Synonyms=4A, B; CC IsoId=P29349-4; Sequence=VSP_005140; CC -!- TISSUE SPECIFICITY: EXPRESSED UNIFORMLY THROUGHOUT ALL TISSUES CC DURING EMBRYOGENESIS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. CC -!- MISCELLANEOUS: THE PTPASE DOMAIN IS INTERRUPTED BY A PTPASE INSERT CC WHICH SHARES NO HOMOLOGIES WITH OTHER PTPASE PROTEINS. THIS PTPASE CC INSERT IS REMINISCENT OF THE KINASE INSERT WITHIN THE KINASE CC CATALYTIC DOMAINS OF SEVERAL RECEPTOR TYROSINE KINASES. CC -!- SIMILARITY: BELONGS TO THE NON-RECEPTOR CLASS OF THE PROTEIN- CC TYROSINE PHOSPHATASE FAMILY. SUBCLASS THAT CONTAINS SH2 DOMAINS. CC -!- SIMILARITY: CONTAINS 2 SH2 DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M94730; AAA28433.1; -. DR EMBL; U19909; AAB02543.1; -. DR EMBL; U19909; AAB02544.1; -. DR EMBL; AY135117; AAN17607.1; -. DR EMBL; AY135117; AAN17608.1; -. DR EMBL; AY135118; AAN17609.1; -. DR EMBL; AY135118; AAN17610.1; -. DR EMBL; AY135119; AAN17611.1; -. DR EMBL; AY135119; AAN17612.1; -. DR EMBL; AY135120; AAN17613.1; -. DR EMBL; AY135120; AAN17614.1; -. DR EMBL; AY135121; AAN17615.1; -. DR EMBL; AY135121; AAN17616.1; -. DR EMBL; AY135122; AAN17617.1; -. DR EMBL; AY135122; AAN17618.1; -. DR EMBL; AY135123; AAN17619.1; -. DR EMBL; AY135123; AAN17620.1; -. DR EMBL; AY135124; AAN17621.1; -. DR EMBL; AY135124; AAN17622.1; -. DR EMBL; AY135125; AAN17623.1; -. DR EMBL; AY135125; AAN17624.1; -. DR EMBL; AY135126; AAN17625.1; -. DR EMBL; AY135126; AAN17626.1; -. DR EMBL; AY135127; AAN17627.1; -. DR EMBL; AY135127; AAN17628.1; -. DR EMBL; AY135128; AAN17629.1; -. DR EMBL; AY135128; AAN17630.1; -. DR EMBL; AY135129; AAN17631.1; -. DR EMBL; AY135129; AAN17632.1; -. DR EMBL; AY135130; AAN17633.1; -. DR EMBL; AY135130; AAN17634.1; -. DR EMBL; AY135131; AAN17635.1; -. DR EMBL; AY135131; AAN17636.1; -. DR EMBL; AY135132; AAN17637.1; -. DR EMBL; AY135132; AAN17638.1; -. DR EMBL; AY135133; AAN17639.1; -. DR EMBL; AY135133; AAN17640.1; -. DR EMBL; AY135134; AAN17641.1; -. DR EMBL; AY135134; AAN17642.1; -. DR EMBL; AE003423; AAF45724.2; -. DR EMBL; AE003423; AAG22389.2; -. DR EMBL; AE003423; AAF45725.1; -. DR EMBL; AL132797; CAB65870.1; -. DR EMBL; AL132797; CAB65871.1; -. DR EMBL; BT001484; AAN71239.1; -. DR PIR; A43254; A43254. DR HSSP; Q06124; 2SHP. DR FlyBase; FBgn0000382; csw. DR GO; GO:0005737; C:cytoplasm; IEP. DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phos...; NAS. DR GO; GO:0004728; F:receptor signaling protein tyrosine phospha...; NAS. DR GO; GO:0008069; P:dorsal/ventral axis determination, follicul...; IMP. DR GO; GO:0007173; P:EGF receptor signaling pathway; IGI. DR GO; GO:0008543; P:FGF receptor signaling pathway; IMP. DR GO; GO:0007444; P:imaginal disc development; IMP. DR GO; GO:0007498; P:mesoderm development; IMP. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA. DR GO; GO:0007465; P:R7 cell fate commitment; IGI. DR GO; GO:0007362; P:terminal region determination; IMP. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR GO; GO:0007427; P:tracheal cell migration (sensu Insecta); IMP. DR GO; GO:0007418; P:ventral midline development; IMP. DR InterPro; IPR000980; SH2. DR InterPro; IPR000387; TYR_phosphatase. DR InterPro; IPR000242; Tyr_PP. DR Pfam; PF00017; SH2; 2. DR Pfam; PF00102; Y_phosphatase; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR PRINTS; PR00401; SH2DOMAIN. DR ProDom; PD000093; SH2; 2. DR SMART; SM00194; PTPc; 1. DR SMART; SM00252; SH2; 2. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. DR PROSITE; PS50001; SH2; 2. KW Hydrolase; SH2 domain; Repeat; Developmental protein; KW Alternative splicing; Polymorphism. FT DOMAIN 6 101 SH2 1. FT DOMAIN 111 205 SH2 2. FT DOMAIN 227 645 PROTEIN-TYROSINE PHOSPHATASE. FT DOMAIN 289 444 PTPASE INSERT (CYS/SER-RICH). FT ACT_SITE 583 583 PHOSPHOCYSTEINE INTERMEDIATE (BY FT SIMILARITY). FT VARSPLIC 1 159 Missing (in isoform 3). FT /FTId=VSP_005139. FT VARSPLIC 1 110 MSSRRWFHPTISGIEAEKLLQEQGFDGSFLARLSSSNPGAF FT TLSVRRGNEVTHIKIQNNGDFFDLYGGEKFATLPELVQYYM FT ENGELKEKNGQAIELKQPLICAEPTTER -> MLFNKCLEK FT LSSSLGNVVNHKLQEKQVYNNNNINNNNNNTLNNNNAYNNQ FT RNFEYERAIQAHYGSKGRRSEERERSGKFKASKGRKAKVTP FT PTETPEAQEPACKNCMTHDELAQIIKGVAKGADAQRNRDNR FT LQRRRRPLSAQPSAAASASTSTESLHRLTPSPQASYPATPT FT SWTATPPQFPAAFGGASCSNSTLSLLATMRVQLHGYT (in FT isoform 4). FT /FTId=VSP_005140. FT VARSPLIC 810 845 GKMQQPAPPLRPRPGILKLLTSPVIFQQNSKTFPKT -> A FT KFKNIPKDMIGLRPPSHAPALPPPPTPPRKT (in FT isoform 1 and isoform 3). FT /FTId=VSP_005141. FT VARIANT 119 119 K -> T (IN STRAINS KENYA-HLA3, FT KENYA-HLA6, KAKAMEGA-B1 AND MAKINDU-B1). FT VARIANT 749 749 G -> S (IN STRAINS ANN ARBOR1, DP CN BW, FT KAKAMEGA-B1, KAKAMEGA-B3, KAKAMEGA-B4, FT KENYA-HLA3, KENYA-HLA6, MAKINDU-B5 AND FT REIDS2). FT CONFLICT 815 815 P -> S (IN REF. 2; AAB02544). SQ SEQUENCE 845 AA; 92975 MW; 2147F0F2576202CC CRC64; MSSRRWFHPT ISGIEAEKLL QEQGFDGSFL ARLSSSNPGA FTLSVRRGNE VTHIKIQNNG DFFDLYGGEK FATLPELVQY YMENGELKEK NGQAIELKQP LICAEPTTER WFHGNLSGKE AEKLILERGK NGSFLVRESQ SKPGDFVLSV RTDDKVTHVM IRWQDKKYDV GGGESFGTLS ELIDHYKRNP MVETCGTVVH LRQPFNATRI TAAGINARVE QLVKGGFWEE FESLQQDSRD TFSRNEGYKQ ENRLKNRYRN ILPYDHTRVK LLDVEHSVAG AEYINANYIR LPTDGDLYNM SSSSESLNSS VPSCPACTAA QTQRNCSNCQ LQNKTCVQCA VKSAILPYSN CATCSRKSDS LSKHKRSESS ASSSPSSGSG SGPGSSGTSG VSSVNGPGTP TNLTSGTAGC LVGLLKRHSN DSSGAVSISM AERERERERE MFKTYIATQG CLLTQQVNTV TDFWNMVWQE NTRVIVMTTK EYERGKEKCA RYWPDEGRSE QFGHARIQCV SENSTSDYTL REFLVSWRDQ PARRIFHYHF QVWPDHGVPA DPGCVLNFLQ DVNTRQSHLA QAGEKPGPIC VHCSAGIGRT GTFIVIDMIL DQIVRNGLDT EIDIQRTIQM VRSQRSGLVQ TEAQYKFVYY AVQHYIQTLI ARKRAEEQSL QVGREYTNIK YTGEIGNDSQ RSPLPPAISS ISLVPSKTPL TPTSADLGTG MGLSMGVGMG VGNKHASKQQ PPLPVVNCNN NNNGIGNSGC SNGGGSSTTS SSNGSSNGNI NALLGGIGLG LGGNMRKSNF YSDSLKQQQQ REEQAPAGAG KMQQPAPPLR PRPGILKLLT SPVIFQQNSK TFPKT // ID CTBP_DROME STANDARD; PRT; 386 AA. AC O46036; O61283; Q9VG02; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE C-terminal binding protein (CtBP protein) (dCtBP). GN CTBP OR CG7583. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=98190087; PubMed=9524128; RA Poortinga G., Watanabe M., Parkhurst S.M.; RT "Drosophila CtBP: a Hairy-interacting protein required for embryonic RT segmentation and hairy-mediated transcriptional repression."; RL EMBO J. 17:2067-2078(1998). RN [2] RP SEQUENCE FROM N.A., AND FUNCTION. RX MEDLINE=98192810; PubMed=9525852; RA Nibu Y., Zhang H., Levine M.; RT "Interaction of short-range repressors with Drosophila CtBP in the RT embryo."; RL Science 280:101-104(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CO-REPRESSOR TARGETING DIVERSE TRANSCRIPTION REGULATORS. CC HAIRY-INTERACTING PROTEIN REQUIRED FOR EMBRYONIC SEGMENTATION AND CC HAIRY-MEDIATED TRANSCRIPTIONAL REPRESSION. CC -!- SUBUNIT: CAN FORM HOMODIMERS. INTERACTS WITH HAIRY, KNIRPS, SNAIL, CC AND ENHANCER OF SPLIT M-DELTA. MAY BE INVOLVED IN TRANSCRIPTIONAL CC REPRESSION. INTERACTS ALSO WITH ADENOVIRUS E1A PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced; CC Name=1; CC IsoId=O46036-1; Sequence=Displayed; CC -!- DEVELOPMENTAL STAGE: TRANSCRIPTS LEVELS INCREASE BOTH EARLY DURING CC OOGENESIS AND EMBRYOGENESIS, AND LATER IN PRE-PUPAE STAGES. CC TRANSCRIPTS ARE DETECTED IN THE GERMANIUM AND IN THE NURSE CELLS CC THROUGHOUT THE EARLY OOGENIC STAGES, PEAKING IN STAGE 10 NURSE CC CELLS. THEY ARE LATER DUMPED INTO THE OOCYTE WHERE THEY ARE CC DISTRIBUTED UBIQUITOUSLY. THE MATERNAL TRANSCRIPT PERSIST CC THROUGHOUT THE EARLY EMBRYONIC STAGES. TRANSCRIPTS LEVELS DROP CC DURING GASTRULATION AND ARE MAINTAINED AT THIS LOWER LEVEL CC THROUGHOUT THE REMAINDER OF EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE D-ISOMER SPECIFIC 2-HYDROXYACID CC DEHYDROGENASES FAMILY. BUT HIGHLY DIVERGENT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ224690; CAA12074.1; -. DR EMBL; AB011840; BAA25287.1; -. DR EMBL; AE003698; AAF54891.1; -. DR HSSP; P17584; 1DXY. DR FlyBase; FBgn0020496; CtBP. DR InterPro; IPR006139; 2-Hacid_DH. DR InterPro; IPR006140; 2-Hacid_DH_C. DR Pfam; PF00389; 2-Hacid_DH; 1. DR Pfam; PF02826; 2-Hacid_DH_C; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; FALSE_NEG. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; FALSE_NEG. KW Alternative splicing; Nuclear protein. FT DOMAIN 362 365 POLY-ALA. FT CONFLICT 299 301 MISSING (IN REF. 2). FT CONFLICT 371 371 A -> S (IN REF. 1). SQ SEQUENCE 386 AA; 42251 MW; 89B9527BFF5224EC CRC64; MDKNLMMPKR SRIDVKGNFA NGPLQARPLV ALLDGRDCSI EMPILKDVAT VAFCDAQSTS EIHEKVLNEA VGALMWHTII LTKEDLEKFK ALRIIVRIGS GTDNIDVKAA GELGIAVCNV PGYGVEEVAD TTMCLILNLY RRTYWLANMV REGKKFTGPE QVREAAHGCA RIRGDTLGLV GLGRIGSAVA LRAKAFGFNV IFYDPYLPDG IDKSLGLTRV YTLQDLLFQS DCVSLHCTLN EHNHHLINEF TIKQMRPGAF LVNTARGGLV DDETLALALK QGRIRAAALD VHENEPYNVF QGALKDAPNL ICTPHAAFFS DASATELREM AATEIRRAIV GNIPDVLRNC VNKEYFMRTP PAAAAGGVAA AVYPEGKLQM ISNQEK // ID CTNA_DROME STANDARD; PRT; 917 AA. AC P35220; Q960Y2; Q9W5V9; DT 01-FEB-1994 (Rel. 28, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-catenin. GN ALPHA-CAT OR CG17947. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93273796; PubMed=8501118; RA Oda H., Uemura T., Shiomi K., Nagafuchi A., Tsukita S., Takeichi M.; RT "Identification of a Drosophila homologue of alpha-catenin and its RT association with the armadillo protein."; RL J. Cell Biol. 121:1133-1140(1993). RN [2] RP REVISIONS TO N-TERMINUS. RA Takeichi M.; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ASSOCIATES WITH THE CYTOPLASMIC DOMAIN OF A VARIETY OF CC CADHERINS. THE ASSOCIATION OF CATENINS TO CADHERINS PRODUCES A CC COMPLEX WHICH IS LINKED TO THE ACTIN FILAMENT NETWORK, AND WHICH CC SEEMS TO BE OF PRIMARY IMPORTANCE FOR CADHERINS CELL-ADHESION CC PROPERTIES. CAN ASSOCIATE WITH THE ARMADILLO PROTEIN. CC -!- SUBCELLULAR LOCATION: FOUND ONLY AT CELL-CELL BOUNDARIES. CC -!- DEVELOPMENTAL STAGE: PRESENT AT ALL STAGES, BUT REACHED THE CC HIGHEST LEVELS DURING EARLY TO MID-EMBRYOGENESIS. CC -!- SIMILARITY: STRONG, TO VINCULINS AND TO OTHER ALPHA-CATENINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D13964; BAA03067.2; -. DR EMBL; AE002656; AAF45466.1; -. DR EMBL; AY051780; AAK93204.1; -. DR PIR; A40694; A40694. DR HSSP; P26231; 1DOV. DR FlyBase; FBgn0010215; alpha-Cat. DR GO; GO:0005912; C:adherens junction; NAS. DR InterPro; IPR001033; Alpha_catenin. DR InterPro; IPR006077; Vinculin/catenin. DR InterPro; IPR000633; Vinculin_2. DR Pfam; PF01044; Vinculin; 1. DR PRINTS; PR00805; ALPHACATENIN. DR PRINTS; PR00806; VINCULIN. DR PROSITE; PS00663; VINCULIN_1; 1. KW Cytoskeleton; Structural protein; Cell adhesion. FT CONFLICT 711 711 F -> S (IN REF. 4). SQ SEQUENCE 917 AA; 102444 MW; 1F0B243DE7474E6F CRC64; MLKPDKMGTL TDFGQIALKW DPKNLEIRTM SVEKTLEPLV LQVTTLVNTK GPSKKKKGKS KRASALVAAV EKATENFIQK GEQIAYENPD ITQEMLTAVD EVKKTGDAMS IAAREFSEDP CSSLKRGNMV RAARNLLSAV TRLLILADMV DVHLLLKSLH IVEDDLNKLK NASSQDELMD NMRQFGRNAG ELIKQAAKRQ QELKDPQLRD DLAAARAMLK KHSTMLLTAS KVYVRHPELD LAKVNRDFIL KQVCDAVNTI SDVAQGKSSQ PTDIYSGAGE LAAALDDFDE GIVMDPMTYS EKRSRQLLEE RLESIISAAA LMADADCTRD ERRERIVAEC NAVRQALQDL LSEYMSNMSQ KDNSPGLSRA IDQMCRKTRD LRRQLRKAVV DHVSDSFLET TTPLLDLIEA AKSGNEKKVR EKSEIFTKHA EKLVEVANLV CSMSNNEDGV KMVRYAAAQI ESLCPQVINA ASILTVRPNS KVAQENMTTY RQAWEVQVRI LTEAVDDITT IDDFLAVSEN HILEDVNKCV MALQVGDARD LRATAGAIQG RSSRVCNVVE AEMDNYEPCI YTKRVLEAVK VLRDQVMMKF DQRVGAAVGA LSNNSNKDVD ENDFIDASRL VYDGVREIRR AVLMNRSSED LDTDTEFEPV EDLTLETRSR SSAHTGDQTV DEYPDISGIC TAREAMRKMT EEDKQKIAQQ VELFRREKLT FDSEVAKWDD TGNDIIFLAK HMCMIMMEMT DFTRGRGPLK TTMDVINAAK KISEAGTKLD KLTREIAEQC PESSTKKDLL AYLQRIALYC HQIQITSKVK ADVQNISGEL IVSGLDSATS LIQAAKNLMN AVVLTVKYSY VASTKYTRQG TVSSPIVVWK MKAPEKKPLV RPEKPEEVRA KVRKGSQKKV QNPIHALSEF QSPADAV // ID CUA1_DROME STANDARD; PRT; 135 AA. AC Q26416; Q9VLY2; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Adult cuticle protein 1 precursor (dACP-1). GN ACP1 OR CG7216. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=95180487; PubMed=7875368; RA Qiu J., Hardin P.E.; RT "Temporal and spatial expression of an adult cuticle protein gene RT from Drosophila suggests that its protein product may impart some RT specialized cuticle function."; RL Dev. Biol. 167:416-425(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE CUTICLE OF THE ADULT FRUIT FLY. COULD CC BE INVOLVED IN THICKENING OF THE HARD ADULT CUTICLE. CC -!- TISSUE SPECIFICITY: DETECTED IN THE EPIDERMIS UNDERLYING THE HEAD CC AND THORAX (INCLUDING LEGS AND WINGS), BUT NOT IN THE ABDOMINAL CC EPIDERMIS OF NEWLY ECLOSED FLIES. CC -!- DEVELOPMENTAL STAGE: EXPRESSION STARTS AROUND 72 HOURS AFTER CC PUPARIATION, PEAKS 12 HOURS AFTER ECLOSION AND DECREASES CC THEREAFTER TO UNDETECTABLE LEVELS BY 3 DAYS AFTER ECLOSION. CC -!- DOMAIN: THE TETRAPEPTIDE (A-A-P-[AV]) REPEATS FOUND THROUGHOUT THE CC PROTEIN ARE ALSO PRESENT IN MANY PROTEINS CONSTITUTING THE CC PROTECTIVE ENVELOPE OF OTHER SPECIES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S76894; AAB33567.2; -. DR EMBL; AE003618; AAF52547.1; -. DR FlyBase; FBgn0014454; Acp1. KW Structural protein; Cuticle; Signal; Repeat. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 135 ADULT CUTICLE PROTEIN 1. FT REPEAT 72 75 1. FT REPEAT 78 81 2. FT REPEAT 128 131 3. SQ SEQUENCE 135 AA; 13119 MW; 76A322083ADC362D CRC64; MKFAVAVIFT LALAMGVQSS VIPLLSQVAG HGLSYTAVSG PAVVASPWAV PAAHWPAAVN VASWPPAAIH AAAPAVLAAP APAVVAAHAP SVVVAPVAHS GVYTAQTRGA IHTAPLAGHI QSVASINAAP APGTL // ID CUL1_DROME STANDARD; PRT; 774 AA. AC Q24311; Q9V312; DT 01-NOV-1997 (Rel. 35, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cullin homolog 1 (Lin-19 homolog protein). GN LIN19 OR CUL-1 OR CG1877. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Brain; RA Filippov V.A., Filippova M.A., Sehnal F.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RA Dealy M.J., Heriche J.K., Nguyen K.V.T., Lo J., Gstaiger M., Krek W., RA Ang D., Bier E., Elson D., Arbeit J., Kipreos E.T., O'Farrell P.H., RA Johnson R.S.; RT "Cul-1 limits cyclin E level in mouse and cyclin E function in RT Drosophila."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE CULLIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L41642; AAA85085.1; -. DR EMBL; AF136343; AAD33676.1; -. DR EMBL; AE003839; AAF59175.1; -. DR EMBL; BT010290; AAQ23608.1; -. DR FlyBase; FBgn0015509; lin19. DR InterPro; IPR001373; Cullin. DR Pfam; PF00888; Cullin; 1. DR SMART; SM00182; CULLIN; 1. DR PROSITE; PS01256; CULLIN_1; 1. DR PROSITE; PS50069; CULLIN_2; 1. FT CONFLICT 266 266 MISSING (IN REF. 1). SQ SEQUENCE 774 AA; 89511 MW; 1AF0D035DE85363C CRC64; MNRSGNSQTT QKLVNLDDIW SELVEGIMQV FEHEKSLTRS QYMRFYTHVY DYCTSVSAAP SGRSSGKTGG AQLVGKKLYD RLEQFLKSYL SELLTKFKAI SGEEVLLSRY TKQWKSYQFS STVLDGICNY LNRNWVKREC EEGQKGIYKI YRLALVAWKG HLFQVLNEPV TKAVLKSIEE ERQGKLINRS LVRDVIECYV ELSFNEEDTD AEQQKLSVYK QNFENKFIAD TSAFYEKESD AFLSTNTVTE YLKHVENRLE EETQRVRGFN SKNGLSYLHE TTADVLKSTC EEVLIEKHLK IFHTEFQNLL NADRNDDLKR MYSLVALSSK NLTDLKSILE NHILHQGTEA IAKCCTTDAA NDPKTYVQTI LDVHKKYNAL VLTAFNNDNG FVAALDKACG KFINSNVVTI ANSASKSPEL LAKYCDLLLK KSSKNPEDKE LEDNLNQVMV VFKYIEDKDV FQKYYSKMLA KRLVNHTSAS DDAEAMMISK LKQTCGYEYT VKLQRMFQDI GVSKDLNSYF KQYLAEKNLT MEIDFGIEVL SSGSWPFQLS NNFLLPSELE RSVRQFNEFY AARHSGRKLN WLYQMCKGEL IMNVNRNNSS TYTLQASTFQ MSVLLQFNDQ LSFTVQQLQD NTQTQQENLI QVLQILLKAK VLTSSDNENS LTPESTVELF LDYKNKKRRI NINQPLKTEL KVEQETVHKH IEEDRKLLIQ AAIVRIMKMR KRLNHTNLIS EVLNQLSTRF KPKVPVIKKC IDILIEKEYL ERMEGHKDTY SYLA // ID CUP7_DROME STANDARD; PRT; 122 AA. AC P27779; Q9VP54; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pupal cuticle protein Edg-78E precursor. GN EDG78E OR EDG-78E OR CG7673. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91323677; PubMed=1713868; RA Apple R.T., Fristrom J.W.; RT "20-Hydroxyecdysone is required for, and negatively regulates, RT transcription of Drosophila pupal cuticle protein genes."; RL Dev. Biol. 146:569-582(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE CUTICLE OF THE PUPA OF FRUIT FLY. CC -!- TISSUE SPECIFICITY: IMAGINAL (ANTERIOR) EPIDERMIS. CC -!- MISCELLANEOUS: THE SEQUENCE SHOWN IS FROM GENOMIC DNA. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M71247; AAA28499.1; -. DR EMBL; M71248; AAA28500.1; -. DR EMBL; AE003594; AAF51702.1; -. DR PIR; A49773; A49773. DR FlyBase; FBgn0000551; Edg78E. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PRINTS; PR00947; CUTICLE. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 122 PUPAL CUTICLE PROTEIN EDG-78E. FT VARIANT 51 51 I -> S (IN CDNA). SQ SEQUENCE 122 AA; 13347 MW; CD68BC35B62F78E0 CRC64; MYKYLFCLAL IGCACADNIN KDAQIRSFQN DATDAEGNYQ YAYETSNGIQ IQEAGNANGA RGAVAYVSPE GEHISLTYTA DEEGYHPVGD HLPTPPPVPA YVLRALEYIR THPPAPAQKE QQ // ID CUP8_DROME STANDARD; PRT; 188 AA. AC P27780; Q9VI43; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pupal cuticle protein Edg-84A precursor. GN EDG84A OR EDG-84A OR CG2345. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91323677; PubMed=1713868; RA Apple R.T., Fristrom J.W.; RT "20-Hydroxyecdysone is required for, and negatively regulates, RT transcription of Drosophila pupal cuticle protein genes."; RL Dev. Biol. 146:569-582(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., RA Palazzolo M.J.; RT "Complete sequence of the Antennapedia complex of Drosophila."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: COMPONENT OF THE CUTICLE OF THE PUPA OF FRUIT FLY. CC -!- TISSUE SPECIFICITY: IMAGINAL (ANTERIOR) EPIDERMIS. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M71249; AAA28501.1; -. DR EMBL; AE001572; AAD19810.1; -. DR EMBL; AE003674; AAF54097.2; -. DR PIR; B49773; B49773. DR FlyBase; FBgn0000552; Edg84A. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PRINTS; PR00947; CUTICLE. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 188 PUPAL CUTICLE PROTEIN EDG-84A. SQ SEQUENCE 188 AA; 20365 MW; 6C273FC9E09D012D CRC64; MLVKTALFVT LIGLAQAGPL PAKSSGSEDT YDSHPQYSFN YDVQDPETGD VKSQSESRDG DVVHGQYSVN DADGYRRTVD YTADDVRGFN AVVRREPLSS AAVVVKPQAT AVVPKVQLKP LKKLPALKPL SQASAVVHRS FAPVVHHAPV THVVHHAAPA HSFVSHHVPV LKTTVHHAHH PHAISYVF // ID CUP9_DROME STANDARD; PRT; 159 AA. AC P27781; Q9VEI1; DT 01-AUG-1992 (Rel. 23, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pupal cuticle protein Edg-91 precursor (Ecdysone-dependent protein DE 91). GN EDG91 OR EDG-91 OR CG7539. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91323677; PubMed=1713868; RA Apple R.T., Fristrom J.W.; RT "20-Hydroxyecdysone is required for, and negatively regulates, RT transcription of Drosophila pupal cuticle protein genes."; RL Dev. Biol. 146:569-582(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE PUPAL CUTICLE. CC -!- TISSUE SPECIFICITY: LARVAL (POSTERIOR) AND IMAGINAL (ANTERIOR) CC EPIDERMIS. CC -!- DEVELOPMENTAL STAGE: PREPUPAL AND EARLY PUPAL STAGES. CC -!- DOMAIN: THIS PROTEIN IS GLYCINE-RICH AND CONTAINS SEVERAL REPEATS CC OF THE MOTIF (G/S)1-4(Y/F) LIKE STRUCTURAL PROTEINS FROM INSECT CC EGG SHELLS, EGG CASES AND VERTEBRATE CYTOKERATINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M71250; AAA28502.1; -. DR EMBL; M71251; AAA28503.1; -. DR EMBL; AE003718; AAF55440.1; -. DR PIR; C49773; C49773. DR FlyBase; FBgn0004554; Edg91. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 21 FT CHAIN 22 159 PUPAL CUTICLE PROTEIN EDG-91. FT DOMAIN 35 159 GLY/TYR-RICH. FT CONFLICT 29 29 S -> R (IN REF. 1). FT CONFLICT 109 109 H -> Y (IN REF. 1). SQ SEQUENCE 159 AA; 15261 MW; 266216A2A39AA06F CRC64; MALVRVSCML ALLLIAGQGQ AAPVKTEGST LGLLGGGFGG SVGLSAGIGV GGGLYSGFGG GGYPGGYASG YPGGYGGGYS GYNGYGGSGF GGGYYPGGGY SGFGHRPHHH GGYYPGGGSY HNQGGSYGGH YSQSQYSNGY YGGGGYGGGG YGGNGFFGK // ID CUPP_DROME STANDARD; PRT; 184 AA. AC P14484; Q9VM52; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pupal cuticle protein precursor. GN PCP OR CG3440. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86079579; PubMed=3079672; RA Henikoff S., Keene M.A., Fechtel K., Fristrom J.W.; RT "Gene within a gene: nested Drosophila genes encode unrelated RT proteins on opposite DNA strands."; RL Cell 44:33-42(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88112752; PubMed=3123310; RA Henikoff S., Eghtedarzadeh M.K.; RT "Conserved arrangement of nested genes at the Drosophila Gart locus."; RL Genetics 117:711-725(1987). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE CUTICLE OF THE PUPA OF FRUIT FLY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT BOTH THE FOURTH AND THE CC FIFTH LARVAL INSTARS. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J02527; AAA28564.1; -. DR EMBL; AE003615; AAF52475.1; -. DR PIR; B24787; UCFFPM. DR FlyBase; FBgn0003046; Pcp. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PRINTS; PR00947; CUTICLE. DR PROSITE; PS00233; CUTICLE; 1. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 15 POTENTIAL. FT CHAIN 16 184 PUPAL CUTICLE PROTEIN. FT CONFLICT 4 4 L -> LQ (IN REF. 1). SQ SEQUENCE 184 AA; 20633 MW; 4493B893F61329C2 CRC64; MYLLVNFIVA LAVLQVQAGS SYIPDSDRNT RTLQNDLQVE RDGKYRYAYE TSNGISASQE GLGGVAVQGG SSYTSPEGEV ISVNYVADEF GYHPVGAHIP QVPDYILRSL EYIRTHPYQI KDYYTGELKT VEHDAAAFNV YTRNIQDHTI PQSRPSTTPK TIYLTHPPTT TSRPLRQRRA LPTH // ID CYA1_DROME STANDARD; PRT; 2248 AA. AC P32870; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ca(2+)/calmodulin-responsive adenylate cyclase (EC 4.6.1.1) (ATP DE pyrophosphate-lyase) (Rutabaga protein). GN RUT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=92154664; PubMed=1739965; RA Levin L.R., Han P.-L., Hwang P.M., Feinstein P.G., Davis R.L., RA Reed R.R.; RT "The Drosophila learning and memory gene rutabaga encodes a RT Ca2+/Calmodulin-responsive adenylyl cyclase."; RL Cell 68:479-489(1992). CC -!- FUNCTION: THIS IS A MEMBRANE-BOUND, CALMODULIN-SENSITIVE ADENYLYL CC CYCLASE. INACTIVATION OF THIS CYCLASE LEADS TO A LEARNING AND CC MEMORY DEFECT. CC -!- CATALYTIC ACTIVITY: ATP = 3',5'-CYCLIC AMP + DIPHOSPHATE. CC -!- COFACTOR: BINDS 2 MAGNESIUM IONS PER SUBUNIT (BY SIMILARITY). CC -!- ENZYME REGULATION: ACTIVATED BY CALCIUM/CALMODULIN AND G PROTEIN. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: MUSHROOM BODIES OF THE FLY BRAIN. CC -!- DOMAIN: COMPOSED OF TWO HOMOLOGOUS DOMAINS. CC -!- SIMILARITY: BELONGS TO THE ADENYLYL CYCLASE CLASS-4/GUANYLYL CC CYCLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81887; AAA28844.1; -. DR PIR; D42088; D42088. DR HSSP; P19754; 1AWK. DR FlyBase; FBgn0003301; rut. DR GO; GO:0019933; P:cAMP-mediated signaling; NAS. DR GO; GO:0007625; P:grooming behavior; NAS. DR GO; GO:0007591; P:molting cycle (sensu Insecta); IGI. DR GO; GO:0008355; P:olfactory learning; NAS. DR GO; GO:0045473; P:response to ethanol (sensu Insecta); NAS. DR InterPro; IPR001054; G_cyclase. DR Pfam; PF00211; guanylate_cyc; 2. DR SMART; SM00044; CYCc; 2. DR PROSITE; PS00452; GUANYLATE_CYCLASES_1; 2. DR PROSITE; PS50125; GUANYLATE_CYCLASES_2; 2. KW Lyase; cAMP biosynthesis; Transmembrane; Glycoprotein; Repeat; KW Metal-binding; Magnesium. FT DOMAIN 1 41 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 42 60 POTENTIAL. FT TRANSMEM 65 84 POTENTIAL. FT TRANSMEM 101 115 POTENTIAL. FT TRANSMEM 122 142 POTENTIAL. FT TRANSMEM 152 174 POTENTIAL. FT TRANSMEM 186 206 POTENTIAL. FT DOMAIN 207 705 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 706 726 POTENTIAL. FT TRANSMEM 730 750 POTENTIAL. FT TRANSMEM 770 791 POTENTIAL. FT DOMAIN 792 813 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 814 834 POTENTIAL. FT TRANSMEM 842 867 POTENTIAL. FT TRANSMEM 868 888 POTENTIAL. FT DOMAIN 889 2248 CYTOPLASMIC (POTENTIAL). FT DOMAIN 318 334 CATALYTIC (POTENTIAL). FT DOMAIN 1013 1029 CATALYTIC (POTENTIAL). FT DOMAIN 515 530 GLY-RICH. FT DOMAIN 569 602 GLY-RICH. FT DOMAIN 1278 1297 GLN-RICH. FT DOMAIN 1767 1810 GLY/SER-RICH. FT DOMAIN 2025 2040 ASP/GLU-RICH (ACIDIC). FT DOMAIN 2200 2241 GLN-RICH. FT METAL 280 280 MAGNESIUM 1 AND 2 (BY SIMILARITY). FT METAL 281 281 MAGNESIUM 2 (VIA CARBONYL OXYGEN) (BY FT SIMILARITY). FT METAL 324 324 MAGNESIUM 1 AND 2 (BY SIMILARITY). FT CARBOHYD 800 800 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 807 807 N-LINKED (GLCNAC...) (POTENTIAL). FT MUTAGEN 1026 1026 G->R: ABOLISHES CATALYTIC ACTIVITY. SQ SEQUENCE 2248 AA; 248899 MW; E459C718BE018868 CRC64; MDHAVKATRG RPLNTLRFEN DELECLYQRY TLKLQRFSVL GVVALVFVLC GVMAALSLTF NNAVTFHNIF NAIVCGLFAV VLVLLQCSVI KDHHLPTLCY GILLFTASIC VVSMPTLGSV FPVDTKEVMA EGVWQIVFVV FLAYAMMPLQ IWEAVAFGIA LPSVHISLTV YKIFTDALRY LEYNQLIANI VIFIGVNVAG LVVNIMMERA QRRTFLDTRN CIASRLEIQD ENEKLERLLL SVLPQHVAMQ MKNDILSPVA GQFHRIYIQK HENVSILFAD IVGFTVLSSQ CSAQELVRLL NELFGRFDQL AHDNHCLRIK ILGDCYYCVS GLPEPRKDHA KCAVEMGLDM IDAIATVVEA TDVILNMRVG IHTGRVLCGV LGLRKWQFDV WSNDVTLANH MESGGEPGRV HVTRATLDSL SGEYEVEAGH GDERSSYLRD HGVDTFFIVP PPHRRKPLML NTLGVRSAIG SRRKLSFRNV SNVVMQLLHT IKFSEPVPFS NIATGSFPSA ASALGGGVSV GGGGGGGGGG VARGSTCEAN SGNVQVSEKG SRKVIRLQKI LHATPPPHGM GYGSVVGSGG GVDSGISGGG GCVSGSIAGG GGVQVTVGTN PNSTASTISR IHRHNHKNNK SQSKVADKFK RPFRKRHSVA AHHQPTNRVN RFLSQAINAR SVDCDKSEHV DRLTLRFRQS DMEREYHKDF DLGFTTAMGC SLLLLILGAA LQVTALPRTL ILLLLFLFAF IWVSAILMLL LAVRLKWIIW DISESFSLRM AITIFTVILI YSVGQVNVFT CVSDHPCSGN GTTSFQNDSH RKCSLPQYVS LSAAFAFLSV SVFLRLPIIF KSLLVLGMGT IYGLFIELSH QNIFECYDNR VNASIPLHLI SLARIAIFMI AILVHGRLVE GTARLDFLWQ LQASQEKKEM DVLQESNKRI LHNLLPAHVA AHFLDAQFRN NMELYHQSYA KVGVIFASVP NFNEFYTEMD GSDQGLECLR LLNEIIADFD ELLKEDRFRG IDKIKTVGST YMAVVGLIPE YKIQPNDPNS VRRHMTALIE YVKAMRHSLQ EINSHSYNNF MLRVGINIGP VVAGVIGARK PQYDIWGNTV NVASRMDSTG VPGYSQVTQE VVDSLVGSHF EFRCRGTIKV KGKGDMVTYF LCDSGNKSLN GEVRNAMSLP QSLHAPDYYM KVSQFPENRV NTDTYSKKEN GHLYAGNGVE EQQLLLQHQH KQHDPLPLPA PPPPVHHHLH QQQQQRLNSK LQKQPIFMAN GGLPNIRENG NGHNGEHQQQ QQQQQHQQQQ QHQQQQQHGG FMVATTTPPA AVAVPLQPQH HQLQFQHPHQ HPLPSAVSVP VQHQILLHHQ LQLQHQPVPS VMLREFNIIE NPTSGGRHQQ MEQLPPHHGS LDLSGMGMGV GAGVLGGDCF MMPRRDRERT YVPPLNQHGH HPPHHLHSNL NLNQSQHPPS FTSLGYGQCR ESEPLLHASS VAPVAKIMPM QHAPKYEPPR YTSPHTMLSQ QHQQQQQHQH QQPQSQSQSA QDQQTHPAQD PHPLQRQYAM YSQQPQLPPK PVLRTYMKPL PKLPTDLEES RDMSSTDDLS SRPHSPSMSS SDESYSKTTE GEGEGDEDSP RMVNGGHLHH RNGYHLPAGG LVNPLQWLYP CDIQVDPTSP VVDMAHLHDF ELSSTTESQG HHTNSNTTSN TQQKGDSCNS FDFQKATVGT AAGAAIATKS PFERELQRLL NESSRARCLA TATTTAGAIS TTDQTASNGS RELSYSLSNG KLSSANGHGV GGSGSGSGSG SGSAVGNGSG GSGSSNGNLG GGSGSNSNSG NNNSSHHKTE QQQNMDHEHL AGGKLLGSNS FMIAKHPVGL EAIKEITRNK NPSESSQMQT SDTESCEILH ENRNQMHVLA MLEMHTAKEL NGSHAHHGQH HHQQPQRTHR QRPRSKELQY SHESLDGLDG AVQSQSQQRN QRYHHHHHHQ QRQQQQQRYN HVQEQEERDD TEDNLADEEF EDDEVGRDVR QKRLQKSELN HKRSEVATEA GNHHDDEVEE EDDDDDEEED HRNGGREAAP LTNGSMRGLE ANVINDELKY GATHLNHQSM DSNPLESQSE WSDDDCREEA TGGAESTGYI TDEPGLENIS LLNEAGLTDA EGALSDVNSL YNAPDVDDTS VSSRASSRLL SLDSLSGLYD CDLDSKHELA IVNASHKISS KFGQPLSPAQ QQHQQQQQQQ QQQQQQHQQQ QLQQNPQHTQ AQSHLAPVQF QSAEELRE // ID CYB5_DROME STANDARD; PRT; 134 AA. AC Q9V4N3; Q8IH75; Q9I7E0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome b5 (CYTB5). GN CYT-B5 OR CG2140. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CYTOCHROME B5 IS A MEMBRANE BOUND HEMOPROTEIN WHICH CC FUNCTION AS AN ELECTRON CARRIER FOR SEVERAL MEMBRANE BOUND CC OXYGENASES (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MICROSOMAL MEMBRANE. BOUND TO THE CC CYTOPLASMIC SIDE OF THE ENDOPLASMIC RETICULUM (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=Q9V4N3-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=A; CC IsoId=Q9V4N3-2; Sequence=VSP_008871; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME B5 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003840; AAF59233.3; -. DR EMBL; AE003840; AAG22305.2; -. DR EMBL; BT001378; AAN71133.1; -. DR EMBL; BT004852; AAO45208.1; -. DR HSSP; P00171; 1WDB. DR FlyBase; FBgn0033189; Cyt-b5. DR InterPro; IPR001199; Cyt_B5. DR Pfam; PF00173; heme_1; 1. DR ProDom; PD000612; Cyt_B5; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. KW Electron transport; Transmembrane; Heme; Iron; Microsome; KW Alternative splicing. FT TRANSMEM 111 131 POTENTIAL. FT METAL 41 41 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT METAL 65 65 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT VARSPLIC 1 40 MSSEETKTFTRAEVAKHNTNKDTWLLIHNNIYDVTAFLNE FT -> MVQSKRNFARVLRIKVSVTLLAYKCQIKS (in FT isoform A). FT /FTId=VSP_008871. SQ SEQUENCE 134 AA; 15206 MW; 11D1FB03EFAB40DC CRC64; MSSEETKTFT RAEVAKHNTN KDTWLLIHNN IYDVTAFLNE HPGGEEVLIE QAGKDATENF EDVGHSNDAR DMMKKYKIGE LVESERTSVA QKSEPTWSTE QQTEESSVKS WLVPLVLCLV ATLFYKFFFG GAKQ // ID CYBR_DROME STANDARD; PRT; 414 AA. AC P19967; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Protein TU-36B (Cytochrome b5-related protein). GN CYT-B5-R. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89366661; PubMed=2549511; RA Levin R.J., Boychuk P.L., Croniger C.M., Kazzaz J.A., Rozek C.E.; RT "Structure and expression of a muscle specific gene which is adjacent RT to the Drosophila myosin heavy-chain gene and can encode a cytochrome RT b related protein."; RL Nucleic Acids Res. 17:6349-6367(1989). CC -!- FUNCTION: MAY PLAY A ROLE IN MUSCLE CELL METABOLISM. CC -!- TISSUE SPECIFICITY: MUSCLE. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE CYTOCHROME CC B5 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15008; CAA33113.1; -. DR PIR; S05441; S05441. DR FlyBase; FBgn0000406; Cyt-b5-r. DR InterPro; IPR001199; Cyt_B5. DR InterPro; IPR005804; FA_desat_fam. DR Pfam; PF00487; FA_desaturase; 1. DR Pfam; PF00173; heme_1; 1. DR ProDom; PD000612; Cyt_B5; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. KW Heme. FT METAL 59 59 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT METAL 82 82 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT VARIANT 202 202 P -> A. FT VARIANT 213 213 T -> I. FT VARIANT 344 344 G -> R. SQ SEQUENCE 414 AA; 47147 MW; C8E49FF43587209C CRC64; MVIEEWKKSG IATKFPTYRN SALITTHSWQ KGKRQDDGAE GLWRINDGIY DFTSFIDKHP GGPFWIRETK GTDITEAFEA HHLTTAPEKM IAKYKVRDAA EPRIYTLTLE EGGFYKTLKE RVREQLKTID KRPKKKSDLI HLGLVVSLYL LGIASAKYNS LLALVLASVA LCWTVIVSHN YFHRRDNWQM YAFNLGMMNF APWRVSHALS HHTYPNSYLN LELSMFEPLL CWVPNPHIKS KLMRYVSWVT EPVAYALAFF IQMGTRIFYS LRHTNILYWH DLLPLTIPIA IYLGTGGSLG IWICVRQWLA MTSIASFSFC LIGLNAAHHD PEIYHEGDAN REDGDWGSSR WTRLSTAVIS SGRSSWCSPT LVTMCSTISS RPWIMASCPP SIRCFTRLSM SSRVISASAT TSST // ID CYB_DROME STANDARD; PRT; 378 AA. AC P18935; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome b. GN MT:CYT-B OR COB OR CYTB. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Bretagne; RX MEDLINE=88212147; PubMed=3130291; RA Garesse R.; RT "Drosophila melanogaster mitochondrial DNA: gene organization and RT evolutionary considerations."; RL Genetics 118:649-663(1988). CC -!- FUNCTION: COMPONENT OF THE UBIQUINOL-CYTOCHROME C REDUCTASE CC COMPLEX (COMPLEX III OR CYTOCHROME B-C1 COMPLEX), WHICH IS A CC RESPIRATORY CHAIN THAT GENERATES AN ELECTROCHEMICAL POTENTIAL CC COUPLED TO ATP SYNTHESIS (BY SIMILARITY). CC -!- COFACTOR: BINDS TWO HEME GROUPS NON-COVALENTLY. HEME 1 (OR BL OR CC B562) IS LOW-POTENTIAL AND ABSORBS AT ABOUT 562, AND HEME 2 (OR BH CC OR B566) IS HIGH-POTENTIAL AND ABSORBS AT ABOUT 566 (BY CC SIMILARITY). CC -!- SUBUNIT: THE MAIN SUBUNITS OF COMPLEX B-C1 ARE: CYTOCHROME B, CC CYTOCHROME C1 AND THE RIESKE PROTEIN (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME B FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37275; AAA69714.1; -. DR EMBL; U37541; AAC47822.1; -. DR PIR; S01190; S01190. DR FlyBase; FBgn0013678; mt:Cyt-b. DR InterPro; IPR005798; Cytb_b6_C. DR InterPro; IPR005797; Cytb_b6_N. DR Pfam; PF00032; cytochrome_b_C; 1. DR Pfam; PF00033; cytochrome_b_N; 1. DR PROSITE; PS00192; CYTOCHROME_B_HEME; 1. DR PROSITE; PS00193; CYTOCHROME_B_QO; 1. KW Electron transport; Mitochondrion; Respiratory chain; Transmembrane; KW Heme. FT METAL 84 84 IRON 1 (HEME B562 AXIAL LIGAND). FT METAL 98 98 IRON 2 (HEME B566 AXIAL LIGAND). FT METAL 183 183 IRON 1 (HEME B562 AXIAL LIGAND). FT METAL 197 197 IRON 2 (HEME B566 AXIAL LIGAND). SQ SEQUENCE 378 AA; 43224 MW; 6CB9067643ABCE83 CRC64; MNKPLRNSHP LFKIANNALV DLPAPINISS WWNFGSLLGL CLIIQILTGL FLAMHYTADI NLAFYSVNHI CRDVNYGWLL RTLHANGASF FFICIYLHVG RGIYYGSYKF TPTWLIGVII LFLVMGTAFM GYVLPWGQMS FWVATVITNL LYAIPYLGMD LVQWLWGGFA VDNATLTRFF TFHFILPFIV LAMTMIHLLF LHQTGSNNPI GLNSNIDKIP FHPYFTFKDI VGFIVMIFIL ISLVLISPNL LGDPDNFIPA TPLVTPAHIQ PEWYFLFAYA ILRSIPNKLG GVIALVLSIA ILMILPFYNL SKFRGIQFYP INQVMFWSML VTVILLTWIG ARPVEEPYVL IGQILTVVYF LYYLVNPLIT KWWDNLLN // ID CYC1_DROME STANDARD; PRT; 104 AA. AC P04657; Q9VJJ4; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome c-1 (Cytochrome c-distal). GN CYT-C-D OR CYTC1 OR DC3 OR CG13263. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85215502; PubMed=2987802; RA Limbach K.J., Wu R.; RT "Characterization of two Drosophila melanogaster cytochrome c genes RT and their transcripts."; RL Nucleic Acids Res. 13:631-644(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ELECTRON CARRIER PROTEIN. THE OXIDIZED FORM OF THE CC CYTOCHROME C HEME GROUP CAN ACCEPT AN ELECTRON FROM THE HEME GROUP CC OF THE CYTOCHROME C1 SUBUNIT OF CYTOCHROME REDUCTASE. CYTOCHROME C CC THEN TRANSFERS THIS ELECTRON TO THE CYTOCHROME OXIDASE COMPLEX, CC THE FINAL PROTEIN CARRIER IN THE MITOCHONDRIAL ELECTRON-TRANSPORT CC CHAIN. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT CONSTANT, BUT RELATIVELY LOW CC LEVELS THROUGHOUT DEVELOPMENT. CC -!- PTM: BINDS 1 HEME GROUP PER MOLECULE. CC -!- MISCELLANEOUS: THERE ARE TWO CYTOCHROME C GENES IN DROSOPHILA: CC CYT-C-D (DISTAL) AND CYT-C-P (PROXIMAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME C FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01761; CAA25901.1; -. DR EMBL; AE003652; AAF53553.1; -. DR EMBL; BT006002; AAO67367.1; -. DR PIR; B23058; B23058. DR HSSP; P00004; 1WEJ. DR FlyBase; FBgn0000408; Cyt-c-d. DR GO; GO:0005739; C:mitochondrion; IDA. DR GO; GO:0005489; F:electron transporter activity; IDA. DR InterPro; IPR003088; Cyt_CI. DR InterPro; IPR002327; Cyt_CIAB. DR InterPro; IPR000345; CytC_heme_BS. DR Pfam; PF00034; cytochrome_c; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR ProDom; PD000375; Cyt_CIAB; 1. DR PROSITE; PS00190; CYTOCHROME_C; 1. KW Mitochondrion; Electron transport; Respiratory chain; Heme. FT INIT_MET 0 0 FT BINDING 16 16 HEME (COVALENT). FT BINDING 19 19 HEME (COVALENT). FT METAL 20 20 IRON (HEME AXIAL LIGAND). FT METAL 82 82 IRON (HEME AXIAL LIGAND). SQ SEQUENCE 104 AA; 11238 MW; 3818D90092876729 CRC64; GSGDAENGKK IFVQKCAQCH TYEVGGKHKV GPNLGGVVGR KCGTAAGYKY TDANIKKGVT WTEGNLDEYL KDPKKYIPGT KMVFAGLKKA EERADLIAFL KSNK // ID CYC2_DROME STANDARD; PRT; 107 AA. AC P00034; P00033; Q9VJJ3; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome c-2 (Cytochrome c-proximal). GN CYT-C-P OR CYTC2 OR DC4 OR CG17903. OS Drosophila melanogaster (Fruit fly), and OS Ceratitis capitata (Mediterranean fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7213; RN [1] RP SEQUENCE. RC SPECIES=D.melanogaster; RX MEDLINE=87137362; PubMed=3029051; RA Inoue S., Inoue H., Hiroyoshi T., Matsubara H., Yamanaka T.; RT "Developmental variation and amino acid sequences of cytochromes c of RT the fruit fly Drosophila melanogaster and the flesh fly Boettcherisca RT peregrina."; RL J. Biochem. 100:955-965(1986). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=85215502; PubMed=2987802; RA Limbach K.J., Wu R.; RT "Characterization of two Drosophila melanogaster cytochrome c genes RT and their transcripts."; RL Nucleic Acids Res. 13:631-644(1985). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=85166253; PubMed=2984675; RA Swanson M.S., Zieminn S.M., Miller D.D., Garber E.A.E., RA Margoliash E.; RT "Developmental expression of nuclear genes that encode mitochondrial RT proteins: insect cytochromes c."; RL Proc. Natl. Acad. Sci. U.S.A. 82:1964-1968(1985). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE. RC SPECIES=C.capitata; RX MEDLINE=75205681; PubMed=167835; RA Fernandez-Sousa J.M., Gavilanes J.G., Municio A.M., Paredes J.A., RA Perez-Aranda A., Rodriguez R.; RT "Primary structure of cytochrome c from the insect Ceratitis RT capitata."; RL Biochim. Biophys. Acta 393:358-367(1975). CC -!- FUNCTION: ELECTRON CARRIER PROTEIN. THE OXIDIZED FORM OF THE CC CYTOCHROME C HEME GROUP CAN ACCEPT AN ELECTRON FROM THE HEME GROUP CC OF THE CYTOCHROME C1 SUBUNIT OF CYTOCHROME REDUCTASE. CYTOCHROME C CC THEN TRANSFERS THIS ELECTRON TO THE CYTOCHROME OXIDASE COMPLEX, CC THE FINAL PROTEIN CARRIER IN THE MITOCHONDRIAL ELECTRON-TRANSPORT CC CHAIN. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT VARYING, BUT RELATIVELY HIGH CC LEVELS THROUGHOUT DEVELOPMENT. CC -!- PTM: BINDS 1 HEME GROUP PER MOLECULE. CC -!- MISCELLANEOUS: THERE ARE TWO CYTOCHROME C GENES IN DROSOPHILA: CC CYT-C-D (DISTAL) AND CYT-C-P (PROXIMAL). CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME C FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01760; CAA25900.1; -. DR EMBL; M11381; AAA28437.1; -. DR EMBL; AE003652; AAF53554.1; -. DR EMBL; AY071701; AAL49323.1; -. DR PIR; A00030; CCFFCM. DR PIR; A22945; CCFFDM. DR HSSP; P00004; 1WEJ. DR FlyBase; FBgn0000409; Cyt-c-p. DR GO; GO:0005739; C:mitochondrion; IDA. DR GO; GO:0005489; F:electron transporter activity; IDA. DR InterPro; IPR003088; Cyt_CI. DR InterPro; IPR002327; Cyt_CIAB. DR InterPro; IPR000345; CytC_heme_BS. DR Pfam; PF00034; cytochrome_c; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR ProDom; PD000375; Cyt_CIAB; 1. DR PROSITE; PS00190; CYTOCHROME_C; 1. KW Mitochondrion; Electron transport; Respiratory chain; Heme. FT INIT_MET 0 0 FT BINDING 18 18 HEME (COVALENT). FT BINDING 21 21 HEME (COVALENT). FT METAL 22 22 IRON (HEME AXIAL LIGAND). FT METAL 84 84 IRON (HEME AXIAL LIGAND). SQ SEQUENCE 107 AA; 11603 MW; C84B69C5BDDEEFEB CRC64; GVPAGDVEKG KKLFVQRCAQ CHTVEAGGKH KVGPNLHGLI GRKTGQAAGF AYTDANKAKG ITWNEDTLFE YLENPKKYIP GTKMIFAGLK KPNERGDLIA YLKSATK // ID CYCL_DROME STANDARD; PRT; 413 AA. AC O61734; O76344; Q9VW44; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cycle protein (Brain and muscle ARNT-like 1) (BMAL1) (MOP3). GN CYC OR CG8727. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=98292178; PubMed=9630224; RA Rutila J.E., Suri V., Le M., So W.V., Rosbash M., Hall J.C.; RT "CYCLE is a second bHLH-PAS clock protein essential for circadian RT rhythmicity and transcription of Drosophila period and timeless."; RL Cell 93:805-814(1998). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Brain, and Muscle; RX MEDLINE=98279147; PubMed=9616122; RA Darlington T.K., Wager-Smith K., Ceriani M.F., Staknis D., Gekakis N., RA Steeves T.D.L., Weitz C.J., Takahashi J.S., Kay S.A.; RT "Closing the circadian loop: CLOCK-induced transcription of its own RT inhibitors per and tim."; RL Science 280:1599-1603(1998). RN [3] RP SEQUENCE FROM N.A. RA Bae K.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PUTATIVE TRANSCRIPTION FACTOR INVOLVED IN THE GENERATION CC OF BIOLOGICAL RHYTHMS. ACTIVATES CYCLING TRANSCRIPTION OF PERIOD CC (PER) AND TIMELESS (TIM) BY BINDING TO THE E-BOX (3'-CACGTG-5') CC PRESENT IN THEIR PROMOTERS. CYC MUTANTS DON'T DISPLAY PER AND TIM CC CYCLING, AND ARE COMPLETELY ARRHYTHMIC. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. FORMS A HETERODIMER WITH CLOCK IN ORDER TO ACTIVATE CC PER AND TIM TRANSCRIPTION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED AT LEAST IN HEAD AND OVARY. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PAS (PER-ARNT-SIM) DIMERIZATION DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PAS-ASSOCIATED C-TERMINAL (PAC) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF065473; AAC39124.1; -. DR EMBL; AF069998; AAC62235.1; -. DR EMBL; AF067206; AAD10629.1; -. DR EMBL; AE003515; AAF49107.1; -. DR HSSP; P22415; 1AN4. DR FlyBase; FBgn0023094; cyc. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0008062; P:eclosion rhythm; NAS. DR GO; GO:0045475; P:locomotor rhythm; NAS. DR GO; GO:0045893; P:positive regulation of transcription, DNA-d...; NAS. DR GO; GO:0045187; P:regulation of sleep; IMP. DR GO; GO:0008341; P:response to cocaine (sensu Insecta); NAS. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR001067; Nuc_translocat. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS_domain. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00989; PAS; 1. DR PRINTS; PR00785; NCTRNSLOCATR. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR PROSITE; PS50888; HLH; 1. DR PROSITE; PS50112; PAS; 2. KW Transcription regulation; DNA-binding; Repeat; Nuclear protein; KW Biological rhythms. FT DNA_BIND 31 43 BASIC DOMAIN. FT DOMAIN 44 84 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 104 175 PAS 1. FT DOMAIN 297 367 PAS 2. FT DOMAIN 372 413 PAC. FT DOMAIN 228 234 POLY-SER. FT CONFLICT 242 242 S -> T (IN REF. 4). FT CONFLICT 308 308 H -> Y (IN REF. 1). FT CONFLICT 362 362 M -> V (IN REF. 1). SQ SEQUENCE 413 AA; 47555 MW; 5349476A05360386 CRC64; MEVQEFCENM EEIEDENYDE EKSARTSDEN RKQNHSEIEK RRRDKMNTYI NELSSMIPMC FAMQRKLDKL TVLRMAVQHL RGIRGSGSLH PFNGSDYRPS FLSDQELKMI ILQASEGFLF VVGCDRGRIL YVSDSVSSVL NSTQADLLGQ SWFDVLHPKD IGKVKEQLSS LEQCPRERLI DAKTMLPVKT DVPQSLCRLC PGARRSFFCR MKLRTASNNQ IKEESDTSSS SRSSTKRKSR LSTGHKYRVI QCTGYLKSWT PIKDEDQDAD SDEQTTNLSC LVAIGRIPPN VRNSTVPASL DNHPNIRHVL FISRHSGEGK FLFIDQRATL VIGFLPQEIL GTSFYEYFHN EDIAALMESH KMVMQVPEKV TTQVYRFRCK DNSYIQLQSE WRAFKNPWTS EIDYIIAKNS VFL // ID CYGE_DROME STANDARD; PRT; 1163 AA. AC Q07553; Q9VKI9; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanylate cyclase 32E precursor (EC 4.6.1.2). GN GYC32E OR GC OR CG33114/CG6275. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE OF 59-1163 FROM N.A., AND CHARACTERIZATION. RC STRAIN=Oregon-R; TISSUE=Embryo, and Head; RX MEDLINE=94009923; PubMed=8104831; RA Gigliotti S., Cavaliere V., Manzi A., Tino A., Graziani F., Malva C.; RT "A membrane guanylate cyclase Drosophila homolog gene exhibits RT maternal and zygotic expression."; RL Dev. Biol. 159:450-461(1993). CC -!- CATALYTIC ACTIVITY: GTP = 3',5'-CYCLIC GMP + DIPHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND CC ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE ADENYLYL CYCLASE CLASS-4/GUANYLYL CC CYCLASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 GUANYLATE CYCLASE DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PROTEIN KINASE-LIKE DOMAIN. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 1058. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003631; AAF53079.3; -. DR EMBL; X72800; CAA51318.1; ALT_FRAME. DR EMBL; X72801; CAA51319.1; ALT_FRAME. DR HSSP; Q02846; 1AWL. DR FlyBase; FBgn0010197; Gyc32E. DR GO; GO:0005887; C:integral to plasma membrane; NAS. DR GO; GO:0004383; F:guanylate cyclase activity; NAS. DR GO; GO:0004872; F:receptor activity; NAS. DR GO; GO:0006182; P:cGMP biosynthesis; NAS. DR InterPro; IPR001828; ANF_receptor. DR InterPro; IPR001054; G_cyclase. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00452; GUANYLATE_CYCLASES_1; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASES_2; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Receptor; Transmembrane; Glycoprotein; Lyase; cGMP biosynthesis; KW Signal. FT SIGNAL 1 25 POTENTIAL. FT CHAIN 26 1163 GUANYLATE CYCLASE 32E. FT DOMAIN 29 469 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 470 490 POTENTIAL. FT DOMAIN 491 1163 CYTOPLASMIC (POTENTIAL). FT DOMAIN 507 800 PROTEIN KINASE-LIKE. FT DOMAIN 873 1003 GUANYLATE CYCLASE. FT DISULFID 454 454 INTERCHAIN (PROBABLE). FT CARBOHYD 147 147 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 206 206 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 368 368 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 390 390 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 59 59 L -> D (IN REF. 3). FT CONFLICT 678 678 A -> L (IN REF. 3). FT CONFLICT 831 841 RTNLLYEEKKK -> ANQFVVRREEE (IN REF. FT 3). FT CONFLICT 893 893 E -> M (IN REF. 3). FT CONFLICT 910 910 S -> W (IN REF. 3). FT CONFLICT 962 962 P -> R (IN REF. 3). SQ SEQUENCE 1163 AA; 130914 MW; 9C0E949DA9FB7E7E CRC64; MPGPCASAAA FSCILVLLLL GCQRSNPLAA GATVSSMRRL TDTINIGFLA EYSQMRVTLG GLPLAIEDVN KNPNLLPGKK LAFKPVDIGH KMSAYRVKPL RAMTQMREAG VTAFIGPDES CTTEALLASA WNTPMLSFKC SDPIVSNKST FHTFARTLAP ASKVSKSVIS LLNAFHWNKF SIVVSSKPIW GSDVARAIQE LAEARNFTIS HFKYISDYIP TTKTLSQIDK IIEETYATTR IYVFIGEHIA MVDFVRGLQN RRLLESGDYI VVSVDDEIYD SNRRVNIMER NYLDPYIRKE KSKSLDKISF RSVIKISMTY PQNPHIRVPI YGLHLYDSVM IYVRAITEVL RLGGDIYDGN LVMSHIFNRS YHSIQGFDVY IDSNGDAEGN YTVITLQNDV GSGASIGSLA KMSMQPVGFF AYDKNSVIPE FRYIKNDRPI QWLNGRPPLA EPLCGFHGEL CPRKKLDWRY LVSGPLCALV VVVAIALLIK HYRYEQTLAG LLWKVDMKDV TVINLGEYNN PTNKNIFQIC RQSILVVGEP NKRSFTNIAL FRGNIVAMKK IHKKSVDITR SIRKELKLMR EVRHENIINF IGASTDHGSV IIFTTYCARG SLEDVLANED LHLDHMFISS LVSDILKGMI YLHDSEIISH GNLRSSNCLI DSRWVCQISD FGLHELKAGQ EEPNKSELEL KRALCMAPEL LRDAYRPGRG SQKGDVYSFG ILLYEMIGRK GPWGDTAYSK EEIIQFVKCP EMLQHGVFRP ALTHTHLDIP DYIRKCLCQC WDEDPEVRPD IRLVRMHLKE LQAGLKPNIF DNMLSIMEKY AYNLEGLVQE RTNLLYEEKK KTDMLLYQML PRPVAELLKR GDPVEAECFD CVTILFSDIV GFTELCTTST PFEVVEMLND WYTCCDSIIS NYDVYKVETI GDAYMVVSGL PLQNGSRHAG EIASLALHLL ETVGNLKIRH KPTETVQLRI GVHSGPCAAG VVGQKMPRYC LFGDTVNTAS RMESTGDSMR IHISEATYQL LQVIGSYVCI ERGLTSIKGK GDMRTYWLTK RQQPELTPDL ISTVDTLDTY CSGPRESMEV SVHQYCSPAS NNYRLGSCNC DTKCLYSRRS DDNVTNSHGT SEFPKVSEPA QVNCNQLCVC RLNSSQMFNN RGPRSAPSIT FRL // ID CYGH_DROME STANDARD; PRT; 683 AA. AC Q07093; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Head-specific guanylate cyclase (EC 4.6.1.2). GN GYC-ALPHA-99B OR GYC-ALPHA-63A OR GYC OR DGC1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=93203896; PubMed=8095978; RA Yoshikawa S., Miyamoto I., Aruga J., Furuichi T., Okano H., RA Mikoshiba K.; RT "Isolation of a Drosophila gene encoding a head-specific guanylyl RT cyclase."; RL J. Neurochem. 60:1570-1573(1993). CC -!- FUNCTION: MAY HAVE A ROLE IN PHOTOTRANSDUCTION. A SECOND SUBUNIT CC MAY BE REQUIRED FOR ENZYME ACTIVITY. CC -!- CATALYTIC ACTIVITY: GTP = 3',5'-CYCLIC GMP + DIPHOSPHATE. CC -!- SUBUNIT: DIMER (PROBABLE). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- TISSUE SPECIFICITY: HEAD, WHERE IT IS PREFERENTIALLY EXPRESSED IN CC THE CNS AND THE RETINA. NOT FOUND IN BODIES. CC -!- SIMILARITY: BELONGS TO THE ADENYLYL CYCLASE CLASS-4/GUANYLYL CC CYCLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S57126; AAB25820.1; -. DR PIR; JH0810; JH0810. DR HSSP; P19687; 1AWN. DR FlyBase; FBgn0013972; Gyc-alpha-99B. DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IDA. DR GO; GO:0004383; F:guanylate cyclase activity; IDA. DR GO; GO:0007634; P:optokinetic behavior; IMP. DR GO; GO:0009586; P:rhodopsin mediated phototransduction; IMP. DR InterPro; IPR001054; G_cyclase. DR Pfam; PF00211; guanylate_cyc; 1. DR SMART; SM00044; CYCc; 1. DR PROSITE; PS00452; GUANYLATE_CYCLASES_1; FALSE_NEG. DR PROSITE; PS50125; GUANYLATE_CYCLASES_2; 1. KW Lyase; cGMP biosynthesis; Multigene family; Vision. FT DOMAIN 465 591 GUANYLATE CYCLASE. SQ SEQUENCE 683 AA; 75906 MW; 12D67C4B79A07C8D CRC64; MACPFFRRAD SLTRQPSVIA EPGGHWALED EELSDDALTL THLQMAIQLL TAPSNEDLNT AVTSLVAKYR QNWPNIHKLK LDPQTFKSCA NYDYLADIQE LLLKMDEASA SEILVLLGEE LITCCCTGII ERAFRCLGTD LQEFLGSLDG VYDVLKLQEE DVTDTGFVCA GEGELIFTSE RPVIAWLLLG SLKALTRMLY KVDVNIKIEP VERCPAVSLP LLAGQGQLPD HADGSSTSVS KTIPETVQRS NSSNASDLQM NSSSFCKMFP WHFIMNEQLE LVQLGRGFSK LYKPYMADFG CQATTYFDFK RPKGLTMKFR DIVRRTYTPF LIGLNNPPGA VDFPAIGLEI KGQMVHCPES NSLLFIGSPF LDGLDGLTCN GLFISDIPLH DATREVILVG EQARAQDGLR RRMDKIKNSI EEANSAVTKE RKKNVSLLHL IFPAEIAEKL WLGSSIDAKT YPDVTILFSD IVGFTSICSR ATPFMVISML EGLYKDFDEF CDFFDVYKVE TIGDAYCVAS GLHRASIYDA HRCLDGLKMI DACSKHITHD GEQIKMRIGL HTGTVLAGVV GRKMPRYCLF GHSVTIANKF ESGSEALKIN VSPTTKDWLT KHEGFEFELQ PRDPSFLPKE FPNPGGTETC YFLESFRNPA LDSELPLVEH INVSMKTISE GAMPRSPVAP IPP // ID CYPH_DROME STANDARD; PRT; 165 AA. AC P25007; Q9VXH8; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (PPIase) (Rotamase) DE (Cyclophilin) (Cyclosporin A-binding protein). GN CYP1 OR CYP-1 OR CG9916. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91199192; PubMed=1707759; RA Stamnes M.A., Sheih B.-H., Chuman L., Harris G.L., Zuker C.S.; RT "The cyclophilin homolog ninaA is a tissue-specific integral membrane RT protein required for the proper synthesis of a subset of Drosophila RT rhodopsins."; RL Cell 65:219-227(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 7-20. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- FUNCTION: PPIASES ACCELERATE THE FOLDING OF PROTEINS. IT CATALYZES CC THE CIS-TRANS ISOMERIZATION OF PROLINE IMIDIC PEPTIDE BONDS IN CC OLIGOPEPTIDES. CC -!- CATALYTIC ACTIVITY: PEPTIDYLPROLINE (OMEGA=180) = PEPTIDYLPROLINE CC (OMEGA=0). CC -!- ENZYME REGULATION: BINDS CYCLOSPORIN A (CSA). CSA MEDIATES SOME OF CC ITS EFFECTS VIA AN INHIBITORY ACTION ON PPIASE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE CYCLOPHILIN-TYPE PPIASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M62398; AAB03701.1; -. DR EMBL; AE003501; AAF48589.1; -. DR EMBL; BT009946; AAQ22415.1; -. DR PIR; B38388; B38388. DR HSSP; P05092; 2CPL. DR FlyBase; FBgn0004432; Cyp1. DR InterPro; IPR002130; CSA_PPIase. DR Pfam; PF00160; pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Cyclosporin; Isomerase; Rotamase; Multigene family. SQ SEQUENCE 165 AA; 17907 MW; FEB85148CA2EE7ED CRC64; MSTLPRVFFD MTADNEPLGR IVMELRSDVV PKTAENFRAL CTGEKGFGYK GSIFHRVIPN FMCQGGDFTN HNGTGGKSIY GNKFPDENFE LKHTGSGILS MANAGANTNG SQFFICTVKT AWLDNKHVVF GEVVEGLDVV KKIESYGSQS GKTSKKIIVA NSGSL // ID CYPR_DROME STANDARD; PRT; 237 AA. AC P15425; Q9VPV0; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Peptidyl-prolyl cis-trans isomerase, rhodopsin specific isozyme DE precursor (EC 5.2.1.8) (PPIase) (Rotamase). GN NINAA OR CG3966. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=89143766; PubMed=2493138; RA Shieh B.-H., Stamnes M.A., Seavello S., Harris G.L., Zuker C.S.; RT "The ninaA gene required for visual transduction in Drosophila RT encodes a homologue of cyclosporin A-binding protein."; RL Nature 338:67-70(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=89315802; PubMed=2664782; RA Schneuwly S., Shortridge R.D., Larrivee D.C., Ono T., Ozaki M., RA Pak W.L.; RT "Drosophila ninaA gene encodes an eye-specific cyclophilin RT (cyclosporine A binding protein)."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5390-5394(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TRANSMEMBRANE RP REGION. RX MEDLINE=91199192; PubMed=1707759; RA Stamnes M.A., Shieh B.-H., Chuman L., Harris G.L., Zuker C.S.; RT "The cyclophilin homolog ninaA is a tissue-specific integral membrane RT protein required for the proper synthesis of a subset of Drosophila RT rhodopsins."; RL Cell 65:219-227(1991). RN [5] RP MUTAGENESIS. RX MEDLINE=92355615; PubMed=1644830; RA Ondek B., Hardy R.W., Baker E.K., Stamnes M.A., Shieh B.-H., RA Zuker C.S.; RT "Genetic dissection of cyclophilin function. Saturation mutagenesis RT of the Drosophila cyclophilin homolog ninaA."; RL J. Biol. Chem. 267:16460-16466(1992). CC -!- FUNCTION: PPIASES ACCELERATE THE FOLDING OF PROTEINS. IT CATALYZES CC THE CIS-TRANS ISOMERIZATION OF PROLINE IMIDIC PEPTIDE BONDS IN CC OLIGOPEPTIDES. ACTS ON THE FOLDING OF RHODOPSIN RH1 AND RH2 (BUT CC NOT RH3) AND IS REQUIRED FOR VISUAL TRANSDUCTION. CC -!- CATALYTIC ACTIVITY: PEPTIDYLPROLINE (OMEGA=180) = PEPTIDYLPROLINE CC (OMEGA=0). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED SPECIFICALLY IN PHOTORECEPTOR CC CELLS. CC -!- SIMILARITY: BELONGS TO THE CYCLOPHILIN-TYPE PPIASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14769; CAA32877.1; -. DR EMBL; M22851; AAA28717.1; -. DR EMBL; AE003588; AAF51437.1; -. DR PIR; A33906; CYFFBE. DR HSSP; P23284; 1CYN. DR FlyBase; FBgn0002936; ninaA. DR GO; GO:0016023; C:cytoplasmic vesicle; IDA. DR GO; GO:0016022; C:endoplasmic reticulum cisterna; IDA. DR GO; GO:0016021; C:integral to membrane; IDA. DR GO; GO:0005624; C:membrane fraction; IDA. DR GO; GO:0016018; F:cyclosporin A binding; IMP. DR GO; GO:0007602; P:phototransduction; IPI. DR GO; GO:0016063; P:rhodopsin biosynthesis; IMP. DR InterPro; IPR002130; CSA_PPIase. DR Pfam; PF00160; pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Isomerase; Rotamase; Vision; Transmembrane; Glycoprotein; Signal; KW Multigene family. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 237 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, FT RHODOPSIN SPECIFIC ISOZYME. FT TRANSMEM 205 225 POTENTIAL. FT CARBOHYD 68 68 N-LINKED (GLCNAC...). SQ SEQUENCE 237 AA; 26351 MW; 1BF3CD01C31119B4 CRC64; MKSLLNRIIL CSAFLAVASG LSFTVTSRIY MDVKHNKKPV GRITFGLFGK LAPKTVANFR HICLRGINGT SYVGSRFHRV VDRFLVQGGD IVNGDGTGSI SIYGDYFPDE DKALAVEHNR PGYLGMANRG PDTNGCQFYV TTVGAKWLDG KHTVFGKVLE GMDTIYAIED VKTDTDDFPV EPVVISNCGE IPTEQFEFYP DDFNILGWIK AAGLPVTSSF CVLLIFHYFF RQLNMYC // ID CYTL_DROME STANDARD; PRT; 126 AA. AC P23779; Q8SZN3; Q9VFI2; DT 01-NOV-1991 (Rel. 20, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cystatin-like protein. GN CYS OR BCDNA:RH72992 OR CG8050. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91071416; PubMed=1701398; RA Delbridge M.L., Kelly L.E.; RT "Sequence analysis, and chromosomal localization of a gene encoding a RT cystatin-like protein from Drosophila melanogaster."; RL FEBS Lett. 274:141-145(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE CYSTATIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55178; CAA38963.1; ALT_INIT. DR EMBL; AE003705; AAF55073.2; -. DR EMBL; AY113633; AAM29638.1; -. DR EMBL; AY070635; AAL48106.1; -. DR PIR; S12913; S12913. DR FlyBase; FBgn0004629; Cys. DR InterPro; IPR000010; Cystatin. DR InterPro; IPR003244; Sarcocystatin. DR Pfam; PF00031; cystatin; 1. DR ProDom; PD031531; Sarcocystatin; 1. DR SMART; SM00043; CY; 1. DR PROSITE; PS00287; CYSTATIN; 1. KW Thiol protease inhibitor. FT ACT_SITE 29 29 REACTIVE SITE (BY SIMILARITY). FT SITE 72 76 SECONDARY AREA OF CONTACT FT (BY SIMILARITY). FT DISULFID 94 115 BY SIMILARITY. FT CONFLICT 37 37 N -> D (IN REF. 1). FT CONFLICT 59 59 P -> H (IN REF. 4; AAL48106). SQ SEQUENCE 126 AA; 13437 MW; 144FA7C42E9B9A73 CRC64; MNVVKSLCIL GLVLVSLIAT QAADEQVVGG VSQLEGNSRK EALELLDATL AQLATGDGPS YKAINVTSVT GQVVAGSLNT YEVELDNGSD KKQCTVKIWT QPWLKENGTN IKIKCSGDDG ELDRTW // ID DAB_DROME STANDARD; PRT; 2411 AA. AC P98081; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Disabled protein. GN DAB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RX MEDLINE=93194063; PubMed=7680635; RA Gertler F.B., Hill K.K., Clark M.J., Hoffmann F.M.; RT "Dosage-sensitive modifiers of Drosophila abl tyrosine kinase RT function: prospero, a regulator of axonal outgrowth, and disabled, a RT novel tyrosine kinase substrate."; RL Genes Dev. 7:441-453(1993). CC -!- FUNCTION: TOGETHER WITH ABL INVOLVED IN EMBRYONIC NEURAL CC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P98081-1; Sequence=Displayed; CC Name=Short; CC IsoId=P98081-2; Sequence=VSP_004185; CC -!- TISSUE SPECIFICITY: CNS AXONS AND BODY WALL MUSCLES. CC -!- DEVELOPMENTAL STAGE: EMBRYONIC AXONOGENESIS. CC -!- PTM: PROBABLY PHOSPHORYLATED BY THE ABL TYROSINE KINASE. CC -!- SIMILARITY: CONTAINS 1 PID DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08845; AAB08527.1; ALT_SEQ. DR PIR; A46299; A46299. DR FlyBase; FBgn0000414; Dab. DR GO; GO:0005737; C:cytoplasm; IDA. DR InterPro; IPR006020; PTB_PID. DR Pfam; PF00640; PID; 1. DR SMART; SM00462; PTB; 1. DR PROSITE; PS01179; PID; 1. KW Alternative splicing; Phosphorylation; Repeat. FT DOMAIN 46 196 PID. FT DOMAIN 1689 1801 REPEAT-RICH REGION. FT REPEAT 1689 1700 ALTERNATE ARG AND ACIDIC RESIDUE. FT REPEAT 1740 1750 ALTERNATE ARG AND ACIDIC RESIDUE. FT REPEAT 1791 1801 ALTERNATE ARG AND ACIDIC RESIDUE. FT MOD_RES 111 111 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 482 482 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 1662 1662 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 1667 1667 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 1701 1701 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 1704 1704 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 1713 1713 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 1739 1739 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 1826 1826 PHOSPHORYLATION (BY ABL) (PROBABLE). FT MOD_RES 1961 1961 PHOSPHORYLATION (BY ABL) (PROBABLE). FT VARSPLIC 462 673 Missing (in isoform Short). FT /FTId=VSP_004185. SQ SEQUENCE 2411 AA; 264046 MW; 579AB9C0243D5FD6 CRC64; MVKSLVAKLS TASSNLSLAS TFGGGSGAAE ETNYAKHRND PGRFFGDGVQ FKAKLIGILE VARPEVIGCA RRRCKISKWH PGGWRAQAAI TIHVTIDGLR LRDEKTGDSL YHHPVHKISF IAQDMTDSRA FGYIFGSPDS GHRFFGIKTD KAASQVVLAM RDLFQVVFEL KKKEIEMARQ QIQGKSLHDH SSQLASLSSL KSSGLGGMGL GHSDLASGGI SSGHALTLLG SSLSTTNGTS RLGVSLDVAK ASGSAAKEVS PESVADLVDL EQELTSLQRG ISQMERITPN EPTTSSTGGA GHPSLAKSAS EDDPFGDSFI YVPSYSILPP PPDSGRNRHK PPNKTPDAVT SLDAMLSPPP GTSSSHGSAS AGLQAADNDD DNWLQELDQQ NDVFDTSKVV SSSGLGSVLA MAPLASSEST ATPTQQLTEV AAGSGPLADL DIGLSTALGN EEQTSTILSL DAFTDLDPLG TGRTRPYVDK KYFFQELKNP PKKLLKELSS GSQAGLGLGL SLGQLDGLFP EDSTTISTTT TTATNITAVL TNRYSNTIIA QRKKSLTTEM HILYYDKRVV HHFWRNFFSV QLEIALSKQL SKVCTCTAGN PQQNSANTLT STASTAASLG QLLSTVALNP DPLPAPISIP TSISHSITPS AELKLLLGHV TNPPNPTGHY YTTEPPTLTS LENPHPPADP VLLPRDTDPF SPTRKKSDPD PFQESDLFAK LDAFEFEAPR GSSSLDSKFG HGDKSECIQW TTSGAIATRE GVAASAASEY GEEPSHSICF RTSKWRSLDV ISSISNKKMP HLFGQADHLA NLGSDIGSSV NMRRLQESDS LSETEAAPEP PPRQTRLRTS EPRPCHPRSS SAIWSSDLHL QIPTQPPTSG RYEYLNSNVT ARRTASSVDA PPIPLPSRRV GRSDGCFPGP GRPRKPGHTE DDYLAPLGAP PPSWPPPSQG SSARVETSTA GFARQAADIY ENKAEDSAGS STGAGQAPEV APSSNTLAPD ITLTQLLTLG MDDLAIKLNV PASKLSTMTL VQLTAYLSEY LSSEKSQVHS QERRSSPANT APAPASTAAV FKVNFDQQTS FVAKFDDTFG EDEPVMPSGS SDSTFVANFA NFNDAPTPMP TVSPVVATVP SADRYAVFRE IIDQELQQQQ QETDLMGDLT PPPVDETQAK EISEGLEVNN VGADVPIDAL DVKPAPKIDT KITEVVAQAK DRYAARGDII LVENLFDKPA IATDTQPEKE KDLLQDFPEF SDEFNEDHDL RQIMDHQNVQ THARDRHGLV DSRGFPTEPS SSALTVGDDD EDEDADAGGE SSLDSNEKDA EPVSGQDQYE KLSTSTQQLD AAAPALEDVQ QQQQQQSLPP KQDQKFLSIL TAPGGGTKDD IEIDELMHRA ISNLSLDSRD RVSPATSSAA PSRGAPGLHT PSQFNDVSTS PIPLQKPGMG PSPVPSQLSA VSQLIDTATK QMMGDKDREK QSWATFDSPK AKGKARLTLP PPPPPASNTS QPDTENRLAV RIPGMTAGQS NSVVGRRRSA TTSSSSRDLS PWDDETPEYL KRRQLAAAQM AHPHQPPMQA PPQHTDRHGY YMRHARRMNS CDEDYDYDGE FVARRDQPQH QQQQRKFKHG LSRSRDNFEL ESPSWYHHPA HHTWSPQEIE QARVRSFDRT AYERSSYGPP PPIYDKRGQL RGKYRGDHRD RERERDRDRE YRDYARPSYD FDYENVYEER GGRSPLAYKP GRGGGDYLYD RERDRDRERD PKSFDRESLE SYESATRRRR SFGSGNDVYG SLDSRDDYRG DRERDRERDR EQMKTRSLRK PTTTSGKLRI SGDIDYEQDS EQDFQQRSGV RSLQLPNQLG GDVVLPSNAV AGPQRFAKSS GSVPGRRGTP CLVRNLGSVQ PALLKPKGDW LRVPERWLWV KLPPMEKKNE DSARKPEPAV PRLSPVGAPS ASTSAPSRSS YGRGIRDNYD YICPGQRNDD DDDDDEDYVD DEPPTDEDKF ERLNRRRHEM HQRMLESERR QMERHQPPSL AKLPGQNRTR GVVVNSDYGF VDSYEQTPTP TPRSNASSTG PGGLMMSGGE SSAGVTSSKF NFDDGFESDF NQSSPPAPAG TASSCNSTPA GPVSANANNG GSKSLFRFSN DFSDREKREQ FEMETPPTST PPITQKLRFD DNVKVSQFDD AAFEDDFAKA SFDFEKEQAG SATAGAGGSG AMSRKQNMRT SKLQQRQELI KKSESVNIFA KKQEDPFEDD EFFKSPDQEQ AMDQHNDDTE GGKFQWSEDR TLQSSMKTCD LTNCLPRHRG SDRIRTSIHT MRDRCVNDTT FILPSQSLLS AAATAQPATE LESPCLLQLA SPAVAGASES ADEEIHRHIY KSLHEPKVKS KPLQQLLRKP KKWKLKCTLD DFLKCLIIAS SEHVYDYDVL W // ID DALY_DROME STANDARD; PRT; 626 AA. AC Q24114; Q9VSQ8; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Division abnormally delayed protein precursor (Dally protein). GN DALLY OR CG4974. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96102814; PubMed=8582281; RA Nakato H., Futch T.A., Selleck S.B.; RT "The division abnormally delayed (dally) gene: a putative integral RT membrane proteoglycan required for cell division patterning during RT postembryonic development of the nervous system in Drosophila."; RL Development 121:3687-3702(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CELL SURFACE PROTEOGLYCAN THAT BEARS HEPARAN SULFATE. CC REQUIRED FOR CELL DIVISION PATTERNING DURING POST-EMBRYONIC CC DEVELOPMENT OF THE NERVOUS SYSTEM. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE GLYPICAN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U31985; AAA97401.1; -. DR EMBL; AE003554; AAF50358.1; -. DR FlyBase; FBgn0011577; dally. DR GO; GO:0008052; P:sensory organ determination; IMP. DR InterPro; IPR001863; Glypican. DR Pfam; PF01153; Glypican; 1. DR PROSITE; PS01207; GLYPICAN; FALSE_NEG. KW Proteoglycan; Heparan sulfate; Glycoprotein; Signal; GPI-anchor. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 ? DIVISION ABNORMALLY DELAYED PROTEIN. FT PROPEP ? 626 REMOVED IN MATURE FORM (POTENTIAL). FT CARBOHYD 101 101 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 150 150 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 187 187 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 549 549 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 569 569 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 573 573 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 601 601 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). SQ SEQUENCE 626 AA; 69031 MW; 1182AD8A0D0E4DD3 CRC64; MAARSVRLAQ LLLFTLLCGF VGLSAAKHLD LDGIHHHQHH LHSATTHHRR RLQRDSRAKD AVGGSTHQCD AVKSYFESID IKSSGTYSEK GAICGGNCCN NATELELRDK AAGMFEQLLH HHTSSLRGVL ETNAKQFQSH VLELAQISEN MTHSLFSKVY TRMVPSSRMM IHQLYTEIMN HLIYTSNYTN SNGQLGRRGI GSVQSNLEEA VRHFFVQLFP VAYHQMVHLS KNNLGDLHED YVNCLQHNFD EMHPFGDIPQ QVQSNLGKSV HMSNVFMNAL LQAAEVLSEA DALYGEQLTD TCKLHLLKMH YCPNCNGHHS SSRSETKLCY GYCKNVMRGC SAEYAGLLDS PWSGVVDSLN NLVTTHILSD TGIINVIKHL QTYFSEAIMA AMHNGPELEK KVKKTCGTPS LTPYSSGEPD ARPPPHKNNV KWATDPDPGM VLFLSTIDKS KEFYTTIVDN FCDEQQHSRD DHSCWSGDRF GDYTQLLINP GTDSQRYNPE VPFNAKAQTG KLNELVDKLF KIRKSIGAAA PSNSIQATHD IQNDMGEGSG GGEGQIGDDE EEYGGAHGSG DGSGDGPHTP IEESEGTTTN EVESRDSGKT SGSNPLEGTA TWMLLTLVTM LFSSCS // ID DA_DROME STANDARD; PRT; 710 AA. AC P11420; Q9VKX3; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Daughterless protein. GN DA OR CG5102. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89077534; PubMed=3203380; RA Caudy M., Vaessin H., Brand M., Tuma R., Jan L.Y., Jan Y.N.; RT "Daughterless, a Drosophila gene essential for both neurogenesis and RT sex determination, has sequence similarities to myc and the RT achaete-scute complex."; RL Cell 55:1061-1067(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=89108000; PubMed=2850968; RA Cronmiller C., Schedl P., Cline T.W.; RT "Molecular characterization of daughterless, a Drosophila sex RT determination gene with multiple roles in development."; RL Genes Dev. 2:1666-1676(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: DAUGHTERLESS/ACHAETE-SCUTE COMPLEX HETERODIMERS ACT AS CC TRANSCRIPTIONAL ACTIVATORS OF NEURAL CELL FATES AND ARE INVOLVED CC IN SEX DETERMINATION. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. INTERACTS WITH AMOS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: UBIQUITOUS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03148; AAA28442.1; -. DR EMBL; Y00221; CAA68368.1; -. DR EMBL; AE003628; AAF52934.2; -. DR PIR; S06891; A31641. DR TRANSFAC; T01034; -. DR FlyBase; FBgn0000413; da. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0007422; P:peripheral nervous system development; NAS. DR GO; GO:0045464; P:R8 cell fate specification; NAS. DR GO; GO:0007530; P:sex determination; NAS. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Neurogenesis; Differentiation; Developmental protein; Nuclear protein; KW Transcription regulation; Activator; DNA-binding; Repeat. FT REPEAT 198 226 HIS-RICH. FT REPEAT 227 256 HIS-RICH. FT DNA_BIND 554 566 BASIC DOMAIN. FT DOMAIN 567 608 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 609 632 CLASS A SPECIFIC DOMAIN. SQ SEQUENCE 710 AA; 73864 MW; C69163BD3F46FEA5 CRC64; MATSDDEPMH LYEVFQNCFN KIANKQPTGT VGADRGGGGG YHSPYGSLGV ENGMYPSDFN SMHDTVNGGN NRYANASTVD QYFDSAAAGS GGAWCQPQMS SANSYMGQSA YQNSGPLSGH SIDQQQQQVH QADGLGMGGG GGGGVGADGM HCPVTTGLPP ISSFRPTSGG IGGPGAGQQA PVNVNVNPPA VFNSPQAHNH NHTVQAQHSA LSTAGPLGHH SLNHTPHAHS HTLPLPHALP HGHTLPHPHH SQQNSPAVQS SDAFSGAGAS VKVAGAGNSS AAALRQQMYM PADQSISSFG SNPSTPVNSP PPLTQSVVGG GGEPSVSGGS GWGHSVLNGG PSSSYASEMV PVSSLHTMAS VFQGVRMEER LDDALNVLRN HCEPEMLAGV NQSLASIDNI DALTSFVPNS PSHLGSGGNS GSVSNTSNAA LVHEVLALGA AAAAGTSGQS VGGAGSLASL KLDRSASTSL PKQTKKRKEH TAISNSVPAG VSTTSSLTSL DISDTKPTSS IESSNSGLQQ HSQGKGTKRP RRYCSSADED DDAEPAVKAI REKERRQANN ARERIRIRDI NEALKELGRM CMTHLKSDKP QTKLGILNMA VEVIMTLEQQ VRERNLNPKA ACLKRREEEK AEDGPKLSAQ HHMIPQPQQV GGTPGSSYHS QPAQLVPPSS QTISTMTISL PVNQANNGLP PHLQQQQQQQ SQLGHAQLPQ // ID DB45_DROME STANDARD; PRT; 521 AA. AC Q07886; Q9V528; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable ATP-dependent RNA helicase Dbp45A (DEAD-box protein 45A). GN DBP45A OR CG12759. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94032476; PubMed=7692973; RA Lavoie C.A., Harvey M., Lasko P.F.; RT "Dbp45A encodes a Drosophila DEAD box protein with similarity to a RT putative yeast helicase involved in ribosome assembly."; RL Biochim. Biophys. Acta 1216:140-144(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLE ATP-BINDING RNA HELICASE. CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13612; AAA16339.1; -. DR EMBL; Z23266; CAA80804.1; -. DR EMBL; AE003834; AAF58994.1; -. DR EMBL; AY058728; AAL13957.1; -. DR PIR; S38329; S38329. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0010220; Dbp45A. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. KW ATP-binding; RNA-binding; Helicase. FT NP_BIND 51 58 ATP (POTENTIAL). FT SITE 157 160 DEAD BOX. FT CONFLICT 161 161 R -> P (IN REF. 1). FT CONFLICT 211 217 SQDSDVA -> CEASAVR (IN REF. 1). FT CONFLICT 224 225 QR -> HG (IN REF. 1). FT CONFLICT 228 229 LC -> VS (IN REF. 1). FT CONFLICT 234 234 R -> P (IN REF. 1). FT CONFLICT 327 327 M -> I (IN REF. 1). FT CONFLICT 407 407 D -> C (IN REF. 1). FT CONFLICT 456 456 P -> S (IN REF. 1). FT CONFLICT 493 493 D -> Y (IN REF. 1). FT CONFLICT 517 521 KKDKA -> NKSKGKIKRDV (IN REF. 1). SQ SEQUENCE 521 AA; 59677 MW; 89C68C43CD947913 CRC64; MQRKEANPFQ ILGLRPWLVK QLTKLGLKGA TPIQQKCIPA ILAGQDCIGA AKTGSGKTFA FALPILERLS EEPVSHFALV LTPTHELAYQ ISEQFLVAGQ AMGVRVCVVS GGTDQMVESQ KLMQRPHIVV AMPGRLADHL TGCDTFSFDN LKYLVVDEAD RMLNGDFDES LSIIERCLPK TRQNLFFSAT MKDFIKESSI FPIASDCFEW SQDSDVATVE TLDQRYLLCA DYDRDMVLIE ALRKYREENE NANVMIFTNT KKYCQLLSMT LKNMEIDNVC LHGFMRQKER VAALSRFKSN QIRTLIATDV AARGLDIPSV ELVMNHMLPR TPKEYIHRVG RTARAGRKGM SISIFRFPRD LELLAAIEEE INTKLTEHPI DQRMVERIFM QVNVTRRESE MQLDNNDFDE RAQNYRRKTW IMEGKDPDQM EALYRKKQKD KLREIRRKRK LQHAEPAASE EGKALLQDER FKSVDSARFE KKGKGRSRAT QEDTPTKPLK RLNKEKPVAQ KGRADVKKDK A // ID DB73_DROME STANDARD; PRT; 687 AA. AC P26802; Q9XZ18; DT 01-AUG-1992 (Rel. 23, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable ATP-dependent RNA helicase Dbp73D (DEAD-box protein 73D). GN DBP73D OR CG9680. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92319633; PubMed=1620603; RA Patterson L.F., Harvey M., Lasko P.F.; RT "Dbp73D, a Drosophila gene expressed in ovary, encodes a novel RT D-E-A-D box protein."; RL Nucleic Acids Res. 20:3063-3067(1992). RN [2] RP REVISIONS. RA Lasko P.F.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RA Rubin G.M., Wan K.H., Harvey D., Lewis S.E., Brokstein P., Tsang G., RA Agbayani A., Arcaina T.T., Baxter E., Blazej R.G., Butenhoff C., RA Champe M., Chavez C., Chew M., Doyle C.M., Farfan D.E., Frise E., RA Galle R., George R.A., Harris N.L., Hoskins R.A., Evans-Holm M., RA Houston K.A., Hummasti S.R., Kim E., Li P., Moshrefi M., Pacleb J.M., RA Park S., Sequeira A., Sethi H., Snir E., Svirskas R.R., Weinburg T., RA Celniker S.E.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE GERM LINE TISSUE OF THE CC OVARY. CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74824; AAC14192.1; -. DR EMBL; AF132173; AAD34761.1; -. DR EMBL; AE003526; AAF49419.1; -. DR EMBL; BT010045; AAQ22514.1; -. DR PIR; S28762; S28762. DR FlyBase; FBgn0004556; Dbp73D. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. KW ATP-binding; RNA-binding; Helicase; Nuclear protein. FT NP_BIND 190 197 ATP (BY SIMILARITY). FT SITE 305 308 DEAD BOX. FT CONFLICT 55 55 L -> P (IN REF. 1). FT CONFLICT 86 86 D -> V (IN REF. 1). FT CONFLICT 594 595 AG -> PR (IN REF. 1). FT CONFLICT 617 687 KALIHKKQEETATVRPLTLMEKLQIKANEIVQSSKKSSETK FT NSKTKADKTKYQPKETKKQIIAKQLKAIEN -> QGIDPQE FT TGGNGHSSSTDVDGKVANQSE (IN REF. 1). SQ SEQUENCE 687 AA; 77590 MW; 252D39D8BB948639 CRC64; MELFTVNRYT EDLKEQKDGA QGTNNEDEIL QKLLKKAAKR KRKHEAIEVV ETPILEKETS DVKESESKEE QVEEPEKPLE VVQEEDVPSN EFQVLGGDDS AAKKKKVQMQ LPNWLAHPTI IEGGSLQPEE EVPASEAIDQ LDYLEKYTCQ ALKQMKIKRL FPVQKQVIPW ILEAHAKPPP FRPRDICVSA PTGSGKTLAF AIPIVQLLSQ RVDCKVRALV VLPVAELALQ VYRVISELCS KTELEVCLLS KQHKLEDEQE KLVEQYKGKY YSKADIVVTT PGRLVDHLHA TKGFCLKSLK FLVIDEADRI MDAVFQNWLY HLDSHVKETT DQLLAGTQAP LCYAELQASF GKQPHKLLFS ATLSQDPEKL QDLRLFQPRL FATVLTMPVL KDATEEGADT EALTDPGQFV GRYTTPAELT EQYCVTELRL KPLTVFALVE KYKWKRFLCF TNSSDQATRL TFVLKVLFQK YSTKVSELSG NLSAKVRNER LRDFAAGKIN GLICSDALAR GIDVADVDVV LSYETPRHIT TYIHRVGRTA RAGRKGTAVT VLTEQDMTLF KKILSDANKG LGEEIHVSPD IEIQHAVEYK EALAGLRSEK VKNKNQKMAE KNRVATKALI HKKQEETATV RPLTLMEKLQ IKANEIVQSS KKSSETKNSK TKADKTKYQP KETKKQIIAK QLKAIEN // ID DB80_DROME STANDARD; PRT; 460 AA. AC O61305; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE DEAD-box helicase Dbp80. GN DBP80 OR HEL80 OR HEL40. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98234298; PubMed=9565667; RA Eisen A., Sattah M., Gazitt T., Neal K., Szauter P., Lucchesi J.; RT "A novel DEAD-box RNA helicase exhibits high sequence conservation RT from yeast to humans."; RL Biochim. Biophys. Acta 1397:131-136(1998). CC -!- FUNCTION: ATP-DEPENDENT RNA HELICASE INVOLVED IN MRNA EXPORT FROM CC THE NUCLEUS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR PORE COMPLEX CC CYTOPLASMIC FIBRILS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. DBP5/DDX19 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF005239; AAC23709.1; -. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0024804; Dbp80. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; FALSE_NEG. KW Helicase; ATP-binding; RNA-binding; Nuclear protein. FT NP_BIND 119 126 ATP (BY SIMILARITY). FT SITE 223 226 DEAD BOX. SQ SEQUENCE 460 AA; 51315 MW; 380DE3A9A0100AB4 CRC64; MGDWAKKSED QEVSKLVDKL NLDSKSGEET DFDVADPAET SLLIKILGKG LVNTKLSLDL QQKNPNSPLH SVKTFEALHL KASLLKGIYA MGFNTPSKIQ ETALPTLLAD PPQNMIAQSQ SGTGKTAAFV LAMLSRVNVC LNHPQVLCLS PTYELAIQTG EVAARMGQFC REIKLRFAVR GEEVDRSKKI EEHILIGTPG KLLDWGIKFR LFDMKKISVF VLDEADVMIA TQGHHDQCIR IHKMLNPHCQ MLFFSATYGK EVMDFARLIV ADPTIIRLMR EEESLENIKQ YYVKCKNEEG KYNAIQNIYG CISVGQAIIF CHTKRTAAWL AAKMTSDGHS VAVLTGDLTV VQRLDVLDRF RSGLEKVLIT TNILSRGIDI EQLQVVVNFD LPVDLDGMAD CETYLHRIGR TGRFGKSGIA INLITDEKTM KVCSDIEKHF NKKIEVLNTD SADDIEKIGT // ID DC11_DROME STANDARD; PRT; 1208 AA. AC P18169; Q8IRP1; DT 01-NOV-1990 (Rel. 16, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Defective chorion-1 protein, FC125 isoform precursor. GN DEC-1 OR CG2175. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=91032553; PubMed=1699826; RA Waring G.L., Hawley R.J., Schoenfeld T.; RT "Multiple proteins are produced from the dec-1 eggshell gene in RT Drosophila by alternative RNA splicing and proteolytic cleavage RT events."; RL Dev. Biol. 142:1-12(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX MEDLINE=88243015; PubMed=3378704; RA Hawley R.J., Waring G.L.; RT "Cloning and analysis of the dec-1 female-sterile locus, a gene RT required for proper assembly of the Drosophila eggshell."; RL Genes Dev. 2:341-349(1988). CC -!- FUNCTION: REQUIRED FOR PROPER ASSEMBLY OF THE EGGSHELL. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=FC125; CC IsoId=P18169-1; Sequence=Displayed; CC Name=FC106; CC IsoId=P18170-1; Sequence=External; CC Name=FC177; CC IsoId=P18171-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: EXPRESSION PEAKS AT EMBRYONIC STAGE 10A, IS CC SLIGHTLY REDUCED BY STAGE 10B, AND UNDETECTED IN STAGE 11. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M35887; AAA28446.1; -. DR EMBL; AE003442; AAN09215.1; -. DR PIR; A44766; A44766. DR FlyBase; FBgn0000427; dec-1. DR GO; GO:0042600; C:chorion; IDA. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0005213; F:structural constituent of chorion (sensu In...; IMP. DR GO; GO:0007306; P:insect chorion formation; IMP. DR InterPro; IPR006720; DEC-1_C. DR InterPro; IPR006719; DEC-1_N. DR InterPro; IPR006718; DEC-1_REPEAT. DR Pfam; PF04626; DEC-1_C; 1. DR Pfam; PF04625; DEC-1_N; 1. DR Pfam; PF04624; DEC-1_REPEAT; 12. KW Chorion; Eggshell; Repeat; Alternative splicing; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 1208 DEFECTIVE CHORION-1 PROTEIN, FC125 FT ISOFORM. FT DOMAIN 493 788 12 X 26 AA APPROXIMATE TANDEM REPEATS, FT GLU, MET-RICH. FT REPEAT 493 518 1. FT REPEAT 519 544 2. FT REPEAT 545 570 3. FT REPEAT 571 596 4. FT REPEAT 597 622 5. FT REPEAT 623 652 6 (APPROXIMATE). FT REPEAT 653 680 7 (APPROXIMATE). FT REPEAT 681 696 8 (APPROXIMATE). FT REPEAT 697 720 9 (APPROXIMATE). FT REPEAT 721 733 10 (APPROXIMATE). FT REPEAT 734 758 11 (APPROXIMATE). FT REPEAT 759 788 12 (APPROXIMATE). FT CONFLICT 17 17 A -> V (IN REF. 1). FT CONFLICT 219 219 Q -> E (IN REF. 1). FT CONFLICT 347 347 D -> H (IN REF. 1). FT CONFLICT 382 382 A -> T (IN REF. 1). FT CONFLICT 847 877 PENEGTARHKVDALGVGGNKRKKSKSKSAPP -> AGERRH FT RQAQSRCPGSWRQQAQEVQVQVGAA (IN REF. 1). FT CONFLICT 888 901 QRPVVQSYGTSYGG -> SVRWFRVTEQATAE (IN REF. FT 1). SQ SEQUENCE 1208 AA; 137444 MW; 2D8D140756FFFDEE CRC64; MRLFSLLPLL ALLVVQAAGQ SEVTSDDPAT DAGSTTNSTT DTKPRIPSQD EILGQMPSIN PIRTGNPQMD AFYMMFPALG SLLKWGSLFP AYSILGAIPD NLQPTAAASK VVLVLADDAT AKTRVARQNP PPNPLGQLMN WPALPQDFQL PSMDLGPQVG SFLAQLPAMP TVPGLLGAAA PVPAPAPAPA AAPPPAPAPA ADPPAAPVPD APQPAILGQA ALQNAFTFFN PANFDASSLL GQSVPTFAPP NLDFVAQMQR QFFPGMTPAQ PAAAGTDAQA SDISEVRVRP EDPYSQEAQM KIKSALEMEQ ERQQQAQVKD QEQVPLLWFR MPTTQNQDAT EEKTLEDLRV EAKLRAFERQ VIAELRMLQK IELMAKQMRS SAAAQNGDSP YRISYPLSRT PIHKITRADI EQALRDDYVR RLVNKEAQRR ARNSGINTQK ANALKRQAKS QDQTLSKEDI VQIMAYAYRM ANEQMESEKG KQDKVYAAYR TEQNPMMMQQ RQWSEEQAKI QQNQQQIQQN PMMMQQRQWS EEQAKIQQNQ QQIQQNPMMM QQRQWSEEQA KIQQNQQQIQ QNPMMMQQRQ WSEEQAKIQQ NQQQIQQNPM MVQQRQWSEE QAKIQQNQQQ IQQNPMMMQQ RQWSEEQAKI QHDQQMAQQM AQQGLMMTEQ RQRQWSEDQA KIQQAQQMAQ QTPMMMPQMQ QRQWTEDPQM VQQMQQRQWA EDQTRMQMAQ QNPMMQQQRQ MAENPQMMQQ RQWSEEQTKI EQAQQMAQQN QMMMQQMQQR QWSEDQAQIQ QQQRQMMQQT PMMMKERQWA EENPQSVQQQ GPMMMQQQMP SMMQREVEDE DNKAEDDLVG EAGPQMPENE GTARHKVDAL GVGGNKRKKS KSKSAPPTVI NYYYAAPQRP VVQSYGTSYG GGGYGSNAYG VPRPVNSYQS QGYRAAVGND EVDEMLRQHQ TMARTINPKQ PGEVGGSESQ KSNSNPPTTL TPAPQEQPQE HRVHKSPSSA PSETEIENAP SSDPQVGSIF TYGEGLLHPF MGLLPVERPD DPWNQKPYDP HHPLYTGGGS YDAYLRDGRH RRDTHIMGQG TQHGILTPGM LERLLRIKMD FQRRFPHLYK GMLNHHTNLT RVEVQPPVLG KISKPKTKTK PKNEDEPVFE LGAAERSLFE DETNDSLEKD PEPEPDEEDD RDVEEPSESS EPRGFSSKKS RDENDIDYFN FDDDDVDD // ID DC12_DROME STANDARD; PRT; 950 AA. AC P18170; P92153; P92154; Q24299; Q26309; Q26310; Q26311; Q8IRP0; DT 01-NOV-1990 (Rel. 16, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Defective chorion-1 protein, F106 isoform precursor. GN DEC-1 OR CG2175. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SEQUENCE OF 279-299, AND ALTERNATIVE SPLICING. RX MEDLINE=91032553; PubMed=1699826; RA Waring G.L., Hawley R.J., Schoenfeld T.; RT "Multiple proteins are produced from the dec-1 eggshell gene in RT Drosophila by alternative RNA splicing and proteolytic cleavage RT events."; RL Dev. Biol. 142:1-12(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 1-369 AND 425-596 FROM N.A. RC STRAIN=Samarkand; RX MEDLINE=92130257; PubMed=1774787; RA Andersson S., Lambertsson A.; RT "Evolution of the dec-1 eggshell locus in Drosophila. I. Restriction RT site mapping and limited sequence comparison in the melanogaster RT species subgroup."; RL J. Mol. Evol. 33:321-331(1991). RN [5] RP SEQUENCE OF 493-698 FROM N.A. (ALLELES FC1; FC2; FC3 AND FC4). RC STRAIN=Samarkand, Israel, Ghanghry, Shahrinau, and Dilizhan; RX MEDLINE=93353525; PubMed=8350348; RA Andersson S., Lambertsson A.; RT "Evolution of the dec-1 eggshell locus in Drosophila. II. RT Intraspecific DNA sequence analysis reveals length mutations in a RT repetitive region in D. melanogaster."; RL J. Mol. Evol. 36:536-544(1993). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX MEDLINE=88243015; PubMed=3378704; RA Hawley R.J., Waring G.L.; RT "Cloning and analysis of the dec-1 female-sterile locus, a gene RT required for proper assembly of the Drosophila eggshell."; RL Genes Dev. 2:341-349(1988). CC -!- FUNCTION: REQUIRED FOR PROPER ASSEMBLY OF THE EGGSHELL. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=FC106; CC IsoId=P18170-1; Sequence=Displayed; CC Name=FC125; CC IsoId=P18169-1; Sequence=External; CC Name=FC177; CC IsoId=P18171-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: SYNTHESIZED IN EARLY STAGE 10 EGG CHAMBERS. CC CLEAVAGE GENERATES S80, A 80 KDA SPECIES, DURING LATE STAGE 10 CC WHICH IS INCORPORATED INTO THE EGGSHELL. DURING THE LATTER STAGES CC OF CHORION FORMATION, S80 IS PROCESSED TO A 60 KDA COMPONENT, S60. CC -!- PTM: PROTEOLYTIC CLEAVAGE OF ISOFORM FC106 GENERATES 2 FURTHER CC PRODUCTS, S80 AND S60. CC -!- MISCELLANEOUS: ALLELE FC1 IS FOUND ONLY IN STRAIN SAMARKAND, CC ALLELE FC3 ONLY IN STRAIN SHAHRINAU AND FC4 ONLY IN STRAIN CC DILIZHAN. ALLELE FC2 IS FOUND IN BOTH STRAINS ISRAEL AND GHANGHRY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITIONS 1097 AND 1205. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M35888; AAA28447.1; ALT_FRAME. DR EMBL; AE003442; AAN09216.1; -. DR EMBL; X76230; CAA53815.1; -. DR EMBL; X76231; CAA53816.1; -. DR EMBL; S64529; AAB27801.2; -. DR EMBL; S64530; AAB27802.2; -. DR EMBL; S64531; AAB27803.2; -. DR EMBL; S64532; AAB27804.2; -. DR EMBL; S64534; AAB27805.2; -. DR PIR; B44766; B44766. DR FlyBase; FBgn0000427; dec-1. DR GO; GO:0042600; C:chorion; IDA. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0005213; F:structural constituent of chorion (sensu In...; IMP. DR GO; GO:0007306; P:insect chorion formation; IMP. DR InterPro; IPR006720; DEC-1_C. DR InterPro; IPR006719; DEC-1_N. DR InterPro; IPR006718; DEC-1_REPEAT. DR Pfam; PF04626; DEC-1_C; 1. DR Pfam; PF04625; DEC-1_N; 1. DR Pfam; PF04624; DEC-1_REPEAT; 12. KW Chorion; Eggshell; Repeat; Alternative splicing; Signal; Polymorphism. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 950 DEFECTIVE CHORION-1 PROTEIN, FC106 FT ISOFORM. FT CHAIN 279 950 S80. FT CHAIN 279 ? S60. FT DOMAIN 493 788 12 X 26 AA APPROXIMATE TANDEM REPEATS, FT GLU, MET-RICH. FT REPEAT 493 518 1. FT REPEAT 519 544 2. FT REPEAT 545 570 3. FT REPEAT 571 596 4. FT REPEAT 597 622 5. FT REPEAT 623 652 6 (APPROXIMATE). FT REPEAT 653 680 7 (APPROXIMATE). FT REPEAT 681 696 8 (APPROXIMATE). FT REPEAT 697 720 9 (APPROXIMATE). FT REPEAT 721 733 10 (APPROXIMATE). FT REPEAT 734 758 11 (APPROXIMATE). FT REPEAT 759 788 12 (APPROXIMATE). FT VARIANT 545 570 MISSING (IN ALLELE DEC-1-FC2-ISRAEL). FT VARIANT 545 622 MISSING (IN ALLELE DEC-1-FC4). FT VARIANT 571 622 MISSING (IN ALLELE DEC-1-FC3). FT VARIANT 597 622 MISSING (IN ALLELE DEC-1-FC2-GHANGHRY). FT VARIANT 627 627 M -> V (IN ALLELE DEC-1-FC3). FT VARIANT 644 644 Q -> H (IN ALLELE DEC-1-FC4). FT VARIANT 690 690 Q -> H (IN ALLELE DEC-1-FC3). FT CONFLICT 17 17 A -> V (IN REF. 1 AND 4; CAA53815). FT CONFLICT 219 219 Q -> E (IN REF. 1). FT CONFLICT 347 347 D -> H (IN REF. 1). FT CONFLICT 382 382 A -> T (IN REF. 1). FT CONFLICT 847 877 PENEGTARHKVDALGVGGNKRKKSKSKSAPP -> AGERRH FT RQAQSRCPGSWRQQAQEVQVQVGAA (IN REF. 1). FT CONFLICT 888 901 QRPVVQSYGTSYGG -> SVRWFRVTEQATAE (IN REF. FT 1). SQ SEQUENCE 950 AA; 108371 MW; 25340DA159E9F508 CRC64; MRLFSLLPLL ALLVVQAAGQ SEVTSDDPAT DAGSTTNSTT DTKPRIPSQD EILGQMPSIN PIRTGNPQMD AFYMMFPALG SLLKWGSLFP AYSILGAIPD NLQPTAAASK VVLVLADDAT AKTRVARQNP PPNPLGQLMN WPALPQDFQL PSMDLGPQVG SFLAQLPAMP TVPGLLGAAA PVPAPAPAPA AAPPPAPAPA ADPPAAPVPD APQPAILGQA ALQNAFTFFN PANFDASSLL GQSVPTFAPP NLDFVAQMQR QFFPGMTPAQ PAAAGTDAQA SDISEVRVRP EDPYSQEAQM KIKSALEMEQ ERQQQAQVKD QEQVPLLWFR MPTTQNQDAT EEKTLEDLRV EAKLRAFERQ VIAELRMLQK IELMAKQMRS SAAAQNGDSP YRISYPLSRT PIHKITRADI EQALRDDYVR RLVNKEAQRR ARNSGINTQK ANALKRQAKS QDQTLSKEDI VQIMAYAYRM ANEQMESEKG KQDKVYAAYR TEQNPMMMQQ RQWSEEQAKI QQNQQQIQQN PMMMQQRQWS EEQAKIQQNQ QQIQQNPMMM QQRQWSEEQA KIQQNQQQIQ QNPMMMQQRQ WSEEQAKIQQ NQQQIQQNPM MVQQRQWSEE QAKIQQNQQQ IQQNPMMMQQ RQWSEEQAKI QHDQQMAQQM AQQGLMMTEQ RQRQWSEDQA KIQQAQQMAQ QTPMMMPQMQ QRQWTEDPQM VQQMQQRQWA EDQTRMQMAQ QNPMMQQQRQ MAENPQMMQQ RQWSEEQTKI EQAQQMAQQN QMMMQQMQQR QWSEDQAQIQ QQQRQMMQQT PMMMKERQWA EENPQSVQQQ GPMMMQQQMP SMMQREVEDE DNKAEDDLVG EAGPQMPENE GTARHKVDAL GVGGNKRKKS KSKSAPPTVI NYYYAAPQRP VVQSYGTSYG GGGYGSNAYG VPRPVNSYQS QGYRAAVGND EVDEMLRQHQ TMARATHFRQ // ID DC13_DROME STANDARD; PRT; 1590 AA. AC P18171; Q9W3P3; DT 01-NOV-1990 (Rel. 16, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Defective chorion-1 protein, FC177 isoform precursor. GN DEC-1 OR CG2175. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=91032553; PubMed=1699826; RA Waring G.L., Hawley R.J., Schoenfeld T.; RT "Multiple proteins are produced from the dec-1 eggshell gene in RT Drosophila by alternative RNA splicing and proteolytic cleavage RT events."; RL Dev. Biol. 142:1-12(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX MEDLINE=88243015; PubMed=3378704; RA Hawley R.J., Waring G.L.; RT "Cloning and analysis of the dec-1 female-sterile locus, a gene RT required for proper assembly of the Drosophila eggshell."; RL Genes Dev. 2:341-349(1988). CC -!- FUNCTION: REQUIRED FOR PROPER ASSEMBLY OF THE EGGSHELL. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=FC177; CC IsoId=P18171-1; Sequence=Displayed; CC Name=FC106; CC IsoId=P18170-1; Sequence=External; CC Name=FC125; CC IsoId=P18169-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING EMBRYONIC STAGE 11. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M35889; AAA28448.1; -. DR EMBL; AE003442; AAF46278.2; -. DR FlyBase; FBgn0000427; dec-1. DR GO; GO:0042600; C:chorion; IDA. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0005213; F:structural constituent of chorion (sensu In...; IMP. DR GO; GO:0007306; P:insect chorion formation; IMP. DR InterPro; IPR006720; DEC-1_C. DR InterPro; IPR006719; DEC-1_N. DR InterPro; IPR006718; DEC-1_REPEAT. DR Pfam; PF04626; DEC-1_C; 1. DR Pfam; PF04625; DEC-1_N; 1. DR Pfam; PF04624; DEC-1_REPEAT; 12. KW Chorion; Eggshell; Repeat; Alternative splicing; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 1590 DEFECTIVE CHORION-1 PROTEIN, FC177 FT ISOFORM. FT DOMAIN 493 788 12 X 26 AA APPROXIMATE TANDEM REPEATS, FT GLU, MET-RICH. FT REPEAT 493 518 1. FT REPEAT 519 544 2. FT REPEAT 545 570 3. FT REPEAT 571 596 4. FT REPEAT 597 622 5. FT REPEAT 623 652 6 (APPROXIMATE). FT REPEAT 653 680 7 (APPROXIMATE). FT REPEAT 681 696 8 (APPROXIMATE). FT REPEAT 697 720 9 (APPROXIMATE). FT REPEAT 721 733 10 (APPROXIMATE). FT REPEAT 734 758 11 (APPROXIMATE). FT REPEAT 759 788 12 (APPROXIMATE). FT CONFLICT 17 17 A -> V (IN REF. 1). FT CONFLICT 219 219 Q -> E (IN REF. 1). FT CONFLICT 347 347 D -> H (IN REF. 1). FT CONFLICT 382 382 A -> T (IN REF. 1). FT CONFLICT 847 877 PENEGTARHKVDALGVGGNKRKKSKSKSAPP -> AGERRH FT RQAQSRCPGSWRQQAQEVQVQVGAA (IN REF. 1). FT CONFLICT 888 901 QRPVVQSYGTSYGG -> SVRWFRVTEQATAE (IN REF. FT 1). FT CONFLICT 995 995 R -> Q (IN REF. 1). FT CONFLICT 1051 1052 SV -> C (IN REF. 1). FT CONFLICT 1296 1296 Q -> P (IN REF. 1). FT CONFLICT 1299 1299 E -> D (IN REF. 1). SQ SEQUENCE 1590 AA; 179187 MW; F78F36B465D1D790 CRC64; MRLFSLLPLL ALLVVQAAGQ SEVTSDDPAT DAGSTTNSTT DTKPRIPSQD EILGQMPSIN PIRTGNPQMD AFYMMFPALG SLLKWGSLFP AYSILGAIPD NLQPTAAASK VVLVLADDAT AKTRVARQNP PPNPLGQLMN WPALPQDFQL PSMDLGPQVG SFLAQLPAMP TVPGLLGAAA PVPAPAPAPA AAPPPAPAPA ADPPAAPVPD APQPAILGQA ALQNAFTFFN PANFDASSLL GQSVPTFAPP NLDFVAQMQR QFFPGMTPAQ PAAAGTDAQA SDISEVRVRP EDPYSQEAQM KIKSALEMEQ ERQQQAQVKD QEQVPLLWFR MPTTQNQDAT EEKTLEDLRV EAKLRAFERQ VIAELRMLQK IELMAKQMRS SAAAQNGDSP YRISYPLSRT PIHKITRADI EQALRDDYVR RLVNKEAQRR ARNSGINTQK ANALKRQAKS QDQTLSKEDI VQIMAYAYRM ANEQMESEKG KQDKVYAAYR TEQNPMMMQQ RQWSEEQAKI QQNQQQIQQN PMMMQQRQWS EEQAKIQQNQ QQIQQNPMMM QQRQWSEEQA KIQQNQQQIQ QNPMMMQQRQ WSEEQAKIQQ NQQQIQQNPM MVQQRQWSEE QAKIQQNQQQ IQQNPMMMQQ RQWSEEQAKI QHDQQMAQQM AQQGLMMTEQ RQRQWSEDQA KIQQAQQMAQ QTPMMMPQMQ QRQWTEDPQM VQQMQQRQWA EDQTRMQMAQ QNPMMQQQRQ MAENPQMMQQ RQWSEEQTKI EQAQQMAQQN QMMMQQMQQR QWSEDQAQIQ QQQRQMMQQT PMMMKERQWA EENPQSVQQQ GPMMMQQQMP SMMQREVEDE DNKAEDDLVG EAGPQMPENE GTARHKVDAL GVGGNKRKKS KSKSAPPTVI NYYYAAPQRP VVQSYGTSYG GGGYGSNAYG VPRPVNSYQS QGYRAAVGND EVDEMLRQHQ TMARTINPKQ PGEVGGSESQ KSNSNPPTTL TPAPQEQPQE HRVHKRLAHF HRFGREAGLN ATTSKGCGCG RLDCLCGRSC RCGRRGLESR VVSSRTSGTC QCKASHRNKR SVEYGTLETI DEGSLNELRR EYKLGLKEIT LSPDEDPAEA LMRYNAASIR EALERASMEP LEIGGDQYEE DAQQEPMEEE QLQHDPNTEP QYNHKDFVRL TTSTASPITS TTEAATPTGS DSTSEATVTP EVTTTTSTST TTTTESTKDE GLDMQQDSQA EAESSHVTKS ISKQEAEIHQ LHSIVEELKN EILKLNLRCS TIISNNVAKE PVTEKNPPVV EEPSKQEDKP KVEEKVIAEE QAPVEQEEEL EEDEDSTSIS TTTETPSPSG SYSTKPGLSL GSPRVDEQSG SSNKLDYDDD NNWQRILANR GYDTDYLTKS HERQFAQGQN LEMPKNCNYD GNGSQEYGPY PEFQADEPST DTEGKAKRAL SVKQQAQLLN AALNDSGSDS SDGTTTTTTP SPYAMRGKFV RRRSTARRVP IPKIGKASDE VWVRSPRQAK MPQRPKKSMS KPKKQSSQVT TQATVSSTKL DSLVDVLKDL VRLQIQKEKK SSLLRTQSNN LSKTKPKSIK PVKVIKRKRL RRRQHKSIAT TIRSPIQTKA // ID DCAM_DROME STANDARD; PRT; 347 AA. AC P91931; P91925; Q9VKY9; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE S-adenosylmethionine decarboxylase proenzyme (EC 4.1.1.50) (AdoMetDC) DE (SamDC) [Contains: S-adenosylmethionine decarboxylase alpha chain; S- DE adenosylmethionine decarboxylase beta chain]. GN SAMDC OR CG5029. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Canton-S; RX MEDLINE=98098079; PubMed=9435790; RA Larsson J., Rasmuson-Lestander A.; RT "Cloning, mapping and mutational analysis of the S-adenosylmethionine RT decarboxylase gene in Drosophila melanogaster."; RL Mol. Gen. Genet. 256:652-660(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = (5-DEOXY-5- CC ADENOSYL)(3-AMINOPROPYL) METHYLSULFONIUM SALT + CO(2). CC -!- COFACTOR: PYRUVOYL GROUP. CC -!- PATHWAY: DECARBOXYLATION OF S-ADENOSYLMETHIONINE PROVIDES THE CC AMINOPROPYL MOIETY REQUIRED FOR SPERMIDINE AND SPERMINE CC BIOSYNTHESIS FROM PUTRESCINE. CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC ADOMETDC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11216; CAA72102.1; -. DR EMBL; Y11820; CAA72505.1; -. DR EMBL; AE003628; AAF52917.1; -. DR HSSP; P17707; 1JEN. DR FlyBase; FBgn0019932; SamDC. DR InterPro; IPR001985; SAM_decarbox. DR Pfam; PF01536; SAM_decarbox; 1. DR ProDom; PD002379; SAM_decarbox; 1. DR TIGRFAMs; TIGR00535; SAM_DCase; 1. DR PROSITE; PS01336; ADOMETDC; 1. KW Spermidine biosynthesis; Lyase; Decarboxylase; Pyruvate; Zymogen. FT CHAIN 1 65 S-ADENOSYLMETHIONINE DECARBOXYLASE BETA FT CHAIN (BY SIMILARITY). FT CHAIN 66 347 S-ADENOSYLMETHIONINE DECARBOXYLASE ALPHA FT CHAIN (BY SIMILARITY). FT SITE 65 66 CLEAVAGE (NONHYDROLYTIC) FT (BY SIMILARITY). FT MOD_RES 66 66 CONVERTED TO A PYRUVOYL GROUP FT (BY SIMILARITY). FT ACT_SITE 10 10 IMPORTANT FOR CATALYTIC ACTIVITY (BY FT SIMILARITY). FT ACT_SITE 13 13 IMPORTANT FOR CATALYTIC ACTIVITY (BY FT SIMILARITY). FT ACT_SITE 80 80 IMPORTANT FOR CATALYTIC ACTIVITY (BY FT SIMILARITY). FT VARIANT 167 167 T -> S (IN STRAIN CANTON-S). FT VARIANT 172 172 S -> T (IN STRAIN CANTON-S). FT VARIANT 346 346 Y -> N (IN STRAIN BERKELEY). SQ SEQUENCE 347 AA; 39817 MW; 48FEDA7CAF6CDA0C CRC64; MLENGSHFFE GVEKLLEIWF EESSNGDDDL RNISRSDWEN VLSNVNCQII STSKNDIIDA FVLSESSMFV SKRRWILKTC GTTTPLKCLG QLLKLAEANG YNVVADLFYS RKNFTRPEAQ ITPHQGFTEE VTYLDSIFPN GRSYCLGSMN LECWYLYTFS RSDIKITPQL ISDEKNVDSD PDQTIEILMQ DLDPETMSIF YKNKFNDANG ATVKSGIDTI LPTMHIDDFL FDPCGYSMNG INDKGEYMTI HITPENQFSY VSFETNVALS NYRKLINQVI NTFKPGKFIV TIFANKCSLA YETMKELEVE YSQGSHWKRT DMQCCNFPSY NLLFAQYSHS EKTGDYL // ID DCE_DROME STANDARD; PRT; 510 AA. AC P20228; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutamate decarboxylase (EC 4.1.1.15) (GAD). GN GAD OR GLB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90155291; PubMed=1689376; RA Jackson F.R., Newby L.M., Kulkarni S.J.; RT "Drosophila GABAergic systems: sequence and expression of glutamic RT acid decarboxylase."; RL J. Neurochem. 54:1068-1078(1990). CC -!- FUNCTION: CATALYZES THE PRODUCTION OF GABA. CC -!- CATALYTIC ACTIVITY: L-GLUTAMATE = 4-AMINOBUTANOATE + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER. CC -!- SIMILARITY: BELONGS TO THE GROUP II DECARBOXYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76198; CAA53791.1; -. DR PIR; JH0192; A30999. DR FlyBase; FBgn0004516; Gad1. DR GO; GO:0004351; F:glutamate decarboxylase activity; IDA. DR GO; GO:0008345; P:larval locomotory behavior; IMP. DR GO; GO:0007528; P:neuromuscular junction development; IMP. DR InterPro; IPR002129; Pyridoxal_deC. DR Pfam; PF00282; pyridoxal_deC; 1. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. KW Neurotransmitter biosynthesis; Lyase; Decarboxylase; KW Pyridoxal phosphate. FT BINDING 322 322 PYRIDOXAL PHOSPHATE (POTENTIAL). SQ SEQUENCE 510 AA; 57758 MW; E9B6DED48B47F1DF CRC64; MSLNPNGYKL SERTGKLTAY DLMPTTVTAG PETREFLLKV IDVLLDFVKA TNDRNEKVLD FHHPEDMKRL LDLDVPDRAL PLQQLIEDCA TTLKYQVKTG HPHFFNQLSN GLDLISMAGE WLTATANTNM FTYEIAPVFI LMENVVLTKM REIIGWSGGD SILAPGGSIS NLYAFLAARH KMFPNYKEHG SVGLPGTLVM LTSDQCHYSI KSCAAVCGLG TDHCIVVPSD EHGKMITSEL ERLILERKAK GDIPFFVNAT AGTTVLGAFD DINTIADICQ KYNCWMHIDA AWGGGLLMSR THRHPRFTGV ERADSVTWNP HKLMGALLQC STIHFKEDGL LISCNQMSAE YLFMTDKQYD ISYDTGDKVI QCGRHNDIFK LWLQWRAKGT EGFEQQQDRL MELVQYQLKR IREQSDRFHL ILEPECVNVS FWYVPKRLRG VPHDAKKEVE LGKICPIIKG RMMQKGTLMV GYQPDDRRPN FFRSIISSAA VNEADVDFML DEIHRLGDDL // ID DCHS_DROME STANDARD; PRT; 847 AA. AC Q05733; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histidine decarboxylase (EC 4.1.1.22) (HDC). GN HDC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93209238; PubMed=8096176; RA Burg M.G., Sarthy P.V., Koliantz G., Pak W.L.; RT "Genetic and molecular identification of a Drosophila histidine RT decarboxylase gene required in photoreceptor transmitter synthesis."; RL EMBO J. 12:911-919(1993). CC -!- FUNCTION: REQUIRED IN PHOTORECEPTOR TRANSMITTER SYNTHESIS. CC -!- CATALYTIC ACTIVITY: L-HISTIDINE = HISTAMINE + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GROUP II DECARBOXYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X70644; CAA49989.1; -. DR PIR; S36337; S36337. DR FlyBase; FBgn0005619; Hdc. DR InterPro; IPR002129; Pyridoxal_deC. DR Pfam; PF00282; pyridoxal_deC; 1. DR PRINTS; PR00800; YHDCRBOXLASE. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. KW Lyase; Decarboxylase; Catecholamine biosynthesis; Pyridoxal phosphate. FT BINDING 304 304 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 847 AA; 94106 MW; 6DFDDE7B9034BC8F CRC64; MDFKEYRQRG KEMVDYIADY LENIRERRVF PDVSPGYMRQ LLPESAPIEG EPWPKIFSDV ERIVMPGITH WQSPHMHAYF PALNSMPSLL GDMLADAINC LGFTWASSPA CTELEIIVMN WLGKMIGLPD AFLHLSSQSQ GGGVLQTTAS EATLVCLLAG RTRAIQRFHE RHPGYQDAEI NARLVAYCSD QAHSSVEKAA LIGLVRMRYI EADEDLAMRG KLLREAIEDD IKQGLVPFWV CATLGTTGSC SFDNLEEIGI VCAEHHLWLH VDAAYAGSAF ICPEFRTWLR GIERADSIAF NPSKWLMVHF DATALWVRDS TAVHRTFNVE PLYLQHENSG VAVDFMHWQI PLSRRFRALK VWFVLRSYGI KGLQRHIREG VRLAQKFEAL VLADHRFELP AKRHLGLVVF RIRGDNEITE KLLKRLNHRG NLHCIPSSLK GQYVIRFTIT STHTTLDDIV KDWMEIRQVA STVLEEMNIT ISNRVYLKET KEKNEAFGSS LLLSNSPLSP KVVNGSFAAI FDADEFLAKT YAGVRIAHQE SPSMRRRVRG ILMSGKQFSL DSHMDVVVQT TLDAGNGATR TSTTNSYGHT TSAAQANSER QASIQEDNEE SPEETELLSL CRTSNVPSPE HAHSLSTPSR SCSSSSHSLT HSLTQSSARS SPVNQFRHIT LCAVPSQSHL SMPLAMPLPN RNVTVSVDSL LNPVTTCNVY HGKRFLEPLE NLAQTSASFS SSIFRLPTPM ATPTRESPED PDWPAKTFSQ LLLERYSSQS QSLGNNSSTE SSSLSGGATP TPTPMSSLDE LVTPLLLSFA SPSQPMLSAH GIGEGQRERG SDSDATVCST TSSMESL // ID DCO1_DROME STANDARD; PRT; 394 AA. AC P40807; Q9V352; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ornithine decarboxylase 1 (EC 4.1.1.17) (ODC). GN ODC1 OR CG8721. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93319633; PubMed=8329117; RA Rom E., Kahana C.; RT "Isolation and characterization of the Drosophila ornithine RT decarboxylase locus: evidence for the presence of two transcribed ODC RT genes in the Drosophila genome."; RL DNA Cell Biol. 12:499-508(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: L-ORNITHINE = PUTRESCINE + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: POLYAMINE BIOSYNTHESIS; FIRST (RATE-LIMITING) STEP. CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF ORNITHINE, DAP, AND ARGININE CC DECARBOXYLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66601; CAA47167.1; -. DR EMBL; X66599; CAA47165.1; -. DR EMBL; AE003839; AAF59150.1; -. DR HSSP; P00860; 7ODC. DR FlyBase; FBgn0013307; Odc1. DR InterPro; IPR000183; Decarbxylse2. DR InterPro; IPR009006; Racem_decarbox_C. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PRINTS; PR01179; ODADCRBXLASE. DR PROSITE; PS00878; ODR_DC_2_1; 1. DR PROSITE; PS00879; ODR_DC_2_2; 1. KW Lyase; Decarboxylase; Pyridoxal phosphate; Polyamine biosynthesis; KW Multigene family. FT BINDING 62 62 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT ACT_SITE 343 343 BY SIMILARITY. FT CONFLICT 44 45 NV -> KL (IN REF. 2). FT CONFLICT 242 242 K -> Q (IN REF. 1; CAA47165). FT CONFLICT 325 325 L -> Q (IN REF. 1; CAA47165). FT CONFLICT 348 348 K -> Q (IN REF. 1; CAA47165). SQ SEQUENCE 394 AA; 44166 MW; CD90520632B7D3B2 CRC64; MAAATPEIQF YERELNIRRV IEECDLQRLD QALNICDLSS VERNVRLWQK LLPRIKPFYA VKCNDDPMVV RLLAQLGAGF DCASKNEVKL VLGFDVSPER IIFANPCRPV SHLEYAKEHQ VSNGTVDNEF EVYKLHTHYP NSNLIVRFKS EAKEAQCPLG DKFGCDADVD AAALMLLAKS LELKVTGTSF HVGSGCSELQ AYDRAIKKAK NLFKFGALLG YDMDFLDIGG GFPGSDDVKF EKIAESVNTS VQRHFPDERV HIIAEPGRFF VAAACTLVCK IHAKREIRNE AGKLDTVMYY LNDGVYGSFN CILYDHQVVI AEHYLDNAES LPHLKSLIWG PSCDALDKIS EDLHLPNLNR GDLLGFRNMG AYTMPIASAF NGFEVPKTLY FQAI // ID DCO2_DROME STANDARD; PRT; 393 AA. AC P40808; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ornithine decarboxylase 2 (EC 4.1.1.17) (ODC). GN ODC2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93319633; PubMed=8329117; RA Rom E., Kahana C.; RT "Isolation and characterization of the Drosophila ornithine RT decarboxylase locus: evidence for the presence of two transcribed ODC RT genes in the Drosophila genome."; RL DNA Cell Biol. 12:499-508(1993). CC -!- CATALYTIC ACTIVITY: L-ORNITHINE = PUTRESCINE + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: POLYAMINE BIOSYNTHESIS; FIRST (RATE-LIMITING) STEP. CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF ORNITHINE, DAP, AND ARGININE CC DECARBOXYLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66600; CAA47166.1; -. DR HSSP; P07805; 1F3T. DR FlyBase; FBgn0013308; Odc2. DR InterPro; IPR000183; Decarbxylse2. DR InterPro; IPR009006; Racem_decarbox_C. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PRINTS; PR01179; ODADCRBXLASE. DR PROSITE; PS00878; ODR_DC_2_1; 1. DR PROSITE; PS00879; ODR_DC_2_2; 1. KW Lyase; Decarboxylase; Pyridoxal phosphate; Polyamine biosynthesis; KW Multigene family. FT BINDING 62 62 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT ACT_SITE 343 343 BY SIMILARITY. SQ SEQUENCE 393 AA; 44140 MW; A6F56F94C1AD5836 CRC64; MVNGDLRIQY YDEELNIRKV IEQADLEHLD QALNICDLSS LERKLRLWHK LMPRIEPHYA VKCNDDPVVV KFLADLGTGF DCASKNELKL VLGFGVSPER IIFAHPCRPA SHLRYAKEQQ VVNGTVDNEY EIYKLRKHYP DSSLIVRFKS EAKKALCPLG DKYGCDAEAD AAALMLLAKA LGLKVTGTSF HVGSGCSEVE AYDRAIEKAE NIFKVGEMIG HKMELLDVGG GFPGIDDEMF KEIAQSVNTS VELRFPDKRI RIISEPGRFF VEAAYTLICK VHAKREVRSK DGKLDTMMYY LNDGIFGAFA GMFYYPEEVA PELYLDEAES LPKLKSVIWG PSCDALDKIS DLLLPNLNPG DLLGFRNMGA YTMPIASPFN GFDVPETRFF KAK // ID DCO_DROME STANDARD; PRT; 440 AA. AC O76324; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Discs overgrown protein kinase (EC 2.7.1.-) (Double-time protein). GN DCO OR DBT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98337188; PubMed=9674431; RA Kloss B., Price J.L., Saez L., Blau J., Rothenfluh A., Wesley C.S., RA Young M.W.; RT "The Drosophila clock gene double-time encodes a protein closely RT related to human casein kinase I epsilon."; RL Cell 94:97-107(1998). RN [2] RP MUTAGENESIS, AND FUNCTION. RX MEDLINE=98337187; PubMed=9674430; RA Price J.L., Blau J., Rothenfluh A., Abodeely M., Kloss B., Young M.W.; RT "Double-time is a novel Drosophila clock gene that regulates PERIOD RT protein accumulation."; RL Cell 94:83-95(1998). CC -!- FUNCTION: INVOLVED IN CIRCADIAN RHYTHMS, VIABILITY AND MOLECULAR CC OSCILLATIONS OF THE CLOCK GENES PERIOD (PER) AND TIMELESS (TIM). CC DBT REDUCES THE STABILITY AND THUS THE ACCUMULATION OF MONOMERIC CC PER PROTEINS, PROBABLY THROUGH PHOSPHORYLATION. NO EVIDENT CC CIRCADIAN OSCILLATION IS DETECTED IN HEAD. CC -!- SUBUNIT: FORMS A COMPLEX WITH PER. CC -!- TISSUE SPECIFICITY: EXPRESSED IN PHOTORECEPTOR CELLS OF THE EYES CC AS WELL AS IN THE REGION SITUATED BETWEEN THE OPTIC LOBE AND THE CC CENTRAL BRAIN. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CASEIN KINASE I SUBFAMILY. COULD BE THE ORTHOLOG OF CKI-EPSILON. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF055583; AAC39134.1; -. DR HSSP; Q06486; 1CKI. DR FlyBase; FBgn0002413; dco. DR GO; GO:0007154; P:cell communication; IMP. DR GO; GO:0007446; P:imaginal disc growth; IMP. DR GO; GO:0045475; P:locomotor rhythm; NAS. DR GO; GO:0008341; P:response to cocaine (sensu Insecta); IMP. DR GO; GO:0030431; P:sleep; NAS. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Biological rhythms; Transferase; Serine/threonine-protein kinase; KW ATP-binding. FT DOMAIN 9 277 PROTEIN KINASE. FT NP_BIND 15 23 ATP (BY SIMILARITY). FT BINDING 38 38 ATP (BY SIMILARITY). FT ACT_SITE 128 128 BY SIMILARITY. FT DOMAIN 319 332 POLY-ALA. FT DOMAIN 336 339 POLY-GLN. FT DOMAIN 347 351 POLY-GLY. FT DOMAIN 414 426 POLY-GLY. FT DOMAIN 430 437 POLY-GLY. FT MUTAGEN 47 47 P->S: IN DBTS; SHORTENS THE BEHAVIORAL FT PERIOD. FT MUTAGEN 80 80 M->I: IN DBTL; LENGTHENS THE BEHAVIORAL FT PERIOD. SQ SEQUENCE 440 AA; 48073 MW; B875891D5747391D CRC64; MELRVGNKYR LGRKIGSGSF GDIYLGTTIN TGEEVAIKLE CIRTKHPQLH IESKFYKTMQ GGIGIPRIIW CGSEGDYNVM VMELLGPSLE DLFNFCSRRF SLKTVLLLAD QMISRIDYIH SRDFIHRDIK PDNFLMGLGK KGNLVYIIDF GLAKKFRDAR SLKHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG YVLMYFNLGA LPWQGLKAAN KRQKYERISE KKLSTSIVVL CKGFPSEFVN YLNFCRQMHF DQRPDYCHLR KLFRNLFHRL GFTYDYVFDW NLLKFGGPRN PQAIQQAQDG ADGQAGHDAV AAAAAVAAAA AASSHQQQQH KVNAALGGGG GSRAQQQLQG GQTLAMLGGN GGGNGSQLIG GNGLNMDDSM AATNSSRPPY DTPERRPSIR MRQGGGGGGG GVGVGGMQSG GGGGGVGNAK // ID DCUP_DROME STANDARD; PRT; 356 AA. AC Q9V595; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Uroporphyrinogen decarboxylase (EC 4.1.1.37) (URO-D) (UPD). GN UPDO OR CG1818. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN-III = COPROPORPHYRINOGEN + 4 CC CO(2). CC -!- PATHWAY: PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE UROPORPHYRINOGEN DECARBOXYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003833; AAF58922.1; -. DR HSSP; P06132; 1URO. DR FlyBase; FBgn0033428; Updo. DR InterPro; IPR006361; HemE. DR InterPro; IPR000257; Uro_decarbxyls. DR Pfam; PF01208; URO-D; 1. DR ProDom; PD003225; Uro_decarbxyls; 1. DR TIGRFAMs; TIGR01464; hemE; 1. DR PROSITE; PS00906; UROD_1; 1. DR PROSITE; PS00907; UROD_2; 1. KW Lyase; Decarboxylase; Porphyrin biosynthesis; Heme biosynthesis. SQ SEQUENCE 356 AA; 39988 MW; 75E2B3AEFD59DBFD CRC64; MKDAKPFPVL KNDNLLRAAR GEVVDRVPVW VMRQAGRYLP EFQELRKHHD FFTVCRTPEL ACEVTMQPLR RFDLDASIIF SDILVIPQAL GLTVEMHAGV GPVLPQPIVV PEDLKRLTPD GALSRLSYVG DAITMMRHKL EGRVPLIGFT GAPWTLMGYM IEGGGSKTMS KAKAWLNEHP EDSKLFLNLL TDAIVDYLEM QVKAGAQMLQ VFESSAEHLS KEQFLQWCVP YLKRIRDELV DRLTKKAIPV VPMTLFAKGA GHSLKEQSEL GYDVIGLDWT VDPLEARNLV GPNITLQGNL DPQDMYRDPD ELRNLTTEMV HKFGKSRYIA NLGHGITPQT PITSMEVLVE AVHKAL // ID DDC_DROME STANDARD; PRT; 510 AA. AC P05031; O18379; P05032; Q24295; Q95SL9; Q9VIZ5; Q9VIZ6; DT 13-AUG-1987 (Rel. 05, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) (AADC) (DOPA DE decarboxylase) (DDC). GN DDC OR CG10697. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS CNS AND HYPODERM), AND TISSUE RP SPECIFICITY. RC STRAIN=Canton-S; RX MEDLINE=87133496; PubMed=3102230; RA Morgan B.A., Johnson W.A., Hirsh J.; RT "Regulated splicing produces different forms of dopa decarboxylase in RT the central nervous system and hypoderm of Drosophila melanogaster."; RL EMBO J. 5:3335-3342(1986). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS CNS AND 3). RC STRAIN=Canton-S; RX MEDLINE=87053836; PubMed=3023054; RA Eveleth D.D., Gietz R.D., Spencer C.A., Nargang F.E., Hodgetts R.B., RA Marsh J.L.; RT "Sequence and structure of the dopa decarboxylase gene of Drosophila: RT evidence for novel RNA splicing variants."; RL EMBO J. 5:2663-2672(1986). RN [3] RP REVISIONS. RC STRAIN=Canton-S; RA Marsh J.L.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. (ISOFORM 3). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 74-510 FROM N.A. RC STRAIN=St. Lucia; RX MEDLINE=99250256; PubMed=9950256; RA Tatarenkov A., Saez A.G., Ayala F.J.; RT "A compact gene cluster in Drosophila: the unrelated Cs gene is RT compressed between duplicated amd and Ddc."; RL Gene 231:111-120(1999). RN [7] RP SEQUENCE OF 493-510 FROM N.A. RX MEDLINE=88038375; PubMed=3478553; RA Eveleth D.D., Marsh J.L.; RT "Overlapping transcription units in Drosophila: sequence and structure RT of the Cs gene."; RL Mol. Gen. Genet. 209:290-298(1987). RN [8] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=87042790; PubMed=3095924; RA Scholnick S.B., Bray S.J., Morgan B.A., McCormick C.A., Hirsh J.; RT "CNS and hypoderm regulatory elements of the Drosophila melanogaster RT dopa decarboxylase gene."; RL Science 234:998-1002(1986). RN [9] RP DEVELOPMENTAL STAGE. RX MEDLINE=86165362; PubMed=3007242; RA Spencer C.A., Gietz R.D., Hodgetts R.B.; RT "Analysis of the transcription unit adjacent to the 3'-end of the dopa RT decarboxylase gene in Drosophila melanogaster."; RL Dev. Biol. 114:260-264(1986). RN [10] RP INDUCTION. RX MEDLINE=86165352; PubMed=3007239; RA Clark W.C., Doctor J., Fristrom J.W., Hodgetts R.B.; RT "Differential responses of the dopa decarboxylase gene to RT 20-OH-ecdysone in Drosophila melanogaster."; RL Dev. Biol. 114:141-150(1986). CC -!- FUNCTION: CATALYZES THE DECARBOXYLATION OF L-3,4- CC DIHYDROXYPHENYLALANINE (DOPA) TO DOPAMINE, L-5-HYDROXYTRYPTOPHAN CC TO SEROTONIN AND L-TRYPTOPHAN TO TRYPTAMINE. CC -!- CATALYTIC ACTIVITY: L-TRYPTOPHAN = TRYPTAMINE + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=CNS; Synonyms=Long; CC IsoId=P05031-1; Sequence=Displayed; CC Name=Hypoderm; Synonyms=Short; CC IsoId=P05031-2; Sequence=VSP_001305; CC Name=3; CC IsoId=P05031-3; Sequence=VSP_001306; CC -!- TISSUE SPECIFICITY: HYPODERM ISOFORM IS EXPRESSED ONLY IN CC HYPODERMAL EPITHELIUM AND THE CNS ISOFORM ONLY IN CENTRAL NERVOUS CC SYSTEM. CC -!- DEVELOPMENTAL STAGE: HIGH EXPRESSION LEVELS IN HYPODERM DURING CC LATE EMBRYOGENESIS, LATE LARVAL DEVELOPMENT, PUPARIATION AND ADULT CC ECLOSION. CONSTANT EXPRESSION LEVEL IN CNS THROUGHOUT THE LIFE CC CYCLE. CC -!- INDUCTION: BY ECDYSONE. IN LARVAL EPIDERMIS, EXPRESSION IS RAPIDLY CC INDUCED. IN ADULT EPIDERMIS EXPRESSION RESPONDS TO A PULSE OF CC HORMONE AND THERE IS A TIME LAG BETWEEN INITIAL EXPOSURE AND CC APPEARANCE OF DDC. CC -!- SIMILARITY: BELONGS TO THE GROUP II DECARBOXYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04661; CAB37087.1; -. DR EMBL; X04661; CAB37088.1; -. DR EMBL; X04426; CAA28022.1; -. DR EMBL; X04426; CAA28023.1; -. DR EMBL; AE003661; AAF53762.1; -. DR EMBL; AE003661; AAF53763.1; -. DR EMBL; AF091328; AAC67582.1; -. DR EMBL; X05991; CAA29409.2; -. DR EMBL; AY060708; AAL28256.1; -. DR PIR; A25697; DCFFD1. DR PIR; A25709; DCFFA. DR PIR; B25697; DCFFD2. DR FlyBase; FBgn0000422; Ddc. DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IMP. DR GO; GO:0007619; P:courtship behavior; NAS. DR GO; GO:0006585; P:dopamine biosynthesis from tyrosine; IMP. DR GO; GO:0008062; P:eclosion rhythm; NAS. DR GO; GO:0007611; P:learning and/or memory; NAS. DR GO; GO:0006587; P:serotonin biosynthesis from tryptophan; IMP. DR InterPro; IPR002129; Pyridoxal_deC. DR Pfam; PF00282; pyridoxal_deC; 1. DR PRINTS; PR00800; YHDCRBOXLASE. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. KW Lyase; Decarboxylase; Catecholamine biosynthesis; Pyridoxal phosphate; KW Alternative splicing. FT BINDING 337 337 PYRIDOXAL PHOSPHATE. FT VARSPLIC 1 35 Missing (in isoform Hypoderm). FT /FTId=VSP_001305. FT VARSPLIC 1 33 MSHIPISNTIPTKQTDGNGKANISPDKLDPKVS -> MSIG FT FRYRANNYARLITKYFCIHIK (in isoform 3). FT /FTId=VSP_001306. FT CONFLICT 32 33 MISSING (IN REF. 1). FT CONFLICT 479 479 R -> A (IN REF. 1). SQ SEQUENCE 510 AA; 57287 MW; 0A850488D407D4BF CRC64; MSHIPISNTI PTKQTDGNGK ANISPDKLDP KVSIDMEAPE FKDFAKTMVD FIAEYLENIR ERRVLPEVKP GYLKPLIPDA APEKPEKWQD VMQDIERVIM PGVTHWHSPK FHAYFPTANS YPAIVADMLS GAIACIGFTW IASPACTELE VVMMDWLGKM LELPAEFLAC SGGKGGGVIQ GTASESTLVA LLGAKAKKLK EVKELHPEWD EHTILGKLVG YCSDQAHSSV ERAGLLGGVK LRSVQSENHR MRGAALEKAI EQDVAEGLIP FYAVVTLGTT NSCAFDYLDE CGPVGNKHNL WIHVDAAYAG SAFICPEYRH LMKGIESADS FNFNPHKWML VNFDCSAMWL KDPSWVVNAF NVDPLYLKHD MQGSAPDYRH WQIPLGRRFR ALKLWFVLRL YGVENLQAHI RRHCNFAKQF GDLCVADSRF ELAAEINMGL VCFRLKGSNE RNEALLKRIN GRGHIHLVPA KIKDVYFLRM AICSRFTQSE DMEYSWKEVS AAADEMEQEQ // ID DDX1_DROME STANDARD; PRT; 727 AA. AC Q9VNV3; O61663; Q24131; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ATP-dependent helicase DDX1 (DEAD box protein 1). GN DDX1 OR CG9054. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=96257224; PubMed=8666277; RA Rafti F., Scarvelis D., Lasko P.F.; RT "A Drosophila melanogaster homologue of the human DEAD-box gene RT DDX1."; RL Gene 171:225-229(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P.F., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 458-727 FROM N.A. RC STRAIN=Berlin; RA Zinsmaier K.E., Eberle K.K., Buchner E.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT. EXPRESSION IS HIGHEST IN EARLY CC EMBRYOS. CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 SPRY DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U34773; AAC47309.1; -. DR EMBL; AE003597; AAF51814.1; -. DR EMBL; AY119661; AAM50315.1; -. DR EMBL; AF057167; AAD09429.1; -. DR FlyBase; FBgn0015075; Ddx1. DR GO; GO:0008026; F:ATP dependent helicase activity; ISS. DR GO; GO:0001700; P:embryonic development (sensu Insecta); IEP. DR GO; GO:0006446; P:regulation of translational initiation; ISS. DR GO; GO:0007046; P:ribosome biogenesis; ISS. DR GO; GO:0000245; P:spliceosome assembly; ISS. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 2. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00622; SPRY; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; FALSE_NEG. KW Hydrolase; ATP-binding; Helicase; RNA-binding. FT DOMAIN 129 245 SPRY. FT NP_BIND 46 53 ATP (POTENTIAL). FT SITE 370 373 DEAD BOX. FT CONFLICT 78 89 KGGAIGGAVTPW -> QGRCNWRSCDSV (IN REF. FT 1). FT CONFLICT 217 217 L -> S (IN REF. 1). FT CONFLICT 274 279 AAGAPS -> DSWST (IN REF. 1). FT CONFLICT 365 365 R -> G (IN REF. 1). FT CONFLICT 429 429 V -> G (IN REF. 1). FT CONFLICT 458 458 S -> C (IN REF. 3). FT CONFLICT 529 530 GG -> D (IN REF. 1). FT CONFLICT 580 589 MINVTLPDDK -> SKFSNFETIT (IN REF. FT 3). FT CONFLICT 682 682 K -> P (IN REF. 1). FT CONFLICT 704 704 V -> E (IN REF. 1). SQ SEQUENCE 727 AA; 80869 MW; 52B7BE91A33599DB CRC64; MTAFEEFGVL PELGMATDEL DWTLPTDVQA EAIPLILGGG DVLMAAETGS GKTGAFCLPI LQIVWETLRD LEEGKAGKGG AIGGAVTPWT MSFFDRGNAL AVTPDGLRCQ SREFKEWHGC RATTGVRGKG KFYFEATVTD EGLCRVGWST QQANLDLGTC RMGFGFGGTG KKSNNRQFDD YGEAFGKADV IGCLLDLKNQ EVSFTKNGQN LGVAFRLPDN LAKETFYPAV VLKNAEMQFN FGKTDFKYAP GNGFVGACQA GPEHSKANPI TGPAAGAPSA KPAPNAPQAI IMEPSRELAE QTYNQIEKFK YHLSNPEVRS LLLIGGVRLE EQKAQLMQGT HIVVGTPGRL EEMINSGLVL LTHCRFFVLD EADALLKQGY TELIDRLHKQ IPKITSDGRR LQMVVCSATL HAFEVKKMAE RLMHFPTWVD LKGEDAVPET VHHVVCLVDP QMDTTWQSLR QPIGTDGVHD RDNVHPGNHS KETLSQAVKL LKGEYCVHAI DKHNMDRAII FCRTKQDCDN LERFLRQRGG KHYSCVCLHG DRKPQERKEN LEMFKRQQVK FLICTDVAAR GLDITGLPFM INVTLPDDKT NYVHRIGRVG RAERMGLAIS LVATVPEKVW YHGEWCKSRG RSCNNTNLTE VRGCCIWYNE PNLLAEVEDH LNITIQQVDK TMDVPVNDFD GKVVYGQKNL RTGSGYEDHV EQLVPTVRKL TELELQSQSL FLKRLKV // ID DEAF_DROME STANDARD; PRT; 576 AA. AC Q24180; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Deformed epidermal autoregulatory factor 1 (DEAF-1 protein). GN DEAF1 OR CG8567. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 252-264 AND 495-519. RC TISSUE=Embryo; RX MEDLINE=96203118; PubMed=8617243; RA Gross C.T., McGinnis W.; RT "DEAF-1, a novel protein that binds an essential region in a Deformed RT response element."; RL EMBO J. 15:1961-1970(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTION FACTOR THAT BINDS THE HOMEOTIC DEFORMED CC (DFD) RESPONSE ELEMENT. HIGH AFFINITY BINDING SITES CONTAIN AT CC LEAST 1 TTCG MOTIF SURROUNDED BY ADDITIONAL TCG SEQUENCES. MAY BE CC INVOLVED IN THE SELECTIVE ACTION OF DFD ON THESE SITES WITHOUT CC BINDING DIRECTLY TO THE DFD PROTEIN. REQUIREMENT OF DEAF1 ACTIVITY CC MAY BE A COMMON FEATURE OF ENHANCERS TARGETED BY DFD. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: UBIQUITOUS THROUGHOUT EMBRYOGENESIS. HIGHLY CC EXPRESSED IN STAGE 3 EMBRYO INDICATING THAT IT IS MATERNALLY CC PROVIDED. AFTER STAGE 15, IT IS MORE PROMINENT IN THE CENTRAL CC NERVOUS SYSTEM. CC -!- SIMILARITY: CONTAINS 1 MYND-TYPE ZINC FINGER. CC -!- SIMILARITY: CONTAINS 1 SAND DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003515; AAF49105.1; -. DR EMBL; U46686; AAC47040.1; -. DR PIR; S69214; S69214. DR FlyBase; FBgn0013799; Deaf1. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IDA. DR InterPro; IPR000770; SAND_domain. DR InterPro; IPR002893; Znf_MYND. DR Pfam; PF01342; SAND; 1. DR Pfam; PF01753; zf-MYND; 1. DR SMART; SM00258; SAND; 1. DR PROSITE; PS50864; SAND; 1. DR PROSITE; PS01360; ZF_MYND_1; 1. DR PROSITE; PS50865; ZF_MYND_2; 1. KW Nuclear protein; DNA-binding; Transcription regulation; KW Trans-acting factor; Zinc-finger. FT DOMAIN 62 208 GLY-RICH. FT DOMAIN 210 291 SAND. FT DOMAIN 324 340 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT ZN_FING 521 557 MYND-TYPE. FT DOMAIN 36 43 POLY-HIS. FT DOMAIN 140 145 POLY-GLN. FT DOMAIN 342 365 ASN-RICH. SQ SEQUENCE 576 AA; 61597 MW; 2D6EB582685D65BB CRC64; MEQVDSSTEL HLNRKDLAAL AEDVVKEEVI LESSSHHHHH HHHQLDTKVR MVTSSSNDNS GSGGASGGTS GAGGGNGGGG VVSVPVSLPI GSMITGTTFN VITPDQLPPH FKPMLCVDNN GYLSGSTVSM GNDLKTIVIQ QQQTQPGGGG GGANNAGTNT TATNTIGLNH DGSGSNNSHD SLATLEHAAG GASGVGGGGG GTGGGSSGWS ENPSTQHNEV FQIRCKTTCA ELYRSKLGSG GRGRCVKYKD KWHTPSEFEH VCGRGSSKDW KRSIKYGGKS LQSLIDEGTL TPHATNCSCT VCCDDEAGES ASGPVRLFTP YKRRKRNQTD LDMESGPKRK RNTHHSNNNN SNTNNNNTSG SGANNCVDVT AAVAAATASV VDENNMFLSE ENITSKDEPW AALNDSLDTS TELVDQSQMG NTYERETFVV NINDGSSIAV LDTSQSMKNI EHVYCTMVKA TNDFKRMLND MKQSFERRIE VLQKERDAAV SAMRVQVHAD IDDPNISGSL HGNEIISAKK CANCNREALA ECSLCRKTPY CSEFCQRKDW NAHQVECTRN PQTTTQQVML LIDDQS // ID DECA_DROME STANDARD; PRT; 588 AA. AC P07713; P91651; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Decapentaplegic protein precursor (DPP-C protein). GN DPP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87090408; PubMed=3467201; RA Padgett R.W., St Johnston R.D., Gelbart W.M.; RT "A transcript from a Drosophila pattern gene predicts a protein RT homologous to the transforming growth factor-beta family."; RL Nature 325:81-84(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=DP CN BW; RX MEDLINE=97225213; PubMed=9071586; RA Richter B., Long M., Lewontin R.C., Nitasaka E.; RT "Nucleotide variation and conservation at the dpp locus, a gene RT controlling early development in Drosophila."; RL Genetics 145:311-323(1997). RN [3] RP CHARACTERIZATION, AND SEQUENCE OF 457-476. RX MEDLINE=90258853; PubMed=1692958; RA Panganiban G.E.F., Rashka K.E., Neitzel M.D., Hoffmann F.M.; RT "Biochemical characterization of the Drosophila dpp protein, a member RT of the transforming growth factor beta family of growth factors."; RL Mol. Cell. Biol. 10:2669-2677(1990). CC -!- FUNCTION: ACTS AS AN EXTRACELLULAR MORPHOGEN TO ESTABLISH AT LEAST CC TWO CELLULAR RESPONSE THRESHOLDS WITHIN THE DORSAL HALF OF THE CC DROSOPHILA EMBRYO. REQUIRED FOR THE PROPER DEVELOPMENT OF THE CC EMBRYONIC DORSAL HYPODERM, FOR VIABILITY OF LARVAE AND FOR CELL CC VIABILITY OF THE EPITHELIAL CELLS IN THE IMAGINAL DISKS. ACTS CC TOGETHER WITH SCW. CC -!- SUBUNIT: HETERODIMERS OF SCW/DPP ARE THE ACTIVE SUBUNIT, DPP/DPP CC HOMODIMERS ELICIT A BASAL RESPONSE AND SCW/SCW HOMODIMERS ALONE CC ARE INEFFECTIVE IN SPECIFYING A DORSAL PATTERN. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE IMAGINAL DISCS ASSOCIATED CC WITH ESTABLISHMENT OF THE PROXIMAL-DISTAL AXIS OF THE APPENDAGES, CC AND MIDGUT MESODERM. CC -!- SIMILARITY: BELONGS TO THE TGF-BETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30116; AAA28482.1; -. DR EMBL; U63857; AAC47552.1; -. DR PIR; A26158; A26158. DR HSSP; P12643; 3BMP. DR FlyBase; FBgn0000490; dpp. DR GO; GO:0005615; C:extracellular space; IDA. DR GO; GO:0005622; C:intracellular; IDA. DR GO; GO:0016015; F:morphogen activity; NAS. DR GO; GO:0005160; F:transforming growth factor-beta receptor bi...; NAS. DR GO; GO:0007378; P:amnioserosa formation; NAS. DR GO; GO:0007448; P:anterior/posterior pattern formation, imagi...; NAS. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0001715; P:ectoderm cell fate specification; NAS. DR GO; GO:0007483; P:genital disc metamorphosis; NAS. DR GO; GO:0007442; P:hindgut morphogenesis; IMP. DR GO; GO:0007560; P:imaginal disc morphogenesis; NAS. DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; NAS. DR GO; GO:0042127; P:regulation of cell proliferation; NAS. DR GO; GO:0019827; P:stem cell maintenance; NAS. DR GO; GO:0007179; P:TGFbeta receptor signaling pathway; NAS. DR GO; GO:0007425; P:tracheal cell fate determination (sensu Ins...; NAS. DR GO; GO:0008586; P:wing vein morphogenesis; IMP. DR GO; GO:0007474; P:wing vein specification; IMP. DR GO; GO:0007352; P:zygotic determination of dorsal/ventral axis; NAS. DR InterPro; IPR002405; Inhibin_alpha. DR InterPro; IPR001839; TGFb. DR InterPro; IPR001111; TGFb_N. DR Pfam; PF00019; TGF-beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR PRINTS; PR00669; INHIBINA. DR ProDom; PD000357; TGFb; 1. DR SMART; SM00204; TGFB; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. KW Growth factor; Developmental protein; Differentiation; Glycoprotein; KW Signal. FT SIGNAL 1 15 POTENTIAL. FT PROPEP 16 456 FT CHAIN 457 588 DECAPENTAPLEGIC PROTEIN. FT DISULFID 487 553 BY SIMILARITY. FT DISULFID 516 585 BY SIMILARITY. FT DISULFID 520 587 BY SIMILARITY. FT DISULFID 552 552 INTERCHAIN (BY SIMILARITY). FT CARBOHYD 120 120 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 342 342 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 377 377 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 529 529 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 59 59 V -> G (IN STRAIN DP CN BW). FT VARIANT 121 121 K -> M (IN STRAIN DP CN BW). FT VARIANT 473 474 HA -> QP (IN STRAIN DP CN BW). SQ SEQUENCE 588 AA; 65850 MW; 3D986A7DF5DF666B CRC64; MRAWLLLLAV LATFQTIVRV ASTEDISQRF IAAIAPVAAH IPLASASGSG SGRSGSRSVG ASTSTALAKA FNPFSEPASF SDSDKSHRSK TNKKPSKSDA NRQFNEVHKP RTDQLENSKN KSKQLVNKPN HNKMAVKEQR SHHKKSHHHR SHQPKQASAS TESHQSSSIE SIFVEEPTLV LDREVASINV PANAKAIIAE QGPSTYSKEA LIKDKLKPDP STLVEIEKSL LSLFNMKRPP KIDRSKIIIP EPMKKLYAEI MGHELDSVNI PKPGLLTKSA NTVRSFTHKD SKIDDRFPHH HRFRLHFDVK SIPADEKLKA AELQLTRDAL SQQVVASRSS ANRTRYQVLV YDITRVGVRG QREPSYLLLD TKTVRLNSTD TVSLDVQPAV DRWLASPQRN YGLLVEVRTV RSLKPAPHHH VRLRRSADEA HERWQHKQPL LFTYTDDGRH KARSIRDVSG GEGGGKGGRN KRHARRPTRR KNHDDTCRRH SLYVDFSDVG WDDWIVAPLG YDAYYCHGKC PFPLADHFNS TNHAVVQTLV NNMNPGKVPK ACCVPTQLDS VAMLYLNDQS TVVLKNYQEM TVVGCGCR // ID DEFI_DROME STANDARD; PRT; 92 AA. AC P36192; Q9V5F5; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Defensin precursor. GN DEF OR CG1385. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94222062; PubMed=8168509; RA Dimarcq J.L., Hoffmann D., Meister M., Bulet P., Lanot R., RA Reichhart J.-M., Hoffmann J.A.; RT "Characterization and transcriptional profiles of a Drosophila gene RT encoding an insect defensin. A study in insect immunity."; RL Eur. J. Biochem. 221:201-209(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RESPONSIBLE FOR THE ANTI GRAM-POSITIVE ACTIVITY OF CC IMMUNE HEMOLYMPH. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ARTHROPOD DEFENSIN FAMILY. SUBFAMILY 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z27247; CAA81760.1; -. DR EMBL; AE003831; AAF58855.1; -. DR PIR; S43228; S43228. DR HSSP; P10891; 1ICA. DR FlyBase; FBgn0010385; Def. DR GO; GO:0008224; F:Gram-positive antibacterial peptide activity; IDA. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IEP. DR InterPro; IPR001542; Defensin_anpod. DR InterPro; IPR003614; Knot1. DR Pfam; PF01097; Arthro_defensin; 1. DR PRINTS; PR00271; DEFENSIN. DR SMART; SM00505; Knot1; 1. DR PROSITE; PS00425; ARTHROPOD_DEFENSINS; 1. KW Insect immunity; Antibiotic; Signal; Defensin. FT SIGNAL 1 20 POTENTIAL. FT PROPEP 21 52 FT CHAIN 53 92 DEFENSIN. FT DISULFID 55 82 BY SIMILARITY. FT DISULFID 68 88 BY SIMILARITY. FT DISULFID 72 90 BY SIMILARITY. SQ SEQUENCE 92 AA; 10190 MW; 3E092BBAC640EDF6 CRC64; MKFFVLVAIA FALLACVAQA QPVSDVDPIP EDHVLVHEDA HQEVLQHSRQ KRATCDLLSK WNWNHTACAG HCIAKGFKGG YCNDKAVCVC RN // ID DEI_DROME STANDARD; PRT; 360 AA. AC P41894; Q9VBF2; DT 01-NOV-1995 (Rel. 32, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Helix-loop-helix protein delilah. GN DEI OR CG5441. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Epidermis; RX MEDLINE=94254871; PubMed=8196652; RA Armand P., Knapp A.C., Hirsch A.J., Wieschaus E.F., Cole M.D.; RT "A novel basic helix-loop-helix protein is expressed in muscle RT attachment sites of the Drosophila epidermis."; RL Mol. Cell. Biol. 14:4145-4154(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLY PLAYS AN IMPORTANT ROLE IN THE DIFFERENTIATION CC OF EPIDERMAL CELLS INTO THE TENDON CELLS THAT FORM THE ATTACHMENT CC SITES FOR ALL MUSCLES. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN, POSSIBLY WITH DAUGHTERLESS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: EXPRESSED ALMOST EXCLUSIVELY IN THE EPIDERMAL CC ATTACHMENTS SITES FOR THE SOMATIC MUSCLES. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L33401; AAA28449.1; -. DR EMBL; AE003756; AAF56590.1; ALT_SEQ. DR PIR; A56066; A56066. DR HSSP; P10085; 1MDY. DR TRANSFAC; T01653; -. DR FlyBase; FBgn0008649; dei. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Developmental protein; Nuclear protein; DNA-binding; KW Transcription regulation. FT DNA_BIND 94 106 BASIC DOMAIN. FT DOMAIN 107 154 HELIX-LOOP-HELIX MOTIF. FT CONFLICT 244 250 IGSPASS -> DWIACLL (IN REF. 1). FT CONFLICT 356 356 A -> P (IN REF. 1). SQ SEQUENCE 360 AA; 38996 MW; 9F731866E025F866 CRC64; MKSNTYELHN YADLNDMARA TDSKDSRKRK TASARGEKYS LRQKRQKRGS NEDGESANLA DFQLELDPIA EPASKSRKNA PTKSKTKAPP LSKYRRKTAN ARERTRMREI NTAFETLRHC VPEAIKGEDA ANTNEKLTKI TTLRLAMKYI TMLTDSIRDP SYESEFIGEC LEESANREAR VDLEANEEAE VELPVPVAKK PAKTKGSGKK SSAASKRQSQ KQAKIVPQIP PISSGESCYA TSSIGSPASS AYASLSSSSN SHSSSSSPGL ELDSLVGLNG ISALDSLLLD TSDGDSLSCL SPGYGSLLTG SGESLLPGCR GDLPMSGLEK SDVELSLRLL DQRFQGFLRL CQRSAAVGLY // ID DEJP_DROME STANDARD; PRT; 31 AA. AC P81160; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ductus ejaculatorius peptide 99B. GN DUP99B. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE OF 1-24 FROM N.A., AND SEQUENCE OF 9-31. RC STRAIN=Oregon-R; TISSUE=Ductus ejaculatorius; RX MEDLINE=21835775; PubMed=11846801; RA Saudan P., Hauck K., Soller M., Choffat Y., Ottiger M., Sporri M., RA Ding Z., Hess D., Gehrig P.M., Klauser S., Hunziker P., Kubli E.; RT "Ductus ejaculatorius peptide 99B (DUP99B), a novel Drosophila RT melanogaster sex-peptide pheromone."; RL Eur. J. Biochem. 269:989-997(2002). CC -!- FUNCTION: INDUCES POST-MATING RESPONSES. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: DUCTUS EJACULATORIUS. CC -!- SIMILARITY: TO PARAGONIAL PEPTIDE B. DR FlyBase; FBgn0024381; Dup99B. DR GO; GO:0045434; P:negative regulation of female receptivity, ...; IMP. DR GO; GO:0046662; P:regulation of oviposition; NAS. KW Behavior; Glycoprotein; Pyrrolidone carboxylic acid. FT MOD_RES 1 1 PYRROLIDONE CARBOXYLIC ACID. FT DISULFID 19 31 FT CARBOHYD 4 4 N-LINKED (GLCNAC...). SQ SEQUENCE 31 AA; 3766 MW; B90A9B99C120EF49 CRC64; QDRNDTEWIQ SQKDREKWCR LNLGPYLGGR C // ID DGRE_DROME STANDARD; PRT; 501 AA. AC O44424; Q8T9F3; Q9W3F2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DGCR14 protein homolog (ES2 protein) (dES2). GN ES2 OR CG1474. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 88-501 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=98167847; PubMed=9499415; RA Lindsay E.A., Harvey E.L., Scambler P.J., Baldini A.B.; RT "ES2, a gene deleted in DiGeorge syndrome, encodes a nuclear protein RT and is expressed during early mouse development, where it shares an RT expression domain with a Goosecoid-like gene."; RL Hum. Mol. Genet. 7:629-635(1998). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE DGCR14 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003444; AAF46375.1; -. DR EMBL; AY069792; AAL39937.1; -. DR EMBL; AF037257; AAC04785.1; -. DR FlyBase; FBgn0023506; Es2. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0007399; P:neurogenesis; ISS. KW Nuclear protein. FT CONFLICT 142 142 R -> W (IN REF. 2). FT CONFLICT 166 167 KL -> NV (IN REF. 3). FT CONFLICT 381 383 RNQ -> PNP (IN REF. 3). FT CONFLICT 469 469 S -> N (IN REF. 3). SQ SEQUENCE 501 AA; 56019 MW; 796B217E368AB78F CRC64; MSATTRTPAT PGTPGTPGSL AMEVARVQNS ALAEFKKPTA MVRHKNKPKI LTEEKYIEEM SKIIQRDFFP DLERLRAQND YLDAESRRDF VQMAEIRERY SLGRISGTGR STSRRNNAMS PATFETPVSQ AKCSNTPLPN SRATDTPFST DGSEKSDAEG RDTTAKLSLD AFLQKYTSED NQSFQEIIET AEAKLRQKYA VLYNHEKLSA EQLQRALMLP SIETQFEEPD PLRKIETWNY TNMNSIMYVP DGVEYTEEER VQLAERKQSI QHNATRLPDE AKHREMDTKK LNDEVPQNGA GGATATPKVR GFDLLRSPSP RPGEAFSPIM TWGEIDGTPF RLDGGDTPLR PTQGPSFRIN ENSRRENIAI ALAERVSERM RNQKQMALDT ARRNIGSPLI RTNMERLASM SPAAQLLATG KLGIRGTPRL RHTPSPMSGR KRKVTPGVVR STNTPILGEP KPKQQAKIST PAKNVTIDTG STLTDDLLKI PTKRRTAADF F // ID DHE3_DROME STANDARD; PRT; 562 AA. AC P54385; P91624; Q8IH05; Q9VCF7; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutamate dehydrogenase, mitochondrial precursor (EC 1.4.1.3) (GDH). GN GDH OR GLUD OR CG5320. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS A AND C), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=20449154; PubMed=10992165; RA Papadopoulou D., Louis C.; RT "The glutamate dehydrogenase gene of Drosophila melanogaster: RT molecular analysis and expression."; RL J. Neurogenet. 14:125-143(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS A AND C). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP CHARACTERIZATION. RX MEDLINE=82283850; PubMed=6810872; RA Caggese C., De Pinto V., Ferrandino A.; RT "Purification and genetic control of NAD-dependent glutamate RT dehydrogenase from Drosophila melanogaster."; RL Biochem. Genet. 20:449-460(1982). CC -!- CATALYTIC ACTIVITY: L-GLUTAMATE + H(2)O + NAD(P)(+) = 2- CC OXOGLUTARATE + NH(3) + NAD(P)H. CC -!- SUBUNIT: HOMOHEXAMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=Long; CC IsoId=P54385-1; Sequence=Displayed; CC Name=C; Synonyms=Short; CC IsoId=P54385-2; Sequence=VSP_001285; CC -!- TISSUE SPECIFICITY: EXPRESSED THROUGHOUT THE EMBRYO DURING EARLY CC STAGES BEFORE BECOMING LOCALISED IN MESODERMAL TISSUE BY STAGE 8. CC AT STAGE 12 EXPRESSION IS CONCENTRATED IN THE POSTERIOR MIDGUT. CC AFTER STAGE 13 EXPRESSION IT IS FOUND IN THE ANTERIOR AND CC POSTERIOR MIDGUT, THE HINDGUT, FAT BODY, MUSCLE, AND CENTRAL CC NERVOUS SYSTEM. IN 3RD INSTAR LARVAE EXPRESSION IS FOUND IN THE CC LEG DISKS, THE WING POUCH OF THE WING DISK, THE EYE-ANTENNA DISK, CC AND THE DEVELOPING BRAIN MEDULLA. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT ALL STAGES. CC -!- SIMILARITY: BELONGS TO THE GLU/LEU/PHE/VAL DEHYDROGENASES FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11314; CAA72173.1; -. DR EMBL; Z29062; CAA82304.1; -. DR EMBL; AE003745; AAF56209.4; ALT_SEQ. DR EMBL; AY061323; AAL28871.1; -. DR EMBL; BT001501; AAN71256.1; ALT_INIT. DR HSSP; P00366; 1HWX. DR FlyBase; FBgn0001098; Gdh. DR InterPro; IPR006095; GLFV_dehydrog. DR InterPro; IPR006096; GLFV_dehydrog_C. DR InterPro; IPR006097; GLFV_dehydrog_N. DR Pfam; PF00208; GLFV_dehydrog; 1. DR Pfam; PF02812; GLFV_dehydrog_N; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. KW Oxidoreductase; NAD; Mitochondrion; Transit peptide; KW Alternative splicing. FT TRANSIT 1 53 MITOCHONDRION (POTENTIAL). FT CHAIN 54 562 GLUTAMATE DEHYDROGENASE. FT ACT_SITE 174 174 BY SIMILARITY. FT VARSPLIC 460 472 Missing (in isoform C). FT /FTId=VSP_001285. FT CONFLICT 6 180 MISSING (IN REF. 4; AAN71256). FT CONFLICT 11 15 GARRQ -> APAAR (IN REF. 1). SQ SEQUENCE 562 AA; 62536 MW; 687A183D3BC0211F CRC64; MYHLKSLARQ GARRQQELAT LAKALPTAVM QSSRGYATEH QIPDRLKDVP TAKDPRFFDM VEYFFHRGCQ IAEESLVDDM KGKLTRDEKK QKVKGILMLM QPCDHIIEIA FPLRRDAGNY EMITGYRAQH STHKTPTKGG IRFSLDVSRD EVKALSALMT FKCACVDVPF GGAKAGLKIN PKEYSEHELE KITRRFTLEL AKKGFIGPGV DVPAPDMGTG EREMSWIADT YAKTIGHLDI NAHACVTGKP INQGGIHGRV SATGRGVFHG LENFINEANY MSQIGTTPGW GGKTFIVQGF GNVGLHTTRY LTRAGATCIG VIEHDGTLYN PEGIDPKLLE DYKNEHGTIV GYQNAKPYEG ENLMFEKCDI FIPAAVEKVI TSENANRIQA KIIAEAANGP TTPAADKILI DRNILVIPDL YINAGGVTVS FFEWLKNLNH VSYGRLTFKY ERESNYHLLA SVQQSIERII NDESVQESLE RRFGRVGGRI PVTPSESFQK RISGASEKDI VHSGLDYTME RSARAIMKTA MKYNLGLDLR TAAYVNSIEK IFTTYRDAGL AF // ID DHGL_DROME STANDARD; PRT; 625 AA. AC P18173; Q9VI87; DT 01-NOV-1990 (Rel. 16, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glucose dehydrogenase [acceptor] precursor (EC 1.1.99.10) [Contains: DE Glucose dehydrogenase [acceptor] short protein]. GN GLD OR CG1152. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90205602; PubMed=2108306; RA Krasney P.A., Carr C.M., Cavener D.R.; RT "Evolution of the glucose dehydrogenase gene in Drosophila."; RL Mol. Biol. Evol. 7:155-177(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-96 FROM N.A. RX MEDLINE=89065357; PubMed=3143620; RA Whetten R., Organ E., Krasney P., Cox-Foster D., Cavener D.R.; RT "Molecular structure and transformation of the glucose dehydrogenase RT gene in Drosophila melanogaster."; RL Genetics 120:475-484(1988). RN [4] RP SIMILARITY TO YEAST ALCOHOL OXIDASE. RX MEDLINE=91163320; PubMed=2002763; RA Cavener D.R., Krasney P.; RT "Drosophila glucose dehydrogenase and yeast alcohol oxidase are RT homologous and share N-terminal homology with other flavoenzymes."; RL Mol. Biol. Evol. 8:144-150(1991). RN [5] RP SELENOCYSTEINE. RA Perlaky S., Merritt K., Cavener D.; RT "Incorporation of selenocysteine at a UGA codon of Gld."; RL (In) 39th Annual Drosophila Research Conference, pp.39:414C-414C, RL Washington D.C. (1998). CC -!- FUNCTION: ESSENTIAL FOR CUTICULAR MODIFICATION DURING DEVELOPMENT. CC -!- CATALYTIC ACTIVITY: D-GLUCOSE + ACCEPTOR = D-GLUCONO-1,5-LACTONE + CC REDUCED ACCEPTOR. CC -!- COFACTOR: FAD. CC -!- SUBCELLULAR LOCATION: SECRETED AS PART OF THE SEMINAL FLUID CC TRANSFERRED TO FEMALES. CC -!- SIMILARITY: BELONGS TO THE GMC OXIDOREDUCTASE FAMILY. CC -!- CAUTION: REF.5 BELIEVES RESIDUE 613 IS A SELENOCYSTEINE. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M29298; AAA28571.1; ALT_SEQ. DR EMBL; AE003672; AAF54038.1; ALT_SEQ. DR EMBL; X13582; CAA31918.1; -. DR PIR; A39019; A39019. DR FlyBase; FBgn0001112; Gld. DR InterPro; IPR000172; GMC_oxred. DR InterPro; IPR007867; GMC_oxred_C. DR Pfam; PF05199; GMC_oxred_C; 1. DR Pfam; PF00732; GMC_oxred_N; 1. DR PROSITE; PS00623; GMC_OXRED_1; 1. DR PROSITE; PS00624; GMC_OXRED_2; 1. KW Oxidoreductase; Flavoprotein; FAD; Signal; Selenium; Selenocysteine. FT SIGNAL 1 42 FT CHAIN 43 625 GLUCOSE DEHYDROGENASE [ACCEPTOR]. FT CHAIN 43 612 GLUCOSE DEHYDROGENASE [ACCEPTOR] SHORT FT PROTEIN. FT NP_BIND 66 95 FAD (ADP PART) (PROBABLE). FT ACT_SITE 549 549 POTENTIAL. FT SE_CYS 613 613 PROBABLE. FT CONFLICT 484 484 Q -> R (IN REF. 1). SQ SEQUENCE 625 AA; 68387 MW; 02664FC3B820EDFC CRC64; MSASASACDC LVGVPTGPTL ASTCGGSAFM LFMGLLEVFI RSQCDLEDPC GRASSRFRSE PDYEYDFIVI GGGSAGSVVA SRLSEVPQWK VLLIEAGGDE PVGAQIPSMF LNFIGSDIDY RYNTEPEPMA CLSSMEQRCY WPRGKVLGGT SVLNGMMYVR GNREDYDDWA ADGNPGWAYN DVLPFFKKSE DNLDLDEVGT EYHAKGGLLP VGKFPYNPPL SYAILKAGEE LGFSVHDLNG QNSTGFMIAQ MTARNGIRYS SARAFLRPAR MRNNLHILLN TTATKILIHP HTKNVLGVEV SDQFGSTRKI LVKKEVVLSA GAVNSPHILL LSGVGPKDEL QQVNVRTVHN LPGVGKNLHN HVTYFTNFFI DDADTAPLNW ATAMEYLLFR DGLMSGTGIS DVTAKLATRY ADSPERPDLQ LYFGGYLASC ARTGQVGELL SNNSRSIQIF PAVLNPRSRG FIGLRSADPL EPPRIVANYL THEQDVKTLV EGIKFVIRLS QTTPLKQYGM RLDKTVVKGC EAHAFGSDAY WECAVRQNTG PENHQAGSCK MGPSHDPMAV VNHELRVHGI RGLRVMDTSI MPKVSSGNTH APAVMIAEKG AYLLKRAWGA KVCRVDATWT LHRVI // ID DHSA_DROME STANDARD; PRT; 661 AA. AC Q94523; Q9I7G3; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Succinate dehydrogenase [ubiquinone] flavoprotein subunit, DE mitochondrial precursor (EC 1.3.5.1) (FP) (Flavoprotein subunit of DE complex II). GN SCS-FP OR CG17246. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 6-527 FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). CC -!- CATALYTIC ACTIVITY: SUCCINATE + UBIQUINONE = FUMARATE + UBIQUINOL. CC -!- COFACTOR: FAD (BY SIMILARITY). CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE. CC -!- SUBUNIT: COMPLEX CONTAINING AT LEAST FOUR DIFFERENT SUBUNITS: A CC FLAVOPROTEIN, AN IRON-SULFUR, AND TWO HYDROPHOBIC ANCHOR PROTEINS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FAD-DEPENDENT OXIDOREDUCTASE FAMILY 2. CC FRD/SDH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003796; AAM70849.1; -. DR EMBL; AY051472; AAK92896.1; -. DR EMBL; Y09064; CAA70285.1; ALT_INIT. DR HSSP; P00363; 1FUM. DR FlyBase; FBgn0017539; Scs-fp. DR InterPro; IPR003953; FAD_bind2. DR InterPro; IPR001327; FAD_pyr_redox. DR InterPro; IPR003952; FRD/SDH_FAD_BS. DR InterPro; IPR004112; Succ_DH_flav_C. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; succ_DH_flav_C; 1. DR PRINTS; PR00368; FADPNR. DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1. KW Tricarboxylic acid cycle; Flavoprotein; FAD; Oxidoreductase; KW Electron transport; Mitochondrion; Transit peptide. FT TRANSIT 1 41 MITOCHONDRION (POTENTIAL). FT CHAIN 42 661 SUCCINATE DEHYDROGENASE [UBIQUINONE] FT FLAVOPROTEIN SUBUNIT. FT NP_BIND 61 75 FAD (AMP PART) (BY SIMILARITY). FT BINDING 96 96 FAD (COVALENT) (BY SIMILARITY). FT ACT_SITE 293 293 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT CONFLICT 207 207 S -> N (IN REF. 3). FT CONFLICT 251 251 I -> L (IN REF. 3). FT CONFLICT 503 503 Q -> L (IN REF. 3). FT CONFLICT 520 520 H -> L (IN REF. 3). SQ SEQUENCE 661 AA; 72343 MW; 301B578C7F765011 CRC64; MSGIMRVPSI LAKNAVASMQ RAAAVGVQRS YHITHGRQQA SAANPDKISK QYPVVDHAYD AIVVGAGGAG LRAAFGLVAE GFRTAVITKL FPTRSHTIAA QGGINAALGN MEEDDWKWHM YDTVKGSDWL GDQDAIHYMT REAPKAVIEL ENYGMPFSRT QDGKIYQRAF GGQSLKFGKG GQAHRCCAVA DRTGHSLLHT LYGQSLSYDC NYFVEYFALD LIFEDGECRG VLALNLEDGT LHRFRAKNTV IATGGYGRAF FSCTSAHTCT GDGTAMVARQ GLPSQDLEFV QFHPTGIYGA GCLITEGCRG EGGYLINGNG ERFMERYAPV AKDLASRDVV SRSMTIEIME GRGAGPEKDH VYLQLHHLPP KQLAERLPGI SETAMIFAGV DVTREPIPVL PTVHYNMGGV PTNYRGQVIT IDKDGKDVIV PGLYAAGEAA SSSVHGANRL GANSLLDLVV FGRACAKTIA ELNKPGAPAP TLKENAGEAS VANLDKLRHA NGQITTADLR LKMQKTMQHH AAVFRDGPIL QDGVNKMKEI YKQFKDIKVV DRSLIWNSDL VETLELQNLL ANAQMTIVSA EARKESRGAH AREDFKVRED EYDFSKPLDG QQKKPMDQHW RKHTLSWVCN DNGDITLDYR NVIDTTLDNE VSTVPPAIRS Y // ID DHSB_DROME STANDARD; PRT; 297 AA. AC P21914; Q9V9A0; DT 01-MAY-1991 (Rel. 18, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Succinate dehydrogenase [ubiquinone] iron-sulfur protein, DE mitochondrial precursor (EC 1.3.5.1) (IP). GN SDHB OR SDH OR CG3283. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95047485; PubMed=7958999; RA Au H.C., Scheffler I.E.; RT "Characterization of the gene encoding the iron-sulfur protein RT subunit of succinate dehydrogenase from Drosophila melanogaster."; RL Gene 149:261-265(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP PRELIMINARY SEQUENCE OF 113-258 FROM N.A. RX MEDLINE=89184541; PubMed=2494655; RA Gould S.J., Subramani S., Scheffler I.E.; RT "Use of the DNA polymerase chain reaction for homology probing: RT isolation of partial cDNA or genomic clones encoding the iron-sulfur RT protein of succinate dehydrogenase from several species."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989). RN [4] RP ERRATUM. RA Gould S.J., Subramani S., Scheffler I.E.; RL Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993). CC -!- CATALYTIC ACTIVITY: SUCCINATE + UBIQUINONE = FUMARATE + UBIQUINOL. CC -!- COFACTOR: BINDS THREE DIFFERENT IRON-SULFUR CLUSTERS: A 2FE-2S, CC A 3FE-4S AND A 4FE-4S (BY SIMILARITY). CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE. CC -!- SUBUNIT: COMPOSED OF A 27 KDA IRON PROTEIN (IP) AND A 70 KDA CC FLAVOPROTEIN (FP). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L27705; AAA61925.1; -. DR EMBL; AE003790; AAF57396.1; -. DR HSSP; P00364; 1FUM. DR FlyBase; FBgn0014028; SdhB. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001450; 4Fe4S_ferredoxin. DR InterPro; IPR004489; DhsB. DR InterPro; IPR001041; Ferredoxin. DR TIGRFAMs; TIGR00384; dhsB; 1. DR PROSITE; PS00197; 2FE2S_FERREDOXIN; 1. DR PROSITE; PS00198; 4FE4S_FERREDOXIN; 1. KW Tricarboxylic acid cycle; Metal-binding; Iron-sulfur; Iron; KW Oxidoreductase; Mitochondrion; Electron transport; 2Fe-2S; 3Fe-4S; KW 4Fe-4S; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 297 SUCCINATE DEHYDROGENASE [UBIQUINONE] FT IRON-SULFUR PROTEIN. FT METAL 100 100 IRON-SULFUR 1 (2FE-2S) (BY SIMILARITY). FT METAL 105 105 IRON-SULFUR 1 (2FE-2S) (BY SIMILARITY). FT METAL 108 108 IRON-SULFUR 1 (2FE-2S) (BY SIMILARITY). FT METAL 120 120 IRON-SULFUR 1 (2FE-2S) (BY SIMILARITY). FT METAL 195 195 IRON-SULFUR 2 (4FE-4S) (BY SIMILARITY). FT METAL 198 198 IRON-SULFUR 2 (4FE-4S) (BY SIMILARITY). FT METAL 201 201 IRON-SULFUR 2 (4FE-4S) (BY SIMILARITY). FT METAL 205 205 IRON-SULFUR 3 (3FE-4S) (BY SIMILARITY). FT METAL 252 252 IRON-SULFUR 3 (3FE-4S) (BY SIMILARITY). FT METAL 258 258 IRON-SULFUR 3 (3FE-4S) (BY SIMILARITY). FT METAL 262 262 IRON-SULFUR 2 (4FE-4S) (BY SIMILARITY). SQ SEQUENCE 297 AA; 33741 MW; 892380E8BAE08FFF CRC64; MLATEARQIL SRVGSLVARN QMRAISNGTA QLEQQAQPKE AQEPQIKKFE IYRWNPDNAG EKPYMQTYEV DLRECGPMVL DALIKIKNEM DPTLTFRRSC REGICGSCAM NIGGTNTLAC ISKIDINTSK SLKVYPLPHM YVVRDLVPDM NNFYEQYRNI QPWLQRKNEA GEKKGKAQYL QSVEDRSKLD GLYECILCAC CSTSCPSYWW NAEKYLGPAV LMQAYRWIID SRDENSAERL NKLKDPFSVY RCHTIMNCTR TCPKGLNPGR AIAEIKKLLS GLASKPAPKL ETAALHK // ID DIA_DROME STANDARD; PRT; 1091 AA. AC P48608; Q9VIJ7; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Diaphanous protein. GN DIA OR CG1768. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95121197; PubMed=7821209; RA Castrillon D.H., Wasserman S.A.; RT "Diaphanous is required for cytokinesis in Drosophila and shares RT domains of similarity with the products of the limb deformity gene."; RL Development 120:3367-3377(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=20214846; PubMed=10751177; RA Afshar K., Stuart B., Wasserman S.A.; RT "Functional analysis of the Drosophila diaphanous FH protein in early RT embryonic development."; RL Development 127:1887-1897(2000). CC -!- FUNCTION: REQUIRED FOR CYTOKINESIS IN BOTH MITOSIS AND MEIOSIS. CC HAS A ROLE IN ACTIN CYTOSKELETON ORGANIZATION AND IS ESSENTIAL FOR CC MANY, IF NOT ALL, ACTIN-MEDIATED EVENTS INVOLVING MEMBRANE CC INVAGINATION. MAY SERVE AS A MEDIATOR BETWEEN SIGNALING MOLECULES CC AND ACTIN ORGANIZERS AT SPECIFIC PHASES OF THE CELL CYCLE. CC POSSIBLE COMPONENT OF THE CONTRACTILE RING OR MAY CONTROL ITS CC FUNCTION. CC -!- SUBCELLULAR LOCATION: LOCALIZES TO THE SITE WHERE THE METAPHASE CC FURROW IS ANTICIPATED TO FORM, TO THE GROWING TIP OF CC CELLULARIZATION FURROWS, AND TO CONTRACTILE RINGS. CC -!- DOMAIN: DRFS ARE REGULATED BY INTRAMOLECULAR GBD-DAD BINDING WHERE CC RHO-GTP ACTIVATES THE DRFS BY DISRUPTING THE GBD-DAD INTERACTION CC (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 1 GTPASE-BINDING (GBD) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 FORMIN HOMOLOGY 1 (FH1) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 FORMIN HOMOLOGY 2 (FH2) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 FORMIN HOMOLOGY 3 (FH3) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 DRF AUTOREGULATORY (DAD) DOMAIN. CC -!- SIMILARITY: BELONGS TO THE FORMIN HOMOLOGY FAMILY. DIAPHANOUS CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11288; AAA67715.1; -. DR EMBL; AE003668; AAF53922.1; -. DR PIR; T13170; T13170. DR FlyBase; FBgn0011202; dia. DR InterPro; IPR003104; FH2. DR Pfam; PF02181; FH2; 1. DR SMART; SM00498; FH2; 1. KW Cell division; Coiled coil. FT DOMAIN 47 242 GBD. FT DOMAIN 143 448 FH3. FT DOMAIN 446 500 COILED COIL (POTENTIAL). FT DOMAIN 512 596 FH1 (PRO-RICH). FT DOMAIN 601 1044 FH2. FT DOMAIN 967 1021 COILED COIL (POTENTIAL). FT DOMAIN 1027 1041 DAD. FT DOMAIN 1050 1053 ARG-RICH (BASIC). FT DOMAIN 512 518 POLY-PRO. FT DOMAIN 519 522 POLY-GLY. FT DOMAIN 524 532 POLY-PRO. FT DOMAIN 539 548 POLY-PRO. FT DOMAIN 554 561 POLY-PRO. FT DOMAIN 566 572 POLY-PRO. FT DOMAIN 581 585 POLY-PRO. FT CONFLICT 733 733 H -> Q (IN REF. 1). SQ SEQUENCE 1091 AA; 123170 MW; A4379D7A089B5EE7 CRC64; MSRHEKTKST GGGLLDSLFG RPSKSKGGTI SSGTLAHGGR PVSADNYVVP GVEDFEQYIQ QLSVAELDAK FLEIIEDMNI PKDKREPLLA KSKEERQKMI MWHLKGKNSL ERSANSRFEK PIDYVEYLQN GEHSTHKVYQ CVESLRVALT SNPISWIKEF GVAGIGTIEK LLARSKNNAS YEKIEFEAIR CLKAIMNNTW GLNVVLNPDQ HSVVLLLAQS LDPRKPQTMC EALKLLASFC IVYERNGYEK VLRAITTIAA TSFKASERFR PIVDALFASD QQDPKRDLAC HSLIFINTLT NTPTDLNFRL HLRCEIMRMG LYDRLDEFTK IVEASNNENL QQHFKIFNEI REDDFEEFVQ RFDNVTFNMD DATDCFDVLK NLVTDTTSEP YFLSILQHLL YIRDDFYFRP AYYQLIEECI SQIVFHKGYC DPNFENRNFN IDTSLLLDDI VEKAKAKESK RSEEYEKKIE QLESAKQEAE AKAAHLEEKV KLMEANGVAA PSPNKLPKVN IPMPPPPPGG GGAPPPPPPP MPGRAGGGPP PPPPPPMPGR AGGPPPPPPP PGMGGPPPPP MPGMMRPGGG PPPPPMMMGP MVPVLPHGLK PKKKWDVKNP MKRANWKAIV PAKMSDKAFW VKCQEDKLAQ DDFLAELAVK FSSKPVKKEQ KDAVDKPTTL TKKNVDLRVL DSKTAQNLAI MLGGSLKHLS YEQIKICLLR CDTDILSSNI LQQLIQYLPP PEHLKRLQEI KAKGEPLPPI EQFAATIGEI KRLSPRLHNL NFKLTYADMV QDIKPDIVAG TAACEEIRNS KKFSKILELI LLLGNYMNSG SKNEAAFGFE ISYLTKLSNT KDADNKQTLL HYLADLVEKK FPDALNFYDD LSHVNKASRV NMDAIQKAMR QMNSAVKNLE TDLQNNKVPQ CDDDKFSEVM GKFAEECRQQ VDVLGKMQLQ MEKLYKDLSE YYAFDPSKYT MEEFFADIKT FKDAFQAAHN DNVRVREELE KKRRLQEARE QSAREQQERQ QRKKAVVDMD APQTQEGVMD SLLEALQTGS AFGQRNRQAR RQRPAGAERR AQLSRSRSRT RVTNGQLMTR EMILNEVLGS A // ID DICH_DROME STANDARD; PRT; 382 AA. AC Q24533; Q9VUD4; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SOX-domain protein dichaete (Fish-hook protein). GN D OR FISH OR SOX70D OR CG5893. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=97108761; PubMed=8951082; RA Russell S.R.H., Sanchez-Soriano N., Wright C.R., Ashburner M.; RT "The Dichaete gene of Drosophila melanogaster encodes a SOX-domain RT protein required for embryonic segmentation."; RL Development 122:3669-3676(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=97108741; PubMed=8951062; RA Nambu P.A., Nambu J.R.; RT "The Drosophila fish-hook gene encodes a HMG domain protein essential RT for segmentation and CNS development."; RL Development 122:3467-3475(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ESSENTIAL FOR SEGMENTATION AND CNS DEVELOPMENT. MAY CC MODULATE THE ACTIONS OF OTHER TRANSCRIPTION FACTORS, INCLUDING GAP CC AND PAIR-RULE PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: INITIALLY EXPRESSED IN A PAIR-RULE-LIKE CC PATTERN WHICH IS RAPIDLY REPLACED BY STRONG NEUROECTODERM CC EXPRESSION. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X96419; CAA65279.1; -. DR EMBL; U68056; AAB49673.1; -. DR EMBL; AE003535; AAF49753.1; -. DR HSSP; P48436; 1SX9. DR FlyBase; FBgn0000411; D. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW Developmental protein; DNA-binding; Nuclear protein. FT DNA_BIND 142 210 HMG BOX. FT DOMAIN 224 251 GLY-RICH. FT DOMAIN 293 298 POLY-ALA. SQ SEQUENCE 382 AA; 40212 MW; B03A267F9230A054 CRC64; MATLSTHPNY GFHLGQAQGL EDYAPQSQLQ LSPGMDMDIK RVLHYSQSLA AMGGSPNGPA GQGVNGSSGM GHHMSSHMTP HHMHQAVSAQ QTLSPNSSIG SAGSLGSQSS LGSNGSGLNS SSGHQSAGMH SLATSPGQEG HIKRPMNAFM VWSRLQRRQI AKDNPKMHNS EISKRLGAEW KLLAESEKRP FIDEAKRLRA LHMKEHPDYK YRPRRKPKNP LTAGPQGGLQ MQAGGMGQQK LGAGPGAGAG GYNPFHQLPP YFAPSHHLDQ GYPVPYFGGF DPLALSKLHQ SQAAAAAAVN NQGQQQGQAP PQLPPTSLSS FYSGIYSGIS APSLYAAHSA NAAGLYPSSS TSSPGSSPGT ITPNGMDGSM DSALRRPVPV LY // ID DIF_DROME STANDARD; PRT; 667 AA. AC P98149; Q9VJE2; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dorsal-related immunity factor Dif. GN DIF OR CG6794. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=94061992; PubMed=8242747; RA Ip Y.T., Reach M., Engstrom Y., Kadalayil L., Cai H., RA Gonzalez-Crespo S., Tatei K., Levine M.A.; RT "Dif, a dorsal-related gene that mediates an immune response in RT Drosophila."; RL Cell 75:753-763(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MEDIATES AN IMMUNE RESPONSE IN DROSOPHILA LARVAE. DIF CC BINDS TO THE KAPPA-B CONSENSUS SEQUENCE 5'-GGRNNYYCC-3', LOCATED CC IN THE ENHANCER REGION OF THE IMMUNITY GENE CECA1. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC; ACCUMULATES IN THE NUCLEUS UPON CC BACTERIAL INFECTION OF INJURY. CC -!- SIMILARITY: BELONGS TO THE REL/DORSAL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L29015; AAA28465.1; -. DR EMBL; AE003655; AAF53608.1; -. DR PIR; A49435; A49435. DR HSSP; Q00653; 1A3Q. DR FlyBase; FBgn0011274; Dif. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003700; F:transcription factor activity; IDA. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR002909; IPT_TIG. DR InterPro; IPR000451; NF_Rel_dor. DR InterPro; IPR008967; P53-like. DR Pfam; PF00554; RHD; 1. DR Pfam; PF01833; TIG; 1. DR PRINTS; PR00057; NFKBTNSCPFCT. DR SMART; SM00429; IPT; 1. DR PROSITE; PS01204; REL_1; 1. DR PROSITE; PS50254; REL_2; 1. KW Nuclear protein; DNA-binding; Transcription regulation; Activator; KW Phosphorylation. FT DOMAIN 78 372 REL-LIKE (RHD). FT DOMAIN 364 368 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT MOD_RES 343 343 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT DOMAIN 548 560 ASN-RICH. FT DOMAIN 582 622 GLN-RICH. FT CONFLICT 403 403 K -> T (IN REF. 1). SQ SEQUENCE 667 AA; 73935 MW; DB548B2AE35AC86C CRC64; MFEEAFGDIQ EIINASMELN GGATGGGSVA GAVGGGGAAH HILSQSTSLP VMPSHIPLHL QNQNMNQNLP EPSARSGPHL RIVEEPTSNI IRFRYKCEGR TAGSIPGMNS SSETGKTFPT IEVCNYDGPV IIVVSCVTSD EPFRQHPHWL VSKEEADACK SGIYQKKLPP EERRLVLQKV GIQCAKKLEM RDSLVERERR NIDPFNAKFD HKDQIDKINR YELRLCYQAF ITVGNSKVPL DPIVSSPIYG KSSELTITRL CSCAATANGG DEIIMLCEKI AKDDIEVRFY ETDKDGRETW FANAEFQPTD VFKQMAIAFK TPRYRNTEIT QSVNVELKLV RPSDGATSAP LPFEYYPNPE LLTKHNRRVA QKTVESLKRS LMSTNLHPSK QVKTSSQYTI FSKPQIATTT PQTQVSPGMP LMFPGGSPNF VQDIKMENGF MDVDSQSSQC PSVERNFASP RSNCSTVDSI PPMQMGQNQT HLYLPDATNF TFNGNFASPS SNCSTVDSIP PFQIGQRNNH MYLPENSNFP VNGCSPTHFS GGSMTPINNN NNVLINNNNN DFLSQKMSAI SIPPQGNFGI KQVYQQTQQF LPQLQPESIP YLAQSHPEQS QYQQQQQPQE QQPPADEPTQ SFSDLISSSI GMAPIDTSEL IQDIEAELNS LGIQPFK // ID DIP2_DROME STANDARD; PRT; 1773 AA. AC Q9W0S9; Q9NGP2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Disco-interacting protein 2. GN DIP2 OR CG7020. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Decroos F.C., Voas M.G., Rebay I.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP TISSUE SPECIFICITY, AND INTERACTION WITH DISCO. RX MEDLINE=22133306; PubMed=12137943; RA Mukhopadhyay M., Pelka P., DeSousa D., Kablar B., Schindler A., RA Rudnicki M.A., Campos A.R.; RT "Cloning, genomic organization and expression pattern of a novel RT Drosophila gene, the disco-interacting protein 2 (dip2), and its RT murine homolog."; RL Gene 293:59-65(2002). CC -!- FUNCTION: MAY PROVIDE POSITIONAL CUES FOR AXON PATHFINDING AND CC PATTERNING IN THE CENTRAL NERVOUS SYSTEM. CC -!- SUBUNIT: INTERACTS WITH DISCO. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: DEVELOPING NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: HIGHLY EXPRESSED IN THE CENTRAL NERVOUS CC SYSTEM (CNS) IN BOTH THE BRAIN LOBES AND THE VENTRAL CORD CC THROUGHOUT EMBRYOGENESIS, FROM EARLY STAGES OF NEUROGENESIS. CC EXPRESSED IN BOTH NEUROBLASTS AND NEURONS. EXPRESSED AT LOWER CC LEVEL IN THE VISCERAL MESODERM DURING STAGE 12. EXPRESSION OF DIP2 CC OVERLAPS WITH THAT OF DISCO IN THE VISCERAL MESODERM AND CNS. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 122. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF246991; AAF64300.1; ALT_FRAME. DR EMBL; AE003467; AAF47364.2; -. DR FlyBase; FBgn0024806; DIP2. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 4. KW Developmental protein; Nuclear protein. FT DOMAIN 56 59 POLY-PRO. FT DOMAIN 1089 1092 POLY-SER. FT DOMAIN 1700 1703 POLY-VAL. FT DOMAIN 1731 1737 POLY-VAL. FT CONFLICT 1038 1048 PLGGIHLCEAR -> LLGAYIYAKHG (IN REF. 1). SQ SEQUENCE 1773 AA; 194152 MW; 2A05C475B47DCF9A CRC64; MEHTASLPGY VREKLAELDL ELSEGDITQK GYEKKRAKLL QPFLKKPEGD KVKSTPPPPY YNVKNANNST NHGNINNDGV IVSSEGYSYV TEVPSLSSSQ QRHSKKIDFH QQAAMSLSSA PQSGNAGAPG YENMRPQGGA VGDPGYQNTR EPSAFQNQQS TNNSQHRQRR TQRKVTHNEK RYHSEVRQEA VQQALAALKG RPKPSLPMPS KRTSVLNRSP GCNDELDSST DDESIPEETI SPDKEYNYPR DHISNSILPP EPIIKPPIRE SSMGSQQHAR TDVKQNQITN QKYTAPNSAP ERRPPQNLPP LPTSEPLSSD YPPIAYKREN DFSDKAFKQK QYNAPDITQF NNAHRAADRV TRYVNVSQNE LNETDANGKW KVSAKIQQLL NTLKRPKRRP LPEFYEDNDI ELEIAANTKD PNAPKPEGST MTPVQGEQLS IPAGLPRTLE CALQRYGTNS FKSPMATVLD PNGKVTTTLT YGKLLSRAQK IAHALSTKIF SKGPEQVTLK PGDRVALVYP NNDPLSFITA WYGCMFRGLV PLPIELPLSS SDTPPQQVGF LLSSCGITVA LTSEACLKGL PKSTTTGEIA KLKGWPRLQW FVTEHLPKPP KEFNVGNLRA DDSAAAYIEY TTDKEGSVMG VTVTRAAMIN HCRALTMACH YTEGETIVCV LDFKREVGLW HSVLTSVLNG MHVIFIPYAL MKLRPSSWMQ LITKHRASCC LVKSRDLHWG LLATKDHKDI SLSSLRMLLV ADGANPWSLS SCDQFLSVFQ AKGLRSDAIC PCASSSEVFT VSLRRPGRGS CGFSPSATGR GVLSMAALSH GVVRVDSEDS LTSLTLQDCG QVMPAAQMVV VRSEGPPVLC KTDQVGEICV TSGSTSASYF GLDGMTNSTF KVQPLLEELE QPKDGNGTVN IISKPIGEDF YVRSGLLGFL GPGGLVFVCG SRDGLMTVTG RKHNADDIIA TVLAVEPMRF IYRGRIAVFS IKVLRDERVC VIAEQRPDCS EEESFQWMSR VLQAVDSIHQ VGIYCLALVP PNHLPKTPLG GIHLCEARRR FLEGSLHPAN VLMCPHTCVT NLPKPRELHQ GVQTAAKLSS SSGCGITDTG VGPASVMVGN LVQGNRLAEA HGRDVGLAED CERKPQLITG VLRWRANTSP DHIIFTLLNS KGAIAKTLTC SELHKRAEKI AALLQERGRI EPGDHVALIF PPGLDLLCAF YGCLYLGAIP ITIRPPHPQN LNTTLPTVRM IVDVSKSGIV LSIQPIIKLL KSREAATSID PKTWPPILDI DDNPKRKYAG IATVSFDSSA YLDFSVSTCG RLSGVNITHR SLSSLCASLK LACELYPSRH VALCLDPYCG LGFVMWTLIG VYSGHHSILI APYEVEANPS LWLSTLSQHR VRDTFCSYGV IELCTKALSN SIPSLKQRNI DLRCVRTCVV VAEERPRVQL TQQFCKLFQA LGLNTRCVST SFGCRVNPAI CVQGASSAES AQVYVDMRAL RNNRVALVER GAPNSLCVIE SGKLLPGVKV IIANPETKGH CGDSHLGEIW VQAPHNANGY FTIYGDETDY NDHFNAKLVT GATSELYART GYLGFLRRTE CSQSASLLDE TTPSVASRDS DTESLNSISQ LQLNFSNVSL GGNSEHSLVG GASNANDQEL HDAVYVVGAV DEVISLRGMN YHPIDIENSV MRCHKKIAEC AVFTWTNLLV VVVELDGNES EALDLVPLVT NTVLEDHQLI VGVVVVVDPG VVPINSRGEK QRMHLRDGFL ADQLDPIYVA YNM // ID DIP_DROME STANDARD; PRT; 106 AA. AC P24492; Q9V8P5; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Diptericin precursor. GN DPT OR DIPT OR CG12763. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=91093098; PubMed=2125051; RA Wicker C., Reichhart J.-M., Hoffmann D., Hultmark D., Samakovlis C., RA Hoffmann J.A.; RT "Insect immunity. Characterization of a Drosophila cDNA encoding a RT novel member of the diptericin family of immune peptides."; RL J. Biol. Chem. 265:22493-22498(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92224885; PubMed=1373375; RA Reichhart J.-M., Meister M., Dimarcq J., Zachary D., Hoffmann D., RA Ruiz C., Richards G., Hoffmann J.A.; RT "Insect immunity: developmental and inducible activity of the RT Drosophila diptericin promoter."; RL EMBO J. 11:1469-1477(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Various strains; RX MEDLINE=97476321; PubMed=9335607; RA Clark A.G., Wang L.; RT "Molecular population genetics of Drosophila immune system genes."; RL Genetics 147:713-724(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- DEVELOPMENTAL STAGE: CONSTITUTIVE EXPRESSION OF DIPTERICIN OCCURS CC IN EARLY PUPAE AND IN ADULTS. CC -!- INDUCTION: BY BACTERIAL INFECTION. CC -!- SIMILARITY: SOME TO ATTACINS, AND TO SARCOTOXINS II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M55432; AAA28466.1; -. DR EMBL; Z11728; CAA77791.1; -. DR EMBL; AF019020; AAB82517.1; -. DR EMBL; AF019022; AAB82519.1; -. DR EMBL; AF019023; AAB82520.1; -. DR EMBL; AF019025; AAB82522.1; -. DR EMBL; AF019026; AAB82523.1; -. DR EMBL; AF019027; AAB82524.1; -. DR EMBL; AF019028; AAB82525.1; -. DR EMBL; AF019029; AAB82526.1; -. DR EMBL; AF019031; AAB82528.1; -. DR EMBL; AE003798; AAF57619.1; -. DR PIR; S20878; S20878. DR FlyBase; FBgn0004240; Dpt. DR GO; GO:0008225; F:Gram-negative antibacterial peptide activity; IEP. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IEP. DR InterPro; IPR005521; Attacin_C. DR Pfam; PF03769; Attacin_C; 1. KW Insect immunity; Antibiotic; Hemolymph; Signal. FT SIGNAL 1 19 PROBABLE. FT PROPEP 20 23 REMOVED BY A DIPEPTIDYLPEPTIDASE FT (PROBABLE). FT CHAIN 24 106 DIPTERICIN. FT DOMAIN 30 37 PRO-RICH. FT DOMAIN 42 106 GLY-RICH. FT DOMAIN 42 46 POLY-GLY. SQ SEQUENCE 106 AA; 11314 MW; 9C498DF4A4DECEF7 CRC64; MQFTIAVALL CCAIASTLAY PMPDDMTMKP TPPPQYPLNL QGGGGGQSGD GFGFAVQGHQ KVWTSDNGRH EIGLNGGYGQ HLGGPYGNSE PSWKVGSTYT YRFPNF // ID DISC_DROME STANDARD; PRT; 568 AA. AC P23792; Q9VXJ4; DT 01-NOV-1991 (Rel. 20, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Disconnected protein. GN DISCO OR CG9908. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=91184126; PubMed=1901262; RA Heilig J.S., Freeman M., Laverty T., Lee K.J., Campos A.R., RA Rubin G.M., Steller H.; RT "Isolation and characterization of the disconnected gene of RT Drosophila melanogaster."; RL EMBO J. 10:809-815(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP DEVELOPMENTAL EXPRESSION. RX MEDLINE=91184127; PubMed=1901263; RA Lee K.J., Freeman M., Steller H.; RT "Expression of the disconnected gene during development of Drosophila RT melanogaster."; RL EMBO J. 10:817-826(1991). CC -!- FUNCTION: REQUIRED FOR THE ESTABLISHMENT OF STABLE CONNECTIONS CC BETWEEN THE LARVAL OPTIC NERVES, THE BOLWIG'S NERVES, AND THEIR CC TARGET CELLS IN THE BRAIN DURING EMBRYONIC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 2 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56232; CAA39689.1; -. DR EMBL; AE003501; AAF48568.1; -. DR PIR; S15008; S15008. DR FlyBase; FBgn0000459; disco. DR GO; GO:0008062; P:eclosion rhythm; IMP. DR GO; GO:0045475; P:locomotor rhythm; IMP. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. KW Developmental protein; Zinc-finger; Metal-binding; DNA-binding; KW Nuclear protein; Vision. FT ZN_FING 92 115 C2H2-TYPE 1. FT ZN_FING 120 145 C2H2-TYPE 2. FT DOMAIN 314 356 GLU/GLN-RICH. FT DOMAIN 499 557 GLN/HIS-RICH. FT MUTAGEN 94 94 C->Y: IN DISCO-1. FT MUTAGEN 127 127 C->S: IN DISCO-1656. FT CONFLICT 412 412 D -> E (IN REF. 1). SQ SEQUENCE 568 AA; 62369 MW; C875E72A2C2E644B CRC64; MEHIMNPFMS PAYLLGHGPH SHQHVHSHLP SHPQPNAASP ASSPGGSSGS GSGSAAGSGT GSGSSLKPRR WGSPPINLAG QFINPATGKK RVQCSICFKT FCDKGALKIH FSAVHLREMH KCTVEGCNMV FSSRRSRNRH SANPNPKLHS PHIRRKISPH DGRTAQQFPV FSPGTAAAAA AVAGRLPVAF PGLLPPPPPH HGHHPYVMFG GQAGLHGLGL LSTGCQDPDS GSVDNEQDAD PEDDNDFVYV DMQANSSSPA ASSEDQEEHE RDNEQDEEMH CSLSLASSSS IAADEERAAD QPLDFSLHKR RKSEQDREQE QEQEQERERE AEKEQEQDVE SDKEHEPEQE HELEREKRSP SDAFSMDQLL GKRKRHDSTA SSSACSTAAA SSASSSSASA SANPPQTSIK MDLDPDSDSA YMTSRRQMLP LPVLDLEEHH HLRLLQTQMF AAAAAAAATS QAPPTAFLPA GSPVDLAKDS PPMWSLLSEM YRSMLLKTQH QQYNHHHQLQ QQHQQEQHHH LTLSHHHQEQ HHHLGHHHMG HHHHHHHQHH QQQPQQQSPA ATNAPISV // ID DIUX_DROME STANDARD; PRT; 116 AA. AC Q9VLK4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Diuretic hormone class-II precursor (Diuretic peptide) (DP) (DH(31)). GN DH31 OR CG13094. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP FUNCTION, AND SYNTHESIS OF 76-106. RX MEDLINE=21216780; PubMed=11316500; RA Coast G.M., Webster S.G., Schegg K.M., Tobe S.S., Schooley D.A.; RT "The Drosophila melanogaster homologue of an insect calcitonin-like RT diuretic peptide stimulates V-ATPase activity in fruit fly Malpighian RT tubules."; RL J. Exp. Biol. 204:1795-1804(2001). CC -!- FUNCTION: REGULATION OF FLUID SECRETION. STIMULATES MALPIGHIAN CC TUBULES FLUID SECRETION BY ACTIVATING THE APICAL MEMBRANE V-ATPASE CC VIA CYCLIC AMP OF PRINCIPAL CELLS IN THE MAIN SECRETORY SEGMENT. CC -!- SUBCELLULAR LOCATION: SECRETED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE DIURETIC HORMONE CLASS II FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003621; AAF52685.1; -. DR FlyBase; FBgn0032048; Dh31. DR GO; GO:0008613; F:diuretic hormone activity; IDA. DR GO; GO:0007589; P:fluid secretion; IDA. KW Hormone; Amidation; Cleavage on pair of basic residues; Signal. FT SIGNAL 1 25 POTENTIAL. FT PROPEP 26 75 POTENTIAL. FT PEPTIDE 76 106 DIURETIC HORMONE CLASS-II. FT PROPEP 112 116 POTENTIAL. FT MOD_RES 106 106 AMIDATION (G-107 PROVIDE AMIDE GROUP) FT (POTENTIAL). SQ SEQUENCE 116 AA; 12622 MW; 1BE68AA1EAA8FA49 CRC64; MTNRCACFAL AFLLFCLLAI SSIEAAPMPS QSNGGYGGAG YNELEEVPDD LLMELMTRFG RTIIRARNDL ENSKRTVDFG LARGYSGTQE AKHRMGLAAA NFAGGPGRRR RSETDV // ID DJ60_DROME STANDARD; PRT; 217 AA. AC P92029; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DnaJ-like protein 60. GN DNAJ-60 OR DMJ60 OR DNAJ60 OR CG12240. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=98039457; PubMed=9372188; RA Iliopoulos I., Toeroek I., Mechler B.M.; RT "The DnaJ60 gene of Drosophila melanogaster encodes a new member of RT the DnaJ family of proteins."; RL Biol. Chem. 378:1177-1181(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY PLAY AN IMPORTANT FUNCTION DURING SPERMATOGENESIS CC AND/OR IN THE MALE GENITAL TRACT. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN TESTIS AND EJACULATORY CC BULB. CC -!- DEVELOPMENTAL STAGE: WEAKLY EXPRESSED IN EMBRYOS, LARVAE AND ADULT CC FEMALES. STRONG EXPRESSION IN ADULT MALES. CC -!- SIMILARITY: CONTAINS 1 J DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11900; CAA72641.1; -. DR EMBL; AE003463; AAF47174.1; -. DR FlyBase; FBgn0020129; DnaJ-60. DR InterPro; IPR001623; DnaJ_N. DR Pfam; PF00226; DnaJ; 1. DR SMART; SM00271; DnaJ; 1. DR PROSITE; PS00636; DNAJ_1; FALSE_NEG. DR PROSITE; PS50076; DNAJ_2; 1. KW Chaperone; Transmembrane; Spermatogenesis. FT DOMAIN 26 93 J-DOMAIN. FT TRANSMEM 141 161 POTENTIAL. SQ SEQUENCE 217 AA; 24780 MW; 5E2FF61832FFD0CC CRC64; MLRLCLPTRA GYVRNFSNDK PRKPETHYEV LNIRNDCSTR EVRNAFVQLS KLYHPDVKSN AACPERTARF VQISEAYKTL IKPERRRDYD DSLLWQPSRS DRSPVGETVN PGQAWDVRPN YDPNPGPYYG IRGLKRVSNW QVAVVLMALG FVGALFGFTS VRSSFKLSRQ IQDEISAEAN SHHAAVVADA QKYGNEEQVR RMVDRMSRSP FNQSSAK // ID DJ_DROME STANDARD; PRT; 248 AA. AC O01352; Q9VI50; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sperm-specific protein Don juan. GN DJ OR CG1980. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97376483; PubMed=9232593; RA Santel A., Winhauer T., Blumer N., Renkawitz-Pohl R.; RT "The Drosophila don juan (dj) gene encodes a novel sperm specific RT protein component characterized by an unusual domain of a repetitive RT amino acid motif."; RL Mech. Dev. 64:19-30(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Celniker S.E., George R.A., Galle R., Svirskas R.R., Hoskins R.A., RA Agbayani A., Arcaina T.T., Baxter E., Blazej R.G., Chavez C., Chew M., RA Doyle C.M., Farfan D.E., Flanagan J., Houston K.A., Hummasti S.R., RA Karra K., Kearney L., Kim S.H., Lee B., Lomotan M.A., Mak J., RA Mazda P., Mok M.S., Moshrefi A.R., Moshrefi M., Nixon K., Pacleb J.M., RA Park S., Pfeiffer B., Punch E., Snir E., Twomey B., Wan K.H., RA Whitelaw K.R., Yee A., Zhang R., Zieran L.L., Kimmel B.E.; RT "Sequencing of ANT-C antennapedia complex."; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: EXPRESSION LIMITED TO MALE GERM CELLS. CC -!- DEVELOPMENTAL STAGE: THE DJ PROTEIN OCCURS JUST POSTMEIOTICALLY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U90537; AAC05722.1; -. DR EMBL; AC004266; -; NOT_ANNOTATED_CDS. DR EMBL; AE003673; AAF54078.1; -. DR FlyBase; FBgn0019828; dj. KW Repeat. FT DOMAIN 147 194 8 X 6 AA TANDEM REPEAT OF D-P-C-K-K-K. FT REPEAT 147 152 1. FT REPEAT 153 158 2. FT REPEAT 159 164 3. FT REPEAT 165 170 4. FT REPEAT 171 176 5. FT REPEAT 177 182 6. FT REPEAT 183 188 7. FT REPEAT 189 194 8. FT CONFLICT 27 27 E -> D (IN REF. 1). FT CONFLICT 39 39 G -> R (IN REF. 1). SQ SEQUENCE 248 AA; 29127 MW; 5294BF0FF60E7361 CRC64; MFKRTALILR RCFQPTFIRP HHINVLENFK EADDLPNQGQ AKFVDVSIHD PQHIRSALVS PMQRKFLQDL EQQQTVRIKW FKEGNQDELE NMKNECRRLA LEIIMAAKGG DIKKACKELA EKEKCKQIEL KKKCKELEKK TKCAKKDPCK KKDPCKKKDP CKKKDPCKKK DPCKKKDPCK KKDPCKKKDP CKKKGGDLKK KCKKLAEKEK CKKLAKKEKM KKLQKKCKKM AQKEKCKKMA KKDKCKKK // ID DLG1_DROME STANDARD; PRT; 960 AA. AC P31007; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Discs large-1 tumor suppressor protein. GN DLG1 OR L(1)DLG1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC TISSUE=Embryo; RX MEDLINE=91330294; PubMed=1651169; RA Woods D.F., Bryant P.J.; RT "The discs-large tumor suppressor gene of Drosophila encodes a RT guanylate kinase homolog localized at septate junctions."; RL Cell 66:451-464(1991). CC -!- FUNCTION: PLAYS A CRITICAL ROLE AT SEPTATE JUNCTIONS IN CELLULAR CC GROWTH CONTROL DURING LARVAL DEVELOPMENT. THE PRESENCE OF A CC GUANYLATE KINASE DOMAIN SUGGESTS INVOLVEMENT IN CELLULAR ADHESION CC AS WELL AS SIGNAL TRANSDUCTION TO CONTROL CELLULAR PROLIFERATION. CC REQUIRED FOR MAINTENANCE OF CELL POLARITY. CC -!- SUBCELLULAR LOCATION: CYTOSKELETON-ASSOCIATED. LOCATED AT THE CC CYTOPLASMIC FACE OF THE MEMBRANE IN THE CELLULAR BLASTODERM AND CC BECOMES ASSOCIATED WITH SEPTATE JUNCTIONS WHICH BEGIN TO FORM CC BETWEEN EPITHELIAL CELLS AT THE TIME OF DORSAL CLOSURE. IN ADULT CC FLIES, LOCATED AT THE APICAL-LATERAL MEMBRANE BOUNDARY OF CC EPITHELIAL CELLS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced; CC Name=1; CC IsoId=P31007-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: IN EMBRYOS, EXPRESSION IS SEEN IN EPITHELIAL CC CELLS AND SOME NERVOUS TISSUE. IN LARVAE, EXPRESSION IS SEEN AS A CC BELT AROUND SALIVARY GLANDS AND IMAGINAL DISKS, ALSO IN CC PROVENTRICULUS AND PARTS OF THE BRAIN. EXPRESSED IN ADULT CC REPRODUCTIVE TISSUES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE MAGUK FAMILY. CC -!- SIMILARITY: CONTAINS 3 PDZ/DHR DOMAINS. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 GUANYLATE KINASE-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M73529; AAA28468.1; -. DR PIR; A39651; A39651. DR HSSP; P31016; 1BFE. DR FlyBase; FBgn0001624; dlg1. DR GO; GO:0045179; C:apical cortex; IDA. DR GO; GO:0016327; C:apicolateral plasma membrane; IDA. DR GO; GO:0005918; C:septate junction; NAS. DR GO; GO:0045175; P:basal protein localization; IMP. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0045197; P:establishment and/or maintenance of epithel...; NAS. DR GO; GO:0016334; P:establishment and/or maintenance of polarit...; IGI. DR GO; GO:0016336; P:establishment and/or maintenance of polarit...; NAS. DR GO; GO:0007399; P:neurogenesis; IMP. DR GO; GO:0007273; P:regulation of synapse; IMP. DR InterPro; IPR008144; Guanylate_kin. DR InterPro; IPR008145; Guanylt/Ca. DR InterPro; IPR001478; PDZ. DR InterPro; IPR001452; SH3. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF00595; PDZ; 3. DR Pfam; PF00018; SH3; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00228; PDZ; 3. DR SMART; SM00326; SH3; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 3. DR PROSITE; PS50002; SH3; 1. KW Transducer; SH3 domain; Alternative splicing; Repeat. FT DOMAIN 40 126 PDZ 1. FT DOMAIN 154 244 PDZ 2. FT DOMAIN 486 566 PDZ 3. FT DOMAIN 600 670 SH3. FT DOMAIN 768 960 GUANYLATE KINASE. SQ SEQUENCE 960 AA; 102468 MW; BF87A4262F1B6AD5 CRC64; MTTRKKKRDG GGSGGGFIKK VSSLFNLDSV NGDDSWLYED IQLERGNSGL GFSIAGGTDN PHIGTDTSIY ITKLISGGAA AADGRLSIND IIVSVNDVSV VDVPHASAVD ALKKAGNVVK LHVKRKRGTA TTPAAGSAAG DARDSAASGP KVIEIDLVKG GKGLGFSIAG GIGNQHIPGD NGIYVTKLTD GGRAQVDGRL SIGDKLIAVR TNGSEKNLEN VTHELAVATL KSITDKVTLI IGKTQHLTTS ASGGGGGGLS SGQQLSQSQS QLATSQSQSQ VHQQQHATPM VNSQSTGALN SMGQTVVDSP SIPQAAAAVA AAANASASAS VIASNNTISN TTVTTVTATA TASNDSSKLP PSLGANSSIS ISNSNSNSNS NNINNINSIN NNNSSSSSTT ATVAAATPTA ASAAAAAASS PPANSFYNNA SMPALPVESN QTNNRSQSPQ PRQPGSRYAS TNVLAAVPPG TPRAVSTEDI TREPRTITIQ KGPQGLGFNI VGGEDGQGIY VSFILAGGPA DLGSELKRGD QLLSVNNVNL THATHEEAAQ ALKTSGGVVT LLAQYRPEEY NRFEARIQEL KQQAALGAGG SGTLLRTTQK RSLYVRALFD YDPNRDDGLP SRGLPFKHGD ILHVTNASDD EWWQARRVLG DNEDEQIGIV PSKRRWERKM RARDRSVKFQ GHAAANNNLD KQSTLDRKKK NFTFSRKFPF MKSRDEKNED GSDQEPNGVV SSTSEIDINN VNNNQSNEPQ PSEENVLSYE AVQRLSINYT RPVIILGPLK DRINDDLISE YPDKFGSCVP HTTRPKREYE VDGRDYHFVS SREQMERDIQ NHLFIEAGQY NDNLYGTSVA SVREVAEKGK HCILDVSGNA IKRLQVAQLY PVAVFIKPKS VDSVMEMNRR MTEEQAKKTY ERAIKMEQEF GEYFTGVVQG DTIEEIYSKV KSMIWSQSGP TIWVPSKESL // ID DL_DROME STANDARD; PRT; 833 AA. AC P10041; Q99108; Q9VDY2; DT 01-MAR-1989 (Rel. 10, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Neurogenic locus Delta protein precursor. GN DL OR CG3619. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RA Vaessin H., Bremer K.A., Knust E., Campos-Ortega J.A.; RT "The neurogenic gene Delta of Drosophila melanogaster is expressed in RT neurogenic territories and encodes a putative transmembrane protein RT with EGF-like repeats."; RL EMBO J. 6:3431-3440(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=89196890; PubMed=3149249; RA Kopczynski C.C., Alton A.K., Fechtel K., Kooh P.J., Muskavitch M.A.T.; RT "Delta, a Drosophila neurogenic gene, is transcriptionally complex and RT encodes a protein related to blood coagulation factors and epidermal RT growth factor of vertebrates."; RL Genes Dev. 2:1723-1735(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 422-621 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=87218537; PubMed=3107986; RA Knust E., Dietrich U., Tepass U., Bremer K.A., Weigel D., Vaessin H., RA Campos-Ortega J.A.; RT "EGF homologous sequences encoded in the genome of Drosophila RT melanogaster, and their relation to neurogenic genes."; RL EMBO J. 6:761-766(1987). RN [5] RP PATTERN OF TRANSCRIPTION, AND CHARACTERIZATION. RX MEDLINE=91209246; PubMed=2128477; RA Haenlin M., Kramatschek B., Campos-Ortega J.A.; RT "The pattern of transcription of the neurogenic gene Delta of RT Drosophila melanogaster."; RL Development 110:905-914(1990). CC -!- FUNCTION: ESSENTIAL FOR PROPER DIFFERENTIATION OF ECTODERM. DL CC IS REQUIRED FOR THE CORRECT SEPARATION OF NEURAL AND EPIDERMAL CC CELL LINEAGES. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: DETECTED IN ALL AREAS WITH NEUROGENIC CC ABILITIES, FOR EXAMPLE THE NEUROGENIC ECTODERM AND THE PRIMORDIA CC OF THE SENSE ORGANS. LATER EXPRESSION IS RESTRICTED TO THOSE CELLS CC THAT HAVE ADOPTED A NEURAL FATE. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC EXPRESSION IS HIGHEST EARLY IN EMBRYONIC DEVELOPMENT (STAGE 5) AND CC REDUCES TO A LOW LEVEL DURING LARVAL STAGES. CC -!- MISCELLANEOUS: SEPARATION OF NEUROBLASTS FROM THE ECTODERM INTO CC THE INNER PART OF EMBRYO IS ONE OF THE FIRST STEPS OF CNS CC DEVELOPMENT IN INSECTS, THIS PROCESS IS UNDER CONTROL OF THE CC NEUROGENIC GENES. CC -!- MISCELLANEOUS: NOTCH AND SERRATE MAY INTERACT AT THE PROTEIN CC LEVEL, IT IS CONCEIVABLE THAT THE SERRATE AND DELTA PROTEINS MAY CC COMPETE FOR BINDING WITH THE NOTCH PROTEIN. CC -!- SIMILARITY: CONTAINS 9 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 DSL DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06289; CAA29617.1; -. DR EMBL; Y00222; CAA68369.1; -. DR EMBL; AE003725; AAF55657.1; -. DR EMBL; X05140; CAA28786.1; -. DR PIR; S00670; S00670. DR PIR; S19087; S19087. DR HSSP; P00740; 1EDM. DR FlyBase; FBgn0000463; Dl. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0005112; F:Notch binding; IDA. DR GO; GO:0007469; P:antennal morphogenesis; IMP. DR GO; GO:0007480; P:leg morphogenesis (sensu Holometabola); IMP. DR GO; GO:0007498; P:mesoderm development; IMP. DR GO; GO:0007219; P:N signaling pathway; NAS. DR GO; GO:0016318; P:ommatidial rotation; NAS. DR GO; GO:0007422; P:peripheral nervous system development; IMP. DR GO; GO:0045465; P:R8 differentiation; NAS. DR GO; GO:0045468; P:regulation of R8 spacing; NAS. DR GO; GO:0007424; P:tracheal system development (sensu Insecta); NAS. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR001774; DSL. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR001438; EGF_II. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR002049; Laminin_EGF. DR Pfam; PF01414; DSL; 1. DR Pfam; PF00008; EGF; 8. DR PRINTS; PR00010; EGFBLOOD. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00051; DSL; 1. DR SMART; SM00179; EGF_CA; 4. DR PROSITE; PS00010; ASX_HYDROXYL; 3. DR PROSITE; PS00022; EGF_1; 9. DR PROSITE; PS01186; EGF_2; 9. DR PROSITE; PS50026; EGF_3; 7. DR PROSITE; PS01187; EGF_CA; 2. KW Developmental protein; Differentiation; Neurogenesis; Repeat; KW Transmembrane; EGF-like domain; Glycoprotein; Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 833 NEUROGENIC LOCUS DELTA PROTEIN. FT DOMAIN 19 594 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 595 617 POTENTIAL. FT DOMAIN 618 833 CYTOPLASMIC (POTENTIAL). FT DOMAIN 164 226 DSL. FT DOMAIN 227 258 EGF-LIKE 1. FT DOMAIN 256 289 EGF-LIKE 2. FT DOMAIN 291 329 EGF-LIKE 3. FT DOMAIN 331 372 EGF-LIKE 4. FT DOMAIN 374 416 EGF-LIKE 5. FT DOMAIN 418 451 EGF-LIKE 6. FT DOMAIN 453 489 EGF-LIKE 7, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 491 527 EGF-LIKE 8. FT DOMAIN 529 565 EGF-LIKE 9, CALCIUM-BINDING (POTENTIAL). FT DISULFID 231 240 BY SIMILARITY. FT DISULFID 235 246 BY SIMILARITY. FT DISULFID 248 257 BY SIMILARITY. FT DISULFID 260 271 BY SIMILARITY. FT DISULFID 266 277 BY SIMILARITY. FT DISULFID 279 288 BY SIMILARITY. FT DISULFID 295 307 BY SIMILARITY. FT DISULFID 301 317 BY SIMILARITY. FT DISULFID 319 328 BY SIMILARITY. FT DISULFID 335 348 BY SIMILARITY. FT DISULFID 342 360 BY SIMILARITY. FT DISULFID 362 371 BY SIMILARITY. FT DISULFID 378 388 BY SIMILARITY. FT DISULFID 383 404 BY SIMILARITY. FT DISULFID 406 415 BY SIMILARITY. FT DISULFID 422 433 BY SIMILARITY. FT DISULFID 427 439 BY SIMILARITY. FT DISULFID 441 450 BY SIMILARITY. FT DISULFID 457 468 BY SIMILARITY. FT DISULFID 462 477 BY SIMILARITY. FT DISULFID 479 488 BY SIMILARITY. FT DISULFID 495 506 BY SIMILARITY. FT DISULFID 500 515 BY SIMILARITY. FT DISULFID 517 526 BY SIMILARITY. FT DISULFID 533 544 BY SIMILARITY. FT DISULFID 538 553 BY SIMILARITY. FT DISULFID 555 564 BY SIMILARITY. FT CARBOHYD 98 98 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 137 137 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 167 167 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 5 5 K -> N (IN REF. 1). FT CONFLICT 67 67 V -> L (IN REF. 1). FT CONFLICT 363 363 A -> R (IN REF. 1). FT CONFLICT 437 438 GK -> ET (IN REF. 3). FT CONFLICT 443 443 A -> S (IN REF. 1 AND 3). FT CONFLICT 459 459 G -> A (IN REF. 3). FT CONFLICT 490 490 S -> T (IN REF. 3). FT CONFLICT 591 591 T -> A (IN REF. 1 AND 3). FT CONFLICT 631 631 D -> N (IN REF. 1). FT CONFLICT 652 652 G -> A (IN REF. 1). FT CONFLICT 662 662 L -> M (IN REF. 1). FT CONFLICT 759 759 S -> T (IN REF. 1). FT CONFLICT 801 804 ACSS -> DLFI (IN REF. 1). FT CONFLICT 812 812 V -> A (IN REF. 2). FT CONFLICT 815 817 SGA -> TD (IN REF. 1). FT CONFLICT 833 833 M -> YVTPKIRKGSWEIRRNPHGGADSTYTKKRLGWVQNV FT RETPKMLLLIEAV (IN REF. 1). SQ SEQUENCE 833 AA; 88840 MW; EDBA107A0003D9A1 CRC64; MHWIKCLLTA FICFTVIVQV HSSGSFELRL KYFSNDHGRD NEGRCCSGES DGATGKCLGS CKTRFRVCLK HYQATIDTTS QCTYGDVITP ILGENSVNLT DAQRFQNKGF TNPIQFPFSF SWPGTFSLIV EAWHDTNNSG NARTNKLLIQ RLLVQQVLEV SSEWKTNKSE SQYTSLEYDF RVTCDLNYYG SGCAKFCRPR DDSFGHSTCS ETGEIICLTG WQGDYCHIPK CAKGCEHGHC DKPNQCVCQL GWKGALCNEC VLEPNCIHGT CNKPWTCICN EGWGGLYCNQ DLNYCTNHRP CKNGGTCFNT GEGLYTCKCA PGYSGDDCEN EIYSCDADVN PCQNGGTCID EPHTKTGYKC HCANGWSGKM CEEKVLTCSD KPCHQGICRN VRPGLGSKGQ GYQCECPIGY SGPNCDLQLD NCSPNPCING GSCQPSGKCI CPAGFSGTRC ETNIDDCLGH QCENGGTCID MVNQYRCQCV PGFHGTHCSS KVDLCLIRPC ANGGTCLNLN NDYQCTCRAG FTGKDCSVDI DECSSGPCHN GGTCMNRVNS FECVCANGFR GKQCDEESYD SVTFDAHQYG ATTQARADGL TNAQVVLIAV FSVAMPLVAV IAACVVFCMK RKRKRAQEKD DAEARKQNEQ NAVATMHHNG SGVGVALASA SLGGKTGSNS GLTFDGGNPN IIKNTWDKSV NNICASAAAA AAAAAAADEC LMYGGYVASV ADNNNANSDF CVAPLQRAKS QKQLNTDPTL MHRGSPAGSS AKGASGGGPG AAEGKRISVL GEGSYCSQRW PSLAAAGVAG ACSSQLMAAA SVAGSGAGTA QQQRSVVCGT PHM // ID DM10_DROME STANDARD; PRT; 54 AA. AC P40658; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SRY-related protein DM10 (Fragment). GN SRY-RDM10. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93184703; PubMed=8443573; RA Coriat A.M., Mueller U., Harry J.L., Uwanogho D., Sharpe P.T.; RT "PCR amplification of SRY-related gene sequences reveals evolutionary RT conservation of the SRY-box motif."; RL PCR Methods Appl. 2:218-222(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86328; AAA28469.1; -. DR HSSP; Q05066; 1HRY. DR FlyBase; FBgn0010271; Sry-rDM10. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW DNA-binding; Nuclear protein. FT NON_TER 1 1 FT DNA_BIND <1 >54 HMG BOX. FT NON_TER 54 54 SQ SEQUENCE 54 AA; 6516 MW; 1677E500C9343C66 CRC64; MAQENPKMHN SEISKRLGAE WKLLADSEKR PFIDEAKRLR ALHMKEYPNY KYRP // ID DM17_DROME STANDARD; PRT; 54 AA. AC P40659; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SRY-related protein DM17 (Fragment). GN SRY-RDM17. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93184703; PubMed=8443573; RA Coriat A.M., Mueller U., Harry J.L., Uwanogho D., Sharpe P.T.; RT "PCR amplification of SRY-related gene sequences reveals evolutionary RT conservation of the SRY-box motif."; RL PCR Methods Appl. 2:218-222(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86329; AAA28470.1; -. DR HSSP; Q05066; 1HRY. DR FlyBase; FBgn0010272; Sry-rDM17. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW DNA-binding; Nuclear protein. FT NON_TER 1 1 FT DNA_BIND <1 >54 HMG BOX. FT NON_TER 54 54 SQ SEQUENCE 54 AA; 6547 MW; B977E50775F98308 CRC64; MALENPKMHN SEISKRLGAE WKLLSEAEKR PYIDEAKRLR AQHMKEYPDY KYRP // ID DM23_DROME STANDARD; PRT; 54 AA. AC P40660; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SRY-related protein DM23 (Fragment). GN SRY-RDM23. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93184703; PubMed=8443573; RA Coriat A.M., Mueller U., Harry J.L., Uwanogho D., Sharpe P.T.; RT "PCR amplification of SRY-related gene sequences reveals evolutionary RT conservation of the SRY-box motif."; RL PCR Methods Appl. 2:218-222(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86330; AAA28471.1; -. DR HSSP; Q05066; 1HRY. DR FlyBase; FBgn0010273; Sry-rDM23. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW DNA-binding; Nuclear protein. FT NON_TER 1 1 FT DNA_BIND <1 >54 HMG BOX. FT NON_TER 54 54 SQ SEQUENCE 54 AA; 6473 MW; 1363E500C82ACD66 CRC64; MAQENPKMHN SEISKRLGAE WKLLAESEKR PFIDEAKRLR ALHMKAYPDY KYRP // ID DM33_DROME STANDARD; PRT; 54 AA. AC P40661; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SRY-related protein DM33 (Fragment). GN SRY-RDM33. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93184703; PubMed=8443573; RA Coriat A.M., Mueller U., Harry J.L., Uwanogho D., Sharpe P.T.; RT "PCR amplification of SRY-related gene sequences reveals evolutionary RT conservation of the SRY-box motif."; RL PCR Methods Appl. 2:218-222(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86331; AAA28472.1; -. DR HSSP; Q05066; 1HRY. DR FlyBase; FBgn0010274; Sry-rDM33. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW DNA-binding; Nuclear protein. FT NON_TER 1 1 FT DNA_BIND <1 >54 HMG BOX. FT NON_TER 54 54 SQ SEQUENCE 54 AA; 6491 MW; 420AB400C82AC00B CRC64; MAQENPKMHN SEISKRLGAE WKLLAESEKR PLIDEAKRLR ALHMNHYPDY KYRP // ID DM36_DROME STANDARD; PRT; 54 AA. AC P40662; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SRY-related protein DM36 (Fragment). GN SRY-RDM36. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93184703; PubMed=8443573; RA Coriat A.M., Mueller U., Harry J.L., Uwanogho D., Sharpe P.T.; RT "PCR amplification of SRY-related gene sequences reveals evolutionary RT conservation of the SRY-box motif."; RL PCR Methods Appl. 2:218-222(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86332; AAA28473.1; -. DR HSSP; Q05066; 1HRY. DR FlyBase; FBgn0010275; Sry-rDM36. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW DNA-binding; Nuclear protein. FT NON_TER 1 1 FT DNA_BIND <1 >54 HMG BOX. FT NON_TER 54 54 SQ SEQUENCE 54 AA; 6457 MW; 9E87EB8A33463F6A CRC64; MALENPKMQN SHISKRLGAE WKLLAASEKR PFIDEAKRLR ALHMKEYPDY KYRP // ID DM63_DROME STANDARD; PRT; 54 AA. AC P40663; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SRY-related protein DM63 (Fragment). GN SRY-RDM63. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93184703; PubMed=8443573; RA Coriat A.M., Mueller U., Harry J.L., Uwanogho D., Sharpe P.T.; RT "PCR amplification of SRY-related gene sequences reveals evolutionary RT conservation of the SRY-box motif."; RL PCR Methods Appl. 2:218-222(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86333; AAA28474.1; -. DR HSSP; Q05066; 1HRY. DR FlyBase; FBgn0010276; Sry-rDM63. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW DNA-binding; Nuclear protein. FT NON_TER 1 1 FT DNA_BIND <1 >54 HMG BOX. FT NON_TER 54 54 SQ SEQUENCE 54 AA; 6516 MW; 1677E5144EFF5456 CRC64; MALENPKMHN SEISKRLGAE WKLLAESEKR PFIDEAKRLR ALHMKEYPNY KYRP // ID DM64_DROME STANDARD; PRT; 54 AA. AC P40664; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SRY-related protein DM64 (Fragment). GN SRY-RDM64. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93184703; PubMed=8443573; RA Coriat A.M., Mueller U., Harry J.L., Uwanogho D., Sharpe P.T.; RT "PCR amplification of SRY-related gene sequences reveals evolutionary RT conservation of the SRY-box motif."; RL PCR Methods Appl. 2:218-222(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86334; AAA28475.1; -. DR HSSP; Q05066; 1HRY. DR FlyBase; FBgn0010277; Sry-rDM64. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW DNA-binding; Nuclear protein. FT NON_TER 1 1 FT DNA_BIND <1 >54 HMG BOX. FT NON_TER 54 54 SQ SEQUENCE 54 AA; 6562 MW; CEA26514521EEC6C CRC64; MALENPKMHN SEISKRLGAE WKDLSESEKR PFIDEAKRLR LVHMKEYPDY KYRP // ID DMYC_DROME STANDARD; PRT; 70 AA. AC P41964; Q9VZQ2; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Drosomycin precursor (Cysteine-rich peptide). GN DRS OR CRP OR CG10810. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 27-70. RC STRAIN=Oregon-R; RX MEDLINE=95105209; PubMed=7806546; RA Fehlbaum P., Bulet P., Michaut L., Lagueux M., Broekaert W.F., RA Hetru C., Hoffmann J.A.; RT "Insect immunity. Septic injury of Drosophila induces the synthesis RT of a potent antifungal peptide with sequence homology to plant RT antifungal peptides."; RL J. Biol. Chem. 269:33159-33163(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP CARBOHYDRATE-LINKAGE SITE ASN-42, MASS SPECTROMETRY, INDUCTION, AND RP TISSUE SPECIFICITY. RX MEDLINE=98409659; PubMed=9736738; RA Uttenweiler-Josepash S., Moniatte M., Lagueux M., Van Dorsselaer A., RA Hoffmann J.A., Bulet P.; RT "Differential display of peptides induced during the immune response RT of Drosophila: a matrix-assisted laser desorption ionization RT time-of-flight mass spectrometry study."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998). RN [4] RP STRUCTURE BY NMR. RX MEDLINE=97445602; PubMed=9300487; RA Landon C., Sodano P., Hetru C., Hoffmann J.A., Ptak M.; RT "Solution structure of drosomycin, the first inducible antifungal RT protein from insects."; RL Protein Sci. 6:1878-1884(1997). CC -!- FUNCTION: POSSESSES ANTIFUNGAL ACTIVITY AND IS ACTIVE AGAINST A CC RELATIVELY BROAD SPECTRUM OF FILAMENTOUS FUNGI. IT INHIBITS SPORE CC GERMINATION AT HIGH CONCENTRATIONS AND AT LOW CONCENTRATIONS CC DELAYS GROWTH OF HYPHAE WHICH SUBSEQUENTLY EXHIBIT ABNORMAL CC MORPHOLOGY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: SYNTHESIZED IN THE FAT BODY AND IS SECRETED CC INTO THE BLOOD. IN HEMOLYMPH 6 HOURS AFTER IMMUNE CHALLENGE, CC LEVELS OF EXPRESSION INCREASE FOR FIRST 24 HOURS AND PERSIST FOR CC THE FOLLOWING THREE WEEKS. CC -!- MASS SPECTROMETRY: MW=4889.5; METHOD=MALDI. CC -!- SIMILARITY: DISTANTLY RELATED TO THE PLANT DEFENSIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75595; CAA53267.1; -. DR EMBL; AE003478; AAF47767.1; ALT_INIT. DR PIR; A55824; A55824. DR PDB; 1MYN; 31-DEC-97. DR FlyBase; FBgn0010381; Drs. DR GO; GO:0003799; F:antifungal peptide activity; IDA. DR GO; GO:0006966; P:antifungal humoral response (sensu Inverteb...; IEP. DR InterPro; IPR008176; Gamma-thionin. DR InterPro; IPR003614; Knot1. DR Pfam; PF00304; Gamma-thionin; 1. DR ProDom; PD002594; G_Purothionin; 1. DR SMART; SM00505; Knot1; 1. KW Glycoprotein; Signal; Fungicide; 3D-structure. FT SIGNAL 1 20 POTENTIAL. FT PROPEP 21 26 FT CHAIN 27 70 DROSOMYCIN. FT DISULFID 28 70 FT DISULFID 37 59 FT DISULFID 45 65 FT DISULFID 49 67 FT CARBOHYD 42 42 N-LINKED (GLCNAC...). FT STRAND 28 29 FT TURN 39 41 FT HELIX 42 52 FT TURN 53 53 FT STRAND 56 59 FT TURN 61 62 FT STRAND 65 68 SQ SEQUENCE 70 AA; 7752 MW; 1A702E959ECEF181 CRC64; MMQIKYLFAL FAVLMLVVLG ANEADADCLS GRYKGPCAVW DNETCRRVCK EEGRSSGHCS PSLKCWCEGC // ID DNJ1_DROME STANDARD; PRT; 334 AA. AC Q24133; Q9VRP0; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DnaJ protein homolog 1 (DROJ1). GN DNAJ-1 OR DROJ1 OR CG10578. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Lee J.Y., Palter K.B.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- INDUCTION: BY HEAT SHOCK. CC -!- SIMILARITY: CONTAINS 1 J DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U34904; AAC23584.1; -. DR EMBL; AE003565; AAF50753.1; -. DR EMBL; AY058788; AAL14017.1; -. DR HSSP; P25685; 1HDJ. DR FlyBase; FBgn0015657; DnaJ-1. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001623; DnaJ_N. DR InterPro; IPR008971; HSP40_DnaJ_pep. DR InterPro; IPR003095; Hsp_DnaJ. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR PRINTS; PR00625; DNAJPROTEIN. DR SMART; SM00271; DnaJ; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. KW Chaperone; Heat shock. FT DOMAIN 4 68 J-DOMAIN. FT CONFLICT 261 261 G -> E (IN REF. 1). SQ SEQUENCE 334 AA; 37028 MW; 60542ABFD47A5689 CRC64; MGKDFYKILG LERKASDDEI KKAYRKLALK YHPDKNKSPQ AEERFKEIAE AYEVLSDKKK RDIFDNYGED GLKGGQPGPD GGGQPGAYTY QFHGDPRATF AQFFGSSDPF GAFFTGGDNM FSGGQGGNTN EIFWNIGGDD MFAFNAQAPS RKRQQDPPIE HDLFVSLEEV DKGCIKKMKI SRMATGSNGP YKEEKVLRIT VKPGWKAGTK ITFPQEGDSA PNKTPADIVF IIRDKPHSLF KREGIDLKYT AQISLKQALC GALVSVPTLQ GSRIQVNPNH EIIKPTTTRR INGLGLPVPK EPSRRGDLIV SFDIKFPDTL APSLQNQLSE LLPN // ID DNK_DROME STANDARD; PRT; 250 AA. AC Q9XZT6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Deoxynucleoside kinase (EC 2.7.1.145) (Deoxyribonucleoside kinase) DE (Dm-dNK) (Multispecific deoxynucleoside kinase). GN DNK OR CG5452. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=99377006; PubMed=10446143; RA Johansson M., Van Rompay A.R., Degreve B., Balzarini J., Karlsson A.; RT "Cloning and characterization of the multisubstrate RT deoxyribonucleoside kinase of Drosophila melanogaster."; RL J. Biol. Chem. 274:23814-23820(1999). RN [2] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Oregon-R; RX MEDLINE=20158988; PubMed=10692477; RA Munch-Petersen B., Knecht W., Lenz C., Sondergaard L., Piskur J.; RT "Functional expression of a multisubstrate deoxyribonucleoside kinase RT from Drosophila melanogaster and its C-terminal deletion mutants."; RL J. Biol. Chem. 275:6673-6679(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP ENZYME ACTIVITY. RX MEDLINE=98129796; PubMed=9461577; RA Munch-Petersen B., Piskur J., Sondergaard L.; RT "Four deoxynucleoside kinase activities from Drosophila melanogaster RT are contained within a single monomeric enzyme, a new multifunctional RT deoxynucleoside kinase."; RL J. Biol. Chem. 273:3926-3931(1998). CC -!- FUNCTION: DEOXYRIBONUCLEOSIDE KINASE THAT HAS A BROAD SPECIFICITY CC PHOSPHORYLATING THYMIDINE, DEOXYADENOSINE, DEOXYCYTIDINE AND CC DEOXYGUANOSINE. SPECIFICITY IS HIGHER FOR PYRIMIDINE NUCLEOSIDES. CC SEVERAL ANTI-VIRAL AND ANTI-CANCER NUCLEOSIDE ANALOGS ARE ALSO CC EFFICIENTLY PHOSPHORYLATED. CC -!- CATALYTIC ACTIVITY: ATP + 2'-DEOXYNUCLEOSIDE = ADP + 2'- CC DEOXYNUCLEOSIDE 5'-PHOSPHATE. CC -!- SUBUNIT: MONOMER. CC -!- MISCELLANEOUS: THE KM FOR THYMIDINE, DEOXYCYTIDINE, DEOXYADENOSINE CC AND DEOXYGUANOSINE ARE 0.9, 1, 109 AND 654 MICROMOL, AND THE VMAX CC IS 29.4, 28.7, 35.5 AND 37.7 MMOL/MIN X MG ENZYME, RESPECTIVELY. CC -!- SIMILARITY: BELONGS TO THE DCK/DGK FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF045610; AAD47355.2; -. DR EMBL; AF185268; AAD56545.1; -. DR EMBL; Y18048; CAB41881.1; -. DR EMBL; AE003724; AAF55615.1; -. DR PDB; 1J90; 28-NOV-01. DR FlyBase; FBgn0022338; dnk. DR GO; GO:0019136; F:deoxynucleoside kinase activity; IDA. DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IDA. DR InterPro; IPR002624; dNK. DR Pfam; PF01712; dNK; 1. KW Transferase; Kinase; DNA synthesis; ATP-binding; 3D-structure. FT NP_BIND 27 34 ATP (POTENTIAL). SQ SEQUENCE 250 AA; 29088 MW; 17C5DF197B8792DB CRC64; MAEAASCARK GTKYAEGTQP FTVLIEGNIG SGKTTYLNHF EKYKNDICLL TEPVEKWRNV NGVNLLELMY KDPKKWAMPF QSYVTLTMLQ SHTAPTNKKL KIMERSIFSA RYCFVENMRR NGSLEQGMYN TLEEWYKFIE ESIHVQADLI IYLRTSPEVA YERIRQRARS EESCVPLKYL QELHELHEDW LIHQRRPQSC KVLVLDADLN LENIGTEYQR SESSIFDAIS SNQQPSPVLV SPSKRQRVAR // ID DOA_DROME STANDARD; PRT; 832 AA. AC P49762; Q8IMM0; Q8T041; Q95RC9; Q9VAR8; DT 01-OCT-1996 (Rel. 34, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein kinase Doa (EC 2.7.1.37) (Protein darkener of DE apricot). GN DOA OR CG1658. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=95011531; PubMed=7926721; RA Yun B., Farkas R., Lee K., Rabinow L.; RT "The Doa locus encodes a member of a new protein kinase family and is RT essential for eye and embryonic development in Drosophila RT melanogaster."; RL Genes Dev. 8:1160-1173(1994). RN [2] RP REVISIONS. RA Rabinow L.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS A AND C). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP FUNCTION, PHOSPHORYLATION OF LYS-508, AND MUTAGENESIS OF LYS-508. RX MEDLINE=97066903; PubMed=8910305; RA Lee K., Du C., Horn M., Rabinow L.; RT "Activity and autophosphorylation of LAMMER protein kinases."; RL J. Biol. Chem. 271:27299-27303(1996). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=20469360; PubMed=11014821; RA Yun B., Lee K., Farkas R., Hitte C., Rabinow L.; RT "The LAMMER protein kinase encoded by the Doa locus of Drosophila is RT required in both somatic and germline cells and is expressed as both RT nuclear and cytoplasmic isoforms throughout development."; RL Genetics 156:749-761(2000). CC -!- FUNCTION: NEGATIVE REGULATOR OF THE COPIA RETROTRANSPOSON ELEMENT CC OF THE WHITE (W) GENE. IN THE EYE, IT IS REQUIRED FOR NORMAL CC PIGMENTATION, PHOTORECEPTOR CELL DEVELOPMENT AND FOR ORGANIZATION CC OF INTEROMMATIDIAL BRISTLES. ALSO ESSENTIAL FOR EMBRYONIC CC SEGMENTATION AND DIFFERENTIATION OF THE NERVOUS SYSTEM. FUNCTIONS CC IN THE CONTROL OF ALTERNATIVE SPLICING BY PHOSPHORYLATING THE CC ARGINE/SERINE-RICH SPLICING FACTORS, SR PROTEINS. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- COFACTOR: MAGNESIUM. CC -!- SUBCELLULAR LOCATION: ISOFORM C IS CYTOSOLIC. ISOFORM A IS MAINLY CC NUCLEAR WITH ONLY LOW LEVELS PRESENT IN THE CYTOPLASM. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=C; Synonyms=105 kDa isoform; CC IsoId=P49762-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=A; Synonyms=55 kDa isoform; CC IsoId=P49762-2; Sequence=VSP_008268, VSP_008270, VSP_008272; CC Name=B; CC IsoId=P49762-3; Sequence=VSP_008269, VSP_008271, VSP_008272; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: UBIQUITOUS EXPRESSION IN EMBRYOS. STAGE 17 CC EMBRYOS SHOW ELEVATED EXPRESSION IN CNS AND BRAIN. UBIQUITOUS CC EXPRESSION IN LARVAL IMAGINAL DISKS. INCREASED EXPRESSION CC POSTERIOR TO THE EYE-ANTENNAL DISK MORPHOGENETIC FURROW. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY (ISOFORM C) AND CC ZYGOTICALLY (ISOFORMS A AND C) IN ALL DEVELOPMENTAL STAGES. CC -!- PTM: AUTOPHOSPHORYLATES ON ALL THREE TYPES OF RESIDUES. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC LAMMER SUBFAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC CHIMERA OF GENOMIC DNA AND CDNA. CC -!- CAUTION: ISOFORM C IS MOST PROBABLY THE 105 KDA ISOFORM THOUGH CC THERE IS NO TRANSLATION SEQUENCE EVIDENCE OF THIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78715; CAA55367.1; ALT_SEQ. DR EMBL; AE003767; AAF56832.3; -. DR EMBL; AE003767; AAF56833.2; -. DR EMBL; AE003767; AAN14305.1; -. DR EMBL; AY061474; AAL29022.1; -. DR EMBL; AY069573; AAL39718.1; -. DR PIR; A54099; A54099. DR FlyBase; FBgn0000480; Doa. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA. DR GO; GO:0007350; P:blastoderm segmentation; IMP. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR GO; GO:0042051; P:eye photoreceptor development (sensu Drosop...; IEP. DR GO; GO:0007399; P:neurogenesis; IMP. DR GO; GO:0007548; P:sex differentiation; IGI. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Vision; Transferase; Serine/threonine-protein kinase; KW Tyrosine-protein kinase; ATP-binding; Developmental protein; KW Nuclear protein; Phosphorylation; Alternative splicing. FT DOMAIN 479 799 PROTEIN KINASE. FT NP_BIND 485 493 ATP (BY SIMILARITY). FT BINDING 508 508 ATP. FT ACT_SITE 605 605 BY SIMILARITY. FT VARSPLIC 1 252 Missing (in isoform A). FT /FTId=VSP_008268. FT VARSPLIC 1 315 Missing (in isoform B). FT /FTId=VSP_008269. FT VARSPLIC 253 453 APQQQSKIGYPRTGAPLTHSASFSSAQRPTALQFHQQHQQQ FT QHLQQQQQHPQQQQHQHSSFGVGMMSRNYYNMPKQPERKPL FT QTFDPYAYPKPNQMQPVKYQQQQQHPHTQFQNASAGGGGGG FT AAGLQYDPNTNTQLFYASPASSSSNKQPQQPQQQQQQQQSQ FT LQQSNSVIFNHSGQQHQPHQQQQNEMSKSALGLHFIE -> FT MQLPSLKDKLMPSGSVQQAKANFSWQSLTQLLSGLWQRLYL FT PRSPFLALPAPPLATPPANTTQRRAKKEMPRTRRLHHSRDR FT SSAGTRDKRRRHDTADHSPPLAEAPSPPRITNTHHTRSAAK FT RRRHELDAKKAQISKEPTFDDSISTRRRKERSKRSHRKSPA FT ASRRQHKYRYRDETSHSSSRRRHRDRAKDERDSGRNNRQSQ FT AK (in isoform A). FT /FTId=VSP_008270. FT VARSPLIC 316 453 GMMSRNYYNMPKQPERKPLQTFDPYAYPKPNQMQPVKYQQQ FT QQHPHTQFQNASAGGGGGGAAGLQYDPNTNTQLFYASPASS FT SSNKQPQQPQQQQQQQQSQLQQSNSVIFNHSGQQHQPHQQQ FT QNEMSKSALGLHFIE -> MPRTRRLHHSRDRSSAGTRDKR FT RRHDTADHSPPLAEAPSPPRITNTHHTRSAAKRRRHELDAK FT KAQISKEPTFDDSISTRRRKERSKRSHRKSPAASRRQHKYR FT YRDETSHSSSRRRHRDRAKDERDSGRNNRQSQAK (in FT isoform B). FT /FTId=VSP_008271. FT VARSPLIC 722 727 Missing (in isoform A and isoform B). FT /FTId=VSP_008272. FT MUTAGEN 508 508 K->R: LOSS OF ACTIVITY. SQ SEQUENCE 832 AA; 95723 MW; 6EC90CB1A031DD68 CRC64; MVAANLEVPT SSSSSAATKR QKDVDNKLEK CLNDMLKLKT SSNNNSTSNS NNNAIMSHSL TGEHKDPKTA LEGPTSSSSS SSSKYIGESQ IPVPVQLYDP QKPLLQQQQQ QQRICYPIGK SNSTSQLPMG GYQRLLQHQQ QQHHQQQQQQ HQEQQQYPQH KRPFLNWNSF ACSAMNGASD PFMQQQHMPA HQQQQHLPHK LQQSYSSSHV PKQAPKSGLA MFLQKNTNKE NKFGQPMQQQ PPGMMPQMYG YQAPQQQSKI GYPRTGAPLT HSASFSSAQR PTALQFHQQH QQQQHLQQQQ QHPQQQQHQH SSFGVGMMSR NYYNMPKQPE RKPLQTFDPY AYPKPNQMQP VKYQQQQQHP HTQFQNASAG GGGGGAAGLQ YDPNTNTQLF YASPASSSSN KQPQQPQQQQ QQQQSQLQQS NSVIFNHSGQ QHQPHQQQQN EMSKSALGLH FIETAKPVIQ DDADGHLIYH TGDILHHRYK IMATLGEGTF GRVVKVKDME RDYCMALKII KNVEKYREAA KLEINALEKI AQKDPHCDHL CVKMIDWFDY HGHMCIVFEM LGLSVFDFLR ENNYEPYPLD QVRHMAYQLC YSVKFLHDNR LTHTDLKPEN ILFVDSDYTS HYNHKINREV RRVKNTDVRL IDFGSATFDH EHHSTIVSTR HYRAPEVILE LGWSQPCDVW SIGCILFELY LGITLFQTHD NREHLAMMER ILGQIPYRMA RNHTLYSKTK TKYFYHGKLD WDEKSSAGRY VRDHCKPLFL CQLSDSEDHC ELFSLIKKML EYEPSSRITL GEALHHPFFD RLPPHHRVGE VSNKQPLSSG SSSRERSHSL SR // ID DOD_DROME STANDARD; PRT; 166 AA. AC P54353; O61344; Q9VRH1; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dodo protein. GN DOD OR CG17051. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Larva, and Pupae; RX MEDLINE=96133954; PubMed=8552658; RA Maleszka R., Hanes S.D., Hackett R.L., de Couet H.G., Miklos G.L.G.; RT "The Drosophila melanogaster dodo (dod) gene, conserved in humans, is RT functionally interchangeable with the ESS1 cell division gene of RT Saccharomyces cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 93:447-451(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98188272; PubMed=9520435; RA Maleszka R., de Couet H.G., Miklos G.L.G.; RT "Data transferability from model organisms to human beings: insights RT from the functional genomics of the flightless region of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE PPIC/PARVULIN ROTAMASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 WW DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U35140; AAC46958.1; -. DR EMBL; AF017777; AAC28408.1; -. DR EMBL; AE003568; AAF50829.1; -. DR PIR; T08426; T08426. DR HSSP; Q13526; 1PIN. DR FlyBase; FBgn0015379; dod. DR InterPro; IPR000297; Rotamase. DR InterPro; IPR001202; WW_Rsp5_WWP. DR Pfam; PF00639; Rotamase; 1. DR Pfam; PF00397; WW; 1. DR SMART; SM00456; WW; 1. DR PROSITE; PS01096; PPIC_PPIASE_1; 1. DR PROSITE; PS50198; PPIC_PPIASE_2; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 1. KW Isomerase; Rotamase. FT DOMAIN 5 39 WW. FT DOMAIN 55 166 PPIC. FT CONFLICT 44 44 A -> T (IN REF. 2). SQ SEQUENCE 166 AA; 18376 MW; 3B4306FA930E7259 CRC64; MPDAEQLPDG WEKRTSRSTG MSYYLNMYTK ESQWDQPTEP AKKAGGGSAG GGDAPDEVHC LHLLVKHKGS RRPSSWREAN ITRTKEEAQL LLEVYRNKIV QQEATFDELA RSYSDCSSAK RGGDLGKFGR GQMQAAFEDA AFKLNVNQLS GIVDSDSGLH IILRKA // ID DOME_DROME STANDARD; PRT; 1282 AA. AC Q9VWE0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytokine receptor precursor (Domeless protein). GN DOME OR CG14226. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21553061; PubMed=11696329; RA Brown S., Hu N., Castelli-Gair Hombria J.; RT "Identification of the first invertebrate interleukin JAK/STAT RT receptor, the Drosophila gene domeless."; RL Curr. Biol. 11:1700-1705(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR EMBRYONIC SEGMENTATION AND TRACHEA CC SPECIFICATION. SIGNAL TRANSDUCING MOLECULE FOR UPD. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: IN STAGE 11 EMBRYOS, TRACHEAL PITS SHOW CC HIGHEST EXPRESSION, AT STAGE 14 HIGH EXPRESSION IS DETECTED IN THE CC POSTERIOR SPIRACLES, GUT AND HEAD. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY IN CC EMBRYOS. CC -!- SIMILARITY: BELONGS TO THE CYTOKINE FAMILY OF RECEPTORS. CC -!- SIMILARITY: CONTAINS 3 FIBRONECTIN TYPE III DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ420377; CAD12503.1; -. DR EMBL; AE003512; AAF49002.1; -. DR FlyBase; FBgn0043903; dome. DR GO; GO:0004888; F:transmembrane receptor activity; IGI. DR GO; GO:0007350; P:blastoderm segmentation; IMP. DR GO; GO:0007259; P:JAK-STAT cascade; IGI. DR GO; GO:0007424; P:tracheal system development (sensu Insecta); IMP. DR InterPro; IPR003961; FN_III. DR InterPro; IPR008957; FN_III-like. DR Pfam; PF00041; fn3; 3. DR SMART; SM00060; FN3; 4. KW Receptor; Signal; Glycoprotein; Transmembrane; Repeat; KW Developmental protein. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 1282 CYTOKINE RECEPTOR. FT DOMAIN 24 889 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 890 910 POTENTIAL. FT DOMAIN 911 1282 CYTOPLASMIC (POTENTIAL). FT DOMAIN 224 315 FIBRONECTIN TYPE-III 1. FT DOMAIN 536 621 FIBRONECTIN TYPE-III 2. FT DOMAIN 633 725 FIBRONECTIN TYPE-III 3. FT DISULFID 47 106 BY SIMILARITY. FT DISULFID 132 142 BY SIMILARITY. FT DISULFID 173 183 BY SIMILARITY. FT DISULFID 472 482 BY SIMILARITY. FT CARBOHYD 44 44 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 87 87 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 114 114 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 143 143 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 156 156 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 184 184 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 230 230 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 235 235 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 278 278 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 298 298 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 310 310 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 376 376 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 448 448 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 466 466 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 568 568 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 581 581 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 626 626 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 676 676 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 703 703 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 777 777 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 790 790 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 862 862 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1282 AA; 142360 MW; 22CE960963B17011 CRC64; MVAQEQLVLL LMLLAGCRGG ANAILDPGWV IPSKVEQLIG GDFNLSCTLN EDYFNGKSAE DCPVEKLYFT GGGRVYRDSK HIRILNNTTI LFSDTNAVEQ ENDYHCMCDE YVINKSKVYV GTRPLLVRDF NCLDYDFQFM VCNFTQPPNT VITKYNISYN TNNDWRYSNT LDCNFDSAPV VTCNLTDDNY KRFSETFYFR LSISNALGHE TQPITINHFE RLVPARPGQN LTLLNRTESS VCLSWEMPRR SNYNRGLVWQ VRVTPQNFEP ITRPSWRNHT LTIKDTLCLT ELPFAGYNYT LRVRVRANQN NTLWSEPMIY AFATAPAPPR RPPRVTYGSF YVYSSEKAMR FYWEPLEEHE LNGPDFRYSI SEYRINGTAV DPGLIKVESN SAMIDHWSMS AVHHFLIRSS NSQGLSVNAT PMTIGPISNR DFKVREPRNI RSVYHPTNKS YTLSWDPPSD QRELQNYTVF WCVPKPGLQS ECEGSIRFAE VASGLHHFTT SPDQLLTLHM AVSANYQSHN TGLHWAICSS DKKDDLAKME PSIDVATSTS LTVSWSERVC AVILAGYNLT YCQRSAGRPD NCTTVTIDRY TNKHVIQNLV PYTDYSVKML MYSDSRVSKY SDELVNRTGE AAPSQPRELQ LIRVTSDSVE LAWKPPLLAN GVVRAYEGTF RSLHDNVTDT FRVSASADEL VNNEKPITYR LGNLTAFTKY EISVRARTVY PSEPSNVILF STAIGVPSPP QLYVINNPDQ SSRLDWEPPR TPAGRIDFYE ISLRDNNASC LTSTILPGRN LSYVMATPRC TSHNPFQLAV RAINVEQHPQ LNGADAAEGA VLLMSTNGKG CEARTDALGE EERLQFEAYA ANMTAYRLYR SDWGIYGFIC TPDTHSVKAM YQTIEVTVAI LVLGVIFYLV YKKYRKMSDI GLVLPQGIME TMKKPIDMGG LGLGLGPDSS VSGGIVCTRV DDSPPYTPQD LPHDFSSCGS ESSKLLLRTA SSSGGGGCVD RDGYDDNHET GPISAVGPPT SYLAMRHGLL VQNDRERERE RDREQERERE QQQQQRESEM DREQSCTNGY IKPTQMKSWG GNGPSDNDHT FSVPSTAMTA PMSQPLSQIP LSGYVPVPIP QSRFNPAPVQ PFGSPAVPSA ATAAAASTFF PPAHLLNMDN YVQASDLHKL KPLVAAPLSQ TGGPAFAGSS PATSPPLQLP PVHAASPAAA TPKMADIGYT TMEQLQLTGL IKPPLAATVG SPTHAAGGAP GGGNQHSRLQ PQINGYVTPQ DLNAMAHNRH VL // ID DOP1_DROME STANDARD; PRT; 511 AA. AC P41596; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dopamine receptor 1 precursor (D-DOP1). GN DOPR1 OR DOPR OR DOPR35EF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berlin; TISSUE=Head; RX MEDLINE=95041081; PubMed=7953290; RA Gotzes F., Balfanz S., Baumann A.; RT "Primary structure and functional characterization of a Drosophila RT dopamine receptor with high homology to human D1/5 receptors."; RL Recept. Channels 2:131-141(1994). CC -!- FUNCTION: RECEPTOR FOR DOPAMINE. THE ACTIVITY OF THIS RECEPTOR IS CC MEDIATED BY G PROTEINS WHICH ACTIVATE ADENYLYL CYCLASE. MIGHT BE CC INVOLVED IN THE PROCESSING OF VISUAL INFORMATION AND/OR VISUAL CC LEARNING. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: SOMATA OF THE OPTIC LOBES. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X77234; CAA54451.1; -. DR PIR; S44275; S44275. DR FlyBase; FBgn0011582; DopR. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Phosphorylation; Lipoprotein; Palmitate; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 511 DOPAMINE RECEPTOR 1. FT DOMAIN 20 142 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 143 169 1 (POTENTIAL). FT DOMAIN 170 179 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 180 206 2 (POTENTIAL). FT DOMAIN 207 216 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 217 239 3 (POTENTIAL). FT DOMAIN 240 258 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 259 279 4 (POTENTIAL). FT DOMAIN 280 310 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 311 331 5 (POTENTIAL). FT DOMAIN 332 391 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 392 412 6 (POTENTIAL). FT DOMAIN 413 427 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 428 450 7 (POTENTIAL). FT DOMAIN 451 511 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 53 53 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 63 63 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 74 74 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 117 117 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 123 123 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 216 302 BY SIMILARITY. FT LIPID 468 468 S-palmitoyl cysteine (Potential). FT LIPID 469 469 S-palmitoyl cysteine (Potential). SQ SEQUENCE 511 AA; 55997 MW; 594685ED99A16A4E CRC64; MYTPHPFGFL IILVPMTNAM RAIAAIAAGV GSVAATVATS TTSSISSSTT IINTSSATTI GGNHTSGSTG FSTNSTLLDA DHLPLQLTTA KVDLDIEIDI QLLTNGYDGT TLTSFYNESS WTNASEMDTI VGEEPEPLSL VSIVVVGIFL SVLIFLSVAG NILVCLAIYT DGSLPRIGNL FLASLAIADL FVASLVMTFA GVNDLLGYWI FGAQFCDTWV AFDVMCSTAS ILNLCAISMD RYIHIKDPLR YGRWVTRRVA VITIAAIWLL AAFVSFVPIS LGIHRPDQPL IFEDNGKKYP TCALDLTPTY AVVSSCISFY FPCVVMIGIY CRLYCYAQKH VKSIKAVTRP GEVAEKQRYK SIRRPKNQPK KFKVRNLHTH SSPYHVSDHK AAVTVGVIMG VFLICWVPFF CVNITAAFCK TCIGGQTFKI LTWLGYSNSA FNPIIYSIFN KEFRDAFKRI LTMRNPWCCA QDVGNIHPRN SDRFITDYAA KNVVVMNSGR SSAELEQVSA I // ID DOP2_DROME STANDARD; PRT; 539 AA. AC Q24563; Q24569; Q9VAJ8; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dopamine receptor 2. GN DOPR2 OR DOPR99B OR DAMB OR CG18741. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=96242088; PubMed=8656286; RA Feng G., Hannan F., Reale V., Hon Y.Y., Kousky C.T., Evans P.D., RA Hall L.M.; RT "Cloning and functional characterization of a novel dopamine receptor RT from Drosophila melanogaster."; RL J. Neurosci. 16:3925-3933(1996). RN [2] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Canton-S; RX MEDLINE=96258265; PubMed=8663989; RA Han K.-A., Millar N.S., Grotewiel M.S., Davis R.L.; RT "DAMB, a novel dopamine receptor expressed specifically in Drosophila RT mushroom bodies."; RL Neuron 16:1127-1135(1996). RN [3] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RECEPTOR FOR DOPAMINE. THE ACTIVITY OF THIS RECEPTOR IS CC MEDIATED BY G PROTEINS WHICH ACTIVATE ADENYLYL CYCLASE. ALSO CC CAPABLE OF GENERATING A CALCIUM SIGNAL. IN TERMS OF ANTAGONIST CC RESPONSES, WOULD BE CLASSED WITH THE D1-LIKE DOPAMINE RECEPTOR CC GROUP. THIS RECEPTOR AN ATTRACTIVE CANDIDATE FOR INITIATING CC BIOCHEMICAL CASCADES UNDERLYING OLFACTORY LEARNING. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q24563-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q24563-2; Sequence=VSP_001877; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: EXPRESSED IN BOTH CENTRAL AND PERIPHERAL CC NERVOUS SYSTEMS. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U34383; AAC47161.1; -. DR EMBL; U61264; AAB08000.1; -. DR EMBL; AE003770; AAF56908.2; -. DR FlyBase; FBgn0015129; DopR2. DR GO; GO:0004952; F:dopamine receptor activity; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00960; LMBPPROTEIN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Phosphorylation; Lipoprotein; Palmitate; Alternative splicing. FT DOMAIN 1 113 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 114 134 1 (POTENTIAL). FT DOMAIN 135 145 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 146 166 2 (POTENTIAL). FT DOMAIN 167 189 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 190 206 3 (POTENTIAL). FT DOMAIN 207 227 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 228 248 4 (POTENTIAL). FT DOMAIN 249 266 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 267 287 5 (POTENTIAL). FT DOMAIN 288 420 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 421 441 6 (POTENTIAL). FT DOMAIN 442 453 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 454 474 7 (POTENTIAL). FT DOMAIN 475 539 CYTOPLASMIC (POTENTIAL). FT DOMAIN 86 89 POLY-GLY. FT DOMAIN 338 351 POLY-GLY. FT DOMAIN 357 367 POLY-HIS. FT CARBOHYD 5 5 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 31 31 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 47 47 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 68 68 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 182 261 BY SIMILARITY. FT LIPID 492 492 S-palmitoyl cysteine (Potential). FT LIPID 493 493 S-palmitoyl cysteine (Potential). FT VARSPLIC 511 539 RFATRRCYSTCSLHGIQHVRHNSCEQTYI -> CHVAAAMV FT AASTSFGYHSVNQIDRTLM (in isoform Short). FT /FTId=VSP_001877. SQ SEQUENCE 539 AA; 59505 MW; 32FDDC0E935AF4B3 CRC64; MVDDNGSSPE VEGAEGAGAP LLALLRVDGL NQTQTRSPSP SFFGSYNISE DVYFYFNGLP TSTELVLNAT TSATSATLSP AMVATGGGGT TTPEPDLSEF LEALPNDRVG LLAFLFLFSF ATVFGNSLVI LAVIRERYLH TATNYFITSL AVADCLVGLV VMPFSALYEV LENTWFFGTD WCDIWRSLDV LFSTASILNL CVISLDRYWA ITDPFSYPMR MTVKRAAGLI AAVWICSSAI SFPAIVWWRA ARDGEMPAYK CTFTEHLGYL VFSSTISFYL PLLVMVFTYC RIYRAAVIQT RSLKIGTKQV LMASGELQLT LRIHRGGTTR DQQNQVSGGG GGGGGGGGGG GSLSHSHSHS HHHHHNHGGG TTTSTPEEPD DEPLSALHNN GLARHRHMGK NFSLSRKLAK FAKEKKAAKT LGIVMGVFII CWLPFFVVNL LSGFCIECIE HEEIVSAIVT WLGWINSCMN PVIYACWSRD FRRAFVRLLC MCCPRKIRRK YQPTMRSKSQ RFATRRCYST CSLHGIQHVR HNSCEQTYI // ID DORS_DROME STANDARD; PRT; 999 AA. AC P15330; O77088; Q9VJD9; Q9VJE0; DT 01-APR-1990 (Rel. 14, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Embryonic polarity dorsal protein. GN DL OR CG6667. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=88042799; PubMed=3118464; RA Steward R.; RT "Dorsal, an embryonic polarity gene in Drosophila, is homologous to RT the vertebrate proto-oncogene, c-rel."; RL Science 238:692-694(1987). RN [2] RP SUBCELLULAR LOCATION, AND REVISIONS (ISOFORM A). RX MEDLINE=90090617; PubMed=2598266; RA Steward R.; RT "Relocalization of the dorsal protein from the cytoplasm to the RT nucleus correlates with its function."; RL Cell 59:1179-1188(1989). RN [3] RP SEQUENCE FROM N.A. (ISOFORM B), FUNCTION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; RX MEDLINE=99173887; PubMed=10072776; RA Gross I., Georgel P., Oertel-Buchheit P., Schnarr M., Reichhart J.M.; RT "Dorsal-B, a splice variant of the Drosophila factor Dorsal, is a RT novel Rel/NF-kappaB transcriptional activator."; RL Gene 228:233-242(1999). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: EMBRYONIC DEVELOPMENTAL PROTEIN. THE LATERAL OR VENTRAL CC IDENTITY OF A CELL DEPENDS UPON THE CONCENTRATION OF DORSAL CC PROTEIN IN ITS NUCLEUS DURING THE BLASTODERM STAGE. DORSAL IS A CC MORPHOGENETIC PROTEIN THAT SPECIFICALLY BINDS TO THE KAPPA B- CC RELATED CONSENSUS SEQUENCE 5'-GRGAAAANCC-3', LOCATED IN THE CC ENHANCER REGION OF ZYGOTIC GENES SUCH AS ZEN, TWIST, SNAIL AND CC DECAPENTAPLEGIC. MEDIATES AN IMMUNE RESPONSE IN DROSOPHILA LARVAE. CC -!- SUBCELLULAR LOCATION: IN VENTRAL REGIONS IT IS FIRST CYTOPLASMIC, CC THEN THE PROTEIN IS RELOCALIZED IN THE NUCLEUS. ITS NUCLEAR CC LOCALIZATION IS ESSENTIAL TO ITS FUNCTION AS A MORPHOGEN. IN CC DORSAL REGIONS IT REMAINS CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=P15330-1; Sequence=Displayed; CC Name=A; CC IsoId=P15330-2; Sequence=VSP_005581, VSP_005582; CC -!- TISSUE SPECIFICITY: IN UNCHALLENGED LARVAE, EXPRESSION OF BOTH CC ISOFORMS IS SEEN IN FAT BODY AND GUT (ISOFORM A IS MORE ABUNDANT). CC AFTER IMMUNE CHALLENGE LEVELS OF BOTH ISOFORMS ARE ENHANCED. CC -!- DEVELOPMENTAL STAGE: ISOFORM A IS EXPRESSED MATERNALLY AND BOTH CC ISOFORMS ARE EXPRESSED ZYGOTICALLY FROM 6-9 HOUR EMBRYOS THROUGH CC TO ADULTHOOD. CC -!- SIMILARITY: BELONGS TO THE REL/DORSAL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23702; AAA28479.1; -. DR EMBL; AF053614; AAC35296.1; -. DR EMBL; AE003655; AAF53610.1; -. DR EMBL; AE003655; AAF53612.1; -. DR PIR; A30350; A30350. DR HSSP; P25799; 1BFS. DR TRANSFAC; T00196; -. DR FlyBase; FBgn0000462; dl. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0009953; P:dorsal/ventral pattern formation; NAS. DR GO; GO:0007398; P:ectoderm development; NAS. DR GO; GO:0007369; P:gastrulation; NAS. DR GO; GO:0006955; P:immune response; IEP. DR GO; GO:0007498; P:mesoderm development; NAS. DR GO; GO:0016481; P:negative regulation of transcription; NAS. DR GO; GO:0007419; P:ventral cord development; NAS. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR002909; IPT_TIG. DR InterPro; IPR000451; NF_Rel_dor. DR InterPro; IPR008967; P53-like. DR Pfam; PF00554; RHD; 1. DR Pfam; PF01833; TIG; 1. DR PRINTS; PR00057; NFKBTNSCPFCT. DR SMART; SM00429; IPT; 1. DR PROSITE; PS01204; REL_1; 1. DR PROSITE; PS50254; REL_2; 1. KW Nuclear protein; DNA-binding; Transcription regulation; Activator; KW Phosphorylation; Developmental protein; Alternative splicing. FT DOMAIN 47 342 REL-LIKE (RHD). FT DOMAIN 756 773 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT MOD_RES 312 312 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT DOMAIN 395 464 GLN-RICH. FT DOMAIN 635 705 PRO-RICH. FT VARSPLIC 330 677 GKHTFWNLHRHLKRKPDEDLFQQILRLDAKREVQPPTIEVI FT DLDTPKIDVQREIPSEMEFNHEESQQSEPALEQEQSVQQEQ FT YTQEQSLQQEQYTQEQSLQQEQYLQQLEQQQSFQLEEPMQQ FT DQELPAQQSFDQAIDHLPDHTSDHIPEDMEAADAHAEAEAH FT RLRSEQEKEIDTIIDEKVRELEQLDLGQQLEPRPLTANDKI FT TEWMKSSEIEQQVHEPSPTAEADVLDSALEISKADKTLDEL FT LETVAELDEIYTDFKVQRDTYKNTIQNELAGLQGRAPLQVE FT DSFDDAATYTSLQIAFKNPVLIPMDDIMPPTPPMSQCAPED FT AHQHYDPVEVNSQARKPETP -> DPAHLRRKRQKTGGDPM FT HLLLQQQQKQQLQNDHQDGRQTNMNCWNTQNIPPIKTEPRD FT TSPQPFGLSYRAPPELTPSPQPLSPSSNYNHNSTPSPYNMA FT SAVTPTNGQQQLMSPNHPQQQQQQQQYGATDLGSNYNPFAQ FT QVLAQQQQHQQQQQQHQHQHQQQHQQQQQQQQQQQQQSLQF FT HANPFGNPGGNSWESKFSAAAVAAAAATATGAAPANGNSNN FT LSNLNNPFTMHNLLTSGGGPGNANNLQWNLTTNHLHNQHTL FT HQQQQLQQQQQQQYDNTAPTNNNANLNNNNNNNNTAGNQAD FT NNGPTLSNLLSFDSGQLVHINSEDQQILRLNSEDLQISNLS FT IST (in isoform A). FT /FTId=VSP_005581. FT VARSPLIC 678 999 Missing (in isoform A). FT /FTId=VSP_005582. FT CONFLICT 391 391 H -> Q (IN REF. 3). FT CONFLICT 401 401 L -> F (IN REF. 3). FT CONFLICT 407 407 V -> SQQEQYTQEQSL (IN REF. 3). FT CONFLICT 698 699 DK -> EQ (IN REF. 3). FT CONFLICT 965 999 ASEFDETSAYYAPVDAGEILTPDEVAKRLAAANGI -> PV FT NLTRPPPTMLPWMLARF (IN REF. 3). SQ SEQUENCE 999 AA; 111551 MW; E29C6594AC07D662 CRC64; MFPNQNNGAA PGQGPAVDGQ QSLNYNGLPA QQQQQLAQST KNVRKKPYVK ITEQPAGKAL RFRYECEGRS AGSIPGVNST PENKTYPTIE IVGYKGRAVV VVSCVTKDTP YRPHPHNLVG KEGCKKGVCT LEINSETMRA VFSNLGIQCV KKKDIEAALK AREEIRVDPF KTGFSHRFQP SSIDLNSVRL CFQVFMESEQ KGRFTSPLPP VVSEPIFDKK AMSDLVICRL CSCSATVFGN TQIILLCEKV AKEDISVRFF EEKNGQSVWE AFGDFQHTDV HKQTAITFKT PRYHTLDITE PAKVFIQLRR PSDGVTSEAL PFEYVPMDSG KHTFWNLHRH LKRKPDEDLF QQILRLDAKR EVQPPTIEVI DLDTPKIDVQ REIPSEMEFN HEESQQSEPA LEQEQSVQQE QYTQEQSLQQ EQYTQEQSLQ QEQYLQQLEQ QQSFQLEEPM QQDQELPAQQ SFDQAIDHLP DHTSDHIPED MEAADAHAEA EAHRLRSEQE KEIDTIIDEK VRELEQLDLG QQLEPRPLTA NDKITEWMKS SEIEQQVHEP SPTAEADVLD SALEISKADK TLDELLETVA ELDEIYTDFK VQRDTYKNTI QNELAGLQGR APLQVEDSFD DAATYTSLQI AFKNPVLIPM DDIMPPTPPM SQCAPEDAHQ HYDPVEVNSQ ARKPETPMRP VPPVPPAILT IQYPPEEDKL PPLPPKRIRK QDSNAENRSI EANTVQTKPS TGESPLNKRL PPAPKNPNFN TLPRQKKPGF FSKLFSRRKS KPDLAQGQEN SSILDSKANS REPSIGHFNM QDPMRASLRS SKSAAPFISN PAPAKSSPVK AKKPGSKLTK PVGRSVSSVS GKRPAYLNAD VVHIPLKGDS VNSLPQQQRT EGYSQSSTIS VGAGLDRRTA SALQLADIPI SEGGMELVAI ADRQSLHNLV SSIEGHFNVQ LDPNLDLTEA EHFALYTSIP PLAAASEFDE TSAYYAPVDA GEILTPDEVA KRLAAANGI // ID DOR_DROME STANDARD; PRT; 1002 AA. AC Q24314; DT 01-NOV-1997 (Rel. 35, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Deep orange protein. GN DOR OR EG171E4.1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97218037; PubMed=9065698; RA Shestopal S.A., Makumin I.V., Belyaeva E.S., Ashburner M.; RT "Molecular characterization of the deep orange (dor) gene of RT Drosophila melanogaster."; RL Mol. Gen. Genet. 253:642-648(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- SIMILARITY: SOME, TO YEAST PEP3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86683; CAA60382.1; -. DR EMBL; AL021726; CAA16809.1; -. DR PIR; S54252; S54252. DR FlyBase; FBgn0000482; dor. DR GO; GO:0006727; P:ommochrome biosynthesis; IMP. DR GO; GO:0006728; P:pteridine biosynthesis; IMP. DR InterPro; IPR000547; Clathrin_repeat. DR InterPro; IPR007810; Pep3_Vps18. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF05131; Pep3_Vps18; 1. DR SMART; SM00184; RING; 1. KW Zinc-finger; Transmembrane. FT ZN_FING 885 910 C3H2C-TYPE. FT TRANSMEM 971 991 POTENTIAL. FT CONFLICT 169 169 A -> P (IN REF. 1). FT CONFLICT 581 581 Q -> H (IN REF. 1). FT CONFLICT 865 865 A -> V (IN REF. 1). SQ SEQUENCE 1002 AA; 115305 MW; D59690A0FC95182F CRC64; MDTSMPNQPK FLPRIEHNSS GATANSYVAT ASGNPFETDE EDEIFSRHKM VLRVPSNCTG DLMHLAVSRN WLVCLLGTPE RTTLLRFFLP RAIPPGEAVL EKYLSGSGYK ITRMFLDPTG HHIIIALVPK SATAGVSPDF LYIHCLESPQ AQQLKVRRIE KFKDHEITAV AFNPYHGNES STGPILLGTS RGLIFETELN PAADGHVQRK QLYDLGLGRP KYPITGLKLL RVPNSSRYII VVTSPECIYT FQETLKAEER SLQAIFAGYV SGVQEPHCEE RKTDLTFSQL RFFAPPNSKY PKQWAWLCGE GIRVGELSIE ANSAATLIGN TLINLDFEKT MHLSYGERRL NTPKAFVLTE YHAVLLYADH VRAICLLNQE QVYQEAFDEA RVGKPLSIER DELTGSIYVY TVKTVFNLRV TREERNVWRI YLDKGQYELA TAHAAEDPEH LQLVLCQRAD AAFADGSYQV AADYYAETDK SFEEVCLKFM VLPDKRPIIN YVKKRLSRVT TKPMETDELD EDKMNIIKAL VIWLIDLYLI QINMPDKDEE WRSSWQTEYD EFMMEAHVLS CTRQNRETVR QLIAEHADPR NMAQFAIAIG DYDEVVAQQL KAECYAEALQ TLINQRNPEL FYKYAPELIT RLPKPTVDAL MAQGSRLEVE KLVPTLIIME NREQREQTQR YLEFAIYKLN TTNDAIHNFL LHLYAEHEPK LLMKYLEIQG RDESLVHYDI YYAHKVCTDL DVKEARVFLE CMLRKWISAV DLALTFDMKL AKETASRPSD SKIRRKLWLR IAYHDIKGTN DVKKALNLLK ECDLLRIEDL LPFFADFEKI DNFKEAICDA LRDYNQRIQE LQREMAETTE QTDRATAELQ QLRQHSLTVE SQDTCEICEM MLLVKPFFIF ICGHKFHSDC LEKHVVPLLT KEQCRRLGTL KQQLEAEVQT QAQPQSGALS KQQAMELQRK RAALKTEIED ILAADCLFCG LLISTIDQPF VDDWEQVNVE WE // ID DPG1_DROME STANDARD; PRT; 1145 AA. AC Q27607; Q8T4E6; Q94906; Q9V442; DT 01-NOV-1997 (Rel. 35, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA polymerase gamma subunit 1, mitochondrial precursor (EC 2.7.7.7) DE (Mitochondrial DNA polymerase catalytic subunit) (Tamas protein). GN TAM OR POLG OR MTPOLA OR CG8987. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97038687; PubMed=8884268; RA Ropp P.A., Copeland W.C.; RT "Cloning and characterization of the human mitochondrial DNA RT polymerase, DNA polymerase gamma."; RL Genomics 36:449-458(1996). RN [2] RP SEQUENCE FROM N.A., PARTIAL SEQUENCE, AND CHARACTERIZATION. RC TISSUE=Ovary; RX MEDLINE=96394437; PubMed=8798543; RA Lewis D.L., Farr C.L., Wang Y., Lagina A.T. III, Kaguni L.S.; RT "Catalytic subunit of mitochondrial DNA polymerase from Drosophila RT embryos. Cloning, bacterial overexpression, and biochemical RT characterization."; RL J. Biol. Chem. 271:23389-23394(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN THE REPLICATION OF MITOCHONDRIAL DNA. HAS CC BOTH 5'->3' DNA POLYMERASE AND 3'->5' EXONUCLEASE ACTIVITY. CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -!- COFACTOR: MAGNESIUM. CC -!- SUBUNIT: HETEROTRIMER COMPOSED OF A CATALYTIC SUBUNIT AND AN CC HOMODIMER OF ACCESSORY SUBUNITS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE DNA POLYMERASE TYPE-A FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U60298; AAC47290.1; -. DR EMBL; U62547; AAC47658.1; -. DR EMBL; AE003408; AAF44822.1; -. DR EMBL; AE003641; AAF53338.1; -. DR EMBL; AY089226; AAL89964.1; -. DR PIR; T13808; T13808. DR PIR; T13810; T13810. DR FlyBase; FBgn0004406; tam. DR GO; GO:0005760; C:gamma DNA polymerase complex; IDA. DR GO; GO:0005739; C:mitochondrion; NAS. DR GO; GO:0003895; F:gamma DNA-directed DNA polymerase activity; IDA. DR GO; GO:0006261; P:DNA dependent DNA replication; IDA. DR InterPro; IPR001098; DNA_pol. DR InterPro; IPR002297; DNA_polG. DR Pfam; PF00476; DNA_pol_A; 1. DR PRINTS; PR00867; DNAPOLG. DR SMART; SM00482; POLAc; 1. DR PROSITE; PS00447; DNA_POLYMERASE_A; 1. KW Transferase; DNA-directed DNA polymerase; DNA replication; KW DNA-binding; Mitochondrion; Magnesium; Transit peptide. FT TRANSIT 1 9 MITOCHONDRION. FT CHAIN 10 1145 DNA POLYMERASE GAMMA SUBUNIT 1. FT CONFLICT 114 114 A -> P (IN REF. 2). FT CONFLICT 241 241 T -> P (IN REF. 2). FT CONFLICT 250 250 T -> S (IN REF. 2). FT CONFLICT 273 273 T -> I (IN REF. 2). FT CONFLICT 319 319 S -> P (IN REF. 2). FT CONFLICT 326 326 V -> L (IN REF. 1). FT CONFLICT 478 478 L -> I (IN REF. 2). FT CONFLICT 530 530 A -> E (IN REF. 2). FT CONFLICT 600 600 H -> R (IN REF. 2). FT CONFLICT 732 732 M -> L (IN REF. 2). FT CONFLICT 952 952 N -> K (IN REF. 1 AND 5). SQ SEQUENCE 1145 AA; 129827 MW; 186AD02B63827707 CRC64; MQFHLIRKYA SKVSREHYAS SSVKIFRRVK PPQKVNKPKK PENVENGPTE YAENLVKVQM ISRNLHAQLF PQAPRSISEQ QVASAKVYKD ELRRHGVDIE SSAPVSDVQL KLPALRGANI EEHFHNIAKE QVQPYEELLL PLVQCEQLPK RPKRWAFHTG WTAYDPEDGT ATPVDHPLEK GLVFDVEVCV SEGQAPVLAT AVSTKRWYSW VSSKLTKHRL SVEKLEPLDV DTDSERPHYT TDELIPLGTT GPGLVVGHNV SYDRARLKEQ YLTEDTGTRF VDTMSLHMCV SGVTSYQRAM LKSKKEPAAE DLGWLEQSSL NSLVEVHRLY CGGDTLSKEP RNIFVEGTLE QVRQSFQSLT NYCASDVEAT HRILRVLYPL YAERFPHPAS LAGMLEMGSA YLPVNSNWER YIREAQLTYE DLSIEAKYHL GRRAEEACSL LLDDQYRQNL WLWDEDWSVQ ELKLKQPPKR KPLPTVELKD SGNTPEERRL QAKFQHLYDQ QALLPARRPL LPGYPLWYRK LCRKPPAKRA DEILEDDEEP WSPGASEIST GMQIAPKLLS LCWEGYPLHY EREQGWGFLV PFRSDSEGVD RLPMEQLLAH CPVPEFARLS ASKAESDMAF DMLPGQVEQH LGKREHYKKL SQKQQRLETQ YQGSGVWCNK VLDDCCFFLK LPHKNGPSFR VGNPLSKDFL NKFAENVLSS GDPSCQAAAR VIDIARMMSY WRNNRDRIMG QMVVWLDSQQ LPNEFTGEKC QPIAYGAICP QVVACGTLTR RAMEPTWMTA SNSRPDRLGS ELRSMVQAPP GYRLVGADVD SQELWIASVL GDAYACGEHG ATPLGWMTLS GSKSNGSDMH SITAKAVGIS RDHAKVINYA RIYGAGQLFA ETLLRQFNPT FSASEAKAKA MKMFSITKGK RVYRLREEFH DELEDRAYSS YEASRLAIQR NRTLAEVFHR PNWQGGTESA MFNRLEEIAT GSQPRTPFLG GRLSRALEAD TGPEQEQRFL PTRINWVVQS GAVDFLHLML VSMRWLMGSH VRFCLSFHDE LRYLVKEELS PKAALAMHIT NLMTRSFCVS RIGLQDLPMS VAFFSSVEVD TVLRKECTMD CKTPSNPHGL RIGYGIQPGQ SLSVAEAIEK AGGNDVSQWD WIKKS // ID DPLD_DROME STANDARD; PRT; 832 AA. AC Q9V4M2; Q95SY8; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Dappled protein. GN DPLD OR CG1624. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=96363925; PubMed=8725239; RA Rodriguez A., Zhou Z., Tang M.L., Meller S., Chen J., Bellen H., RA Kimbrell D.A.; RT "Identification of immune system and response genes, and novel RT mutations causing melanotic tumor formation in Drosophila RT melanogaster."; RL Genetics 143:929-940(1996). CC -!- FUNCTION: VITAL FOR LARVAL DEVELOPMENT. PLAYS A ROLE IN TUMOR CC FORMATION. CC -!- TISSUE SPECIFICITY: EXPRESSED IN NUMEROUS EMBRYONIC, LARVAL AND CC ADULT TISSUES. CC -!- SIMILARITY: CONTAINS 2 B BOX-TYPE ZINC FINGERS. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 591. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003841; AAF59245.2; -. DR EMBL; AY060421; AAL25460.1; ALT_FRAME. DR EMBL; BT010087; AAQ22556.1; -. DR FlyBase; FBgn0015930; dpld. DR GO; GO:0002168; P:larval development (sensu Insecta); IMP. DR GO; GO:0000074; P:regulation of cell cycle; IMP. DR InterPro; IPR001258; NHL. DR InterPro; IPR000315; Znf_Bbox. DR Pfam; PF01436; NHL; 5. DR Pfam; PF00643; zf-B_box; 2. DR SMART; SM00336; BBOX; 2. DR PROSITE; PS50119; ZF_BBOX; 2. KW Developmental protein; Metal-binding; Zinc; Zinc-finger; Repeat. FT ZN_FING 118 163 B BOX-TYPE 1. FT ZN_FING 184 224 B BOX-TYPE 2. SQ SEQUENCE 832 AA; 90573 MW; A5672AFC3FDE1FE1 CRC64; MMELLSNNSV PQQMASSNAP SANNVAHSST ANGSGGGSVS SNASNSSERL LAGILESFPA WDLNVGLLPN VGQSSPPRAD FFINNFLGGL DTHGDFSIGP IGSGARSNPK MSPESSNNSS ISCGWCEVSA SIRCLECNEF MCNDCLREHR NSPLSSNHSI VSLPTPIGAS PTGGSSVNAQ TPPSGNFICD IHNEMLRYVC DYCRKLVCQC CTLHEHKEHS YASIQSFMVG SKEKLEGAIE SSQVGTRCIK SSIDKALAFI RLIERNCSEL SDNIRKAFRQ FIIAIEDRER FLLDFVEKLR QRRLAILHDQ MAGLKSALAG LSETSDMLSK VADNACNMDQ IEIAMKLTNG QRQMEQFAGI YKDLQPKQEV FAFAPPDYSL LQDIRNQGGV ILVDDKNLPI VSSSNGIVPS VSSVNAVAAA SVGVVGGVAG VVGGVGVSNG LDLAFGMNMP NNPLSVASSS VRRPLLRDNS FRIPSPIMQP RGGSACGMSS GMSSAALDWE LNGLRSSPGL HFSAPRTTQA IPGCMDLVKV RNSNALSLSF ATEGHEDGQV SRPWGLCVDK MGHVLVSDRR NNRVQVFNPD GSLKFKFGRK GVGNGEFDLP AGICVDVDNR IIVVDKDNHR VQIFTASGVF LLKFGSYGKE YGQFQYPWDV AVNSRRQIVV TDSRNHRIQQ FDSEGRFIRQ IVFDNHGQTK GIASPRGVCY TPTGNIIVSD FDNHCLYLID PDINDILSVK GHEGSGFHEF NRPSGLCCDD EGRIIVADSK NQRILVFNQN LDFMWDIEVR PSINPLMPPT LDEKDRTCDV AIMPDGRIVF LIELSPDSKE GSNPYKRFVH VF // ID DPN_DROME STANDARD; PRT; 435 AA. AC Q26263; Q9V384; DT 15-DEC-1998 (Rel. 37, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Deadpan protein. GN DPN OR CG8704. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93051333; PubMed=1427077; RA Bier E., Vaessin H., Younger-Shepherd S., Jan L.Y., Jan Y.N.; RT "Deadpan, an essential pan-neural gene in Drosophila, encodes a RT helix-loop-helix protein similar to the hairy gene product."; RL Genes Dev. 6:2137-2151(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP WRPW MOTIF. RX MEDLINE=95094252; PubMed=8001118; RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., RA Brent R., Ish-Horowicz D.; RT "Groucho is required for Drosophila neurogenesis, segmentation, and RT sex determination and interacts directly with hairy-related bHLH RT proteins."; RL Cell 79:805-815(1994). CC -!- FUNCTION: TRANSCRIPTIONAL REPRESSOR OF GENES THAT REQUIRE A BHLH CC PROTEIN FOR THEIR TRANSCRIPTION. LIKELY TO BE INVOLVED IN THE CC FUNCTIONAL RATHER THAN THE MORPHOLOGICAL DIFFERENTIATION OF CC NEURONS. LOSS OF DPN FUNCTION RESULTS IN WEAK MOTOR ACTIVITY, CC LETHARGIC BEHAVIOR, AND DEATH. IMPLICATED IN SEX DETERMINATION AS CC GROUCHO-DPN COMPLEX ACT DIRECTLY TO REPRESS SXL TRANSCRIPTION. CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: EXPRESSED IN PRIMARY NEURAL PRECURSORS. CC -!- DEVELOPMENTAL STAGE: FIRST DETECTED IN PREBLASTODERM CYCLE 12 IN CC ALL NUCLEI. DURING MIDDLE TO LATE CYCLE 13, EXPRESSED IN EIGHT CC STRIPES THAT OVERLAP THOSE OF THE HAIRY PROTEIN. CC -!- DOMAIN: HAS A PARTICULAR TYPE OF BASIC DOMAIN (PRESENCE OF A CC HELIX-INTERRUPTING PROLINE) THAT BINDS TO THE N-BOX (CACNAG), CC RATHER THAN THE CANONICAL E-BOX (CANNTG). CC -!- DOMAIN: THE CARBOXYL-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL CC REPRESSION DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S48025; AAB24149.1; -. DR EMBL; AE003838; AAF59113.1; -. DR FlyBase; FBgn0010109; dpn. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; NAS. DR GO; GO:0008344; P:adult locomotory behavior; IMP. DR GO; GO:0007549; P:dosage compensation; IMP. DR GO; GO:0008345; P:larval locomotory behavior; IMP. DR GO; GO:0016481; P:negative regulation of transcription; NAS. DR GO; GO:0007540; P:sex determination, establishment of X:A ratio; IGI. DR GO; GO:0007530; P:sex determination; NAS. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Developmental protein; Nuclear protein; DNA-binding; KW Neurogenesis; Repressor; Transcription regulation. FT DNA_BIND 41 53 BASIC DOMAIN. FT DOMAIN 54 98 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 386 389 POLY-GLN. FT DOMAIN 432 435 WRPW MOTIF. FT CONFLICT 339 339 M -> L (IN REF. 1). SQ SEQUENCE 435 AA; 46551 MW; 9511A6C5F5019A29 CRC64; MDYKNDINSD DDFDCSNGYS DSYGSNGRMS NPNGLSKAEL RKTNKPIMEK RRRARINHCL NELKSLILEA MKKDPARHTK LEKADILEMT VKHLQSVQRQ QLNMAIQSDP SVVQKFKTGF VECAEEVNRY VSQMDGIDTG VRQRLSAHLN QCANSLEQIG SMSNFSNGYR GGLFPATAVT AAPTPLFPSL PQDLNNNSRT ESSAPAIQMG GLQLIPSRLP SGEFALIMPN TGSAAPPPGP FAWPGSAAGV AAGTASAALA SIANPTHLND YTQSFRMSAF SKPVNTSVPA NLPENLIHTL PGQTQLPVKN STSPPLSPIS SISSHCEESR AASPTVDVMS KHSFAGVFST PPPTSAETSF NTSGSLNLSA GSHDSSGCSR PLAHLQQQQV SSTSGIAKRD REAEAESSDC SLDEPSSKKF LAGAIEKSSS AWRPW // ID DPOA_DROME STANDARD; PRT; 1505 AA. AC P26019; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE DNA polymerase alpha catalytic subunit (EC 2.7.7.7). GN POLA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 131-136; 181-188 AND 238-251. RC STRAIN=Oregon-R; RX MEDLINE=92020137; PubMed=1923767; RA Hirose F., Yamaguchi M., Nishida Y., Masutani M., Miyazawa H., RA Hanaoka F., Matsukage A.; RT "Structure and expression during development of Drosophila RT melanogaster gene for DNA polymerase alpha."; RL Nucleic Acids Res. 19:4991-4998(1991). CC -!- FUNCTION: POLYMERASE ALPHA IN A COMPLEX WITH DNA PRIMASE IS A CC REPLICATIVE POLYMERASE. IN ADDITION TO POLYMERASE ACTIVITY, THIS CC DNA POLYMERASE EXHIBITS 3' TO 5' EXONUCLEASE ACTIVITY. CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -!- CATALYTIC ACTIVITY: DEGRADATION OF SINGLE-STRANDED DNA. IT ACTS CC PROGRESSIVELY IN A 3'- TO 5'-DIRECTION, RELEASING NUCLEOSIDE 5'- CC PHOSPHATES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: HIGH IN UNFERTILIZED EGGS AND EARLY EMBRYOS, CC RELATIVELY HIGH IN ADULT FEMALE FLIES AND SECOND-INSTAR LARVA, AND CC LOW IN BODIES AT OTHER STAGES OF DEVELOPMENT. CC -!- MISCELLANEOUS: IN EUKARYOTES THERE ARE FIVE DNA POLYMERASES: CC ALPHA, BETA, GAMMA, DELTA, AND EPSILON WHICH ARE RESPONSIBLE FOR CC DIFFERENT REACTIONS OF DNA SYNTHESIS. CC -!- MISCELLANEOUS: CONSERVED REGIONS II, IV, III AND I ARE THOUGHT TO CC BE INVOLVED IN SUBSTRATE RECOGNITION, BINDING OR PP(I) HYDROLYSIS. CC -!- SIMILARITY: BELONGS TO THE DNA POLYMERASE TYPE-B FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D90310; BAA14340.1; -. DR PIR; S28079; S28079. DR FlyBase; FBgn0004493; DNApol-alpha-180. DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA. DR GO; GO:0003889; F:alpha DNA polymerase activity; IDA. DR InterPro; IPR006172; DNA_pol_B. DR InterPro; IPR006134; DNA_pol_B_dom. DR InterPro; IPR006133; DNA_pol_B_exo. DR InterPro; IPR004578; Pol2. DR Pfam; PF00136; DNA_pol_B; 1. DR Pfam; PF03104; DNA_pol_B_exo; 1. DR PRINTS; PR00106; DNAPOLB. DR SMART; SM00486; POLBc; 1. DR TIGRFAMs; TIGR00592; pol2; 1. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. KW Transferase; DNA-directed DNA polymerase; DNA replication; KW DNA-binding; Hydrolase; Nuclease; Exonuclease; DNA repair; KW Multifunctional enzyme; Nuclear protein. FT DOMAIN 96 103 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DNA_BIND 675 734 POTENTIAL. FT DNA_BIND 1256 1385 POTENTIAL. FT DOMAIN 638 758 CONTAINS CONSERVED RESIDUES ESSENTIAL FOR FT 3' -> 5' EXONUCLEASE ACTIVITIES. SQ SEQUENCE 1505 AA; 171168 MW; A66B9442A9D79464 CRC64; MSESPSEPRA KRQRVDKNGR FAAMERLRQL KGTKNKCKVE DQVDDVYDVV DEREYAKRAQ EKYGDDWIEE DGTGYAEDLR DFFEDEDEYS DGEEDRKDSK KKKGVAPNSK KRPRENAKPV TGKASIKNLF SNAVPKKMDV KTSVKDDDIL ADILGEIKEE PAATSEKAEK VIAPAKISVT SRKFDAAAAK EYMNSFLNNM KVQEQERKKA EASSDNEMLE RILKPKAAVP NTKVAFFSSP TIKKEPMPEK TPAKKATEDP FSDNEMDFSC LDDDENQFDV EKTQQTEKVS QTKTAAEKTS QSKVAEKSAP KKETTGSPKE SESEDISRLL NNWESICQMD DDFEKSVLTT EQDSTISSDQ QLRLWYWEAY EDPVKIPGQV FLFGRTADGK SVCLRVQNIN RVLYLLPRQF LLDPISKEPT KQKVTVADIY KEFDSEVANQ LKLEFFRSRK VTKSFAHHAI GIEVPQSCDY LEVHYDGNKP LPNLSADKKY NSIAHIFGAT TNALERFLLD RKIKGPCWLQ VTGFKVSPTP MSWCNTEVTL TEPKNVELVQ DKGKPAPPPP LTLLSLNVRT SMNPKTSRNE ICMISMLTHN RFHIDRPAPQ PAFNRHMCAL TRPAVVSWPL DLNFEMAKYK STTVHKHDSE RALLSWFLAQ YQKIDADLIV TFDSMDCQLN VITDQIVALK IPQWSRMGRL RLSQSFGKRL LEHFVGRMVC DVKRSAEECI RARSYDLQTL CKQVLKLKES ERMEVNADDL LEMYEKGESI TKLISLTMQD NSYLLRLMCE LNIMPLALQI TNICGNTMTR TLQGGRSERN EFLLLHASTE KNYIVPDKKP VSKRSGAGDT DRTLSGADAT MQTKKKAAYA GGLVLEPMRG LYEKYVLLMD LNSLYPSIIQ EYNICFNPVQ QPVDADELPT LPDSKTEPGI LPLQLKRLVE SRKEVKKLMA APDLSPELQM QYHIRQMALK LTANSMYGCL GFAHSRFFAQ HLAALVTHKG RDLTNTQQLV QKMNYDVVYG DTDSLMINTN ITDYDQVYKI GHNIKQSVNK LYKQLELDID GVFGCLLLLK KKKYAAIKLS KDSKGNLRRE QEHKGLDIVR RDWSQLAVMV GKAVLDEVLS EKPLEEKLDA VHAQLEKIKT QIAEGVVPLP LFVITKQLTR TPQDYRNSAS LPHVQVALRM NRERNRRYKK GDMVDLCDCL DGTTNAAMQR AYHLDELKTS EDKKLQLDTN YYLGHQIHPV VTRMVEVLEG TDASRIAECL GMDPTKFRQN AQRTQRENTE QSEGESLLKT TLQLYRLCEP FRFQCVTCKT EQLMASAYRP GPSNSHIAVL QQCVSPSAKR HRFSTWQACA ILQLSMVQRF YKNWLVCDHP DCNFNTRTHS LRKKSHRPLC QKCRSGSCWS VYGAGPVQSA VLPAIHVRPR QANAAAKTLV SLSFTAFHIE IIFCPYYQAT LTPELEQAYQ LLYETVDQQL QSSSYVIISL SKLFARSLAQ MSCNRAWRSP HRSNSECFGG CGLSV // ID DPOD_DROME STANDARD; PRT; 1092 AA. AC P54358; Q9VUW8; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA polymerase delta catalytic subunit (EC 2.7.7.7). GN POLD OR DNAPOL-DELTA OR CG5949. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96125196; PubMed=8543168; RA Chiang C.S., Lehman I.R.; RT "Isolation and sequence determination of the cDNA encoding DNA RT polymerase delta from Drosophila melanogaster."; RL Gene 166:237-242(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: POSSESSES TWO ENZYMATIC ACTIVITIES: DNA SYNTHESIS CC (POLYMERASE) AND AN EXONUCLEOLYTIC ACTIVITY THAT DEGRADES SINGLE CC STRANDED DNA IN THE 3' TO 5' DIRECTION. REQUIRED WITH ITS CC ACCESSORY PROTEINS (PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) AND CC REPLICATION FACTOR C (RFC) OR ACTIVATOR 1) FOR LEADING STRAND CC SYNTHESIS. ALSO INVOLVED IN COMPLETING OKAZAKI FRAGMENTS INITIATED CC BY THE DNA POLYMERASE ALPHA/PRIMASE COMPLEX (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -!- SUBUNIT: HETERODIMER WITH SUBUNITS OF 125 KDA AND 50 KDA. THE 125 CC KDA SUBUNIT CONTAINS THE POLYMERASE ACTIVE SITE AND MOST LIKELY CC THE ACTIVE SITE FOR THE 3'-5' EXONUCLEASE ACTIVITY (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: IN EUKARYOTES THERE ARE FIVE DNA POLYMERASES: CC ALPHA, BETA, GAMMA, DELTA, AND EPSILON WHICH ARE RESPONSIBLE FOR CC DIFFERENT REACTIONS OF DNA SYNTHESIS. CC -!- SIMILARITY: BELONGS TO THE DNA POLYMERASE TYPE-B FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X88928; CAA61369.1; -. DR EMBL; AE003529; AAF49555.1; -. DR FlyBase; FBgn0012066; DNApol-delta. DR GO; GO:0005659; C:delta DNA polymerase complex; IDA. DR GO; GO:0008296; F:3'-5' exodeoxyribonuclease activity; IDA. DR GO; GO:0003891; F:delta DNA polymerase activity; IDA. DR InterPro; IPR006172; DNA_pol_B. DR InterPro; IPR006134; DNA_pol_B_dom. DR InterPro; IPR006133; DNA_pol_B_exo. DR InterPro; IPR004578; Pol2. DR Pfam; PF00136; DNA_pol_B; 1. DR Pfam; PF03104; DNA_pol_B_exo; 1. DR PRINTS; PR00106; DNAPOLB. DR SMART; SM00486; POLBc; 1. DR TIGRFAMs; TIGR00592; pol2; 1. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. KW Transferase; DNA-directed DNA polymerase; DNA replication; KW DNA-binding; Hydrolase; Exonuclease; Zinc-finger; Nuclear protein. FT DOMAIN 4 19 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT ZN_FING 997 1017 C4-TYPE (POTENTIAL). FT ZN_FING 1046 1064 C4-TYPE (POTENTIAL). FT CONFLICT 492 492 L -> S (IN REF. 1). SQ SEQUENCE 1092 AA; 124904 MW; 2FA380420298EA5C CRC64; MDGKRKFNGT SNGHAKKPRN PDDDEEMGFE AELAAFENSE DMDQTLLMGD GPENQTTSER WSRPPPPELD PSKHNLEFQQ LDVENYLGQP LPGMPGAQIG PVPVVRMFGV TMEGNSVCCH VHGFCPYFYI EAPSQFEEHH CEKLQKALDQ KVIADIRNNK DNVQEAVLMV ELVEKLNIHG YNGDKKQRYI KISVTLPRFV AAASRLLKKE VIMSEIDFQD CRAFENNIDF DIRFMVDTDV VGCNWIELPM GHWRIRNSHS KPLPESRCQI EVDVAFDRFI SHEPEGEWSK VAPFRILSFD IECAGRKGIF PEAKIDPVIQ IANMVIRQGE REPFIRNVFT LNECAPIIGS QVLCHDKETQ MLDKWSAFVR EVDPDILTGY NINNFDFPYL LNRAAHLKVR NFEYLGRIKN IRSVIKEQML QSKQMGRREN QYVNFEGRVP FDLLFVLLRD YKLRSYTLNA VSYHFLQEQK EDVHHSIITD LQNGDEQTRR RLAMYCLKDA YLPLRLLEKL MAIVNYMEMA RVTGVPLESL LTRGQQIKVL SQLLRKAKTK GFIMPSYTSQ GSDEQYEGAT VIEPKRGYYA DPISTLDFAS LYPSIMMAHN LCYTTLVLGG TREKLRQQEN LQDDQVERTP ANNYFVKSEV RRGLLPEILE SLLAARKRAK NDLKVETDPF KRKVLDGRQL ALKISANSVY GFTGAQVGKL PCLEISGSVT AYGRTMIEMT KNEVESHYTQ ANGYENNAVV IYGDTDSVMV NFGVKTLERS MELGREAAEL VSSKFVHPIK LEFEKVYYPY LLINKKRYAG LYFTRPDTYD KMDCKGIETV RRDNSPLVAN LMNSCLQKLL IERDPDGAVA YVKQVIADLL CNRIDISHLV ITKELAKTDY AAKQAHVELA AKMKKRDPGT APKLGDRVPY VICAAAKNTP AYQKAEDPLY VLENSVPIDA TYYLEQQLSK PLLRIFEPIL GDNAESILLK GEHTRTRTVV TSKVGGLAGF MTKKTSCLGC KSLMPKGYEQ ACLCPHCEPR MSELYQKEVG AKRELEETFS RLWTECQRCQ ESLHEEVICS NRDCPIFYMR QKVRMDLDNQ EKRVLRFGLA EW // ID DPP3_DROME STANDARD; PRT; 786 AA. AC Q9VHR8; Q8IHE9; Q961F1; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Dipeptidyl-peptidase III (EC 3.4.14.4) (DPP III) (Dipeptidyl DE aminopeptidase III) (Dipeptidyl arylamidase III). GN DPPIII OR CG7415. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Berkeley; TISSUE=Embryo, Head, and Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP IDENTIFICATION (ISOFORM 2). RX MEDLINE=21443463; PubMed=11559363; RA Mazzocco C., Fukasawa K.M., Raymond A.-A., Puiroux J.; RT "Purification, partial sequencing and characterization of an insect RT membrane dipeptidyl aminopeptidase that degrades the insect RT neuropeptide proctolin."; RL Eur. J. Biochem. 268:4940-4949(2001). RN [5] RP FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION (ISOFORM 2). RX MEDLINE=22731170; PubMed=12846841; RA Mazzocco C., Fukasawa K.M., Auguste P., Puiroux J.; RT "Characterization of a functionally expressed dipeptidyl RT aminopeptidase III from Drosophila melanogaster."; RL Eur. J. Biochem. 270:3074-3082(2003). CC -!- FUNCTION: DEGRADES NEUROPEPTIDE PROCTOLIN (RYLPT) BY CLEAVAGE CC BETWEEN TYR AND LEU RESIDUES. CC -!- CATALYTIC ACTIVITY: RELEASE OF AN N-TERMINAL DIPEPTIDE FROM A CC PEPTIDE COMPRISING FOUR OR MORE RESIDUES, WITH BROAD SPECIFICITY. CC ALSO ACTS ON DIPEPTIDYL 2-NAPHTHYLAMIDES. CC -!- COFACTOR: BINDS 1 ZINC ION PER SUBUNIT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN AND CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=A; CC IsoId=Q9VHR8-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; Synonyms=B; CC IsoId=Q9VHR8-2; Sequence=VSP_007939; CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M49. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003678; AAF54231.2; -. DR EMBL; AE003678; AAF54232.1; -. DR EMBL; AY051625; AAK93049.1; ALT_INIT. DR EMBL; BT001283; AAN71039.1; -. DR EMBL; BT001401; AAN71156.1; -. DR EMBL; BT001402; AAN71157.1; -. DR EMBL; BT001639; AAN71394.1; -. DR MEROPS; M49.001; -. DR FlyBase; FBgn0037580; DppIII. DR InterPro; IPR005317; Peptidase_M49. DR Pfam; PF03571; Peptidase_M49; 1. KW Hydrolase; Metalloprotease; Aminopeptidase; Zinc; Transmembrane; KW Alternative splicing. FT DOMAIN 1 108 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 109 129 POTENTIAL. FT DOMAIN 130 594 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 595 615 POTENTIAL. FT DOMAIN 616 786 CYTOPLASMIC (POTENTIAL). FT METAL 506 506 ZINC (CATALYTIC) (BY SIMILARITY). FT ACT_SITE 507 507 BY SIMILARITY. FT METAL 511 511 ZINC (CATALYTIC) (BY SIMILARITY). FT VARSPLIC 1 63 Missing (in isoform 2). FT /FTId=VSP_007939. SQ SEQUENCE 786 AA; 89194 MW; C13B945177F9D2D7 CRC64; MFWLRGLQRS RQQLNRLCHF RSRLNYGTSP SIRSVQPSIS RSLGFCSSLV RYSCSTNLPQ PAEMASKTAH FVLPNTQPIA DLDCKSAFEN LTEKEKLYAH HFSQASWDGG LIALIQSSPE APLIFSLLHR IFLAEKIPVL RAKALEAGVS ADDFTAFLVY ACGVFANAGN YKGMGDSKIV PNLSEKQFET IVKASAAYSD EPRVGKIFEK VKNLIYALES RNEILGFAPD GITTYWSDNC TKEDSEIVNA WLTSKRIEPY MCRTFKIVEN GQTVYDVKLG SVAESTQDGI TLPLEEYNGN KFRVTRGDYQ KLLQRVNQHL LQAQKYAANE NESKMIEHYV RSFEQGSLDE HKNGSRWWIK DKGPVIETYI GFIETYRDPA GGRAEFEGFV AMVNKESSAK FSELVNRAEK LIEYLPWTEP YEKDSYLKPD FTSLDVLTFA GSGVPAGINI PNYDEIRQDE GFKNVSLGNV LANINRKDPI PFLTEEDQTL MKEYKVKAFE VQVGLHELLG HGSGKLFRID ENGVYNFDKE NTKNLVTGEP ITKWYLPGET YDTKFGAIGS SYEECRAEAV GLYLSLQRDI LEIFGFKDKA EQDNIIYVNW LSLIWNGMGV ALEMFNPKSK LWLQAHSRAR FVIMKVLLEA GEGLVKVEET EKGKNLLLTV DRSKIDTVGR KALGDFLTKL QVYKSTADIE AASKMYEHYS KVDESGSHPW AKWRDICLAH KKPRMILVQA NTAIGQDQKV QLKTYEPTHE GYIQSWVERY PNTDIDDLLE SIVEKDKKYF PTAFNN // ID DRK_DROME STANDARD; PRT; 211 AA. AC Q08012; Q9V6Q5; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein E(sev)2B (SH2-SH3 adapter protein drk). GN DRK OR E(SEV)2B OR CG6033. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye; RX MEDLINE=93214989; PubMed=8462097; RA Simon M.A., Dodson G.S., Rubin G.M.; RT "An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds RT to sevenless and Sos proteins in vitro."; RL Cell 73:169-177(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=93214990; PubMed=8462098; RA Olivier J.P., Raabe T., Henkemeyer M., Dickson B., Mbamalu G., RA Margolis B., Schlessinger J., Hafen E., Pawson T.; RT "A Drosophila SH2-SH3 adaptor protein implicated in coupling the RT sevenless tyrosine kinase to an activator of Ras guanine nucleotide RT exchange, Sos."; RL Cell 73:179-191(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Ann Arbor1, Ann Arbor3, Ann Arbor16, Ann Arbor18, Ann Arbor20, RC CA2, CT1, Georgia-5b, Kakamega-2, Kakamega-b1, Kakamega-b2, RC Kenya-HLa3, Kenya-HLa4, Kenya-HLa6, Kenya-LGC, Makindu-1, Makindu-b1, RC Makindu-b5, M2, PYR2, Reids2, and Sapporo; RA Riley R.M., Jin W., Gibson G.; RT "Contrasting selection pressures on components of the Ras-mediated RT signal transduction pathway in Drosophila."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR PROPER SIGNALING BY SEVENLESS. MAY ACT TO CC STIMULATE THE ABILITY OF SOS TO CATALYZE RAS1 ACTIVATION BY CC LINKING SEVENLESS AND SOS IN A SIGNALING COMPLEX. CAN BIND, IN CC VITRO, TO SEVENLESS AND TO SOS. CC -!- TISSUE SPECIFICITY: FOUND MAINLY IN THE DEVELOPING EYE AND IN THE CC ANTENNAL DISK. ALSO OBSERVED IN OTHER IMAGINAL DISKS TESTED AND IN CC THE EMBRYO. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 2 SH3 DOMAINS. CC -!- SIMILARITY: BELONGS TO THE GRB2 / SEM-5 / DRK FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L12446; AAA28898.1; -. DR EMBL; L13173; -; NOT_ANNOTATED_CDS. DR EMBL; AY135053; AAN17564.1; -. DR EMBL; AY135054; AAN17565.1; -. DR EMBL; AY135055; AAN17566.1; -. DR EMBL; AY135056; AAN17567.1; -. DR EMBL; AY135057; AAN17568.1; -. DR EMBL; AY135058; AAN17569.1; -. DR EMBL; AY135059; AAN17570.1; -. DR EMBL; AY135060; AAN17571.1; -. DR EMBL; AY135061; AAN17572.1; -. DR EMBL; AY135062; AAN17573.1; -. DR EMBL; AY135063; AAN17574.1; -. DR EMBL; AY135064; AAN17575.1; -. DR EMBL; AY135065; AAN17576.1; -. DR EMBL; AY135066; AAN17577.1; -. DR EMBL; AY135067; AAN17578.1; -. DR EMBL; AY135068; AAN17579.1; -. DR EMBL; AY135069; AAN17580.1; -. DR EMBL; AY135070; AAN17581.1; -. DR EMBL; AY135071; AAN17582.1; -. DR EMBL; AY135072; AAN17583.1; -. DR EMBL; AY135073; AAN17584.1; -. DR EMBL; AY135074; AAN17585.1; -. DR EMBL; AE003818; AAM68581.1; -. DR EMBL; AY061142; AAL28690.1; -. DR PIR; A46444; A46444. DR HSSP; P29354; 1GRI. DR FlyBase; FBgn0004638; drk. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0005070; F:SH3/SH2 adaptor protein activity; NAS. DR GO; GO:0007265; P:RAS protein signal transduction; IPI. DR InterPro; IPR000108; Neu_cyt_fact_2. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3; 2. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 2. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 2. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 2. KW SH2 domain; SH3 domain; Repeat; Transducer. FT DOMAIN 1 58 SH3 1. FT DOMAIN 60 151 SH2. FT DOMAIN 152 211 SH3 2. FT MUTAGEN 67 67 R->H: IN SU(SEVS11)R1 MUTANT; OMMATIDIAL FT CELL DEVELOPMENT OBSTRUCTION. FT MUTAGEN 106 106 H->Y: IN E(SEV)2B MUTANT; OMMATIDIAL CELL FT DEVELOPMENT OBSTRUCTION. SQ SEQUENCE 211 AA; 24435 MW; A1D0614AF358F3C0 CRC64; MEAIAKHDFS ATADDELSFR KTQILKILNM EDDSNWYRAE LDGKEGLIPS NYIEMKNHDW YYGRITRADA EKLLSNKHEG AFLIRISESS PGDFSLSVKC PDGVQHFKVL RDAQSKFFLW VVKFNSLNEL VEYHRTASVS RSQDVKLRDM IPEEMLVQAL YDFVPQESGE LDFRRGDVIT VTDRSDENWW NGEIGNRKGI FPATYVTPYH S // ID DROS_DROME STANDARD; PRT; 64 AA. AC P36193; Q9V749; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Drosocin precursor. GN DRO OR CG10816. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SEQUENCE OF 22-40, AND CARBOHYDRATE-LINKAGE SITE RP THR-32. RC STRAIN=Oregon-R; RX MEDLINE=93315464; PubMed=8325867; RA Bulet P., Dimarcq J.-L., Hetru C., Lagueux M., Charlet M., Hegy G., RA van Dorsselaer A., Hoffmann J.A.; RT "A novel inducible antibacterial peptide of Drosophila carries an O- RT glycosylated substitution."; RL J. Biol. Chem. 268:14893-14897(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=97100194; PubMed=8944755; RA Charlet M., Lagueux M., Reichhart J.-M., Hoffmann D., Braun A., RA Meister M.; RT "Cloning of the gene encoding the antibacterial peptide drosocin RT involved in Drosophila immunity. Expression studies during the immune RT response."; RL Eur. J. Biochem. 241:699-706(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP CARBOHYDRATE-LINKAGE SITE SER-28, INDUCTION, MASS SPECTROMETRY, AND RP TISSUE SPECIFICITY. RX MEDLINE=98409659; PubMed=9736738; RA Uttenweiler-Josepash S., Moniatte M., Lagueux M., Van Dorsselaer A., RA Hoffmann J.A., Bulet P.; RT "Differential display of peptides induced during the immune response RT of Drosophila: a matrix-assisted laser desorption ionization RT time-of-flight mass spectrometry study."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998). RN [5] RP STRUCTURE BY NMR. RX MEDLINE=99105821; PubMed=9888811; RA McManus A.M., Otvos L. Jr., Hoffmann R., Craik D.J.; RT "Conformational studies by NMR of the antimicrobial peptide, drosocin, RT and its non-glycosylated derivative: effects of glycosylation on RT solution conformation."; RL Biochemistry 38:705-714(1999). CC -!- FUNCTION: ANTIBACTERIAL PEPTIDE WITH STRONG ANTI-GRAM-NEGATIVE CC BACTERIA ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: IN HEMOLYMPH 6 HOURS AFTER IMMUNE CHALLENGE, CC LEVELS OF EXPRESSION INCREASE FOR FIRST 24 HOURS AND PERSIST FOR CC THE FOLLOWING TWO WEEKS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN LARVAE AND IN ADULTS. CC -!- INDUCTION: BY BACTERIAL INFECTION. CC -!- PTM: O-GLYCOSYLATION IS ESSENTIAL FOR FULL BIOLOGICAL ACTIVITY. CC -!- MASS SPECTROMETRY: MW=2401.9; METHOD=MALDI; RANGE=ISOFORM WITH CC MONOSACCHARIDE ON THR-32. CC -!- MASS SPECTROMETRY: MW=2564.4; METHOD=MALDI; RANGE=ISOFORM WITH CC DISACCHARIDE ON SER-28 AND THR-32. CC -!- SIMILARITY: TO P.APTERUS PYRRHOCORICIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z21942; CAA79936.1; -. DR EMBL; X98416; CAA67062.1; -. DR EMBL; AE003813; AAF58216.1; -. DR PIR; S35984; A47103. DR FlyBase; FBgn0010388; Dro. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0008225; F:Gram-negative antibacterial peptide activity; IDA. DR GO; GO:0008224; F:Gram-positive antibacterial peptide activity; IDA. DR GO; GO:0006964; P:anti-Gram-negative bacterial polypeptide in...; IDA. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IEP. KW Antibiotic; Signal; Glycoprotein; Insect immunity. FT SIGNAL 1 19 POTENTIAL. FT PROPEP 20 21 FT PEPTIDE 22 40 DROSOCIN. FT PROPEP 43 64 POTENTIAL. FT CARBOHYD 28 28 O-LINKED (GALNAC...). FT CARBOHYD 32 32 O-LINKED (GALNAC...). FT CONFLICT 17 17 A -> G (IN REF. 3). FT CONFLICT 52 52 A -> T (IN REF. 3). SQ SEQUENCE 64 AA; 7068 MW; 51CE9C9A42FCAD10 CRC64; MKFTIVFLLL ACVFAMAVAT PGKPRPYSPR PTSHPRPIRV RREALAIEDH LAQAAIRPPP ILPA // ID DSH_DROME STANDARD; PRT; 623 AA. AC P51140; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Segment polarity protein dishevelled. GN DSH. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94116855; PubMed=8288125; RA Klingensmith J., Nusse R., Perrimon N.; RT "The Drosophila segment polarity gene dishevelled encodes a novel RT protein required for response to the wingless signal."; RL Genes Dev. 8:118-130(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94200163; PubMed=8149913; RA Theisen H., Purcell J., Bennett M., Kansagara D., Syed A., Marsh J.L.; RT "Dishevelled is required during wingless signaling to establish both RT cell polarity and cell identity."; RL Development 120:347-360(1994). RN [3] RP PHOSPHORYLATION. RX MEDLINE=95262901; PubMed=7744250; RA Yanagawa S.-I., van Leeuwen F., Wodarz A., Klingensmith J., Nusse R.; RT "The dishevelled protein is modified by wingless signaling in RT Drosophila."; RL Genes Dev. 9:1087-1097(1995). CC -!- FUNCTION: REQUIRED TO ESTABLISH COHERENT ARRAYS OF POLARIZED CELLS CC AND SEGMENTS IN EMBRYOS. PLAYS A ROLE IN WINGLESS (WG) SIGNALING, CC POSSIBLY THROUGH THE RECEPTION OF THE WG SIGNAL BY TARGET CELLS CC AND SUBSEQUENT REDISTRIBUTION OF ARM PROTEIN IN RESPONSE TO THAT CC SIGNAL IN EMBRYOS. THIS SIGNAL SEEMS TO BE REQUIRED TO ESTABLISH CC PLANAR CELL POLARITY AND IDENTITY. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. ASSOCIATED WITH THE MEMBRANE CC WHEN HYPERPHOSPHORYLATED. CC -!- TISSUE SPECIFICITY: FOUND IN EGG CHAMBERS OF THE OVARY AND CC UBIQUITOUSLY THROUGHOUT EMBRYOGENESIS AND IN DISCS. EXPRESSION IS CC NOT SEEN IN SALIVARY GLANDS, MUSCLES OR VENTRAL GANGLIA BUT IS CC OBSERVED IN BRAIN LOBES. CC -!- PTM: PHOSPHORYLATED. WG SIGNALING GENERATES HYPERPHOSPHORYLATED CC FORMS OF DSH WHICH ARE THE ACTIVE FORMS. CC -!- SIMILARITY: BELONGS TO THE DSH FAMILY. CC -!- SIMILARITY: CONTAINS 1 DEP DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PDZ/DHR DOMAIN. CC -!- SIMILARITY: CONTAINS 1 DIX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L26974; AAA16535.1; -. DR EMBL; U02491; AAA20216.1; -. DR PIR; A49840; A49840. DR HSSP; Q12923; 3PDZ. DR FlyBase; FBgn0000499; dsh. DR GO; GO:0005112; F:Notch binding; NAS. DR GO; GO:0006928; P:cell motility; IMP. DR GO; GO:0045198; P:establishment of epithelial cell polarity; IMP. DR GO; GO:0007164; P:establishment of tissue polarity; NAS. DR GO; GO:0008585; P:female gonad development; IMP. DR GO; GO:0007222; P:frizzled signaling pathway; NAS. DR GO; GO:0016318; P:ommatidial rotation; NAS. DR GO; GO:0007423; P:sensory organ development; NAS. DR InterPro; IPR000591; DEP. DR InterPro; IPR008339; Dishevell. DR InterPro; IPR003351; Dishevelled. DR InterPro; IPR001158; DIX. DR InterPro; IPR001478; PDZ. DR Pfam; PF00610; DEP; 1. DR Pfam; PF02377; Dishevelled; 1. DR Pfam; PF00778; DIX; 1. DR Pfam; PF00595; PDZ; 1. DR PRINTS; PR01760; DISHEVELLED. DR ProDom; PD003639; DIX; 1. DR SMART; SM00021; DAX; 1. DR SMART; SM00049; DEP; 1. DR SMART; SM00228; PDZ; 1. DR PROSITE; PS50186; DEP; 1. DR PROSITE; PS50841; DIX; 1. DR PROSITE; PS50106; PDZ; 1. KW Wnt signaling pathway; Developmental protein; KW Segmentation polarity protein; Phosphorylation. FT DOMAIN 8 91 DIX. FT DOMAIN 252 324 PDZ. FT DOMAIN 404 478 DEP. FT DOMAIN 119 146 POLY-GLN. FT DOMAIN 154 159 POLY-GLN. FT DOMAIN 551 557 POLY-SER. FT DOMAIN 599 608 POLY-GLY. FT CONFLICT 276 276 D -> N (IN REF. 2). FT CONFLICT 565 565 T -> I (IN REF. 2). FT CONFLICT 619 619 S -> F (IN REF. 2). SQ SEQUENCE 623 AA; 68845 MW; 0BA253CE4C0B71F5 CRC64; MDADRGGGQE TKVIYHIDDE TTPYLVKIPI PSAQVTLRDF KLVLNKQNNN YKYFFKSMDA DFGVVKEEIA DDSTILPCFN GRVVSWLVSA DGTNQSDNCS ELPTSECELG MGLTNRKLQQ QQQQHQQQQQ QQQQQHQQQQ QQQQQQVQPV QLAQQQQQQV LHHQKMMGNP LLQPPPLTYQ SASVLSSDLD STSLFGTESE LTLDRDMTDY SSVQRLQVRK KPQRRKKRAP SMSRTSSYSS ITDSTMSLNI ITVSINMEAV NFLGISIVGQ SNRGGDGGIY VGSIMKGGAV ALDGRIEPGD MILQVNDVNF ENMTNDEAVR VLREVVQKPG PIKLVVAKCW DPNPKGYFTI PRTEPVRPID PGAWVAHTQA LTSHDSIIAD IAEPIKERLD QNNLEEIVKA MTKPDSGLEI RDRMWLKITI PNAFIGADAV NWVLENVEDV QDRREARRIV SAMLRSNYIK HTVNKLTFSE QCYYVVNEER NPNLLGRGHL HPHQLPHGHG GHALSHADTE SITSDIGPLP NPPIYMPYSA TYNPSHGYQP IQYGIAERHI SSGSSSSDVL TSKDTSASQS DITSVIHQAN QLTIAAHGSN KSSGSSNRGG GGGGGGGGNN TNDQDVSVSN YVL // ID DSK_DROME STANDARD; PRT; 141 AA. AC P09040; Q8MYU9; Q9VMY4; DT 01-NOV-1988 (Rel. 09, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Drosulfakinins precursor [Contains: Drosulfakinin 0 (DSK-0); DE Drosulfakinin I (DSK-I); Drosulfakinin II (DSK-II)]. GN DSK OR BCDNA:RH46857 OR CG18090. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88314994; PubMed=2842322; RA Nichols R., Schneuwly S.A., Dixon J.E.; RT "Identification and characterization of a Drosophila homologue to the RT vertebrate neuropeptide cholecystokinin."; RL J. Biol. Chem. 263:12167-12170(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 126-139, SULFATION OF TYR-134, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- SIMILARITY: BELONGS TO THE GASTRIN/CHOLECYSTOKININ FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 10. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03957; AAB03703.1; ALT_FRAME. DR EMBL; AE003607; AAF52173.2; -. DR EMBL; AY113595; AAM29600.1; -. DR PIR; A31101; A31101. DR FlyBase; FBgn0000500; Dsk. DR GO; GO:0005184; F:neuropeptide hormone activity; NAS. DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS. DR InterPro; IPR001651; Gastrin. DR PROSITE; PS00259; GASTRIN; 2. KW Hormone; Cleavage on pair of basic residues; Amidation; Sulfation; KW Signal. FT SIGNAL 1 33 POTENTIAL. FT PROPEP 34 73 FT PEPTIDE 76 82 DROSULFAKININ 0 (POTENTIAL). FT PROPEP 86 111 FT PEPTIDE 114 122 DROSULFAKININ I (POTENTIAL). FT PEPTIDE 126 139 DROSULFAKININ II. FT MOD_RES 82 82 AMIDATION (G-83 PROVIDE AMIDE GROUP) FT (POTENTIAL). FT MOD_RES 117 117 SULFATION (POTENTIAL). FT MOD_RES 122 122 AMIDATION (G-123 PROVIDE AMIDE GROUP) FT (POTENTIAL). FT MOD_RES 134 134 SULFATION. FT MOD_RES 139 139 AMIDATION (G-140 PROVIDE AMIDE GROUP). SQ SEQUENCE 141 AA; 16150 MW; 496AD66494696C88 CRC64; MGPRSCTHFA TLFMPLWALA FCFLVVLPIP AQTTSLQNAK DDRRLQELES KIGGEIDQPI ANLVGPSFSL FGDRRNQKTM SFGRRVPLIS RPIIPIELDL LMDNDDERTK AKRFDDYGHM RFGKRGGDDQ FDDYGHMRFG R // ID DSOR_DROME STANDARD; PRT; 393 AA. AC Q24324; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Dual specificity mitogen-activated protein kinase kinase dSOR1 DE (EC 2.7.1.-) (Downstream of RAF) (MAPKK). GN DSOR1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93161415; PubMed=8381718; RA Tsuda L., Inoue Y.H., Yoo M.-A., Mizuno M., Hata M., Lim Y.-M., RA Adachi-Yamada T., Ryo H., Masamune Y., Nishida Y.; RT "A protein kinase similar to MAP kinase activator acts downstream of RT the raf kinase in Drosophila."; RL Cell 72:407-414(1993). CC -!- FUNCTION: REQUIRED DOWNSTREAM OF RAF IN THE SEVENLESS (SEV), TORSO CC (TOR), AND DROSOPHILA EGF RECEPTOR HOMOLOG (DER) SIGNAL CC TRANSDUCTION PATHWAYS. INVOLVED IN BOTH POSITIVE REGULATION (AT CC THE POSTERIOR TERMINUS) AND NEGATIVE REGULATION (AT THE ANTERIOR CC DOMAIN) OF TLL, AS IN OTHER TERMINAL CLASS GENE PRODUCTS, MAYBE CC VIA THE ERK-A KINASE. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, WITH CC HIGHEST LEVELS IN EARLY EMBRYOS, SUGGESTING A MATERNAL CC CONTRIBUTION. CC -!- PTM: MAPKK IS ITSELF DEPENDENT ON SER/THR PHOSPHORYLATION FOR CC ACTIVITY CATALYZED BY MAP KINASE KINASE KINASES (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. MAP CC KINASE KINASE SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D13782; BAA02925.1; -. DR PIR; A45176; A45176. DR FlyBase; FBgn0010269; Dsor1. DR GO; GO:0000165; P:MAPKKK cascade; NAS. DR GO; GO:0007165; P:signal transduction; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; Tyrosine-protein kinase; KW ATP-binding; Phosphorylation; Developmental protein. FT DOMAIN 84 361 PROTEIN KINASE. FT NP_BIND 90 98 ATP (BY SIMILARITY). FT BINDING 113 113 ATP (BY SIMILARITY). FT ACT_SITE 206 206 BY SIMILARITY. FT MOD_RES 234 234 PHOSPHORYLATION (BY RAF) (BY SIMILARITY). FT MOD_RES 238 238 PHOSPHORYLATION (BY RAF) (BY SIMILARITY). SQ SEQUENCE 393 AA; 43544 MW; 865A347DA6C2CAD3 CRC64; MSKNKLNLVL PPVNTEATVA AATVAPTPPF KTPSGTDLLG KPKTSIDALT ETLEGLDMGD TERKRIKMFL SQKEKIGELS DEDLEKLGEL GSGNGGVVMK VRHTHTHLIM ARKLIHLEVK PAIKKQILRE LKVLHECNFP HIVGFYGAFY SDGEISICME YMDGGSLDLI LKRAGRIPES ILGRITLAVL KGLSYLRDNH AIIHRDVKPS NILVNSSGEI KICDFGVSGQ LIDSMANSFV GTRSYMSPER LQGTHYSVQS DIWSLGLSLV EMAIGMYPIP PPNTATLESI FADNAEESGQ PTDEPRAMAI FELLDYIVNE PPPKLEHKIF STEFKDFVDI CLKKQPDERA DLKTLLSHPW IRKAELEEVD ISGWVCKTMD LPPSTPKRNT SPN // ID DSX_DROME STANDARD; PRT; 549 AA. AC P23023; P23022; Q9VHY0; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Doublesex protein. GN DSX OR CG11094. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS FEMALE AND MALE). RC TISSUE=Larva, and Pupae; RX MEDLINE=89168451; PubMed=2493994; RA Burtis K.C., Baker B.S.; RT "Drosophila doublesex gene controls somatic sexual differentiation by RT producing alternatively spliced mRNAs encoding related sex-specific RT polypeptides."; RL Cell 56:997-1010(1989). RN [2] RP SEQUENCE FROM N.A. (ISOFORM MALE). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP DNA-BINDING. RX MEDLINE=91330881; PubMed=1907913; RA Burtis K.C., Coschigano K.T., Baker B.S., Wensink P.C.; RT "The doublesex proteins of Drosophila melanogaster bind directly to a RT sex-specific yolk protein gene enhancer."; RL EMBO J. 10:2577-2582(1991). RN [4] RP DNA-BINDING DOMAIN, AND MUTAGENESIS. RX MEDLINE=93178426; PubMed=8440242; RA Erdman S.E., Burtis K.C.; RT "The Drosophila doublesex proteins share a novel zinc finger related RT DNA binding domain."; RL EMBO J. 12:527-535(1993). RN [5] RP FUNCTION. RC STRAIN=Canton-S; RX MEDLINE=22323098; PubMed=12435630; RA Dauwalder B., Tsujimoto S., Moss J., Mattox W.; RT "The Drosophila takeout gene is regulated by the somatic sex- RT determination pathway and affects male courtship behavior."; RL Genes Dev. 16:2879-2892(2002). CC -!- FUNCTION: CONTROLS SOMATIC SEXUAL DIFFERENTIATION. BINDS DIRECTLY CC AND SPECIFICALLY TO THE FBE (FAT BODY ENHANCER) OF THE YOLK CC PROTEIN 1 AND 2 GENES (YP1 AND YP2). THIS ENHANCER IS SUFFICIENT CC TO DIRECT THE FEMALE-SPECIFIC TRANSCRIPTION CHARACTERISTIC OF THE CC YP GENES IN ADULT FAT BODIES. INVOLVED IN REGULATION OF MALE- CC SPECIFIC EXPRESSION OF TAKEOUT IN BRAIN-ASSOCIATED FAT BODY. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Male; CC IsoId=P23023-1; Sequence=Displayed; CC Name=Female; CC IsoId=P23023-2; Sequence=VSP_001321, VSP_001322; CC -!- MISCELLANEOUS: EXPERIMENTALLY SHOWN TO BIND ZINC. CC -!- SIMILARITY: CONTAINS 1 DM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M25292; AAA17840.1; -. DR EMBL; M25293; AAA17841.1; -. DR EMBL; M25294; AAA17842.1; -. DR EMBL; AE003676; AAF54168.1; -. DR PIR; A32372; A32372. DR PIR; B32372; B32372. DR PDB; 1LPV; 02-OCT-02. DR TRANSFAC; T00955; -. DR TRANSFAC; T00956; -. DR FlyBase; FBgn0000504; dsx. DR GO; GO:0003729; F:mRNA binding; NAS. DR GO; GO:0003700; F:transcription factor activity; NAS. DR GO; GO:0007619; P:courtship behavior; NAS. DR GO; GO:0045497; P:female analia morphogenesis (sensu Holometa...; NAS. DR GO; GO:0007486; P:female genital morphogenesis (sensu Holomet...; IGI. DR GO; GO:0019101; P:female somatic sex determination; NAS. DR GO; GO:0007483; P:genital disc metamorphosis; NAS. DR GO; GO:0045496; P:male analia morphogenesis (sensu Holometabola); NAS. DR GO; GO:0045433; P:male courtship behavior (sensu Insecta), so...; NAS. DR GO; GO:0007485; P:male genital morphogenesis (sensu Holometab...; IGI. DR GO; GO:0019102; P:male somatic sex determination; NAS. DR GO; GO:0045892; P:negative regulation of transcription, DNA-d...; NAS. DR GO; GO:0045893; P:positive regulation of transcription, DNA-d...; NAS. DR GO; GO:0007548; P:sex differentiation; NAS. DR InterPro; IPR001275; DM_DNA-binding. DR Pfam; PF00751; DM-domain; 1. DR SMART; SM00301; DM; 1. DR PROSITE; PS40000; DM_DOMAIN_1; 1. DR PROSITE; PS50809; DM_DOMAIN_2; 1. KW Sexual differentiation; Alternative splicing; DNA-binding; KW Transcription regulation; Nuclear protein; Zinc; Metal-binding; KW 3D-structure. FT DNA_BIND 44 91 DM. FT DOMAIN 119 224 HIS-RICH. FT DOMAIN 267 296 SER/GLY-RICH. FT VARSPLIC 398 427 ARVEINRTVAQIYYNYYTPMALVNGAPMYL -> GQYVVNE FT YSRQHNLNIYDGGELRNTTRQCG (in isoform FT Female). FT /FTId=VSP_001321. FT VARSPLIC 428 549 Missing (in isoform Female). FT /FTId=VSP_001322. FT MUTAGEN 47 47 C->A,H: ABOLISHES DNA-BINDING. FT MUTAGEN 50 50 H->Y: ABOLISHES DNA-BINDING. FT MUTAGEN 59 59 H->Y: ABOLISHES DNA-BINDING. FT MUTAGEN 68 68 C->D,Y: ABOLISHES DNA-BINDING. FT MUTAGEN 70 70 C->Y: ABOLISHES DNA-BINDING. FT MUTAGEN 91 91 R->Q: ABOLISHES DNA-BINDING. SQ SEQUENCE 549 AA; 57409 MW; 3C1B92724E4CE083 CRC64; MVSEENWNSD TMSDSDMIDS KNDVCGGASS SSGSSISPRT PPNCARCRNH GLKITLKGHK RYCKFRYCTC EKCRLTADRQ RVMALQTALR RAQAQDEQRA LHMHEVPPAN PAATTLLSHH HHVAAPAHVH AHHVHAHHAH GGHHSHHGHV LHHQQAAAAA AAAPSAPASH LGGSSTAASS IHGHAHAHHV HMAAAAAASV AQHQHQSHPH SHHHHHQNHH QHPHQQPATQ TALRSPPHSD HGGSVGPATS SSGGGAPSSS NAAAATSSNG SSGGGGGGGG GSSGGGAGGG RSSGTSVITS ADHHMTTVPT PAQSLEGSCD SSSPSPSSTS GAAILPISVS VNRKNGANVP LGQDVFLDYC QKLLEKFRYP WELMPLMYVI LKDADANIEE ASRRIEEARV EINRTVAQIY YNYYTPMALV NGAPMYLTYP SIEQGRYGAH FTHLPLTQIC PPTPEPLALS RSPSSPSGPS AVHNQKPSRP GSSNGTVHSA ASPTMVTTMA TTSSTPTLSR RQRSRSATPT TPPPPPPAHS SSNGAYHHGH HLVSSTAAT // ID DS_DROME STANDARD; PRT; 3503 AA. AC Q24292; Q9VPS4; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dachsous protein precursor (Adherin). GN DS OR CG17941. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Embryo; RX MEDLINE=95324813; PubMed=7601355; RA Clark H.F., Brentrup D., Schneitz K., Bieber A., Goodman C., Noll M.; RT "Dachsous encodes a member of the cadherin superfamily that controls RT imaginal disc morphogenesis in Drosophila."; RL Genes Dev. 9:1530-1542(1995). RN [2] RP REVISIONS. RA Noll M.; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: INVOLVED IN MORPHOGENESIS. MAY ALSO BE INVOLVED IN CELL CC ADHESION. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN EMBRYONIC ECTODERM. IN LARVAE, CC EXPRESSION IS RESTRICTED TO IMAGINAL DISKS AND BRAIN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYOGENESIS WHERE IT CC IS FIRST DETECTED DURING GASTRULATION. ALSO EXPRESSED IN LARVAE CC AND ADULTS. CC -!- SIMILARITY: CONTAINS 27 CADHERIN DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08811; AAA79329.2; -. DR EMBL; AE003588; AAF51468.3; ALT_INIT. DR HSSP; P15116; 1NCJ. DR FlyBase; FBgn0000497; ds. DR GO; GO:0005887; C:integral to plasma membrane; ISS. DR GO; GO:0008014; F:calcium-dependent cell adhesion molecule ac...; ISS. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion; ISS. DR GO; GO:0008283; P:cell proliferation; IMP. DR GO; GO:0000904; P:cellular morphogenesis during differentiation; IMP. DR GO; GO:0045317; P:equator specification; IMP. DR GO; GO:0045198; P:establishment of epithelial cell polarity; IMP. DR GO; GO:0018149; P:protein-protein cross-linking; IPI. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR000233; Cadherin_C_term. DR Pfam; PF00028; cadherin; 26. DR Pfam; PF01049; Cadherin_C_term; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 25. DR PROSITE; PS00232; CADHERIN_1; 20. DR PROSITE; PS50268; CADHERIN_2; 27. KW Cell adhesion; Glycoprotein; Transmembrane; Calcium; Calcium-binding; KW Repeat; Signal; Developmental protein. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 3503 DACHSOUS PROTEIN. FT DOMAIN 21 3045 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 3046 3066 POTENTIAL. FT DOMAIN 3067 3503 CYTOPLASMIC (POTENTIAL). FT DOMAIN 22 121 CADHERIN 1. FT DOMAIN 122 233 CADHERIN 2. FT DOMAIN 234 340 CADHERIN 3. FT DOMAIN 345 451 CADHERIN 4. FT DOMAIN 452 558 CADHERIN 5. FT DOMAIN 559 662 CADHERIN 6. FT DOMAIN 663 774 CADHERIN 7. FT DOMAIN 775 878 CADHERIN 8. FT DOMAIN 879 983 CADHERIN 9. FT DOMAIN 984 1100 CADHERIN 10. FT DOMAIN 1101 1203 CADHERIN 11. FT DOMAIN 1205 1312 CADHERIN 12. FT DOMAIN 1313 1432 CADHERIN 13. FT DOMAIN 1433 1549 CADHERIN 14. FT DOMAIN 1556 1666 CADHERIN 15. FT DOMAIN 1667 1794 CADHERIN 16. FT DOMAIN 1796 1899 CADHERIN 17. FT DOMAIN 1900 2004 CADHERIN 18. FT DOMAIN 2005 2111 CADHERIN 19. FT DOMAIN 2114 2269 CADHERIN 20. FT DOMAIN 2270 2375 CADHERIN 21. FT DOMAIN 2375 2479 CADHERIN 22. FT DOMAIN 2489 2595 CADHERIN 23. FT DOMAIN 2596 2699 CADHERIN 24. FT DOMAIN 2701 2809 CADHERIN 25. FT DOMAIN 2810 2916 CADHERIN 26. FT DOMAIN 2919 3028 CADHERIN 27. FT CONFLICT 1070 1070 V -> I (IN REF. 1). FT CONFLICT 1490 1490 R -> S (IN REF. 1). FT CONFLICT 1636 1636 G -> S (IN REF. 1). FT CONFLICT 1692 1692 S -> P (IN REF. 1). FT CONFLICT 1804 1804 V -> I (IN REF. 1). FT CONFLICT 2029 2029 L -> I (IN REF. 1). FT CONFLICT 2210 2210 P -> A (IN REF. 1). FT CONFLICT 2289 2289 A -> S (IN REF. 1). FT CONFLICT 2536 2536 S -> T (IN REF. 1). FT CONFLICT 2862 2862 R -> Q (IN REF. 1). FT CONFLICT 3038 3038 S -> G (IN REF. 1). SQ SEQUENCE 3503 AA; 379774 MW; 975B09F059F7EEF5 CRC64; MLRSSLLILL AIVLLGSSQA ASHDQERERK LEVFEGVAVD YQIGYIGDFG GIDSGPPYII VAEAGVETDL AIDRATGEIR TKVKLDRETR ASYSLVAIPL SGRNIRVLVT VKDENDNAPT FPQTSMHIEF PENTPREVKR TLLPARDLDL EPYNTQRYNI VSGNVNDAFR LSSHRERDGV LYLDLQISGF LDRETTPGYS LLIEALDGGT PPLRGFMTVN ITIQDVNDNQ PIFNQSRYFA TVPENATVGT SVLQVYASDT DADENGLVEY AINRRQSDKE QMFRIDPRTG AIYINKALDF ETKELHELVV VAKDHGEQPL ETTAFVSIRV TDVNDNQPTI NVIFLSDDAS PKISESAQPG EFVARISVHD PDSKTEYANV NVTLNGGDGH FALTTRDNSI YLVIVHLPLD REIVSNYTLS VVATDKGTPP LHASKSIFLR ITDVNDNPPE FEQDLYHANV MEVADPGTSV LQVLAHDRDE GLNSALTYSL AETPETHAQW FQIDPQTGLI TTRSHIDCET EPVPQLTVVA RDGGVPPLSS TATVLVTIHD VNDNEPIFDQ SFYNVSVAEN EPVGRCILKV SASDPDCGVN AMVNYTIGEG FKHLTEFEVR SASGEICIAG ELDFERRSSY EFPVLATDRG GLSTTAMIKM QLTDVNDNRP VFYPREYKVS LRESPKASSQ ASSTPIVAVV ATDPDYGNFG QVSYRIVAGN EAGIFRIDRS TGEIFVVRPD MLSVRTQPMH MLNISATDGG NLRSNADAVV FLSIIDAMQR PPIFEKARYN YYVKEDIPRG TVVGSVIAAS GDVAHRSPVR YSIYSGDPDG YFSIETNSGN IRIAKPLDHE AKSQVLLNIQ ATLGEPPVYG HTQVNIEVED VNDNAPEFEA SMVRISVPES AELGAPLYAA HAHDKDSGSS GQVTYSLVKE SGKGLFAIDA RSGHLILSQH LDYESSQRHT LIVTATDGGV PSLSTNLTIL VDVQDVNDNP PVFEKDEYSV NVSESRSINA QIIQVNASDL DTGNNARITY RIVDAGVDNV TNSISSSDVS QHFGIFPNSG WIYLRAPLDR ETRDRYQLTV LATDNGTPAA HAKTRVIVRV LDANDNDPKF QKSKYEFRIE ENLRRGSVVG VVTASDLDLG ENAAIRYSLL PINSSFQVHP VTGEISTREP LDRELRELYD LVVEARDQGT PVRSARVPVR IHVSDVNDNA PEIADPQEDV VSVREEQPPG TEVVRVRAVD RDHGQNASIT YSIVKGRDSD GHGLFSIDPT SGVIRTRVVL DHEERSIYRL GVAASDGGNP PRETVRMLRV EVLDLNDNRP TFTSSSLVFR VREDAALGHV VGSISPIERP ADVVRNSVEE SFEDLRVTYT LNPLTKDLIE AAFDIDRHSG NLVVARLLDR EVQSEFRLEI RALDTTASNN PQSSAITVKI EVADVNDNAP EWPQDPIDLQ VSEATPVGTI IHNFTATDAD TGTNGDLQYR LIRYFPQLNE SQEQAMSLFR MDSLTGALSL QAPLDFEAVQ EYLLIVQALD QSSNVTERLQ TSVTVRLRIL DANDHAPHFV SPNSSGGKTA SLFISDATRI GEVVAHIVAV DEDSGDNGQL TYEITGGNGE GRFRINSQTG IIELVKSLPP ATEDVEKGGR FNLIIGAKDH GQPEPKKSSL NLHLIVQGSH NNPPRFLQAV YRATILENVP SGSFVLQVTA KSLHGAENAN LSYEIPAGVA NDLFHVDWQR GIITTRGQFD RESQASYVLP VYVRDANRQS TLSSSAVRKQ RSSDSIGDTS NGQHFDVATI YITVGDVNDN SPEFRPGSCY GLSVPENSEP GVIHTVVASD LDEGPNADLI YSITGGNLGN KFSIDSSSGE LSARPLDREQ HSRYTLQIQA SDRGQPKSRQ GHCNITIFVE DQNDNAPRFK LSKYTGSVQE DAPLGTSVVQ ISAVDADLGV NARLVYSLAN ETQWQFAIDG QSGLITTVGK LDRELQASYN FMVLATDGGR YEVRSATVPV QINVLDINDN RPIFERYPYI GQVPALIQPG QTLLKVQALD ADLGANAEIV YSLNAENSAV SAKFRINPST GALSASQSLA SESGKLLHLE VVARDKGNPP QSSLGLIELL IGEAPQGTPV LRFQNETYRV MLKENSPSGT RLLQVVALRS DGRRQKVQFS FGAGNEDGIL SLDSLSGEIR VNKPHLLDYD RFSTPSMSAL SRGRALHYEE EIDESSEEDP NNSTRSQRAL TSSSFALTNS QPNEIRVVLV ARTADAPFLA SYAELVIELE DENDNSPKFS QKQFVATVSE GNNKGTFVAQ VHAFDSDAGS NARLRYHIVD GNHDNAFVIE PAFSGIVRTN IVLDREIRDI YKLKIIATDE GVPQMTGTAT IRVQIVDVND NQPTFPPNNL VTVSEATELG AVITSISAND VDTYPALTYR LGAESTVDIE NMSIFALDRY SGKLVLKRRL DYELQQEYEL DVIASDAAHE ARTVLTVRVN DENDNAPVFL AQQPPAYFAI LPAISEISES LSVDFDLLTV NATDADSEGN NSKVIYIIEP AQEGFSVHPS NGVVSVNMSR LQPAVSSSGD YFVRIIAKDA GKPALKSSTL LRVQANDNGS GRSQFLQNQY RAQISEAAPL GSVVLQLGQD ALDQSLAIIA GNEESAFELL QSKAIVLVKP LDRERNDLYK LRLVLSHPHG PPLISSLNSS SGISVIITIL DANDNFPIFD RSAKYEAEIS ELAPLRYSIA QLQAIDADQE NTPNSEVVYD ITSGNDEHMF TIDLVTGVLF VNNRLDYDSG AKSYELIIRA CDSHHQRPLC SLQPFRLELH DENDNEPKFP LTEYVHFLAE NEPVGSSVFR AHASDLDKGP FGQLNYSIGP APSDESSWKM FRVDSESGLV TSAFVFDYEQ RQRYDMELLA SDMGGKKASV AVRVEIESRD EFTPQFTERT YRFVLPAAVA LPQGYVVGQV TATDSDSGPD GRVVYQLSAP HSHFKVNRSS GAVLIKRKLK LDGDGDGNLY MDGRDISLVI SASSGRHNSL SSMAVVEIAL DPLAHPGTNL ASAGGSSSGS IGDWAIGLLV AFLLVLCAAA GIFLFIHMRS RKPRNAVKPH LATDNAGVGN TNSYVDPSAF DTIPIRGSIS GGAAGAASGQ FAPPKYDEIP PFGAHAGSSG AATTSELSGS EQSGSSGRGS AEDDGEDEEI RMINEGPLHH RNGGAGAGSD DGRISDISVQ NTQEYLARLG IVDHDPSGAG GGASSMAGSS HPMHLYHDDD ATARSDITNL IYAKLNDVTG AGSEIGSSAD DAGTTAGSIG TIGTAITHGH GVMSSYGEVP VPVPVVVGGS NVGGSLSSIV HSEEELTGSY NWDYLLDWGP QYQPLAHVFS EIARLKDDTL SEHSGSGASS SAKSKHSSSH SSAGAGSVVL KPPPSAPPTH IPPPLLTNVA PRAINLPMRL PPHLSLAPAH LPRSPIGHEA SGSFSTSSAM SPSFSPSLSP LATRSPSISP LGAGPPTHLP HVSLPRHGHA PQPSQRGNVG TRM // ID DX_DROME STANDARD; PRT; 738 AA. AC Q23985; Q86P53; Q9W3Z1; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Deltex protein. GN DX OR CG3929. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94200599; PubMed=8150285; RA Busseau I., Diederich R.J., Xu T., Artavanis-Tsakonas S.; RT "A member of the Notch group of interacting loci, deltex encodes a RT cytoplasmic basic protein."; RL Genetics 136:585-596(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 17-738 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, AND INTERACTION WITH NOTCH. RX MEDLINE=95401878; PubMed=7671825; RA Matsuno K., Diederich R.J., Go M.J., Blaumueller C.M., RA Artavanis-Tsakonas S.; RT "Deltex acts as a positive regulator of Notch signaling through RT interactions with the Notch ankyrin repeats."; RL Development 121:2633-2644(1995). RN [5] RP FUNCTION. RX MEDLINE=21575956; PubMed=11719214; RA Ramain P., Khechumian K., Seugnet L., Arbogast N., Ackermann C., RA Heitzler P.; RT "Novel Notch alleles reveal a Deltex-dependent pathway repressing RT neural fate."; RL Curr. Biol. 11:1729-1738(2001). RN [6] RP FUNCTION, HOMOMULTIMERIZATION, AND MUTAGENESIS OF 476-ARG--PRO-484; RP HIS-571 AND HIS-574. RX MEDLINE=21850204; PubMed=11861487; RA Matsuno K., Ito M., Hori K., Miyashita F., Suzuki S., Kishi N., RA Artavanis-Tsakonas S., Okano H.; RT "Involvement of a proline-rich motif and RING-H2 finger of Deltex in RT the regulation of Notch signaling."; RL Development 129:1049-1059(2002). CC -!- FUNCTION: REGULATOR OF NOTCH SIGNALING, A SIGNALING PATHWAY CC INVOLVED IN CELL-CELL COMMUNICATIONS THAT REGULATES A BROAD CC SPECTRUM OF CELL-FATE DETERMINATIONS. MAINLY ACTS AS A POSITIVE CC REGULATOR OF NOTCH, BUT IT MAY ALSO ACT AS A NEGATIVE REGULATOR, CC DEPENDING ON THE DEVELOPMENTAL AND CELL CONTEXT. MEDIATES THE CC ANTINEURAL ACTIVITY OF NOTCH. MAY FUNCTION AS AN UBIQUITIN LIGASE CC PROTEIN IN THE NOTCH PATHWAY. CC -!- SUBUNIT: HOMOMULTIMER; THE OLIGOMERIZATION IS REQUIRED FOR ITS CC FUNCTION. INTERACTS WITH THE ANKYRIN REPEATS OF NOTCH. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: UBIQUITOUS. EXPRESSED AT LOW LEVELS THROUGHOUT CC EMBRYOGENESIS AND IN LARVAE. CC -!- DOMAIN: THE WWE DOMAINS ARE THOUGHT TO MEDIATE SOME PROTEIN- CC PROTEIN INTERACTION, AND ARE FREQUENTLY FOUND IN UBIQUITIN LIGASES CC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE DELTEX FAMILY. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -!- SIMILARITY: CONTAINS 2 WWE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U09789; AAA18501.1; -. DR EMBL; AE003437; AAF46170.1; -. DR EMBL; BT003476; AAO39479.1; ALT_INIT. DR PIR; S47857; S47857. DR FlyBase; FBgn0000524; dx. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0007219; P:N signaling pathway; IGI. DR GO; GO:0045746; P:negative regulation of N signaling pathway; IDA. DR GO; GO:0045747; P:positive regulation of N signaling pathway; IDA. DR GO; GO:0016055; P:Wnt receptor signaling pathway; IMP. DR InterPro; IPR004170; WWE_dom. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF02825; WWE; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00678; WWE; 1. DR PROSITE; PS50918; WWE; 2. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW SH3-binding; Repeat; Metal-binding; Zinc; Zinc-finger. FT DOMAIN 35 118 WWE 1. FT DOMAIN 119 201 WWE 2. FT ZN_FING 548 603 RING-TYPE. FT DOMAIN 1 304 INTERACTION WITH NOTCH. FT DOMAIN 251 303 GLN/HIS-RICH (OPA-REPEAT). FT DOMAIN 332 472 SER-RICH. FT DOMAIN 489 514 POLY-GLN (OPA-REPEAT). FT SITE 480 484 SH3-BINDING (POTENTIAL). FT MUTAGEN 571 571 H->A: LOSS OF FUNCTION; ABOLISHES FT HOMOMULTIMERIZATION; WHEN ASSOCIATED WITH FT A-574. FT MUTAGEN 574 574 H->A: LOSS OF FUNCTION; ABOLISHES FT HOMOMULTIMERIZATION; WHEN ASSOCIATED WITH FT A-571. FT MUTAGEN 476 484 MISSING: DOMINANT-NEGATIVE MUTANT THAT FT INHIBITS NOTCH SIGNALING. FT CONFLICT 107 108 AG -> R (IN REF. 1). FT CONFLICT 120 120 F -> L (IN REF. 1). FT CONFLICT 188 189 QL -> HV (IN REF. 1). FT CONFLICT 268 268 H -> L (IN REF. 1). FT CONFLICT 444 444 R -> S (IN REF. 3). FT CONFLICT 468 468 L -> V (IN REF. 1). SQ SEQUENCE 738 AA; 82186 MW; 7B1CF29E024D26AF CRC64; MASSAGSAAS GSVVPGGGGS AASSCATMAL STAGSGGPPV NHAHAVCVWE FESRGKWLPY SPAVSQHLER AHAKKLTRVM LSDADPSLEQ YYVNVRTMTQ ESEAETAGSG LLTIGVRRMF YAPSSPAGKG TKWEWSGGSA DSNNDWRPYN MHVQCIIEDA WARGEQTLDL CNTHIGLPYT INFCNLTQLR QPSGPMRSIR RTQQAPYPLV KLTPQQANQL KSNSASVSSQ YNTLPKLGDT KSLHRVPMTR QQHPLPTSHQ VQQQQHQHQH QQQQQQQHHH QHQQQQHQQQ QQHQMQHHQI HHQTAPRKPP KKHSEISTTN LRQILNNLNI FSSSTKHQSN MSTAASASSS SSSASLHHAN HLSHAHFSHA KNMLTASMNS HHSRCSEGSL QSQRSSRMGS HRSRSRTRTS DTDTNSVKSH RRRPSVDTVS TYLSHESKES LRSRNFAISV NDLLDCSLGS DEVFVPSLPP SSLGERAPVP PPLPLHPRQQ QQQQQQQQQL QMQQQQQAQQ QQQQSIAGSI VGVDPASDMI SRFVKVVEPP LWPNAQPCPM CMEELVHSAQ NPAISLSRCQ HLMHLQCLNG MIIAQQNEMN KNLFIECPVC GIVYGEKVGN QPIGSMSWSI ISKNLPGHEG QNTIQIVYDI ASGLQTEEHP HPGRAFFAVG FPRICYLPDC PLGRKVLRFL KIAFDRRLLF SIGRSVTTGR EDVVIWNSVD HKTQFNMFPD PTYLQRTMQQ LVHLGVTD // ID DYHC_DROME STANDARD; PRT; 4639 AA. AC P37276; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dynein heavy chain, cytosolic (DYHC). GN CDHC OR DHC64C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94375524; PubMed=8089180; RA Li M., McGrail M., Serr M., Hays T.S.; RT "Drosophila cytoplasmic dynein, a microtubule motor that is RT asymmetrically localized in the oocyte."; RL J. Cell Biol. 126:1475-1494(1994). RN [2] RP SEQUENCE OF 1877-1998 FROM N.A. RX MEDLINE=94243034; PubMed=8186464; RA Rasmusson K., Serr M., Gepner J., Gibbons I., Hays T.S.; RT "A family of dynein genes in Drosophila melanogaster."; RL Mol. Biol. Cell 5:45-55(1994). CC -!- FUNCTION: CYTOPLASMIC DYNEIN ACTS AS A MOTOR FOR THE INTRACELLULAR CC RETROGRADE MOTILITY OF VESICLES AND ORGANELLES ALONG MICROTUBULES. CC DYNEIN HAS ATPASE ACTIVITY; THE FORCE-PRODUCING POWER STROKE IS CC THOUGHT TO OCCUR ON RELEASE OF ADP. CC -!- SUBUNIT: CONSISTS OF AT LEAST TWO HEAVY CHAINS AND A NUMBER OF CC INTERMEDIATE AND LIGHT CHAINS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- DOMAIN: DYNEIN HEAVY CHAINS PROBABLY CONSIST OF AN N-TERMINAL STEM CC (WHICH BINDS CARGO AND INTERACTS WITH OTHER DYNEIN COMPONENTS), CC AND THE HEAD OR MOTOR DOMAIN. THE MOTOR CONTAINS SIX TANDEMLY- CC LINKED AAA DOMAINS IN THE HEAD, WHICH FORM A RING. A STALK-LIKE CC STRUCTURE (FORMED BY TWO OF THE COILED COIL DOMAINS) PROTRUDES CC BETWEEN AAA 4 AND AAA 5 AND TERMINATES IN A MICROTUBULE-BINDING CC SITE. A SEVENTH DOMAIN MAY ALSO CONTRIBUTE TO THIS RING; IT IS NOT CC CLEAR WHETHER THE N-TERMINUS OR THE C-TERMINUS FORMS THIS EXTRA CC DOMAIN. THERE ARE FOUR WELL-CONSERVED AND TWO NON-CONSERVED ATPASE CC SITES, ONE PER AAA DOMAIN. PROBABLY ONLY ONE OF THESE (WITHIN AAA CC 1) ACTUALLY HYDROLYZES ATP, THE OTHERS MAY SERVE A REGULATORY CC FUNCTION. CC -!- SIMILARITY: BELONGS TO THE DYNEIN HEAVY CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L23195; AAA60323.1; -. DR EMBL; L25122; AAA28492.1; -. DR PIR; A54794; A54794. DR FlyBase; FBgn0010349; Dhc64C. DR GO; GO:0045169; C:fusome; NAS. DR GO; GO:0005875; C:microtubule associated complex; IDA. DR GO; GO:0008567; F:dynein ATPase activity; IDA. DR GO; GO:0003777; F:microtubule motor activity; IDA. DR GO; GO:0007098; P:centrosome cycle; IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0045478; P:fusome organization and biogenesis; NAS. DR GO; GO:0007018; P:microtubule-based movement; IDA. DR GO; GO:0007294; P:oocyte cell fate determination (sensu Insecta); IMP. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR004273; Dynein_heavy. DR Pfam; PF03028; Dynein_heavy; 1. DR SMART; SM00382; AAA; 4. KW Motor protein; Dynein; Microtubule; ATP-binding; Repeat; Coiled coil. FT DOMAIN 1 1856 STEM (BY SIMILARITY). FT DOMAIN 1857 2084 AAA 1 (BY SIMILARITY). FT DOMAIN 2166 2437 AAA 2 (BY SIMILARITY). FT DOMAIN 2541 2790 AAA 3 (BY SIMILARITY). FT DOMAIN 2884 3153 AAA 4 (BY SIMILARITY). FT DOMAIN 3189 3478 STALK (BY SIMILARITY). FT DOMAIN 3539 3768 AAA 5 (BY SIMILARITY). FT DOMAIN 3989 4205 AAA 6 (BY SIMILARITY). FT DOMAIN 530 565 COILED COIL (POTENTIAL). FT DOMAIN 774 794 COILED COIL (POTENTIAL). FT DOMAIN 1264 1368 COILED COIL (POTENTIAL). FT DOMAIN 3189 3261 COILED COIL (POTENTIAL). FT DOMAIN 3382 3478 COILED COIL (POTENTIAL). FT DOMAIN 3723 3782 COILED COIL (POTENTIAL). FT NP_BIND 1895 1902 ATP (POTENTIAL). FT NP_BIND 2210 2217 ATP (POTENTIAL). FT NP_BIND 2580 2587 ATP (POTENTIAL). FT NP_BIND 2922 2929 ATP (POTENTIAL). SQ SEQUENCE 4639 AA; 530152 MW; 057A7D8800CCD07E CRC64; MGDSLENPDT SVDPIVNLSI ANYDAFANYL RKAVTILLPE DDVVPASLND ALDDPVNQDT IRKFLSDPQV QALYVQRNCI KEDDSEQPAE GEDEKEQVTY QISNDVHFTN SRMASLACIK RGLVVEADKS IHSQLRLINF SDGSPYETLH VFISKSLAPY FKSYVKESGR ADRDGDKMAP SVEKKLAELE MGLLHLQQNI DIPEITLTAH QTVNNVIRKC AEENRKAKVA DFGDKVEDSS FLNLLQNGVN RWIAEIKKVT KLNRDPGSGT ALQEISFWLN LERALYRIQE KRESPEVALT LDILKHGKRF HATVSFDTDT GLKQALATVA DYNPLMKDFP INDLLSATEL EKIRPAVQQI FAHLRKVRNT KYPIQRCLKL IEAISRDLSQ QLLKVLGTRR LMHIPFDEFE RVMNQCFEIF SCWDDEYDKL QGLLRDIVKK KRDEHLKMVW RVSPAHKKLQ TRMEHMRKFR RQHEQLRTVI LRVLRPTKPA VGDDGNVVET KQPYSLDAAD ANAIEEVNLA YENVKEVDCL DITKEGSEAW EAAVKRYEEK IDRVETRITA HLRDQLGTAK NANEMFRIFS RFNALFVRPH IRGAIREYQT QLIQRVKDDI EALHEKFKVQ YPQSKSCRLS SVRDLPPVAG SIIWARQIDN QLTMYLKRVE DVLGKGWETH IEGQKLKADG DSFRAKLSIS DVFHEWARKV QERNFGSTGR IFTIESTRSR IGRGNVLRLR VNFLPEIITL AKEVRNIKNL GFRVPLTIVN KAHQANQIYP YAISLIESVR TYERTLEKIE DRASIVPLVA GLRKDVLNLV SEGIGLIWES YKLDPYVIRL SECVTQFQEK VDDLLVVEEQ LDVDVRSLET CPYSAATFVE ILSKIQHAVD DLSLRQYSNL SVWVTRLDEE VEKKLALRLQ AGIQAWTEAL TGNKKEVDTS MDTDAPAQPT HKLGGDPQIQ NAVHEIRITN QQMYLYPSIE EARFQIMQQF FAWQAIVTSQ VRLQSTRYQV GLEKHVSQTY RNLLTKLPEG KILENAYGAI EQKVSEVRNY VDEWLRYQSL WDLQADMLYG RLGEDVNLWI KCLNDIKQSR TTFDTSDTRR AYGPIIIDYA KVQAKVTLKY DSWHKEALGK FGTLLGTEMT SFHSKVSKSR TDLEMQSIEA ASTSDAVSFI TYVQSLKKDM IAWDKQVEVF REAQRILERQ RFQFPNTWLH VDNIEGEWSA FNEIIKRKDT AIQTQVASLQ AKIVAEDKAV ETRTVDFLND WEKTKPTGGK IRPDDALQQL QIFESKYSRL KEERDNVVKA KEALELQESA VPNNSAERMN VALEELQDLR GVWSELSKVW TQIDETREKP WLSVQPRKLR QQLEAMMAQL KELPARLRMY ESYEYVKKLI QSYIKVNMLI VELKSDALKE RHWKQLTKQL RVNWVLSDLS LGQVWDVNLQ KNEGIVKDII LVAQGEMALE EFLKQVRESW QNYELDLINY QNKCRIIRGW DDLFNKVKEH INSVAAMKLS PYYKVFEEEA LTWEEKLNRI NALFDVWIDV QRRWVYLEGI FSGSADIKTL LPVETSRFQS ISSEFLGLMK KVTKSPKVMD VLNIPAVQRS LERLADLLGK IQKALGEYLE RERTSFPRFY FVGDEDLLEI IGNSKNIARL QKHFKKMFAG VAAILLNEEN NVILGISSRE GEEVHFMNPV STVEHPKINE WLSLVEKQMR FTLASLLAQA VQDIKQFRDG KIDPQAYMEW CDKYQAQIVV LAAQILWSED VESALQQASE NNQSKPMQRV LGNVESTLNV LADSVLQEQP PLRRRKLEHL INEFVHKRTV TRRLLNNGVT SPKSFQWLCE MRFYFDPRQT EVLQQLTIHM ANARFFYGFE YLGVQDRLVQ TPLTDRCYLT MTQALESRLG GSPFGPAGTG KTESVKALGN QLGRFVLVFN CDETFDFQAM GRIFVGLCQV GAWGCFDEFN RLEERMLSAC SQQIQTIQEA LKYEMDSNKE SITVELVGKQ VRVSPDMAIF ITMNPGYAGH SNLPDNLKKL FRSLAMTTPD RQLIAEVMLF SQGFRSAEKL ACKIVPFFKL CDEQLSNQSH YDFGLRALKS VLISAGNVKR DRIMKIKEQM KQRGDENIDE ASVAENLPEQ EILIQSVCET MVPKLVAEDI PLLFSLLSDV FPNVGYTRAE MKGLKEEIRK VCQEDYLVCG EGDEQGAAWM EKVLQLYQIS NLNHGLMMVG PSGSGKSTAW KTLLKALERF EGVEGVAHVI DPKAISKEAL YGVLDPNTRE WTDGLFTHIL RKIIDNVRGE INKRQWIIFD GDVDPEWVEN LNSVLDDNKL LTLPNGERLS LPPNVRVMFE VQDLKFATLA TVSRCGMAWF SEDVLSTEMI FENYLSRLRT IPLEDGDEDF VGVIKPAKDK EEEVSPSLQV QRDIALLLLP FFSADGIVVR TLEYAMDQEH IMDFTRLRAL SSLFSMLNQA ARNVLTFNAQ HPDFPCSADQ LEHYIPKALV YSVLWSFAGD AKLKVRIDLG DFVRSVTTVP LPGAAGAPII DYEVNMSGDW VPWSNKVPVI EVETHKVATP DIVVPTLDTV RHESLLYTWL AEHKPLVLCG PPGSGKTMTL FSALRALPDM EVVGLNFSSA TTPELLLKTF DHYCEYRKTP NGVVLSPVQI GKWLVLFCDE INLPDMDSYG TQRVISFLRQ LVEHKGFYRA SDQAWVSLER IQFVGACNPP TDPGRKPLSH RFLRHVPIIY VDYPGETSLK QIYGTFSRAM LRLMPALRGY AEPLTNAMVE FYLASQDRFT QDMQPHYVYS PREMTRWVRG ICEAIRPLDS LPVEGLVRLW AHEALRLFQD RLVDDSERRW TNENIDLVGQ KHFPGINQEE ALQRPILYSN WLSKDYMPVN REELREYVHA RLKVFYEEEL DVPLVLFDEV LDHVLRIDRI FRQPQGHLLL IGVSGAGKTT LSRFVAWMNG LSIFQIKVHN KYTSEDFDED LRCVLRRSGC KDEKIAFILD ESNVLDSGFL ERMNTLLANG EVPGLFEGDE YTTLMTQCKE GAQREGLMLD SSDELYKWFT QQVMRNLHVV FTMNPSTDGL KDRAATSPAL FNRCVLNWFG DWSDSALFQV GKEFTTRVDL EKPNWHAPDF FPSVCPLVPA NPTHRDAVIN SCVYVHQTLH QANARLAKRG GRTMAVTPRH YLDFIHHFVK LYNEKRSDLE EQQLHLNVGL NKIAETVEQV EEMQKSLAVK KQELQAKNEA ANAKLKQMFQ DQQEAEKKKI QSQEIQIRLA DQTVKIEEKR KYVMADLAQV EPAVIDAQAA VKSIRKQQLV EVRTMANPPS VVKLALESIC LLLGENATDW KSIRAVIMRE NFINSIVSNF GTENITDDVR EKMKSKYLSN PDYNFEKVNR ASMACGPMVK WAIAQIEYAD MLKRVEPLRE ELRSLEEQAD VNLASAKETK DLVEQLERSI AAYKEEYAQL ISQAQAIKTD LENVQAKVDR SIALLKSLNI ERERWESTSE TFKSQMSTII GDVLLSAAFI AYGGYFDQHY RLNLFTTWSQ HLQAASIQYR ADIARTEYLS NPDERLRWQA NALPTDDLCT ENAIMLKRFN RYPLIIDPSG QATTFLLNEY AGKKITKTSF LDDSFRKNLE SALRFGNPLL VQDVENYDPI LNPVLNRELR RTGGRVLITL GDQDIDLSPS FVIFLSTRDP TVEFPPDICS RVTFVNFTVT RSSLQSQCLN QVLKAERPDI DEKRSDLLKL QGEFRLRLRQ LEKSLLQALN DAKGKILDDD SVITTLETLK KEAYDINQKV DETDKVIAEI ETVSQQYLPL SVACSNIYFT MDSLNQVHFL YQYSLKMFLD IFSTVLYNNP KLEGRTDHSE RLGIVTRDLF QVCYERVARG MIHNDRLTFA LLMCKIHLKG TSESNLDAEF NFFLRSREGL LANPTPVEGL SAEQIESVNR LALRLPIFRK LLEKVRSIPE LGAWLQQSSP EQVVPQLWDE SKALSPIASS VHQLLLIQAF RPDRVIAAAH NVVNTVLGED FMPNAEQELD FTSVVDKQLN CNTPALLCSV PGFDASGRVD DLAAEQNKQI SSIAIGSAEG FNQAERAINM ACKTGRWVLL KNVHLAPQWL VQLEKKMHSL QPHSGFRLFL TMEINPKVPV NLLRAGRIFV FEPPPGIRAN LLRTFSTVPA ARMMKTPSER ARLYFLLAWF HAIVQERLRY VPLGWAKKYE FNESDLRVAC DTLDTWIDTT AMGRTNLPPE KVPWDALVTL LSQSIYGGKI DNDFDQRLLT SFLKKLFTAR SFEADFALVA NVDGASGGLR HITMPDGTRR DHFLKWIENL TDRQTPSWLG LPNNAEKVLL TTRGTDLVSK LLKMQQLEDD DELAYSVEDQ SEQSAVGRGE DGRPSWMKAL HNSATAWLEL LPKNLQVLKR TVENIKDPLY RYFEREVTSG SRLLQTVILD LQDVVLICQG EKKQTNHHRS MLSELVRGII PKGWKRYTVP AGCTVIQWIT DFSNRVQQLQ KVSQLVSQAG AKELQGFPVW LGGLLNPEAY ITATRQCVAQ ANSWSLEELA LDVTITDAGL KNDQKDCCFG VTGLKLQGAQ CKNNELLLAS TIMMDLPVTI LKWIKISSEP RISKLTLPVY LNSTRTELLF TVDLAVAAGQ ESHSFYERGV AVLTSTALN // ID DYIN_DROME STANDARD; PRT; 663 AA. AC Q24246; O96508; O96510; O96511; O96512; O96513; O96514; O96515; AC O96516; Q86BQ5; Q9NG49; Q9TZR7; Q9TZR8; Q9TZR9; Q9TZS0; Q9VR78; DT 01-NOV-1997 (Rel. 35, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dynein intermediate chain, cytosolic (DH IC) (Cytoplasmic dynein DE intermediate chain) (Short wing protein). GN SW OR CDIC OR DIC19B OR CG18000. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1A; 1B; 1C; 2A; 2B; 2C; 3A; 3B; 4; 5A AND RP 5B), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Ovary; RX MEDLINE=98449968; PubMed=9774695; RA Nurminsky D.I., Nurminskaya M.V., Benevolenskaya E.V., Shevelyov Y.Y., RA Hartl D.L., Gvozdev V.A.; RT "Cytoplasmic dynein intermediate-chain isoforms with different RT targeting properties created by tissue-specific alternative RT splicing."; RL Mol. Cell. Biol. 18:6816-6825(1998). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 2B), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Ovary; RX MEDLINE=20525500; PubMed=11071907; RA Boylan K., Serr M., Hays T.S.; RT "A molecular genetic analysis of the interaction between the RT cytoplasmic dynein intermediate chain and the glued (Dynactin) RT complex."; RL Mol. Biol. Cell 11:3791-3803(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 101-663 FROM N.A. (ISOFORM 4). RX MEDLINE=95225982; PubMed=7710691; RA Benevolenskaya E.V., Nurminsky D.I., Gvozdev V.A.; RT "Structure of the Drosophila melanogaster annexin X gene."; RL DNA Cell Biol. 14:349-357(1995). CC -!- FUNCTION: THE INTERMEDIATE CHAINS SEEM TO HELP DYNEIN BIND TO CC DYNACTIN 150 KDA COMPONENT. CC -!- SUBUNIT: CONSISTS OF AT LEAST TWO HEAVY CHAINS AND A NUMBER OF CC INTERMEDIATE AND LIGHT CHAINS. CC -!- SUBCELLULAR LOCATION: ISOFORM 2C AGGREGATES IN CYTOPLASM AROUND CC LYSOSOMES AND ISOFORMS 2A AND 2B AROUND THE NUCLEUS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=11; CC Name=5a; Synonyms=J; CC IsoId=Q24246-11; Sequence=Displayed; CC Name=1a; Synonyms=A; CC IsoId=Q24246-2; Sequence=VSP_001345; CC Name=1b; Synonyms=B; CC IsoId=Q24246-3; Sequence=VSP_001346; CC Name=1c; Synonyms=C; CC IsoId=Q24246-4; Sequence=VSP_001347; CC Name=2a; Synonyms=D; CC IsoId=Q24246-5; Sequence=VSP_001348; CC Name=2b; Synonyms=E; CC IsoId=Q24246-6; Sequence=VSP_007686; CC Name=2c; Synonyms=F; CC IsoId=Q24246-7; Sequence=VSP_007686, VSP_007687; CC Name=3a; Synonyms=G; CC IsoId=Q24246-8; Sequence=VSP_001342, VSP_001348; CC Name=3b; Synonyms=H; CC IsoId=Q24246-9; Sequence=VSP_001342; CC Name=4; Synonyms=I; CC IsoId=Q24246-10; Sequence=VSP_001343; CC Name=5b; Synonyms=K; CC IsoId=Q24246-12; Sequence=VSP_007685; CC -!- TISSUE SPECIFICITY: HIGH LEVELS OF ISOFORMS 1B, 1C, 3A AND 4 CC ACCUMULATES IN EARLY EGG CHAMBERS AND AT STAGE 9 BECOME CC CONCENTRATED AT THE POSTERIOR OF THE OOCYTE. ISOFORMS 5A AND 5B CC ARE HIGHLY EXPRESSED IN ADULT HEAD AND TO A LESSER EXTENT IN ADULT CC TORSO. ISOFORMS 1A, 2A AND 2B ARE FOUND IN ALL TISSUES EXAMINED, CC INCLUDING OVARIES, MIDGUT, TORSO AND HEAD. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC ABUNDANT IN EMBRYOS AND ADULTS, LOW LEVELS IN LARVA AND PUPAE. CC ISOFORMS 1A, 2A AND 2B ARE CONSTITUTIVELY EXPRESSED AT HIGH LEVELS CC AND ISOFORM 2C AT LOW LEVELS IN EMBRYOS AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE DYNEIN INTERMEDIATE CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 7 WD REPEATS. CC -!- CAUTION: REF.1 (AAC78306 AND AAC70942) SEQUENCES DIFFER FROM THAT CC SHOWN DUE TO ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF070687; AAC78306.1; ALT_SEQ. DR EMBL; AF070689; AAC70933.1; -. DR EMBL; AF070690; AAC70934.1; -. DR EMBL; AF070691; AAC70935.1; -. DR EMBL; AF070692; AAC70936.1; -. DR EMBL; AF070693; AAC70937.1; -. DR EMBL; AF070694; AAC70938.1; -. DR EMBL; AF070695; AAC70939.1; -. DR EMBL; AF070696; AAC70940.1; -. DR EMBL; AF070697; AAC70941.1; -. DR EMBL; AF070698; AAC70942.1; ALT_SEQ. DR EMBL; AF070699; AAC70943.1; -. DR EMBL; AF263371; AAF73046.1; -. DR EMBL; AE003572; AAF50928.2; -. DR EMBL; AE003572; AAN09553.1; -. DR EMBL; AE003572; AAN09554.1; -. DR EMBL; AE003572; AAN09555.1; -. DR EMBL; AE003572; AAN09556.1; -. DR EMBL; AE003572; AAN09557.1; -. DR EMBL; AE003572; AAN09558.1; -. DR EMBL; AE003572; AAN09559.1; -. DR EMBL; AE003572; AAN09560.1; -. DR EMBL; AE003572; AAN09561.1; -. DR EMBL; AE003572; AAN09562.1; -. DR EMBL; AE002611; -; NOT_ANNOTATED_CDS. DR EMBL; L41945; AAB51185.1; -. DR FlyBase; FBgn0003654; sw. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 4. DR SMART; SM00320; WD40; 6. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Motor protein; Microtubule; Dynein; Repeat; WD repeat; KW Alternative splicing. FT REPEAT 311 360 WD 1. FT REPEAT 364 404 WD 2. FT REPEAT 413 454 WD 3. FT REPEAT 463 503 WD 4. FT REPEAT 508 553 WD 5. FT REPEAT 556 596 WD 6. FT REPEAT 602 641 WD 7. FT VARSPLIC 144 153 Missing (in isoform 5b). FT /FTId=VSP_007685. FT VARSPLIC 144 164 Missing (in isoform 2a, isoform 2b and FT isoform 2c). FT /FTId=VSP_007686. FT VARSPLIC 144 171 Missing (in isoform 3a and isoform 3b). FT /FTId=VSP_001342. FT VARSPLIC 144 187 VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWED FT EFT -> AHATDYYVLAFDAQG (in isoform 1a). FT /FTId=VSP_001345. FT VARSPLIC 144 187 VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWED FT EFT -> AHATDYYG (in isoform 1b). FT /FTId=VSP_001346. FT VARSPLIC 144 187 VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWED FT EFT -> AHATDYY (in isoform 1c). FT /FTId=VSP_001347. FT VARSPLIC 146 187 SCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEF FT T -> AFDAQG (in isoform 4). FT /FTId=VSP_001343. FT VARSPLIC 187 187 T -> TVLAFDAQG (in isoform 2c). FT /FTId=VSP_007687. FT VARSPLIC 187 187 T -> TG (in isoform 2a and isoform 3a). FT /FTId=VSP_001348. FT CONFLICT 47 47 D -> G (IN REF. 1; EXCEPT IN AAC78306). FT CONFLICT 139 145 GGNGDVL -> AETAMV (IN REF. 5). FT CONFLICT 235 235 V -> L (IN REF. 5). FT CONFLICT 296 297 HA -> SM (IN REF. 5). FT CONFLICT 521 522 NQ -> KP (IN REF. 5). FT CONFLICT 537 548 DWTIKLWSLKDT -> KIWSLKLPISSCQFSVVSGINSN FT (IN REF. 5). FT CONFLICT 579 579 G -> A (IN REF. 5). FT CONFLICT 593 593 E -> K (IN REF. 5). FT CONFLICT 628 628 L -> Q (IN REF. 5). FT CONFLICT 645 663 WSRFNTHLSEIKMNQSDEV -> IKMNQSVRSRTI (IN FT REF. 5). SQ SEQUENCE 663 AA; 73917 MW; 4C726D4C5F47FAF7 CRC64; MDRKAELERK KAKLAALREE KDRRRREKEI KDMEEAAGRI GGGAGIDKDQ RKDLDEMLSS LGVAPVSEVL SSLSSVNSMT SDNSNTQTPD ASLQATVNGQ SGGKKQPLNL SVYNVQATNI PPKETLVYTK QTQTTSTGGG NGDVLSCHSS PLSGYMEDWW RPRKAHATDY YDEYNLNPGL EWEDEFTDDE ESSLQNLGNG FTSKLPPGYL THGLPTVKDV APAITPLEIK KETEVKKEVN ELSEEQKQMI ILSENFQRFV VRAGRVIERA LSENVDIYTD YIGGGDSEEA NDERSHARLS LNRVFYDERW SKNRCITSMD WSTHFPELVV GSYHNNEESP NEPDGVVMVW NTKFKKSTPE DVFHCQSAVM STCFAKFNPN LILGGTYSGQ IVLWDNRVQK RTPIQRTPLS AAAHTHPVYC LQMVGTQNAH NVISISSDGK LCSWSLDMLS QPQDTLELQQ RQSKAIAITS MAFPANEINS LVMGSEDGYV YSASRHGLRS GVNEVYERHL GPITGISTHY NQLSPDFGHL FLTSSIDWTI KLWSLKDTKP LYSFEDNSDY VMDVAWSPVH PALFAAVDGS GRLDLWNLNQ DTEVPTASIV VAGAPALNRV SWTPSGLHVC IGDEAGKLYV YDVAENLAQP SRDEWSRFNT HLSEIKMNQS DEV // ID DYL1_DROME STANDARD; PRT; 89 AA. AC Q24117; Q9V3Y6; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dynein light chain 1, cytoplasmic (8 kDa dynein light chain) (Cut up DE protein). GN CTP OR CDLC1 OR DDLC1 OR CG6998. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96189078; PubMed=8628263; RA Dick T., Ray K., Salz H.K., Chia W.; RT "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and RT apoptotic cell death in Drosophila melanogaster."; RL Mol. Cell. Biol. 16:1966-1977(1996). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Head, and Ovary; RA Li M.-G., Serr M., Hays T.S.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN SOME ASPECTS OF DYNEIN-RELATED CC INTRACELLULAR TRANSPORT AND MOTILITY. MAY PLAY A ROLE IN CHANGING CC OR MAINTAINING THE SPATIAL DISTRIBUTION OF CYTOSKELETAL CC STRUCTURES. CC -!- SUBUNIT: CONSISTS OF AT LEAST TWO HEAVY CHAINS AND A NUMBER OF CC INTERMEDIATE AND LIGHT CHAINS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: UBIQUITOUS. CC -!- SIMILARITY: BELONGS TO THE DYNEIN LIGHT CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U32855; AAB04148.1; -. DR EMBL; U48846; AAD00072.1; -. DR EMBL; U48848; AAD00074.1; -. DR EMBL; AE003431; AAF45975.1; -. DR HSSP; Q15701; 1F95. DR FlyBase; FBgn0011760; ctp. DR InterPro; IPR001372; Dynein_light1. DR Pfam; PF01221; Dynein_light; 1. DR ProDom; PD005145; Dynein_light1; 1. DR PROSITE; PS01239; DYNEIN_LIGHT_1; 1. KW Motor protein; Microtubule; Dynein. SQ SEQUENCE 89 AA; 10374 MW; 44871BC030423A8F CRC64; MSDRKAVIKN ADMSEEMQQD AVDCATQALE KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR NFGSYVTHET RHFIYFYLGQ VAILLFKSG // ID DYL2_DROME STANDARD; PRT; 89 AA. AC O96860; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dynein light chain 2, cytoplasmic (8 kDa dynein light chain). GN CDLC2 OR CG5450. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RA Li M.-G., Serr M., Hays T.S.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN SOME ASPECTS OF DYNEIN-RELATED CC INTRACELLULAR TRANSPORT AND MOTILITY. MAY PLAY A ROLE IN CHANGING CC OR MAINTAINING THE SPATIAL DISTRIBUTION OF CYTOSKELETAL CC STRUCTURES. CC -!- SUBUNIT: CONSISTS OF AT LEAST TWO HEAVY CHAINS AND A NUMBER OF CC INTERMEDIATE AND LIGHT CHAINS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE DYNEIN LIGHT CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U48847; AAD00073.1; -. DR EMBL; AE003586; AAF51383.1; -. DR HSSP; Q15701; 1F95. DR FlyBase; FBgn0026141; Cdlc2. DR InterPro; IPR001372; Dynein_light1. DR Pfam; PF01221; Dynein_light; 1. DR ProDom; PD005145; Dynein_light1; 1. DR PROSITE; PS01239; DYNEIN_LIGHT_1; 1. KW Motor protein; Microtubule; Dynein. SQ SEQUENCE 89 AA; 10358 MW; 538C7661E0423A8F CRC64; MSDRKAVIKN ADMSEEMQQD AVDCATQALE KYNIEKDIAA FIKKEFDKKY NPTWHCIVGR NFGSYVTHET RHFIYFYLGQ VAILLFKSG // ID DYLX_DROME STANDARD; PRT; 111 AA. AC Q94524; Q9VE95; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cytoplasmic dynein light chain (TCTEX-1 protein homolog). GN DLC90F OR TCTEX OR CG12363. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=21298452; PubMed=11405626; RA Caggese C., Moschetti R., Ragone G., Barsanti P., Caizzi R.; RT "dtctex-1, the Drosophila melanogaster homolog of a putative murine t- RT complex distorter encoding a dynein light chain, is required for RT production of functional sperm."; RL Mol. Genet. Genomics 265:436-444(2001). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE TCTEX1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y08968; CAA70165.1; -. DR EMBL; AF123058; AAD30033.1; -. DR EMBL; AE003721; AAF55532.1; -. DR FlyBase; FBgn0024432; Dlc90F. DR InterPro; IPR005334; Tctex. DR Pfam; PF03645; Tctex-1; 1. KW Motor protein; Microtubule; Dynein. SQ SEQUENCE 111 AA; 12479 MW; 544CC39F5B318137 CRC64; MDDSREESQF IVDDVSKTIK EAIETTIGGN AYQHDKVNNW TGQVVENCLT VLTKEQKPYK YIVTAMIMQK NGAGLHTASS CYWNNDTDGS CTVRWENKTM YCIVSVFGLA V // ID DYNA_DROME STANDARD; PRT; 1265 AA. AC P13496; Q9VUA1; DT 01-JAN-1990 (Rel. 13, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 150 kDa dynein-associated polypeptide (DP-150) (DAP-150) (Glued DE protein). GN GL OR CG9206. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Canton-S; RX MEDLINE=87317680; PubMed=2819881; RA Swaroop A., Swaroop M., Garen A.; RT "Sequence analysis of the complete cDNA and encoded polypeptide for RT the Glued gene of Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6501-6505(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE CYTOPLASMIC DYNEIN-DRIVEN RETROGRADE CC MOVEMENT OF VESICLES AND ORGANELLES ALONG MICROTUBULES. DYNEIN- CC DYNACTIN INTERACTION IS A KEY COMPONENT OF THE MECHANISM OF AXONAL CC TRANSPORT OF VESICLES AND ORGANELLES. CC -!- SUBUNIT: LARGE MACROMOLECULAR COMPLEX OF AT LEAST 10 COMPONENTS; CC P150(GLUED) BINDS DIRECTLY TO MICROTUBULES AND TO CYTOPLASMIC CC DYNEIN. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE DYNACTIN 150 KDA SUBUNIT FAMILY. CC -!- SIMILARITY: CONTAINS 1 CAP-GLY DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC FRAMESHIFTS AT POSITIONS 32; 174 TO 220; 648 T0 672 AND 1208. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J02932; -; NOT_ANNOTATED_CDS. DR EMBL; AE003536; AAF49788.1; -. DR PIR; A28313; A28313. DR FlyBase; FBgn0001108; Gl. DR GO; GO:0001709; P:cell fate determination; IMP. DR GO; GO:0007467; P:photoreceptor differentiation (sensu Drosop...; IMP. DR GO; GO:0042052; P:rhabdomere development; IMP. DR GO; GO:0016330; P:second mitotic wave (sensu Drosophila); IMP. DR InterPro; IPR000938; CAP-Gly. DR Pfam; PF01302; CAP_GLY; 1. DR PROSITE; PS00845; CAP_GLY_1; 1. DR PROSITE; PS50245; CAP_GLY_2; 1. KW Motor protein; Microtubule; Dynein; Coiled coil; Cytoskeleton. FT DOMAIN 27 69 CAP-GLY. FT DOMAIN 105 138 SER-RICH. FT DOMAIN 213 570 COILED COIL (POTENTIAL). FT DOMAIN 812 836 COILED COIL (POTENTIAL). FT DOMAIN 967 1084 COILED COIL (POTENTIAL). FT DOMAIN 1128 1160 COILED COIL (POTENTIAL). FT CONFLICT 708 708 D -> A (IN REF. 1). FT CONFLICT 875 875 L -> V (IN REF. 1). FT CONFLICT 888 888 A -> R (IN REF. 1). FT CONFLICT 1043 1043 S -> C (IN REF. 1). SQ SEQUENCE 1265 AA; 141217 MW; 2038A200282B2755 CRC64; MSEKNLKVGA RVELTGKDLL GTVAYVGMTS FAVGKWVGVV LDEPKGKNSG SIKGQQYFQC DENCGMFVRP TQLRLLEAAP GSRRSIEDVS GATPTAAQPT KARLSSSRTS LSSSRQSLLG SRTQLTTSLS ERTASSSSIG PRKSLAPQNS KDKESPSTSL AEGAPAASGG NGAASHASSK RASFVETGFL EILKPQFTPS QPLRSPSFTM PSNSGAEDKV ALLEAQKTSA ELQAQLADLT EKLETLKQRR NEDKERLREF DKMKIQFEQL QEFRTKIMGA QASLQKELLR AKQEAKDAIE AKEQHAQEMA DLADNVEMIT LDKEMAEEKA DTLQLELESS KERIEELEVD LELLRSEMQN KAESAIGNIS GGGDSPGLST YEFKQLEQQN IRLKETLVRL RDLSAHDKHD IQKLSKELEM KRSEVTELER TKEKLSAKID ELEAIVADLQ EQVDAALGAE EMVEQLAEKK MELEDKVKLL EEEIAQLEAL EEVHEQLVES NHELELDLRE ELDLANGAKK EVLRERDAAI ETIYDRDQTI VKFRELVQKL NDQLTELRDR NSSNEKESLQ DPSLKMVTET IDYKQMFAES KAYTRAIDVQ LRQIELSQAN EHVQMLTAFM PESFMSRGGD HDSILVILLI SRIVFKCDIV VSQTRERFPP VDAITREAVT QGHAVQQYAF KCRLLHYVHS LQCALHQILY GLNSCQPDTL LRAGSSLPEM VAQEKIVDGI IELLKSNQLD ENSTTDNIEK CVAFFNAMNS VLLAGEQLLN EIQMIRDCVA SLGAACESIL SDTAIAKVII QEAGATSDSV LLIQFLNENM ESVRQQVKLI KRRLPSDQHV IKSGLSQHKV EAMRGLAQNI SRIMSAMHQA TKQSLAAIVS TIESDNAAEH TLPQEKYWAL LTASCERIYE QDDRGPTQNF KTLLAQANSD LQLIAQHLLD KEYDIISAAN NASNQQKSGA HSTPITQRAQ LIKKQLEQKN VLAATLENRE ADVKQLKVAA KMKQNELSEM QIRKDLAEKK LSVLQNEYEH AVDKWKQKYE ETSLQLQLKE KEFEETMDHL QSDIDALESE KSDLRDKLKL NSTTGKVQPG SESHSPHNIS LSGNTSTAPG ISNVSYSAPA GTAPVVAEEV ELLKNAFNQE RNQRLRLQAQ DMRAKLSQFE PLHVPQPQDQ RITALESELT RMKHAWVLSL LQVRSQDSVN SGTRIDAVAL QRRNQPVPLK GEISSKASQL ASDILTEYLQ RKPHRATHGQ FASFPTVDVK RVLQI // ID DYN_DROME STANDARD; PRT; 877 AA. AC P27619; Q9VXM2; DT 01-AUG-1992 (Rel. 23, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Dynamin (EC 3.6.1.50) (dDyn) (Shibire protein). GN SHI OR CG18102. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Canton-S; RX MEDLINE=91260878; PubMed=1828536; RA Chen M.S., Obar R.A., Schroeder C.C., Austin T.W., Poodry C.A., RA Wadsworth S.C., Vallee R.B.; RT "Multiple forms of dynamin are encoded by shibire, a Drosophila gene RT involved in endocytosis."; RL Nature 351:583-586(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), AND MUTAGENESIS OF GLY-141 AND RP GLY-268. RC STRAIN=Oregon-R; RX MEDLINE=91238973; PubMed=1674590; RA van der Bliek A.M., Meyerowitz E.M.; RT "Dynamin-like protein encoded by the Drosophila shibire gene RT associated with vesicular traffic."; RL Nature 351:411-414(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MICROTUBULE-ASSOCIATED FORCE-PRODUCING PROTEIN WHICH IS CC INVOLVED IN THE PRODUCTION OF MICROTUBULE BUNDLES AND WHICH IS CC ABLE TO BIND AND HYDROLYZE GTP. IMPLICATED IN ENDOCYTIC PROTEIN CC SORTING. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MICROTUBULE-ASSOCIATED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=4, D; CC IsoId=P27619-1; Sequence=Displayed; CC Name=2; Synonyms=3, B, C; CC IsoId=P27619-2; Sequence=VSP_001330, VSP_001331; CC -!- MISCELLANEOUS: SHIBIRE MUTATION IS THE CAUSE OF TEMPERATURE- CC SENSITIVE PARALYSIS. THIS IS BELIEVED TO BE DUE TO A REVERSIBLE CC BLOCK OF ENDOCYTOSIS, WHICH PREVENTS MEMBRANE CYCLING AND THUS CC DEPLETES SYNAPTIC VESICLES. CC -!- MISCELLANEOUS: 'SHIBIRE' MEANS 'PARALYZED' IN JAPANESE. CC -!- SIMILARITY: BELONGS TO THE DYNAMIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- CAUTION: REF.1 AND REF.2 (CAA42061) SEQUENCES DIFFER FROM THAT CC SHOWN AT POSITION 634 DUE TO A 6 AMINO ACID INSERTION, THEY ARE A CC CHIMERA OF DNA FROM CHROMOSOME ARMS X AND 3L. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X59449; CAA42068.1; ALT_SEQ. DR EMBL; X59448; CAA42067.1; ALT_SEQ. DR EMBL; X59435; CAA42061.1; ALT_SEQ. DR EMBL; X59436; CAA42062.1; -. DR EMBL; AE003500; AAF48536.2; -. DR EMBL; AE003500; AAN09372.1; -. DR EMBL; BT010049; AAQ22518.1; -. DR PIR; S15413; S15413. DR PIR; S16130; S16130. DR PIR; S17974; S17974. DR PIR; S17975; S17975. DR HSSP; Q05193; 2DYN. DR FlyBase; FBgn0003392; shi. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0003779; F:actin binding; IDA. DR GO; GO:0008549; F:dynamine GTPase activity; NAS. DR GO; GO:0008017; F:microtubule binding; IDA. DR InterPro; IPR001401; Dynamin. DR InterPro; IPR000375; Dynamin_central. DR InterPro; IPR003130; GED. DR InterPro; IPR001849; PH. DR Pfam; PF00350; dynamin; 1. DR Pfam; PF01031; dynamin_2; 1. DR Pfam; PF02212; GED; 1. DR Pfam; PF00169; PH; 1. DR PRINTS; PR00195; DYNAMIN. DR SMART; SM00053; DYNc; 1. DR SMART; SM00302; GED; 1. DR SMART; SM00233; PH; 1. DR PROSITE; PS00410; DYNAMIN; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. KW Hydrolase; Motor protein; GTP-binding; Microtubule; KW Alternative splicing; Endocytosis. FT NP_BIND 33 40 GTP (POTENTIAL). FT NP_BIND 131 135 GTP (POTENTIAL). FT NP_BIND 200 203 GTP (POTENTIAL). FT DOMAIN 513 621 PH. FT DOMAIN 744 827 PRO-RICH. FT VARSPLIC 830 830 V -> R (in isoform 2). FT /FTId=VSP_001330. FT VARSPLIC 831 877 Missing (in isoform 2). FT /FTId=VSP_001331. FT MUTAGEN 141 141 G->S: TEMPERATURE SENSITIVE LARVAL AND FT ADULT PARALYSIS; IN ALLELE SHI-TS2. FT MUTAGEN 268 268 G->D: TEMPERATURE SENSITIVE LARVAL AND FT ADULT PARALYSIS; IN ALLELE SHI-TS1. FT CONFLICT 594 594 K -> R (IN REF. 1). SQ SEQUENCE 877 AA; 97808 MW; 5B85F96491490B14 CRC64; MDSLITIVNK LQDAFTSLGV HMQLDLPQIA VVGGQSAGKS SVLENFVGKD FLPRGSGIVT RRPLILQLIN GVTEYGEFLH IKGKKFSSFD EIRKEIEDET DRVTGSNKGI SNIPINLRVY SPHVLNLTLI DLPGLTKVAI GDQPVDIEQQ IKQMIFQFIR KETCLILAVT PANTDLANSD ALKLAKEVDP QGVRTIGVIT KLDLMDEGTD ARDILENKLL PLRRGYIGVV NRSQKDIEGR KDIHQALAAE RKFFLSHPSY RHMADRLGTP YLQRVLNQQL TNHIRDTLPG LRDKLQKQML TLEKEVEEFK HFQPGDASIK TKAMLQMIQQ LQSDFERTIE GSGSALVNTN ELSGGAKINR IFHERLRFEI VKMACDEKEL RREISFAIRN IHGIRVGLFT PDMAFEAIVK RQIALLKEPV IKCVDLVVQE LSVVVRMCTA KMSRYPRLRE ETERIITTHV RQREHSCKEQ ILLLIDFELA YMNTNHEDFI GFANAQNKSE NANKTGTRQL GNQVIRKGHM VIQNLGIMKG GSRPYWFVLT SESISWYKDE DEKEKKFMLP LDGLKLRDIE QGFMSMSRRV TFALFSPDGR NVYKDYKQLE LSCETVEDVE SWKASFLRAG VYPEKQETQE NGDESASEES SSDPQLERQV ETIRNLVDSY MKIVTKTTRD MVPKAIMMLI INNAKDFING ELLAHLYASG DQAQMMEESA ESATRREEML RMYRACKDAL QIIGDVSMAT VSSPLPPPVK NDWLPSGLDN PRLSPPSPGG VRGKPGPPAQ SSLGGRNPPL PPSTGRPAPA IPNRPGGGAP PLPGGRPGGS LPPPMLPSRV SGAVGGAIVQ QSGANRYVPE SMRGQVNQAV GQAAINELSN AFSSRFK // ID DYR3_DROME STANDARD; PRT; 828 AA. AC P83102; Q8MT39; Q9Y1N4; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative dual-specificity tyrosine-phosphorylation regulated kinase 3 DE homolog (EC 2.7.1.-). GN DYRK3 OR BCDNA:RE60792. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 76-290 FROM N.A. RA Wallrath L.L., Cryderman D.E., Morris E.J., Pavlova M., Biessmann H., RA Levis R.W., Elgin S.C.R.; RT "Telomere swapping alters chromosomal properties."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. CC -!- PTM: AUTOPHOSPHORYLATED ON TYR RESIDUES (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC MNB/DYRK SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY118401; AAM48430.1; -. DR EMBL; AF103941; AAD39356.1; ALT_SEQ. DR FlyBase; FBgn0027101; Dyrk3. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Hypothetical protein; Transferase; Serine/threonine-protein kinase; KW Tyrosine-protein kinase; ATP-binding; Phosphorylation. FT DOMAIN 276 589 PROTEIN KINASE. FT NP_BIND 282 290 ATP (BY SIMILARITY). FT BINDING 305 305 ATP (BY SIMILARITY). FT ACT_SITE 402 402 BY SIMILARITY. SQ SEQUENCE 828 AA; 92739 MW; 9A4AFB31AE52F3E1 CRC64; MVGSQEKKNN HIELSETPAT DKNNLNTTHL ENTQLSKALS PPTSLPQIQI QMINQNLTHT GIAQNNTEKA NRHQYRDSGL QYLTRCFEPL AMLNDSKEDF PTQPSNNIAN YPGDIQILPI FDCCEISESI QAISLPNVTS PSKTKDVPGL FLRTISENSK SKSEPECESL ISVKESSVME NHTFLFHEQI IMSGQQKCEL HEKPKVLVVS PQQVMILYMN KLTPYERTEI LTYPQIYFIG ANAKKRPGVY GPNNSEYDNE QGAYIHVPHD HVAYRYEMLK IIGKGSFGQV IKAYDHKTHE HVALKIVRNE KRFHRQAQEE IRILHHLRRH DKYNTMNIIH MFDYFTFRNH TCITFELLSI NLYELIKKNG FKGFSLQLVR KFAHSLLQCL DALYKNDIIH CDMKPENVLL KQQGRSGIKV IDFGSSCFEN QRIYTYIQSR FYRAPEVILG GKYGRAIDMW SLGCILAELL SGHALFPGEN ESDQLACIIE VLGMPNKNIL ASSKRSKSFF SPKGYPRYCT VRTMSDGMVV LIGGQSRRGK QRGPPCSKSL SKALDGCKDP LFLNFIRGCL EWDADKRLTP SEALKHPWLR RRLPRPPSSS SGCGGVSGLC SSRNESPVTG QNRNFAAETT ASSTSATSIS LTIKRENSHS SLRLHHGAVP ETDFKLIKSV PEGSSTATKE PMMNSDILPE SFRQTTVVSP SKHSADSGGM SCLSAVDVGP SRYYPYMNNN ENNRLFSSSL NSSANSLSHL EQATKLDALG EYSASTTPNL LSKNTGYSFN SGSINIDVAQ ESLVNIASNY ALDKSIDIIG KSNVSLHTNK LKVQSKDM // ID DYR_DROME STANDARD; PRT; 182 AA. AC P17719; Q9VEU4; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dihydrofolate reductase (EC 1.5.1.3). GN DHFR OR CG14887. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 155-176. RC STRAIN=Canton-S; RX MEDLINE=94253079; PubMed=8195153; RA Hao H., Tyshenko M.G., Walker V.K.; RT "Dihydrofolate reductase of Drosophila. Cloning and expression of a RT gene with a rare transcript."; RL J. Biol. Chem. 269:15179-15185(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-23. RC STRAIN=Canton-S; RX MEDLINE=90335257; PubMed=2116172; RA Rancourt S.L., Walker V.K.; RT "The purification of dihydrofolate reductase from Drosophila RT melanogaster."; RL Biochim. Biophys. Acta 1039:261-268(1990). CC -!- CATALYTIC ACTIVITY: 5,6,7,8-TETRAHYDROFOLATE + NADP(+) = 7,8- CC DIHYDROFOLATE + NADPH. CC -!- PATHWAY: ESSENTIAL STEP FOR DE NOVO GLYCINE AND PURINE SYNTHESIS, CC DNA PRECURSOR SYNTHESIS, AND FOR THE CONVERSION OF DUMP TO DTMP. CC -!- SUBUNIT: MONOMER. CC -!- SIMILARITY: BELONGS TO THE DIHYDROFOLATE REDUCTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U06861; AAA19051.1; -. DR EMBL; AE003713; AAF55324.1; -. DR PIR; A53803; A53803. DR PIR; S10759; A33105. DR HSSP; P00374; 1DRF. DR FlyBase; FBgn0004087; Dhfr. DR InterPro; IPR001796; DHFR. DR Pfam; PF00186; DiHfolate_red; 1. DR PRINTS; PR00070; DHFR. DR PROSITE; PS00075; DHFR; 1. KW Oxidoreductase; NADP; One-carbon metabolism. FT CONFLICT 3 3 R -> T (IN REF. 3). FT CONFLICT 11 11 C -> S (IN REF. 3). FT CONFLICT 134 134 K -> Q (IN REF. 1). SQ SEQUENCE 182 AA; 20775 MW; D2C9198F1D2CE430 CRC64; MLRFNLIVAV CENFGIGIRG DLPWRIKSEL KYFSRTTKRT SDPTKQNAVV MGRKTYFGVP ESKRPLPDRL NIVLSTTLQE SDLPKGVLLC PNLETAMKIL EEQNEVENIW IVGGSGVYEE AMASPRCHRL YITKIMQKFD CDTFFPAIPD SFREVAPDSD MPLGVQEENG IKFEYKILEK HS // ID E2F_DROME STANDARD; PRT; 805 AA. AC Q27368; O77035; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor E2f (dE2F). GN E2F OR E2F1 OR CG6376. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye imaginal disk; RX MEDLINE=94294381; PubMed=8022787; RA Dynlacht B.D., Brook A., Dembski M., Yenush L., Dyson N.; RT "DNA-binding and trans-activation properties of Drosophila E2F and DP RT proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6359-6363(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94158833; PubMed=8114698; RA Ohtani K., Nevins J.R.; RT "Functional properties of a Drosophila homolog of the E2F1 gene."; RL Mol. Cell. Biol. 14:1603-1612(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=99077992; PubMed=9858578; RA Sasaki T., Sawado T., Yamaguchi M., Shinomiya T.; RT "Specification of regions of DNA replication initiation during RT embryogenesis in the 65-kilobase DNApolalpha-dE2F locus of Drosophila RT melanogaster."; RL Mol. Cell. Biol. 19:547-555(1999). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP FUNCTION. RX MEDLINE=97415323; PubMed=9271122; RA Royzman I., Whittaker A.J., Orr-Weaver T.L.; RT "Mutations in Drosophila DP and E2F distinguish G1-S progression from RT an associated transcriptional program."; RL Genes Dev. 11:1999-2011(1997). RN [6] RP FUNCTION. RX MEDLINE=98078671; PubMed=9418862; RA Duronio R.J., Bonnette P.C., O'Farrell P.H.; RT "Mutations of the Drosophila dDP, dE2F, and cyclin E genes reveal RT distinct roles for the E2F-DP transcription factor and cyclin E RT during the G1-S transition."; RL Mol. Cell. Biol. 18:141-151(1998). RN [7] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=96087653; PubMed=8537434; RA Hao X.F., Alphey L., Bandara L.R., Lam E.W., Glover D., RA La Thangue N.B.; RT "Functional conservation of the cell cycle-regulating transcription RT factor DRTF1/E2F and its pathway of control in Drosophila RT melanogaster."; RL J. Cell Sci. 108:2945-2954(1995). CC -!- FUNCTION: TRANSCRIPTIONAL ACTIVATOR THAT BINDS TO E2F SITES. CC REQUIRED FOR WILD-TYPE GROWTH IN MITOTIC AND POLYTENE TISSUES, CC CONTRIBUTES TO THE EXPRESSION OF REPLICATION GENES AT THE G1-S CC TRANSITION AND CYCLIN E. CC -!- SUBUNIT: HETERODIMER OF E2F AND DP. COOPERATE TO GIVE SEQUENCE- CC SPECIFIC DNA BINDING AND OPTIMAL TRANS-ACTIVATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: SEGMENTALLY REPEATED EXPRESSION THROUGHOUT CC EARLY EMBRYOS IS RESTRICTED TO THE VENTRAL NERVE CORD IN LATER CC EMBRYOS. CC -!- DEVELOPMENTAL STAGE: THROUGHOUT EMBRYONIC DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE E2F/DP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78421; CAA55186.1; -. DR EMBL; U10184; AAA19003.1; -. DR EMBL; AB011813; BAA32746.1; -. DR EMBL; AE003735; AAF55904.1; -. DR PIR; A56199; A56199. DR HSSP; Q16254; 1CF7. DR TRANSFAC; T01547; -. DR FlyBase; FBgn0011766; E2f. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IDA. DR GO; GO:0008284; P:positive regulation of cell proliferation; NAS. DR GO; GO:0045850; P:positive regulation of nurse cell apoptosis; IMP. DR GO; GO:0000074; P:regulation of cell cycle; NAS. DR InterPro; IPR003316; E2F_TDP. DR Pfam; PF02319; E2F_TDP; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW Developmental protein; Activator. FT DNA_BIND 253 318 POTENTIAL. FT DOMAIN 318 411 DIMERIZATION (POTENTIAL). FT DOMAIN 14 19 POLY-SER. FT DOMAIN 64 68 POLY-ASN. FT DOMAIN 115 125 POLY-ALA. FT DOMAIN 129 143 GLY-RICH. FT DOMAIN 245 249 POLY-SER. FT DOMAIN 519 573 GLY-RICH. FT DOMAIN 525 533 POLY-GLN. FT DOMAIN 594 601 POLY-ALA. FT DOMAIN 701 710 POLY-GLY. FT CONFLICT 127 127 H -> Q (IN REF. 1 AND 2). SQ SEQUENCE 805 AA; 87460 MW; BD49C813DDB2A77D CRC64; MSKFFVNVAP INNSNSSSSH TTTSSNTQRH QQHQQHYGGS GTTGHTMVAR RLNYDLHGGT TSINNNNNIV IKNESVDLDY DHVLSSSDSN SNGGVAAHLR DHVYISLDKG HNTGAVATAA AAATAGHTQQ QLQQQHHHQN QQQRKATGKS NDITNYYKVK RRPHAVSDEI HPKKQAKQSA HHQTVYQKHT ASSAPQQLRH SHHQLRHDAD AELDEDVVER VAKPASHHPF SLSTPQQQLA ASVASSSSSG DRNRADTSLG ILTKKFVDLL QESPDGVVDL NEASNRLHVQ KRRIYDITNV LEGINILEKK SKNNIQWRCG QSMVSQERSR HIEADSLRLE QQENELNKAI DLMRENLAEI SQEVENSGGM AYVTQNDLLN VDLFKDQIVI VIKAPPEAKL VLPNTKLPRE IYVKAENSGE INVFLCHDTS PENSPIAPGA GYVGAPGAGC VRTATSTRLH PLTNQRLNDP LFNNIDAMST KGLFQTPYRS ARNLSKSIEE AAKQSQPEYN NICDIAMGQH HNLNQQQQQQ QQQLLQQPEE DDVDVELNQL VPTLTNPVVR THQFQQHQQP SIQELFSSLT ESSPPTPTKR RREAAAAAIA AGSSTTATTT LNSHNNRNHS NHSNHSNHSS SNNSKSQPPT IGYGSSQRRS DVPMYNCAME GATTTSATAD TTAATSRSAA ASSLQMQFAA VAESNNGSSS GGGGGGGGYG SIAGAGANAD PHQPYSHDRN SLPPGVADCD ANSNSSSVTL QGLDALFNDI GSDYFSNDIA FVSINPPDDN DYPYALNANE GIDRLFDFGS DAYGP // ID E2K3_DROME STANDARD; PRT; 1162 AA. AC Q9NIV1; Q8SX61; Q9VNB8; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic translation initiation factor 2-alpha kinase precursor DE (EC 2.7.1.-) (PRKR-like endoplasmic reticulum kinase) (PERK) (PEK) DE (DmPEK). GN EIF2AK3 OR PEK OR CG2087. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=20143423; PubMed=10677345; RA Sood R., Porter A.C., Ma K., Quilliam L.A., Wek R.C.; RT "Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) RT homologues in humans, Drosophila melanogaster and Caenorhabditis RT elegans that mediate translational control in response to endoplasmic RT reticulum stress."; RL Biochem. J. 346:281-293(2000). RN [2] RP SEQUENCE FROM N.A. RA Pomar-Ballestero N.; RL Thesis (2001), Universidad Autonoma de Madrid, Spain. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PHOSPHORYLATES THE ALPHA SUBUNIT OF EUKARYOTIC CC TRANSLATION-INITIATION FACTOR 2 (EIF2), LEADING TO ITS CC INACTIVATION AND THUS TO A RAPID REDUCTION OF TRANSLATIONAL CC INITIATION AND REPRESSION OF GLOBAL PROTEIN SYNTHESIS (BY CC SIMILARITY). CC -!- ENZYME REGULATION: PERTURBATION IN PROTEIN FOLDING IN THE CC ENDOPLASMIC RETICULUM (ER) PROMOTES REVERSIBLE DISSOCIATION FROM CC HSPA5/BIP AND OLIGOMERIZATION, RESULTING IN CC TRANSAUTOPHOSPHORYLATION AND KINASE ACTIVITY INDUCTION (BY CC SIMILARITY). CC -!- SUBUNIT: FORMS DIMERS WITH HSPA5/BIP IN RESTING CELLS. CC OLIGOMERIZES IN ER-STRESSED CELLS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM (BY SIMILARITY). CC -!- INDUCTION: BY ER STRESS. CC -!- DOMAIN: THE LUMENAL DOMAIN SENSES PERTURBATIONS IN PROTEIN FOLDING CC IN THE ER, PROBABLY THROUGH REVERSIBLE INTERACTION WITH HSPA5/BIP CC (BY SIMILARITY). CC -!- PTM: AUTOPHOSPHORYLATED (BY SIMILARITY). CC -!- PTM: N-GLYCOSYLATED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. GCN2 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF193340; AAF61200.1; -. DR EMBL; AJ313085; CAC85207.1; -. DR EMBL; AE003602; AAF52028.2; -. DR EMBL; AY094831; AAM11184.1; -. DR FlyBase; FBgn0037327; PEK. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00564; PQQ; 2. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Serine/threonine-protein kinase; Transferase; Translation regulation; KW Unfolded protein response; Endoplasmic reticulum; Phosphorylation; KW ATP-binding; Signal; Transmembrane; Glycoprotein. FT SIGNAL 1 39 POTENTIAL. FT CHAIN 40 1162 EUKARYOTIC TRANSLATION INITIATION FACTOR FT 2-ALPHA KINASE. FT DOMAIN 40 537 LUMENAL (POTENTIAL). FT TRANSMEM 538 558 POTENTIAL. FT DOMAIN 559 1162 CYTOPLASMIC (POTENTIAL). FT DOMAIN 642 1130 PROTEIN KINASE. FT NP_BIND 648 656 ATP (BY SIMILARITY). FT BINDING 671 671 ATP (BY SIMILARITY). FT ACT_SITE 980 980 BY SIMILARITY. FT DOMAIN 1155 1158 POLY-SER. FT CARBOHYD 193 193 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 260 260 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 353 353 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 461 461 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 505 505 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 516 516 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 629 629 H -> D (IN REF. 1). SQ SEQUENCE 1162 AA; 131038 MW; F3D6B4C87159D95B CRC64; MQDDLDGIVR HRRRSLSFLQ IVTLTMAGLV AFDPAQVLAG HPTTDSELQT AGSPRPPGLE HCVDQEERRV ARRLLYISTL DGRLSALDIA KSGKLRWSVP TGPGPLISSS IHRLELTNNG QFVRMIPSLS GGIYKFDGDS IDPIPITAEH LLSSSAKFSD DLVISGGKET RSYGVSVRTG QLLYECSLNG CVNSTEEGLA IDDTIREPDE EDQLEDGEQL RDEAGYIVRH DPLLDDVIIV RRQTQTVRAV ESRTGVERWN FSVGQHELDL VRPSECQLQP RDELELAVLD VDIKVVVPEG IICAFSKSEP QTMLWKYKFD HPIVSAWNTN ADDELQPIDL FSSAQWLWDQ DENDTELPNA PQSPPSIYLG MYDKQLYIQE SIRLRQEIMD QTKVYQQLTG DTSLMPRIPW KPISASSKSL VIFRKDQEDP EMIAEGAVAQ GGELVPYDDE NFAVAAQSVL NASEFVNGNG FYFYTTGDLN GPQECSTQNN PTDLPAITAP TSPTNATSEG TEATGNHSVN DDLGFSLDDI DAPVKVVILS LWFWWKEIVV IAFTSAVILN IFMGQRNQRV EREYLVIERH VPVQTAIEAT EASTQALLGP VVPMQRPGNR FSFPPGQANQ RTISESTTHS GEHYTSRFQS DFELMQCLGR GGFGVVFEAK NKLDENRYAI KRITLPNKES SRQRVLREAR TLASCEHHNI VRYFHSWTET PPTGWQEEED RKLLAHELST SIQIETPDDS TMPSLTEQLK EKRQQQLLSW VSDAANSTAC SHDFHLPGES SLKNIREEYD YDEEEDSLIE FRSESQSAAL RAEEEDDTDD DYEEDEEQQG DHEKRHRSSV SIDIHSASFD LKNINYSQHQ LVSNSFQIES VRPKSSGSDD ANDDNKARRK PLTLALAQNH NNNQNGSQPT PSSATILNGT VAKPSKVYLY IQMQLCRKES LRDWLRDNRS ETRAAHIGDI FHQIVDAVDY VHLKGLIHRD LKPSNIFFSQ DGQIKIGDFG LVTDMADIPN LVAKCGDQSG LPSCARHTQQ VGTHLYMSPE QLLGQHYDYK VDIYSLGLIF FELHVYFSTE MERIKTLRSL RDGQYPKDFA VNYPQQYDLL QQMLSAQPEQ RPQTKQLKSQ LRNILQLPHL LSEGQSEQAE LAERARRLSR SRTFSSSSEP HQ // ID E631_DROME STANDARD; PRT; 193 AA. AC P48593; Q9I7T4; Q9VZL0; DT 01-FEB-1996 (Rel. 33, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Calcium-binding protein E63-1. GN EIP63F-1 OR E63-1 OR CG15855. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95401881; PubMed=7671827; RA Andres A.J., Thummel C.S.; RT "The Drosophila 63F early puff contains E63-1, an ecdysone-inducible RT gene that encodes a novel Ca(2+)-binding protein."; RL Development 121:2667-2679(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- INDUCTION: BY ECDYSONE. CC -!- SIMILARITY: CONTAINS 4 EF-HAND CALCIUM-BINDING DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U25882; AAB61120.1; -. DR EMBL; AE003479; AAG22243.1; -. DR HSSP; P02593; 1FW4. DR FlyBase; FBgn0004910; Eip63F-1. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0005509; F:calcium ion binding; IDA. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 4. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND; 3. KW Calcium-binding; Repeat. FT CA_BIND 48 59 EF-HAND 1 (POTENTIAL). FT DOMAIN 98 109 ANCESTRAL CALCIUM SITE 2 (POTENTIAL). FT CA_BIND 140 151 EF-HAND 3 (POTENTIAL). FT CA_BIND 176 187 EF-HAND 4 (POTENTIAL). FT CONFLICT 171 171 L -> M (IN REF. 1). SQ SEQUENCE 193 AA; 21995 MW; 98C117B944727578 CRC64; MSPMSGLRQQ LKMLGTALLG KRATKSVKKK PFTEVEIKDL RTAFDLLDRN RDGRVTANEL QFMLKNLGIN VSDELIHDLI REASHSGNGL INEAEFLQWV GRIQALRDEQ HSHEDSKDSK PVDEADDVTE DLIAAFRVFD RDGNGFITRD ELQTAMEMIG EPLNEQQLEQ LLVIADLDQD GRINYEEFTR LLL // ID E74A_DROME STANDARD; PRT; 829 AA. AC P20105; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ecdysone-induced protein 74EF isoform A (ETS-related protein E74A). GN EIP74EF OR E74. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=90199900; PubMed=2107982; RA Burtis K.C., Thummel C.S., Jones C.W., Karim F.D., Hogness D.S.; RT "The Drosophila 74EF early puff contains E74, a complex ecdysone- RT inducible gene that encodes two ets-related proteins."; RL Cell 61:85-99(1990). RN [2] RP DEVELOPMENTAL STAGE. RX MEDLINE=94038699; PubMed=8223281; RA Huet F., Ruiz C., Richards G.; RT "Puffs and PCR: the in vivo dynamics of early gene expression during RT ecdysone responses in Drosophila."; RL Development 118:613-627(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=E74A; CC IsoId=P20105-1; Sequence=Displayed; CC Name=B; Synonyms=E74B; CC IsoId=P11536-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: IN MID INSTAR LARVAE SALIVARY GLANDS LEVELS CC ARE LOW DURING PUFF STAGE 1 AND INCREASE DURING PUFF STAGE 2 TO CC BECOME THE PREDOMINANT FORM IN STAGE 3. LEVELS REACH MAXIMUM IN CC LATE LARVAE DURING PUFF STAGES 8-10, DECREASING ABRUPTLY AT STAGE CC 11. THIS EXPRESSION PATTERN IS ALSO SEEN IN MALPIGHIAN TUBULES AND CC WING DISK. LEVELS AT PUFF STAGE 11 ARE APPRECIABLE IN THE GUT AND CC FAT BODY. TRANSCRIPTS ARE DETECTED AGAIN IN SALIVARY GLANDS FROM CC PUFF STAGES 12-14 AND 17-21. CC -!- INDUCTION: THE EXPRESSION OF THIS PROTEIN IS DEVELOPMENTALLY CC REGULATED AND IS CORRELATED WITH THE 20-OH-ECDYSONE INDUCED CC ACTIVITY OF PUFF 74EF. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37082; AAA28493.1; -. DR HSSP; P14921; 2STT. DR TRANSFAC; T00208; -. DR FlyBase; FBgn0000567; Eip74EF. DR GO; GO:0006914; P:autophagy; IMP. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR Pfam; PF00178; Ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW Nuclear protein; Transcription regulation; DNA-binding; KW Alternative splicing. FT DNA_BIND 733 815 ETS-DOMAIN. FT DOMAIN 126 129 POLY-ASN. FT DOMAIN 187 190 POLY-SER. FT DOMAIN 191 201 POLY-ALA. FT DOMAIN 208 219 POLY-ASN. FT DOMAIN 227 232 POLY-GLY. FT DOMAIN 318 324 POLY-GLN. FT DOMAIN 352 361 POLY-GLN. FT DOMAIN 380 383 POLY-GLN. FT DOMAIN 432 435 POLY-SER. FT DOMAIN 456 470 POLY-ALA. FT DOMAIN 560 576 POLY-GLN. FT DOMAIN 585 588 POLY-GLN. FT DOMAIN 597 607 POLY-GLN. FT DOMAIN 641 649 POLY-ALA. FT DOMAIN 653 657 POLY-SER. FT DOMAIN 658 663 POLY-ALA. FT DOMAIN 667 679 POLY-ALA. FT VARIANT 813 813 H -> Q. SQ SEQUENCE 829 AA; 87147 MW; 6E3CF7CF0A1D7F5D CRC64; MPFIDDALLW CPDNDGRLVG GLDLGTCIAD DSTANGTENL NPSIQSAGNP NNPQQSVGGE ILGSVESAGN ELNGAAARNV NVVVEPLCGG DSSDELFRSF SESNFEIESL LSDLATVEVK VENEENNNNV ITDDDFASVA AAVVANDDLL AKENAQLSAQ GLVDSVAASL ADSGDAGGQQ ALLAFGSSSS AASAIAAAAA ALCGDLINNN NNNSNSNNNS NGNGNHGGGG GGASSGGGVA GDCATKLEYA LMGGQPLAEE PRFVTSAAAN PLLVEKLMSK CLNIEKRMDK LSDTEIPIVK QSTSPAPQQQ LQQQHHLQQQ QQQQPHNGST FAGATALLHI KTEQNTLLTP LQLQQQQQQQ QGLHGAAGNG GSSNGNNAHQ QQQPLAIPQR PLLHNLLSGG AIHNPHHRNY TTATTGSFPP SPADSGVSDV DSSSSGGQPC ADELKARLGM PPATSASAAA AAAAAAAAAA HLHTGTFLHP NLYQNNAANS LRNIWNRSVG VPDNYYGSSG AGSGGTQPGG PGNPQTPGYL TTSYFNAPTA ATAAASQRGT TINGYHSLHQ QQQQQQQSQQ SQQQQQLAHQ QLSHQQQQAL HQQLSHQQQQ QQQQQQQHPH SQLNGPHPHS HPHSHPHSHP HAGQHTHSTI AAAAAAAAAS VVSSSSSAVA AAAMLSASAA AAATAAAAAG GSQSVIQPAT SSVSYDLSYM LELGGFQQRK AKKPRKPKLE MGVKRRSREG STTYLWEFLL KLLQDREYCP RFIKWTNREK GVFKLVDSKA VSRLWGMHKN KPDMNYETMG RALRYYYQRG ILAKVDGQRL VYHFVDVPKD IIEIDCNGV // ID E74B_DROME STANDARD; PRT; 883 AA. AC P11536; Q9VVI7; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ecdysone-induced protein 74EF isoform B (ETS-related protein E74B). GN EIP74EF OR E74 OR CG6285. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89315191; PubMed=2501755; RA Janknecht R., Taube W., Luedecke H.-J., Pongs O.; RT "Characterization of a putative transcription factor gene expressed RT in the 20-OH-ecdysone inducible puff 74EF in Drosophila RT melanogaster."; RL Nucleic Acids Res. 17:4455-4464(1989). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=90199900; PubMed=2107982; RA Burtis K.C., Thummel C.S., Jones C.W., Karim F.D., Hogness D.S.; RT "The Drosophila 74EF early puff contains E74, a complex ecdysone- RT inducible gene that encodes two ets-related proteins."; RL Cell 61:85-99(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP DEVELOPMENTAL STAGE. RX MEDLINE=94038699; PubMed=8223281; RA Huet F., Ruiz C., Richards G.; RT "Puffs and PCR: the in vivo dynamics of early gene expression during RT ecdysone responses in Drosophila."; RL Development 118:613-627(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; Synonyms=E74B; CC IsoId=P11536-1; Sequence=Displayed; CC Name=A; Synonyms=E74A; CC IsoId=P20105-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: IN MID INSTAR LARVAE SALIVARY GLANDS LEVELS CC INCREASE DURING 86-94 HOURS OF DEVELOPMENT AND REPRESENT THE CC PREDOMINANT ISOFORM DURING PUFF STAGE 1. LEVELS REMAIN RELATIVELY CC CONSTANT IN LATE LARVAE UNTIL THE PREMETAMORPHIC PULSE OF CC ECDYSONE. TRANSCRIPTS ARE DETECTED AGAIN FROM PUFF STAGES 12-14 CC AND 17-21. CC -!- INDUCTION: THE EXPRESSION OF THIS PROTEIN IS DEVELOPMENTALLY CC REGULATED AND IS CORRELATED WITH THE 20-OH-ECDYSONE INDUCED CC ACTIVITY OF PUFF 74EF. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15087; CAA33195.1; -. DR EMBL; M37083; AAA28494.1; -. DR EMBL; AE003523; AAF49324.1; -. DR PIR; S04722; S04722. DR HSSP; P14921; 2STT. DR TRANSFAC; T00210; -. DR FlyBase; FBgn0000567; Eip74EF. DR GO; GO:0006914; P:autophagy; IMP. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR Pfam; PF00178; Ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW Nuclear protein; Transcription regulation; DNA-binding; KW Alternative splicing; Developmental protein; Polymorphism. FT DOMAIN 78 280 ASP/GLU-RICH (ACIDIC). FT DOMAIN 281 759 ALA/GLN/SER-RICH. FT DOMAIN 760 883 ARG/LYS-RICH (BASIC). FT DNA_BIND 787 869 ETS-DOMAIN. FT DOMAIN 27 51 POLY-SER. FT DOMAIN 72 79 POLY-ALA. FT DOMAIN 289 299 POLY-ALA. FT DOMAIN 372 378 POLY-GLN. FT DOMAIN 406 415 POLY-GLN. FT DOMAIN 434 437 POLY-GLN. FT DOMAIN 486 489 POLY-SER. FT DOMAIN 510 524 POLY-ALA. FT DOMAIN 614 630 POLY-GLN. FT DOMAIN 639 642 POLY-GLN. FT DOMAIN 651 661 POLY-GLN. FT DOMAIN 695 703 POLY-ALA. FT DOMAIN 707 711 POLY-SER. FT DOMAIN 712 717 POLY-ALA. FT DOMAIN 721 733 POLY-ALA. FT VARIANT 867 867 H -> Q. SQ SEQUENCE 883 AA; 94820 MW; 148D5031A18D1409 CRC64; MIMVQHLVAA SAHNFASQAA ASLVNVSSSS SSSSSSSSSS LSLSSSSSSS SLSSATPTPV ASPVTPTSPP PAAAAPAEAS PPAGAELQED GQQAKTQEDP TMKDQDMLEK TRQEVKDPVN VEEPGAIVDT ESVMARQSPS PVASTKVPES LEEISNKSPP VQEDEEESES VASDCREFKV LYNHLRQQQH HHSPSSPDKT RSTLDDVSKI LWERKQQLQR SSVITAAPTL QPQQHQQPMS DIEDEETLED VDDADADVEA DAEDEELLEQ YQNGYDSPLD LSLGGATSAA ASAAAAASAV SRRRGRTYSG TESDDSAQCE RARMRLKPER KAERSAAYKK SLMKRYYTEI PIVKQSTSPA PQQQLQQQHH LQQQQQQQPH NGSTFAGATA LLHIKTEQNT LLTPLQLQQQ QQQQQGLHGA AGNGGSSNGN NAHQQQQPLA IPQRPLLHNL LSGGAIHNPH HRNYTTATTG SFPPSPADSG VSDVDSSSSG GQPCADELKA RLGMPPATSA SAAAAAAAAA AAAAHLHTGT FLHPNLYQNN AANSLRNIWN RSVGVPDNYY GSSGAGSGGT QPGGPGNPQT PGYLTTSYFN APTAATAAAS QRGTTINGYH SLHQQQQQQQ QSQQSQQQQQ LAHQQLSHQQ QQALHQQLSH QQQQQQQQQQ QHPHSQLNGP HPHSHPHSHP HSHPHAGQHT HSTIAAAAAA AAASVVSSSS SAVAAAAMLS ASAAAAATAA AAAGGSQSVI QPATSSVSYD LSYMLELGGF QQRKAKKPRK PKLEMGVKRR SREGSTTYLW EFLLKLLQDR EYCPRFIKWT NREKGVFKLV DSKAVSRLWG MHKNKPDMNY ETMGRALRYY YQRGILAKVD GQRLVYHFVD VPKDIIEIDC NGV // ID E75A_DROME STANDARD; PRT; 1237 AA. AC P17671; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ecdysone-induced protein 75B isoform A (E75-A). GN EIP75B OR NR1D3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; RX MEDLINE=90249727; PubMed=2110921; RA Segraves W.A., Hogness D.S.; RT "The E75 ecdysone-inducible gene responsible for the 75B early puff RT in Drosophila encodes two new members of the steroid receptor RT superfamily."; RL Genes Dev. 4:204-219(1990). RN [2] RP DEVELOPMENTAL STAGE. RX MEDLINE=94038699; PubMed=8223281; RA Huet F., Ruiz C., Richards G.; RT "Puffs and PCR: the in vivo dynamics of early gene expression during RT ecdysone responses in Drosophila."; RL Development 118:613-627(1993). CC -!- FUNCTION: IMPLICATED IN THE REGULATION OF ECDYSONE-TRIGGERED GENE CC HIERARCHIES. PROBABLY PLAYS A KEY ROLE IN MEDIATING THE REGULATION CC OF THE LARVAL MOLT BY 20-OH-ECDYSONE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; Synonyms=E75A; CC IsoId=P17671-1; Sequence=Displayed; CC Name=B; Synonyms=E75B; CC IsoId=P17672-1; Sequence=External; CC Name=C; Synonyms=E75C; CC IsoId=P13055-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: IN MID INSTAR LARVAE SALIVARY GLANDS, LOW CC BASAL LEVELS ARE OBSERVED IN PUFF STAGE 1. LEVELS INCREASE IN LATE CC LARVAE FROM PUFF STAGES 3-10, THEN DECREASE ABRUPTLY AT STAGE 11. CC IN PREPUPAE, ISOFORM A IS THE PREDOMINANT FORM DURING THE CC TRANSITION BETWEEN PUFF STAGES 18-19. AT PUFF STAGE 1, EXPRESSION CC IS ALSO PRESENT IN THE GUT. BY STAGE 3 IT IS PRESENT IN THE WING CC DISKS, MALPIGHIAN TUBULES AND THE FAT BODY. AT STAGE 11, CC EXPRESSION IS ONLY PRESENT IN THE GUT AND WING DISKS. CC -!- INDUCTION: THE EXPRESSION OF THIS PROTEIN IS DEVELOPMENTALLY CC REGULATED AND IS CORRELATED WITH THE 20-OH-ECDYSONE INDUCED CC ACTIVITY OF PUFF 75B. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR1 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51548; CAA35923.1; -. DR PIR; A34598; A34598. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T01367; -. DR FlyBase; FBgn0000568; Eip75B. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Metal-binding; Zinc; Zinc-finger; Alternative splicing; KW Developmental protein. FT DNA_BIND 245 311 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 245 265 C4-TYPE. FT ZN_FING 282 306 C4-TYPE. FT DOMAIN 380 590 LIGAND-BINDING (POTENTIAL). FT DOMAIN 721 729 POLY-GLN. FT DOMAIN 1041 1077 SER-RICH. SQ SEQUENCE 1237 AA; 133331 MW; BC59260CFC3E4C70 CRC64; MLMSADSSDS AKTSVICSTV SASMLAPPAP EQPSTTAPPI LGVTGRSHLE NALKLPPNTS VSAYYQHNSK LGMGQNYNPE FRSLVAPVTD LDTVPPTGVT MASSSNSPNS SVKLPHSGVI FVSKSSAVST TDGPTAVLQQ QQPQQQMPQH FESLPHHHPQ QEHQPQQQQQ QHHLQHHPHP HVMYPHGYQQ ANLHHSGGIA VVPADSRPQT PEYIKSYPVM DTTVASSVKG EPELNIEFDG TTVLCRVCGD KASGFHYGVH SCEGCKGFFR RSIQQKIQYR PCTKNQQCSI LRINRNRCQY CRLKKCIAVG MSRDAVRFGR VPKREKARIL AAMQQSTQNR GQQRALATEL DDQPRLLAAV LRAHLETCEF TKEKVSAMRQ RARDCPSYSM PTLLACPLNP APELQSEQEF SQRFAHVIRG VIDFAGMIPG FQLLTQDDKF TLLKAGLFDA LFVRLICMFD SSINSIICLN GQVMRRDAIQ NGANARFLVD STFNFAERMN SMNLTDAEIG LFCAIVLITP DRPGLRNLEL IEKMYSRLKG CLQYIVAQNR PDQPEFLAKL LETMPDLRTL STLHTEKLVV FRTEHKELLR QQMWSMEDGN NSDGQQNKSP SGSWADAMDV EAAKSPLGSV SSTESADLDY GSPSSSQPQG VSLPSPPQQQ PSALASSAPL LAATLSGGCP LRNRANSGSS GDSGAAEMDI VGSHAHLTQN GLTITPIVRH QQQQQQQQQI GILNNAHSRN LNGGHAMCQQ QQQHPQLHHH LTAGAARYRK LDSPTDSGIE SGNEKNECKA VSSGGSSSCS SPRSSVDDAL DCSDAAANHN QVVQHPQLSV VSVSPVRSPQ PSTSSHLKRQ IVEDMPVLKR VLQAPPLYDT NSLMDEAYKP HKKFRALRHR EFETAEADAS SSTSGSNSLS AGSPRQSPVP NSVATPPPSA ASAAAGNPAQ SQLHMHLTRS SPKASMASSH SVLAKSLMAE PRMTPEQMKR SDIIQNYLKR ENSTAASSTT NGVGNRSPSS SSTPPPSAVQ NQQRWGSSSV ITTTCQQRQQ SVSPHSNGSS SSSSSSSSSS SSSSSTSSNC SSSSASSCQY FQSPHSTSNG TSAPASSSSG SNSATPLLEL QVDIADSAQP LNLSKKSPTP PPSKLHALVA AANAVQRYPT LSADVTVTAS NGGSSVGGGE SGRQQQSAGE CGLPQSGPER RRAQGNAGGV RAGGGRWFYA EKWERQRLGV AVQRSRKQDH LERRELN // ID E75B_DROME STANDARD; PRT; 1394 AA. AC P17672; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ecdysone-induced protein 75B isoform B (E75-B). GN EIP75B OR NR1D3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; RX MEDLINE=90249727; PubMed=2110921; RA Segraves W.A., Hogness D.S.; RT "The E75 ecdysone-inducible gene responsible for the 75B early puff RT in Drosophila encodes two new members of the steroid receptor RT superfamily."; RL Genes Dev. 4:204-219(1990). RN [2] RP DEVELOPMENTAL STAGE. RX MEDLINE=94038699; PubMed=8223281; RA Huet F., Ruiz C., Richards G.; RT "Puffs and PCR: the in vivo dynamics of early gene expression during RT ecdysone responses in Drosophila."; RL Development 118:613-627(1993). CC -!- FUNCTION: IMPLICATED IN THE REGULATION OF ECDYSONE-TRIGGERED GENE CC HIERARCHIES. PROBABLY PLAYS A KEY ROLE IN MEDIATING THE REGULATION CC OF THE LARVAL MOLT BY 20-OH-ECDYSONE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=B; Synonyms=E75B; CC IsoId=P17672-1; Sequence=Displayed; CC Name=A; Synonyms=E75A; CC IsoId=P17671-1; Sequence=External; CC Name=C; Synonyms=E75C; CC IsoId=P13055-2; Sequence=External; CC -!- DEVELOPMENTAL STAGE: IN MID INSTAR LARVAE SALIVARY GLANDS, LEVELS CC ARE LOW DURING PUFF STAGE 1, INCREASE DURING PUFF STAGES 2-4 AND CC DIMINISH FROM STAGE 5 ONWARDS. IN PREPUPAE, ISOFORM B IS THE CC PREDOMINANT FORM DURING PUFF STAGE 19 AND THE TRANSITION TO STAGE CC 20. BY STAGE 3 IT IS PRESENT IN THE GUT, MALPIGHIAN TUBULES AND CC THE FAT BODY, LEVELS PERSIST BEYOND STAGE 11. CC -!- INDUCTION: THE EXPRESSION OF THIS PROTEIN IS DEVELOPMENTALLY CC REGULATED AND IS CORRELATED WITH THE 20-OH-ECDYSONE INDUCED CC ACTIVITY OF PUFF 75B. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR1 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51549; CAA35924.1; -. DR PIR; B34598; B34598. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T01368; -. DR FlyBase; FBgn0000568; Eip75B. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Metal-binding; Zinc; Zinc-finger; Alternative splicing; KW Developmental protein. FT DOMAIN 12 21 POLY-GLN. FT DOMAIN 24 31 POLY-GLN. FT DOMAIN 104 107 POLY-GLN. FT DOMAIN 116 123 POLY-GLN. FT DOMAIN 135 139 POLY-GLN. FT DOMAIN 147 150 POLY-THR. FT DOMAIN 166 172 POLY-GLN. FT DOMAIN 181 184 POLY-ALA. FT DOMAIN 300 306 POLY-GLN. FT DOMAIN 311 325 POLY-GLN. FT DOMAIN 878 886 POLY-GLN. FT DOMAIN 906 910 POLY-GLN. FT DOMAIN 1164 1169 POLY-SER. FT DOMAIN 1206 1225 POLY-SER. FT DOMAIN 1228 1234 POLY-SER. FT DOMAIN 1253 1260 POLY-SER. SQ SEQUENCE 1394 AA; 152097 MW; 45CACF77BDE9FB80 CRC64; MVCAMQEVAA VQHQQQQQQL QLPQQQQQQQ QTTQQQHATT IVLLTGNGGG NLHIVATPQQ HQPMHQLHHQ HQHQHQHQQQ AKSQQLKQQH SALVKLLESA PIKQQQQTPK QIVYLQQQQQ QPQRKRLKNE AAIVQQQQQT PATLVKTTTT SNSNSNNTQT TNSISQQQQQ HQIVLQHQQP AAAATPKPCA DLSAKNDSES GIDEDCPNSD EDCPNANPAG TSLEDSSYEQ YQCPWKKIRY ARELLKQREL EQQQTTGGSN AQQQVEAKPA AIPTSNIKQL HCDSPFSAQT HKEIANLLRQ QSQQQQVVAT QQQQQQQQQH QHQQQRRDSS DSNCSLMSNS SNSSAGNCCT CNAGDDQQLE EMDEAHDSGC DDELCEQHHQ RLDSSQLNYL CQKFDEKLDT ALSNSSANTG RNTPAVTANE DADGFFRRSI QQKIQYRPCT KNQQCSILRI NRNRCQYCRL KKCIAVGMSR DAVRFGRVPK REKARILAAM QQSTQNRGQQ RALATELDDQ PRLLAAVLRA HLETCEFTKE KVSAMRQRAR DCPSYSMPTL LACPLNPAPE LQSEQEFSQR FAHVIRGVID FAGMIPGFQL LTQDDKFTLL KAGLFDALFV RLICMFDSSI NSIICLNGQV MRRDAIQNGA NARFLVDSTF NFAERMNSMN LTDAEIGLFC AIVLITPDRP GLRNLELIEK MYSRLKGCLQ YIVAQNRPDQ PEFLAKLLET MPDLRTLSTL HTEKLVVFRT EHKELLRQQM WSMEDGNNSD GQQNKSPSGS WADAMDVEAA KSPLGSVSST ESADLDYGSP SSSQPQGVSL PSPPQQQPSA LASSAPLLAA TLSGGCPLRN RANSGSSGDS GAAEMDIVGS HAHLTQNGLT ITPIVRHQQQ QQQQQQIGIL NNAHSRNLNG GHAMCQQQQQ HPQLHHHLTA GAARYRKLDS PTDSGIESGN EKNECKAVSS GGSSSCSSPR SSVDDALDCS DAAANHNQVV QHPQLSVVSV SPVRSPQPST SSHLKRQIVE DMPVLKRVLQ APPLYDTNSL MDEAYKPHKK FRALRHREFE TAEADASSST SGSNSLSAGS PRQSPVPNSV ATPPPSAASA AAGNPAQSQL HMHLTRSSPK ASMASSHSVL AKSLMAEPRM TPEQMKRSDI IQNYLKRENS TAASSTTNGV GNRSPSSSST PPPSAVQNQQ RWGSSSVITT TCQQRQQSVS PHSNGSSSSS SSSSSSSSSS SSTSSNCSSS SASSCQYFQS PHSTSNGTSA PASSSSGSNS ATPLLELQVD IADSAQPLNL SKKSPTPPPS KLHALVAAAN AVQRYPTLSA DVTVTASNGG SSVGGGESGR QQQSAGECGL PQSGPERRRA QGNAGGVRAG GGRWFYAEKW ERQRLGVAVQ RSRKQDHLER RELN // ID E75C_DROME STANDARD; PRT; 1443 AA. AC P13055; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ecdysone-induced protein 75B isoform C (E75-C). GN EIP75B OR NR1D3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=90016778; PubMed=2508058; RA Feigl G., Gram M., Pongs O.; RT "A member of the steroid hormone receptor gene family is expressed in RT the 20-OH-ecdysone inducible puff 75B in Drosophila melanogaster."; RL Nucleic Acids Res. 17:7167-7178(1989). RN [2] RP DEVELOPMENTAL STAGE. RX MEDLINE=94038699; PubMed=8223281; RA Huet F., Ruiz C., Richards G.; RT "Puffs and PCR: the in vivo dynamics of early gene expression during RT ecdysone responses in Drosophila."; RL Development 118:613-627(1993). CC -!- FUNCTION: IMPLICATED IN THE REGULATION OF ECDYSONE-TRIGGERED GENE CC HIERARCHIES. PROBABLY PLAYS A KEY ROLE IN MEDIATING THE REGULATION CC OF THE LARVAL MOLT BY 20-OH-ECDYSONE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=C; Synonyms=E75C; CC IsoId=P13055-2; Sequence=Displayed; CC Name=A; Synonyms=E75A; CC IsoId=P17671-1; Sequence=External; CC Name=B; Synonyms=E75B; CC IsoId=P17672-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: IN MID INSTAR LARVAE SALIVARY GLANDS, LEVELS CC INCREASE DURING PUFF STAGE 1, THEN REMAIN RELATIVELY CONSTANT CC UNTIL THE PREMETAMORPHIC PULSE OF ECDYSONE AT PUFF STAGE 5. LEVELS CC INCREASE AGAIN IN LATE LARVAE AT PUFF STAGES 9-10. AT PUFF STAGE 1 CC EXPRESSION IS ALSO SEEN IN THE GUT. LEVELS ARE LOW IN THE GUT, CC MALPIGHIAN TUBULES, FAT BODY AND WING DISKS BETWEEN STAGES 1 AND CC 11. CC -!- INDUCTION: THE EXPRESSION OF THIS PROTEIN IS DEVELOPMENTALLY CC REGULATED AND IS CORRELATED WITH THE 20-OH-ECDYSONE INDUCED CC ACTIVITY OF PUFF 75B. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR1 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15586; CAA33611.1; -. DR PIR; S05979; S05979. DR HSSP; P20393; 1A6Y. DR FlyBase; FBgn0000568; Eip75B. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Metal-binding; Zinc; Zinc-finger; Alternative splicing; KW Developmental protein. FT DNA_BIND 454 520 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 454 474 C4-TYPE. FT ZN_FING 491 515 C4-TYPE. FT DOMAIN 589 797 LIGAND-BINDING (POTENTIAL). FT DOMAIN 181 190 POLY-GLN. FT DOMAIN 198 204 POLY-GLN. FT DOMAIN 271 285 POLY-PRO. FT DOMAIN 286 291 POLY-GLN. FT DOMAIN 325 335 POLY-GLN. FT DOMAIN 347 355 POLY-SER. FT DOMAIN 362 365 POLY-SER. FT DOMAIN 374 379 POLY-SER. FT DOMAIN 384 391 POLY-GLN. FT DOMAIN 401 408 POLY-PRO. FT DOMAIN 414 418 POLY-SER. FT DOMAIN 421 424 POLY-SER. FT DOMAIN 429 433 POLY-SER. FT DOMAIN 928 936 POLY-GLN. FT DOMAIN 956 960 POLY-GLN. FT DOMAIN 1214 1219 POLY-SER. FT DOMAIN 1255 1274 POLY-SER. FT DOMAIN 1277 1283 POLY-SER. SQ SEQUENCE 1443 AA; 156265 MW; D4DAE926B697FE37 CRC64; MHGGGPGSSG SNIIRRSSGS FPGSGSGSAS KLIKTEPIDF EMLHLEENER QQDIEREPSS SNSNSNSNSL TPQRYTHVQV QTVPPRQPTG LTTPGGTQKV ILTPRVEYVQ QRATSSTGGG MKHVYSQQQG TAASRSAPPE TTALLTTTSG TPQIIITRTL PSNQHLSRRH SASPSALHHY QQQQQPQRQQ SPPPLHHQQQ QQQQHVRVIR DGRLYDEATV VVAARRHSVS PPPLHHHSRS APVSPVIARR GGAAAYMDQQ YQQRQTPPLA PPPPPPPPPP PPPPPQQQQQ QYISTGVPPP TAAARKFVVS TSTRHVNVIA SNHFQQQQQQ HQAQQHQQQH QQHVIASVSS SSSSSAIGSG GSSSSHIFRT PVVSSSSSSN MHHQQQQQQQ QSSLGNSVMR PPPPPPPPKV KHASSSSSGN SSSSNTNNSS SSSNGEEPSS SIPDLEFDGT TVLCRVCGDK ASGFHYGVHS CEGCKGFFRR SIQQKIQYRP CTKNQQCSIL RINRNRCQYC RLKKCIAVGM SRDAVRFGRV PKREKARIWR PCNRAPRIAA SSDPSPPSWM TSHASSPPCC CAHLETCEFT KEKVSAMRHG RGLPSTPCHT SGLSAEPAPE LQSEQEFSQR FAHVIRGVID FAGMIPGFQL LTQDDKFTLL KAGLFDALFV RLICMFDSSI NSIICLNGQV MRRDAIQNGA NARFLVDSTF NFAERMNSMN LTDAEIGLFC AIVLITPDRP GLRNLELIEK MYSRLKGCLQ YIVAQNRPDQ PEFLAKLLET MPDLRTLSTL HTEKLVVFRT EHKELLRQQM WSMEDGNNSD GQQNKSPSGS WADAMDVEAA KSPLGSVSST ESADLDYGSP SSSQPQGVSL PSPPQQQPSA LASSAPLLAA TLSGGCPLRN RANSGSSGDS GAAEMDIVGS HAHLTQNGLT ITPIVRHQQQ QQQQQQIGIL NNAHSRNLNG GHAMCQQQQQ HPQLHHHLTA GAARYRKLDS PTDSGIESGN EKNECKAVSS GGSSSCSSPR SSVDDALDCS DAAANHNQVV QHPQLSVVSV SPVRSPQPST SSHLKRQIVE DMPVLKRVLQ APPLYDTNSL MDEAYKPHKK FRALRHREFE TAEADASSST SGSNSLSAGS PRQSPVPNSV ATPPPVAASA AAGNPAQSQL HMHLTRSSPK ASMASSHSVL AKSLMAEPRM TPEQMKRSDI IQNYLKRENS TAASSTTNGL GNRSPSSSST PPPSVQNQQR WGSSSVITTT CQQRQQSVSP HSNGSSSSSS SSSSSSSSSS STSSNCSSSS ASSCQYFQSP HSTSIGTGEP DGAPVRDRTA PRPCWNCRWT LLTRRTSQFV QEIAHAAAQQ AARSGGRRQC RSKVSHIVRR RHSDSLQWRS SVGGGESGAQ QQSAGECGLP QSGPERRRAQ GNAGGVRAGG GRWFYAEKWE RQRLGVAVQR SRKQDHLERR ELN // ID E78A_DROME STANDARD; PRT; 866 AA. AC P45447; O18395; O18396; Q8IPT7; Q9NBW8; Q9NBW9; Q9VP64; DT 01-NOV-1995 (Rel. 32, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ecdysone-induced protein 78C (DR-78). GN EIP78C OR NR1E1 OR CG18023. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS A AND B), FUNCTION, AND INDUCTION. RC STRAIN=Canton-S; TISSUE=Larva, and Pupae; RX MEDLINE=94006562; PubMed=8402914; RA Stone B.L., Thummel C.S.; RT "The Drosophila 78C early late puff contains E78, an ecdysone- RT inducible gene that encodes a novel member of the nuclear hormone RT receptor superfamily."; RL Cell 75:307-320(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS A AND B), AND FUNCTION. RC STRAIN=Canton-S; TISSUE=Pupae; RX MEDLINE=97032934; PubMed=8878682; RA Russell S.R.H., Heimbeck G., Goddard C.M., Carpenter A.T.C., RA Ashburner M.; RT "The Drosophila Eip78C gene is not vital but has a role in regulating RT chromosome puffs."; RL Genetics 144:159-170(1996). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RA Nairz K., Hafen E.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE OF 321-433 FROM N.A. (ISOFORM A). RX MEDLINE=94060116; PubMed=8241283; RA Martin-Blanco E., Kornberg T.B.; RT "DR-78, a novel Drosophila melanogaster genomic DNA fragment highly RT homologous to the DNA-binding domain of thyroid hormone-retinoic RT acid-vitamin D receptor subfamily."; RL Biochim. Biophys. Acta 1216:339-341(1993). CC -!- FUNCTION: INDUCES THE EARLY LATE PUFF 78C WHICH TRIGGERS PUPARIUM CC FORMATION AND DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=E78A; CC IsoId=P45447-1; Sequence=Displayed; CC Name=B; Synonyms=E78B; CC IsoId=P45447-2; Sequence=VSP_003654; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: ISOFORM A IS EXPRESSED ONLY IN MID-PUPAL CC STAGES, WHILE ISOFORM B IS MAXIMALLY EXPRESSED IN NEWLY FORMED CC PREPUPAE AND IMMEDIATELY FOLLOWING ISOFORM A IN MID-PUPAE. CC -!- INDUCTION: BOTH ISOFORMS REQUIRE ECDYSONE FOR ACTIVITY. ISOFORM B CC ALSO REQUIRES ECDYSONE-INDUCED PROTEINS FOR MAXIMAL EXPRESSION. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR1 CC SUBFAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS CC IN POSITIONS 567 AND 625. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U01087; AAA19975.1; ALT_FRAME. DR EMBL; U01088; AAA19976.2; ALT_FRAME. DR EMBL; X98881; CAA67384.1; -. DR EMBL; X98882; CAA67385.1; -. DR EMBL; AE003593; AAF51692.2; -. DR EMBL; AE003593; AAN12161.1; -. DR EMBL; AF238308; AAF69494.1; -. DR EMBL; AF238309; AAF69495.1; -. DR EMBL; X73045; CAA51523.1; -. DR PIR; S43435; S43435. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T02743; -. DR FlyBase; FBgn0004865; Eip78C. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Transcription regulation; DNA-binding; Nuclear protein; Metal-binding; KW Zinc; Zinc-finger; Alternative splicing. FT DNA_BIND 367 432 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 367 387 C4-TYPE. FT ZN_FING 403 427 C4-TYPE. FT DOMAIN 64 80 POLY-GLU. FT DOMAIN 182 188 POLY-GLN. FT DOMAIN 192 202 POLY-GLN. FT DOMAIN 240 247 POLY-SER. FT DOMAIN 271 279 POLY-SER. FT DOMAIN 312 315 POLY-GLN. FT DOMAIN 321 333 POLY-GLN. FT DOMAIN 336 339 POLY-GLN. FT DOMAIN 346 349 POLY-SER. FT DOMAIN 354 357 POLY-ASN. FT DOMAIN 481 486 POLY-GLN. FT DOMAIN 490 500 POLY-GLN. FT DOMAIN 546 554 POLY-ASN. FT VARSPLIC 2 475 Missing (in isoform B). FT /FTId=VSP_003654. FT CONFLICT 39 40 ED -> DH (IN REF. 2; CAA67384). FT CONFLICT 79 82 MISSING (IN REF. 4; AAF51692). FT CONFLICT 321 331 QLQQQQQHQQQ -> SCNSSSSTSSR (IN REF. 6). FT CONFLICT 325 326 QQ -> HE (IN REF. 2; CAA67384). FT CONFLICT 430 430 A -> V (IN REF. 6). FT CONFLICT 433 433 S -> K (IN REF. 6). FT CONFLICT 483 489 MISSING (IN REF. 4; AAF69495). FT CONFLICT 502 502 Q -> P (IN REF. 1; AAA19975, 2; CAA67384 FT AND 3; AAF69494). FT CONFLICT 515 515 MISSING (IN REF. 2). FT CONFLICT 734 734 MISSING (IN REF. 1). SQ SEQUENCE 866 AA; 95249 MW; FA79F52576F2F727 CRC64; MDVYQIELEE QAQIRSKLLV ETCVKHSSSE QQQLQVKQED LIKDFTRDEE EQPSEEEAEE EDNEEDEEEE GEEEEEDEEE DEDEEALLPV VNFNANSDFN LHFFDTPEDS STQGAYSEAN SLESEQEEEK QTQQHQQQKQ HHRDLEDCLS AIEADPLQLL HCDDFYRTSA LAESVAASLS PQQQQQRQHT HQQQQQQQQQ QQHPGQQQHQ LNCTLSNGGG ALYTISSVHQ FGPASNHNTS SSSPSSSAAH SSPDSGCSSA SSSGSSRSCG SSSASSSSSA VSSTISSGRS SNNSVVNPAA TSSSVAHLNK EQQQQPLPTT QLQQQQQHQQ QLQHPQQQQS FGLADSSSSN GSSNNNNGVS SKSFVPCKVC GDKASGYHYG VTSCEGCKGF FRRSIQKQIE YRCLRDGKCL VIRLNRNRCQ YCRFKKCLSA GMSRDSVRYG RVPKRSRELN GAAASSAAAG APASLNVDDS TSSTLHPSHL QQQQQQHLLQ QQQQQQHQPQ LQQHHQLQQQ PHVSGVRVKT PSTPQTPQMC SIASSPSELG GCNSANNNNN NNNNSSSGNA SGGSGVSVGV VVVGGHQQLV GGSMVGMAGM GTDAHQVGMC HDGLAGTANE LTVYDVIMCV SQAHRLNCSY TEELTRELMR RPVTVPQNGI ASTVAESLEF QKIWLWQQFS ARVTPGVQRI VEFAKRVPGF CDFTQDDQLI LIKLGFFEVW LTHVARLINE ATLTLDDGAY LTRQQLEILY DSDFVNALLN FANTLNAYGL SDTEIGLFSA MVLLASDRAG LSEPKVIGRA RELVAEALRV QILRSRAGSP QALQLMPALE AKIPELRSLG AKHFSHLDWL RMNWTKLRLP PLFAEIFDIP KADDEL // ID EAST_DROME STANDARD; PRT; 392 AA. AC P13582; Q9VF90; DT 01-JAN-1990 (Rel. 13, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Serine protease easter precursor (EC 3.4.21.-). GN EA OR CG4920. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89119561; PubMed=2492450; RA Chasan R., Anderson K.V.; RT "The role of easter, an apparent serine protease, in organizing the RT dorsal-ventral pattern of the Drosophila embryo."; RL Cell 56:391-400(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP MUTAGENESIS. RX MEDLINE=90182675; PubMed=2107028; RA Jin Y., Anderson K.V.; RT "Dominant and recessive alleles of the Drosophila easter gene are RT point mutations at conserved sites in the serine protease catalytic RT domain."; RL Cell 60:873-881(1990). CC -!- FUNCTION: EXTRACYTOPLASMIC SERINE PROTEASE WHICH PLAYS A ROLE IN CC THE ORGANIZATION OF THE DORSAL-VENTRAL PATTERN OF THE EMBRYO. THE CC PROTEOLYTIC CLEAVAGE CATALYZED BY EASTER MAY BE A CRITICAL, CC REGULATED STEP THAT DEFINES CELL IDENTITIES ALONG THE DORSAL- CC VENTRAL CONTINUUM. CC -!- MISCELLANEOUS: IT IS POSSIBLE THAT EITHER TOLL OR SNAKE ENCODES CC THE SUBSTRATE FOR THE EASTER PROTEASE. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03154; AAA28496.1; -. DR EMBL; AE003708; AAF55170.1; -. DR EMBL; BT009978; AAQ22447.1; -. DR PIR; A30100; A30100. DR HSSP; P00763; 1DPO. DR MEROPS; S01.201; -. DR FlyBase; FBgn0000533; ea. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA. DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP. DR GO; GO:0008063; P:Tl signaling pathway; NAS. DR InterPro; IPR006604; CLIP. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00680; CLIP; 1. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Developmental protein; Serine protease; Hydrolase; Zymogen; Signal. FT SIGNAL 1 19 PROBABLE. FT PROPEP 20 127 ACTIVATION PEPTIDE (POTENTIAL). FT CHAIN 128 392 SERINE PROTEASE EASTER. FT ACT_SITE 173 173 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 240 240 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 338 338 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 158 174 BY SIMILARITY. FT DISULFID 307 324 BY SIMILARITY. FT DISULFID 334 367 BY SIMILARITY. FT MUTAGEN 131 131 G->E: DOMINANT ALLELE EA 20N. FT MUTAGEN 172 172 S->L: RECESSIVE ALLELE EA 111. FT MUTAGEN 283 283 G->S: DOMINANT ALLELE EA 84B. FT MUTAGEN 324 324 C->Y: RECESSIVE ALLELE EA 818. FT MUTAGEN 325 325 A->V: DOMINANT ALLELES EA 83I & EA 4102. FT MUTAGEN 335 335 R->C: DOMINANT ALLELE EA 125.3. FT MUTAGEN 336 336 G->S: DOMINANT ALLELE EA 12A. FT MUTAGEN 338 338 S->A: DESTROYS ACTIVITY. FT MUTAGEN 339 339 G->R: RECESSIVE ALLELE EA 1. FT MUTAGEN 360 360 V->M: DOMINANT ALLELE EA 5.13. FT MUTAGEN 363 363 G->E: RECESSIVE ALLELE EA 8. FT MUTAGEN 371 371 G->R: DOMINANT ALLELE EA 161.13. FT MUTAGEN 373 373 P->S: DOMINANT ALLELE EA 5022. FT CONFLICT 302 302 S -> F (IN REF. 2). SQ SEQUENCE 392 AA; 43065 MW; 1309C41E6FC176B6 CRC64; MLKPSIICLF LGILAKSSAG QFYFPNEAAQ VPNYGRCITP NRERALCIHL EDCKYLYGLL TTTPLRDTDR LYLSRSQCGY TNGKVLICCP DRYRESSSET TPPPKPNVTS NSLLPLPGQC GNILSNRIYG GMKTKIDEFP WMALIEYTKS QGKKGHHCGG SLISTRYVIT ASHCVNGKAL PTDWRLSGVR LGEWDTNTNP DCEVDVRGMK DCAPPHLDVP VERTIPHPDY IPASKNQVND IALLRLAQQV EYTDFVRPIC LPLDVNLRSA TFDGITMDVA GWGKTEQLSA SNLKLKAAVE GSRMDECQNV YSSQDILLED TQMCAGGKEG VDSCRGDSGG PLIGLDTNKV NTYYFLAGVV SFGPTPCGLA GWPGVYTLVG KYVDWIQNTI ES // ID EAS_DROME STANDARD; PRT; 517 AA. AC P54352; Q9VXI7; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ethanolamine kinase (EC 2.7.1.82) (EK) (Easily shocked protein). GN EAS OR CG3525. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=95007778; PubMed=7923374; RA Pavlidis P., Ramaswami M., Tanouye M.A.; RT "The Drosophila easily shocked gene: a mutation in a phospholipid RT synthetic pathway causes seizure, neuronal failure, and paralysis."; RL Cell 79:23-33(1994). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: ATP + ETHANOLAMINE = ADP + O- CC PHOSPHOETHANOLAMINE. CC -!- PATHWAY: PHOSPHATIDYLETHANOLAMINE BIOSYNTHESIS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P54352-1; Sequence=Displayed; CC Name=Short; CC IsoId=P54352-2; Sequence=VSP_001068; CC -!- MISCELLANEOUS: MUTATIONS IN EAS CAUSES SEIZURE, NEURONAL FAILURE, CC AND PARALYSIS. THIS IS DUE TO AN EXCITABILITY DEFECT CAUSED BY CC ALTERED MEMBRANE PHOSPHOLIPID COMPOSITION. CC -!- SIMILARITY: BELONGS TO THE CHOLINE/ETHANOLAMINE KINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L35603; AAC37209.1; -. DR EMBL; L35604; AAC37210.1; -. DR EMBL; AE003501; AAF48574.1; -. DR PIR; A54980; A54980. DR FlyBase; FBgn0000536; eas. DR GO; GO:0004305; F:ethanolamine kinase activity; IDA. DR GO; GO:0007638; P:mechanosensory behavior; IMP. DR GO; GO:0009612; P:response to mechanical stimulus; IMP. DR InterPro; IPR002573; Choline_kinase. DR Pfam; PF01633; Choline_kinase; 1. KW Transferase; Kinase; Alternative splicing. FT ACT_SITE 374 374 BY SIMILARITY. FT VARSPLIC 130 151 Missing (in isoform Short). FT /FTId=VSP_001068. SQ SEQUENCE 517 AA; 59208 MW; BA35636B07DF6786 CRC64; MGTETKSNSY TGQISTSGGN PKVMKDSLSL VRQTVNQQTL SLSQSNQVQN QLNSHSNSNS YPNPSGSENK NENEQNSRDI RAKPEDKSRK EAIVPFVPIF VEEADVIQGA KELLKVIRPT WDLSHVEFKI RVVPQIEDRV SGPKCDGDDD ASFTDGITNK LVGCFHKEIS KLNDENGGSY LPIKTQGLSP VQSEDPVIIE KEDDDEFTDD RAADDGSPVQ YSDNVVLVRI YGNKTDLLID RKAETQNFLL LHTYGLAPSL YATFKNGLVY EYVPGTTLNT DSVLCPEIWP LVARRMAEMH RKVRKHGDSS ATKPMPMIWK KTQSFLDLVP ERFSDAEKHK RVKETFLPIG RLREEFNKLY EYLEALDSPI VFSHNDLLLG NVIYTQSLNT VNFIDYEYAD YNFQAFDIGN HFAEMCGVDE VDYSRYPKRE FQLQWLRVYL EEYLQRSNIQ NDEVELLYVQ VNQFALASHI FWTVWSLLQA EHSTIDFDYV GYAFLRYNEY LARKVEFLSL TAAKNNK // ID ECLH_DROME STANDARD; PRT; 97 AA. AC Q07892; Q9VEJ8; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eclosion hormone precursor (Ecdysis activator) (EH). GN EH OR CG5400. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93345507; PubMed=8344291; RA Horodyski F.M., Ewer J., Riddiford L.M., Truman J.W.; RT "Isolation, characterization and expression of the eclosion hormone RT gene of Drosophila melanogaster."; RL Eur. J. Biochem. 215:221-228(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NEUROPEPTIDE THAT TRIGGERS THE PERFORMANCE OF ECDYSIS CC BEHAVIORS AT THE END OF A MOLT. IT TRIGGERS ADULT BEHAVIOR CC PATTERNS: LARVAL, PUPAL AND ADULT ECDYSIS, AND PLASTICIZATION CC DURING THE MOLT. CC -!- SIMILARITY: HIGH, TO OTHER INSECTS ECLOSION HORMONE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X72302; CAA51050.1; -. DR EMBL; X72303; CAA51051.1; -. DR EMBL; AE003717; AAF55423.1; -. DR PIR; S34769; S34769. DR FlyBase; FBgn0000564; Eh. DR GO; GO:0008031; F:eclosion hormone activity; NAS. DR InterPro; IPR006825; Eclosion. DR Pfam; PF04736; Eclosion; 1. KW Hormone; Neuropeptide; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 97 ECLOSION HORMONE. FT DISULFID 48 72 BY SIMILARITY. FT DISULFID 52 68 BY SIMILARITY. FT DISULFID 55 83 BY SIMILARITY. SQ SEQUENCE 97 AA; 10609 MW; 6AF87A75041C532C CRC64; MNCKPLILCT FVAVAMCLVH FGNALPAISH YTHKRFDSMG GIDFVQVCLN NCVQCKTMLG DYFQGQTCAL SCLKFKGKAI PDCEDIASIA PFLNALE // ID ECR_DROME STANDARD; PRT; 878 AA. AC P34021; Q9V9K8; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ecdysone receptor (Ecdysteroid receptor) (20-hydroxy-ecdysone DE receptor) (20E receptor). GN ECR OR NR1H1 OR CG1765. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92005697; PubMed=1913820; RA Koelle M.R., Talbot W.S., Segraves W.A., Bender M.T., Cherbas P., RA Hogness D.S.; RT "The Drosophila EcR gene encodes an ecdysone receptor, a new member RT of the steroid receptor superfamily."; RL Cell 67:59-77(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP ALTERNATIVE SPLICING. RX MEDLINE=93313962; PubMed=8324824; RA Talbot W.S., Swyryd E.A., Hogness D.S.; RT "Drosophila tissues with different metamorphic responses to ecdysone RT express different ecdysone receptor isoforms."; RL Cell 73:1323-1337(1993). RN [4] RP SUBUNITS. RX MEDLINE=94067348; PubMed=8247157; RA Yao T.-P., Froman B.M., Jiang Z., Cherbas L., Chen J.-D., RA McKeown M.M., Cherbas P., Evans R.M.; RT "Functional ecdysone receptor is the product of EcR and Ultraspiracle RT genes."; RL Nature 366:476-479(1993). RN [5] RP DEVELOPMENTAL STAGE. RX MEDLINE=94038699; PubMed=8223281; RA Huet F., Ruiz C., Richards G.; RT "Puffs and PCR: the in vivo dynamics of early gene expression during RT ecdysone responses in Drosophila."; RL Development 118:613-627(1993). CC -!- FUNCTION: RECEPTOR FOR ECDYSONE. BINDS TO ECDYSONE RESPONSE CC ELEMENTS (ECRES). CC -!- SUBUNIT: HETERODIMER OF USP AND ECR. ONLY THE HETERODIMER IS CC CAPABLE OF HIGH-AFFINITY BINDING TO ECDYSONE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=ECR-B1; CC IsoId=P34021-1; Sequence=Displayed; CC Name=ECR-A; CC IsoId=P34021-2; Sequence=VSP_003661; CC Name=ECR-B2; CC IsoId=P34021-3; Sequence=VSP_003662; CC -!- TISSUE SPECIFICITY: ISOFORM B1 PREDOMINATES OVER ISOFORM A IN CC LARVAL TISSUES, IMAGINAL HISTOBLAST NESTS AND MIDGUT ISLANDS. CC ISOFORM A PREDOMINATES OVER B1 IN IMAGINAL DISKS, AND THE LARVAL CC PROTHORACIC GLAND. CC -!- DEVELOPMENTAL STAGE: IN THE SALIVARY GLANDS OF MID INSTAR LARVAE CC LEVELS INCREASE DURING PUFF STAGE 1 AT 86-94 HOURS OF DEVELOPMENT CC THEN REMAIN RELATIVELY CONSTANT UNTIL THE PREMETAMORPHIC PULSE OF CC ECDYSONE IN LATE LARVAE. LEVELS DIMINISH DRAMATICALLY FROM PUFF CC STAGE 7 ONWARDS. LEVELS INCREASE IN THE PREPUPAL PERIOD DURING CC PUFF STAGE 13-14, THE LEVEL REMAINS STABLE UNTIL STAGE 21. A CC DECREASE IN LEVELS AT PUFF STAGE 7 IS ALSO SEEN IN THE MALPIGHIAN CC TUBULES AND LESS DRAMATICALLY IN THE FAT BODY AND GUT. IN THE WING CC DISK THE RELATIVELY LOW LEVEL REMAINS UNCHANGED. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR1 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74078; AAA28498.1; -. DR EMBL; S63761; AAB27496.2; -. DR EMBL; AE003784; AAF57280.2; -. DR PIR; A41055; A41055. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T00217; -. DR FlyBase; FBgn0000546; EcR. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004884; F:ecdysteroid hormone receptor activity; IDA. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR GO; GO:0016322; P:neuronal remodeling; IMP. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Alternative splicing. FT DOMAIN 1 263 MODULATING. FT DNA_BIND 264 329 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 264 284 C4-TYPE. FT ZN_FING 300 324 C4-TYPE. FT DOMAIN 431 651 HORMONE-BINDING. FT DOMAIN 165 211 GLY-RICH. FT DOMAIN 193 197 POLY-GLY. FT DOMAIN 700 705 POLY-ALA. FT DOMAIN 706 781 GLN/PRO-RICH. FT VARSPLIC 1 226 MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSS FT LDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAM FT HGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGAL FT ANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNL FT GGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGG FT GVGGLGMQHTPRSDSVNSISS -> MLTTSGQQQSKQKLST FT LPSHILLQQQLAASAGPSSSVSLSPSSSAALTLHVASANGG FT ARETTSAAAVKDKLRPTPTAIKIEPMPDVISVGTVAGGSSV FT ATVVAPAATTTSNKPNSTAAPSTSAAAANGHLVLVPNKRPR FT LDVTEDWMSTPSPGSVPSSAPPLSPSPGSQNHSYNMSNGYA FT SPMSAGSYDPYSPTGKT (in isoform ECR-A). FT /FTId=VSP_003661. FT VARSPLIC 1 226 MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSS FT LDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAM FT HGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGAL FT ANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNL FT GGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGG FT GVGGLGMQHTPRSDSVNSISS -> MDTCGLVAELAHYIDA FT Y (in isoform ECR-B2). FT /FTId=VSP_003662. SQ SEQUENCE 878 AA; 93853 MW; B48D610D722F014F CRC64; MKRRWSNNGG FMRLPEESSS EVTSSSNGLV LPSGVNMSPS SLDSHDYCDQ DLWLCGNESG SFGGSNGHGL SQQQQSVITL AMHGCSSTLP AQTTIIPING NANGNGGSTN GQYVPGATNL GALANGMLNG GFNGMQQQIQ NGHGLINSTT PSTPTTPLHL QQNLGGAGGG GIGGMGILHH ANGTPNGLIG VVGGGGGVGL GVGGGGVGGL GMQHTPRSDS VNSISSGRDD LSPSSSLNGY SANESCDAKK SKKGPAPRVQ EELCLVCGDR ASGYHYNALT CEGCKGFFRR SVTKSAVYCC KFGRACEMDM YMRRKCQECR LKKCLAVGMR PECVVPENQC AMKRREKKAQ KEKDKMTTSP SSQHGGNGSL ASGGGQDFVK KEILDLMTCE PPQHATIPLL PDEILAKCQA RNIPSLTYNQ LAVIYKLIWY QDGYEQPSEE DLRRIMSQPD ENESQTDVSF RHITEITILT VQLIVEFAKG LPAFTKIPQE DQITLLKACS SEVMMLRMAR RYDHSSDSIF FANNRSYTRD SYKMAGMADN IEDLLHFCRQ MFSMKVDNVE YALLTAIVIF SDRPGLEKAQ LVEAIQSYYI DTLRIYILNR HCGDSMSLVF YAKLLSILTE LRTLGNQNAE MCFSLKLKNR KLPKFLEEIW DVHAIPPSVQ SHLQITQEEN ERLERAERMR ASVGGAITAG IDCDSASTSA AAAAAQHQPQ PQPQPQPSSL TQNDSQHQTQ PQLQPQLPPQ LQGQLQPQLQ PQLQTQLQPQ IQPQPQLLPV SAPVPASVTA PGSLSAVSTS SEYMGGSAAI GPITPATTSS ITAAVTASST TSAVPMGNGV GVGVGVGGNV SMYANAQTAM ALMGVALHSH QEQLIGGVAV KSEHSTTA // ID EF11_DROME STANDARD; PRT; 463 AA. AC P08736; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Elongation factor 1-alpha (EF-1-alpha) (50 kDa female-specific DE protein). GN EF1-ALPHA-48D OR F1 OR EF1B. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Walldorf U., Hovemann B., Bautz E.K.F.; RT "F1 and F2: two similar genes regulated differently during development RT of Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 82:5795-5799(1985). RN [2] RP IDENTIFICATION OF FUNCTION BY SIMILARITY. RX MEDLINE=88289361; PubMed=3135536; RA Henikoff S., Wallace J.C.; RT "Detection of protein similarities using nucleotide sequence RT databases."; RL Nucleic Acids Res. 16:6191-6204(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88233916; PubMed=3131735; RA Hovemann B., Richter S., Walldorf U., Cziepluch C.; RT "Two genes encode related cytoplasmic elongation factors 1 alpha RT (EF-1 alpha) in Drosophila melanogaster with continuous and stage RT specific expression."; RL Nucleic Acids Res. 16:3175-3194(1988). RN [4] RP SEQUENCE OF 292-311. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- FUNCTION: THIS PROTEIN PROMOTES THE GTP-DEPENDENT BINDING OF CC AMINOACYL-TRNA TO THE A-SITE OF RIBOSOMES DURING PROTEIN CC BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GTP-BINDING ELONGATION FACTOR FAMILY. CC EF-TU/EF-1A SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11744; AAA28526.1; -. DR EMBL; X06869; CAA29993.1; -. DR PIR; S00676; S00676. DR HSSP; P07157; 1AIP. DR FlyBase; FBgn0000556; Ef1-alpha-48D. DR InterPro; IPR004539; EF1_alpha. DR InterPro; IPR000795; EF_GTPbind. DR InterPro; IPR004160; EFTU_Cterm. DR InterPro; IPR004161; EFTU_D2. DR InterPro; IPR009001; Elong_init_C. DR InterPro; IPR009000; Translat_factor. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR TIGRFAMs; TIGR00483; EF-1_alpha; 1. DR PROSITE; PS00301; EFACTOR_GTP; 1. KW Elongation factor; Protein biosynthesis; GTP-binding; KW Multigene family. FT NP_BIND 14 21 GTP (BY SIMILARITY). FT NP_BIND 91 95 GTP (BY SIMILARITY). FT NP_BIND 153 156 GTP (BY SIMILARITY). SQ SEQUENCE 463 AA; 50281 MW; 07ED7C5F4F2FF37C CRC64; MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL DKLKAERERG ITIDIALWKF ETAKYYVTII DAPGHRDFIK NMITGTSQAD CAVQIDAAGT GEFEAGISKN DQTREHALLA FTLGVKQLIV GVNKMDSSEP PYSEARYEEI KKEVSSYIKK VGYNPAAVAF VPISGWHGDN MLEPSTNMPW FKGWEVGRKE GNADGKTLVD ALDAILPPAR PTDKALRLPL QDVYKIGGIG TVPVGRVETG VLKPGTVVVF APANITTEVK SVEMHHEALQ EAVPGDNVGF NVKNVSVKEL RRGYVAGDSK ANPPKGAADF TAQVIVLNHP GQIANGYTPV LDCHTAHIAC KFAEILEKVD RRSGKTTEEN PKFIKSGDAA IVNLVPSKPL CVEAFQEFPP LGRFAVRDMR QTVAVGVIKA VNFKDASGGK VTKAAEKATK GKK // ID EF12_DROME STANDARD; PRT; 462 AA. AC P05303; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Elongation factor 1-alpha (EF-1-alpha). GN F2 OR EF1A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88233916; PubMed=3131735; RA Hovemann B., Richter S., Walldorf U., Cziepluch C.; RT "Two genes encode related cytoplasmic elongation factors 1 alpha RT (EF-1 alpha) in Drosophila melanogaster with continuous and stage RT specific expression."; RL Nucleic Acids Res. 16:3175-3194(1988). RN [2] RP IDENTIFICATION OF FUNCTION BY SIMILARITY. RX MEDLINE=88289361; PubMed=3135536; RA Henikoff S., Wallace J.C.; RT "Detection of protein similarities using nucleotide sequence RT databases."; RL Nucleic Acids Res. 16:6191-6204(1988). CC -!- FUNCTION: THIS PROTEIN PROMOTES THE GTP-DEPENDENT BINDING OF CC AMINOACYL-TRNA TO THE A-SITE OF RIBOSOMES DURING PROTEIN CC BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GTP-BINDING ELONGATION FACTOR FAMILY. CC EF-TU/EF-1A SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06870; CAA29994.1; -. DR PIR; S01193; S01193. DR HSSP; P07157; 1AIP. DR FlyBase; FBgn0000557; Ef1-alpha-100E. DR InterPro; IPR004539; EF1_alpha. DR InterPro; IPR000795; EF_GTPbind. DR InterPro; IPR004160; EFTU_Cterm. DR InterPro; IPR004161; EFTU_D2. DR InterPro; IPR009001; Elong_init_C. DR InterPro; IPR009000; Translat_factor. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR TIGRFAMs; TIGR00483; EF-1_alpha; 1. DR PROSITE; PS00301; EFACTOR_GTP; 1. KW Elongation factor; Protein biosynthesis; GTP-binding; KW Multigene family. FT NP_BIND 14 21 GTP (BY SIMILARITY). FT NP_BIND 91 95 GTP (BY SIMILARITY). FT NP_BIND 153 156 GTP (BY SIMILARITY). SQ SEQUENCE 462 AA; 50609 MW; 9FCB06D243519BE0 CRC64; MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL DKLKAERERG ITIDIALWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIDAAGT GEFEAGISKN GQTREHALLA FTLGVKQLIV GVNKMDSTEP PYSEARYEEI KKEVSSYIKK IGYNPASVAF VPISGWHGDN MLEPSEKMPW FKGWSVERKE GKAEGKCLID ALDAILPPQR PTDKPLRLPL QDVYKIGGIG TVPVGRVETG LLKPGMVVNF APVNLVTEVK SVEMHHEALT EAMPGDNVGF NVKNVSVKEL RRGYVAGDSK NNPPRGAADF TAQVIVLNHP GQIANGYTPV LDCHTAHIAC KFSEIKEKYD RRTGGTTEDG PKAIKSGDAA IIVLVPSKPL CVESFQEFPP LGRFAVRDMR QTVAVGVIKS VNFKETTSGK VTKAAEKAQK KK // ID EF1B_DROME STANDARD; PRT; 221 AA. AC O96827; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable elongation factor 1-beta (EF-1-beta). GN EF1-BETA OR EG:EG0003.7 OR BCDNA:LD24492 OR CG6341. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: EF-1-BETA AND EF-1-DELTA STIMULATE THE EXCHANGE OF CC GDP BOUND TO EF-1-ALPHA TO GTP. CC -!- SUBUNIT: EF-1 IS COMPOSED OF FOUR SUBUNITS: ALPHA, BETA, CC BETA', AND GAMMA. CC -!- PTM: PHOSPHORYLATION AFFECTS THE GDP/GTP EXCHANGE RATE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE EF-1-BETA/EF-1-DELTA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003805; AAF57941.1; -. DR EMBL; AL031863; CAA21314.1; -. DR EMBL; AF172636; AAD46929.2; ALT_INIT. DR PIR; T13689; T13689. DR FlyBase; FBgn0028737; Ef1-beta. DR GO; GO:0005829; C:cytosol; NAS. DR InterPro; IPR001326; EF1_BD. DR Pfam; PF00736; EF1BD; 1. DR PROSITE; PS00824; EF1BD_1; 1. DR PROSITE; PS00825; EF1BD_2; 1. KW Elongation factor; Protein biosynthesis; Phosphorylation. FT INIT_MET 0 0 BY SIMILARITY. FT MOD_RES 104 104 PHOSPHORYLATION (BY CK2) (BY FT SIMILARITY). SQ SEQUENCE 221 AA; 24116 MW; 5E2897655F84472D CRC64; AFGDVTTPQG LKELNAFLAD NSYISGYTPS KADLSVFDAL GKAPSADNVN VARWYRHIAS FEAAERAAWS GTPLPQLAGG KPTVAAAAKP AADDDDDVDL FGSDDEEDEE AERIKQERVA AYAAKKSKKP ALIAKSSVLL DVKPWDDETD MKEMENNVRT IEMDGLLWGA SKLVPVGYGI NKLQIMCVIE DDKVSIDLLQ EKIEEFEDFV QSVDIAAFNK I // ID EF1D_DROME STANDARD; PRT; 256 AA. AC Q9VL18; Q9VL19; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable elongation factor 1-delta (EF-1-delta). GN EEF1-DELTA OR CG4912. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: EF-1-BETA AND EF-1-DELTA STIMULATE THE EXCHANGE OF GDP CC BOUND TO EF-1-ALPHA TO GTP (BY SIMILARITY). CC -!- SUBUNIT: EF-1 IS COMPOSED OF FOUR SUBUNITS: ALPHA, BETA, DELTA, CC AND GAMMA (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=Q9VL18-1; Sequence=Displayed; CC Name=A; CC IsoId=Q9VL18-2; Sequence=VSP_001360; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE EF-1-BETA/EF-1-DELTA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003627; AAF52879.1; -. DR EMBL; AE003627; AAF52880.1; -. DR EMBL; BT003281; AAO25038.1; ALT_INIT. DR FlyBase; FBgn0032198; eEF1-delta. DR InterPro; IPR001326; EF1_BD. DR Pfam; PF00736; EF1BD; 1. DR PROSITE; PS00824; EF1BD_1; 1. DR PROSITE; PS00825; EF1BD_2; 1. KW Elongation factor; Protein biosynthesis; Alternative splicing. FT VARSPLIC 29 55 Missing (in isoform A). FT /FTId=VSP_001360. SQ SEQUENCE 256 AA; 28934 MW; FFA9F2052B27D339 CRC64; MKVEALDKFW ADKSRYDLAE KRFYEGPQKV TDRSHYSPLV SEIAKAREHI QNSLEKIDGV TLDDGLNSEL AKRLAQLEGE HKELKTQVSL LNELLTATVK RLETQLKLTN GVSKEPEVEA KKPEANDDDD DVDLFGSDSE EEDGEAARIR EERLAAYAAK KAKKVQIIAK SNIILDVKPW DDETDLKVME TEIRKITQDG LLWGASKFVP VAFGIQKLSI SCVVEDDKVS IDWLTEEIEK LEDFVQSVDI AAFNKI // ID EF1G_DROME STANDARD; PRT; 431 AA. AC Q9NJH0; Q9NJH1; Q9VAM7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Elongation factor 1-gamma (EF-1-gamma) (eEF-1B gamma). GN EF1G OR CG11901. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Chaney L.C., Hitte C., Kinzy T., Horn M., Rabinow L.; RT "Characterization of the Drosophila translational elongation factor 1 RT gamma (EF1g)."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLY PLAYS A ROLE IN ANCHORING THE COMPLEX TO OTHER CC CELLULAR COMPONENTS. CC -!- SUBUNIT: EF-1 IS COMPOSED OF FOUR SUBUNITS: ALPHA, BETA, DELTA, CC AND GAMMA. CC -!- SIMILARITY: CONTAINS 1 GST-LIKE DOMAIN. CC -!- SIMILARITY: CONTAINS 1 EF-1-GAMMA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF148814; AAF26671.1; -. DR EMBL; AF148813; AAF26670.1; -. DR EMBL; AE003768; AAF56877.1; -. DR FlyBase; FBgn0029176; Ef1-gamma. DR InterPro; IPR001662; EF1_G. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00647; EF1G_domain; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR ProDom; PD006217; EF1_G; 1. DR PROSITE; PS50040; EF1G; 1. KW Elongation factor; Protein biosynthesis. FT DOMAIN 1 194 GST. FT CONFLICT 5 5 MISSING (IN REF. 2). FT CONFLICT 112 112 V -> D (IN REF. 1; AAF26671). SQ SEQUENCE 431 AA; 48967 MW; 9303BACAA3E160D1 CRC64; MVKGTLYTYP ENFRAYKALI AAQYSGAQVK VADNFKFGET NKSAEFLKKF PGGKVPAFET AEGQYLSESN AIAYLLANEQ LRGGKCPFVQ AQVQQWISFA DNEIVPASCA WVFPLLGILP QQKNSTAKQE AEAVLQQLNQ KLQDATFLAG ERITLADIVV FSSLLHLYEY VLEPSVRSAF GNVNRWFVTI LNQKQVQAVV KDYKLCEKAL VFDPKKYAEF QAKTGAAKPQ QQAQQQKQEK KPKEKKEAPK KAAEPAEELD AADEALAAEP KSKDPFDALP KGTFNFDDFK RVYSNEDEAK SIPYFFDKFD AENYSIWFGE YKYNEELSKV FMSCNLITGM FQRLDKMRKA AFASVCLFGE DGNSTISGIW VWRGQDLAFT LSPDWQIDYE VYDWKKLDAK SEETKKLVTQ YFSWSGTDKD GRKFNQGKIF K // ID EF2_DROME STANDARD; PRT; 843 AA. AC P13060; Q9I7H2; Q9V9R0; DT 01-JAN-1990 (Rel. 13, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Elongation factor 2 (EF-2). GN EF2B OR CG2238. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RX MEDLINE=90016792; PubMed=2508059; RA Grinblat Y., Brown N.H., Kafatos F.C.; RT "Isolation and characterization of the Drosophila translational RT elongation factor 2 gene."; RL Nucleic Acids Res. 17:7303-7314(1989). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS PROTEIN PROMOTES THE GTP-DEPENDENT TRANSLOCATION OF CC THE NASCENT PROTEIN CHAIN FROM THE A-SITE TO THE P-SITE OF THE CC RIBOSOME. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P13060-1; Sequence=Displayed; CC Name=Short; CC IsoId=P13060-2; Sequence=VSP_001361, VSP_001362; CC Note=No experimental confirmation available; CC -!- PTM: PHOSPHORYLATION BY EF-2 KINASE COMPLETELY INACTIVATES EF-2. CC -!- SIMILARITY: BELONGS TO THE GTP-BINDING ELONGATION FACTOR FAMILY. CC EF-G/EF-2 SUBFAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15805; CAA33804.1; -. DR EMBL; AE003781; AAF57226.1; ALT_SEQ. DR EMBL; AE003781; AAG22125.1; ALT_SEQ. DR PIR; S05988; S05988. DR FlyBase; FBgn0000559; Ef2b. DR InterPro; IPR000795; EF_GTPbind. DR InterPro; IPR000640; EFG_C. DR InterPro; IPR009022; EFG_III_V. DR InterPro; IPR005517; EFG_IV. DR InterPro; IPR004161; EFTU_D2. DR InterPro; IPR005225; Small_GTP. DR InterPro; IPR009000; Translat_factor. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; EFACTOR_GTP; 1. KW Elongation factor; GTP-binding; Protein biosynthesis; Phosphorylation; KW Alternative splicing. FT INIT_MET 0 0 BY SIMILARITY. FT NP_BIND 25 32 GTP (BY SIMILARITY). FT NP_BIND 107 111 GTP (BY SIMILARITY). FT NP_BIND 161 164 GTP (BY SIMILARITY). FT MOD_RES 56 56 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 58 58 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 700 700 DIPHTHAMIDE (BY SIMILARITY). FT VARSPLIC 700 710 HRGGGQIIPTT -> TSKCSWLSGKA (in isoform FT Short). FT /FTId=VSP_001361. FT VARSPLIC 711 843 Missing (in isoform Short). FT /FTId=VSP_001362. FT CONFLICT 606 606 D -> E (IN REF. 1). SQ SEQUENCE 843 AA; 94327 MW; C4BEE437F23E5593 CRC64; VNFTVDEIRG LMDKKRNIRN MSVIAHVDHG KSTLTDSLVS KAGIIAGAKA GETRFTDTRK DEQERCITIK STAISMYFEV EEKDLVFITH PDQREKECKG FLINLIDSPG HVDFSSEVTA ALRVTDGALV VVDCVSGVCV QTETVLRQAI AERIKPILFM NKMDRALLEL QLDAEELYQT FQRIVENVNV IIATYNDDGG PMGEVRVDPS KGSVGFGSGL HGWAFTLKQF SEMYSEKFKI DVVKLMNRLW GENFFNAKTK KWQKQKEADN KRSFCMYILD PIYKVFDAIM NYKKEEIGTL LEKIGVTLKH EDKDKDGKAL LKTVMRTWLP AGEALLQMIA IHLPSPVVAQ KYRMEMLYEG PHDDEAAIAV KSCDPDGPLM MYISKMVPTS DKGRFYAFGR VFAGKVATGQ KCRIMGPNYT PGKKEDLYEK AIQRTILMMG RYVEAIEDVP SGNICGLVGV DQFLVKTGTI TTFKDAHNMK VMKFSVSPVV RVAVEPKNPA DLPKLVEGLK RLAKSDPMVQ CIIEESGEHI IAGAGELHLE ICLKDLEEDH ACIPLKKSDP VVSYRETVSE ESDQMCLSKS PNKHNRLLMK ALPMPDGLPE DIDNGDVSAK DEFKARARYL SEKYDYDVTE ARKIWCFGPD GTGPNFILDC TKSVQYLNEI KDSVVAGFQW ASKEGILADE NLRGVRFNIY DVTLHADAIH RGGGQIIPTT RRCLYAAAIT AKPRLMEPVY LCEIQCPEVA VGGIYGVLNR RRGHVFEENQ VVGTPMFVVK AYLPVNESFG FTADLRSNTG GQAFPQCVFD HWQVLPGDPS EPSSKPYAIV QDTRKRKGLK EGLPDLSQYL DKL // ID EFL2_DROME STANDARD; PRT; 187 AA. AC P82147; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lethal(2)essential for life protein (Protein Efl21). GN L(2)EFL OR CG4533. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Oregon-R; RA Czaja J., Kurzik-Dumke U.; RT "Tissue specificity and subcellular localisation of the Efl21 protein RT encoded by the heat shock related gene l(2)efl."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. (ISOFORM LONG), AND CHARACTERIZATION. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=95196997; PubMed=7890160; RA Kurzik-Dumke U., Lohmann E.; RT "Sequence of the new Drosophila melanogaster small heat-shock-related RT gene, lethal(2) essential for life [l(2)efl], at locus 59F4,5."; RL Gene 154:171-175(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: VITAL ROLE IN EMBRYONIC DEVELOPMENT. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P82147-1; Sequence=Displayed; CC Name=Short; CC IsoId=P82147-2; Sequence=VSP_002420, VSP_002421; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED DURING EMBRYOGENESIS CC WITH NO SIGN OF TISSUE SPECIFICITY IN EXPRESSION UP TO STAGE 16. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. HIGHEST CC EXPRESSION DURING LARVAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ250883; CAB60198.1; -. DR EMBL; X77635; CAB55438.1; -. DR EMBL; AE003461; AAF47041.1; -. DR EMBL; AY047516; AAK77248.1; -. DR EMBL; BT001462; AAN71217.1; ALT_SEQ. DR PIR; S42032; S42032. DR FlyBase; FBgn0011296; l(2)efl. DR InterPro; IPR001436; Crystallin_alpha. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Developmental protein; Alternative splicing. FT VARSPLIC 131 145 DVNPDTVTSSLSSDG -> ESEFHQQNRKYAKRV (in FT isoform Short). FT /FTId=VSP_002420. FT VARSPLIC 146 187 Missing (in isoform Short). FT /FTId=VSP_002421. SQ SEQUENCE 187 AA; 21309 MW; FF1742AD4E29EEDB CRC64; MSVVPLMFRD WWDELDFPMR TSRLLDQHFG QGLKRDDLMS SVWNSRPTVL RSGYLRPWHT NSLQKQESGS TLNIDSEKFE VILDVQQFSP SEITVKVADK FVIVEGKHEE KQDEHGYVSR QFSRRYQLPS DVNPDTVTSS LSSDGLLTIK APMKALPPPQ TERLVQITQT GPSSKEDNAK KVETSTA // ID EGFR_DROME STANDARD; PRT; 1426 AA. AC P04412; O18370; O61601; P81868; Q9W2G0; DT 13-AUG-1987 (Rel. 05, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Epidermal growth factor receptor precursor (EC 2.7.1.112) (Egfr) DE (Gurken receptor) (Torpedo protein) (Drosophila relative of ERBB). GN EGFR OR TOP OR C-ERBB OR DER OR CG10079. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS TYPES I AND II). RX MEDLINE=94350209; PubMed=8070664; RA Clifford R., Schupbach T.; RT "Molecular analysis of the Drosophila EGF receptor homolog reveals RT that several genetically defined classes of alleles cluster in RT subdomains of the receptor protein."; RL Genetics 137:531-550(1994). RN [2] RP REVISIONS. RA Clifford R., Schupbach T.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=85124611; PubMed=2982499; RA Livneh E., Glazer L., Segal D., Schlessinger J., Shilo B.-Z.; RT "The Drosophila EGF receptor gene homolog: conservation of both RT hormone binding and kinase domains."; RL Cell 40:599-607(1985). RN [4] RP SEQUENCE FROM N.A., CHARACTERIZATION, AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=87002474; PubMed=3093080; RA Schejter E.D., Segal D., Glazer L., Shilo B.-Z.; RT "Alternative 5' exons and tissue-specific expression of the RT Drosophila EGF receptor homolog transcripts."; RL Cell 46:1091-1101(1986). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS TYPE I AND TYPE II), TISSUE SPECIFICITY, RP AND MUTATION ANALYSIS. RX MEDLINE=99102120; PubMed=9882502; RA Lesokhin A.M., Yu S.-Y., Katz J., Baker N.E.; RT "Several levels of EGF receptor signaling during photoreceptor RT specification in wild-type, Ellipse, and null mutant Drosophila."; RL Dev. Biol. 205:129-144(1999). RN [6] RP SEQUENCE FROM N.A. (ISOFORM TYPE I). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [7] RP SEQUENCE OF 959-1078 FROM N.A. RC STRAIN=Daekwanryeong; RX MEDLINE=85137938; PubMed=2983232; RA Wadsworth S.C., Vincent W.S. III, Bilodeau-Wentworth D.; RT "A Drosophila genomic sequence with homology to human epidermal RT growth factor receptor."; RL Nature 314:178-180(1985). RN [8] RP SEQUENCE OF 1069-1121 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). RN [9] RP SEQUENCE OF 1133-1137; 1155-1167 AND 1209-1216 FROM N.A., AND MUTATION RP ANALYSIS. RX MEDLINE=92038942; PubMed=1936959; RA Raz E., Schejter E.D., Shilo B.Z.; RT "Interallelic complementation among DER/flb alleles: implications for RT the mechanism of signal transduction by receptor-tyrosine kinases."; RL Genetics 129:191-201(1991). RN [10] RP REVIEW. RX MEDLINE=97248481; PubMed=9094709; RA Perrimon N., Perkins L.A.; RT "There must be 50 ways to rule the signal: the case of the Drosophila RT EGF receptor."; RL Cell 89:13-16(1997). CC -!- FUNCTION: BINDS TO FOUR LIGANDS: SPITZ, GURKEN, VEIN AND ARGOS, CC WHICH IS AN ANTAGONIST. TRANSDUCES THE SIGNAL THROUGH THE RAS-RAF- CC MAPK PATHWAY. INVOLVED IN A MYRIAD OF DEVELOPMENTAL DECISIONS. CC CRITICAL FOR THE PROLIFERATION OF IMAGINAL TISSUES, AND FOR THE CC DETERMINATION OF BOTH THE ANTERO-POSTERIOR AND DORSO-VENTRAL CC POLARITIES OF THE OOCYTE. IN THE EMBRYO, PLAYS A ROLE IN THE CC ESTABLISHMENT OF VENTRAL CELL FATES, MAINTENANCE OF AMNIOSEROSA CC AND VENTRAL NEUROECTODERMAL CELLS, GERM BAND RETRACTION, CELL FATE CC SPECIFICATION IN THE CENTRAL NERVOUS SYSTEM AND PRODUCTION OF CC CUTICLE. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Type I; CC IsoId=P04412-1; Sequence=Displayed; CC Name=Type II; CC IsoId=P04412-2; Sequence=VSP_002897; CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED IN EMBRYOS. IN LARVAE, CC UNIFORM EXPRESSION IS SEEN IN WING DISKS, GENITAL DISK, ANLAGEN OF CC TESTIS AND OVARY, AND BRAIN CORTEX. IN EYE-ANTENNA DISK, HIGHEST CC EXPRESSION IS ANTERIOR TO MORPHOGENETIC FURROW, LEVELS REMAIN HIGH CC IN PHOTORECEPTOR PRECURSOR CELLS. THIS PATTERN IS REVERSED IN CC POSTERIOR EYE DISK. IN ADULTS EXPRESSION IS HIGH IN BRAIN CORTEX CC AND THORACIC AND ABDOMINAL GANGLIA. CC -!- SIMILARITY: BELONGS TO THE EGF RECEPTOR FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF052754; AAC08536.1; -. DR EMBL; AF052753; AAC08536.1; JOINED. DR EMBL; AF052754; AAC08535.1; -. DR EMBL; AF052752; AAC08535.1; JOINED. DR EMBL; K03054; AAA51462.1; -. DR EMBL; K03417; AAA51460.1; -. DR EMBL; K03416; AAA50965.1; -. DR EMBL; AF109077; AAD26134.1; -. DR EMBL; AF109078; AAD26132.1; -. DR EMBL; AF109082; AAD26132.1; JOINED. DR EMBL; AF109078; AAD26133.1; -. DR EMBL; AF109084; AAD26133.1; JOINED. DR EMBL; AF109079; AAD26130.1; -. DR EMBL; AF109081; AAD26130.1; JOINED. DR EMBL; AF109079; AAD26131.1; -. DR EMBL; AF109083; AAD26131.1; JOINED. DR EMBL; AF109080; AAD26135.1; -. DR EMBL; AE003454; AAF46732.1; -. DR EMBL; X02293; CAA26157.1; -. DR EMBL; AJ002912; CAA05747.1; -. DR EMBL; X78920; CAA55523.1; -. DR EMBL; X78918; CAA55521.1; -. DR EMBL; X78919; CAA55522.1; -. DR PIR; A00640; GQFFE. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0003731; Egfr. DR GO; GO:0007469; P:antennal morphogenesis; NAS. DR GO; GO:0006916; P:anti-apoptosis; NAS. DR GO; GO:0030381; P:eggshell pattern formation (sensu Insecta); IGI. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR GO; GO:0007390; P:germ-band shortening; IMP. DR GO; GO:0007444; P:imaginal disc development; IMP. DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IMP. DR GO; GO:0008071; P:maternal determination of dorsal/ventral ax...; IMP. DR GO; GO:0007477; P:notum morphogenesis; IMP. DR GO; GO:0007314; P:oocyte anterior/posterior axis determination; NAS. DR GO; GO:0045468; P:regulation of R8 spacing; NAS. DR GO; GO:0016330; P:second mitotic wave (sensu Drosophila); IMP. DR GO; GO:0007476; P:wing morphogenesis; IMP. DR InterPro; IPR000494; EGFR_L_domain. DR InterPro; IPR006211; Furin-like. DR InterPro; IPR006212; Furin_repeat. DR InterPro; IPR009030; Grow_fac_recep. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00757; Furin-like; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF01030; Recep_L_domain; 2. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00261; FU; 7. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. KW Transmembrane; Glycoprotein; Receptor; Phosphorylation; Transferase; KW Tyrosine-protein kinase; ATP-binding; Signal; Alternative splicing; KW Developmental protein. FT SIGNAL 1 30 POTENTIAL. FT CHAIN 31 1426 EPIDERMAL GROWTH FACTOR RECEPTOR. FT DOMAIN 31 868 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 869 889 POTENTIAL. FT DOMAIN 890 1426 CYTOPLASMIC (POTENTIAL). FT DOMAIN 938 1198 PROTEIN KINASE. FT NP_BIND 944 952 ATP (BY SIMILARITY). FT BINDING 971 971 ATP (BY SIMILARITY). FT ACT_SITE 1063 1063 BY SIMILARITY. FT MOD_RES 902 902 PHOSPHORYLATION (BY PKC) (BY SIMILARITY). FT MOD_RES 1309 1309 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT CARBOHYD 128 128 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 241 241 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 419 419 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 443 443 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 482 482 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 569 569 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 599 599 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 617 617 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 816 816 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 823 823 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 828 828 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 101 MLLRRRNGPCPFPLLLLLLAHCICIWPASAARDRYARQNNR FT QRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGV FT TIPTSLEDKNKNEFVKGKI -> MMIISMWMSISRGLWDSS FT SILSVLLILACMASITTSSSVSNAGYVDNGNMKV (in FT isoform Type II). FT /FTId=VSP_002897. FT MUTAGEN 793 793 C->R: IN EGFR-ELP-1. FT MUTAGEN 936 936 A->T: IN EGFR-ELP-B1 AND EGFR-ELP-B1RB1. FT MUTAGEN 1058 1058 R->Q: IN EGFR-ELP-B1RB1. FT MUTAGEN 1135 1135 T->I: IN EGFR-2W74. FT MUTAGEN 1156 1156 G->S: IN EGFR-2C82. FT MUTAGEN 1162 1162 P->L: IN EGFR-1F26. FT MUTAGEN 1166 1166 S->L: IN EGFR-2L65. FT MUTAGEN 1210 1216 DKFTRLP->EKVHPAA: IN EGFR-2X51. FT CONFLICT 137 137 K -> E (IN REF. 5 AND 6). FT CONFLICT 329 331 AVS -> GVC (IN REF. 5 AND 6). FT CONFLICT 458 458 R -> L (IN REF. 5 AND 6). FT CONFLICT 789 789 R -> C (IN REF. 5 AND 6). FT CONFLICT 959 959 P -> A (IN REF. 7). FT CONFLICT 995 995 E -> V (IN REF. 5 AND 6). FT CONFLICT 1072 1080 QTPSLVKIT -> RLLAGEDH (IN REF. 3, 4 AND FT 8). FT CONFLICT 1097 1098 AA -> I (IN REF. 8). FT CONFLICT 1118 1118 T -> R (IN REF. 8). FT CONFLICT 1242 1242 K -> E (IN REF. 5 AND 6). FT CONFLICT 1265 1265 M -> I (IN REF. 5 AND 6). FT CONFLICT 1287 1287 R -> T (IN REF. 5 AND 6). FT CONFLICT 1325 1325 M -> I (IN REF. 6). FT CONFLICT 1383 1383 G -> V (IN REF. 5 AND 6). FT CONFLICT 1412 1426 ELQPLHRNRNTETRV -> SCSHASKPQHGDEGVGSSRVGA FT IANEEGESCQVPLEAMRYAFAGCYLR (IN REF. 3 AND FT 4). SQ SEQUENCE 1426 AA; 159717 MW; 4D424C3C99DA4AF4 CRC64; MLLRRRNGPC PFPLLLLLLA HCICIWPASA ARDRYARQNN RQRHQDIDRD RDRDRFLYRS SSAQNRQRGG ANFALGLGAN GVTIPTSLED KNKNEFVKGK ICIGTKSRLS VPSNKEHHYR NLRDRYTNCT YVDGNLKLTW LPNENLDLSF LDNIREVTGY ILISHVDVKK VVFPKLQIIR GRTLFSLSVE EEKYALFVTY SKMYTLEIPD LRDVLNGQVG FHNNYNLCHM RTIQWSEIVS NGTDAYYNYD FTAPERECPK CHESCTHGCW GEGPKNCQKF SKLTCSPQCA GGRCYGPKPR ECCHLFCAGG CTGPTQKDCI ACKNFFDEAV SKEECPPMRK YNPTTYVLET NPEGKYAYGA TCVKECPGHL LRDNGACVRS CPQDKMDKGG ECVPCNGPCP KTCPGVTVLH AGNIDSFRNC TVIDGNIRIL DQTFSGFQDV YANYTMGPRY IPLDPERREV FSTVKEITGY LNIEGTHPQF RNLSYFRNLE TIHGRQLMES MFAALAIVKS SLYSLEMRNL KQISSGSVVI QHNRDLCYVS NIRWPAIQKE PEQKVWVNEN LRADLCEKNG TICSDQCNED GCWGAGTDQC LTCKNFNFNG TCIADCGYIS NAYKFDNRTC KICHPECRTC NGAGADHCQE CVHVRDGQHC VSECPKNKYN DRGVCRECHA TCDGCTGPKD TIGIGACTTC NLAIINNDAT VKRCLLKDDK CPDGYFWEYV HPQEQGSLKP LAGRAVCRKC HPLCELCTNY GYHEQVCSKC THYKRREQCE TECPADHYTD EEQRECFQRH PECNGCTGPG ADDCKSCRNF KLFDANETGP YVNSTMFNCT SKCPLEMRHV NYQYTAIGPY CAASPPRSSK ITANLDVNMI FIITGAVLVP TICILCVVTY ICRQKQKAKK ETVKMTMALS GCEDSEPLRP SNIGANLCKL RIVKDAELRK GGVLGMGAFG RVYKGVWVPE GENVKIPVAI KELLKSTGAE SSEEFLREAY IMASEEHVNL LKLLAVCMSS QMMLITQLMP LGCLLDYVRN NRDKIGSKAL LNWSTQIAKG MSYLEEKRLV HRDLAARNVL VQTPSLVKIT DFGLAKLLSS DSNEYKAAGG KMPIKWLALE CIRNRVFTSK SDVWAFGVTI WELLTFGQRP HENIPAKDIP DLIEVGLKLE QPEICSLDIY CTLLSCWHLD AAMRPTFKQL TTVFAEFARD PGRYLAIPGD KFTRLPAYTS QDEKDLIRKL APTTDGSEAI AKPDDYLQPK AAPGPSHRTD CTDEMPKLNR YCKDPSNKNS STGDDERDSS AREVGVGNLR LDLPVDEDDY LMPTCQPGPN NNNNMNNPNQ NNMAAVGVAA GYMDLIGVPV SVDNPEYLLN AQTLGVGESP IPTQTIGIPV MGGPGTMEVK VPMPGSEPTS SDHEYYNDTQ RELQPLHRNR NTETRV // ID EGH_DROME STANDARD; PRT; 457 AA. AC O01346; O01347; Q9V3B0; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Egghead protein (Zeste-white 4 protein). GN EGH OR ZW4 OR L(1)3AE OR EG:BACR25B3.8 OR CG9659. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97164700; PubMed=9012507; RA Goode S., Melnick M., Chou T.B., Perrimon N.; RT "The neurogenic genes egghead and brainiac define a novel signaling RT pathway essential for epithelial morphogenesis during Drosophila RT oogenesis."; RL Development 122:3863-3879(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Simmerl E., Hollmann M., Lammermann U., Ruebsam R., Schaefer U., RA Buening J., Schaefer M.A.; RT "Characterization of a viable egh allele."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NEUROGENIC PROTEIN IMPLICATED IN EPITHELIAL DEVELOPMENT. CC CRITICAL COMPONENT OF A DIFFERENTIAL OOCYTE-FOLLICLE CELL ADHESIVE CC SYSTEM. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: STRONG, TO C.ELEGANS B0464.6. CC -!- CAUTION: REF.1 DIFFERS FROM THAT SHOWN DUE TO A FRAMESHIFT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U15602; AAB49734.1; -. DR EMBL; U21218; AAB49735.1; ALT_FRAME. DR EMBL; AF233288; AAF43419.1; -. DR EMBL; AL138972; CAB72293.1; -. DR EMBL; AE003424; AAF45792.1; -. DR FlyBase; FBgn0001404; egh. KW Developmental protein; Transmembrane. FT TRANSMEM 8 28 POTENTIAL. FT TRANSMEM 35 55 POTENTIAL. FT TRANSMEM 57 77 POTENTIAL. FT TRANSMEM 346 366 POTENTIAL. FT TRANSMEM 378 398 POTENTIAL. FT TRANSMEM 415 435 POTENTIAL. FT CONFLICT 262 262 S -> R (IN REF. 1; AAB49735). SQ SEQUENCE 457 AA; 51984 MW; F5781C27FAF4A4B5 CRC64; MNSTTKHLLH CTLLITVIVT FEVFSGGIKI DENSFTLVDP WTEYGQLATV LLYLLRFLTL LTLPQVLFNF CGLVFYNAFP EKVVLKGSPL LAPFICIRVV TRGDFPDLVK TNVLRNMNTC LDTGLENFLI EVVTDKAVNL SQHRRIREIV VPKEYKTRTG ALFKSRALQY CLEDNVNVLN DSDWIVHLDE ETLLTENSVR GIINFVLDGK HPFGQGLITY ANENVVNWLT TLADSFRVSD DMGKLRLQFK LFHKPLFSWK GSYVVTQVSA ERSVSFDNGI DGSVAEDCFF AMRAFSQGYT FNFIEGEMYE KSPFTLLDFL QQRKRWLQGI LLVVHSKMIP FKHKLLLGIS VYSWVTMPLS TSNIIFAALY PIPCPNLVDF VCAFIAAINI YMYVFGVIKS FSLYRFGLFR FLACVLGAVC TIPVNVVIEN VAVIWGLVGK KHKFYVVQKD VRVLETV // ID EGON_DROME STANDARD; PRT; 373 AA. AC P15370; Q9VNY0; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Embryonic gonad protein (Eagle protein) (Spready protein). GN EG OR EGON OR SPRY OR NR0A3 OR CG7383. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90059895; PubMed=2555153; RA Rothe M., Nauber U., Jaeckle H.; RT "Three hormone receptor-like Drosophila genes encode an identical RT DNA-binding finger."; RL EMBO J. 8:3087-3094(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96189342; PubMed=8625804; RA Higashijima S., Shishido E., Matsuzaki M., Saigo K.; RT "Eagle, a member of the steroid receptor gene superfamily, is RT expressed in a subset of neuroblasts and regulates the fate of their RT putative progeny in the Drosophila CNS."; RL Development 122:527-536(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR0 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16631; CAA34626.1; -. DR EMBL; D43635; BAA07743.1; -. DR EMBL; D43634; BAA07742.1; -. DR EMBL; AE003595; AAF51783.1; -. DR PIR; S06010; S06010. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T02774; -. DR FlyBase; FBgn0000560; eg. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 5 71 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 5 25 C4-TYPE. FT ZN_FING 42 66 C4-TYPE. FT CONFLICT 325 325 H -> P (IN REF. 3). SQ SEQUENCE 373 AA; 39601 MW; 012FF997BA9A5760 CRC64; MNQLCKVCGE PAAGFHFGAF TCEGCKSFFG RTYNNIAAIA GCKHNGDCVI NKKNRTACKA CRLRKCLLVG MSKSGSRYGR RSNWFKIHCL LQEQQTTSGL GGGSSVGSGS GGGVSSASLE QLARLQQASN QARQTYQDKT NPCIKSATAT TSPRIEGAAV GTGIGGGASP SFLQAAKLHH QRQLKLDSRL SNTPSDSGAS SAGDPNEDGV TSVLGGQIAT PSSTNATSLP KLDLRHPNFP ATSEPDADMQ RQRHQELLEI FRSHSEPLYS SFAPFSHLPP VLLAAGVPQL PIFKDQFKAE LLFPTTSSPE LEEPIDLSFR SRADHASPMA HNSNSPSLSE PAAASHCLGE STNFVRKSTP LDLTLVRSQT LTG // ID EI28_DROME STANDARD; PRT; 255 AA. AC P08761; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ecdysone-induced protein 28/29 kDa. GN EIP28/29. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS EIP28 AND EIP29). RC STRAIN=Canton-S; RX MEDLINE=87060956; PubMed=3097323; RA Cherbas L., Schulz R.A., Koehler M.M.D., Savakis C., Cherbas P.; RT "Structure of the Eip28/29 gene, an ecdysone-inducible gene from RT Drosophila."; RL J. Mol. Biol. 189:617-631(1986). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Eip28; CC IsoId=P08761-1; Sequence=Displayed; CC Name=Eip29; CC IsoId=P08761-2; Sequence=VSP_003279; CC -!- INDUCTION: BY ECDYSONE. CC -!- SIMILARITY: BELONGS TO THE MSRA MET SULFOXIDE REDUCTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58286; CAA41223.1; -. DR EMBL; X04024; CAA27657.1; -. DR EMBL; X04024; CAA27658.1; -. DR EMBL; X04521; CAA28205.1; -. DR PIR; A24254; A24254. DR HSSP; P54149; 1FVA. DR FlyBase; FBgn0000565; Eip71CD. DR GO; GO:0000096; P:sulfur amino acid metabolism; NAS. DR InterPro; IPR002569; PMSR. DR Pfam; PF01625; PMSR; 1. DR ProDom; PD003489; PMSR; 1. DR TIGRFAMs; TIGR00401; msrA; 1. KW Alternative splicing. FT VARSPLIC 79 82 Missing (in isoform Eip29). FT /FTId=VSP_003279. FT CONFLICT 252 252 V -> L (IN MRNA). SQ SEQUENCE 255 AA; 28332 MW; 343DDC8C81E125FC CRC64; MSLTITSSVT HPELKDLSTV RNEQKELNIS PVHDVNVTKA TATFGMGCFW GAESLYGATR GVLRTTVGYA GGSSDLPTYR KMGDHTEVLE IDYDPTVISF KELLDLFWNN HEYGLTTPIK RQYASLILYH DEEQKQVAHA SKLEEQERRA PEIITTEIAS KENFYPAEAY HQKYRLQGHK DLASSLNLSP KLLQTSYVAT KLNGYLAGVG GIEQFKAEAE TTGSDAHPAA VLLLPRGAER GPGSLLLTWP NVHRR // ID ELAV_DROME STANDARD; PRT; 483 AA. AC P16914; Q9V3F6; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Elav protein (Embryonic lethal abnormal visual protein). GN ELAV OR EG:65F1.2 OR CG4262. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89072740; PubMed=3144044; RA Robinow S., Campos A.R., Yao K.-M., White K.; RT "The elav gene product of Drosophila, required in neurons, has three RT RNP consensus motifs."; RL Science 242:1570-1572(1988). RN [2] RP ERRATUM. RA Robinow S., Campos A.R., Yao K.-M., White K.; RL Science 243:12-12(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR THE PROPER DEVELOPMENT AND MAINTENANCE CC OF NEURONS PRESUMABLY BY AFFECTING RNA METABOLISM. CC -!- SIMILARITY: BELONGS TO THE ELAV FAMILY OF RNP PROTEINS. CC -!- SIMILARITY: CONTAINS 3 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M21152; AAA28506.1; -. DR EMBL; AE003417; AAF45517.2; -. DR EMBL; AL022139; CAB37430.1; -. DR EMBL; AY051822; AAK93246.1; -. DR PIR; A33130; A33130. DR HSSP; P19339; 2SXL. DR FlyBase; FBgn0000570; elav. DR GO; GO:0015030; C:Cajal body; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR InterPro; IPR006548; ELAD_HUD_SF. DR InterPro; IPR002343; Hud_Sxl_RNA. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 3. DR PRINTS; PR00961; HUDSXLRNA. DR SMART; SM00360; RRM; 3. DR TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1. DR PROSITE; PS50102; RRM; 3. DR PROSITE; PS00030; RRM_RNP_1; 2. KW RNA-binding; Repeat. FT DOMAIN 24 126 ALA/GLN-RICH. FT DOMAIN 149 240 RNA-BINDING (RRM) 1. FT DOMAIN 248 329 RNA-BINDING (RRM) 2. FT DOMAIN 402 480 RNA-BINDING (RRM) 3. SQ SEQUENCE 483 AA; 50817 MW; E57336106310810B CRC64; MDFIMANTGA GGGVDTQAQL MQSAAAAAAV AATNAAAAPV QNAAAVAAAA QLQQQQVQQA ILQVQQQQTQ QAVAAAAAAV TQQLQQQQQA VVAQQAVVQQ QQQQAAAVVQ QAAVQQAVVP QPQQAQPNTN GNAGSGSQNG SNGSTETRTN LIVNYLPQTM TEDEIRSLFS SVGEIESVKL IRDKSQVYID PLNPQAPSKG QSLGYGFVNY VRPQDAEQAV NVLNGLRLQN KTIKVSFARP SSDAIKGANL YVSGLPKTMT QQELEAIFAP FGAIITSRIL QNAGNDTQTK GVGFIRFDKR EEATRAIIAL NGTTPSSCTD PIVVKFSNTP GSTSKIIQPQ LPAFLNPQLV RRIGGAMHTP VNKGLARFSP MAGDMLDVML PNGLGAAAAA ATTLASGPGG AYPIFIYNLA PETEEAALWQ LFGPFGAVQS VKIVKDPTTN QCKGYGFVSM TNYDEAAMAI RALNGYTMGN RVLQVSFKTN KAK // ID ELF1_DROME STANDARD; PRT; 1333 AA. AC P13002; Q86PE1; Q8MMA8; Q8MMB0; Q8MMB1; Q960H2; Q9TYG4; Q9V889; AC Q9V890; Q9V891; DT 01-JAN-1990 (Rel. 13, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Protein grainy-head (DNA-binding protein ELF-1) (Element I-binding DE activity) (Transcription factor NTF-1). GN GRH OR ELF1 OR EG:191D12.1 OR CG5058. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM N). RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=90006735; PubMed=2792757; RA Bray S.J., Burke B., Brown N.H., Hirsh J.; RT "Embryonic expression pattern of a family of Drosophila proteins that RT interact with a central nervous system regulatory element."; RL Genes Dev. 3:1130-1145(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS E; F AND G). RC STRAIN=Berkeley; TISSUE=Head, Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 1-415 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [6] RP SEQUENCE OF 198-1333 FROM N.A. (ISOFORM N), AND FUNCTION. RC TISSUE=Embryo; RX MEDLINE=90108664; PubMed=2606344; RA Dynlacht B.D., Attardi L.D., Admon A., Freeman M., Tjian R.; RT "Functional analysis of NTF-1, a developmentally regulated Drosophila RT transcription factor that binds neuronal cis elements."; RL Genes Dev. 3:1677-1688(1989). CC -!- FUNCTION: BINDS A CNS-SPECIFIC REGULATORY ELEMENT OF THE CC DROSOPHILA DOPA DECARBOXYLASE GENE. ALSO INTERACTS WITH SEQUENCES CC ADJACENT TO OTHER TRANSCRIPTION UNITS, INCLUDING ULTRABITHORAX AND CC ENGRAILED. ACTIVITY IN VIVO MAY BE REQUIRED ONLY AT HIGH CC LEVELS TRANSIENTLY TO ACTIVATE THE EXPRESSION OF DDC IN THE CNS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Additional isoforms seem to exist; CC Name=D; CC IsoId=P13002-6; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=N; Synonyms=A; CC IsoId=P13002-1; Sequence=VSP_008611; CC Name=B; CC IsoId=P13002-2; Sequence=VSP_008611, VSP_008612; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=P13002-3; Sequence=VSP_008612; CC Note=No experimental confirmation available; CC Name=E; CC IsoId=P13002-5; Sequence=VSP_008609, VSP_008612; CC Note=No experimental confirmation available; CC Name=F; CC IsoId=P13002-7; Sequence=VSP_008610, VSP_008612, VSP_008613, CC VSP_008614; CC Note=No experimental confirmation available; CC Name=G; CC IsoId=P13002-4; Sequence=VSP_008609; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: RESTRICTED, DURING EMBRYOGENESIS, TO TISSUES CC DERIVED FROM ECTODERM, PREDOMINANTLY THE CENTRAL NERVOUS SYSTEM CC (CNS) AND THE EPIDERMIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15657; CAA33692.1; -. DR EMBL; AE003801; AAF57782.3; -. DR EMBL; AE003801; AAF57783.2; -. DR EMBL; AE003801; AAF57784.3; -. DR EMBL; AE003801; AAM68467.2; -. DR EMBL; AE003801; AAM68468.2; -. DR EMBL; AE003801; AAM68472.2; -. DR EMBL; AY052066; AAK93490.1; -. DR EMBL; BT001414; AAN71169.1; -. DR EMBL; BT003182; AAO24937.1; -. DR EMBL; AL035312; CAA22954.1; -. DR PIR; S06206; S06206. DR TRANSFAC; T01019; -. DR FlyBase; FBgn0004586; grh. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0003704; F:specific RNA polymerase II transcription fa...; IDA. DR GO; GO:0008362; P:embryonic cuticle biosynthesis (sensu Insecta); IMP. DR InterPro; IPR007604; CP2. DR Pfam; PF04516; CP2; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW Alternative splicing. FT DOMAIN 21 36 HIS-RICH. FT DOMAIN 134 137 POLY-GLY. FT DOMAIN 153 195 GLN-RICH. FT DOMAIN 293 300 POLY-ALA. FT DOMAIN 465 516 GLN-RICH. FT DOMAIN 748 775 GLN-RICH. FT VARSPLIC 1 604 Missing (in isoform E and isoform G). FT /FTId=VSP_008609. FT VARSPLIC 1 1089 Missing (in isoform F). FT /FTId=VSP_008610. FT VARSPLIC 553 822 Missing (in isoform B and isoform N). FT /FTId=VSP_008611. FT VARSPLIC 1133 1163 Missing (in isoform B, isoform C, isoform FT E and isoform F). FT /FTId=VSP_008612. FT VARSPLIC 1271 1275 IENKY -> DYCEN (in isoform F). FT /FTId=VSP_008613. FT VARSPLIC 1276 1333 Missing (in isoform F). FT /FTId=VSP_008614. FT CONFLICT 262 262 P -> R (IN REF. 1). FT CONFLICT 415 415 S -> R (IN REF. 5). FT CONFLICT 610 610 G -> C (IN REF. 4; AAK93490). FT CONFLICT 999 999 C -> V (IN REF. 1). FT CONFLICT 1006 1007 NA -> KS (IN REF. 1). FT CONFLICT 1233 1233 R -> S (IN REF. 4; AAK93490). FT CONFLICT 1322 1322 L -> R (IN REF. 4; AAO24937). SQ SEQUENCE 1333 AA; 143914 MW; 71EBE69DAE6D071C CRC64; MSTSTATTSV ITSNELSLSG HAHGHGHAHQ LHQHTHSRLG VGVGVGILSD ASLSPIQQGS GGHSGGGNTN SSPLAPNGVP LLTTMHRSPD SPQPELATMT NVNVLDLHTD NSKLYDKEAV FIYETPKVVM PADGGGGNNS DEGHAIDARI AAQMGNQAQQ QQQQQQQTEH QPLAKIEFDE NQIIRVVGPN GEQQQIISRE IINGEHHILS RNEAGEHILT RIVSDPSKLM PNDNAVATAM YNQAQKMNND HGQAVYQTSP LPLDASVLHY SGGNDSNVIK TEADIYEDHK KHAAAAAAAA GGGSIIYTTS DPNGVNVKQL PHLTVPQKLD PDLYQADKHI DLIYNDGSKT VIYSTTDQKS LEIYSGGDIG SLVSDGQVVV QAGLPYATTT GAGGQPVYIV ADGALPAGVE EHLQSGKLNG QTTPIDVSGL SQNEIQGFLL GSHPSSSATV STTGVVSTTT ISHHQQQQQQ QQQQQQQQQQ QHQQQQQHPG DIVSAAGVGS TGSIVSSAAQ QQQQQQLISI KREPEDLRKD PKNGNIAGAA TANGPGSVIT QKILHVDAPT ASEADRPSTP SSSINSTENT ESDSQSVSGS ESGSPGARTT ATLEMYATTG GTQIYLQTSH PSTASGAGGG AGPAGAAGGG GVSMQAQSPS PGPYITANDY GMYTASRLPP GPPPTSTTTF IAEPSYYREY FAPDGQGGYV PASTRSLYGD VDVSVSQPGG VVTYEGRFAG SVPPPATTTV LTSVHHHQQQ QQQQQQHQQQ QQQQQHHQQQ QHHSQDGKSN GGATPLYAKA ITAAGLTVDL PSPDSGIGTD AITPRDQTNI QQSFDYTELC QPGTLIDANG SIPVSVNSIQ QRTAVHGSQN SPTTSLVDTS TNGSTRSRPW HDFGRQNDAD KIQIPKIFTN VGFRYHLESP ISSSQRREDD RITYINKGQF YGITLEYVHD AEKPIKNTTV KSVIMLMFRE EKSPEDEIKA WQFWHSRQHS VKQRILDADT KNSVGLVGCI EEVSHNAIAV YWNPLESSAK INIAVQCLST DFSSQKGVKG LPLHVQIDTF EDPRDTAVFH RGYCQIKVFC DKGAERKTRD EERRAAKRKM TATGRKKLDE LYHPVTDRSE FYGMQDFAKP PVLFSPAEDM EKVGQLGIGA ATGMTFNPLS NGNSNSNSHS SLQSFYGHET DSPDLKGASP FLLHGQKVAT PTLKFHNHFP PDMQTDKKDH ILDQNMLTST PLTDFGPPMK RGRMTPPTSE RVMLYVRQEN EEVYTPLHVV PPTTIGLLNA IENKYKISTT SINNIYRTNK KGITAKIDDD MISFYCNEDI FLLEVQQIED DLYDVTLTEL PNQ // ID ELG_DROME STANDARD; PRT; 464 AA. AC Q04688; Q9VBA4; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-binding protein D-ELG. GN ETS97D OR ELG OR CG6338. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93096481; PubMed=1461651; RA The S.M., Xie X., Smyth F., Papas T.S., Watson D.K., Schultz R.A.; RT "Molecular characterization and structural organization of D-elg, an RT ets proto-oncogene-related gene of Drosophila."; RL Oncogene 7:2471-2478(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 323-463 FROM N.A. RX MEDLINE=91319397; PubMed=1713660; RA Pribyl L.J., Watson D.K., Schulz R.A., Papas T.S.; RT "D-elg, a member of the Drosophila ets gene family: sequence, RT expression and evolutionary comparison."; RL Oncogene 6:1175-1183(1991). RN [4] RP SEQUENCE OF 298-449 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Larva; RX MEDLINE=92249640; PubMed=1577186; RA Chen T., Bunting M., Karim F.D., Thummel C.S.; RT "Isolation and characterization of five Drosophila genes that encode RT an ets-related DNA binding domain."; RL Dev. Biol. 151:176-191(1992). CC -!- FUNCTION: MAY HAVE A ROLE IN GERMLINE DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: UNIFORM DISTRIBUTION THROUGHOUT EMBRYONIC CC DEVELOPMENT, WITH SLIGHTLY HIGHER EXPRESSION IN POLE CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT WITH LOWER CC LEVELS DURING LARVAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -!- SIMILARITY: CONTAINS 1 POINTED (PNT) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X68259; CAA48327.1; -. DR EMBL; AE003758; AAF56638.1; -. DR EMBL; X58481; CAA41390.1; ALT_INIT. DR EMBL; M88471; AAC34199.1; -. DR PIR; S24300; S24300. DR PIR; S37616; S37616. DR HSSP; Q00422; 1AWC. DR TRANSFAC; T02085; -. DR FlyBase; FBgn0004510; Ets97D. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR InterPro; IPR003118; SAM_PNT. DR Pfam; PF00178; Ets; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SMART; SM00251; SAM_PNT; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW DNA-binding; Nuclear protein. FT DOMAIN 186 269 POINTED. FT DNA_BIND 346 425 ETS-DOMAIN. FT CONFLICT 454 454 L -> V (IN REF. 2). SQ SEQUENCE 464 AA; 52658 MW; 258A1F7C8DF427A2 CRC64; MNSSNDLSDE LIRRLSVGGA LEEVIASEMF EDSIDVETEA EPDDIIIVHM DIREPLSMLK SLVEQKIGVC LNYYTFWLQD AQELESHKNL VDQCVKGEGL VQINVQIQTI RKRINIADVL KPTEAALAAL AEEVVGQLSP PETASQKSSS SESPIKTPLK RMHKEDSEEE SVEGKDVKPV LNWVLDSKFK REQIRLKIPE AANEWTHAHV TYWLEWAVKQ FELVGINMSD WQMNGQELCA MTHEEFNQKL PRDPGNIFWT HLQLLKECNF VSVVHKRAEE QRKPKQPRIM SANSISTNSG GSLSLEQRIM RKSYQSVKSS DSVESTTSSM NPSNYTTIGS GNNGQVQLWQ FLLEILTDCE HTDVIEWVGT EGEFKLTDPD RVARLWGEKK NKPAMNYEKL SRALRYYYDG DMISKVSGKR FAYKFDCDLK LLIGYDANEL STLVSEGKTA PERLAATETI TEDT // ID EMC_DROME STANDARD; PRT; 199 AA. AC P18491; Q9W0N0; DT 01-NOV-1990 (Rel. 16, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Extra-macrochaetae protein. GN EMC OR CG1007. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90199895; PubMed=1690605; RA Garrell J., Modolell J.; RT "The Drosophila extramacrochaetae locus, an antagonist of proneural RT genes that, like these genes, encodes a helix-loop-helix protein."; RL Cell 61:39-48(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90199894; PubMed=1690604; RA Ellis H.M., Spann D.R., Posakony J.W.; RT "Extramacrochaetae, a negative regulator of sensory organ development RT in Drosophila, defines a new class of helix-loop-helix proteins."; RL Cell 61:27-38(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PARTICIPATES IN SENSORY ORGAN PATTERNING BY ANTAGONIZING CC THE NEUROGENIC ACTIVITY OF THE ACHAETE-SCUTE COMPLEX (AS-C). IT CC LACKS A BASIC DNA-BINDING DOMAIN BUT IS ABLE TO FORM HETERODIMERS CC WITH OTHER HLH PROTEINS, THEREBY INHIBITING DNA BINDING. MAY CC SEQUESTER PRONEURAL PROTEINS IN COMPLEXES INEFFICIENT FOR DNA CC INTERACTION. EMC ALSO AFFECTS VEIN DIFFERENTIATION. INHIBITS THE CC ACTIVITY OF AS-C PROTEINS BY FORMING AN NON-DNA BINDING CC HETERODIMER. CC -!- SUBUNIT: HETERODIMER WITH OTHER HLH PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M31900; AAA28510.1; -. DR EMBL; M31901; AAA28510.1; JOINED. DR EMBL; M31902; AAA28509.1; -. DR EMBL; M32637; AAA28511.1; -. DR EMBL; M32636; AAA28511.1; JOINED. DR EMBL; AE003469; AAF47413.2; -. DR EMBL; AY069405; AAL39550.1; -. DR PIR; A34689; A34689. DR TRANSFAC; T00274; -. DR FlyBase; FBgn0000575; emc. DR GO; GO:0007422; P:peripheral nervous system development; IMP. DR GO; GO:0007461; P:restriction of R8 fate; NAS. DR GO; GO:0007530; P:sex determination; IGI. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Phosphorylation; Nuclear protein; Repressor; Transcription regulation. FT DOMAIN 36 76 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 102 122 ASP/GLU-RICH (HIGHLY ACIDIC). FT DOMAIN 161 181 GLN-RICH. FT MOD_RES 106 106 PHOSPHORYLATION (POTENTIAL). FT CONFLICT 123 123 I -> V (IN REF. 1). SQ SEQUENCE 199 AA; 21978 MW; 08C1683352B26F0E CRC64; MKSLTAVCQT GASGMPALNA SGRIQRHPTH RGDGENAEMK MYLSKLKDLV PFMPKNRKLT KLEIIQHVID YICDLQTELE THPEMGNFDA AAALTAVNGL HEDEDSDMED ADAEAEAEVD PDILAQRLNA EQPAKVSSPA ARLPLTDRQT PNTLVAPAHP QQHQQQQQLQ LQQQQLQSQQ QLSNSLATPQ NAEKDSRQS // ID ENO_DROME STANDARD; PRT; 433 AA. AC P15007; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Enolase (EC 4.2.1.11) (2-phosphoglycerate dehydratase) (2-phospho-D- DE glycerate hydro-lyase). GN ENO. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90174924; PubMed=2106662; RA Bishop J.G. III, Corces V.G.; RT "The nucleotide sequence of a Drosophila melanogaster enolase gene."; RL Nucleic Acids Res. 18:191-191(1990). RN [2] RP SEQUENCE OF 33-49. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- CATALYTIC ACTIVITY: 2-PHOSPHO-D-GLYCERATE = PHOSPHOENOLPYRUVATE + CC H(2)O. CC -!- COFACTOR: MAGNESIUM IS REQUIRED FOR CATALYSIS AND FOR STABILIZING CC THE DIMER. CC -!- PATHWAY: GLYCOLYSIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE ENOLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17034; CAA34895.1; -. DR PIR; S07586; S07586. DR HSSP; P56252; 1PDZ. DR FlyBase; FBgn0000579; Eno. DR InterPro; IPR000941; Enolase. DR Pfam; PF00113; enolase; 1. DR Pfam; PF03952; enolase_N; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. KW Lyase; Glycolysis; Magnesium. FT ACT_SITE 158 158 BY SIMILARITY. FT METAL 245 245 MAGNESIUM (BY SIMILARITY). FT METAL 294 294 MAGNESIUM (BY SIMILARITY). FT METAL 319 319 MAGNESIUM (BY SIMILARITY). SQ SEQUENCE 433 AA; 46563 MW; 83CBB9091969F5F5 CRC64; MTIKAIKARQ IYDSRGNPTV EVDLTTELGL FRAAVPSGAS TGVHEALELR DNDKANYHGK SVLKAVGHVN DTLGPELIKA NLDVVDQASI DNFMIKLDGT ENKSKFGANA ILGVSLAVAK AGAAKKGVPL YKHIADLAGN KEIILPVPAF NVINGGSHAG NKLAMQEFMI LPTGATSFTE AMKMGSEVYH HLKNVIKAKF GLDATAVGDE GGFAPNIQSN KEALNLISDA IAKAGYTGKI EIGMDVAASE FYKDGQYDLD FKNEKSDKSQ WLPADKLANL YKEFIKDFPI VSIEDPFDQD HWEAWSNLTG CTDIQIVGDD LTVTNPKRIA TAVEKKACNC LLLKVNQIGT VTESIAAHLL AKKNGWGTMV SHRSGETEDS FIGDLVVGLS TGQIKTGAPC RSERLAKYNQ ILRIEEEIGA GVKFAGKSFG KPQ // ID ENV1_DROME STANDARD; PRT; 509 AA. AC P10403; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Retrovirus-related ENV polyprotein (Transposon gypsy). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87064379; PubMed=3023871; RA Marlor R.L., Parkhurst S.M., Corces V.G.; RT "The Drosophila melanogaster gypsy transposable element encodes RT putative gene products homologous to retroviral proteins."; RL Mol. Cell. Biol. 6:1129-1134(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92293139; PubMed=1318501; RA Smith P.A., Corces V.G.; RT "The suppressor of Hairy-wing binding region is required for gypsy RT mutagenesis."; RL Mol. Gen. Genet. 233:65-70(1992). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12927; AAA70220.1; ALT_INIT. DR PIR; C25666; VCFFGY. DR FlyBase; FBgn0014964; gypsy\env. KW Glycoprotein; Coat protein; Polyprotein; Transposable element. FT CARBOHYD 73 73 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 392 392 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 494 494 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 509 AA; 56852 MW; 7F8E6BA7D64F5A48 CRC64; TFPLQLGSKL CQGKSEHCSI TLSLISRFTL MMFIPLVVAN ARITDFSHAN YIPVLDGDVL VFEQRDLLKH SSNLSEYASM IDETQKLSES FPHSHMRKLL EVDTDHLRTL LSVLKVHHRI ARSLDFLGTA LKVVAGTPDA TDLFKIKITE AQLVESNSRQ IAINSETQKQ INKLTDTINK VINARKGDLV DTPHLYEALL ARNRMLSTEI QNLILTITLV KSNIINPTIL DHADLKPLVE QDTPIVSLIE ASKIRVLQSE NSIHILIAYP RVKFSCKKVA VYPVSHQHTI LRLDEDTLAE CEHDTFAVTG CTDTTHFTFC ERSRRETCVR SLHAGNAAQC HTQPSHLREI NPVDDGVVII NEAAAHVSTD GSPETLIEGT YLVTFERTAT INGSEFVNLR KTLSKQPGIV RSPLLNIVGH DPVLSIPLLH RMSNENLHSI QNLMDDVESE GSPRLWFVAG VVLNFGLIGS LALYLALRRR RASREIQRTI DTFNMTEDGH KLEGGVVNN // ID ENV2_DROME STANDARD; PRT; 471 AA. AC P20829; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Retrovirus-related ENV polyprotein (Transposon 297). GN ENV. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86108354; PubMed=2417839; RA Inouye S., Yuki S., Saigo K.; RT "Complete nucleotide sequence and genome organization of a Drosophila RT transposable genetic element, 297."; RL Eur. J. Biochem. 154:417-425(1986). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03431; CAB57797.1; ALT_SEQ. DR PIR; C24872; C24872. DR FlyBase; FBgn0027623; 297\env. KW Glycoprotein; Coat protein; Polyprotein; Transposable element. FT CARBOHYD 3 3 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 59 59 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 167 167 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 325 325 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 363 363 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 383 383 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 403 403 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 471 AA; 55245 MW; 5EE32D4F09B17960 CRC64; TLNFTGTWYP ITLLFILITA VHGQQIQINN IDTNHGYLLF SDKPVQIPSS FEHHSLKINL TEIDIVVDYF EQRLRTDYHA PQINFLYNKI KRELARITLK HRNKRGFINI VGSGFKYLFG TLDENDRVEI QKKLEINVHN SVKLHELNDA IRLINDGMQK IQNYENNHTI IDSLLFELMQ FTEYIEDLEM AMQLSRLGLF NPKLLNYDKL ENVNSQNILN IKTSTWINYN DNQVLIISHI PIYLSLISTI KIIPYPDSNG YQLDYTDTQS YFEKENKVYN TENKEVKNEC VTNIIKHLNP ICNFKPVHTN EIIKYIEPNT IVTWNLTQTI LNQNCQNSIN KIKIEGNKMI RVTQCKIEIN NINFSETLLE PEIDLTPLYT PLNITKIKIV KHNDIIEMIS ENNITLYIQM IIVIIALILL YSYLRYVSFK PFMMLYAKLK IRKNQNQNTP QQTEIEEIPF PTLYPSIPAQ V // ID ERD2_DROME STANDARD; PRT; 212 AA. AC O76767; Q9VKW0; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ER lumen protein retaining receptor. GN KDELR OR ERD2 OR CG5183. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RA Banfield D.K., Pelham H.R.B.; RT "Cloning and expression of a D. melanogaster ERD2 cDNA."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE RETENTION OF LUMINAL ENDOPLASMIC CC RETICULUM PROTEINS. DETERMINES THE SPECIFICITY OF THE LUMINAL ER CC PROTEIN RETENTION SYSTEM. ALSO REQUIRED FOR NORMAL VESICULAR CC TRAFFIC THROUGH THE GOLGI (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ERD2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF081126; AAC31955.1; -. DR EMBL; AF132559; AAD27858.1; -. DR EMBL; AE003628; AAF52948.1; -. DR FlyBase; FBgn0022268; KdelR. DR InterPro; IPR000133; ERret_receptor. DR Pfam; PF00810; ER_lumen_recept; 1. DR PRINTS; PR00660; ERLUMENR. DR ProDom; PD005774; ERret_receptor; 1. DR PROSITE; PS00951; ER_LUMEN_RECEPTOR_1; 1. DR PROSITE; PS00952; ER_LUMEN_RECEPTOR_2; 1. KW Endoplasmic reticulum; Transmembrane; Protein transport; Receptor. FT DOMAIN 1 2 LUMENAL (POTENTIAL). FT TRANSMEM 3 21 POTENTIAL. FT DOMAIN 22 35 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 36 53 POTENTIAL. FT DOMAIN 54 61 LUMENAL (POTENTIAL). FT TRANSMEM 62 80 POTENTIAL. FT DOMAIN 81 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 110 POTENTIAL. FT DOMAIN 111 117 LUMENAL (POTENTIAL). FT TRANSMEM 118 137 POTENTIAL. FT DOMAIN 138 149 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 150 168 POTENTIAL. FT DOMAIN 169 178 LUMENAL (POTENTIAL). FT TRANSMEM 179 199 POTENTIAL. FT DOMAIN 200 212 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 212 AA; 24482 MW; BBFBE4AB97C6591F CRC64; MNIFRFAGDL SHVFAIIILL LKIWKTRSCA GISGKSQILF AVVYLTRYLD LFTTYVSLYN SVMKVLFLAT SGATVYLMYV KFKATYDHNH DSFRIEFLLV PCALLSLVIN HEFTVMEVLW TFSIYLESVA ILPQLFLVSR TGEAESITSH YLFALGSYRA LYLLNWVYRY MVESHYDLIA IFAGVVQTVL YCDFFYLYIT KVLKGKKLQL PA // ID ERF1_DROME STANDARD; PRT; 438 AA. AC Q9VPH7; Q8T071; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic peptide chain release factor subunit 1 (eRF1) (Eukaryotic DE release factor 1). GN ERF1 OR CG5605. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: DIRECTS THE TERMINATION OF NASCENT PEPTIDE SYNTHESIS CC (TRANSLATION) IN RESPONSE TO THE TERMINATION CODONS UAA, UAG AND CC UGA (BY SIMILARITY). CC -!- SUBUNIT: HETERODIMER OF TWO SUBUNITS, ONE OF WHICH BINDS GTP. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC RELEASE FACTOR 1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003591; AAF51575.2; -. DR EMBL; AY069511; AAL39656.1; -. DR HSSP; P46055; 1DT9. DR FlyBase; FBgn0036974; eRF1. DR InterPro; IPR004403; eRF1. DR InterPro; IPR005140; eRF1_1. DR InterPro; IPR005141; eRF1_2. DR InterPro; IPR005142; eRF1_3. DR Pfam; PF03463; eRF1_1; 1. DR Pfam; PF03464; eRF1_2; 1. DR Pfam; PF03465; eRF1_3; 1. DR TIGRFAMs; TIGR00108; eRF; 1. KW Protein biosynthesis. SQ SEQUENCE 438 AA; 49160 MW; E16B3C08FBA1C485 CRC64; MSGEETSADR NVEIWKIKKL IKSLEMARGN GTSMISLIIP PKDQISRVSK MLADEFGTAS NIKSRVNRLS VLGAITSVQH RLKLYTKVPP NGLVIYCGTI VTEEGKEKKV NIDFEPFKPI NTSLYLCDNK FHTEALTALL ADDNKFGFIV MDGNGALFGT LQGNTREVLH KFTVDLPKKH GRGGQSALRF ARLRMEKRHN YVRKVAEVAT QLFITNDKPN IAGLILAGSA DFKTELSQSD MFDPRLQSKV IKLVDVSYGG ENGFNQAIEL AAESLQNVKF IQEKKLIGRY FDEISQDTGK YCFGVEDTLR ALELGSVETL ICWENLDIQR YVLKNHANST STTVLHLTPE QEKDKSHFTD KESGVEMELI ESQPLLEWLA NNYKMFGATL EIITDKSQEG SQFVRGFGGI GGILRYKVDF QSMQLDELDN DGFDLDDY // ID ERKA_DROME STANDARD; PRT; 376 AA. AC P40417; Q9W5M2; Q9W5M3; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitogen-activated protein kinase ERK-A (EC 2.7.1.37) (Extracellular- DE regulated kinase A) (Rolled protein). GN RL OR ERKA OR CG12559. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND RP PHOSPHORYLATION. RC STRAIN=Oregon-R; TISSUE=Embryo, and Imaginal disks; RX MEDLINE=92335284; PubMed=1378625; RA Biggs W.H. III, Zipursky S.L.; RT "Primary structure, expression, and signal-dependent tyrosine RT phosphorylation of a Drosophila homolog of extracellular signal- RT regulated kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992). RN [2] RP ERRATUM. RA Biggs W.H. III, Zipursky S.L.; RL Proc. Natl. Acad. Sci. U.S.A. 90:6377-6377(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). RN [4] RP SEQUENCE OF 1-132 FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP CHARACTERIZATION. RC STRAIN=Oregon-R; RX MEDLINE=94208532; PubMed=8157002; RA Biggs W.H. III, Zavitz K.H., Dickson B., van der Straten A., RA Brunner D., Hafen E., Zipursky S.L.; RT "The Drosophila rolled locus encodes a MAP kinase required in the RT sevenless signal transduction pathway."; RL EMBO J. 13:1628-1635(1994). CC -!- FUNCTION: REQUIRED DOWNSTREAM OF RAF IN THE SEVENLESS (SEV), TORSO CC (TOR), AND DROSOPHILA EGF RECEPTOR HOMOLOG (DER) SIGNAL CC TRANSDUCTION PATHWAYS. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- COFACTOR: MAGNESIUM (BY SIMILARITY). CC -!- ENZYME REGULATION: ACTIVATED BY TYROSINE AND THREONINE CC PHOSPHORYLATION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: IN THIRD INSTAR LARVAE, EXPRESSED IN EYE CC IMAGINAL DISKS. IN ADULTS, EXPRESSED IN HEAD AND BODY. CC -!- DEVELOPMENTAL STAGE: EMBRYOS, LARVAE AND ADULTS. CC -!- PTM: PHOSPHORYLATED ON TYROSINE RESIDUE(S) IN RESPONSE TO INSULIN. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. MAP CC KINASE SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95124; AAA28677.1; -. DR PIR; A46036; A46036. DR HSSP; P27703; 2ERK. DR FlyBase; FBgn0003256; rl. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004705; F:JUN kinase activity; IDA. DR GO; GO:0004707; F:MAP kinase activity; NAS. DR GO; GO:0006916; P:anti-apoptosis; NAS. DR GO; GO:0007369; P:gastrulation; NAS. DR GO; GO:0000165; P:MAPKKK cascade; NAS. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kin...; IMP. DR InterPro; IPR008349; Erk_1_2_MAPK. DR InterPro; IPR008350; Erk_3_4_MAPK. DR InterPro; IPR008351; JNK_MAPK. DR InterPro; IPR003527; MAP_kin. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR01770; ERK1ERK2MAPK. DR PRINTS; PR01771; ERK3ERK4MAPK. DR PRINTS; PR01772; JNKMAPKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Cell cycle; Phosphorylation. FT DOMAIN 38 326 PROTEIN KINASE. FT NP_BIND 44 52 ATP (BY SIMILARITY). FT BINDING 67 67 ATP (BY SIMILARITY). FT ACT_SITE 162 162 BY SIMILARITY. FT MOD_RES 198 198 PHOSPHORYLATION (ACTIVATES THE KINASE) FT (BY SIMILARITY). FT MOD_RES 200 200 PHOSPHORYLATION (ACTIVATES THE KINASE) FT (BY SIMILARITY). SQ SEQUENCE 376 AA; 43151 MW; 2642B3CBB0F234D2 CRC64; MEEFNSSGSV VNGTGSTEVP QSNAEVIRGQ IFEVGPRYIK LAYIGEGAYG MVVSADDTLT NQRVAIKKIS PFEHQTYCQR TLREITILTR FKHENIIDIR DILRVDSIDQ MRDVYIVQCL METDLYKLLK TQRLSNDHIC YFLYQILRGL KYIHSANVLH RDLKPSNLLL NKTCDLKICD FGLARIADPE HDHTGFLTEY VATRWYRAPE IMLNSKGYTK SIDIWSVGCI LAEMLSNRPI FPGKHYLDQL NHILGVLGSP SRDDLECIIN EKARNYLESL PFKPNVPWAK LFPNADALAL DLLGKMLTFN PHKRIPVEEA LAHPYLEQYY DPGDEPVAEV PFRINMENDD ISRDALKSLI FEETLKFKER QPDNAP // ID ER_DROME STANDARD; PRT; 104 AA. AC Q24337; Q9W3B1; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of rudimentary protein. GN E(R) OR CG1871. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95203685; PubMed=7896098; RA Wojcik E., Murphy A.M., Fares H., Dang-Vu K., Tsubota S.I.; RT "Enhancer of rudimentaryp1, e(r)p1, a highly conserved enhancer of RT the rudimentary gene."; RL Genetics 138:1163-1170(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTS AS AN ENHANCER OF THE RUDIMENTARY GENE. CC MAY HAVE A ROLE IN THE CELL CYCLE. CC -!- SIMILARITY: BELONGS TO THE E(R) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L36921; AAA74593.1; -. DR EMBL; AE003445; AAF46421.1; -. DR PIR; S50341; S50341. DR FlyBase; FBgn0011586; e(r). DR InterPro; IPR000781; Enh_rudimentary. DR Pfam; PF01133; ER; 1. DR ProDom; PD008105; Enh_rudimentary; 1. DR PROSITE; PS01290; ER; 1. SQ SEQUENCE 104 AA; 12188 MW; 294A50E7CF61B045 CRC64; MSHTILLVQP GARPETRTYC DYESVNECME GVCKIYEEHL KRRNPNTPTI TYDISQLFDF IDTMVDISCM VYQKSTNTYA PYNKDWIKEK IYVLLRQAAF SSNT // ID ESCA_DROME STANDARD; PRT; 470 AA. AC P25932; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Escargot protein (Fleabag protein). GN ESG OR FLG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92239373; PubMed=1571289; RA Whiteley M.H., Noguchi P.D., Sensabaugh S.M., Odenwald W., RA Kassis J.A.; RT "The Drosophila gene escargot encodes a zinc finger motif found in RT snail-related genes."; RL Mech. Dev. 36:117-127(1992). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE SNAIL FAMILY OF ZINC FINGER PROTEINS. CC -!- SIMILARITY: CONTAINS 5 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M83207; AAA28513.1; -. DR PIR; S33639; S33639. DR HSSP; P15822; 1BBO. DR TRANSFAC; T02329; -. DR FlyBase; FBgn0001981; esg. DR GO; GO:0007424; P:tracheal system development (sensu Insecta); NAS. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 5. DR ProDom; PD000003; Znf_C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. KW Developmental protein; Zinc-finger; Metal-binding; DNA-binding; KW Repeat. FT DOMAIN 101 116 POLY-ALA. FT ZN_FING 309 331 C2H2-TYPE 1. FT ZN_FING 344 366 C2H2-TYPE 2. FT ZN_FING 370 392 C2H2-TYPE 3. FT ZN_FING 398 420 C2H2-TYPE 4. FT ZN_FING 426 449 C2H2-TYPE 5. SQ SEQUENCE 470 AA; 51950 MW; 3E66707443B0B8EF CRC64; MHTVEDMLVE KNYSKCPLKK RPVNYQFEAP QNHSNTPNEP QDLCVKKMEI LEENPSEELI NVSDCCEDEG VDVDHTDDEH IEEEDEDVDV DVDSDPNQTQ AAALAAAAAV AAAAAASVVV PTPTYPKYPW NNFHMSPYTA EFYRTINQPG HQILPLRGDL IAPSSPSDSL GSLSPPPHHY LHGRASSVSP PMRSEMIHRP IGVRQHRFLP YPQMPGYPSL GGYTHTHHHH APISPAYSEN SYYSMRSMTP ESSCSSSLPE DLSLKHKNLN LNLNTSQPGE QAAAKTGDMS PETMPNASAK KDKNQPPRYQ CPDCQKSYST FSGLTKHQQF HCPAAEGNQV KKSFSCKDCD KTYVSLGALK MHIRTHTLPC KCNLCGKAFS RPWLLQGHIR THTGEKPFSC QHCHRAFADR SNLRAHLQTH SDIKKYSCTS CSKTFSRMSL LTKHSEGGCP GGSAGSSSSS ELNYAGYAEP // ID ESC_DROME STANDARD; PRT; 425 AA. AC Q24338; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Polycomb protein Esc (Extra sex combs protein). GN ESC OR CG14941. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, CHARACTERIZATION, AND MUTANT RP ESC1. RC TISSUE=Embryo; RX MEDLINE=96016202; PubMed=7556071; RA Gutjahr T., Frei E., Spicer C., Baumgartner S., White R.A.H., Noll M.; RT "The Polycomb-group gene, extra sex combs, encodes a nuclear member of RT the WD-40 repeat family."; RL EMBO J. 14:4296-4306(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP INTERACTION WITH E(Z). RX MEDLINE=98226554; PubMed=9566901; RA Jones C.A., Ng J., Peterson A.J., Morgan K., Simon J.A., Jones R.S.; RT "The Drosophila esc and E(z) proteins are direct partners in polycomb RT group-mediated repression."; RL Mol. Cell. Biol. 18:2825-2834(1998). RN [5] RP PHOSPHORYLATION, AND MUTAGENESIS OF 210-GLY-GLY-211 AND RP 216-ARG--GLU-218. RX MEDLINE=20221553; PubMed=10757791; RA Ng J., Hart C.M., Morgan K., Simon J.A.; RT "A Drosophila ESC-E(Z) protein complex is distinct from other polycomb RT group complexes and contains covalently modified ESC."; RL Mol. Cell. Biol. 20:3069-3078(2000). RN [6] RP IDENTIFICATION IN A COMPLEX WITH RPD3; E(Z) AND CAF1. RX MEDLINE=21064443; PubMed=11124122; RA Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.; RT "The Drosophila polycomb group proteins ESC and E(Z) are present in a RT complex containing the histone-binding protein p55 and the histone RT deacetylase RPD3."; RL Development 128:275-286(2001). RN [7] RP IDENTIFICATION IN A COMPLEX WITH RPD3; PHO AND E(Z), AND RP TRANSIENT INTERACTION WITH THE PRC1 COMPLEX. RX MEDLINE=21464651; PubMed=11581156; RA Poux S., Melfi R., Pirrotta V.; RT "Establishment of Polycomb silencing requires a transient interaction RT between PC and ESC."; RL Genes Dev. 15:2509-2514(2001). RN [8] RP IDENTIFICATION IN A ESC/E(Z) COMPLEX WITH E(Z); CAF1; RPD3 AND RP SU(Z)12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX. RX MEDLINE=22296673; PubMed=12408863; RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.; RT "Drosophila enhancer of Zeste/ESC complexes have a histone H3 RT methyltransferase activity that marks chromosomal Polycomb sites."; RL Cell 111:185-196(2002). RN [9] RP IDENTIFICATION IN A ESC/E(Z) COMPLEX WITH E(Z); CAF1 AND SU(Z)12, AND RP METHYLTRANSFERASE ACTIVITY OF THE COMPLEX. RX MEDLINE=22296674; PubMed=12408864; RA Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., RA Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.; RT "Histone methyltransferase activity of a Drosophila Polycomb group RT repressor complex."; RL Cell 111:197-208(2002). CC -!- FUNCTION: POLYCOMB GROUP (PCG) PROTEIN. IN CONTRAST TO OTHER PCG CC PROTEIN, IT IS SPECIFICALLY REQUIRED DURING THE FIRST 6 HOURS OF CC EMBRYOGENESIS TO ESTABLISH PCG SILENCING. PCG PROTEINS ACT BY CC FORMING MULTIPROTEIN COMPLEXES, WHICH ARE REQUIRED TO MAINTAIN THE CC TRANSCRIPTIONALLY REPRESSIVE STATE OF HOMEOTIC GENES THROUGHOUT CC DEVELOPMENT. PCG PROTEINS ARE NOT REQUIRED TO INITIATE REPRESSION, CC BUT TO MAINTAIN IT DURING LATER STAGES OF DEVELOPMENT. THEY CC PROBABLY ACT VIA A METHYLATION OF HISTONES, RENDERING CHROMATIN CC HERITABLY CHANGED IN ITS EXPRESSIBILITY. COMPONENT OF THE ESC/E(Z) CC COMPLEX, WHICH METHYLATES LYS-9 AND LYS-27 RESIDUES OF HISTONE H3. CC THE ESC/E(Z) COMPLEX IS NECESSARY BUT NOT SUFFICIENT TO RECRUIT A CC FUNCTIONAL PCG REPRESSIVE COMPLEX THAT REPRESSES TARGET GENES, CC SUGGESTING THAT THE RECRUITMENT OF THE DISTINCT PRC1 COMPLEX IS CC ALSO REQUIRED TO ALLOW A SUBSEQUENT REPRESSION. CC -!- SUBUNIT: COMPONENT OF THE ESC/E(Z) COMPLEX, COMPOSED OF ESC, E(Z), CC SU(Z)12, RPD3, CAF1 AND PROBABLY PHO. THIS COMPLEX IS DISTINCT CC FROM THE PRC1 COMPLEX, WHICH CONTAINS MANY OTHER PCG PROTEINS LIKE CC PC, PH, PSC, SU(Z)2. THE TWO COMPLEXES HOWEVER COOPERATE AND CC INTERACT TOGETHER DURING THE FIRST 3 HOURS OF DEVELOPMENT TO CC ESTABLISH PCG SILENCING. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC STRONGLY EXPRESSED IN THE OOCYTE AND IN EARLY EMBRYOS, THEN CC DECREASES AT THE END OF EMBRYOGENESIS. WEAKLY EXPRESSED IN THIRD CC INSTAR LARVAE. TRANSIENTLY REQUIRED BETWEEN 2 AND 6 HOURS OF CC EMBRYOGENESIS TO ESTABLISH PCG SILENCING AND PROMOTE VIABLE CC ADULTS. CC -!- PTM: PHOSPHORYLATED. CC -!- SIMILARITY: BELONGS TO THE WD-REPEAT ESC FAMILY. CC -!- SIMILARITY: CONTAINS 7 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L41867; AAA86427.1; -. DR EMBL; AE003634; AAF53124.1; -. DR EMBL; AY069796; AAL39941.1; -. DR PIR; S58672; S58672. DR TRANSFAC; T02156; -. DR FlyBase; FBgn0000588; esc. DR GO; GO:0000790; C:nuclear chromatin; ISS. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0006342; P:chromatin silencing; ISS. DR GO; GO:0048096; P:chromatin-mediated maintenance of transcrip...; NAS. DR GO; GO:0016458; P:gene silencing; IGI. DR GO; GO:0006340; P:negative regulation of transcription of hom...; IPI. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 3. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Transcription regulation; Repressor; Developmental protein; KW Nuclear protein; Repeat; WD repeat; Phosphorylation. FT REPEAT 71 114 WD 1. FT REPEAT 126 165 WD 2. FT REPEAT 168 208 WD 3. FT REPEAT 214 253 WD 4. FT REPEAT 284 321 WD 5. FT REPEAT 340 379 WD 6. FT REPEAT 388 424 WD 7. FT MUTAGEN 64 64 Y->F: IN ESC1; INDUCES HOMEOTIC FT TRANSFORMATION; WHEN ASSOCIATED WITH R- FT 240. FT MUTAGEN 210 211 GG->AA: STRONGLY REDUCES PHOSPHORYLATION FT AND THE INTERACTION WITH E(Z). FT MUTAGEN 216 218 RDE->AAA: STRONGLY REDUCES FT PHOSPHORYLATION AND THE INTERACTION WITH FT E(Z). FT MUTAGEN 240 240 L->R: IN ESC1; INDUCES HOMEOTIC FT TRANSFORMATION; WHEN ASSOCIATED WITH FT F-64. SQ SEQUENCE 425 AA; 47987 MW; 511C305E5DE86727 CRC64; MSSDKVKNGN EPEESEESCG DESASYTTNS TTSRSKSPSS STRSKRRGRR STKSKPKSRA AYKYDTHVKE NHGANIFGVA FNTLLGKDEP QVFATAGSNR VTVYECPRQG GMQLLHCYAD PDPDEVFYTC AWSYDLKTSS PLLAAAGYRG VIRVIDVEQN EAVGNYIGHG QAINELKFHP HKLQLLLSGS KDHAIRLWNI QSHVCIAILG GVEGHRDEVL SIDFNMRGDR IVSSGMDHSL KLWCLNTPEF HHKIELSNTF SQEKSTLPFP TVTKHFPDFS TRDIHRNYVD CVQWFGNFVL SKSCENAIVC WKPGQLHQSF EQVKPSDSSC TIIAEFEYDE CEIWFVRFGF NPWQKVIALG NQQGKVYVWE LDPSDPEGAH MTTLHNSRSV ATVRQIAFSR DASVLVYVCD DATVWRWNRR QTTSI // ID ESM1_DROME STANDARD; PRT; 156 AA. AC O97176; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split M1 protein precursor (E(spl)m1). GN M1 OR CG8342. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=99173785; PubMed=10072784; RA Wurmbach E., Wech I., Preiss A.; RT "The Enhancer of split complex of Drosophila melanogaster harbors RT three classes of Notch responsive genes."; RL Mech. Dev. 80:171-180(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT THE TIME WHEN SEPARATION OF CC NEURAL AND EPIDERMAL PRECURSORS CELLS OCCURS. ACCUMULATES CC TRANSIENTLY AT THE FUSION SITES OF ANTERIOR AND POSTERIOR MIDGUT CC AND VERY SPECIFICALLY TO HIGH LEVELS IN THE PROVENTRICULUS OF THE CC EMBRYO. CC -!- SIMILARITY: CONTAINS 1 KAZAL-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ010167; CAB39163.1; -. DR EMBL; AE003754; AAF56548.1; -. DR FlyBase; FBgn0002578; m1. DR InterPro; IPR002350; kazal. DR Pfam; PF00050; kazal; 1. DR SMART; SM00280; KAZAL; 2. DR PROSITE; PS00282; KAZAL; FALSE_NEG. KW Serine protease inhibitor; Differentiation; Neurogenesis; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 156 ENHANCER OF SPLIT M1 PROTEIN. FT DOMAIN 29 75 KAZAL-LIKE. SQ SEQUENCE 156 AA; 17339 MW; 5C29F73AE89F6949 CRC64; MMSQTLTLCC LALVACVYGN TVSTNDTACP TFCPSIYKPV CGTDGQNFKE FASTCNLLSH NCRRERNSVQ AYAATDAAWC SSEFVENLHE KLGNFKLEVK ECFKPCSMIY QPVCITNGKY RAELANSCLL ENFNCALQVS GAQPAELFRL LREEKC // ID ESM2_DROME STANDARD; PRT; 218 AA. AC O97177; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split M2 protein (E(spl)m2). GN M2 OR CG6104. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=99173785; PubMed=10072784; RA Wurmbach E., Wech I., Preiss A.; RT "The Enhancer of split complex of Drosophila melanogaster harbors RT three classes of Notch responsive genes."; RL Mech. Dev. 80:171-180(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PART OF THE NOTCH SIGNALING PATHWAY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT THE TIME WHEN SEPARATION OF CC NEURAL AND EPIDERMAL PRECURSORS CELLS OCCURS. DETECTED IN THE CC NEURO-ECTODERM OF STAGE 9 EMBRYOS. AT STAGE 10/11, ACCUMULATES AT CC HIGH LEVELS IN THE PRESUMPTIVE MESODERM, HOWEVER, IT DISAPPEARS CC QUICKLY WITH THE ONSET OF GERM BAND RETRACTION. IN EYE DISK, CC EXPRESSION OCCURS CLOSE TO, AS WELL AS POSTERIOR TO THE CC MORPHOGENETIC FURROW. IN THE WING DISK, FOUND IN THE PRONEURAL CC CLUSTERS AREAS, THE DORSO-VENTRAL BOUNDARY AND VEIN/INTERVEIN CC REGIONS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ010168; CAB39174.1; -. DR EMBL; AE003754; AAF56549.1; -. DR FlyBase; FBgn0002592; m2. KW Differentiation; Neurogenesis. FT DOMAIN 66 74 POLY-GLN. FT DOMAIN 152 157 POLY-SER. FT VARIANT 186 186 G -> D. SQ SEQUENCE 218 AA; 24117 MW; 8DC97662E9B0BE13 CRC64; MYLDTKNLTA SSTSALTAAT ASNSKSTRRM RNVWKPLSRL LKVGGKGRTA QATLAHPNNV DLNNTQQQQQ QQQQELLIED DTKSTPEESI HKYGLELRQL PEEEQVSLTQ PPNTPTLISS VHVDKVSAQS CGNCQHGRNC QHRHHSSSNI NSSSSSSNMN SSSATQLPSN LWDLQLPLQY ISTDNGTFFW ANTQDRVDDD LLHALLCQSF SQLPGTLC // ID ESM3_DROME STANDARD; PRT; 224 AA. AC Q01068; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split m3 protein (E(spl)m3) (HLH-m3). GN HLHM3 OR CG8346. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92409590; PubMed=1528887; RA Delidakis C., Artavanis-Tsakonas S.; RT "The Enhancer of split [E(spl)] locus of Drosophila encodes seven RT independent helix-loop-helix proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8731-8735(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93051287; PubMed=1427040; RA Knust E., Schrons H., Grawe F., Campos-Ortega J.A.; RT "Seven genes of the Enhancer of split complex of Drosophila RT melanogaster encode helix-loop-helix proteins."; RL Genetics 132:505-518(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP WRPW MOTIF. RX MEDLINE=95094252; PubMed=8001118; RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., RA Brent R., Ish-Horowicz D.; RT "Groucho is required for Drosophila neurogenesis, segmentation, and RT sex determination and interacts directly with hairy-related bHLH RT proteins."; RL Cell 79:805-815(1994). CC -!- FUNCTION: TRANSCRIPTIONAL REPRESSOR OF GENES THAT REQUIRE A BHLH CC PROTEIN FOR THEIR TRANSCRIPTION. MAY SERVE AS A TRANSCRIPTIONAL CC REGULATOR OF THE ACHAETE-SCUTE COMPLEX (ASC) GENES. BELONGS TO CC NOTCH SIGNALING PATHWAY AND DEPENDS ON SU(H) FOR TRANSCRIPTIONAL CC ACTIVATION. CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: THE RNA IS SUPPLIED MATERNALLY, AND LATER ON, CC EXPRESSION IS UBIQUITOUS DURING ALL STAGES OF EMBRYONIC CC DEVELOPMENT. CC -!- DOMAIN: HAS A PARTICULAR TYPE OF BASIC DOMAIN (PRESENCE OF A CC HELIX-INTERRUPTING PROLINE) THAT BINDS TO THE N-BOX (CACNAG), CC RATHER THAN THE CANONICAL E-BOX (CANNTG). CC -!- DOMAIN: THE C-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL REPRESSION CC DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96165; AAA28908.1; -. DR EMBL; X67046; CAA47431.1; -. DR EMBL; AE003754; AAF56550.1; -. DR PIR; D46177; D46177. DR FlyBase; FBgn0002609; HLHm3. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Neurogenesis; DNA-binding; Transcription regulation; KW Nuclear protein; Coiled coil. FT DNA_BIND 12 24 BASIC DOMAIN. FT DOMAIN 25 69 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 127 155 COILED COIL (POTENTIAL). FT DOMAIN 143 155 POLY-GLN. FT DOMAIN 174 179 POLY-ALA. FT DOMAIN 221 224 WRPW MOTIF. FT CONFLICT 150 150 MISSING (IN REF. 2). FT CONFLICT 174 176 AAA -> SRR (IN REF. 2). FT CONFLICT 179 179 MISSING (IN REF. 2). SQ SEQUENCE 224 AA; 24983 MW; E16D13530FD283C9 CRC64; MVMEMSKTYQ YRKVMKPLLE RKRRARINKC LDDLKDLMVE CLQQEGEHVT RLEKADILEL TVDHMRKLKQ RGGLSLQGVV AGVGSPPTST STAHVESFRS GYVHAADQIT QVLLQTQQTD EIGRKIMKFL STRLIELQTQ LLQQQQQQQQ HQQQQIPQSS GRLAFPLLGG YGPAAAAAAI SYSSFLTSKD ELIDVTSVDG NALSETASVS SQESGASEPV WRPW // ID ESM4_DROME STANDARD; PRT; 152 AA. AC P13095; Q9VBI9; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split m4 protein (E(spl)m4). GN M4 OR CG6099. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89231619; PubMed=2540957; RA Klaembt C., Knust E., Tietze K., Campos-Ortega J.A.; RT "Closely related transcripts encoded by the neurogenic gene complex RT enhancer of split of Drosophila melanogaster."; RL EMBO J. 8:203-210(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PART OF THE NOTCH SIGNALING PATHWAY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT THE TIME WHEN SEPARATION OF CC NEURAL AND EPIDERMAL PRECURSORS CELLS OCCURS. MESECTODERMAL CC EXPRESSION APPEARS SHORTLY BEFORE THE ONSET OF GASTRULATION. IN CC IMAGINAL DISKS, EXPRESSION IS SEEN PRIMARILY WITHIN PRESUMPTIVE CC PRONEURAL CLUSTERS OF EYE-ANTENNAL, WING AND LEG DISKS. CC -!- SIMILARITY: BELONGS TO THE M4-LIKE PROTEIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16551; CAA34551.1; -. DR EMBL; AE003754; AAF56551.1; -. DR PIR; S03630; S03630. DR FlyBase; FBgn0002629; m4. KW Differentiation; Neurogenesis; Coiled coil. FT DOMAIN 23 61 COILED COIL (POTENTIAL). SQ SEQUENCE 152 AA; 17250 MW; D7F642838BD2DA0C CRC64; MCQNKINTNN TMTIKSNKKL SYSVKKLLQK IFKQQQRVEE EQNLKNALKA NSLESLESME NSRNADLESA SICASLESCE NEANERLSQS CEIEDYDFEQ LPTVPVHFVR TAHGTFFWTA VSDLPADNDL VEPLYCSTSN AIAIPQDRWV QA // ID ESM5_DROME STANDARD; PRT; 178 AA. AC P13096; Q9VBI8; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split m5 protein (E(spl)m5). GN HLHM5 OR CG6096. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89231619; PubMed=2540957; RA Klaembt C., Knust E., Tietze K., Campos-Ortega J.A.; RT "Closely related transcripts encoded by the neurogenic gene complex RT enhancer of split of Drosophila melanogaster."; RL EMBO J. 8:203-210(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP WRPW MOTIF. RX MEDLINE=95094252; PubMed=8001118; RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., RA Brent R., Ish-Horowicz D.; RT "Groucho is required for Drosophila neurogenesis, segmentation, and RT sex determination and interacts directly with hairy-related bHLH RT proteins."; RL Cell 79:805-815(1994). CC -!- FUNCTION: PARTICIPATES IN THE CONTROL OF CELL FATE CHOICE BY CC UNCOMMITTED NEURODECTODERMAL CELLS IN THE EMBRYO. TRANSCRIPTIONAL CC REPRESSOR. BINDS DNA ON N-BOX MOTIFS: 5'-CACNAG-3'. CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO). FORMS HOMODIMERS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT THE TIME WHEN SEPARATION OF CC NEURAL AND EPIDERMAL PRECURSORS CELLS OCCURS. MESECTODERMAL CC EXPRESSION APPEARS SHORTLY BEFORE THE ONSET OF GASTRULATION. CC -!- DOMAIN: THE ORANGE DOMAIN AND THE BASIC HELIX-LOOP-HELIX MOTIF CC MEDIATE REPRESSION OF SPECIFIC TRANSCRIPTIONAL ACTIVATORS, SUCH CC AS BASIC HELIX-LOOP-HELIX PROTEIN DIMERS. CC -!- DOMAIN: THE C-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL REPRESSION CC DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16552; CAA34552.1; -. DR EMBL; AE003754; AAF56552.1; -. DR PIR; S03629; S03629. DR TRANSFAC; T01644; -. DR FlyBase; FBgn0002631; HLHm5. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Neurogenesis; Nuclear protein; DNA-binding; KW Transcription regulation; Repressor. FT DNA_BIND 19 33 BASIC DOMAIN. FT DOMAIN 34 74 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 88 129 ORANGE. FT DOMAIN 175 178 WRPW MOTIF. SQ SEQUENCE 178 AA; 19923 MW; 19363D0F6043C84F CRC64; MAPQSNNSTT FVSKTQHYLK VKKPLLERQR RARMNKCLDT LKTLVAEFQG DDAILRMDKA EMLEAALVFM RKQVVKQQAP VSPLPMDSFK NGYMNAVSEI SRVMACTPAM SVDVGKTVMT HLGVEFQRML QADQVQTSVT TSTPRPLSPA SSGYHSDNED SQSAASPKPV EETMWRPW // ID ESM6_DROME STANDARD; PRT; 70 AA. AC O97179; Q9VBI7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split m6 protein (E(spl)m6). GN M6 OR CG8354. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=99173785; PubMed=10072784; RA Wurmbach E., Wech I., Preiss A.; RT "The Enhancer of split complex of Drosophila melanogaster harbors RT three classes of Notch responsive genes."; RL Mech. Dev. 80:171-180(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT THE TIME WHEN SEPARATION OF CC NEURAL AND EPIDERMAL PRECURSORS CELLS OCCURS. EXPRESSED WITHIN CC NEURONAL CELLS IN THE EMBRYO. LATER IN DEVELOPMENT, ACCUMULATES CC WITHIN THE DEVELOPING CENTRAL NERVOUS SYSTEM. AFTER GERM BAND CC RETRACTION, FOUND IN BRAIN, VENTRAL NERVE CHORD AND IN PRESUMPTIVE CC PERIPHERAL NERVOUS SYSTEM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ012204; CAB39177.1; -. DR EMBL; AE003754; AAF56553.1; -. DR FlyBase; FBgn0002632; m6. KW Differentiation; Neurogenesis. FT VARIANT 20 20 S -> L. FT CONFLICT 21 21 Q -> H (IN REF. 1). SQ SEQUENCE 70 AA; 8059 MW; 03EBCC8B54BC01AA CRC64; MSKVKNLLAK MLQRFGKNSS QADSQRYDSL EEIAQNQANE RMLRATQVGL EEHLVICLET EAGSFYWHSQ // ID ESM7_DROME STANDARD; PRT; 186 AA. AC P13097; Q9VBI6; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split m7 protein (E(spl)m7). GN HLHM7 OR CG8361. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89231619; PubMed=2540957; RA Klaembt C., Knust E., Tietze K., Campos-Ortega J.A.; RT "Closely related transcripts encoded by the neurogenic gene complex RT enhancer of split of Drosophila melanogaster."; RL EMBO J. 8:203-210(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP WRPW MOTIF. RX MEDLINE=95094252; PubMed=8001118; RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., RA Brent R., Ish-Horowicz D.; RT "Groucho is required for Drosophila neurogenesis, segmentation, and RT sex determination and interacts directly with hairy-related bHLH RT proteins."; RL Cell 79:805-815(1994). CC -!- FUNCTION: PARTICIPATES IN THE CONTROL OF CELL FATE CHOICE BY CC UNCOMMITTED NEUROECTODERMAL CELLS IN THE EMBRYO. TRANSCRIPTIONAL CC REPRESSOR. BINDS DNA ON N-BOX MOTIFS: 5'-CACNAG-3'. CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO). FORMS HOMODIMERS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT THE TIME WHEN SEPARATION OF CC NEURAL AND EPIDERMAL PRECURSORS CELLS OCCURS. MESECTODERMAL CC EXPRESSION APPEARS SHORTLY BEFORE THE ONSET OF GASTRULATION. IN CC IMAGINAL DISKS, EXPRESSION IS SEEN PRIMARILY WITHIN PRESUMPTIVE CC PRONEURAL CLUSTERS OF EYE-ANTENNAL, WING AND LEG DISKS. CC -!- DOMAIN: THE ORANGE DOMAIN AND THE BASIC HELIX-LOOP-HELIX MOTIF CC MEDIATE REPRESSION OF SPECIFIC TRANSCRIPTIONAL ACTIVATORS, SUCH CC AS BASIC HELIX-LOOP-HELIX PROTEIN DIMERS. CC -!- DOMAIN: THE C-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL REPRESSION CC DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16553; CAA34553.1; -. DR EMBL; AE003754; AAF56554.1; -. DR PIR; S03626; S03626. DR TRANSFAC; T01645; -. DR FlyBase; FBgn0002633; HLHm7. DR GO; GO:0005578; C:extracellular matrix; ISS. DR GO; GO:0008189; F:apoptosis inhibitor activity; ISS. DR GO; GO:0042056; F:chemoattractant activity; ISS. DR GO; GO:0005125; F:cytokine activity; ISS. DR GO; GO:0003793; F:defense/immunity protein activity; ISS. DR GO; GO:0008083; F:growth factor activity; ISS. DR GO; GO:0005178; F:integrin binding; ISS. DR GO; GO:0006916; P:anti-apoptosis; ISS. DR GO; GO:0007267; P:cell-cell signaling; ISS. DR GO; GO:0007160; P:cell-matrix adhesion; ISS. DR GO; GO:0030595; P:immune cell chemotaxis; ISS. DR GO; GO:0006954; P:inflammatory response; ISS. DR GO; GO:0030502; P:negative regulation of bone mineralization; ISS. DR GO; GO:0042102; P:positive regulation of T-cell proliferation; ISS. DR GO; GO:0045637; P:regulation of myeloid blood cell differenti...; ISS. DR GO; GO:0042088; P:T-helper 1 type immune response; ISS. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Neurogenesis; Nuclear protein; DNA-binding; KW Transcription regulation; Repressor. FT DNA_BIND 14 28 BASIC DOMAIN. FT DOMAIN 29 69 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 82 123 ORANGE. FT DOMAIN 183 186 WRPW MOTIF. SQ SEQUENCE 186 AA; 20686 MW; 9330530963CDCE15 CRC64; MATKYEMSKT YQYRKVMKPL LERKRRARIN KCLDELKDLM AECVAQTGDA KFEKADILEV TVQHLRKLKE SKKHVPANPE QSFRAGYIRA ANEVSRALAS LPRVDVAFGT TLMTHLGMRL NQLEQPMEQP QAVNTPLSIV CGSSSSSSTY SSASSCSSIS PVSSGYASDN ESLLQISSPG QVWRPW // ID ESM8_DROME STANDARD; PRT; 179 AA. AC P13098; Q9VBI5; DT 01-JAN-1990 (Rel. 13, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split m8 protein (E(spl)m8). GN E(SPL) OR M8 OR CG8365. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89231619; PubMed=2540957; RA Klaembt C., Knust E., Tietze K., Campos-Ortega J.A.; RT "Closely related transcripts encoded by the neurogenic gene complex RT enhancer of split of Drosophila melanogaster."; RL EMBO J. 8:203-210(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP WRPW MOTIF. RX MEDLINE=95094252; PubMed=8001118; RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., RA Brent R., Ish-Horowicz D.; RT "Groucho is required for Drosophila neurogenesis, segmentation, and RT sex determination and interacts directly with hairy-related bHLH RT proteins."; RL Cell 79:805-815(1994). CC -!- FUNCTION: PARTICIPATES IN THE CONTROL OF CELL FATE CHOICE BY CC UNCOMMITTED NEURODECTODERMAL CELLS IN THE EMBRYO. TRANSCRIPTIONAL CC REPRESSOR. BINDS DNA ON N-BOX MOTIFS: 5'-CACNAG-3'. CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO). FORMS HOMODIMERS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: MESECTODERMAL EXPRESSION APPEARS SHORTLY CC BEFORE THE ONSET OF GASTRULATION. IN IMAGINAL DISKS, EXPRESSION IS CC SEEN PRIMARILY WITHIN PRESUMPTIVE PRONEURAL CLUSTERS OF EYE- CC ANTENNAL, WING AND LEG DISKS. CC -!- DOMAIN: THE ORANGE DOMAIN AND THE BASIC HELIX-LOOP-HELIX MOTIF CC MEDIATE REPRESSION OF SPECIFIC TRANSCRIPTIONAL ACTIVATORS, SUCH CC AS BASIC HELIX-LOOP-HELIX PROTEIN DIMERS. CC -!- DOMAIN: THE C-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL REPRESSION CC DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16553; CAA34554.1; -. DR EMBL; AE003754; AAF56555.1; -. DR PIR; S03627; S03627. DR TRANSFAC; T01646; -. DR FlyBase; FBgn0000591; E(spl). DR GO; GO:0007173; P:EGF receptor signaling pathway; NAS. DR GO; GO:0007498; P:mesoderm development; IMP. DR GO; GO:0007219; P:N signaling pathway; NAS. DR GO; GO:0045468; P:regulation of R8 spacing; NAS. DR GO; GO:0008587; P:wing margin morphogenesis; NAS. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Neurogenesis; DNA-binding; Nuclear protein; KW Transcription regulation; Repressor. FT DNA_BIND 12 25 BASIC DOMAIN. FT DOMAIN 26 66 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 82 123 ORANGE. FT DOMAIN 176 179 WRPW MOTIF. FT CONFLICT 165 167 APS -> PPT (IN REF. 1). SQ SEQUENCE 179 AA; 20303 MW; 017B139DE0C328B4 CRC64; MEYTTKTQIY QKVKKPMLER QRRARMNKCL DNLKTLVAEL RGDDGILRMD KAEMLESAVI FMRQQKTPKK VAQEEQSLPL DSFKNGYMNA VNEVSRVMAS TPGMSVDLGK SVMTHLGRVY KNLQQFHEAQ SAADFIQNSM DCSSMDKAPL SPASSGYHSD CDSPAPSPQP MQQPLWRPW // ID ESMA_DROME STANDARD; PRT; 138 AA. AC O97178; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split malpha protein (E(spl)malpha). GN M-ALPHA OR CG8337. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=99173785; PubMed=10072784; RA Wurmbach E., Wech I., Preiss A.; RT "The Enhancer of split complex of Drosophila melanogaster harbors RT three classes of Notch responsive genes."; RL Mech. Dev. 80:171-180(1999). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=20072615; PubMed=10603347; RA Lai E.C., Bodner R., Kavaler J., Freschi G., Posakony J.W.; RT "Antagonism of Notch signaling activity by members of a novel protein RT family encoded by the Bearded and Enhancer of split gene complexes."; RL Development 127:291-306(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PART OF THE NOTCH SIGNALING PATHWAY. CC -!- DEVELOPMENTAL STAGE: MESECTODERMAL EXPRESSION APPEARS SHORTLY CC BEFORE THE ONSET OF GASTRULATION. LATER IT IS DETECTED IN THE CC NEURO-ECTODERM AS WELL AS IN THE MESODERM IN A HIGHLY DYNAMIC CC PATTERN IN MANY STAGES OF EMBRYOGENESIS. IN IMAGINAL DISKS, CC EXPRESSED AS FOLLOWING: IN THE EYE DISK, WITHIN AND POSTERIOR TO CC THE MORPHOGENETIC FURROW; IN THE WING POUCH, IN THE PRESUMPTIVE CC INTERVEIN REGIONS AND WING MARGIN; IN THE LEG DISK, GENERAL CC EXPRESSION. CC -!- SIMILARITY: BELONGS TO THE M4-LIKE PROTEIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ011140; CAB39164.1; -. DR EMBL; AF115456; AAF12878.1; -. DR EMBL; AE003754; AAF56547.1; -. DR FlyBase; FBgn0002732; m-alpha. FT DOMAIN 5 8 POLY-VAL. SQ SEQUENCE 138 AA; 15876 MW; B277BCC25CD82F59 CRC64; MCQQVVVVAN TNNKMKTSYS IKQVLKTLFK KQQKQQQKPQ GSLESLESVD NLRNAQVEEA YYAEIDENAA NEKLAQLAHS QEFEIVEEQE DEEDVYVPVR FARTTAGTFF WTTNLQPVAS VEPAMCYSMQ FQDRWAQA // ID ESMB_DROME STANDARD; PRT; 195 AA. AC Q01069; Q01906; Q9VBJ0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split mbeta protein (E(spl)mbeta) (HLH-mbeta) (Split locus DE enhancer protein mA). GN HLHM-BETA OR CG14548. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92409590; PubMed=1528887; RA Delidakis C., Artavanis-Tsakonas S.; RT "The Enhancer of split [E(spl)] locus of Drosophila encodes seven RT independent helix-loop-helix proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8731-8735(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93051287; PubMed=1427040; RA Knust E., Schrons H., Grawe F., Campos-Ortega J.A.; RT "Seven genes of the Enhancer of split complex of Drosophila RT melanogaster encode helix-loop-helix proteins."; RL Genetics 132:505-518(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTIONAL REPRESSOR OF GENES THAT REQUIRE A BHLH CC PROTEIN FOR THEIR TRANSCRIPTION. MAY SERVE AS A TRANSCRIPTIONAL CC REGULATOR OF THE ACHAETE-SCUTE COMPLEX (ASC) GENES. CONTRIBUTES TO CC THE NEURAL-EPIDERMAL LINEAGE DECISION DURING EARLY NEUROGENESIS. CC PART OF THE NOTCH SIGNALING PATHWAY. CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO) (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: IN IMAGINAL DISKS, EXPRESSED AS FOLLOWING: IN CC THE EYE DISK, WITHIN AND POSTERIOR TO THE MORPHOGENETIC FURROW; IN CC THE WING POUCH, IN THE PRESUMPTIVE INTERVEIN REGIONS AND WING CC MARGIN; IN THE LEG DISK, GENERAL EXPRESSION. CC -!- DOMAIN: HAS A PARTICULAR TYPE OF BASIC DOMAIN (PRESENCE OF A CC HELIX-INTERRUPTING PROLINE) THAT BINDS TO THE N-BOX (CACNAG), CC RATHER THAN THE CANONICAL E-BOX (CANNTG). CC -!- DOMAIN: THE C-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL REPRESSION CC DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96166; AAA28909.1; -. DR EMBL; X67047; CAA47432.1; -. DR EMBL; AE003754; AAF56546.1; -. DR PIR; C46177; C46177. DR FlyBase; FBgn0002733; HLHm-beta. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Neurogenesis; DNA-binding; Transcription regulation; KW Nuclear protein. FT DNA_BIND 14 26 BASIC DOMAIN. FT DOMAIN 27 71 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 192 195 WRPW MOTIF. FT CONFLICT 170 170 D -> G (IN REF. 2). FT CONFLICT 171 171 S -> T (IN REF. 1). FT CONFLICT 176 176 A -> R (IN REF. 1). SQ SEQUENCE 195 AA; 21494 MW; 8ECAAC7E55D081DC CRC64; MVLEMEMSKT YQYRKVMKPM LERKRRARIN KCLDELKDIM VECLTQEGEH ITRLEKADIL ELTVEHMKKL RAQKQLRLSS VTGGVSPSAD PKLSIAESFR AGYVHAANEV SKTLAAVPGV SVDLGTQLMS HLGHRLNYLQ VVVPSLPIGV PLQAPVEDQA MVTPPPSECD SLESGACSPA PSEASSTSGP MWRPW // ID ESMC_DROME STANDARD; PRT; 205 AA. AC Q01070; Q01898; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split mgamma protein (E(spl)mgamma) (HLH-mgamma) (Split DE locus enhancer protein mB). GN HLHM-GAMMA OR CG8333. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=92409590; PubMed=1528887; RA Delidakis C., Artavanis-Tsakonas S.; RT "The Enhancer of split [E(spl)] locus of Drosophila encodes seven RT independent helix-loop-helix proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8731-8735(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93051287; PubMed=1427040; RA Knust E., Schrons H., Grawe F., Campos-Ortega J.A.; RT "Seven genes of the Enhancer of split complex of Drosophila RT melanogaster encode helix-loop-helix proteins."; RL Genetics 132:505-518(1992). RN [3] RP SEQUENCE FROM N.A. RA Cooper M.T.D., Tyler D.M., Furriols M., Chalkiadaki A., Delidakis C., RA Bray S.; RT "Spatially restricted factors co-operate with Notch in the regulation RT of Enhancer of split genes."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTIONAL REPRESSOR OF GENES THAT REQUIRE A BHLH CC PROTEIN FOR THEIR TRANSCRIPTION. MAY SERVE AS A TRANSCRIPTIONAL CC REGULATOR OF THE ACHAETE-SCUTE COMPLEX (ASC) GENES. CONTRIBUTES TO CC THE NEURAL-EPIDERMAL LINEAGE DECISION DURING EARLY NEUROGENESIS. CC PART OF THE NOTCH SIGNALING PATHWAY. CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO) (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DOMAIN: HAS A PARTICULAR TYPE OF BASIC DOMAIN (PRESENCE OF A CC HELIX-INTERRUPTING PROLINE) THAT BINDS TO THE N-BOX (CACNAG), CC RATHER THAN THE CANONICAL E-BOX (CANNTG). CC -!- DOMAIN: THE C-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL REPRESSION CC DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96167; AAA28910.1; -. DR EMBL; X67049; CAA47434.1; -. DR EMBL; AJ276315; CAB77021.1; -. DR EMBL; AE003754; AAF56545.1; -. DR PIR; B46177; B46177. DR FlyBase; FBgn0002735; HLHm-gamma. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Neurogenesis; DNA-binding; Transcription regulation; KW Nuclear protein. FT DNA_BIND 16 28 BASIC DOMAIN. FT DOMAIN 29 73 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 202 205 WRPW MOTIF. FT CONFLICT 166 166 S -> T (IN REF. 2). SQ SEQUENCE 205 AA; 23135 MW; 4183A35D66DAB7E5 CRC64; MSSLQMSEMS KTYQYRKVMK PMLERKRRAR INKCLDELKD LMVATLESEG EHVTRLEKAD ILELTVTHLQ KMKQQRQHKR ASGDESLTPA EGFRSGYIHA VNEVSRSLSQ LPGMNVSLGT QLMTHLGQRL NQIQPAEKEV LPVTAPLSVH IANRDAYSVP ISPISSYAGS PNSNTSSTSH SLLTTIDVTK MEDDSEDEEN VWRPW // ID ESMD_DROME STANDARD; PRT; 173 AA. AC Q01071; Q01897; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Enhancer of split mdelta protein (E(spl)mdelta) (HLH-mdelta) (Split DE locus enhancer protein mC). GN HLHM-DELTA OR CG8328. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=92409590; PubMed=1528887; RA Delidakis C., Artavanis-Tsakonas S.; RT "The Enhancer of split [E(spl)] locus of Drosophila encodes seven RT independent helix-loop-helix proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8731-8735(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93051287; PubMed=1427040; RA Knust E., Schrons H., Grawe F., Campos-Ortega J.A.; RT "Seven genes of the Enhancer of split complex of Drosophila RT melanogaster encode helix-loop-helix proteins."; RL Genetics 132:505-518(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP WRPW MOTIF. RX MEDLINE=95094252; PubMed=8001118; RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., RA Brent R., Ish-Horowicz D.; RT "Groucho is required for Drosophila neurogenesis, segmentation, and RT sex determination and interacts directly with hairy-related bHLH RT proteins."; RL Cell 79:805-815(1994). CC -!- FUNCTION: TRANSCRIPTIONAL REPRESSOR OF GENES THAT REQUIRE A BHLH CC PROTEIN FOR THEIR TRANSCRIPTION. MAY SERVE AS A TRANSCRIPTIONAL CC REGULATOR OF THE ACHAETE-SCUTE COMPLEX (ASC) GENES. CONTRIBUTES TO CC THE NEURAL-EPIDERMAL LINEAGE DECISION DURING EARLY NEUROGENESIS. CC PART OF THE NOTCH SIGNALING PATHWAY. CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO) (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DOMAIN: HAS A PARTICULAR TYPE OF BASIC DOMAIN (PRESENCE OF A CC HELIX-INTERRUPTING PROLINE) THAT BINDS TO THE N-BOX (CACNAG), CC RATHER THAN THE CANONICAL E-BOX (CANNTG). CC -!- DOMAIN: THE C-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL REPRESSION CC DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96168; AAA28911.1; -. DR EMBL; X67048; CAA47433.1; -. DR EMBL; AE003754; AAF56544.1; -. DR PIR; A46177; A46177. DR FlyBase; FBgn0002734; HLHm-delta. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Neurogenesis; DNA-binding; Transcription regulation; KW Nuclear protein. FT DNA_BIND 16 28 BASIC DOMAIN. FT DOMAIN 29 73 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 170 173 WRPW MOTIF. FT DOMAIN 72 75 POLY-GLN. FT CONFLICT 82 82 S -> W (IN REF. 2). SQ SEQUENCE 173 AA; 20195 MW; F44DA6100CE0874F CRC64; MAVQGQRFMT KTQHYRKVTK PLLERKRRAR MNLYLDELKD LIVDTMDAQG EQVSKLEKAD ILELTVNYLK AQQQQRVANP QSPPPDQVNL DKFRAGYTQA AYEVSHIFST VPGLDLKFGT HLMKQLGHQL KDMKQEEEII DMAEEPVNLA DQKRSKSPRE EDIHHGEEVW RPW // ID EST6_DROME STANDARD; PRT; 544 AA. AC P08171; P91646; P91647; P91648; P91649; P91650; P92173; P92195; AC P92200; Q8SWT4; Q9U797; Q9U798; Q9U799; Q9U7A0; Q9V3U8; Q9XTN6; DT 01-AUG-1988 (Rel. 08, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Esterase 6 precursor (EC 3.1.1.1) (Est-6) (Carboxylic-ester DE hydrolase 6) (Carboxylesterase-6). GN EST-6 OR EST6 OR CG6917. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90136038; PubMed=2105433; RA Collet C., Nielsen K.M., Russell R.J., Karl M., Oakeshott J.G., RA Richmond R.C.; RT "Molecular analysis of duplicated esterase genes in Drosophila RT melanogaster."; RL Mol. Biol. Evol. 7:9-28(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=89145255; PubMed=2493155; RA Cooke P.H., Oakeshott J.G.; RT "Amino acid polymorphisms for esterase-6 in Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1426-1430(1989). RN [3] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=87204136; PubMed=3106966; RA Oakeshott J.G., Collet C., Phillis R.W., Nielsen K.M., Russell R.J., RA Chambers G.K., Ross V., Richmond R.C.; RT "Molecular cloning and characterization of esterase-6, a serine RT hydrolase of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 84:3359-3363(1987). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=94F, 174F, 357F, 377F, 517S, 510S, 521S, and 581F; RX MEDLINE=20014926; PubMed=10545464; RA Balakirev E.S., Balakirev E.I., Rodriguez-Trelles F., Ayala F.J.; RT "Molecular evolution of two linked genes, Est-6 and Sod, in Drosophila RT melanogaster."; RL Genetics 153:1357-1369(1999). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=F-96S, F-274F, F-517F, F-531F, F-611F, F-775F, F-1461S, S-5F, RC S-26F, S-114S, S-255S, S-438S, S-483F, S-498F, S-501S, S-521F, S-549S, RC S-565F, S-968F, S-1224F, S-2588S, and US-255F; RX MEDLINE=22030465; PubMed=12034506; RA Balakirev E.S., Balakirev E.I., Ayala F.J.; RT "Molecular evolution of the Est-6 gene in Drosophila melanogaster: RT contrasting patterns of DNA variability in adjacent functional RT regions."; RL Gene 288:167-177(2002). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [7] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [8] RP SEQUENCE OF 1-538 FROM N.A. RC STRAIN=DPF-62, MA-10.2, DPF-2, VC-805, VC-815, MA-4.2, MA-4.4, RC DPF-30, DPF-13, 709.6, DPF-46, DPF-77, 178.7, DPF-82.1, and EM-10; RX MEDLINE=97132593; PubMed=8978045; RA Hasson E., Eanes W.F.; RT "Contrasting histories of three gene regions associated with RT In(3L)Payne of Drosophila melanogaster."; RL Genetics 144:1565-1575(1996). CC -!- FUNCTION: TRANSFERRED FROM THE EJACULATORY BULBS OF MALES TO CC THE FEMALE GENITALS UPON COPULATION, PLAYS AN IMPORTANT ROLE CC IN THE REPRODUCTIVE BIOLOGY. CC -!- CATALYTIC ACTIVITY: A CARBOXYLIC ESTER + H(2)O = AN ALCOHOL + A CC CARBOXYLIC ANION. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: SPECIFICALLY EXPRESSED IN THE EJACULATORY CC BULBS OF MALE. CC -!- SIMILARITY: BELONGS TO THE TYPE-B CARBOXYLESTERASE/LIPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33780; AAA28519.1; -. DR EMBL; J04167; AAA28518.1; -. DR EMBL; M15961; AAA28517.1; -. DR EMBL; AF147095; AAD39958.1; -. DR EMBL; AF147096; AAD39959.1; -. DR EMBL; AF147097; AAD39960.1; -. DR EMBL; AF147098; AAD39961.1; -. DR EMBL; AF147099; AAD39962.1; -. DR EMBL; AF147100; AAD39963.1; -. DR EMBL; AF147101; AAD39964.1; -. DR EMBL; AF147102; AAD39965.1; -. DR EMBL; AF217624; AAF61043.1; -. DR EMBL; AF217625; AAF61044.1; -. DR EMBL; AF217626; AAF61045.1; -. DR EMBL; AF217627; AAF61046.1; -. DR EMBL; AF217628; AAF61047.1; -. DR EMBL; AF217629; AAF61048.1; -. DR EMBL; AF217630; AAF61049.1; -. DR EMBL; AF217631; AAF61050.1; -. DR EMBL; AF217632; AAF61051.1; -. DR EMBL; AF217633; AAF61052.1; -. DR EMBL; AF217634; AAF61053.1; -. DR EMBL; AF217635; AAF61054.1; -. DR EMBL; AF217636; AAF61055.1; -. DR EMBL; AF217637; AAF61056.1; -. DR EMBL; AF217638; AAF61057.1; -. DR EMBL; AF217639; AAF61058.1; -. DR EMBL; AF217640; AAF61059.1; -. DR EMBL; AF217641; AAF61060.1; -. DR EMBL; AF217642; AAF61061.1; -. DR EMBL; AF217643; AAF61062.1; -. DR EMBL; AF217644; AAF61063.1; -. DR EMBL; AF217645; AAF61064.1; -. DR EMBL; AE003542; AAF49946.1; -. DR EMBL; AY095091; AAM11419.1; ALT_SEQ. DR EMBL; U57474; AAB46692.1; -. DR EMBL; U57475; AAB46693.1; -. DR EMBL; U57476; AAB46694.1; -. DR EMBL; U57477; AAB46695.1; -. DR EMBL; U57478; AAB46696.1; -. DR EMBL; U57479; AAB46697.1; -. DR EMBL; U57480; AAB46698.1; -. DR EMBL; U57481; AAB46699.1; -. DR EMBL; U57482; AAB46700.1; -. DR EMBL; U57483; AAB46701.1; -. DR EMBL; U57484; AAB46702.1; -. DR EMBL; U57485; AAB46703.1; -. DR EMBL; U57486; AAB46704.1; -. DR EMBL; U57487; AAB46705.1; -. DR EMBL; U57488; AAB46706.1; -. DR PIR; A34089; A34089. DR FlyBase; FBgn0000592; Est-6. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00135; COesterase; 1. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. KW Hydrolase; Serine esterase; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 21 FT CHAIN 22 544 ESTERASE 6. FT ACT_SITE 209 209 BY SIMILARITY. FT ACT_SITE 466 466 BY SIMILARITY. FT DISULFID 86 105 BY SIMILARITY. FT DISULFID 261 273 BY SIMILARITY. FT DISULFID 514 535 POTENTIAL. FT CARBOHYD 42 42 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 420 420 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 456 456 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 506 506 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 10 10 I -> T (IN STRAINS MA-4.4, DPF-30, DPF- FT 13, 178.7, DPF-82.1, EM-10, F-1461S, F- FT 274F, F-517F, 357F AND 517S). FT VARIANT 24 24 T -> I (IN STRAINS MA-4.4, DPF-30, DPF- FT 13, 178.7, DPF-82.1, EM-10, F-1461S, F- FT 274F, F-517F, F-775F, 377F, 357F AND FT 517S). FT VARIANT 58 58 T -> I (IN STRAINS VC-805, MA-4.2, DPF- FT 30, DPF-13, 178.7, DPF-82.1, EM-10, F- FT 1461S, F-274F, 357F AND 517S). FT VARIANT 120 120 S -> T (IN STRAINS DPF-2 AND 521S). FT VARIANT 258 258 N -> D (IN STRAINS MA-4.2, DPF-30, DPF- FT 13, 709.6, DPF-46, DPF-77, 178.7, DPF- FT 82.1, EM-10, F-96S, F-1461S, F-274F, F- FT 517F, F-531F, F-611F, F-775F, 357F AND FT 517S). FT VARIANT 268 268 T -> A (IN STRAINS VC-815, MA-4.2, DPF- FT 30, DPF-13, 709.6, DPF-46, DPF-77, 178.7, FT DPF-82.1, EM-10, F-96S, S-114S, S- 549S, FT F-1461S, S-2588S, F-274F, F-517F, F-531F, FT F-611F, F-775F, 174F, 357F AND 517S). FT VARIANT 276 276 S -> P (IN STRAIN VC-805). FT VARIANT 356 356 I -> T (IN STRAIN F-775F). FT VARIANT 363 363 E -> D (IN STRAIN F-775F). FT VARIANT 371 371 Y -> H (IN STRAIN F-775F). FT VARIANT 397 397 G -> R (IN STRAIN). FT VARIANT 409 409 L -> V (IN STRAINS VC-805, DPF-30, DPF- FT 13, F-96S, S-114S, S-549S, F-1461S, S- FT 2588S, F-274F, F-517F, 357F AND 517S). FT VARIANT 492 492 R -> K (IN STRAINS MA-4.2, F-531F, F- FT 611F, 92F AND 174F). FT VARIANT 508 508 S -> A (IN STRAINS VC-805, MA-4.2, DPF- FT 30, DPF-13, F-96S, F-1461S, F-517F, 357F FT AND 517S). FT CONFLICT 519 519 N -> S (IN REF. 2). FT CONFLICT 534 544 GCQNRQHVEFP -> AARIGSMWNFRKLHE (IN FT REF. 3). SQ SEQUENCE 544 AA; 61125 MW; 5D99B80DF588F268 CRC64; MNYVGLGLII VLSCLWLGSN ASDTDDPLLV QLPQGKLRGR DNGSYYSYES IPYAEPPTGD LRFEAPEPYK QKWSDIFDAT KTPVACLQWD QFTPGANKLV GEEDCLTVSV YKPKNSKRNS FPVVAHIHGG AFMFGAAWQN GHENVMREGK FILVKISYRL GPLGFVSTGD RDLPGNYGLK DQRLALKWIK QNIASFGGEP QNVLLVGHSA GGASVHLQML REDFGQLARA AFSFSGNALD PWVIQKGARG RAFELGRNVG CESAEDSTSL KKCLKSKPAS ELVTAVRKFL IFSYVPFAPF SPVLEPSDAP DAIITQDPRD VIKSGKFGQV PWAVSYVTED GGYNAALLLK ERKSGIVIDD LNERWLELAP YLLFYRDTKT KKDMDDYSRK IKQEYIGNQR FDIESYSELQ RLFTDILFKN STQESLDLHR KYGKSPAYAY VYDNPAEKGI AQVLANRTDY DFGTVHGDDY FLIFENFVRD VEMRPDEQII SRNFINMLAD FASSDNGSLK YGECDFKDNV GSEKFQLLAI YIDGCQNRQH VEFP // ID ESTP_DROME STANDARD; PRT; 544 AA. AC P18167; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Esterase P precursor (EC 3.1.1.1) (Est-P) (Carboxylic-ester DE hydrolase P) (Carboxylesterase-P). GN EST-P OR ESTP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90136038; PubMed=2105433; RA Collet C., Nielsen K.M., Russell R.J., Karl M., Oakeshott J.G., RA Richmond R.C.; RT "Molecular analysis of duplicated esterase genes in Drosophila RT melanogaster."; RL Mol. Biol. Evol. 7:9-28(1990). CC -!- CATALYTIC ACTIVITY: A CARBOXYLIC ESTER + H(2)O = AN ALCOHOL + A CC CARBOXYLIC ANION. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- DEVELOPMENTAL STAGE: MAINLY IN LATE LARVAE. CC -!- SIMILARITY: BELONGS TO THE TYPE-B CARBOXYLESTERASE/LIPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33780; AAA28520.1; -. DR PIR; B34089; B34089. DR HSSP; P37967; 1QE3. DR FlyBase; FBgn0000594; Est-P. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00135; COesterase; 1. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. KW Hydrolase; Serine esterase; Glycoprotein; Signal. FT SIGNAL 1 19 FT CHAIN 20 544 ESTERASE P. FT ACT_SITE 206 206 BY SIMILARITY. FT ACT_SITE 466 466 BY SIMILARITY. FT DISULFID 83 102 BY SIMILARITY. FT DISULFID 258 270 BY SIMILARITY. FT DISULFID 514 535 POTENTIAL. FT CARBOHYD 75 75 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 114 114 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 262 262 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 456 456 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 544 AA; 61230 MW; 6B60C5D9468CA43D CRC64; MSIFKRLLCL TLLWIAALES EADPLIVEIT NGKIRGKDNG LYYSYESIPY AEHPTGALRF EAPQPYSHHW TDVFNATQSP VECMQWNQFI NENNKLMGDE DCLTVSIYKP KKPNRSSFPV VVLLHGGAFM FGSGSIYGHD SIMREGTLLV VKISYRLGPL GFASTGDRHL PGNYGLKDQR LALQWIKKNI AHFGGMPDNI VLIGHSAGGA SAHLQLLHED FKHLAKGAIS VSGNALDPWV IQQGGRRRAF ELGRIVGCGH TNVSAELKDC LKSKPASDIV SAVRSFLVFS YVPFSAFGPV VEPSDAPDAF LTEDPRAVIK SGKFAQVPWA VTYTTEDGGY NAAQLLERNK LTGESWIDLL NDRWFDWAPY LLFYRDAKKT IKDMDDLSFD LRQQYLADRR FSVESYWNVQ RMFTDVLFKN SVPSAIDLHR KYGKSPVYSF VYDNPTDSGV GQLLSNRTDV HFGTVHGDDF FLIFNTAAYR IGIRPDEEVI SKKFIGMLED FALNDKGTLT FGECNFQNNV NSKEYQVLRI SRNACKNEEY ARFP // ID ETS3_DROME STANDARD; PRT; 490 AA. AC P29774; Q95T62; Q95TB2; Q9VRU3; Q9VRU4; Q9VRU5; DT 01-APR-1993 (Rel. 25, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-binding protein D-ETS-3. GN ETS65A OR ETS3 OR CG7018/CG6882/CG13294. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 405-490 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Larva; RX MEDLINE=92249640; PubMed=1577186; RA Chen T., Bunting M., Karim F.D., Thummel C.S.; RT "Isolation and characterization of five Drosophila genes that encode RT an ets-related DNA binding domain."; RL Dev. Biol. 151:176-191(1992). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=P29774-1; Sequence=Displayed; CC Name=B; CC IsoId=P29774-2; Sequence=VSP_001470, VSP_001471; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: EMBRYONIC VENTRAL NERVOUS SYSTEM, HIGHER IN CC THE THORACIC THAN ABDOMINAL SEGMENTS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003564; AAF50697.2; -. DR EMBL; AE003564; AAF50696.2; -. DR EMBL; AY060316; AAL25355.1; -. DR EMBL; AY060250; AAL25289.1; ALT_SEQ. DR EMBL; M88473; AAA28450.2; -. DR PIR; S28820; S28820. DR HSSP; Q01543; 1FLI. DR FlyBase; FBgn0005658; Ets65A. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0003700; F:transcription factor activity; ISS. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR Pfam; PF00178; Ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW DNA-binding; Nuclear protein; Alternative splicing. FT DOMAIN 188 280 SER-RICH. FT DNA_BIND 317 397 ETS-DOMAIN. FT VARSPLIC 1 233 Missing (in isoform B). FT /FTId=VSP_001470. FT VARSPLIC 234 260 ISGSKSSNTSGTGGGASASGGGGSALY -> MLDIKSSADY FT LSRSTGSFSNFSMLFAD (in isoform B). FT /FTId=VSP_001471. SQ SEQUENCE 490 AA; 52055 MW; B5BB281B13DDEA97 CRC64; MYENSCSYQT ALDLKRVSPP TLAQVKTEEC LALGQCSPEW TSYRFHQSTF EQLKQSVEKA KAALQDRSSF FGASSAFSDI YSSQRLTDSL DTLPVQSGNG GGNCLGLPHN PNVGVGVAGV LNYNAVSSST AGVLSSSGNG VQRHRLDTLQ PPSGCSPAVT QHGVITSSAG QVTSGTLDAV SAAPALPSLT ASSSSHVEHK VRADKSTLDC ATTSSHAAAP SSSSSASDHQ QGRISGSKSS NTSGTGGGAS ASGGGGSALY SSYKSSWGSH SSTQSQGYSS NALGIKHDPH SQLRQPDPYQ MFGPTSSRLA SSGSGQIQLW QFLLELLSDS NNASCITWEG TNGEFKLTDP DEVARRWGER KSKPNMNYDK LSRALRYYYD KNIMTKVHGK RYAYKFDFQG LAAATQPAAS DPTYKYQSDL FMTPYHHSAK LSSFMSPHHG MTSSSASIFP SAASWGNWGS PATNLYQPHS MSHVTPSHVA PHLSSYPHYA // ID ETS4_DROME STANDARD; PRT; 504 AA. AC P29775; Q9VB00; DT 01-APR-1993 (Rel. 25, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-binding protein D-ETS-4. GN ETS98B OR ETS-4 OR CG5583. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 391-504 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Larva; RX MEDLINE=92249640; PubMed=1577186; RA Chen T., Bunting M., Karim F.D., Thummel C.S.; RT "Isolation and characterization of five Drosophila genes that encode RT an ets-related DNA binding domain."; RL Dev. Biol. 151:176-191(1992). CC -!- FUNCTION: MAY HAVE A ROLE IN GERMLINE DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: TRANSIENT HIGH EXPRESSION IN POLE CELLS DURING CC EMBRYONIC STAGES 8-11. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT WITH LOWER CC LEVELS DURING LARVAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003762; AAF56746.1; -. DR EMBL; M88474; AAA28451.1; -. DR PIR; S28821; S28821. DR HSSP; P28324; 1BC8. DR FlyBase; FBgn0005659; Ets98B. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR InterPro; IPR003118; SAM_PNT. DR Pfam; PF00178; Ets; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SMART; SM00251; SAM_PNT; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW DNA-binding; Nuclear protein. FT DNA_BIND 416 499 ETS-DOMAIN. SQ SEQUENCE 504 AA; 56038 MW; 89D821ACF7C1E7D7 CRC64; MPHSPQLKPH QFQAHTPTDQ YSSYADNFDL SLLPQESASI PTTVFQYNAP QIKVECAWDS QPIQQQQQPT APYTNPSSHQ LIPPPAYPHS AYPSPQSSPL QSEFAAYGLG RFGGSYDSLN SPSPSLEAVS IKQELHILPP SPPESNCETP SPRSSCGESI KAEPLDADIE SLIDLNSLLQ QQSLQSPQNL QDTKPDHQLL RECLEDTSFQ KRHNLKPLAL ESFIGGLAEV RGDFEPVISL ALEHAKREAD AICAELQISQ DPNGWSPAQV HAWLRSTLAQ FRLPPVADLE LHFCENGAAL ALLSEEEFVR RLPESGSTLH AQLEIWKMAY ADQPAHQQHS QQSASTDHWP ASYAMPHLDL DYNEDSEDDD DMEADAQVAP LNGSTTSPPA TNASNGGTAT VKRPNGGRTG GGGSHIHLWQ FLKELLASPQ VNGTAIRWID RSKGIFKIED SVRVAKLWGR RKNRPAMNYD KLSRSIRQYY KKGIMKKTER SQRLVYQFCH PYSQ // ID ETS6_DROME STANDARD; PRT; 475 AA. AC P29776; Q9VPQ9; DT 01-APR-1993 (Rel. 25, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-binding protein D-ETS-6. GN ETS21C OR ETS-6 OR CG2914. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 235-352 FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Canton-S; TISSUE=Larva; RX MEDLINE=92249640; PubMed=1577186; RA Chen T., Bunting M., Karim F.D., Thummel C.S.; RT "Isolation and characterization of five Drosophila genes that encode RT an ets-related DNA binding domain."; RL Dev. Biol. 151:176-191(1992). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EMBRYONIC VENTRAL NERVOUS SYSTEM AND 1 PAIR OF CC NEURONS IN EACH THORACIC SEGMENT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 242. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003589; AAF51484.1; -. DR EMBL; M88475; AAA28452.1; ALT_FRAME. DR HSSP; Q01543; 1FLI. DR FlyBase; FBgn0005660; Ets21C. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR InterPro; IPR003118; SAM_PNT. DR Pfam; PF00178; Ets; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW DNA-binding; Nuclear protein. FT DNA_BIND 255 335 ETS-DOMAIN. SQ SEQUENCE 475 AA; 51802 MW; 0D382C41C03B1502 CRC64; MAILQNSRQS HKQLPIISQT IRSAWCQQRP INAMHQDVRQ KSIGSGNETK LEAKETEVPT NRRRRRRRCS SSSTSDSSAS SYSSTDSDSG SSTSSSSIRS QLPALNLPVP LPLATPTPPA VSSPHQAPSP RRNSSDSNRS VSPVEVPVDP HAWTPEDIAS WVRWATRKFK LDPEPDIDRF PKDAQELCDL SRADFWVCAG SRRGGMLLAQ HFAISLYHAT GRETSPMLND DEPNPYQLLN AASHRLVAQG SGGQIQLWQF LLELLADSSN ANAISWEGQS GEFRLIDPDE VARRWGERKA KPNMNYDKLS RALRYYYDKN IMTKVHGKRY AYKFDFHGLM AACQAQAQGG DPASSMLGSY NHHAGGAMQL GRHPPPLHHH PQHSHPHHQL GQPHFLHPHH SSPASNSSSL GFPSSSTASS QASPGQAPAS SSASTSNFTA PFQGGTAGVD PARTSTSSAG NYDQGPVTPT TNAFN // ID EWG_DROME STANDARD; PRT; 733 AA. AC Q24312; Q8SXJ1; Q9NF76; Q9W5G8; Q9W5G9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-binding protein Ewg (Erect wing protein). GN EWG OR EG:BACR37P7.7 OR CG3114. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=93268313; PubMed=8388540; RA DeSimone S.M., White K.; RT "The Drosophila erect wing gene, which is important for both neuronal RT and muscle development, encodes a protein which is similar to the sea RT urchin P3A2 DNA binding protein."; RL Mol. Cell. Biol. 13:3641-3649(1993). RN [2] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RC TISSUE=Head; RX MEDLINE=99262971; PubMed=10330140; RA Koushika S.P., Soller M., DeSimone S.M., Daub D.M., White K.; RT "Differential and inefficient splicing of a broadly expressed RT Drosophila erect wing transcript results in tissue-specific enrichment RT of the vital EWG protein isoform."; RL Mol. Cell. Biol. 19:3998-4007(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM 3). RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [6] RP SEQUENCE FROM N.A. (ISOFORM 4). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY FUNCTION AS A POSITIVE REGULATOR OF TRANSCRIPTION IN CC DEVELOPING AND DIFFERENTIATED NEURONS, REGULATING COMMON ASPECTS CC OF NEURONAL DIFFERENTIATION AND MAINTENANCE. REQUIREMENT IN THE CC CNS MAY BE HIGHER THAN IN THE PERIPHERAL SYSTEM. VITAL FOR CC DEVELOPMENT OF THE INDIRECT FLIGHT MUSCLES. CC -!- SUBUNIT: HOMODIMER. BINDS DNA AS A DIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR; NOT IN NUCLEOLUS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist. Experimental CC confirmation may be lacking for some isoforms; CC Name=1; CC IsoId=Q24312-1; Sequence=Displayed; CC Name=2; CC IsoId=Q24312-2; Sequence=VSP_003602; CC Name=3; CC IsoId=Q24312-3; Sequence=VSP_003601; CC Name=4; CC IsoId=Q24312-4; Sequence=VSP_003600, VSP_003603; CC -!- TISSUE SPECIFICITY: ISOFORM 1 IS HIGHLY EXPRESSED IN POSSIBLY ALL CC EMBRYONIC NEURONS AND IS ENRICHED IN ADULT HEADS. OTHER ISOFORMS CC SHOW SIMILAR EXPRESSION AT A MUCH LOWER LEVEL. TRANSIENT CC EXPRESSION IN MIGRATING MYOBLASTS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, BEGINNING CC AT EMBRYONIC STAGE 12 WHEN LEVELS STEADILY INCREASE AND THEN DROP CC DRAMATICALLY AT THIRD-INSTAR LARVAE. LEVELS INCREASE IN 24 HOUR CC PUPAE AND REMAIN UNTIL ADULTHOOD. CC -!- SIMILARITY: BELONGS TO THE NRF1 / EWG FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L11345; AAA28478.1; -. DR EMBL; AF135590; AAD34460.1; -. DR EMBL; AE003417; AAF45491.3; -. DR EMBL; AE003417; AAF45492.3; -. DR EMBL; AL050231; CAB43325.1; ALT_SEQ. DR EMBL; AY089609; AAL90347.1; -. DR FlyBase; FBgn0005427; ewg. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0003704; F:specific RNA polymerase II transcription fa...; ISS. DR GO; GO:0007417; P:central nervous system development; IMP. DR GO; GO:0007560; P:imaginal disc morphogenesis; IMP. DR GO; GO:0007517; P:muscle development; IMP. KW Transcription regulation; DNA-binding; Activator; Nuclear protein; KW Phosphorylation; Alternative splicing. FT DOMAIN 69 136 DIMERIZATION (BY SIMILARITY). FT DOMAIN 86 124 ASP/GLU-RICH (ACIDIC). FT DOMAIN 126 144 ALA-RICH. FT DOMAIN 146 174 NUCLEAR LOCALIZATION SIGNAL FT (BY SIMILARITY). FT DOMAIN 167 379 DNA-BINDING (BY SIMILARITY). FT DOMAIN 375 663 REQUIRED FOR TRANSCRIPTIONAL ACTIVATION FT (BY SIMILARITY). FT DOMAIN 442 528 ALA/GLN-RICH. FT MOD_RES 97 97 PHOSPHORYLATION (BY CK2) (BY SIMILARITY). FT MOD_RES 110 110 PHOSPHORYLATION (BY CK2) (BY SIMILARITY). FT VARSPLIC 1 86 Missing (in isoform 4). FT /FTId=VSP_003600. FT VARSPLIC 669 669 V -> VDTSINRSTSTAASSSSSLGNGGVQCYSLISAGSSV FT LSRRSGGVIGHQVTPGERYYLATTTSSSLGLNNNNNCTLAN FT NNNSVKMPIVLATPSIPQVANKRSTGKRSTGV (in FT isoform 3). FT /FTId=VSP_003601. FT VARSPLIC 669 669 V -> VDTSINRSTSTAASSSSSLGNGGVQCYSLISAGSSV FT LSRRSGGVIGHQVTPGERYYLATTTSSSLGLNNNNNCTLAN FT NNNSVKMPIVLATPSIPQVANKRSTGKRSTGVSGGDDVMVQ FT KRGRPNSSSRSKSQLNANENAHSSGTSSSIRCVDSASLTNV FT (in isoform 2). FT /FTId=VSP_003602. FT VARSPLIC 670 733 ENGDQLETITMSPGMHQMMIQGGPGQEPQLVQVVSLKDATL FT LSKAMEAINSGNVKSEDTIIMEQ -> DTSINRSTSTAASS FT SSSLGNGGVQCYSLISAGSSVLSRRSGGVIGHQVTPGERYY FT LATTTSSSLGLNNNNNCTLANNNNSVKMPIVLATPSIPQVA FT NKRSTGKRSTGASGGDDVMVQKRGRPNSSSRSKSQLNANEN FT AHSSGTSSSIRCVDSASLTNVQLQLPAIKLEHLG (in FT isoform 4). FT /FTId=VSP_003603. FT CONFLICT 172 173 KL -> NV (IN REF. 1). SQ SEQUENCE 733 AA; 77763 MW; A1CA6CD7AB3177A3 CRC64; MATTSYRLVV APAGSQRSST GNVVVTTTSS GSHSSNGANG GTGGTSAGSS TLGSGLNVTT ITATSGGQLQ SAGNTSQSNG TTYKIEMLEE DIQSLGSDDD DEDLISSDGS LYEGDLGSMP VNDDVAHQLA AAGPVGVAAA AAIASSKKRK RPHCFETNPS VRKRQQNRLL RKLRAIIYEF TGRVGKQAVV LVATPGKPNT SYKVFGAKPL EDVLRNLKNI VMDELDNALA QQAPPPPQDD PSLFELPGLV IDGIPTPVEK MTQAQLRAFI PLMLKYSTGR GKPGWGREST RPPWWPKELP WANVRMDARS EDDKQKISWT HALRKIVINC YKYHGREDLL PTFADDEDKV NALISQSGDE DEDMELSNPP TIHTVTTMTP PTGNSNQPQQ VNVVKINSAG TVITTHTAQS NTPAPTIIQS TNNQHVTTTA TLPASTKIEI CQAPAQNQQH HQHHQTHLPN AVHIQPVAGG QPQTIQLTTA SGTATATAVQ TTAAAVSAAQ AHAHSQSQAH SQSSANQTVT AQQIANAQVC IEPITLSDVD YTTQTVLSQN ADGTVSLIQV DPNNPIITLP DGTTAQVQGV ATLHQGEGGA TIQTVQSLTD VNGHENMTVD LTETQDGQIY ITTEDGQGYP VSVSNVISVP VSMYQSVMAN VQQIQTNSDG TVCLAPMQVE NGDQLETITM SPGMHQMMIQ GGPGQEPQLV QVVSLKDATL LSKAMEAINS GNVKSEDTII MEQ // ID EX70_DROME STANDARD; PRT; 693 AA. AC Q9VSJ8; Q8T0E9; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 70 kDa exocyst complex protein. GN EXO70 OR CG7127. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, AND SUBUNIT. RX MEDLINE=20370889; PubMed=10908590; RA Littleton J.T.; RT "A genomic analysis of membrane trafficking and neurotransmitter RT release in Drosophila."; RL J. Cell Biol. 150:F77-F82(2000). CC -!- FUNCTION: REQUIRED FOR EXOCYTOSIS. THOUGHT TO FUNCTION IN CC INTRACELLULAR VESICLE TARGETING AND DOCKING BEFORE SNARE COMPLEX CC FORMATION. CC -!- SUBUNIT: SEC5, SEC6, SEC8, SEC10, SEC15, EXO70, EXO84 AND SEM1 CC ARE COMPONENTS OF THE EXOCYST COMPLEX. CC -!- SIMILARITY: BELONGS TO THE EXO70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003555; AAF50421.2; -. DR EMBL; AY069366; AAL39511.1; -. DR FlyBase; FBgn0035892; exo70. DR GO; GO:0000145; C:exocyst; ISS. DR GO; GO:0005326; F:neurotransmitter transporter activity; ISS. DR GO; GO:0006887; P:exocytosis; ISS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016081; P:synaptic vesicle docking; ISS. DR GO; GO:0016080; P:synaptic vesicle targeting; ISS. DR InterPro; IPR004140; Exo70. DR Pfam; PF03081; Exo70; 1. KW Exocytosis; Transport; Protein transport. FT CONFLICT 543 543 L -> F (IN REF. 2). SQ SEQUENCE 693 AA; 80026 MW; 53FA91C081A39851 CRC64; MNNLDSSLQA HNKLEKEATN LALLKDRVDK YHDLSTQMSS ILTIFEKRLG NLEQTILPVY QETEQLQKRQ QNLEATLNCL ESVLSHYDVS QEVCQLIHQG PVEGNISVFL DALAKLRDAN DYFRHNNSQS VELENVTSLF NTGCEGLSQH YSMLLKKHSA PLKPVELLDL IYIEDDSSDE YTSFRQLSQT TREELYTISH WLEQNLREYT NIYATERGEV VLRSLQLLKD HQKSNSWGHE ALRPRHSGRQ TEPKKTTSAR LQQIFEKKAN KLYLRATQTI EQSTGFSIKK ASSHSDHLTS EDLMDGDQEL DKYLVMLLGL QRLLNWERAI MIDIIPQSKH NEVFATLAYN AIDLVVKDAE AITQRILRCI SRKEWTSALG IFSALKRVIL LQPDIDRTYD PAQREQLKKV LKKLQHTGAK ALEHFLDVVK GESSTNIVGQ SNVPKDATVH ELTSNTIWFI EHLYDHFDVI GSILAQDVLY STQLDTILMK KALPVEERNK ALLAIYIKKA LAELNLSIMN KCEQYNDQAT KHLFRLNNIH YILKSLQRSN LIDLVTLAEP ECEHSYMEMI RELKASYQKT WSKMLVGIYS LDELPKPVAG KVKDKDRSVL KERFSNFNKD FEEACKIQRG ISIPDVILRE GIKRDNVEHI LPIYNRFYEI YSGVHFSKNP DKYVKYRQHE INAMLSKLFD DSA // ID EXD_DROME STANDARD; PRT; 376 AA. AC P40427; Q9V3S2; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein extradenticle. GN EXD OR DBPX OR CG8933. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94006521; PubMed=8104703; RA Rauskolb C., Peifer M., Wieschaus E.; RT "Extradenticle, a regulator of homeotic gene activity, is a homolog RT of the homeobox-containing human proto-oncogene pbx1."; RL Cell 74:1101-1112(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 1-365 FROM N.A. RC STRAIN=Y(2)W(BF); RX MEDLINE=93298652; PubMed=8100142; RA Flegel W.A., Singson A.W., Margolis J.S., Bang A.G., RA Posakony J.W., Murre C.; RT "Dpbx, a new homeobox gene closely related to the human RT proto-oncogene pbx1 molecular structure and developmental RT expression."; RL Mech. Dev. 41:155-161(1993). RN [5] RP CHARACTERIZATION. RX MEDLINE=94341269; PubMed=7914871; RA Rauskolb C., Wieschaus E.; RT "Coordinate regulation of downstream genes by extradenticle and the RT homeotic selector proteins."; RL EMBO J. 13:3561-3569(1994). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 238-300 IN COMPLEX WITH UBX. RX MEDLINE=99165220; PubMed=10067897; RA Passner J.M., Ryoo H.-D., Shen L., Mann R.S., Aggarwal A.K.; RT "Structure of a DNA-bound Ultrabithorax-Extradenticle homeodomain RT complex."; RL Nature 397:714-719(1999). CC -!- FUNCTION: TRANSCRIPTION FACTOR WHICH ACTS WITH THE SELECTOR CC HOMEODOMAIN PROTEINS ALTERING THE REGULATION OF DOWNSTREAM TARGET CC GENES SUCH AS WINGLESS, TEASHIRT AND DECAPENTAPLEGIC. THUS CC AFFECTING SEGMENTAL IDENTITY. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: PRIOR TO FULL GERMBAND RETRACTION IT IS CC UBIQUITOUSLY PRESENT, AFTER GERMBAND RETRACTION, MOSTLY PRESENT IN CC THE ANTERIOR PORTION OF THE VENTRAL NERVE CORD. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT ALL STAGES OF DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE TALE/PBX HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U33747; AAC46903.1; -. DR EMBL; L19295; AAC37182.1; -. DR EMBL; AE003500; AAF48556.1; -. DR EMBL; AY061065; AAL28613.1; -. DR EMBL; Z18864; CAA79313.1; -. DR PIR; A48840; A48840. DR PDB; 1B8I; 12-APR-99. DR TRANSFAC; T01482; -. DR FlyBase; FBgn0000611; exd. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007420; P:brain development; IMP. DR GO; GO:0007438; P:oenocyte development; IMP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR005542; PBX. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF03792; PBX; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; DNA-binding; Homeobox; Nuclear protein; KW Developmental protein; 3D-structure. FT DOMAIN 127 135 POLY-ALA. FT DNA_BIND 238 300 HOMEOBOX (TALE-TYPE). FT CONFLICT 98 98 E -> G (IN REF. 4). FT CONFLICT 344 344 M -> K (IN REF. 4). FT CONFLICT 363 363 M -> T (IN REF. 4). FT HELIX 247 259 FT TURN 268 269 FT HELIX 270 278 FT HELIX 282 297 FT TURN 298 298 SQ SEQUENCE 376 AA; 41692 MW; 79E3DC8F1F6B711F CRC64; MEDPNRMLAH TGGMMAPQGY GLSGQDDGQN AGSENEVRKQ KDIGEILQQI MSISEQSLDE AQARKHTLNC HRMKPALFSV LCEIKEKTVL SIRNTQEEEP PDPQLMRLDN MLIAEGVAGP EKGGGGAAAA SAAAASQGGS LSIDGADNAI EHSDYRAKLA QIRQIYHQEL EKYEQACNEF TTHVMNLLRE QSRTRPITPK EIERMVQIIH KKFSSIQMQL KQSTCEAVMI LRSRFLDARR KRRNFSKQAS EILNEYFYSH LSNPYPSEEA KEELARKCGI TVSQVSNWFG NKRIRYKKNI GKAQEEANLY AAKKAAGASP YSMAGPPSGT TTPMMSPAPP QDSMGYPMGS GGYDQQQPYD NSMGGYDPNL HQDLSP // ID EXPA_DROME STANDARD; PRT; 1429 AA. AC Q07436; DT 01-OCT-1996 (Rel. 34, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Expanded protein. GN EX. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Imaginal disks; RX MEDLINE=94094747; PubMed=8269855; RA Boedigheimer M., Laughon A.; RT "Expanded: a gene involved in the control of cell proliferation in RT imaginal discs."; RL Development 118:1291-1301(1993). RN [2] RP REVISIONS. RA Boedigheimer M.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE CONTROL OF CELL PROLIFERATION IN CC IMAGINAL DISCS. MAY BIND TO CERTAIN PROTEINS OF SIGNAL CC TRANSDUCTION PATHWAYS BY INTERACTION WITH THEIR SH3 DOMAINS. CC -!- SUBCELLULAR LOCATION: APICAL SURFACE OF DISC CELLS. CC -!- DISEASE: MUTATIONS OF EXPANDED PROTEIN CAUSE HYPERPLASMIA OF THE CC IMAGINAL DISC RESULTING IN WING OVERGROWTH. THIS OVERGROWTH IS CC LIMITED TO SPECIFIC REGIONS ALONG THE 2 WING AXES. DEFECTS ALSO CC IN EYES, HEAD, THORAX AND LIMBS WHERE DUPLICATION AND BULGING CC OFTEN OCCUR. CC -!- SIMILARITY: CONTAINS 1 FERM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L14768; AAB39774.1; -. DR PIR; T13720; T13720. DR FlyBase; FBgn0004583; ex. DR InterPro; IPR000299; Band_4.1. DR Pfam; PF00373; Band_41; 1. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; FALSE_NEG. DR PROSITE; PS50057; FERM_3; 1. KW Developmental protein; SH3-binding. FT DOMAIN 26 399 FERM. FT SITE 1008 1016 SH3-BINDING (POTENTIAL). FT SITE 1012 1020 SH3-BINDING (POTENTIAL). FT SITE 1149 1157 SH3-BINDING (POTENTIAL). FT DOMAIN 409 412 POLY-GLU. FT DOMAIN 782 788 POLY-PRO. FT DOMAIN 952 955 POLY-HIS. FT DOMAIN 1002 1005 POLY-PRO. FT DOMAIN 1011 1017 POLY-PRO. FT DOMAIN 1081 1084 POLY-PRO. FT DOMAIN 1149 1154 POLY-PRO. FT DOMAIN 1158 1168 POLY-ALA. FT DOMAIN 1170 1174 POLY-SER. FT DOMAIN 1199 1205 POLY-PRO. FT DOMAIN 1416 1424 POLY-GLN. SQ SEQUENCE 1429 AA; 153886 MW; 3CB08D2FC4862062 CRC64; MRAFCTVSAP LEVCASSAEQ LSPGSRFLAL RLLGQQQPKT LYFLVDAKSR VREVYTQTCL HFATQGMLDT ELFGLAVLID GEYMFADPES KLSKYGPKSW RSSHTHGLDA NGRPLLELHF RVQFYIESPF MLKDETSRHN YYLQLRHNIL QRDLPREQAD EALVFLAGLA LQADLGDAPP GTSNSKDDSG EETLASPSNG GRGLSATTTL PKISKRANER MLRLSTYVAS TSKRETIPLP PSLPPNGADY YRIEDYLPSG LHTPWARSAM RACHREHLGM ATAEAELLYI QQACSLHETI NAHTYRMRLA KSEQGSGSAW FVVYAKGIKI LGGESTNSSS NPETTTSLWP NITKLSFERK KFEIRSGESR ITLYAASDEK NKLLLTLCKD THQWSMKLAA RLKEVSKREE EEAAESQRLH ASYACSRSLL LPYKSKNEQR ISVISSTSSN TTSGIVSDRV HSEDELEIMI NTPPAPLAAP STESLALAHL LDRPSVSRQT SSVGQMSLKD LEEQLAALSV RPQDASSNGA TIVTNSSVQR NSMGTTANDS STATDSPSSQ HNTGSQCSST CSTVVVTSPV NGAGASSSGA PIPVHSTSSS LELGFSHTAQ NSALSETSPD DFLSTSAREE TESVSGASGV YTLAHGAPPT ETSGVYTMHS SELTGQSSEI DESEKSSHYG MFQPQKLEET HVSHSDSVDG KKKEDFRPRS DSNVSTGSSF RGDGSDPTDN KHSLLSAEEL TNLIVGRGTY PSRKTVSSSL HSDCDYVTLP LGDQGEEEVD QPPAPPPPYS ARHEKTGLCG PPIAKPIPKP IAVVAPKPDS PPCSPPVPPA PIPAPPPAIR RRDPPPYSIS SKPRPTSLIS VSSSAHPAPS AAGSMSSLKS EEVTARFITT RPQISILKAH TSLIPDGAKP SYAAPHHCSS VASSNGSVCS HQLSQQSLHN SNYAGGSQAS LHHHHVPSHH RHSGSAAIGI VPYGLHKSTA SLHHQQSCVL LPVIKPRQFL APPPPSLPRQ PPPPPPPNHP HLASHLYERE MARKQLELYQ QQLYSDVDYV IYPIQDPAVS QQEYLDAKQG SLLAAMAQAA PPPPHHPYLA MQVSPAIYRS TPYLPLTLST HSRYASTQNL SDTYVQLPGP GYSPLYSPSM ASLCSSYEPP PPPPLHPAAL AAAAAAGAGS SSSSMFARSR SDDNILNSLD LLPKGKRLPP PPPPPYVNRR LKKPPMPAPS EKPPPIPSKP IPSRMSPIPP RKPPTLNPHH ANSPLTKTSS GAQWAGERPR PDLGLGLGLN RGNNSILAQL QAFNVAQSHA QAQAQALDIA LLREKSKHLD LPLISALCND RSLLKQTKVV INPKTGQEMP TSSAQPSGAT TNGVANSSAG AGTLSKARKG STVSHRHPQD KLPPLPVQQL AEANNYVIDP AVMMKQQQQQ QQQQHNKTS // ID EXU_DROME STANDARD; PRT; 532 AA. AC P28750; Q9V967; DT 01-DEC-1992 (Rel. 24, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Maternal exuperantia protein. GN EXU OR CG8994. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92097546; PubMed=1756733; RA Marcey D., Watkins W.S., Hazelrigg T.; RT "The temporal and spatial distribution pattern of maternal RT exuperantia protein: evidence for a role in establishment but not RT maintenance of bicoid mRNA localization."; RL EMBO J. 10:4259-4266(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92090725; PubMed=1752438; RA Macdonald P.M., Luk S.K.-S., Kilpatrick M.; RT "Protein encoded by the exuperantia gene is concentrated at sites of RT bicoid mRNA accumulation in Drosophila nurse cells but not in oocytes RT or embryos."; RL Genes Dev. 5:2455-2466(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ENSURES THE PROPER LOCALIZATION OF THE MRNA OF THE CC BICOID GENE TO THE ANTERIOR REGIONS OF THE OOCYTE THUS PLAYING CC A FUNDAMENTAL ROLE IN THE ESTABLISHMENT OF THE POLARITY OF THE CC OOCYTE. MAY BIND THE BCD MRNA. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S72757; AAB20673.1; -. DR EMBL; S72363; AAB20670.1; -. DR EMBL; AE003791; AAF57429.1; -. DR EMBL; AY051739; AAK93163.1; -. DR PIR; S18643; S18643. DR FlyBase; FBgn0000615; exu. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0045450; P:bicoid mRNA localization; IMP. KW Developmental protein; RNA-binding. FT DOMAIN 207 246 SER-RICH. FT VARIANT 223 223 M -> I. FT VARIANT 339 339 R -> S (IN PJ42 MUTANT, LOSS OF EXU FT FUNCTION IN FEMALE). FT CONFLICT 176 176 K -> Q (IN REF. 1). SQ SEQUENCE 532 AA; 57974 MW; 50BD15B712A62C4E CRC64; MVADNIDAGV AIAVADQSSS PVGDKVELPA GNYILVGVDI DTTGRRLMDE IVQLAAYTPT DHFEQYIMPY MNLNPAARQR HQVRVISIGF YRMLKSMQTY KIIKSKSEIA ALKDFLNWLE QLKTKAGPSS DGIVLIYHEE RKFIPYMILE SLKKYGLLER FTASVKSFAN SINLAKASIG DANIKNYSLR KLSKILSTTK EEDAACSAST SGSGSGLGSG SSMVSDSVSI SPRDSTVTNG DDKQSSKNAV QGKRELFDGN ASVRAKLAFD VALQLSNSDG KPEPKSSEAL ENMFNAIRPF AKLVVSDVLE LDIQIENLER QNSFRPVFLN YFKTTLYHRV RAVKFRIVLA ENGFDLNTLS AIWAEKNIEG LDIALQSIGR LKSKDKAELL ELLDSYFDPK KTTVKPVVKG NSNNNNNYRR RNRRGGRQSV KDARPSSSPS ASTEFGAGGD KSRSVSSLPD STTKTPSPNK PRMHRKRNSR QSLGATPNGL KVAAEISSSG VSELNNSAPP AVTISPVVAQ PSPTPVAITA SN // ID EYA_DROME STANDARD; PRT; 766 AA. AC Q05201; Q961V4; Q9VMC1; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Developmental protein eyes absent (Protein Clift). GN EYA OR CLI OR CG9554. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RX MEDLINE=93161413; PubMed=8431945; RA Bonini N.M., Leiserson W.M., Benzer S.; RT "The eyes absent gene: genetic control of cell survival and RT differentiation in the developing Drosophila eye."; RL Cell 72:379-395(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR THE SURVIVAL OF EYE PROGENITOR CELLS AT A CC CRITICAL STAGE IN MORPHOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q05201-1; Sequence=Displayed; CC Name=2; CC IsoId=Q05201-2; Sequence=VSP_001500; CC -!- SIMILARITY: BELONGS TO THE EYA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08501; AAA28723.1; -. DR EMBL; L08502; AAA28310.1; -. DR EMBL; AE003614; AAF52400.1; -. DR EMBL; AY047539; AAK77271.1; -. DR PIR; A45174; A45174. DR FlyBase; FBgn0000320; eya. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0016787; F:hydrolase activity; NAS. DR GO; GO:0007455; P:eye-antennal disc metamorphosis; IMP. DR InterPro; IPR006545; EYA. DR InterPro; IPR005834; Hydrolase. DR Pfam; PF00702; Hydrolase; 1. DR TIGRFAMs; TIGR01658; EYA-cons_domain; 1. KW Developmental protein; Nuclear protein; Alternative splicing. FT DOMAIN 46 57 POLY-GLN. FT DOMAIN 60 68 POLY-GLN. FT DOMAIN 92 108 POLY-GLY. FT DOMAIN 253 260 POLY-ALA. FT DOMAIN 268 271 POLY-TYR. FT DOMAIN 305 311 POLY-ALA. FT DOMAIN 428 434 POLY-ALA. FT VARSPLIC 1 23 MVTLMPYNYAAPRCGLIDKMIEP -> MLYNVPCYQNFSTL FT DYY (in isoform 2). FT /FTId=VSP_001500. SQ SEQUENCE 766 AA; 80656 MW; 3581C26AB1811E74 CRC64; MVTLMPYNYA APRCGLIDKM IEPKVKRPKT DHTDTHERNR LCNLSQQQQQ QQPQQQQTHQ QQQQQQQQSH QQSHSSTVLA SNGPSSAGAG MGVGVGGGGG SGGGVGGGVG QCSPLGLPPQ SQPLQPTIGS LASLSGHYSN GNANPNVNSS SCSLATASSF AQSAGSSFST YQQAGGTSGG VSGEDGVVGG ATVMSHWTHD GTGSSAAVKS ESRSPGQVHA SLDNGSVAGS NLYGCSSASN PLDGGAVAVN SSAVAAAAAA VYDGKHDYYY YNSMQQYTPP PFYSGYGTPY AAATAARQAK MEPGAAAAAA AYLTPSYAAS GNNNSQLYSS PYAGYNNFGQ QDYGGYYNEQ YGNYYSPANY SPYAVSSPSS SASHGHGFHV AASSNLSESP TDTHSTTPVH QTTHSPHSPL PISPSTGSGI GPLGNVSAAA AAAALNSSGG SSVGTAGSGG VATSKTTPTG KTGRARGRRH QQPSPTRSTA SDTGNSEAVK PPERVFVWDL DETLIIFHTL LSGSYANRYT KDHSSLMTIA FRMEEMVFNM ADTHFFFNEI EECDQVHIDD VSSDDNGQDL SAYNFATDGF HTNTPPGAPP NLCLPTGVRG GVDWMRKLAF RYRKIKDIYN SYRGNVGTLL GPGKREAWLQ IRSEIEVATD NWATLALKCL SMISQRENCV NVLVTSTQLA PALAKVLLFG LGGIFNIENI YSAHKIGHET CYERIVTRFG RKSTYVVIGD GNEEETAAKA MNFPFWRISA HSDIRALYTA LDMGFL // ID EZ_DROME STANDARD; PRT; 760 AA. AC P42124; Q9VTA3; DT 01-NOV-1995 (Rel. 32, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polycomb protein E(z) (Enhancer of zeste protein). GN E(Z) OR CG6502. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94019309; PubMed=8413234; RA Jones R.S., Gelbart W.M.; RT "The Drosophila Polycomb-group gene Enhancer of zeste contains a RT region with sequence similarity to trithorax."; RL Mol. Cell. Biol. 13:6357-6366(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP CHARACTERIZATION. RX MEDLINE=97164720; PubMed=9012527; RA Carrington E.A., Jones R.S.; RT "The Drosophila Enhancer of zeste gene encodes a chromosomal protein: RT examination of wild-type and mutant protein distribution."; RL Development 122:4073-4083(1996). RN [5] RP INTERACTION WITH ESC. RX MEDLINE=98226554; PubMed=9566901; RA Jones C.A., Ng J., Peterson A.J., Morgan K., Simon J.A., Jones R.S.; RT "The Drosophila esc and E(z) proteins are direct partners in polycomb RT group-mediated repression."; RL Mol. Cell. Biol. 18:2825-2834(1998). RN [6] RP IDENTIFICATION IN A COMPLEX WITH RPD3; ESC AND CAF1. RX MEDLINE=21064443; PubMed=11124122; RA Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.; RT "The Drosophila Polycomb group proteins ESC and E(z) are present in a RT complex containing the histone-binding protein p55 and the histone RT deacetylase RPD3."; RL Development 128:275-286(2001). RN [7] RP IDENTIFICATION IN A COMPLEX WITH RPD3; PHO AND ESC, AND RP TRANSIENT INTERACTION WITH THE PRC1 COMPLEX. RX MEDLINE=21464651; PubMed=11581156; RA Poux S., Melfi R., Pirrotta V.; RT "Establishment of Polycomb silencing requires a transient interaction RT between PC and ESC."; RL Genes Dev. 15:2509-2514(2001). RN [8] RP IDENTIFICATION IN A ESC/E(Z) COMPLEX WITH ESC; RPD3; CAF1 AND SU(Z)12, RP METHYLTRANSFERASE ACTIVITY OF THE COMPLEX, AND MUTAGENESIS OF RP 702-ASN--HIS-703. RX MEDLINE=22296673; PubMed=12408863; RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.; RT "Drosophila Enhancer of zeste/ESC complexes have a histone H3 RT methyltransferase activity that marks chromosomal Polycomb sites."; RL Cell 111:185-196(2002). RN [9] RP IDENTIFICATION IN A COMPLEX WITH ESC; CAF1 AND SU(Z)12, RP METHYLTRANSFERASE ACTIVITY OF THE COMPLEX, AND MUTAGENESIS OF ARG-699 RP AND HIS-703. RX MEDLINE=22296674; PubMed=12408864; RA Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., RA Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.; RT "Histone methyltransferase activity of a Drosophila Polycomb group RT repressor complex."; RL Cell 111:197-208(2002). CC -!- FUNCTION: POLYCOMB GROUP (PCG) PROTEIN. PCG PROTEINS ACT BY CC FORMING MULTIPROTEIN COMPLEXES, WHICH ARE REQUIRED TO MAINTAIN THE CC TRANSCRIPTIONALLY REPRESSIVE STATE OF HOMEOTIC GENES THROUGHOUT CC DEVELOPMENT. PCG PROTEINS ARE NOT REQUIRED TO INITIATE REPRESSION, CC BUT TO MAINTAIN IT DURING LATER STAGES OF DEVELOPMENT. THEY CC PROBABLY ACT VIA THE METHYLATION OF HISTONES, RENDERING CHROMATIN CC HERITABLY CHANGED IN ITS EXPRESSIBILITY. COMPONENT OF THE ESC/E(Z) CC COMPLEX, WHICH METHYLATES LYS-9 AND LYS-27 RESIDUES OF HISTONE H3. CC ALTHOUGH NOT SUFFICIENT TO METHYLATE HISTONE H3 BY ITSELF, IT CC PROBABLY REPRESENTS THE CATALYTIC SUBUNIT OF THE ESC/E(Z) COMPLEX. CC THE ESC/E(Z) COMPLEX, WHICH MAY RECRUITED TO DNA BY PHO, IS CC NECESSARY BUT NOT SUFFICIENT TO RECRUIT A FUNCTIONAL PCG CC REPRESSIVE COMPLEX THAT REPRESSES TARGET GENES, SUGGESTING THAT CC THE RECRUITMENT OF THE DISTINCT PRC1 COMPLEX IS ALSO REQUIRED TO CC ALLOW A SUBSEQUENT REPRESSION. CC -!- SUBUNIT: COMPONENT OF THE ESC/E(Z) COMPLEX, COMPOSED OF ESC, E(Z), CC SU(Z)12, RPD3, CAF1 AND PROBABLY PHO. THIS COMPLEX IS DISTINCT CC FROM THE PRC1 COMPLEX, WHICH CONTAINS MANY OTHER PCG PROTEINS LIKE CC PC, PH, PSC, SU(Z)2. THE TWO COMPLEXES HOWEVER COOPERATE AND CC INTERACT TOGETHER DURING THE FIRST 3 HOURS OF DEVELOPMENT TO CC ESTABLISH PCG SILENCING. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE EZ FAMILY. CC -!- SIMILARITY: CONTAINS 1 SANT DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SET DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U00180; AAC46462.1; -. DR EMBL; AE003547; AAF50149.1; -. DR EMBL; AY051785; AAK93209.1; -. DR FlyBase; FBgn0000629; E(z). DR GO; GO:0005634; C:nucleus; IDA. DR InterPro; IPR001005; Myb_DNA_binding. DR InterPro; IPR001214; SET. DR Pfam; PF00856; SET; 1. DR SMART; SM00717; SANT; 2. DR SMART; SM00317; SET; 1. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS50090; MYB_3; FALSE_NEG. KW Transcription regulation; Repressor; Developmental protein; KW Nuclear protein. FT DOMAIN 505 510 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 625 745 SET. FT DOMAIN 443 491 SANT. FT DOMAIN 538 619 CYS-RICH. FT MUTAGEN 699 699 R->A,H: STRONGLY REDUCES METHYTRANSFERASE FT ACTIVITY OF THE ESC/E(Z) COMPLEX. FT MUTAGEN 702 703 NH->AA: ABOLISHES METHYTRANSFERASE FT ACTIVITY OF THE ESC/E(Z) COMPLEX. FT MUTAGEN 703 703 H->A,K: STRONGLY REDUCES METHYTRANSFERASE FT ACTIVITY OF THE ESC/E(Z) COMPLEX. FT CONFLICT 185 187 GTA -> STS (IN REF. 1). FT CONFLICT 194 194 T -> P (IN REF. 1). FT CONFLICT 213 213 G -> C (IN REF. 1). FT CONFLICT 223 223 D -> E (IN REF. 1). FT CONFLICT 230 230 E -> D (IN REF. 1). FT CONFLICT 240 240 L -> V (IN REF. 1). FT CONFLICT 250 250 D -> A (IN REF. 1). SQ SEQUENCE 760 AA; 86935 MW; 022360ED7772EB60 CRC64; MNSTKVPPEW KRRVKSEYIK IRQQKRYKRA DEIKEAWIRN WDEHNHNVQD LYCESKVWQA KPYDPPHVDC VKRAEVTSYN GIPSGPQKVP ICVINAVTPI PTMYTWAPTQ QNFMVEDETV LHNIPYMGDE VLDKDGKFIE ELIKNYDGKV HGDKDPSFMD DAIFVELVHA LMRSYSKELE EAAPGTATAI KTETLAKSKQ GEDDGVVDVD ADGESPMKLE KTDSKGDLTE VEKKETEEPL ETEDADVKPD VEEVKDKLPF PAPIIFQAIS ANFPDKGTAQ ELKEKYIELT EHQDPERPQE CTPNIDGIKA ESVSRERTMH SFHTLFCRRC FKYDCFLHRL QGHAGPNLQK RRYPELKPFA EPCSNSCYML IDGMKEKLAA DSKTPPIDSC NEASSEDSND SNSQFSNKDF NHENSKDNGL TVNSAAVAEI NSIMAGMMNI TSTQCVWTGA DQALYRVLHK VYLKNYCAIA HNMLTKTCRQ VYEFAQKEDA EFSFEDLRQD FTPPRKKKKK QRLWSLHCRK IQLKKDSSSN HVYNYTPCDH PGHPCDMNCS CIQTQNFCEK FCNCSSDCQN RFPGCRCKAQ CNTKQCPCYL AVRECDPDLC QACGADQFKL TKITCKNVCV QRGLHKHLLM APSDIAGWGI FLKEGAQKNE FISEYCGEII SQDEADRRGK VYDKYMCSFL FNLNNDFVVD ATRKGNKIRF ANHSINPNCY AKVMMVTGDH RIGIFAKRAI QPGEELFFDY RYGPTEQLKF VGIEREMEIV // ID FAC2_DROME STANDARD; PRT; 302 AA. AC Q9U1H8; Q8SZZ3; Q9VRM4; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE CAAX prenyl protease 2 (EC 3.4.22.-) (Prenyl protein-specific DE endoprotease 2) (Farnesylated-proteins converting enzyme 2) (FACE-2) DE (Severas protein). GN SRAS OR CG4852. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Weinzierl-Hinum A., Toeroek I., Kiss I., Farkas R., Mechler B.M.; RT "The severas gene of Drosophila encodes a CAAX-protease and acts as a RT tumour suppressor."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROTEOLYTICALLY REMOVES THE C-TERMINAL THREE RESIDUES OF CC FARNESYLATED AND GERANYLATED PROTEINS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY U48. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ252068; CAB64383.1; ALT_INIT. DR EMBL; AE003565; AAF50770.3; -. DR EMBL; AY069692; AAL39837.1; -. DR MEROPS; U48.UPW; -. DR FlyBase; FBgn0029121; Sras. DR InterPro; IPR003675; Abi. DR Pfam; PF02517; Abi; 1. KW Hydrolase; Transmembrane; Endoplasmic reticulum. FT TRANSMEM 27 47 POTENTIAL. FT TRANSMEM 64 84 POTENTIAL. FT TRANSMEM 104 124 POTENTIAL. FT TRANSMEM 171 191 POTENTIAL. FT TRANSMEM 212 232 POTENTIAL. FT TRANSMEM 236 256 POTENTIAL. FT TRANSMEM 268 288 POTENTIAL. FT CONFLICT 94 95 KL -> NV (IN REF. 1). FT CONFLICT 122 122 I -> M (IN REF. 1). FT CONFLICT 138 138 D -> H (IN REF. 1). SQ SEQUENCE 302 AA; 34415 MW; 84A9EE949F1993C3 CRC64; MKNLSETEAE VTMQENVVHE SLPQIPVATS VSCCFVLAVL YVGSLYIWST KHNRDHPTTV KRRFASVSMV MLAAPFFVYF FSSPELLSRV PFPKLLGLRL EGLWQAVVIP YSLTVLLFLG PIFVNMQNES VRSYFDLDYW RGSFGSIIWV RNHVIAPLSE EFVFRACMMP LILQSFSPLV AVFITPLFFG VAHLHHIAER LSLGVELSTA LLIGLFQFIY TTLFGFYSAF LFARTGHVMA PILVHAFCNH MGLPDLQDLW QQDLWRRVVA IILYLAGFVG WMFLVPLATD PSIYDNTLYW NA // ID FAF_DROME STANDARD; PRT; 2778 AA. AC P55824; Q9V9T6; Q9Y0Z7; DT 01-NOV-1997 (Rel. 35, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable ubiquitin carboxyl-terminal hydrolase FAF (EC 3.1.2.15) DE (Ubiquitin thiolesterase FAF) (Ubiquitin-specific processing protease DE FAF) (Deubiquitinating enzyme FAF) (Fat facets protein). GN FAF OR BCDNA:LD22582 OR CG1945. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY. RC TISSUE=Eye imaginal disk; RX MEDLINE=93202020; PubMed=1295747; RA Fischer-Vize J.A., Rubin G.M., Lehmann R.; RT "The fat facets gene is required for Drosophila eye and embryo RT development."; RL Development 116:985-1000(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 1089-2778 FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: REQUIRED FOR EYE AND EMBRYO DEVELOPMENT, AND PLAYS A CC ROLE IN COMPOUND EYE ASSEMBLY AND OOGENESIS RESPECTIVELY. IN THE CC LARVAL EYE DISKS, CELLS OUTSIDE THE ASSEMBLING FACETS REQUIRE THIS CC PROTEIN FOR SHORT-RANGE CELL INTERACTIONS THAT PREVENT THE MYSTERY CC CELLS FROM BECOMING PHOTORECEPTORS. IT IS ALSO REQUIRED FOR CC NUCLEAR MIGRATION AND CELLULARIZATION IN EARLY EMBRYOGENESIS AND CC COULD PLAY A ROLE IN POLE CELL DETERMINATION, DEVELOPMENT OR CC FUNCTION. CC -!- CATALYTIC ACTIVITY: UBIQUITIN C-TERMINAL THIOLESTER + H(2)O = CC UBIQUITIN + A THIOL. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; CC IsoId=P55824-1; Sequence=Displayed; CC Name=2; CC IsoId=P55824-2; Sequence=VSP_005270; CC Name=3; CC IsoId=P55824-3; Sequence=VSP_005269; CC -!- TISSUE SPECIFICITY: EYE DISKS AND OVARIES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C19. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L04959; AAF01345.1; -. DR EMBL; L04958; AAF01346.1; -. DR EMBL; L04960; AAF01347.1; -. DR EMBL; L04960; AAF01348.1; -. DR EMBL; AE003779; AAF57198.1; -. DR EMBL; AE003779; AAN14291.1; -. DR EMBL; AF145677; AAD38652.1; -. DR MEROPS; C19.007; -. DR FlyBase; FBgn0005632; faf. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0007349; P:cellularization; IMP. DR GO; GO:0009795; P:embryonic morphogenesis; IMP. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR GO; GO:0008583; P:mystery cell fate differentiation (sensu Dr...; IMP. DR GO; GO:0007097; P:nuclear migration; IMP. DR GO; GO:0016579; P:protein deubiquitination; IDA. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolism; IGI. DR InterPro; IPR001394; Peptidase_C19. DR Pfam; PF00443; UCH; 1. DR PROSITE; PS00972; UCH_2_1; 1. DR PROSITE; PS00973; UCH_2_2; 1. DR PROSITE; PS50235; UCH_2_3; 1. KW Ubl conjugation pathway; Hydrolase; Thiol protease; KW Developmental protein; Vision; Alternative splicing. FT ACT_SITE 1677 1677 BY SIMILARITY. FT ACT_SITE 1978 1978 BY SIMILARITY. FT ACT_SITE 1986 1986 BY SIMILARITY. FT VARSPLIC 2705 2778 KCRRVIIKKLVESKDEEDATTATTAATTEVTTSPATAIATA FT ATLEPAGMSELTTMVEKNLIISQENPQAKSSLQ -> VTRA FT NNV (in isoform 3). FT /FTId=VSP_005269. FT VARSPLIC 2742 2778 IATAATLEPAGMSELTTMVEKNLIISQENPQAKSSLQ -> FT SQRQQL (in isoform 2). FT /FTId=VSP_005270. FT CONFLICT 234 234 E -> D (IN REF. 1). FT CONFLICT 2725 2725 T -> S (IN REF. 1; AAF01345). SQ SEQUENCE 2778 AA; 311139 MW; FFB90438BA53A02B CRC64; MTFDTRRHTT GQPGSTAPSS SSSTTSTTTT TTSPAQSAGS GSGIGTGTGT VANSSLPGGG SGSLDGNQDQ QPATDSQSSD DVAASLSANS VDSTITIVPP EKLISSFPTT KLRSLTQKIS NPRWVVPVLP EQELEVLLNA AIELTQAGVD HDCEPCVEFY RNGLSTSFAK ILTDEAVNSW KNNIHHCILV SCGKLLHLIA IHMQRDNPYL LDLLAIVFDP ENKFNTFNAG RQPECFAAPD YIWGQLDSNK MYARPPPEPK NARGWLVDLI NRFGQLGGFD NLLERFNIGL ELLKRNQNKC TGKNISVEGR VENGAQDNRL TLALIHSLLR PFGQCYELLM PATIAKYFMP TWNVVLDLLD SFTDEELKRE VKPEGRNDYI NGIVKSARLL ASRLTGQEEL IRDLEMFRLK MILRLLQVSS FNGKMNALNE INKVLSSVAY FSHRSQPLPH CMPEDEMDWL TADRMAQWIK SSDVLGVVLK DSLHQPQYVE KLEKIIRFLI KEQALTLDDL DAVWRAQAGK HEAIVKNVHD LLAKLAWDFT PEQLDHLFEA FQASMTTANK RQRERLLELI RRLAEDDKNG VMAQKVLKLF WTLAHSQEVP PEVLDQALGA HVKILDYSCS QERDAQKTIW LDKCVDELKS GDGWVLPALR LIRDICCLYD TTTNHAQRTQ TSTNRQQVIE RLQNDYSLVI LVTNSLTAYM EKVRQMVTDS PGLDATRILI DGRFPHHVQI AERLEFLKFL LKDGQLWLCA DQAKQIWHCL AVNAVFPADR EECFRWFGKL MGEEPDLDPG INKDFFENNI LQLDPHLLTE SGIKCFERFF KAVNSKEDKL KAIHRGYMLD NEDLIGKDYL WRVITTGGEE IASKAIDLLK EVSTALGPRL QENIAEFHEM FIGECCSRLR THYGNIVILG KTQLQEELDA PDQSDNTNDE SKDSKMRFIE AEKMCRILKV LQEYVKECDR SFSGDRVHLP LSRVTRGKNT ILYIRFQNPG RSIDDMEIVT HSNETMAAFK RNLLKRIKGT STANIKVDLF YANDEMIGVS DEINPLYQYT IRDKMNLTAK LTPVGTGLAS SPDSSSDSST GSPPRPCPDM QRVESESTLP GVIISQNYQY TEFFLKLYQL GSDLEHGRLR DSAKVLLHLL PCDRQTIRQL KIMCKVPKAA VTVAVTGDKI AKDEEEKLYP TEQAGIEDEE EHCTPEQMFL HPTPAQVLYN LSVLHGLLIP ALDPLGESAL LVQSAWMHSG CAHFVLELLT KNNFLPSADM HTKRASFQCV LRLAKLFLYI VGSVLSRVGD EPMICDLDNG SRSQVDILKQ NFSTMPSSSQ GTLRAISAKL AVILAREMLS ASPEGDRCRT LFSSTLQWSC PDISTIKAVV QLAWASSCGN LQALGNSSGD FEDEVIVPDG QDFSMCKEAL EVLTISFILN PSANEALTSD PNWPKFITSI VLKNPLRHVR QVASEQLFLA STYCAGDRRP FVYMVNLLVG ALKTLVPQYE STCAEFFSVL CRTLSYGCIY NWPLQISEGL LGDEIKWLQR IRENVHATGD TQVHEELLEG HLCLAKELMF FLGADSKAQL NELIHELIDD FLFTASREFL HLRRHGSLRQ DTVPPPVCRS PHTIAAACDL LIALCQLCVP NMKLLTNTLI DFVCTDTDPL REWDYLPPVG ARPTKGFCGL KNAGATCYMN SVLQQLYMVP AVRVGILRAH GAATTDGEDF SGDSDLTGGG LGSALFSGPA SALVSLPSSS STIEDGLHDV RKNYHVVILK HVQAIFAHLG HSALQYYVPR GLWTHFKLLG EPVNLREQQD AVEFFMSLLE SLDEGLKALG QPQLMNATLG GSFSDQKICQ ECPHRYSKEE PFSVFSVDIR NHSSLTESLE QYVKGELLEG ADAYHCDKCD KKVVTVKRVC VKKLPPVLAI QLKRFEYDYE RVCAIKFNDY FEFPRILDME PYTVSGLAKL EGEVVEVGDN CQTNVETTKY ELTGIVVHSG QASGGHYFSY ILSKNPANGK CQWYKFDDGE VTECKMHEDE EMKAECFGGE YMGETYDNNL KRMQYRRQKR WWNAYMLFYT RCDQTPVQYE PSVEQLSLAE SRNMVLPLPK PIERSVRHQN IRFLHSRSIF SVEFFNFIKK LVSCNLLSAR SNKITPAAEE LSLLGVQLAS QFLFHTGFRT KKSLRGPVME WYDALSHHIR SSALVRKWFA NHALLSPPSR LGEYILMAPS PDVRTVFVKL VVFFCHFAIN DEPLTGYDGA NLCEQVLISV LRLLKSEAAD YGKHLPHYFS LFSMYVGLGT REKQQLLRLN VPLQFIQVAL DDGPGPAIKY QYPEFSKLHQ VVSHLIRCSD VSEKCQSSNQ NARPLSNPFK DPNVAHEELT PLSTECMDLL FNRTGYIKKV IEDTNVGDEG LKLLQYCSWE NPHFSRAVLT ELLWQCGFAY CHDMRHHTDL LLNILLIDDS WQHHRIHNAL NGVAEEREGL LETIQRAKTH YQKRAYQIIK CLTQLFHKSP IALQMLHTNS NITRHWSIAV EWLQGELDRQ RGIGCQYNSY SWSPPAQSND NTNGYMLERS QSAKNTWSMA FELCPDEVSE KTDENNEPNL ETNMDENKSE PVAQPGGVLE GSTGGTEQLP ENKTPTTSSP STAAWPARGD SNAIPRLSRQ LFGAYTSTGS GSTSGGSAPT SALTTTAGSG ANSETESSAQ ETTGETTING LTNSLDQMEI TAKKKCRRVI IKKLVESKDE EDATTATTAA TTEVTTSPAT AIATAATLEP AGMSELTTMV EKNLIISQEN PQAKSSLQ // ID FAS1_DROME STANDARD; PRT; 652 AA. AC P10674; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Fasciclin I precursor (FAS I) (FCN). GN FAS1 OR CG6588. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88223351; PubMed=3370670; RA Zinn K., McAllister L., Goodman C.; RT "Sequence analysis and neuronal expression of fasciclin I in RT grasshopper and Drosophila."; RL Cell 53:577-587(1988). RN [2] RP SEQUENCE FROM N.A. RA McAllister L., Zinn K., Rehm J., Goodman C.S.; RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP GPI-ANCHOR. RX MEDLINE=90368690; PubMed=2394715; RA Hortsch M., Goodman C.S.; RT "Drosophila fasciclin I, a neural cell adhesion molecule, has a RT phosphatidylinositol lipid membrane anchor that is developmentally RT regulated."; RL J. Biol. Chem. 265:15104-15109(1990). CC -!- FUNCTION: NEURAL CELL ADHESION MOLECULE. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR. CC -!- TISSUE SPECIFICITY: EXPRESSED ON DIFFERENT SUBSETS OF AXON BUNDLES CC (FASCICLES) IN INSECT EMBRYOS. CC -!- SIMILARITY: CONTAINS 4 FAS1 DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M20545; AAA28531.1; -. DR EMBL; M32311; AAA28529.1; -. DR EMBL; AE003714; AAN13715.1; -. DR PIR; B29900; B29900. DR PDB; 1O70; 13-FEB-03. DR FlyBase; FBgn0000634; Fas1. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0007411; P:axon guidance; IGI. DR GO; GO:0008038; P:neuronal cell recognition; IDA. DR InterPro; IPR000782; BIgH3_FAS1. DR Pfam; PF02469; Fasciclin; 3. DR SMART; SM00554; FAS1; 4. DR PROSITE; PS50213; FAS1; 4. KW Cell adhesion; Glycoprotein; Lipoprotein; Membrane; Repeat; Signal; KW GPI-anchor; 3D-structure. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 625 FASCICLIN I. FT PROPEP 626 652 REMOVED IN MATURE FORM (POTENTIAL). FT DOMAIN 22 144 FAS1 1. FT DOMAIN 166 310 FAS1 2. FT DOMAIN 317 463 FAS1 3. FT DOMAIN 467 616 FAS1 4. FT LIPID 625 625 GPI-anchor amidated alanine (Potential). FT CARBOHYD 47 47 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 368 368 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 416 416 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 441 441 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 497 497 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 652 AA; 72598 MW; 4D846358A47DBFD6 CRC64; MLNAAALLLA LLCAANAAAA ADLADKLRDD SELSQFYSLL ESNQIANSTL SLRSCTIFVP TNEAFQRYKS KTAHVLYHIT TEAYTQKRLP NTVSSDMAGN PPLYITKNSN GDIFVNNARI IPSLSVETNS DGKRQIMHII DEVLEPLTVK AGHSDTPNNP NALKFLKNAE EFNVDNIGVR TYRSQVTMAK KESVYDAAGQ HTFLVPVDEG FKLSARSSLV DGKVIDGHVI PNTVIFTAAA QHDDPKASAA FEDLLKVTVS FFKQKNGKMY VKSNTIVGDA KHRVGVVLAE IVKANIPVSN GVVHLIHRPL MIIDTTVTQF LQSFKENAEN GALRKFYEVI MDNGGAVLDD INSLTEVTIL APSNEAWNSS NINNVLRDRN KMRQILNMHI IKDRLNVDKI RQKNANLIAQ VPTVNNNTFL YFNVRGEGSD TVITVEGGGV NATVIQADVA QTNGYVHIID HVLGVPYTTV LGKLESDPMM SDTYKMGKFS HFNDQLNNTQ RRFTYFVPRD KGWQKTELDY PSAHKKLFMA DFSYHSKSIL ERHLAISDKE YTMKDLVKFS QESGSVILPT FRDSLSIRVE EEAGRYVIIW NYKKINVYRP DVECTNGIIH VIDYPLLEEK DVVVAGGSYL PESSICIILA NLIMITVAKF LN // ID FAS2_DROME STANDARD; PRT; 873 AA. AC P34082; P34083; Q9W4M6; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fasciclin II precursor (FAS II). GN FAS2 OR EG:EG0007.3 OR CG3665. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, RP AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; RX MEDLINE=92005695; PubMed=1913818; RA Grenningloh G., Rehm E.J., Goodman C.S.; RT "Genetic analysis of growth cone guidance in Drosophila: fasciclin II RT functions as a neuronal recognition molecule."; RL Cell 67:45-57(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 22-873 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- FUNCTION: NEURONAL RECOGNITION MOLECULE FOR THE MP1 AXON PATHWAY, CC PATHWAY RECOGNITION FOR AXONS DURING THE DEVELOPMENT OF NERVE CC FASCICLES. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (ISOFORM 1); CC ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR (ISOFORM 2). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; Synonyms=A, Membrane-linked; CC IsoId=P34082-1; Sequence=Displayed; CC Name=2; Synonyms=C, Phosphatidylinositol-linked; CC IsoId=P34082-2; Sequence=VSP_002508, VSP_002509; CC Name=3; Synonyms=B; CC IsoId=P34082-3; Sequence=VSP_002506, VSP_002507; CC -!- TISSUE SPECIFICITY: IN EMBRYOS, BOTH ISOFORMS ARE INITIALLY CC EXPRESSED ON THE SURFACE OF THE AXONS IN THE MP1 PATHWAY AND LATER CC ON SEVERAL OTHER LONGITUDINAL AXON FASCICLES. CC -!- SIMILARITY: CONTAINS 5 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -!- SIMILARITY: CONTAINS 2 FIBRONECTIN TYPE III DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77165; AAA28527.1; -. DR EMBL; M77166; AAA28528.1; -. DR EMBL; AL033125; CAA21825.1; -. DR EMBL; AE003430; AAF45925.2; -. DR EMBL; AE003430; AAN09119.1; -. DR EMBL; AL033125; CAA21826.1; -. DR PIR; A41054; A41054. DR FlyBase; FBgn0000635; Fas2. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0007156; P:homophilic cell adhesion; IDA. DR GO; GO:0007611; P:learning and/or memory; IMP. DR GO; GO:0016319; P:mushroom body development; IMP. DR GO; GO:0008038; P:neuronal cell recognition; IDA. DR GO; GO:0045473; P:response to ethanol (sensu Insecta); NAS. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003961; FN_III. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR Pfam; PF00041; fn3; 2. DR Pfam; PF00047; ig; 5. DR SMART; SM00060; FN3; 2. DR SMART; SM00408; IGc2; 3. DR PROSITE; PS50835; IG_LIKE; 5. KW Cell adhesion; Glycoprotein; Repeat; Alternative splicing; KW Immunoglobulin domain; Transmembrane; GPI-anchor; Signal; KW Neurogenesis. FT SIGNAL 1 28 POTENTIAL. FT CHAIN 29 873 FASCICLIN II. FT DOMAIN 29 751 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 752 769 POTENTIAL. FT DOMAIN 770 873 CYTOPLASMIC (POTENTIAL). FT DOMAIN 31 131 IG-LIKE C2-TYPE 1. FT DOMAIN 138 223 IG-LIKE C2-TYPE 2. FT DOMAIN 230 318 IG-LIKE C2-TYPE 3. FT DOMAIN 323 423 IG-LIKE C2-TYPE 4. FT DOMAIN 428 520 IG-LIKE C2-TYPE 5. FT DOMAIN 544 619 FIBRONECTIN TYPE-III 1. FT DOMAIN 648 705 FIBRONECTIN TYPE-III 2. FT DISULFID 54 116 POTENTIAL. FT DISULFID 159 207 POTENTIAL. FT DISULFID 251 302 POTENTIAL. FT DISULFID 343 407 POTENTIAL. FT DISULFID 451 504 POTENTIAL. FT CARBOHYD 74 74 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 250 250 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 330 330 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 448 448 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 458 458 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 576 576 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 737 773 GIDVIQVAERQVFSSAAIVGIAIGGVLLLLFVVDLLC -> FT DNPHPSTSGAAPLAQLLVIFTALPTMLLILPPTTHTA (in FT isoform 3). FT /FTId=VSP_002506. FT VARSPLIC 774 873 Missing (in isoform 3). FT /FTId=VSP_002507. FT VARSPLIC 738 811 IDVIQVAERQVFSSAAIVGIAIGGVLLLLFVVDLLCCITVH FT MGVMATMCRKAKRSPSEIDDEAKLGSGQLVKEP -> ESDS FT ANNNLGTLLYSAGFNSGVGALHKRLFTTTTTTTATSTTTIT FT SITTATTTIITLATTISITLLSVLASMLA (in isoform FT 2). FT /FTId=VSP_002508. FT VARSPLIC 812 873 Missing (in isoform 2). FT /FTId=VSP_002509. FT CONFLICT 804 804 S -> R (IN REF. 4; CAA21826). SQ SEQUENCE 873 AA; 96926 MW; E48F0484CCE62AC9 CRC64; MGELPPNSVG VFLALLLCSC SLIELTRAQS PILEIYPKQE VQRKPVGKPL ILTCRPTVPE PSLVADLQWK DNRNNTILPK PNGRNQPPMY TETLPGESLA LMITSLSVEM GGKYYCTASY ANTEILEKGV TIKTYVAITW TNAPENQYPT LGQDYVVMCE VKADPNPTID WLRNGDPIRT TNDKYVVQTN GLLIRNVQES DEGIYTCRAA VIETGELLER TIRVEVFIQP EIISLPTNLE AVEGKPFAAN CTARGKPVPE ISWIRDATQL NVATADRFQV NPQTGLVTIS SVSQDDYGTY TCLAKNRAGV VDQKTKLNVL VRPQIYELYN VTGARTKEIA ITCRAKGRPA PAITFRRWGT QEEYTNGQQD DDPRIILEPN FDEERGESTG TLRISNAERS DDGLYQCIAR NKGADAYKTG HITVEFAPDF SHMKELPPVF SWEQRKANLS CLAMGIPNAT IEWHWNGRKI KDLYDTNLKI VGTGPRSDLI VHPVTRQYYS GYKCIATNIH GTAEHDMQLK EARVPDFVSE AKPSQLTATT MTFDIRGPST ELGLPILAYS VQYKEALNPD WSTAYNRSWS PDSPYIVEGL RPQTEYSFRF AARNQVGLGN WGVNQQQSTP RRSAPEEPKP LHNPVQHDKE EPVVVSPYSD HFELRWGVPA DNGEPIDRYQ IKYCPGVKIS GTWTELENSC NTVEVMETTS FEMTQLVGNT YYRIELKAHN AIGYSSPASI IMKTTRGIDV IQVAERQVFS SAAIVGIAIG GVLLLLFVVD LLCCITVHMG VMATMCRKAK RSPSEIDDEA KLGSGQLVKE PPPSPLPLPP PVKLGGSPMS TPLDEKEPLR TPTGSIKQNS TIEFDGRFVH SRSGEIIGKN SAV // ID FAS3_DROME STANDARD; PRT; 508 AA. AC P15278; Q8SXX9; Q9VJ89; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fasciclin III precursor (FAS III). GN FAS3 OR CG5803. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=90030406; PubMed=2509076; RA Snow P.M., Bieber A.J., Goodman C.S.; RT "Fasciclin III: a novel homophilic adhesion molecule in Drosophila."; RL Cell 59:313-323(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MEDIATES CELL ADHESION IN A CA(2+)-INDEPENDENT MANNER. CC IT PLAYS A ROLE IN AXON OUTGROWTH, GUIDANCE AND FASCICULATION OF CC THE DEVELOPING NERVOUS SYSTEM. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=P15278-1; Sequence=Displayed; CC Name=B; CC IsoId=P15278-2; Sequence=VSP_007949, VSP_007950; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: EXPRESSED ON DIFFERENT SUBSETS OF AXON BUNDLES CC (FASCICLES) IN INSECT EMBRYOS. CC -!- SIMILARITY: CONTAINS 2 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 IMMUNOGLOBULIN-LIKE V-TYPE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27813; AAA28532.1; -. DR EMBL; AE003658; AAF53665.2; -. DR EMBL; AE003658; AAN11002.1; -. DR EMBL; AY075516; AAL68324.1; -. DR PIR; A33378; A33378. DR FlyBase; FBgn0000636; Fas3. DR GO; GO:0016323; C:basolateral plasma membrane; NAS. DR GO; GO:0007411; P:axon guidance; IEP. DR GO; GO:0008039; P:synaptic target recognition; IDA. DR InterPro; IPR007110; Ig-like. DR PROSITE; PS50835; IG_LIKE; 1. KW Cell adhesion; Glycoprotein; Repeat; Immunoglobulin domain; KW Transmembrane; Signal; Neurogenesis; Phosphorylation; KW Pyrrolidone carboxylic acid; Alternative splicing. FT SIGNAL 1 20 FT CHAIN 21 508 FASCICLIN III. FT DOMAIN 21 346 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 347 370 POTENTIAL. FT DOMAIN 371 508 CYTOPLASMIC (POTENTIAL). FT DOMAIN 44 106 IG-LIKE V-TYPE. FT DOMAIN 126 223 IG-LIKE C2-TYPE 1. FT DOMAIN 236 310 IG-LIKE C2-TYPE 2. FT MOD_RES 21 21 PYRROLIDONE CARBOXYLIC ACID (PROBABLE). FT DISULFID 150 211 POTENTIAL. FT CARBOHYD 62 62 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 160 160 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 257 257 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 300 300 N-LINKED (GLCNAC...) (POTENTIAL). FT MOD_RES 382 382 PHOSPHORYLATION (POTENTIAL). FT MOD_RES 459 459 PHOSPHORYLATION (POTENTIAL). FT VARSPLIC 391 401 SDTESADIKAT -> KTNNSSMLNLY (in isoform FT B). FT /FTId=VSP_007949. FT VARSPLIC 402 508 Missing (in isoform B). FT /FTId=VSP_007950. SQ SEQUENCE 508 AA; 55883 MW; 6E39EA0580697D4F CRC64; MSRIVFICLA AILTDALTWA QVNVEPNTAL LNEGDRTELL CRYGRSINYC RIEIPGEQKV LNLSPEWSKT PGFTYFGAGL TAGQCGVSIE RVKASNNGQV KCSLGVEGEE LSGTIDLVVA LRPQQPIIEL LSRPNREGYF NEGTEFRARC SVRDGRPPAN ISWYIDNMPA NKRTTPLEVM SSTNDNVELS TSVQEIQWHL SPEDSNRKLV CRSHHQTDRE SVPPQEAAYI INVRYAPVHQ PDAAVYGLYL EHTAIVNITI RASPQPKIEW TIDGAIVGQG RTDGRYSAYE PQYLGNDEYN VTLAIAGLTL EDTTKIYNLR ASNELGLTDY QVRISSSSKP PSSSLDVAAI VGIVVAVAVL VLVVLLIVFA RATGRWCFGG KSIKTPTNET SDTESADIKA TSTATATTTM GGVGVSAEEE ETVNEQESPQ EQQQQQQKKA KRLPAFAAAI LRRFNEKDSR KYKDNQESLN IVEGSVQEIP ATNNAIDGND NEPKAIVWQS TSPVWTFK // ID FAT2_DROME STANDARD; PRT; 4705 AA. AC Q9VW71; Q95S51; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative fat-like cadherin-related tumor suppressor homolog DE precursor. GN FAT2 OR CG7749. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE OF 3837-4705 FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: CONTAINS 34 CADHERIN DOMAINS. CC -!- SIMILARITY: CONTAINS 5 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 LAMININ G-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003515; AAF49078.2; -. DR EMBL; AY060955; AAL28503.1; ALT_INIT. DR EMBL; AY118666; AAM50035.1; ALT_INIT. DR HSSP; P15116; 1NCI. DR FlyBase; FBgn0036930; fat2. DR GO; GO:0005887; C:integral to plasma membrane; ISS. DR GO; GO:0008014; F:calcium-dependent cell adhesion molecule ac...; ISS. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion; ISS. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006210; IEGF. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF00028; cadherin; 31. DR Pfam; PF00008; EGF; 5. DR Pfam; PF00054; laminin_G; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 34. DR SMART; SM00181; EGF; 6. DR SMART; SM00282; LamG; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS00232; CADHERIN_1; 18. DR PROSITE; PS50268; CADHERIN_2; 34. DR PROSITE; PS00022; EGF_1; 5. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 5. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS50025; LAM_G_DOMAIN; 1. KW Hypothetical protein; Cell adhesion; Signal; Glycoprotein; KW Transmembrane; Calcium; Calcium-binding; Repeat; EGF-like domain. FT SIGNAL 1 35 POTENTIAL. FT CHAIN 36 4705 PUTATIVE FAT-LIKE CADHERIN-RELATED TUMOR FT SUPPRESSOR HOMOLOG. FT DOMAIN 36 1647 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1648 1668 POTENTIAL. FT DOMAIN 1669 4705 CYTOPLASMIC (POTENTIAL). FT DOMAIN 60 180 CADHERIN 1. FT DOMAIN 181 288 CADHERIN 2. FT DOMAIN 285 397 CADHERIN 3. FT DOMAIN 398 504 CADHERIN 4. FT DOMAIN 505 610 CADHERIN 5. FT DOMAIN 611 713 CADHERIN 6. FT DOMAIN 770 874 CADHERIN 7. FT DOMAIN 875 977 CADHERIN 8. FT DOMAIN 978 1085 CADHERIN 9. FT DOMAIN 1086 1195 CADHERIN 10. FT DOMAIN 1191 1296 CADHERIN 11. FT DOMAIN 1297 1402 CADHERIN 12. FT DOMAIN 1405 1503 CADHERIN 13. FT DOMAIN 1504 1609 CADHERIN 14. FT DOMAIN 1610 1714 CADHERIN 15. FT DOMAIN 1715 1812 CADHERIN 16. FT DOMAIN 1813 1929 CADHERIN 17. FT DOMAIN 1930 2030 CADHERIN 18. FT DOMAIN 2031 2137 CADHERIN 19. FT DOMAIN 2138 2238 CADHERIN 20. FT DOMAIN 2239 2338 CADHERIN 21. FT DOMAIN 2339 2465 CADHERIN 22. FT DOMAIN 2466 2567 CADHERIN 23. FT DOMAIN 2568 2670 CADHERIN 24. FT DOMAIN 2671 2779 CADHERIN 25. FT DOMAIN 2780 2876 CADHERIN 26. FT DOMAIN 2877 2983 CADHERIN 27. FT DOMAIN 2984 3088 CADHERIN 28. FT DOMAIN 3084 3185 CADHERIN 29. FT DOMAIN 3186 3289 CADHERIN 30. FT DOMAIN 3290 3394 CADHERIN 31. FT DOMAIN 3395 3499 CADHERIN 32. FT DOMAIN 3500 3604 CADHERIN 33. FT DOMAIN 3605 3712 CADHERIN 34. FT DOMAIN 3819 3879 EGF-LIKE 1. FT DOMAIN 3881 3919 EGF-LIKE 2. FT DOMAIN 3937 4121 LAMININ G-LIKE. FT DOMAIN 4129 4166 EGF-LIKE 3. FT DOMAIN 4168 4205 EGF-LIKE 4. FT DOMAIN 4243 4279 EGF-LIKE 5. FT DISULFID 3823 3835 POTENTIAL. FT DISULFID 3830 3867 POTENTIAL. FT DISULFID 3869 3878 POTENTIAL. FT DISULFID 3885 3896 POTENTIAL. FT DISULFID 3890 3907 POTENTIAL. FT DISULFID 3909 3918 POTENTIAL. FT DISULFID 4133 4144 POTENTIAL. FT DISULFID 4138 4154 POTENTIAL. FT DISULFID 4156 4165 POTENTIAL. FT DISULFID 4172 4183 POTENTIAL. FT DISULFID 4177 4193 POTENTIAL. FT DISULFID 4195 4204 POTENTIAL. FT DISULFID 4247 4258 POTENTIAL. FT DISULFID 4252 4267 POTENTIAL. FT DISULFID 4269 4278 POTENTIAL. FT CARBOHYD 65 65 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 156 156 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 364 364 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 779 779 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 843 843 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 923 923 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1106 1106 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1198 1198 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1312 1312 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1439 1439 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1473 1473 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1511 1511 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 3962 3962 G -> E (IN REF. 3; AAL28503). SQ SEQUENCE 4705 AA; 524564 MW; 6D387A489D2C33DE CRC64; MKIKKYVTPV KRKAFTILQW ISLLCSLWLI PTVQSKADEK HTATLEYRLE NQLQDLYRFS HSVYNVTIPE NSLGKTYAKG VLHERLAGLR VGLNAEVKYR IISGDKEKLF KAEEKLVGDF AFLAIRTRTN NVVLNREKTE EYVIRVKAHV HLHDRNVSSY ETEANIHIKV LDRNDLSPLF YPTQYTVVIP EDTPKYQSIL KVTADDADLG INGEIYYSLL MDSEYFAIHP TTGEITLLQQ LQYAENSHFE LTVVAYDRGS WVNHQNHQAS KTKVSISVKQ VNFYAPEIFT KTFSSVTPTS NPLIYGIVRV NDKDTGINGN IGRLEIVDGN PDGTFLLKAA ETKDEYYIEL NQFAHLNQQH FIYNLTLLAE DLGTPRRFAY KSVPIQIKPE SKNIPIFTQE IYEVSIPETA PINMPVIRLK VSDPDLGKNA LVYLEIVGGN EGDEFRINPD SGMLYTAKQL DAEKKSSYTL TVSAIDQANV GSRKQSSAKV KISVQDMNDN DPIFENVNKV ISINENNLAG SFVVKLTAKD RDSGENSYIS YSIANLNAVP FEIDHFSGIV KTTSLLDFET MKRNYELIIR ASDWGLPYRR QTEIKLSIVV KDINDNRPQF ERVNCYGKVT KSAPMGTEVF VTSAIDFDAG DIISYRLSDG NEDGCFNLDP TSGSLSISCD LKKTTLTNRI LKVSATDGTH FSDDLIINVH LMPEDLGGDS SILHGFGSFE CRETGVARRL AETLSLAEKN NVKSASPSVF SDLSLTPSRY GQNVHRPEFV NFPQELSINE SVQLGETVAW IEAKDRDLGY NGKLVFAISD GDYDSVFRID PDRGELQIIG YLDRERQNEY VLNITVYDLG NPTKSTSKML PITILDVNDN RPVIQKTLAT FRLTESARIG TVVHCLHATD ADSGINAQVT YALSVECSDF TVNATTGCLR LNKPLDREKQ DNYALHITAK DGGSPVLSSE ALVYVLVDDV NDNAPVFGVQ EYIFKVREDL PRGTVLAVIE AVDEDIGPNA EIQFSLKEET QDEELFRIDK HTGAIRTQGY LDYENKQVHN LIVSAIDGGD PSLTSDMSIV IMIIDVNENR FAPEFDDFVY EGKVKENKPK GTFVMNVTAR DMDTVDLNSK ITYSITGGDG LGIFAVNDQG SITSLSQLDA ETKNFYWLTL CAQDCAIVPL SNCVEVYIQV ENENDNIPLT DKPVYYVNVT EASVENVEII TLKAFDPDID PTQTITYNIV SGNLVGYFEI DSKTGVIKTT ERKLDRENQA EHILEVAISD NGSPVLSSTS RIVVSVLDIN DNSPEFDQRV YKVQVPSSAT VNQSIFQVHA IDSDSGENGR ITYSIKSGKG KNKFRIDSQR GHIHIAKPLD SDNEFEIHIK AEDNGIPKKS QTARVNIVVV PVNPNSQNAP LIVRKTSENV VDLTENDKPG FLVTQILAVD DDNDQLWYNI SNGNDDNTFY IGQDNGNILL SKYLDYETQQ SYNLTISVTD GTFTAFTNLL VQVIDINDNP PQFAKDVYHV NISENIEEES VIMQLHATDR DEDKKLFYHL HATQDPSSLA LFRIDSISGN VIVTQRLDFE KTAQHILIVF VKDQGAPGKR NYAKIIVNVH DHNDHHPEFT AKIIQSKVPE SAAIGSKLAE VRAIDRDSGH NAEIQYSIIT GNVGSVFEID PTFGIITLAG NLNINKIQEY MLQVKAVDLG NPPLSSQIPV HIIVTMSEND PPKFPTNNIA IEIFENLPIG TFVTQVTARS SSSIFFNIIS GNINESFRIN PSTGVIVING NIDYESIKVF NLTVKGTNMA AESSCQNIII HILDANDNIP YFVQNEYVGA LPESAAIGSY VLKVHDSSKD HLTLQVKDAD VGVNGMVEYH IVDDLAKNFF KIDSTTGAIE LLRQLDYETN AGYTFDVTVS DMGKPKLHST TTAHVTIRVI NVNDCPPVFN ERELNVTLFL PTFENVFVRQ VSAKDADNDT LRFDIVDGNT NECFQIEKYT GIITTRNFEI LNNENDRDYA LHVRASDGIF SAILIVKIKV LSAIDSNFAF QRESYRFSAF ENNTKVATIG LVNVIGNTLD ENVEYRILNP TQLFDIGISS GALKTTGVIF DREVKDLYRL FVEAKSMLYD GMNSNVRRAV TSIDISVLDV NDNCPLFVNM PYYATVSIDD PKGTIIMQVK AIDLDSAENG EVRYELKKGN GELFKLDRKS GELSIKQHVE GHNRNYELTV AAYDGAITPC SSEAPLQVKV IDRSMPVFEK QFYTVSVKED VEMYSALSVS IEAESPLGRS LIYTISSESQ SFEIDYNTGS IFVVNELDYE KISSHDVSIR ATDSLSGVYA EVVLSVSIMD VNDCYPEIES DIYNLTIPEN ASFGTQILKI NATDNDSGAN AKLSYYIESI NGQNNSELFY IDVTDGNLYL KTPLDYEQIK YHHIVVNVKD HGSPSLSSRS NVFITGRILC RFISYKLIYD SIIPVKDLND NAPCFVEPSY FTKVSVAAVR GQFVALPKAY DKDISDTDSL EYKIVYGNEL QTYSIDKLTG VISLQNMLNF TDKSSTVLNI SVSDGVHTAY ARLKISLLPE NVYSPLFDQS TYEAQVPENL LHGHNIITVK ASDGDFGTYA NLYYEIVSEE MKKIFLIDQT TGVITSKVTF DREKKDEYVV LLKVSDGGGK FGFASLKVIV VDVNDNVPYF LLKEYKMVVS TTVEANQTIL TVKAKDDDIV DNGSVHFQIV QKSNDKAVKD VIEINEKTGD IVFKSKAESY GVNSYQFFVR ASDRGEPQFH SEVPVSIEII ETDANIPTFE KSSVLLKIIE STPPGTVLTK LHMIGNYTFK FSIAADQDHF MISDSGELIL QQTLDREQQE SHNLIVVAET STVPVFFAYA DVLIDVRDEN DNYPKFDNTF YSASVAENSE KVISLVKVSA TDADTGPNGD IRYYLESDTE NIQNIFDIDI YSGWITLLTS LDREVQSEYN FKVIAADNGH PKHDAKVPVT IKIVDYNDNA PVFKLPIEGL SVFENALPGT VLINLLLIDP DIEKQEMDFF IVSGDKQAQF QIGKSGELFI AKPLDREQLM FYNLSIIATD GKFTAKANVE IDVKDINDNT PYCLKPRYHI STNESISIGT TLVEVKAIDF DFQSKLRFYL SGKGADDFSI GKESGILKVA SALDRETTPK YKLVAHVQDG KDFTQECFSE IIITVNDIND NMPIFSMAQY RVSVPEDAQL NTLITKVHAM DKDFGVNRQI KYSLMGENHD YFKISKSTGI IRLHKSLDRE TISLFNLTVK AEDCGVPKLH SIATVAVNIL DINDNPPEFS MRQYSCKILE NATHGTEVCK VYATSIDIGV NADIHYFIMS GNEQGKFKMD STTGDLVLNA TLDYEMSKFY FLTIQAIDGG TPPLSNNAYV NISILDINDN SPTFLQNLYR INVNEDIFVG SKILDVKATD EDSDVNGLVT YNIERGDNIG QFSIDPKNGT ISVSRPLDRE TISHYTLEIQ ACDQGDPQRC NSVPININIL DTNDNAPIFS SSNYSVVLQE NRLLGYVFLT FKISDADETP NTTPYTFDIR SGNEGGLFRL EQDGSLRTAS RFNHNLQDEF VIQVRVFDNG TPPLYSDAWV VVKIIEESQY PPIVTPLEVT INSFEDDFSG AFIGKVHASD QDKYDELNFS LVSGPDDMYQ SSKLFNISNN TGKIYAISNL DIGLYKLNVS VSDGKFHVFS IVKINVELVT NDMLKESVVI RFRRISASEF LLSHRKTFMR SIRNIMRCRQ KDVILITLQS DYQKASQHAV GNRRARSIDS DLNVVFAVRK QQIIPDSDEF FTSDEIRQTL IDKKNEIENE TNLVVEDVLP STCQSNKNDC VHGECKQILQ ILKNNVTTTF TDVISFAAPS YIPVNTCVCR PGFDGKHCKE TVNACSTDPC SPQRICMPSG SALGYQCVCP KGFSGTYCER KSSKCSNESC DMGLFTAVSF GGKSYAHYKI NKVKAKFTLE NGFSYSLQIR TVQQTGTLLY ASGKVDYNIL EIINGAVQYR FDLGSGEGVI SVSSINISDG EWHQISLERS LNSAKVMVDN KHVSHGSAPG VNGILNIQSN DIFVGAEVRP HPSIIGYEDI QRGFIGCMAN IKIAKESLPL YISGGSTIAA LKRFTNVEFK CDPSNVLVRL GICGSQPCAN SGICKELDTD VFECACQPRY SGKHCEIDLD PCSSGPCLFG GRCDYHGPNN YSCTCPIHLS GKRCEYGKFC TPNPCKNGGI CEEGDGISHC MCRGYTGPTC EIDVDECENQ PCGNGATCIN EPGSFRCICP SYLTGASCGD PLYSNSISTK LKNFSIEHIS GIISGVAVVL VIISCVLCCV VLKRSSSSKR RNRLEKDKNK SSYKEANLNS LVDKDNYCKP NVKLSNLEVN QRPISYTAVP NDNLVLSNRN FVNNLDILRS YGSAGDELEN VPFEYQKVNR NKQHVNINSC HSTDADNAYK QEWCEQMHLR TFSENKLNNE LKRDFGPSVS RFSTGKLIQV EMPNVCHSSS ANFVDYSALA NGQYHWDCSD WVRKSHNPLP DITEVPGAEI ADSSSLHSND SNESKSKKAF FVHREDGDVD PTRDIAALNE DIGSEYLDSE AESCLEPFML PRSSNQPLSR LSSFNNIENE DYKSNTGKVY LRHPDSYLPT MHFPSETDGE SSMTEGPISR MEIKTRRTIS ENSEEAYLFP CTVGEIGSNS NISVRLCEIE DSELEEFLPQ QQTNN // ID FAT_DROME STANDARD; PRT; 5147 AA. AC P33450; Q9VQX5; DT 01-FEB-1994 (Rel. 28, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cadherin-related tumor suppressor precursor (Fat protein). GN FT OR CG3352. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92069752; PubMed=1959133; RA Mahoney P.A., Weber U., Onofrechuk P., Biessmann H., Bryant P.J., RA Goodman C.S.; RT "The fat tumor suppressor gene in Drosophila encodes a novel member RT of the cadherin gene superfamily."; RL Cell 67:853-868(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COULD FUNCTION AS A CELL-ADHESION PROTEIN. ACTS AS A CC TUMOR SUPPRESSOR. REQUIRED FOR CORRECT MORPHOGENESIS. CC -!- SIMILARITY: CONTAINS 34 CADHERIN DOMAINS. CC -!- SIMILARITY: CONTAINS 5 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 2 LAMININ G-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M80537; AAA28530.1; -. DR EMBL; AE003577; AAF51036.1; -. DR HSSP; P00740; 1EDM. DR FlyBase; FBgn0001075; ft. DR GO; GO:0005887; C:integral to plasma membrane; NAS. DR GO; GO:0008014; F:calcium-dependent cell adhesion molecule ac...; NAS. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion; NAS. DR GO; GO:0008283; P:cell proliferation; IMP. DR GO; GO:0000904; P:cellular morphogenesis during differentiation; IMP. DR GO; GO:0045317; P:equator specification; IMP. DR GO; GO:0045198; P:establishment of epithelial cell polarity; IMP. DR GO; GO:0007446; P:imaginal disc growth; IMP. DR GO; GO:0018149; P:protein-protein cross-linking; IPI. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006210; IEGF. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF00028; cadherin; 34. DR Pfam; PF00008; EGF; 4. DR Pfam; PF00054; laminin_G; 2. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 34. DR SMART; SM00181; EGF; 4. DR SMART; SM00282; LamG; 2. DR PROSITE; PS00232; CADHERIN_1; 22. DR PROSITE; PS50268; CADHERIN_2; 34. DR PROSITE; PS00022; EGF_1; 4. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 4. DR PROSITE; PS50025; LAM_G_DOMAIN; 2. KW Cell adhesion; Signal; Transmembrane; Glycoprotein; Calcium-binding; KW Repeat; EGF-like domain. FT SIGNAL 1 35 POTENTIAL. FT CHAIN 36 5147 CADHERIN-RELATED TUMOR SUPPRESSOR. FT DOMAIN 36 4583 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 4584 4609 POTENTIAL. FT DOMAIN 4610 5147 CYTOPLASMIC (POTENTIAL). FT DOMAIN 36 156 CADHERIN 1. FT DOMAIN 157 270 CADHERIN 2. FT DOMAIN 271 382 CADHERIN 3. FT DOMAIN 383 494 CADHERIN 4. FT DOMAIN 495 599 CADHERIN 5. FT DOMAIN 600 708 CADHERIN 6. FT DOMAIN 709 820 CADHERIN 7. FT DOMAIN 821 942 CADHERIN 8. FT DOMAIN 943 1049 CADHERIN 9. FT DOMAIN 1050 1153 CADHERIN 10. FT DOMAIN 1154 1278 CADHERIN 11. FT DOMAIN 1279 1384 CADHERIN 12. FT DOMAIN 1385 1489 CADHERIN 13. FT DOMAIN 1490 1601 CADHERIN 14. FT DOMAIN 1602 1713 CADHERIN 15. FT DOMAIN 1714 1823 CADHERIN 16. FT DOMAIN 1824 1922 CADHERIN 17. FT DOMAIN 1923 2027 CADHERIN 18. FT DOMAIN 2028 2167 CADHERIN 19. FT DOMAIN 2168 2278 CADHERIN 20. FT DOMAIN 2279 2385 CADHERIN 21. FT DOMAIN 2386 2491 CADHERIN 22. FT DOMAIN 2492 2596 CADHERIN 23. FT DOMAIN 2597 2703 CADHERIN 24. FT DOMAIN 2704 2810 CADHERIN 25. FT DOMAIN 2811 2913 CADHERIN 26. FT DOMAIN 2914 3013 CADHERIN 27. FT DOMAIN 3014 3124 CADHERIN 28. FT DOMAIN 3125 3229 CADHERIN 29. FT DOMAIN 3230 3334 CADHERIN 30. FT DOMAIN 3335 3439 CADHERIN 31. FT DOMAIN 3440 3545 CADHERIN 32. FT DOMAIN 3546 3651 CADHERIN 33. FT DOMAIN 3652 3756 CADHERIN 34. FT DOMAIN 3950 4011 EGF-LIKE 1. FT DOMAIN 4013 4049 EGF-LIKE 2. FT DOMAIN 4052 4090 EGF-LIKE 3. FT DOMAIN 4092 4128 EGF-LIKE 4. FT DOMAIN 4129 4320 LAMININ G-LIKE 1. FT DOMAIN 4321 4362 EGF-LIKE 5. FT DOMAIN 4402 4569 LAMININ G-LIKE 2. FT DISULFID 3954 3966 BY SIMILARITY. FT DISULFID 3960 3999 BY SIMILARITY. FT DISULFID 4001 4010 BY SIMILARITY. FT DISULFID 4017 4028 BY SIMILARITY. FT DISULFID 4022 4037 BY SIMILARITY. FT DISULFID 4039 4048 BY SIMILARITY. FT DISULFID 4056 4067 BY SIMILARITY. FT DISULFID 4061 4078 BY SIMILARITY. FT DISULFID 4080 4089 BY SIMILARITY. FT DISULFID 4096 4107 BY SIMILARITY. FT DISULFID 4101 4116 BY SIMILARITY. FT DISULFID 4118 4127 BY SIMILARITY. FT DISULFID 4325 4341 BY SIMILARITY. FT DISULFID 4334 4350 BY SIMILARITY. FT DISULFID 4352 4361 BY SIMILARITY. FT CARBOHYD 239 239 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 257 257 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 276 276 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 280 280 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 402 402 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 461 461 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 605 605 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 631 631 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1155 1155 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1367 1367 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1458 1458 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1751 1751 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1831 1831 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1880 1880 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2080 2080 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2171 2171 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2247 2247 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2290 2290 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2437 2437 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2581 2581 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2799 2799 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2920 2920 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2946 2946 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2967 2967 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3167 3167 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3303 3303 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3386 3386 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3389 3389 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3525 3525 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3852 3852 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3865 3865 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3905 3905 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4306 4306 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4414 4414 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4471 4471 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4487 4487 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4539 4539 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4550 4550 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 1229 1229 S -> G. FT VARIANT 1233 1233 G -> S. FT CONFLICT 676 676 S -> P (IN REF. 1). FT CONFLICT 718 718 A -> T (IN REF. 1). FT CONFLICT 889 889 T -> S (IN REF. 1). FT CONFLICT 1298 1298 T -> M (IN REF. 1). FT CONFLICT 1338 1338 G -> A (IN REF. 1). FT CONFLICT 1366 1366 S -> T (IN REF. 1). FT CONFLICT 1408 1408 A -> G (IN REF. 1). FT CONFLICT 1755 1755 T -> V (IN REF. 1). FT CONFLICT 2168 2168 I -> V (IN REF. 1). FT CONFLICT 2266 2266 I -> V (IN REF. 1). FT CONFLICT 2665 2665 H -> T (IN REF. 1). FT CONFLICT 2712 2712 A -> T (IN REF. 1). FT CONFLICT 2816 2816 N -> T (IN REF. 1). FT CONFLICT 2893 2893 M -> L (IN REF. 1). FT CONFLICT 3359 3359 A -> T (IN REF. 1). FT CONFLICT 3674 3674 I -> M (IN REF. 1). FT CONFLICT 3722 3722 I -> V (IN REF. 1). FT CONFLICT 3869 3869 Y -> N (IN REF. 1). FT CONFLICT 4187 4187 G -> D (IN REF. 1). FT CONFLICT 4309 4309 L -> S (IN REF. 1). SQ SEQUENCE 5147 AA; 564776 MW; 6A5A4743FC7E07D0 CRC64; MERLLLLFFL LLAGRESLCQ TGDTKLELLA PRGRSYATTY EQYAAFPRRR SSSSSPSGEM QSRAVDTSAD FEVLEGQPRG TTVGFIPTKP KFSYRFNEPP REFTLDPVTG EVKTNVVLDR EGMRDHYDLV VLSSQPTYPI EVRIKVLDVN DNSPEFPEPS IAISFSESAT SGTRLLLDAA TDADVGENGV TDQYEIVAGN VDNKFRLVTT ANPSGDTSYL HLETTGNLDR ESRGSYQLNI SARDGGSPPR FGYLQVNVTI LDVNDNPPIF DHSDYNVSLN ETALPGTPVV TVMASDNDLG DNSKITYYLA ETEHQFTVNP ETGVISTTER VNCPQQTNVK SSASQKSCVF TVFARDHGSP RQDGRTYVTV NLLDTNDHDP IISFRFFPDG GKVATVDENA VNGTVVAAVA VKDSDSGLNG RTSVRIVSGN ELGHFRLEEA ADLHIVRVNG VLDREEIGKY NLTVVAMDQG TPARTTTAHL IIDVNDVNDH EPVFEKSEYS AVLSELAPTG SFVASITATD EDTGVNAQVH YDILSGNELK WFSMDPLTGL IVTTGPLDRE IRDTVELSIS ARDGGPNPKF AYTQLKVIIL DENDEAPQFS QREQNVTLGE DAPPQTIVAL MTATDHDQGT NGSVTFALAP SVERLYPLQF ALDALTGQLT TRRPLDREKM SQYEISVIAR DQGAPTPQSA TATVWLNVAD VNDNDPQFYP RHYIYSLADD DDDIKLKKEV EKERILLHVT ASDKDDGDNA LIEYRLESGG EGLFQLDARS GAISLRGDAP ASMHWKPHYK LLVSARDAGQ RRSQQDAIVE IVLKSKLEML ECGQAQAGGY EFQMVEDHEQ QRNSQPNREV GIVQVKSTNG KANSHIEYDI IQGDRAQNFR IDTRSGRITT ARPLDREEQA NYRLTILASS SSSSSAAASS VSYGQCIVNI AIIDLNDNAP VFALDRESEP TISLPENAAV GQEIYLSRVR DRDAGVNSRI SYSLTNNPNQ QFRIGPVTGV LYLQRPIRAE PGSLIHVELM ATDAGSPPLS SKLSLSVLIA DVNDHTPVFD HTSYETSLPE TTKVNTRFFA LAATDIDLGD NGRISYEIIE GNTERMFGVF PDGYLFVRAP LDREERDYYA LTVSCRDAGQ PSRSSVVPVV IHVIDENDNA PQFTNSTFTF SIPENAPADT FVGKLTAVDR DIGRNAELSF TLSSQTQDFT IDTRNGFIKT LRPFDREALV KVSRNAEASG EDGSLRGSMA GNYMLLEATV SDNGIPRLQD KVKVKVIVTD VNDNAPEFLR APYHVTISEG ASEGTHITHV FTQDADEGLN GDVYYSLAKG NEAGQFNLDS ATGQLSLGRR LDRESQEIHH LIVVAKDAAL KHPLSSNASI TIVVLDENDN APEFTQSSSE VSVLETSPTG TELMRFRASD ADQGVNSQVV FSISAGNRRD TFHIDSITGS LYLHKPLDYE DITSYTLNIT ASDCGTPSLS TTVLYNVLVV DDNDNPPIFP STAIVRQIKE GIPLKTPIVT VTADDPDSGL NGKVSYAISK QEPQLPQGRH FGINTETGVI HTLREIDRES IDTFRLTVVA TDRAQPSERQ LSTEKLVTVI VEDINDNAPV FVSMNAAILP PKFSTSKGSS TAVMQVHAKD ADSSSNGLVT YEIVSGPQEL FKLQRNTGII TFTPGPQFKQ EVRYQLTLKS TDEAVQSERR SSEVYITIIT PGSGGSESSV PQFEQRSKLS GSVYENEPIG TSILTVTAHL ASAEIEYFVT NVTATGSRGQ VDRLFDIDAK LGILSTAAEL DREAGPEEYE VEVYAIALGG QPRTSRTKVR VTVLDKNDSP PQFLDTPFVY NVSEDLQIGH TISTLRAHDP DTLGSVTFLL MDGHDGKFLL EPSTGKLILN DTLDRETKSK YELRIRVSDG VQYTEAYATI QVSDTNDNPP LFEDTVYSFD IPENAQRGYQ VGQIVARDAD LGQNAQLSYG VVSDWANDVF SLNPQTGMLT LTARLDYEEV QHYILIVQAQ DNGQPSLSTT ITVYCNVLDL NDNAPIFDPM SYSSEVFENV PIATEVVTVS AKDIDSGNNG LIEYSITAGD VDSEFGIDSN GTIRTRRNLD REHRSTYTLT VTARDCADEF ASFSELEETQ LKLKYRSPRK YQQTRQEFLA HQKQQRLSST VKVTILIKDV NDEVPVFISA NETAIMENVA INTVVIAVKA VDNDEGRNGY IDYLMKEARD EDMGQSDPLP FSLNPTDGQL RVVDALDREL RSSYLLNITA RDRGEPPQST ESQLLIRILD ENDNSPVFDP KQYSASVAEN ASIGAMVLQV SATDVDEGAN GRIRYSIVLG DQNHDFSISE DTGVVRVAKN LNYERLSRYS LTVRAEDCAL ENPAGDTAEL TINILDINDN RPTFLDSPYL ARVMENTVPP NGGYVLTVNA YDADTPPLNS QVRYFLKEGD SDLFRINASS GDIALLKPLD REQQSEYTLT LVAMDTGSPP LTGTGIVRVE VQDINDNDPV FELQSYHATV RENLPSGTHV LTPRATDKDE GLNAKLRFNL LGEHMHRFHI DSETGEISTA TTLDREETSV YHLTLMAQDS SITEPRASSV NLTISVSDVN DNIPKFDSTT YNVAVPERIS KGEFVFGARA LDLDDGENAV VHYTISGRDQ HYFDINTKTG VVSTKLELKT KTKSHDDLTY TIVISAMDQG EQSLSSKAEL TVILRPPELF PTFAYMANSH FAMSEDVRPG KMITKVSATS PKKGLVGKIR YAIAGGIMGD SLRVDPNSGL LSVGQDGLDY ELTHLYEIWI EAADGDTPSL RSVTLITLNV TDANDNAPVM EQLIYNAEVL EEESPPQLIA VVKASDRDSG DNGNVIYRLQ NDFDGTFEIT ESGEIYTRMR LDREEIGDYA FVVEAVDQGV PHMTGTASVL LHLLDKNDNP PKFTRLFSLN VTENAEIGSF VIRVTSSDLD LGANANASYS FSENPGEKFR IEPQSGNITV AGHLDREQQD EYILKVVASD GAWRAETPIT ITIQDQNDNA PEFEHSFYSF SFPELQQSIA LVGQIIATDR DKQGPNSVIS YSLQQPSPMF SIDPATGEVF SKKAVRFKHS QYVRSPENMY ALTVLATDNG KPPLYSECLV NINIVDAHNN PPKFEQAEYL APLPQDAVRG QRIVRVHAND KQDLGTNEMD YSLMTFNLSS IFSVGRHDGW ITLVKPIQVP PNTRYELVVR ATDRGVPPQS DETRVVIVVT GENMDTPRFS VNSYQVIVPE NEPVGSTILT VGATDDDTGP NGMLRYSISG GNERQDFSVD ERTGGIVIQQ QLDYDLIQEY HLNITVQDLG YHPLSSVAML TIILTDVNDN PPVFNHKEYH CYIPENKPVG TFVFQAHAAD KDSPKNAIIH YAFLPSGPDR HFFIMNQSNG TISSAVSFDY EERRIYTLQI KAKNPDSSME SYANLYVHVL GVNEFYPQFL QPVFHFDVSE TSAVGTRVGA VQATDKDSGE DGRVYYLLVG SSNDKGFRID TNTGLIYVAR HLDRETQNRV VLTVMAKNYG SIRGNDTDEA QVIISIQDGN DPPEFIKHYY TSTISEAAPV GTKVTTVKAI DKDVRTQNNQ FSYSIINGNL KQSFKIDVQT GEISTASRLD REETSTYNLV IGAIDTGLPP QTGSATVHIE LEDVNDNGPT FTPEGLNGYI SENEPAGTSI MTLIASDPDL PRNGGPFTYQ LIGGKHKSWL SVDRNSGVVR STTSFDREMT PILEAIIEVE DSGKPKQKSQ HLLTITVLDQ NDNPSTTRSL HIAVSLFNGD LPSNVKLADV RPNDIDIVGD YRCRLQKNPA QSQLQLAIPR ACDLITTSHT TPIASVFSYT GNDGKHGDVS SKVSVAFQSF NNETLANSVS IMVRNMTAYH FLANHYRPIL EMIKSRMSNE DEVILYSLLE GGSGNSTNLQ LLMAVRLAKT SYQQPKYLIE RLREKRSAFS ELLQKEVIVG YEPCSEPDVC ENGGVCSATM RLLDAHSFVI QDSPALVLSG PRVVHDYSCQ CTSGFSGEQC SRRQDPCLPN PCHSQVQCRR LGSDFQCMCP ANRDGKHCEK ERSDVCYSKP CRNGGSCQRS PDGSSYFCLC RPGFRGNQCE SVSDSCRPNP CLHGGLCVSL KPGYKCNCTP GRYGRHCERF SYGFQPLSYM TFPALDVTTN DISIVFATTK PNSLLLYNYG MQSGGRSDFL AIELVHGRAY FSSGGARTAI STVIAGRNLA DGGWHKVTAT RNGRVMSLSV AKCADSGDVC TECLPGDSSC YADEVGPVGT LNFNKQPLMI GGLSSADPIL ERPGQVHSDD LVGCLHSVHI GGRALNLSLP LQQKGILAGC NRQACQPALA AERCGGFAGQ CIDRWSSSLC QCGGHLQSPD CSDSLEPITL GEGAFVEFRI SEIYRRMQLL DNLYNSKSAW LDNQQMRERR AVSNFSTASQ IYEAPKMLSM LFRTYKDQGQ ILYAATNQMF TSLSLREGRL VYYSKQHLTI NMTVQETSTL NDGKWHNVSL FSESRSLRLI VDGRQVGDEL DIAGVHDFLD PYLTILNVGG EAFVGCLANV TVNNELQPLN GSGSIFPEVR YHGKIESGCR GDIGQDAAQV ADPLSIGFTL VIVFFVILVV AILGSYVIYR FRGKQEKIGS LSCGVPGFKI KHPGGPVTQS QVDHVLVRNL HPSEAPSPPV GAGDHMRPPV GSHHLVGPEL LTKKFKEPTA EMPQPQQQQQ RPQRPDIIER ESPLIREDHH LPIPPLHPLP LEHASSVDMG SEYPEHYDLE NASSIAPSDI DIVYHYKGYR EAAGLRKYKA SVPPVSAYTH HKHQNSGSQQ QQQQHRHTAP FVTRNQGGQP PPPPTSASRT HQSTPLARLS PSSELSSQQP RILTLHDISG KPLQSALLAT TSSSGGVGKD VHSNSERSLN SPVMSQLSGQ SSSASRQKPG VPQQQAQQTS MGLTAEEIER LNGRPRTCSL ISTLDAVSSS SEAPRVSSSA LHMSLGGDVD AHSSTSTDES GNDSFTCSEI EYDNNSLSGD GKYSTSKSLL DGRSPVSRAL SGGETSRNPP TTVVKTPPIP PHAYDGFESS FRGSLSTLVA SDDDIANHLS GIYRKANGAA SPSATTLGWE YLLNWGPSYE NLMGVFKDIA ELPDTNGPSQ QQQQQTQVVS TLRMPSSNGP AAPEEYV // ID FAU_DROME STANDARD; PRT; 668 AA. AC Q9VGX3; Q95S18; Q9VGX1; Q9VGX2; Q9Y0F9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Anoxia upregulated protein. GN FAU OR CG6544. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=99097004; PubMed=9878744; RA Ma E., Xu T., Haddad G.G.; RT "Gene regulation by O2 deprivation: an anoxia-regulated novel gene in RT Drosophila melanogaster."; RL Brain Res. Mol. Brain Res. 63:217-224(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM E). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PLAYS AN IMPORTANT ROLE IN THE REGULATION OF TISSUE CC RESPONSIVENESS TO OXYGEN DEPRIVATION. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=A; CC IsoId=Q9VGX3-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9VGX3-2; Sequence=VSP_004048, VSP_004049; CC Name=C; CC IsoId=Q9VGX3-3; Sequence=VSP_004046, VSP_004047; CC Name=D; CC IsoId=Q9VGX3-4; Sequence=VSP_004050, VSP_004051; CC Name=E; CC IsoId=Q9VGX3-5; Sequence=VSP_004052; CC -!- TISSUE SPECIFICITY: CONCENTRATED IN LAMINA NEURONS, FIRST OPTIC CC LOBE NEURONS AND CORTICAL NEURONS OF CENTRAL BRAIN. CC -!- INDUCTION: BY ANOXIA. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF154418; AAD38397.1; -. DR EMBL; AE003688; AAF54549.2; -. DR EMBL; AE003688; AAF54550.1; -. DR EMBL; AE003688; AAF54551.1; -. DR EMBL; AE003688; AAF54552.1; -. DR EMBL; AY060997; AAL28545.1; -. DR EMBL; AY119569; AAM50223.1; -. DR FlyBase; FBgn0020439; fau. DR GO; GO:0006979; P:response to oxidative stress; IDA. KW Alternative splicing. FT DOMAIN 88 143 THR-RICH. FT DOMAIN 354 668 ALA/GLU-RICH. FT VARSPLIC 26 131 YPSVEKVTRVYKSSYPIYSSYSVPRRVYGATRVVTSPIRVV FT TSPARVVSRVIHSPSPVRVVRTTTRVISSPERTTYSYTTPS FT TYYSPSYLPSTYTSTYIPTSYTTY -> TPRLDLCTDRPGS FT HRSRASSDYSYTSKSSVEKSSYDSSNPHSYRPERSTYTSTV FT EKTSRSGPGGSYNYSTERTSTTGAGPGGYSYSSTTSGNLPG FT GTKYRHFSYHV (in isoform C). FT /FTId=VSP_004046. FT VARSPLIC 132 668 Missing (in isoform C). FT /FTId=VSP_004047. FT VARSPLIC 26 163 YPSVEKVTRVYKSSYPIYSSYSVPRRVYGATRVVTSPIRVV FT TSPARVVSRVIHSPSPVRVVRTTTRVISSPERTTYSYTTPS FT TYYSPSYLPSTYTSTYIPTSYTTYTPSYAYSPTTVTRVYAP FT RSSLSPLRITPSPVR -> RTKRTPIDWEKVPFVPRPSLIS FT DPVTAFGVRRPDLERRQRSILDPINRASIKPDYKLAYEPIE FT PYVSTRDKNRTRILGMVRQHIDTVEAGGNTAGRTFRDSLDA FT QLPRLHRAVSESLPVRRETYRNERSGAMVTKYSY (in FT isoform B). FT /FTId=VSP_004048. FT VARSPLIC 164 668 Missing (in isoform B). FT /FTId=VSP_004049. FT VARSPLIC 36 98 YKSSYPIYSSYSVPRRVYGATRVVTSPIRVVTSPARVVSRV FT IHSPSPVRVVRTTTRVISSPER -> SIWFSSLSPTSLVII FT HLSMDYYYSFLLTYITHCSITSITSSSLEKQIRLVISPHII FT VLFRLKH (in isoform D). FT /FTId=VSP_004050. FT VARSPLIC 99 668 Missing (in isoform D). FT /FTId=VSP_004051. FT VARSPLIC 280 328 Missing (in isoform E). FT /FTId=VSP_004052. SQ SEQUENCE 668 AA; 74487 MW; 4507369593D1DD3B CRC64; MVYESGFTTR RTYSSRPVTT SYAVTYPSVE KVTRVYKSSY PIYSSYSVPR RVYGATRVVT SPIRVVTSPA RVVSRVIHSP SPVRVVRTTT RVISSPERTT YSYTTPSTYY SPSYLPSTYT STYIPTSYTT YTPSYAYSPT TVTRVYAPRS SLSPLRITPS PVRVITSPVR SVPSYLKRLP PGYGARALTN YLNTEPFTTF SEETSRIRNR AQSLIRDLHT PVVRRARSCT PFPVTGYTYE PASQLALDAY VARVTNPVRH IAKEVHNISH YPRPAVKYVV RICGDKAYNV RSPLYDTDKV RTDINLLSWY LRHPTWKNDK KSQDPVKEDA ELDPNRPSRK FSAPRPLEDP LDVEAKEKQR LRQERLLTVN EEALDEVDLE KKRAQKADEA KRREERALKE ERDRLTAEAE KQAAAKAKKA AEEAAKIAAE EALLAEAAAQ KAAEEAKALK AAEDAAQKAA EEARLAEEAA AQKVAEEAAQ KAAEEARLAE EAAAQKAAEE AAQKAAEEAA LKAAEEARLA EEAAQKAAEE AALKAVEEAR AAEEAAQKAA EEARVAEEAR LEEEQRVREQ ELERLAEIEK ESEGELARQA AELAEIARQE SELAAQELQA IQKNENETSE PVVEEPVTPV EEQEPIIELG SNVTPTGGNS YEEDLDAEEE EDEEEEEE // ID FBP1_DROME STANDARD; PRT; 1030 AA. AC Q04691; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Fat-body protein-1 precursor (P1 protein). GN FBP1 OR P1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Fat body; RX MEDLINE=90339481; PubMed=1696317; RA Maschat F., Dubertret M.-L., Therond P., Claverie J.-M., RA Lepesant J.-A.; RT "Structure of the ecdysone-inducible P1 gene of Drosophila RT melanogaster."; RL J. Mol. Biol. 214:359-372(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94123973; PubMed=8293980; RA Lapie P., Nasr F., Lepesant J.-A., Deutsch J.; RT "Deletion scanning of the regulatory sequences of the Fbp1 gene of RT Drosophila melanogaster using P transposase-induced deficiencies."; RL Genetics 135:801-816(1993). CC -!- TISSUE SPECIFICITY: FAT BODY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING THE LATE THIRD LARVAL CC STAGE. CC -!- INDUCTION: BY ECDYSONE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54997; CAA38744.1; -. DR EMBL; X69965; CAA49588.1; -. DR PIR; S11034; S11034. DR FlyBase; FBgn0000639; Fbp1. DR GO; GO:0008565; F:protein transporter activity; IPI. DR GO; GO:0015032; P:storage protein uptake; IPI. DR InterPro; IPR005203; hemocyanin_C. DR InterPro; IPR005204; hemocyanin_N. DR InterPro; IPR007110; Ig-like. DR Pfam; PF03723; hemocyanin_C; 1. DR Pfam; PF03722; hemocyanin_N; 1. KW Signal; Glycoprotein. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 1030 FAT-BODY PROTEIN-1. FT DOMAIN 360 371 POLY-ASP. FT DOMAIN 580 590 POLY-ASP. FT CARBOHYD 741 741 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1030 AA; 119365 MW; 63D7491229B0F9A8 CRC64; MNRIMLLVAF AAGVVAAGRI TTNQDRVQGI DRMSLEDLQL QKFILDIVQN IRQPLQQSEL INLDVGLIAD SQRYRGGIDK VMQNVIDLDR QRRLLDEHQV YSVGRLEHVQ QLRGIYRLLA RAQDLDTLRR NVVYLRRNIN PVLLVNALAL AIRDREDTQT LIVPAVQELL PELYLDEEVI QQVRSVLREQ TQRPSLMDIV GMRQRAMNPV MSILMPQREI HMQMALRKQQ NIQNVLGQKR VVVRAENQGQ VEGTSLLTDD IELQNFVQNL IQELALLEDV TQLEQSQLIN NDQREEQWVG RQRVQYQDNN RERDLGNDVD TGRPTPCESA AGLLEQQDEY QGQNIYGNQK DRFQRLLRRD DDNDDNDDDD DQDIRMGRVQ LQRGISQGGL RIGGARNLPT VSVNSDRLLH VSRRRLNAIQ QDQQQDQLNG RQRFMGLVRG DRLSEGRRVG QLDDVRQERQ NNWQKQDYIL TQGRTFGVQQ ERQNYADQLE SVSRDDERLV HINRRRLNQD NQDIQQQQMN FPRRINSIGE GRRRHGRAPI QDEDILKLIR GENRLKLMTD DEILEMLQRN RQQRLQKHQN DDDDDDNDDD VNVVHRQGLR SRRSLPNLRQ QNNRLSEIVL HNLRQLVARL NQESIAQGQL IEEQQQLINN PRLTQSERYA LRLNQIRINS QRSRQVLAQI GQIEQRIQEV IGQVLSQVNV NSLRGQVIDQ RQVESLIADV LLGRLGQVGI MTIIRQVVQD NNSEQIDRNG LGIRLSDPVV QYTLRRIVRI VDEQREQILG GYRQEQLQMR GVSINDVRVD KLRTRIEEHE LDLSNLVEQQ VQGIQQEIVG RQRRLNNKAF TIDMDITSDQ DQDAIIRIFL GPAEDQQGRQ GASLDERRRD FVLLDAIQVQ LENGRNRIQR RSIDIPWTTS DVTPLVEIYR QVMLQLKGQQ AQQVVGIQQL VGENGRFPQH LLLPRGRPEG LPMQLLVVVS PLVELQVQDI VPAITIGIGS ASLRDARPLG YPLDRPIHNE QELLQLTNVL LQDVVIIQEN // ID FBP2_DROME STANDARD; PRT; 256 AA. AC P54398; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fat body protein P6. GN FBP2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92015272; PubMed=1920455; RA Rat L., Veuille M., Lepesant J.-A.; RT "Drosophila fat body protein P6 and alcohol dehydrogenase are derived RT from a common ancestral protein."; RL J. Mol. Evol. 33:194-203(1991). CC -!- SIMILARITY: BELONGS TO THE SHORT-CHAIN DEHYDROGENASES/REDUCTASES CC (SDR) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S57693; AAB19930.1; -. DR FlyBase; FBgn0000640; Fbp2. DR InterPro; IPR002198; ADH_short. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; FALSE_NEG. KW Oxidoreductase. FT NP_BIND 10 34 NAD OR NADP (BY SIMILARITY). FT ACT_SITE 151 151 BY SIMILARITY. SQ SEQUENCE 256 AA; 29060 MW; 732413D1BBA5E086 CRC64; MFDWTGKNVV YVGSFSGIGW QMMMQLMQKD IKMMGIMHRM ENVEMMKKLQ AINPSVKVVF MQMNLMEKMS IEQAMKKMGQ MMGHIDVMIN GEGVLLDKDV ETTMGMNLTG MIQSTMMAMP YMDKTQMGMG GMVVNMSSVY GLEPAPAFSV YAAAMHGILG FTRSMGDKMI YQKTGVMFMA MCPGLTNSEM MMNLRDNVTW HHSESMVEAI ESAKRQMPEE AAMQMIHAME MMKNGSMWIV NMGQLKEVTP TMHWQM // ID FCL_DROME STANDARD; PRT; 321 AA. AC Q9W1X8; Q8MS16; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable GDP-L-fucose synthetase (EC 1.1.1.271) (FX protein) (GDP-4- DE keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase). GN GMER OR CG3495. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP HOMOLOGY. RX MEDLINE=21671316; PubMed=11698403; RA Roos C., Kolmer M., Mattila P., Renkonen R.; RT "Composition of Drosophila melanogaster proteome involved in RT fucosylated glycan metabolism."; RL J. Biol. Chem. 277:3168-3175(2002). CC -!- FUNCTION: TWO STEP NADP-DEPENDENT CONVERSION OF GDP-4-DEHYDRO-6- CC DEOXY-D-MANNOSE TO GDP-FUCOSE, INVOLVING AN EPIMERASE AND A CC REDUCTASE REACTION (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: GDP-L-FUCOSE + NADP(+) = GDP-4-DEHYDRO-6- CC DEOXY-D-MANNOSE + NADPH. CC -!- PATHWAY: CONVERSION OF GDP-MANNOSE TO GDP-FUCOSE; SECOND STEP. CC -!- PATHWAY: CONVERSION OF GDP-MANNOSE TO GDP-FUCOSE; THIRD (LAST) CC STEP. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FUCOSE SYNTHETASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003458; AAF46924.1; -. DR EMBL; AY060873; AAL28421.1; -. DR EMBL; AY119148; AAM51008.1; -. DR HSSP; P32055; 1BSV. DR FlyBase; FBgn0034794; Gmer. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-O...; ISS. DR GO; GO:0016857; F:racemase and epimerase activity, acting on ...; ISS. DR GO; GO:0006005; P:L-fucose biosynthesis; ISS. KW Isomerase; Oxidoreductase; NADP; Multifunctional enzyme. FT NP_BIND 3 32 NADP (POTENTIAL). FT CONFLICT 112 112 P -> R (IN REF. 2; AAM51008). SQ SEQUENCE 321 AA; 36123 MW; E4167CE378D2D8E5 CRC64; MKKVLVTGGT GLVGKALEAV IKEQSPEDEQ WFFAGSKDAD LTNLAATQAL FAREKPTHVI HLAAMVGGLF HNMNNNLDFL RNNLLINDNV LQTAHEQGCV KVVSCLSTCI FPDKTSYPID ETMVHNGPPH PSNYGYSYAK RLIDVQNHAY HDKYGRVYTS VIPCNIFGPH DNYNPEVSHV IPGMIYRMHQ LVTEKTDVPE NDKVFTVFGS GMPLRQFVYS RDLAELMIWV LRNYESVEPI ILSADEVQEV TIFEVAQAVA KAFNFNGRLV CDTSKSDGQY KKTASNAKLR SFLPDYAFTD LETAINASVK WYIENYDQAR K // ID FD2_DROME STANDARD; PRT; 365 AA. AC Q02360; Q9VZK0; DT 01-JUL-1993 (Rel. 26, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fork head domain protein FD2. GN FD64A OR FD2 OR CG1132. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 76-209 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=92409595; PubMed=1356269; RA Haecker U., Grossniklaus U., Gehring W.J., Jaeckle H.; RT "Developmentally regulated Drosophila gene family encoding the fork RT head domain."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8754-8758(1992). CC -!- FUNCTION: INVOLVED IN DEVELOPMENT DURING EMBRYOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN EMBRYONIC POSTERIOR MESODERM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN EMBRYOS, MAXIMAL LEVEL BETWEEN CC 5-12 HOURS. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003480; AAF47821.1; -. DR EMBL; M96441; AAA28533.1; -. DR PIR; B46178; B46178. DR HSSP; Q63245; 2HFH. DR FlyBase; FBgn0004895; fd64A. DR InterPro; IPR001766; TF_Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR ProDom; PD000425; TF_Fork_head; 1. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DNA_BIND 90 181 FORK-HEAD. SQ SEQUENCE 365 AA; 40635 MW; 4FCEF59A285FCA0F CRC64; MLPSCYANGS MLPDNEELVN SMLANPDYLR TQVSPNPLAP SAVGGAGMEG LMCGSFSPAF YYQGIDSFLA LHNNIWGLPI SFLHNSHRPE KPPFSYIALI AMAISSAPNQ RLTLSGIYKF IMDKFPYYRE NKQGWQNSIR HNLSLNDCFV KIPRDKNTIE DNDSAGKGSY WMLDSSASDM FEQGNYRRRR TRRQRHCGHP NRYERESGKD SNDGNSSAAE IRSPSEPLSD FDIFCNERPN YSDRITDLHR QYLSVSLGFN SLFNNEARGL RPLPEIRECP DDVDASSSSS KAMQSSMELH EELHSPSAFT PPLNRRETSS SGAPVLAEAF NGIKDVVDAP GSSPVASSNR SKTTLFTIDN IIGKP // ID FD3_DROME STANDARD; PRT; 456 AA. AC Q02361; Q9W1Y5; DT 01-JUL-1993 (Rel. 26, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fork head domain protein FD3. GN FD59A OR FD3 OR CG3668. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 70-197 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=92409595; PubMed=1356269; RA Haecker U., Grossniklaus U., Gehring W.J., Jaeckle H.; RT "Developmentally regulated Drosophila gene family encoding the fork RT head domain."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8754-8758(1992). CC -!- FUNCTION: INVOLVED IN DEVELOPMENT DURING EMBRYOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: DURING EMBRYOGENESIS, EXPRESSED IN NEUROBLASTS CC DERIVED FROM PROCEPHALIC REGION, VENTRAL NERVOUS SYSTEM, THORACIC CC SENSORY NEURONS AND BRAIN CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT VERY LOW LEVELS DURING CC EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003458; AAF46917.1; -. DR EMBL; M96442; AAA28534.1; -. DR PIR; C46178; C46178. DR HSSP; Q63245; 2HFH. DR FlyBase; FBgn0004896; fd59A. DR InterPro; IPR001766; TF_Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR ProDom; PD000425; TF_Fork_head; 1. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DNA_BIND 84 175 FORK-HEAD. SQ SEQUENCE 456 AA; 49054 MW; 208FEAF27C953F4B CRC64; MHTSTDPMHT LHDSVSLSPP LIKSSRGGSS IGNGIGCSAS SRTAAADAMS MGCDDSDIEP SSMGGSGAAG GNGDGSGSSG GPLVKPPYSY IALITMAILQ SPHKKLTLSG ICDFIMSRFP YYKDKFPAWQ NSIRHNLSLN DCFIKVPREP GNPGKGNFWT LDPLAEDMFD NGSFLRRRKR YKRAPTMQRF SFPAVFGTLS PFWIRKPVPL VPVHFNVPNF NGSREFDVVH NPADVFDSAL RADKKFNFFA NAEASFYQGS QSGDKFDRLP FMNRGRGADV LDALPHSSGS GGGVGGGSES SRGSKYKSPY AFDVATVASA AGIPGHRDYA ERLSAGGGYM DLNVYNDDAD TEADAEAEGD DDSCEDKIDV ESGNEQEDSH ISDSVDSACT NRLDAPPEAL IFEASAEASD SSPRRRFDSE PLVLRTSKQS SAKDFRIETL IGHHLHRGGS QEETSD // ID FD4_DROME STANDARD; PRT; 372 AA. AC P32028; Q9VBY1; DT 01-JUL-1993 (Rel. 26, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fork head domain protein FD4. GN FD96CA OR FD4 OR CG11921. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-125 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=92409595; PubMed=1356269; RA Haecker U., Grossniklaus U., Gehring W.J., Jaeckle H.; RT "Developmentally regulated Drosophila gene family encoding the fork RT head domain."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8754-8758(1992). CC -!- FUNCTION: INVOLVED IN DEVELOPMENT DURING EMBRYOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN EARLY EMBRYOGENESIS IN 14 CC SYMMETRICAL PAIRS OF SEGMENTALLY ARRANGED NEUROBLASTS. ALSO, LATER CC IN EMBRYOGENESIS, IN A CLUSTER OF CELLS IN HEAD REGION. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN 5-12 HOUR EMBRYOS. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003750; AAF56396.1; -. DR EMBL; M96443; AAF02179.1; ALT_INIT. DR HSSP; Q63245; 2HFH. DR FlyBase; FBgn0004897; fd96Ca. DR InterPro; IPR001766; TF_Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR ProDom; PD000425; TF_Fork_head; 1. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DNA_BIND 12 103 FORK-HEAD. SQ SEQUENCE 372 AA; 41723 MW; C3BEBEDC0EDAC1E3 CRC64; MPRPSRESYG EQKPPYSYIS LTAMAIWSSP EKMLPLSDIY KFITDRFPYY RKNTQRWQNS LRHNLSFNDC FIKVPRRPDR PGKGAYWALH PQAFDMFENG SLLRRRKRFK LHKNDKDLLN EELTALANLN RFFFTTRNGG SAAHMSPLDM NNAAAMRLDP LPRSTAHMPN SLGPGVPLPH VMPASMSGAD HTNLADMGLT NLPALTSSEI EGPLSLRPKR SFTIESLITP DKPEHPSEDE DDEDDRVDID VVECSGISRY PTTPAASEEY MSASRSSRTE DPLPPMHTIN AGAHVPFLHY ATGANVAGLP ASGIPNSPTT YELAISHPLF MMAAPIANMH NIYYNNVTLV APAQQYRSPE VQNRIDNDMR TI // ID FD5_DROME STANDARD; PRT; 271 AA. AC P32029; Q9VBY0; DT 01-JUL-1993 (Rel. 26, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fork head domain protein FD5. GN FD96CB OR FD5 OR CG11922. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-125 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=92409595; PubMed=1356269; RA Haecker U., Grossniklaus U., Gehring W.J., Jaeckle H.; RT "Developmentally regulated Drosophila gene family encoding the fork RT head domain."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8754-8758(1992). CC -!- FUNCTION: INVOLVED IN DEVELOPMENT DURING EMBRYOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN EARLY EMBRYOGENESIS IN 14 CC SYMMETRICAL PAIRS OF SEGMENTALLY ARRANGED NEUROBLASTS AND IN CC DEVELOPING PERIPHERAL NERVOUS SYSTEM. ALSO, LATER IN CC EMBRYOGENESIS, IN A CLUSTER OF CELLS IN HEAD REGION. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN EMBRYOS (MAXIMAL LEVEL BETWEEN CC 5-12 HOURS) AND AT A LOW LEVEL IN LARVAE. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003750; AAF56397.1; -. DR EMBL; M96444; AAF02178.1; ALT_INIT. DR PIR; E46178; E46178. DR HSSP; Q63245; 2HFH. DR FlyBase; FBgn0004898; fd96Cb. DR InterPro; IPR001766; TF_Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR ProDom; PD000425; TF_Fork_head; 1. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DNA_BIND 12 103 FORK-HEAD. FT CONFLICT 33 34 LL -> FV (IN REF. 2). SQ SEQUENCE 271 AA; 31012 MW; AE7C06114CEDDCC2 CRC64; MPRPLKMSYG DQKPPYSYIS LTAMAIIHSP QRLLPLSEIY RFIMDQFPFY RKNTQKWQNS LRHNLSFNDC FIKVPRNVTK AGKGSYWTLH PMAFDMFENG SLLRRRKRFR VKQLEKDISN WKLAAAANTE MVTHYLDDQL TQMAFADPAR HGHVLANASA AQMSPYKATP PILPTTVTQL PARPKRAFTI ESLMAPDPAS TPNEGLVPME YGSPDAVALE KPPFNLPFNF NELAAQYQLY FPSFFYNGQY GNIPCYQKTP PLFHNGPLPV F // ID FDL_DROME STANDARD; PRT; 660 AA. AC Q8WSF3; Q8MZ16; Q95RY8; Q9V6C8; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable beta-hexosaminidase fdl precursor (EC 3.2.1.52) (Fused lobes DE protein). GN FDL OR CG8824. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=20091303; PubMed=10623899; RA Boquet I., Hitier R., Dumas M., Chaminade M., Preat T.; RT "Central brain postembryonic development in Drosophila: implication of RT genes expressed at the interhemispheric junction."; RL J. Neurobiol. 42:33-48(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION IN N-GLYCAN PROCESSING. RA Leonard R., Altmann F.; RL Submitted (APR-2003) to Swiss-Prot. CC -!- FUNCTION: INVOLVED IN BRAIN RESTRUCTURIZATION VIA HORMONAL CONTROL CC DURING METAMORPHOSIS. IMPLICATED IN N-GLYCAN PROCESSING. CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF TERMINAL NON-REDUCING N- CC ACETYL-D-HEXOSAMINE RESIDUES IN N-ACETYL-BETA-D- CC HEXOSAMINIDES. CC -!- TISSUE SPECIFICITY: IN THIRD INSTAR LARVAL AND EARLY PUPAL BRAINS, CC EXPRESSED IN CELLS SENDING PROJECTIONS ACROSS THE INTERHEMISPHERIC CC JUNCTION. IN ADULT BRAIN, EXPRESSED IN MUSHROOM BODY, ELLIPSOID CC BODY AND PARS INTERCEREBRALIS. CC -!- SIMILARITY: BELONGS TO FAMILY 20 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF323977; AAL55992.1; -. DR EMBL; AE003822; AAM68691.1; -. DR EMBL; AY113418; AAM29423.1; -. DR EMBL; AY061037; AAL28585.1; ALT_INIT. DR FlyBase; FBgn0045063; fdl. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; ISS. DR GO; GO:0007420; P:brain development; IMP. DR InterPro; IPR001540; Glyco_hydro_20. DR Pfam; PF00728; Glyco_hydro_20; 1. DR Pfam; PF02838; Glyco_hydro_20b; 1. DR PRINTS; PR00738; GLHYDRLASE20. KW Hydrolase; Glycosidase; Developmental protein; Signal; Glycoprotein. FT SIGNAL 1 36 POTENTIAL. FT CHAIN 37 660 PROBABLE BETA-HEXOSAMINIDASE FDL. FT CARBOHYD 210 210 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 412 412 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 452 452 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 154 154 V -> G (IN REF. 4; AAM29423). FT CONFLICT 495 495 C -> R (IN REF. 4; AAM29423). FT CONFLICT 551 551 P -> Q (IN REF. 4; AAM29423). SQ SEQUENCE 660 AA; 75486 MW; 0F14B47C9A55CD74 CRC64; MSLAVSLRRA LLVLLTGAIF ILTVLYWNQG VTKAQAYNEA LERPHSHHDA SGFPIPVEKS WTYKCENDRC MRVGHHGKSA KRVSFISCSM TCGDVNIWPH PTQKFLLSSQ THSFSVEDVQ LHVDTAHREV RKQLQLAFDW FLKDLRLIQR LDYVGSSSEP TVSESSSKSR HHADLEPAAT LFGATFGVKK AGDLTSVQVK ISVLKSGDLN FSLDNDETYQ LSTQTEGHRL QVEIIANSYF GARHGLSTLQ QLIWFDDEDH LLHTYANSKV KDAPKFRYRG LMLDTSRHFF SVESIKRTIV GMGLAKMNRF HWHLTDAQSF PYISRYYPEL AVHGAYSESE TYSEQDVREV AEFAKIYGVQ VIPEIDAPAH AGNGWDWGPK RGMGELAMCI NQQPWSFYCG EPPCGQLNPK NNYTYLILQR IYEELLQHTG PTDFFHLGGD EVNLDCWAQY FNDTDLRGLW CDFMLQAMAR LKLANNGVAP KHVAVWSSAL TNTKCLPNSQ FTVQVWGGST WQENYDLLDN GYNVIFSHVD AWYLDCGFGS WRATGDAACA PYRTWQNVYK HRPWERMRLD KKRKKQVLGG EVCMWTEQVD ENQLDNRLWP RTAALAERLW TDPSDDHDMD IVPPDVFRRI SLFRNRLVEL GIRAEALFPK YCAQNPGECI // ID FGR1_DROME STANDARD; PRT; 729 AA. AC Q07407; O18371; Q26294; Q9VED5; DT 01-NOV-1995 (Rel. 32, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fibroblast growth factor receptor homolog 1 precursor (EC 2.7.1.112) DE (Heartless protein). GN HTL OR FR1 OR TK1 OR CG7223. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94156202; PubMed=8112607; RA Ito M., Matsui T., Taniguchi T., Chihara K.; RT "Alternative splicing generates two distinct transcripts for the RT Drosophila melanogaster fibroblast growth factor receptor homolog."; RL Gene 139:215-218(1994). RN [2] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Canton-S; TISSUE=Pupae; RX MEDLINE=93321617; PubMed=8330538; RA Shishido E., Higashijima S.-I., Emori Y., Saigo K.; RT "Two FGF-receptor homologues of Drosophila: one is expressed in RT mesodermal primordium in early embryos."; RL Development 117:751-761(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 560-615 FROM N.A. RX MEDLINE=92008631; PubMed=1915852; RA Shishido E., Emori Y., Saigo K.; RT "Identification of seven novel protein-tyrosine kinase genes of RT Drosophila by the polymerase chain reaction."; RL FEBS Lett. 289:235-238(1991). RN [6] RP SEQUENCE OF 562-614 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). CC -!- FUNCTION: MAY BE REQUIRED FOR PATTERNING OF MUSCLE PRECURSOR CC CELLS. MAY BE ESSENTIAL FOR GENERATION OF MESODERMAL AND CC ENDODERMAL LAYERS, INVAGINATIONS OF VARIOUS TYPES OF CELLS AND CC CNS FORMATION. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: IN EARLY EMBRYOS, EXPRESSION IS SPECIFIC TO CC MESODERMAL PRIMORDIUM AND INVAGINATED MESODERMAL CELLS. AT LATER CC STAGES, EXPRESSION IS SEEN IN PUTATIVE MUSCLE PRECURSOR CELLS AND CC IN THE CNS. CC -!- DEVELOPMENTAL STAGE: EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE FIBROBLAST GROWTH FACTOR RECEPTOR CC FAMILY. CC -!- SIMILARITY: CONTAINS 2 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-16 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D14976; BAA03616.1; -. DR EMBL; D14977; BAA03617.1; -. DR EMBL; X74030; CAA52189.1; -. DR EMBL; AE003720; AAF55489.1; -. DR EMBL; AY051812; AAK93236.1; -. DR EMBL; S55969; AAB19903.1; -. DR EMBL; AJ002913; CAA05748.1; -. DR PIR; A49120; A49120. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0010389; htl. DR GO; GO:0016021; C:integral to membrane; ISS. DR GO; GO:0005007; F:fibroblast growth factor receptor activity; ISS. DR GO; GO:0004713; F:protein-tyrosine kinase activity; ISS. DR GO; GO:0007417; P:central nervous system development; IEP. DR GO; GO:0007493; P:endoderm cell fate determination; IEP. DR GO; GO:0008543; P:FGF receptor signaling pathway; ISS. DR GO; GO:0007369; P:gastrulation; NAS. DR GO; GO:0008354; P:germ-cell migration; IMP. DR GO; GO:0008347; P:glia cell migration; IMP. DR GO; GO:0007506; P:gonadal mesoderm development; IMP. DR GO; GO:0007507; P:heart development; IEP. DR GO; GO:0007523; P:larval visceral muscle development; IMP. DR GO; GO:0007500; P:mesoderm cell fate determination; IEP. DR GO; GO:0008078; P:mesoderm cell migration; IMP. DR GO; GO:0007509; P:mesoderm migration; NAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; ISS. DR GO; GO:0007525; P:somatic muscle development; IMP. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003599; Ig. DR InterPro; IPR003598; Ig_c2. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00047; ig; 1. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. KW Receptor; Glycoprotein; Tyrosine-protein kinase; ATP-binding; KW Transferase; Phosphorylation; Transmembrane; Immunoglobulin domain; KW Repeat; Signal; Developmental protein. FT SIGNAL 1 36 POTENTIAL. FT CHAIN 37 729 FIBROBLAST GROWTH FACTOR RECEPTOR HOMOLOG FT 1. FT DOMAIN 37 309 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 310 330 POTENTIAL. FT DOMAIN 331 729 CYTOPLASMIC (POTENTIAL). FT DOMAIN 106 192 IG-LIKE C2-TYPE 1. FT DOMAIN 203 279 IG-LIKE C2-TYPE 2. FT DOMAIN 416 692 PROTEIN KINASE. FT NP_BIND 422 430 ATP (BY SIMILARITY). FT BINDING 443 443 ATP (BY SIMILARITY). FT ACT_SITE 556 556 BY SIMILARITY. FT MOD_RES 587 587 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT DISULFID 125 174 POTENTIAL. FT DISULFID 220 272 POTENTIAL. FT CARBOHYD 60 60 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 70 70 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 96 96 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 134 134 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 140 140 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 171 171 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 207 207 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 213 213 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 242 242 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 246 246 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 282 282 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 21 21 V -> L (IN REF. 3 AND 4). FT CONFLICT 29 29 T -> S (IN REF. 3 AND 4). FT CONFLICT 77 77 A -> V (IN REF. 2). FT CONFLICT 167 167 G -> A (IN REF. 2). FT CONFLICT 218 218 M -> S (IN REF. 1). FT CONFLICT 237 237 C -> V (IN REF. 1). FT CONFLICT 358 358 I -> II (IN REF. 1). FT CONFLICT 430 430 V -> M (IN REF. 2). FT CONFLICT 504 504 K -> R (IN REF. 2). FT CONFLICT 507 508 PF -> RS (IN REF. 2). FT CONFLICT 562 562 V -> L (IN REF. 2). FT CONFLICT 568 568 MISSING (IN REF. 6). FT CONFLICT 570 570 L -> Q (IN REF. 1). SQ SEQUENCE 729 AA; 82586 MW; D2B2447D3E0802BB CRC64; MAAAWSWRAS HSTITMTSGS VVVLFLLLTI WQPAVQVEGR RQMANSQEMI KDHLGARSQN KTPAITNNAN QSSTSSADLD DGAADDDDNK ADLPVNVSSK PYWRNPKKMS FLQTRPSGSL LTLNCHALGN PEPNITWYRN GTVDWTRGYG SLKRNRWTLT MEDLVPGDCG NYTCKVCNSL GCIRHDTQVI VSDRVNHKPI LMTGPLNLTL VVNSTGSMHC KYLSDLTSKK AWIFVPCHGM TNCSNNRSII AEDKDQLDFV NVRMEQEGWY TCVESNSLGQ SNSTAYLRVV RSLHVLEAGV ASGSLHSTSF VYIFVFGGLI FIFMTTLFVF YAIRKMKHEK VLKQRIETVH QWTKKVIIFK PEGGGDSSGS MDTMIMPVVR IQKQRTTVLQ NGNEPAPFNE YEFPLDSNWE LPRSHLVLGA TLGEGAFGRV VMAEVNNAIV AVKMVKEGHT DDDIASLVRE MEVMKIIGRH INIINLLGCC SQNGPLYVIV EYAPHGNLKD FLYKNRPFGR DQDRDSSQPP PSPPAHVITE KDLIKFAHQI ARGMDYLASR RCIHRDLAAR NVLVSDDYVL KIADFGLARD IQSTDYYRKN TNGRLPIKWM APESLQEKFY DSKSDVWSYG ILLWEIMTYG QQPYPTIMSA EELYTYLMSG QRMEKPAKCS MNIYILMRQC WHFNADDRPP FTEIVEYMDK LLQTKEDYLD VDIANLDTPP STSDEEEDET DNLQKWCNY // ID FGR2_DROME STANDARD; PRT; 1052 AA. AC Q09147; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fibroblast growth factor receptor homolog 2 precursor (EC 2.7.1.112) DE (Breathless protein) (dFGF-R1). GN BTL OR FR2 OR DTK2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93321617; PubMed=8330538; RA Shishido E., Higashijima S.-I., Emori Y., Saigo K.; RT "Two FGF-receptor homologues of Drosophila: one is expressed in RT mesodermal primordium in early embryos."; RL Development 117:751-761(1993). RN [2] RP SEQUENCE OF 1-240 FROM N.A. RX MEDLINE=92387542; PubMed=1325393; RA Klaembt C., Glazer L., Shilo B.-Z.; RT "Breathless, a Drosophila FGF receptor homolog, is essential for RT migration of tracheal and specific midline glial cells."; RL Genes Dev. 6:1668-1678(1992). RN [3] RP SEQUENCE OF 267-1052 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=91184623; PubMed=1849109; RA Glazer L., Shilo B.-Z.; RT "The Drosophila FGF-R homolog is expressed in the embryonic tracheal RT system and appears to be required for directed tracheal cell RT extension."; RL Genes Dev. 5:697-705(1991). RN [4] RP SEQUENCE OF 868-923 FROM N.A. RX MEDLINE=92008631; PubMed=1915852; RA Shishido E., Emori Y., Saigo K.; RT "Identification of seven novel protein-tyrosine kinase genes of RT Drosophila by the polymerase chain reaction."; RL FEBS Lett. 289:235-238(1991). CC -!- FUNCTION: MAY BE REQUIRED FOR PATTERNING OF MUSCLE PRECURSOR CC CELLS. WOULD THUS APPEAR ESSENTIAL FOR GENERATION OF MESODERMAL CC AND ENDODERMAL LAYERS, INVAGINATIONS OF VARIOUS TYPES OF CELLS, CC AND CNS FORMATION. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: MESODERM. CC -!- DEVELOPMENTAL STAGE: EMBRYOGENESIS. DFR2 EXPRESSION OCCURS IN CC ENDODERMAL PRECURSOR CELLS, CNS MIDLINE CELLS AND CERTAIN CC ECTODERMAL CELLS SUCH AS THOSE OF TRACHEA AND SALIVARY DUCT. CC -!- SIMILARITY: BELONGS TO THE FIBROBLAST GROWTH FACTOR RECEPTOR CC FAMILY. CC -!- SIMILARITY: CONTAINS 5 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X74031; CAA52190.1; -. DR EMBL; X72830; CAA51340.1; -. DR EMBL; X57746; CAA40912.1; -. DR EMBL; S55971; AAB19904.1; -. DR PIR; B49120; B49120. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0005592; btl. DR GO; GO:0008543; P:FGF receptor signaling pathway; NAS. DR GO; GO:0008347; P:glia cell migration; IMP. DR GO; GO:0007428; P:primary tracheal branching (sensu Insecta); IMP. DR GO; GO:0007435; P:salivary gland morphogenesis; NAS. DR GO; GO:0007429; P:secondary tracheal branching (sensu Insecta); IMP. DR GO; GO:0007430; P:terminal branching of trachea, cytoplasmic ...; IMP. DR GO; GO:0007427; P:tracheal cell migration (sensu Insecta); IMP. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00047; ig; 4. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00408; IGc2; 3. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50835; IG_LIKE; 4. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. KW Receptor; Glycoprotein; Tyrosine-protein kinase; ATP-binding; KW Transferase; Phosphorylation; Transmembrane; Immunoglobulin domain; KW Repeat; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 1052 FIBROBLAST GROWTH FACTOR RECEPTOR HOMOLOG FT 2. FT DOMAIN 20 600 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 601 626 POTENTIAL. FT DOMAIN 627 1052 CYTOPLASMIC (POTENTIAL). FT DOMAIN 23 117 IG-LIKE C2-TYPE 1. FT DOMAIN 124 230 IG-LIKE C2-TYPE 2. FT DOMAIN 240 340 IG-LIKE C2-TYPE 3. FT DOMAIN 393 478 IG-LIKE C2-TYPE 4. FT DOMAIN 487 585 IG-LIKE C2-TYPE 5. FT DOMAIN 712 1000 PROTEIN KINASE. FT NP_BIND 718 726 ATP (BY SIMILARITY). FT BINDING 748 748 ATP (BY SIMILARITY). FT ACT_SITE 864 864 BY SIMILARITY. FT MOD_RES 895 895 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT DISULFID 30 90 POTENTIAL. FT DISULFID 164 217 POTENTIAL. FT DISULFID 262 329 POTENTIAL. FT DISULFID 416 462 POTENTIAL. FT DISULFID 507 566 POTENTIAL. FT CARBOHYD 99 99 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 137 137 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 163 163 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 175 175 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 226 226 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 249 249 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 257 257 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 423 423 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 444 444 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 494 494 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 500 500 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 526 526 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 541 541 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 546 546 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 555 555 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 576 576 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 181 181 I -> N (IN REF. 2). FT CONFLICT 287 287 L -> F (IN REF. 3). FT CONFLICT 293 293 E -> D (IN REF. 3). FT CONFLICT 480 481 ND -> KH (IN REF. 3). FT CONFLICT 565 565 S -> T (IN REF. 3). FT CONFLICT 845 845 P -> A (IN REF. 3). FT CONFLICT 911 921 ESLQEKKYDSQ -> SRCRRRSTTH (IN REF. 3). FT CONFLICT 982 982 E -> Q (IN REF. 3). SQ SEQUENCE 1052 AA; 117824 MW; 1E8B980E16DC8D15 CRC64; MAKVPITLVM IIAIVSAAAD LGCDYGHHRC YIDVTVENSP RQRHLLSDMD ITLQCVRPMA KWFYEDKFQL RATLLRLERA QSGNSGNYGC LDSQNRWYNI SLVIGHKEPV GNDIASFVKL EDAPAIPESD LFFQPLNESR SLKLLQPLPK TVQRTAGGLF QLNCSPMDPD AKGVNISWLH IDTQILGGRG RIKLKRWSLT VGQLQPEDAG SYHCELCVEQ DCQRSNPTQL EVISRKHTVP MLKPGYPRNT SIALGDNVSI ECLLEDSALE PKITWLHKGN ADNIDDLLQR LREQSQLPVD VTRLITRMDE PQVLRLGNVL MEDGGWYICI AENQVGRTVA ASYVDLYSPS DTTTVRTTTT TTVASPIPTA STGEDNDDDV ENPAADASGG VGPPVFRKEL KRLQHSLSGN TVNLACPVYG KANITWTKDK KPLNRELGVY VQKNWTLRFV EATSEDSGLY NCKVCNAWGC IQFDFSVQIN DRTRSAPIIV VPQNQTVKVN GSLVMKCTVY SDLHPTVSWK RVVLKNASLD GLQSVEIQNL NFTVTNDSVV LTLRNVTFDQ EGWYSCLASS GLGRSNSSVY LRVVSPLPPL EIYALLHAHP LGFTLAAITI VALFLLGSAF ITFMLRRLRR EKLLKLRIET VHQWTKKVII YRPGGEEGSG CSSGDLQMPV IRIEKQRTTV STTGTGGTDP AQGFNEYEFP LDSNWEIPRQ QLSLGSILGE GAFGRVVMAE AEGLPRSPQL AETIVAVKMV KEEHTDTDMA SLVREMEVMK MIGKHINIIN LLGCCSQGGP LWVIVEYAPH GNLKDFLKQN RPGAPQRRSD SDGYLDDKPL ISTQHLGEKE LTKFPFQIAR GMEYLASRRC IHRDLAARNV LVSDGYVMKI ADFGLARDIQ DTEYYRKNTN GRLPIKWMAP ESLQEKKYDS QSDVWSYGVL LWEIMTYGDQ PYPHILSAEE LYSYLITGQR MEKPAKCSLN IYVVMRQCWH FESCARPTFA ELVESFDGIL QQASSNPNDA YLDLSMPMLE TPPSSGDEDD GSDTETFRET SPLRYQYTYK FN // ID FKB1_DROME STANDARD; PRT; 108 AA. AC P48375; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 12 kDa FK506-binding protein (FKBP) (Peptidyl-prolyl cis-trans DE isomerase) (PPIase) (EC 5.2.1.8) (Macrolide binding protein). GN FK506-BP2 OR FKBP12. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RA Mounsey A.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RA Wang T., Li B.Y., Danielson P.D., Shah P.C., Rockwell S., RA Lechleider R.J., Martin J., Manganaro T., Donahoe P.K.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PPIASES ACCELERATE THE FOLDING OF PROTEINS. IT CATALYZES CC THE CIS-TRANS ISOMERIZATION OF PROLINE IMIDIC PEPTIDE BONDS IN CC OLIGOPEPTIDES. CC -!- CATALYTIC ACTIVITY: PEPTIDYLPROLINE (OMEGA=180) = PEPTIDYLPROLINE CC (OMEGA=0). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE FKBP-TYPE PPIASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z49079; CAA88904.1; -. DR EMBL; U41441; AAA91178.1; -. DR PIR; S54139; S54139. DR HSSP; P18203; 1FKL. DR FlyBase; FBgn0013954; FK506-bp2. DR InterPro; IPR001179; FKBP_PPIase. DR Pfam; PF00254; FKBP; 1. DR PROSITE; PS00453; FKBP_PPIASE_1; 1. DR PROSITE; PS00454; FKBP_PPIASE_2; 1. DR PROSITE; PS50059; FKBP_PPIASE_3; 1. KW Isomerase; Rotamase. SQ SEQUENCE 108 AA; 11597 MW; 48BCF993AC8D350A CRC64; MGVQVVPIAP GDGSTYPKNG QKVTVHYTGT LDDGTKFDSS RDRNKPFKFT IGKGEVIRGW DEGVAQLSVG QSAKLICSPD YAYGSRGHPG VIPPNSTLTF DVELLKVE // ID FKB4_DROME STANDARD; PRT; 357 AA. AC P54397; Q9VF88; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 39 kDa FK506-binding nuclear protein (EC 5.2.1.8) (Peptidyl-prolyl DE cis-trans isomerase) (PPIase) (Rotamase). GN FK506-BP1 OR FKBP39 OR CG6226. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95278752; PubMed=7538962; RA Theopold U., Dal Zotto L., Hultmark D.; RT "FKBP39, a Drosophila member of a family of proteins that bind the RT immunosuppressive drug FK506."; RL Gene 156:247-251(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PPIASES ACCELERATE THE FOLDING OF PROTEINS. FKBP506 CC MAY FUNCTION IN A SIGNAL TRANSDUCTION CASCADE DURING EARLY CC DEVELOPMENT. CC -!- CATALYTIC ACTIVITY: PEPTIDYLPROLINE (OMEGA=180) = PEPTIDYLPROLINE CC (OMEGA=0). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED, HIGHEST LEVELS IN CC OVARY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING ALL STAGES OF DEVELOPMENT CC WITH HIGHEST EXPRESSION IN EARLY EMBRYO. CC -!- SIMILARITY: BELONGS TO THE FKBP-TYPE PPIASE FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-3 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z46894; CAA86996.1; -. DR EMBL; AE003708; AAF55171.2; -. DR EMBL; AY094814; AAM11167.1; -. DR PIR; JC4090; JC4090. DR HSSP; P27124; 1ROT. DR FlyBase; FBgn0013269; FK506-bp1. DR GO; GO:0005528; F:FK506 binding; IDA. DR InterPro; IPR001179; FKBP_PPIase. DR Pfam; PF00254; FKBP; 1. DR PROSITE; PS00453; FKBP_PPIASE_1; FALSE_NEG. DR PROSITE; PS00454; FKBP_PPIASE_2; 1. DR PROSITE; PS50059; FKBP_PPIASE_3; 1. KW Isomerase; Rotamase; Nuclear protein. FT DOMAIN 89 99 ASP/GLU-RICH (HIGHLY ACIDIC). FT DOMAIN 119 183 ASP/GLU-RICH (HIGHLY ACIDIC). FT DOMAIN 186 247 LYS-RICH (BASIC). FT DOMAIN 269 357 PPIASE, FKBP-TYPE. FT CONFLICT 187 187 A -> R (IN REF. 1). SQ SEQUENCE 357 AA; 39343 MW; EF0AB7831738BB30 CRC64; MSMFWGLNMK PERKYSQTII KSFHISGVAL DKGQEAKLYL AAEKQEYIVA TVTKAIPQVA LDLNFSKGDR IMFYTAGDAS VSLLGYLHDI DSEDDEDDDQ MTIENLLNSK AIKNSKKSED DEDENESGEE DEEDTDDDSQ IIEEYESFLE NGEEEDDDDV DEDNEESGEE DEQDSDDSEA EEEQPKAKVA KLSPGASAKK SGKEQNGVAK KEEAKQQQKK KEKPEAKKEQ PKAKEPAKQQ PASKDPRTIT GGVKIVDQVV GKGEEAKQGK RVSVYYIGRL QSNNKTFDSL LKGKPFKFAL GGGEVIKGWD VGVAGMKVGG KRVITCPPHM AYGARGAPPK IGPNSTLVFE VELKAVH // ID FKH_DROME STANDARD; PRT; 510 AA. AC P14734; Q9VAV0; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fork head protein. GN FKH OR CG10002. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89249328; PubMed=2566386; RA Weigel D., Juergens G., Kuettner F., Seifert E., Jaeckle H.; RT "The homeotic gene fork head encodes a nuclear protein and is RT expressed in the terminal regions of the Drosophila embryo."; RL Cell 57:645-658(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: FKH PROMOTES TERMINAL AS OPPOSED TO SEGMENTAL CC DEVELOPMENT. IN THE ABSENCE OF FKH, THIS DEVELOPMENTAL SWITCH DOES CC NOT OCCUR. THE NUCLEAR LOCALIZATION OF THE FKH PROTEIN SUGGEST CC THAT FKH REGULATES THE TRANSCRIPTION OF OTHER, SUBORDINATE, CC GENES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03177; AAA28535.1; -. DR EMBL; AE003766; AAF56798.1; -. DR PIR; A32380; A32380. DR HSSP; Q63245; 2HFH. DR TRANSFAC; T01054; -. DR FlyBase; FBgn0000659; fkh. DR GO; GO:0007435; P:salivary gland morphogenesis; IMP. DR InterPro; IPR001766; TF_Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR ProDom; PD000425; TF_Fork_head; 1. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 21 40 GLY-RICH. FT DOMAIN 340 356 HIS-RICH. FT DNA_BIND 209 300 FORK-HEAD. SQ SEQUENCE 510 AA; 54285 MW; 2B86E807CBF7881B CRC64; MQKLYAEPPP SSAPVSMASS GGGGPPSGGG GGGGGGGGGG PPPPSNNNPN PTSNGGSMSP LARSAYTMNS MGLPVGGMSS VSPQAAATFS SSVLDSAAAV ASMSASMSAS MSASMNASMN GSMGAAAMNS MGGNCMTPSS MSYASMGSPL GNMGGCMAMS AASMSAAGLS GTYGAMPPGS REMETGSPNS LGRSRVDKPT TYRRSYTHAK PPYSYISLIT MAIQNNPTRM LTLSEIYQFI MDLFPFYRQN QQRWQNSIRH SLSFNDCFVK IPRTPDKPGK GSFWTLHPDS GNMFENGCYL RRQKRFKDEK KEAIRQLHKS PSHSSLEATS PGKKDHEDSH HMHHHHHSRL DHHQHHKEAG GASIAGVNVL SAAHSKDAEA LAMLHANAEL CLSQQPQHVP THHHHQHHQL QQEELSAMMA NRCHPSLITD YHSSMHPLKQ EPSGYTPSSH PFSINRLLPT ESKADIKMYD MSQYAGYNAL SPLTNSHAAL GQDSYYQSLG YHAPAGTTSL // ID FLII_DROME STANDARD; PRT; 1256 AA. AC Q24020; Q24088; Q9VRH0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Flightless-I protein. GN FLII OR CG1484. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94068608; PubMed=8248259; RA Campbell H.D., Schimansky T., Claudianos C., Ozsarac N., RA Kasprzak A.B., Cotsell J.N., Young I.G., de Couet H.G., Miklos G.L.G.; RT "The Drosophila melanogaster flightless-I gene involved in RT gastrulation and muscle degeneration encodes gelsolin-like and RT leucine-rich repeat domains and is conserved in Caenorhabditis elegans RT and humans."; RL Proc. Natl. Acad. Sci. U.S.A. 90:11386-11390(1993). RN [2] RP SEQUENCE FROM N.A., AND VARIANT SER-601. RC STRAIN=Canton-S; RX MEDLINE=96129280; PubMed=8582612; RA de Couet H.G., Fong K.S.K., Weeds A.G., McLaughlin P.J., RA Miklos G.L.G.; RT "Molecular and mutational analysis of a gelsolin-family member encoded RT by the flightless I gene of Drosophila melanogaster."; RL Genetics 141:1049-1059(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98188272; PubMed=9520435; RA Maleszka R., de Couet H.G., Miklos G.L.G.; RT "Data transferability from model organisms to human beings: insights RT from the functional genomics of the flightless region of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY PLAY A KEY ROLE IN EMBRYONIC CELLULARIZATION BY CC INTERACTING WITH BOTH THE CYTOSKELETON AND OTHER CELLULAR CC COMPONENTS. ALTERNATIVELY, IT MAY PLAY A STRUCTURAL ROLE IN CC INDIRECT FLIGHT MUSCLE. VITAL FOR EMBRYONIC DEVELOPMENT. CC -!- TISSUE SPECIFICITY: FOUND IN OVARIES, LARVAL FAT BODIES, BRAIN AND CC ADULT THORAX. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- DOMAIN: CONSISTS OF A LEUCINE-RICH AMINO TERMINAL HALF, WHICH IS CC LIKELY TO BE INVOLVED IN PROTEIN-PROTEIN INTERACTION, AND A CC CARBOXYTERMINAL HALF WHICH HAS HIGH SEQUENCE SIMILARITY TO CC GELSOLIN AND IS THEREFORE LIKELY TO BE INVOLVED IN ACTIN-BINDING. CC -!- SIMILARITY: BELONGS TO THE VILLIN/GELSOLIN FAMILY. CC -!- SIMILARITY: CONTAINS 15 LEUCINE-RICH (LRR) REPEATS. CC -!- SIMILARITY: CONTAINS 4 GELSOLIN-LIKE REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U01182; AAC03566.1; -. DR EMBL; AF017777; AAC28407.1; -. DR EMBL; AF132184; AAD34772.1; -. DR EMBL; AE003568; AAF50830.2; -. DR PIR; S60461; S60461. DR HSSP; P02640; 2VIL. DR FlyBase; FBgn0000709; fliI. DR InterPro; IPR007122; Gelsolin. DR InterPro; IPR007123; Gelsoln. DR InterPro; IPR001611; LRR. DR InterPro; IPR003591; LRR_typ. DR Pfam; PF00626; Gelsolin; 5. DR Pfam; PF00560; LRR; 12. DR PRINTS; PR00597; GELSOLIN. DR PRINTS; PR00019; LEURICHRPT. DR SMART; SM00262; GEL; 6. DR SMART; SM00369; LRR_TYP; 1. KW Developmental protein; Repeat; Leucine-rich repeat; Actin-binding; KW Polymorphism. FT REPEAT 4 28 LRR 1. FT REPEAT 29 51 LRR 2. FT REPEAT 52 74 LRR 3. FT REPEAT 75 99 LRR 4. FT REPEAT 100 122 LRR 5. FT REPEAT 124 145 LRR 6. FT REPEAT 147 169 LRR 7. FT REPEAT 171 192 LRR 8. FT REPEAT 218 241 LRR 9. FT REPEAT 243 264 LRR 10. FT REPEAT 265 287 LRR 11. FT REPEAT 289 312 LRR 12. FT REPEAT 313 335 LRR 13. FT REPEAT 336 358 LRR 14. FT REPEAT 360 381 LRR 15. FT REPEAT 499 557 GELSOLIN-LIKE 1. FT REPEAT 746 789 GELSOLIN-LIKE 2. FT REPEAT 1064 1102 GELSOLIN-LIKE 3. FT REPEAT 1165 1206 GELSOLIN-LIKE 4. FT VARIANT 601 601 G -> S. FT CONFLICT 1067 1070 STFC -> HYFS (IN REF. 5). FT CONFLICT 1068 1068 T -> A (IN REF. 2). SQ SEQUENCE 1256 AA; 143681 MW; CF0056EFAA88DB92 CRC64; MSVLPFVRGV DFTKNDFSAT FPSSMRQMSR VQWLTLDRTQ LAEIPEELGH LQKLEHLSLN HNRLEKIFGE LTELSCLRSL DLRHNQLKNS GIPPELFHLE ELTTLDLSHN KLKEVPEGLE RAKNLIVLNL SNNQIESIPT PLFIHLTDLL FLDLSHNRLE TLPPQTRRLI NLKTLDLSHN PLELFQLRQL PSLQSLEVLK MSGTQRTLLN FPTSIDSLAN LCELDLSHNS LPKLPDCVYN VVTLVRLNLS DNELTELTAG VELWQRLESL NLSRNQLVAL PAALCKLPKL RRLLVNDNKL NFEGIPSGIG KLGALEVFSA ANNLLEMVPE GLCRCGALKQ LNLSCNRLIT LPDAIHLLEG LDQLDLRNNP ELVMPPKPSE ASKATSLEFY NIDFSLQTQL RLAGAAVPPS MPSSATPKDS TARKIRLRRG PRSEGDQDAA KVLKGMKDVA KDKDNEAGAV PEDGKPESLK PKRWDESLEK PQLDYSKFFE KDDGQLPGLT IWEIENFLPN KIEEVVHGKF YEGDCYIVLK TKFDDLGLLD WEIFFWIGNE ATLDKRACAA IHAVNLRNFL GARCRTVREE QGDESEQFLS LFETEVIYIE GGRTATGFYT IEEMIHITRL YLVHAYGATI HLEPVAPAIT SLDPRHAFVL DLGTHIYIWM GERSKNTLNS KARLMAEKIS KTERKNKCEI QLERQGEESA EFWQGLGMTS EEADAAEPPK EHVPEDYQPV QPRLYQVQLG MGYLELPQVE LPEQKLCHTL LNSKHVYILD CYTDLFVWFG KKSTRLVRAA AVKLSRELFN MMDRPDYALV MRVPEGNEMQ IFRTKFAGWD EVMAVDFTRT AKSVAKTGAN LTQWARQQET RTDLAALFMP RQSAMPLAEA EQLEEEWNYD LEMMEAFVLE NKKFVRLPEE ELGRFYTGEC YVFLCRYCIP IEEPENGSED GANPAADVSK SSANNQPEDE IQCVVYFWQG RNAGNMGWLT FTFTLQKKFK AMFGEELEVV RIFQQQENLK FMSHFKRKFI IHTGKRKDKA HTAKGKSPVE FFHLRSNGGA LTTRLIQINP DAVHLNSTFC YILHVPFETE DDSQSGIVYV WIGSKACNEE AKLVQDIAEQ MFNSPWVSLQ ILNEGDEPEN FFWVALGGRK PYDTDAEYMN YTRLFRCSNE RGYYTVAEKC ADFCQDDLAD DDIMILDNGE HVFLWMGPRC SEVEVKLAYK SAQVYIQHMR IKQPERPRKL FLTMKNKESR RFTKCFHGWS AFKVYL // ID FLT1_DROME STANDARD; PRT; 426 AA. AC O61491; Q9V7D7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Flotillin-1. GN FLO OR FLODM-1 OR CG8200. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM SHORT), AND TISSUE SPECIFICITY. RX MEDLINE=98248905; PubMed=9573373; RA Galbiati F., Volonte D., Goltz J.S., Steele Z., Sen J., Jurcsak J., RA Stein D., Stevens L., Lisanti M.P.; RT "Identification, sequence and developmental expression of RT invertebrate flotillins from Drosophila melanogaster."; RL Gene 210:229-237(1998). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY ACT AS A SCAFFOLDING PROTEIN WITHIN CAVEOLAR CC MEMBRANES, FUNCTIONALLY PARTICIPATING IN FORMATION OF CAVEOLAE OR CC CAVEOLAE-LIKE VESICLES. CC -!- SUBUNIT: HETERO-OLIGOMERIC COMPLEX OF FLOTILLINS 1 AND 2 AND CC CAVEOLINS 1 AND 2 (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED PROTEIN OF CAVEOLAE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Short; CC IsoId=O61491-1; Sequence=Displayed; CC Name=Long; CC IsoId=O61491-2; Sequence=VSP_000506; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: EXPRESSED IN BRAIN AND VENTRAL NERVE CORD FROM CC STAGE 12-16 OF EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE BAND 7 / MEC-2 FAMILY. FLOTILLIN CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF044734; AAC39012.1; -. DR EMBL; AE003810; AAF58120.1; -. DR EMBL; AE003810; AAF58121.1; -. DR EMBL; AY058794; AAL14023.1; -. DR FlyBase; FBgn0024754; Flo. DR GO; GO:0016600; C:flotillin complex; NAS. DR GO; GO:0005198; F:structural molecule activity; IEP. DR InterPro; IPR001107; Band_7. DR InterPro; IPR004851; Flotillin. DR Pfam; PF01145; Band_7; 1. DR Pfam; PF03149; Flotillin; 1. DR SMART; SM00244; PHB; 1. KW Membrane; Developmental protein; Alternative splicing. FT VARSPLIC 162 162 G -> GDSKG (in isoform Long). FT /FTId=VSP_000506. SQ SEQUENCE 426 AA; 47135 MW; 64C99F9CB4676C0C CRC64; MTWGFVTCGP NEALVVSGCC YMKPLLVPGG RAFVWPVGQQ VQRISLNTMT LQVESPCVYT SQGVPISVTG IAQVKVQGQN EDMLLTACEQ FLGKSEAEIN HIALVTLEGH QRAIMGSMTV EEIYKDRKKF SKQVFEVASS DLANMGITVV SYTIKDLRDE EGYLRSLGMA RTAEVKRDAR IGEAEARAEA HIKEAIAEEQ RMAARFLNDT DIAKAQRDFE LKKAAYDVEV QTKKAEAEMA YELQAAKTKQ RIKEEQMQVK VIERTQEIAV QEQEIMRRER ELEATIRRPA EAEKFRMEKL AEANKQRVVM EAEAEAESIR IRGEAEAFAI AAKAKAEAEQ MAMKAEAYRE YREAAMVEML LDTLPKVAAE VAAPLSQAKK ITMVSSGTGD IGAAKLTGEV LSIVNKVPEL VKNITGVDIA RSVHAG // ID FLT2_DROME STANDARD; PRT; 438 AA. AC O61492; Q8SZW0; Q9I7S0; Q9VXZ9; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Flotillin-2. GN FLO-2 OR FLODM-2 OR CG32593/CG11547/CG14409. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORM C). RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 50-438 FROM N.A. (ISOFORM B). RX MEDLINE=98248905; PubMed=9573373; RA Galbiati F., Volonte D., Goltz J.S., Steele Z., Sen J., Jurcsak J., RA Stein D., Stevens L., Lisanti M.P.; RT "Identification, sequence and developmental expression of RT invertebrate flotillins from Drosophila melanogaster."; RL Gene 210:229-237(1998). CC -!- FUNCTION: MAY ACT AS A SCAFFOLDING PROTEIN WITHIN CAVEOLAR CC MEMBRANES, FUNCTIONALLY PARTICIPATING IN FORMATION OF CAVEOLAE OR CC CAVEOLAE-LIKE VESICLES. MAY BE INVOLVED IN EPIDERMAL CELL ADHESION CC AND EPIDERMAL STRUCTURE AND FUNCTION. CC -!- SUBUNIT: HETERO-OLIGOMERIC COMPLEX OF FLOTILLINS 1 AND 2 AND CC CAVEOLINS 1 AND 2 (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED PROTEIN OF CAVEOLAE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=A; CC IsoId=O61492-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=B; CC IsoId=O61492-2; Sequence=VSP_000509; CC Name=C; CC IsoId=O61492-3; Sequence=VSP_000507; CC Note=No experimental confirmation available; CC Name=D; CC IsoId=O61492-4; Sequence=VSP_000508; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE BAND 7 / MEC-2 FAMILY. FLOTILLIN CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003497; AAF48393.3; -. DR EMBL; AE003497; AAN09343.1; -. DR EMBL; AE003497; AAN09346.1; -. DR EMBL; AE003497; AAN09348.1; -. DR EMBL; AY069755; AAL39900.1; -. DR EMBL; BT009962; AAQ22431.1; -. DR EMBL; AF044916; AAC39013.1; -. DR FlyBase; FBgn0024753; Flo-2. DR GO; GO:0016600; C:flotillin complex; NAS. DR GO; GO:0005198; F:structural molecule activity; IEP. DR GO; GO:0007155; P:cell adhesion; NAS. DR InterPro; IPR001107; Band_7. DR InterPro; IPR004851; Flotillin. DR Pfam; PF01145; Band_7; 1. DR Pfam; PF03149; Flotillin; 1. DR SMART; SM00244; PHB; 1. KW Cell adhesion; Membrane; Alternative splicing. FT VARSPLIC 1 92 MGNIHTTGPNEALIVSGGCCGSTKKRTIVGGWAWAWWLVTD FT VQRLSLNVMTLNPMCENVETSQGVPLTVTGVAQCKIMKSSS FT YKQTDYHNDE -> MPSHTCTPTRGHSHNETTHTHTHTQTL FT THTHTNTLTHTHKHKHVQMMNVYYFHHQ (in isoform FT C). FT /FTId=VSP_000507. FT VARSPLIC 1 157 Missing (in isoform D). FT /FTId=VSP_000508. FT VARSPLIC 80 92 Missing (in isoform B). FT /FTId=VSP_000509. FT CONFLICT 183 183 A -> G (IN REF. 1). FT CONFLICT 249 249 E -> Q (IN REF. 1). SQ SEQUENCE 438 AA; 48158 MW; 8A842EEF25B05C41 CRC64; MGNIHTTGPN EALIVSGGCC GSTKKRTIVG GWAWAWWLVT DVQRLSLNVM TLNPMCENVE TSQGVPLTVT GVAQCKIMKS SSYKQTDYHN DEADELLGTA SEQFLGKSVK EIKQTILQTL EGHLRAILGT LTVEEVYKDR DQFAALVREV AAPDVGRMGI EILSFTIKDV YDDVQYLASL GKAQTAVVKR DADAGVAEAN RDAGIREAEC EKSAMDVKYS TDTKIEDNTR MYKLQKANFD QEINTAKAES QLAYELQAAK IRQRIRNEEI QIEVVERRKQ IEIESQEVQR KDRELTGTVK LPAEAEAFRL QTLAQAKQCQ TIEGARAEAE RIRKIGSAEA HAIELVGKAE AERMRMKAHV YKQYGDAAIM NIVLESLPKI AAEVAAPLAK TDEIVLIGGN DNITNDVTRL VAQLPPSINA LTGVDLSKVL SKIPGAKA // ID FMRF_DROME STANDARD; PRT; 347 AA. AC P10552; Q9V5D8; DT 01-JUL-1989 (Rel. 11, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE FMRFamide-related peptides precursor. GN FMRF OR CG2346. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90216720; PubMed=2324103; RA Schneider L.E., Taghert P.H.; RT "Organization and expression of the Drosophila Phe-Met-Arg-Phe-NH2 RT neuropeptide gene."; RL J. Biol. Chem. 265:6890-6895(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=88158119; PubMed=3162321; RA Schneider L.E., Taghert P.H.; RT "Isolation and characterization of a Drosophila gene that encodes RT multiple neuropeptides related to Phe-Met-Arg-Phe-NH2 (FMRFamide)."; RL Proc. Natl. Acad. Sci. U.S.A. 85:1993-1997(1988). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=90274871; PubMed=2350439; RA Chin A.C., Reynolds E.R., Scheller R.H.; RT "Organization and expression of the Drosophila FMRFamide-related RT prohormone gene."; RL DNA Cell Biol. 9:263-271(1990). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=90166480; PubMed=3272155; RA Nambu J.R., Murphy-Erdosh C., Andrews P.C., Feistner G.J., RA Scheller R.H.; RT "Isolation and characterization of a Drosophila neuropeptide gene."; RL Neuron 1:55-61(1988). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [7] RP PARTIAL SEQUENCE (DPKQDFMRF-AMIDE; TPAEDFMRF-AMIDE AND SDNFMRF-AMIDE). RX MEDLINE=93002195; PubMed=1390001; RA Nichols R.; RT "Isolation and structural characterization of Drosophila RT TDVDHVFLRFamide and FMRFamide-containing neural peptides."; RL J. Mol. Neurosci. 3:213-218(1992). RN [8] RP SEQUENCE OF 149-157; 160-168; 171-179; 182-190; 193-201; 204-212; RP 215-223; 226-232 AND 253-259, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- FUNCTION: IN INSECTS, FMRFAMIDE AND RELATED PEPTIDES HAVE CC MODULATORY ACTIONS AT SKELETAL NEUROMUSCULAR JUNCTIONS, AND CC PEPTIDES THAT ARE IMMUNOLOGICALLY RELATED TO FMRFAMIDE ARE CC RELEASED INTO THE CIRCULATION FROM NEUROHEMAL ORGANS. CC -!- PTM: THIS PRECURSOR INCLUDES 13 PEPTIDES THAT HAVE FMRF OR RELATED CC SEQUENCES AT THEIR C-TERMINI, AND OTHER PUTATIVE NEUROPEPTIDES. CC -!- SIMILARITY: BELONGS TO THE FARP (FMRFAMIDE RELATED PEPTIDE) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32641; AAA28537.1; -. DR EMBL; J03232; AAA28536.1; -. DR EMBL; M37711; AAA28538.1; -. DR EMBL; X53301; CAA37389.1; -. DR EMBL; X76204; CAA53798.1; -. DR EMBL; AE003831; AAF58874.1; -. DR EMBL; AY070639; AAL48110.1; -. DR PIR; A34616; A34616. DR FlyBase; FBgn0000715; Fmrf. DR GO; GO:0005179; F:hormone activity; NAS. DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS. DR InterPro; IPR002544; FARP. DR Pfam; PF01581; FARP; 13. KW Neuropeptide; Repeat; Signal; Cleavage on pair of basic residues; KW Amidation. FT SIGNAL 1 22 POTENTIAL. FT PROPEP 23 102 FT PEPTIDE 106 114 FMRFAMIDE A. FT PEPTIDE 118 138 CORTICOTROPIN-RELEASING FACTOR LIKE. FT PEPTIDE 141 146 AAMDRY-AMIDE. FT PEPTIDE 149 157 DPKQDFMRF-AMIDE. FT PEPTIDE 160 168 DPKQDFMRF-AMIDE. FT PEPTIDE 171 179 DPKQDFMRF-AMIDE. FT PEPTIDE 182 190 DPKQDFMRF-AMIDE. FT PEPTIDE 193 201 DPKQDFMRF-AMIDE. FT PEPTIDE 204 212 TPAEDFMRF-AMIDE. FT PEPTIDE 215 223 TPAEDFMRF-AMIDE. FT PEPTIDE 226 232 SDNFMRF-AMIDE. FT PROPEP 235 240 FT PEPTIDE 242 250 SPKQDFMRF-AMIDE. FT PEPTIDE 253 259 PDNFMRF-AMIDE. FT PEPTIDE 262 270 SAPQDFVRS-AMIDE. FT PEPTIDE 273 280 MDSNFIRF-AMIDE. FT PROPEP 283 347 FT MOD_RES 114 114 AMIDATION (G-115 PROVIDE AMIDE GROUP). FT MOD_RES 146 146 AMIDATION (G-147 PROVIDE AMIDE GROUP). FT MOD_RES 157 157 AMIDATION (G-158 PROVIDE AMIDE GROUP). FT MOD_RES 168 168 AMIDATION (G-169 PROVIDE AMIDE GROUP). FT MOD_RES 179 179 AMIDATION (G-180 PROVIDE AMIDE GROUP). FT MOD_RES 190 190 AMIDATION (G-191 PROVIDE AMIDE GROUP). FT MOD_RES 201 201 AMIDATION (G-202 PROVIDE AMIDE GROUP). FT MOD_RES 212 212 AMIDATION (G-213 PROVIDE AMIDE GROUP). FT MOD_RES 223 223 AMIDATION (G-224 PROVIDE AMIDE GROUP). FT MOD_RES 232 232 AMIDATION (G-233 PROVIDE AMIDE GROUP). FT MOD_RES 250 250 AMIDATION (G-251 PROVIDE AMIDE GROUP). FT MOD_RES 259 259 AMIDATION (G-260 PROVIDE AMIDE GROUP). FT MOD_RES 270 270 AMIDATION (G-271 PROVIDE AMIDE GROUP). FT MOD_RES 280 280 AMIDATION (G-281 PROVIDE AMIDE GROUP). FT CONFLICT 36 36 A -> T (IN REF. 2). FT CONFLICT 39 39 E -> Q (IN REF. 3). FT CONFLICT 43 43 S -> P (IN REF. 5 AND 6). FT CONFLICT 62 63 EL -> DV (IN REF. 4). FT CONFLICT 130 130 G -> E (IN REF. 1, 5 AND 6). FT CONFLICT 207 207 E -> A (IN REF. 3). FT CONFLICT 239 240 EL -> DV (IN REF. 3 AND 4). FT CONFLICT 263 263 A -> R (IN REF. 3 AND 4). SQ SEQUENCE 347 AA; 40100 MW; C07014CBDF39C7E8 CRC64; MGIALMFLLA LYQMQSAIHS EIIDTPNYAG NSLQDADSEV SPSQDNDLVD ALLGNDQTER AELEFRHPIS VIGIDYSKNA VVLHFQKHGR KPRYKYDPEL EAKRRSVQDN FMHFGKRQAE QLPPEGSYAG SDELEGMAKR AAMDRYGRDP KQDFMRFGRD PKQDFMRFGR DPKQDFMRFG RDPKQDFMRF GRDPKQDFMR FGRTPAEDFM RFGRTPAEDF MRFGRSDNFM RFGRSPHEEL RSPKQDFMRF GRPDNFMRFG RSAPQDFVRS GKMDSNFIRF GKSLKPAAPE SKPVKSNQGN PGERSPVDKA MTELFKKQEL QDQQVKNGAQ ATTTQDGSVE QDQFFGQ // ID FNG_DROME STANDARD; PRT; 412 AA. AC Q24342; Q9VP97; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fringe glycosyltransferase (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N- DE acetylglucosaminyltransferase). GN FNG OR CG10580. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Wing imaginal disk; RX MEDLINE=95042757; PubMed=7954826; RA Irvine K.D., Wieschaus E.; RT "Fringe, a boundary-specific signaling molecule, mediates interactions RT between dorsal and ventral cells during Drosophila wing development."; RL Cell 79:595-606(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 40-44. RX MEDLINE=97330691; PubMed=9187150; RA Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D., RA Vogt T.F.; RT "A family of mammalian Fringe genes implicated in boundary RT determination and the Notch pathway."; RL Development 124:2245-2254(1997). RN [6] RP SIMILARITY WITH LEX1 FAMILY. RX MEDLINE=97148682; PubMed=9019410; RA Yuan Y.P., Schultz J., Mlodzik M., Bork P.; RT "Secreted fringe-like signaling molecules may be RT glycosyltransferases."; RL Cell 88:9-11(1997). RN [7] RP CHARACTERIZATION. RX MEDLINE=20388669; PubMed=10935626; RA Moloney D.J., Panin V.M., Johnston S.H., Chen J., Shao L., Wilson R., RA Wang Y., Stanley P., Irvine K.D., Haltiwanger R.S., Vogt T.F.; RT "Fringe is a glycosyltransferase that modifies Notch."; RL Nature 406:369-375(2000). RN [8] RP CHARACTERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-236. RX MEDLINE=20359806; PubMed=10899003; RA Munro S., Freeman M.; RT "The notch signalling regulator fringe acts in the Golgi apparatus and RT requires the glycosyltransferase signature motif DXD."; RL Curr. Biol. 10:813-820(2000). RN [9] RP CHARACTERIZATION. RX MEDLINE=20439513; PubMed=10985380; RA Blair S.S.; RT "Notch signaling: Fringe really is a glycosyltransferase."; RL Curr. Biol. 10:R608-R612(2000). CC -!- FUNCTION: GLYCOSYLTRANSFERASE INVOLVED IN THE ELONGATON OF O- CC LINKED LIGANDS TO ACTIVATE NOTCH SIGNALING. POSSESSES FUCOSE- CC SPECIFIC BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE ACTIVITY. CC BOUNDARY-SPECIFIC CELL-SIGNALING MOLECULE THAT IS RESPONSIBLE FOR CC DORSAL-VENTRAL CELL INTERACTIONS DURING WING DEVELOPMENT. CC -!- CATALYTIC ACTIVITY: TRANSFERS A BETA-D-GLCNAC RESIDUE FROM UDP-D- CC GLCNAC TO THE FUCOSE RESIDUE OF A FUCOSYLATED PROTEIN ACCEPTOR. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI. CC -!- TISSUE SPECIFICITY: EXPRESSED IN DORSAL CELLS. CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 31. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L35770; AAA64525.1; -. DR EMBL; AE003592; AAF51658.2; -. DR EMBL; AY070927; AAL48549.1; -. DR PIR; A55376; A55376. DR FlyBase; FBgn0011591; fng. DR GO; GO:0005783; C:endoplasmic reticulum; IDA. DR GO; GO:0005795; C:Golgi stack; IDA. DR GO; GO:0016757; F:transferase activity, transferring glycosyl...; IMP. DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA. DR GO; GO:0007450; P:dorsal/ventral pattern formation, imaginal ...; IDA. DR GO; GO:0007293; P:egg chamber formation (sensu Insecta); IMP. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IDA. DR GO; GO:0007478; P:leg disc metamorphosis; IDA. DR GO; GO:0008593; P:regulation of N signaling pathway; IMP. DR GO; GO:0008587; P:wing margin morphogenesis; IMP. DR InterPro; IPR003378; Fringe. DR Pfam; PF02434; Fringe; 1. KW Developmental protein; Transferase; Glycosyltransferase; KW Transmembrane; Signal-anchor; Golgi stack. FT DOMAIN 1 15 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 16 34 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 35 412 LUMENAL (POTENTIAL). FT MUTAGEN 236 236 D->A: ACTIVITY ABOLISHED. SQ SEQUENCE 412 AA; 46992 MW; 0B1D23EFC4B7686B CRC64; MMSLTVLSPP QRFKRILQAM MLAVAVVYMT LLLYQSAYGY PGIQVPHSQV DALASEAVTT HRDQLLQDYV QSSTPTQPGA GAPAASPTTV IIRKDIRSFN FSDIEVSERP TATLLTELAR RSRNGELLRD LSQRAVTATP QPPVTELDDI FISVKTTKNY HDTRLALIIK TWFQLARDQT WFFTDTDDHY YQEKTKGHLI NTKCSQGHFR KALCCKMSAE LDVFLESGKK WFCHFDDDNY VNVPRLVKLL DEYSPSVDWY LGKPSISSPL EIHLDSKNTT TNKKITFWFA TGGAGFCLSR ALTLKMLPIA GGGKFISIGD KIRFPDDVTM GFIIEHLLKV PLTVVDNFHS HLEPMEFIRQ DTFQDQVSFS YAHMKNQWNV IKVDGFDMKT DPKRFYSLHC QLFPYFSFCP PR // ID FOG_DROME STANDARD; PRT; 730 AA. AC P40795; Q9VR71; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Folded gastrulation protein precursor. GN FOG OR CG9559. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94185167; PubMed=8137424; RA Costa M., Wilson E.T., Wieschaus E.; RT "A putative cell signal encoded by the folded gastrulation gene RT coordinates cell shape changes during Drosophila gastrulation."; RL Cell 76:1075-1089(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COORDINATES CELL SHAPE CHANGES DURING FORMATION OF THE CC VENTRAL FURROW AND INVAGINATION OF THE POSTERIOR MIDGUT CC PRIMORDIUM, BY INDUCING APICAL CONSTRICTION OF CELLS IN SPATIALLY CC AND TEMPORALLY DEFINED MANNERS. FOG COULD FUNCTION AS A SECRETED CC SIGNAL TO INITIATE APICAL CONSTRICTION BY ACTING AS A LIGAND FOR CC AN UNIDENTIFIED G PROTEIN-COUPLED RECEPTOR, WHICH IN TURN CC ACTIVATES THE G PROTEIN ALPHA SUBUNIT ENCODED BY CONCERTINA, IN CC NEIGHBORING CELLS. SUCH AN INTRACELLULAR PATHWAY WOULD ULTIMATELY CC INDUCE CONTRACTION OF THE APICAL ACTIN-MYOSIN NETWORK. IN THE CC VENTRAL FURROW, FOG APPEARS TO ENSURE THAT ALL THE CELLS INITIATE CC CONSTRICTION WITHIN SEVERAL MINUTES OF EACH OTHER. IN THE CC POSTERIOR MIDGUT INVAGINATION, FOG APPEARS TO DIRECT THE ORDERED CC PROGRESSION OF CONSTRICTION INITIATIONS OUT FROM A CENTRAL REGION CC AND ALSO TO DELIMIT THE PERIPHERAL EXTENT OF THIS SPREADING. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE INVAGINATION PRIMORDIA IN A CC PATTERN THAT PRECISELY PRECEDES THE PATTERN OF CONSTRICTIONS. CC -!- DEVELOPMENTAL STAGE: MATERNAL TRANSCRIPTS ARE DEPOSITED INTO THE CC EGG AND UNIFORMLY DISTRIBUTED THROUGHOUT THE CORTEX OF CLEAVAGE CC STAGE AND SYNCYTIAL BLASTODERM EMBRYOS. ZYGOTIC TRANSCRIPTION IS CC FIRST FOUND IN THE VENTRAL FURROW PRIMORDIUM DURING THE BEGINNING CC OF CELLULARIZATION, ABOUT 30 MIN BEFORE THE START OF CONSTRICTIONS CC ALSO EXPRESSED ABOUT 30 MIN BEFORE THE START OF CONSTRICTIONS IN CC THE POSTERIOR MIDGUT PRIMORDIUM. THE VENTRAL-MOST CELLS ARE LAST CC TO EXPRESS FOG. CC -!- INDUCTION: CONTROLLED BY ZYGOTIC PATTERNING GENES. CC -!- PTM: THIS PROTEIN MAY BE HIGHLY O-GLYCOSYLATED AT ITS SER/THR-RICH CC C-TERMINAL. THIS COULD ANCHOR THE PROTEIN IN THE EXTRACELLULAR CC MATRIX UPON SECRETION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03717; AAA18955.1; -. DR EMBL; AE003573; AAF50935.1; -. DR PIR; A53064; A53064. DR FlyBase; FBgn0000719; fog. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0007374; P:posterior midgut invagination; IDA. DR GO; GO:0007435; P:salivary gland morphogenesis; NAS. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR GO; GO:0007370; P:ventral furrow formation; IDA. KW Developmental protein; Signal; Gastrulation; Extracellular matrix; KW Glycoprotein. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 730 FOLDED GASTRULATION PROTEIN. FT PEPTIDE 57 167 G PROTEIN-COUPLED RECEPTOR LIGAND FT (POTENTIAL). FT DOMAIN 579 586 POLY-THR. FT CARBOHYD 51 51 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 193 193 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 252 252 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 289 289 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 459 459 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 590 590 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 639 639 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 678 678 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 730 AA; 78250 MW; D00D426139AB987C CRC64; MSPPNCLLAV LALTVFIGAN NALPITSRPI EGNVQRMVWE DWVNLDPEQR NLTKEKKITA KSIFTLPFRH CPQGHTLFNQ LCIPQSNIDP TDLVKQELIL AGGSNGSPPP PPIGDYDYGD DEESEEIVYD LSVIPTAMQD GLPPSVGTGD QALPSEDAPL KFNIFEKKFP TGTGEHEEMP LPPDMAAATY AKNISTTPET STSITPTSTT TFAVPSVPSG EASNRIPGGV DLLAAPSDAF STSTTLSMPT SNTTTTSNKD IGQVESIVLP ADQEHDGLVH LVTSSLSDND SDDSSTTLNG FNAEADLAQL LKVDAFWPVY DGSIELLPPL FSHRKVAPPL SADQDVKTKH AVDAAEKVGA ELEEEVGEEE VTATDILPSE EDEYTTETAT TTGDTTVAEA SMDTSTATST SGQSSPHPPE EPEIDERENR LVLIKSKVQP VQLTTTTSAT ATTAADVANS SSSTDRFHYQ HFVEDESSTT TATPEPSSST PGDPIEQSDM PASDNDNLMT NTIGGRGDDD DDGGHKATSE IHVQQELRLI NELVKGKQRQ QHQPQKQQLE PTSTEITSAL TSTSTEDATT TTTTTTAYTN WSKVMPQLGQ STSETAATTE TVATSGQVNE ISLTATSAST EVKHFSITNR SYRNSKIIRE DRLTVEPEGI VESAASTESA GTAATTPNSS SNPDGYTPLW WLPSIGWRLD RHLDGNGEDQ SLLLRFFSTF RGSNTAATTR // ID FOJO_DROME STANDARD; PRT; 583 AA. AC P54360; Q24176; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Four-jointed protein. GN FJ. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye imaginal disk; RX MEDLINE=96038089; PubMed=7555705; RA Villano J.L., Katz F.N.; RT "four-jointed is required for intermediate growth in the proximal- RT distal axis in Drosophila."; RL Development 121:2767-2777(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96187865; PubMed=8606003; RA Brodsky M.H., Steller H.; RT "Positional information along the dorsal-ventral axis of the RT Drosophila eye: graded expression of the four-jointed gene."; RL Dev. Biol. 173:428-446(1996). CC -!- FUNCTION: REQUIRED FOR INTERMEDIATE GROWTH IN THE PROXIMAL-DISTAL CC AXIS. MAY BE REQUIRED FOR CELL-CELL SIGNALING DURING DISC CC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U28837; AAA69524.1; -. DR EMBL; U44904; AAB01809.1; -. DR FlyBase; FBgn0000658; fj. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0007267; P:cell-cell signaling; IDA. DR GO; GO:0045198; P:establishment of epithelial cell polarity; IMP. DR GO; GO:0007446; P:imaginal disc growth; IMP. DR GO; GO:0016348; P:leg joint morphogenesis (sensu Holometabola); IMP. DR GO; GO:0007474; P:wing vein specification; IMP. KW Transmembrane; Signal-anchor. FT DOMAIN 1 78 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 79 99 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 100 583 EXTRACELLULAR (POTENTIAL). FT CARBOHYD 310 310 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 379 379 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 491 491 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 126 126 T -> S (IN REF. 2). FT CONFLICT 193 193 M -> L (IN REF. 2). FT CONFLICT 288 288 P -> R (IN REF. 2). FT CONFLICT 330 330 R -> A (IN REF. 2). SQ SEQUENCE 583 AA; 65504 MW; 82F1EA2A299DB284 CRC64; MYDIKRLEAG QQKLQQAQQP LGLDLSGQQQ QLTCSVITAP EHRANPNSSS ISQSNPSEAT HMTLLTLRRR RSLQRRACLL SILAAFVFGM ALGVVVPMFG LPRHQDSPPD LPEEQIQMVA VEPLSTYRVE FIKETDELSA EQVFRNAFHL EQDKDAPDSM VVKKLDTNDG SIKEFHVQRT ASGRYRKGPE RRMSKKMPER VQPQETSRSP TTSPTNPTSE HQAGLIEEDV YWGPTVEQAL PKGFAAKDQV SWERFVGEQG RVVRLEQGCG RMQNRMVVFA DGTRACAPYR QNTDQIQGEI FSYYLGQLLN ISNLAPSAAT VVDTSTPNWR AALGDITQAQ WKERRPVVLT RWLSDLEPAG IPQPFQPLER HLNKHDVWNL TRHMQSERQA QSQPHGLLKR LGAASSPGSA HQSNAIEETG TGTETANGAL VQRLIELAQW SDLIVFDYLI ANLDRVVNNL YNFQWNADIM AAPAHNLARQ SASQLLVFLD NESGLLHGYR LLKKYEAYHS LLLDNLCVFR RPTIDALRRL RAAGAGRRLR DLFERTTSAG VRDVLPSLPD KSVKILVERI DRVLGQVQKC QGS // ID FPS_DROME STANDARD; PRT; 804 AA. AC P18106; Q27576; Q9TYI1; Q9VHE7; Q9VHE8; DT 01-NOV-1990 (Rel. 16, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase Fps85D (EC 2.7.1.112) (dFer). GN FPS85D OR FPS OR FER OR HD-179 OR CG8874. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM P92), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC TISSUE=Embryo, and Head; RX MEDLINE=91094836; PubMed=1898762; RA Katzen A.L., Montarras D., Jackson J., Paulson R.F., Kornberg T., RA Bishop J.M.; RT "A gene related to the proto-oncogene fps/fes is expressed at diverse RT times during the life cycle of Drosophila melanogaster."; RL Mol. Cell. Biol. 11:226-239(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS P45 AND P92), AND SUBCELLULAR LOCATION. RC TISSUE=Embryo, and Head; RX MEDLINE=97190216; PubMed=9038371; RA Paulson R.F., Jackson J., Immergluck K., Bishop J.M.; RT "The DFer gene of Drosophila melanogaster encodes two membrane- RT associated proteins that can both transform vertebrate cells."; RL Oncogene 14:641-652(1997). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS P92 AND 3). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 669-719 FROM N.A. RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=p92; CC IsoId=P18106-1; Sequence=Displayed; CC Name=p45; CC IsoId=P18106-2; Sequence=VSP_004985, VSP_004986; CC Name=3; CC IsoId=P18106-3; Sequence=VSP_004987, VSP_004988; CC -!- TISSUE SPECIFICITY: EXPRESSED IN MANY TISSUES DURING EMBRYONIC CC DEVELOPMENT, SOME EXPRESSION IS TRANSIENT AND ABSENT FROM MOST OF CC NERVOUS SYSTEM. LARVAE EXHIBIT GRADED EXPRESSION IN ALL IMAGINAL CC DISKS AND EXPRESSION IN NEURAL TISSUES. PUPAL EXPRESSION IS SEEN CC IN MUSCLES AND VARIES DURING DEVELOPMENT. EXPRESSION IN ADULTS IS CC STRONG IN THE RETINA AND PRESENT IN OVARIES, NO EXPRESSION IS CC PRESENT IN ADULT BRAIN. CC -!- DEVELOPMENTAL STAGE: ISOFORMS P92 AND P45 ARE EXPRESSED IN CC IDENTICAL PATTERNS DURING ALL STAGES OF DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. FES/FPS CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 FCH DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52844; CAA37036.1; -. DR EMBL; U50450; AAA93470.1; -. DR EMBL; AE003682; AAF54366.1; -. DR EMBL; AE003682; AAF54367.1; -. DR EMBL; AJ002916; CAA05751.1; -. DR PIR; A39670; OKFFPS. DR HSSP; P08631; 1AD5. DR FlyBase; FBgn0000723; Fps85D. DR GO; GO:0005886; C:plasma membrane; IDA. DR InterPro; IPR001060; Cdc15_Fes_CIP4. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000980; SH2. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00611; FCH; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00017; SH2; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000093; SH2; 1. DR SMART; SM00055; FCH; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50133; FCH; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 1. KW Transferase; Kinase; Tyrosine-protein kinase; ATP-binding; KW Phosphorylation; SH2 domain; Membrane; Alternative splicing; KW Developmental protein. FT DOMAIN 1 82 FCH. FT DOMAIN 439 530 SH2. FT DOMAIN 542 797 PROTEIN KINASE. FT NP_BIND 548 556 ATP (BY SIMILARITY). FT BINDING 571 571 ATP (BY SIMILARITY). FT ACT_SITE 664 664 BY SIMILARITY. FT MOD_RES 692 692 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT VARSPLIC 1 10 MGFSSALQSR -> MLLLAQPGAS (in isoform FT p45). FT /FTId=VSP_004985. FT VARSPLIC 11 425 Missing (in isoform p45). FT /FTId=VSP_004986. FT VARSPLIC 1 213 MGFSSALQSRAAHEALIVRQDAELRLMETMKRSIQMKAKCD FT KEYAISLTAVAQQGLKIDRADEMQGSLISKSWRSYMDELDH FT QAKQFKFNAEQLEVVCDKLTHLSQDKRKARKAYQEEHAKIA FT ARLNHLTDEVVRKKSEYQKHLEGYKALRTRFEENYIKAPSR FT SGRKLDDVRDKYQKACRKLHLTHNEYVLSITEAIEVEKDFR FT NVLLPGLL -> MIKCALNEVGCEELPSGCDDDLTLEQNFI FT ENGYNNEQQSNSNHSASQSTIITSTITTTITTTTTTTPSKE FT NSRLKFKVPKIQKKSKAIRNTFRSKLLNFQLKRSKPCKQCT FT KRRRIHPSKSVFDFAKEFEVEQPAGSAADEQFCNCPPAGQK FT PVKPSVQISGHKDHPFESSSGELDENSDRDIDNDEEEEDSA FT SDDVLSMKDHCYCVPSLAAS (in isoform 3). FT /FTId=VSP_004987. FT VARSPLIC 214 425 Missing (in isoform 3). FT /FTId=VSP_004988. FT CONFLICT 58 58 I -> T (IN REF. 1). FT CONFLICT 230 248 ILQEAAQYGDLTADKYKEI -> TCRRRPSMATSRPTSTRR FT F (IN REF. 1). FT CONFLICT 320 341 GAVRDCQEKQMKMIEHVNGGSP -> EPSGLPGEADEDDRA FT CEWWLA (IN REF. 1). FT CONFLICT 364 364 S -> D (IN REF. 1). FT CONFLICT 529 529 P -> T (IN REF. 1). FT CONFLICT 640 640 Q -> E (IN REF. 1). SQ SEQUENCE 804 AA; 92439 MW; 6666EA45BF6E5784 CRC64; MGFSSALQSR AAHEALIVRQ DAELRLMETM KRSIQMKAKC DKEYAISLTA VAQQGLKIDR ADEMQGSLIS KSWRSYMDEL DHQAKQFKFN AEQLEVVCDK LTHLSQDKRK ARKAYQEEHA KIAARLNHLT DEVVRKKSEY QKHLEGYKAL RTRFEENYIK APSRSGRKLD DVRDKYQKAC RKLHLTHNEY VLSITEAIEV EKDFRNVLLP GLLEHQQSVQ ESFILLWRNI LQEAAQYGDL TADKYKEIQK RIDTVIGSIN PTEEYGEFTE KYKTSPTTPL LFQFDETLIQ DIPGKLQSST LTVDNLTVDW LRNRLQELEG AVRDCQEKQM KMIEHVNGGS PVANGSIISN GSNTSNGIQS NKDSLCRQSK DLNALRCQEK QKQKLVDMIK CALNEVGCEE LPSGCDDDLT LEQNFIENGY NNEQQISLST NRPLYEEEWF HGVLPREEVV RLLNNDGDFL VRETIRNEES QIVLSVCWNG HKHFIVQTTG EGNFRFEGPP FASIQELIMH QYHSELPVTV KSGAILRRPV CRERWELSND DVVLLERIGR GNFGDVYKAK LKSTKLDVAV KTCRMTLPDE QKRKFLQEGR ILKQYDHPNI VKLIGICVQK QPIMIVMELV LGGSLLTYLR KNSNGLTTRQ QMGMCRDAAA GMRYLESKNC IHRDLAARNC LVDLEHSVKI SDFGMSREEE EYIVSDGMKQ IPVKWTAPEA LNFGKYTSLC DVWSYGILMW EIFSKGDTPY SGMTNSRARE RIDTGYRMPT PKSTPEEMYR LMLQCWAADA ESRPHFDEIY NVVDALILRL DNSH // ID FRA_DROME STANDARD; PRT; 595 AA. AC P21525; Q9BH37; Q9NBW7; Q9VAH5; DT 01-MAY-1991 (Rel. 18, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor dFra (Fos-related antigen) (AP-1) (Kayak DE protein). GN KAY OR FRA OR CG15509. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=90337318; PubMed=2116361; RA Perkins K.K., Admon A., Patel N., Tjian R.; RT "The Drosophila Fos-related AP-1 protein is a developmentally RT regulated transcription factor."; RL Genes Dev. 4:822-834(1990). RN [2] RP SEQUENCE FROM N.A. RA Nairz K., Hafen E.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 18-207 FROM N.A. RA Rousseau E.D.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DEVELOPMENTALLY REGULATED TRANSCRIPTION FACTOR AP-1 CC BINDS AND RECOGNIZES THE ENHANCER DNA SEQUENCE: TGA(C/G)TCA. MAY CC PLAY A ROLE IN THE FUNCTION OR DETERMINATION OF A PARTICULAR CC SUBSET OF CELLS IN THE DEVELOPING EMBRYO. IT IS ABLE TO CARRY OUT CC ITS FUNCTION EITHER INDEPENDENTLY OF OR IN CONJUNCTION WITH DJRA. CC -!- SUBUNIT: MAY FORM DIMER OF IDENTICAL CHAINS AND MAY ALSO INTERACTS CC WITH DJRA TO FORM AN HETERODIMER. DFRA-DJRA COMPLEX IS BOUND MORE CC STABLY TO THE AP-1 SITE THAN EITHER OF THE TWO PROTEINS ALONE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: CELLS TYPE OF THE EMBRYO THAT ARE INVOLVED IN CC THE DEVELOPMENT OF THE HEAD AND NERVOUS SYSTEM. CC -!- SIMILARITY: BELONGS TO THE BZIP FAMILY. FOS SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54143; CAA38082.1; -. DR EMBL; AF238310; AAF69496.1; -. DR EMBL; AE003771; AAF56935.2; -. DR EMBL; AF332659; AAK11268.2; -. DR EMBL; AF332660; AAK11267.2; -. DR PIR; A35847; A35847. DR HSSP; P01100; 1FOS. DR TRANSFAC; T01997; -. DR FlyBase; FBgn0001297; kay. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IDA. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0007297; P:follicle cell migration (sensu Insecta); IMP. DR GO; GO:0007254; P:JNK cascade; NAS. DR GO; GO:0009611; P:response to wounding; IMP. DR InterPro; IPR008917; Euk_transcr_DNA. DR InterPro; IPR000837; Leuzip_Fos. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF00170; bZIP; 1. DR PRINTS; PR00042; LEUZIPPRFOS. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW Transcription regulation; DNA-binding; Activator; Nuclear protein. FT DNA_BIND 260 279 BASIC MOTIF. FT DOMAIN 286 314 LEUCINE-ZIPPER. FT CONFLICT 19 19 D -> N (IN REF. 5). FT CONFLICT 453 453 A -> P (IN REF. 1). SQ SEQUENCE 595 AA; 62811 MW; 99B46F99444141A7 CRC64; MKVKVERTTK KPAIRKPEDP DPAEEDRVKM VQDDPEDQEN QAVDEEELDF LPADLSAAIS TATTKIATPT RNLILGNFET GQSVLTLTTP TLTPTTTRNI EDTLGHLLSD TQTDRVAGCA GFAVPKVLPN AIDVLGMGIP TGVSSLPLQQ TFDLSLGQGS ESEDSNASYN DTQMNEEQDT TDTSSAHTDS TSYQAGHIMA GSVNGGGVNN FSNVLAAVSS SRGSASVGSS NANTSNTPAR RGGGRRPNRS TNMTPEEEQK RAVRRERNKQ AAARCRKRRV DQTNELTEEV EQLEKRGESM RKEIEVLTNS KNQLEYLLAT HRATCQKIRS DMLSVVTCNG LIAPAGLLSA GSSGSGASSH HNHNSNDSSN GTITGMDATL NSTGRSNSPL DLKPAANIDS LLMHIKDEPL DGAIDSGSSL DQDGPPPSKR ITLPPMSTMP HVHLSTILTP TGASSGSLQT PITSTAPGGF GSAFPVTSNG SSINNINSIG NNMNSPTLNA HNKVPKERPN TLAFQRPLGQ MHLTMANNKA GGPTQIQGVP IQTPSTGTFN FDSLMDGGTG LTPVSGPLVP NSSSTNKHPL ELPTPTAEPS KLVSL // ID FRDA_DROME STANDARD; PRT; 190 AA. AC Q9W385; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Frataxin homolog, mitochondrial precursor. GN FH OR CG8971. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20509989; PubMed=11054533; RA Canizares J., Blanca J.M., Navarro J.A., Monros E., Palau F., RA Molto M.D.; RT "dfh is a Drosophila homologue of the Friedreich's ataxia disease RT gene."; RL Gene 256:35-42(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLY INVOLVED IN IRON HOMEOSTASIS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FRATAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF208492; AAG35733.1; -. DR EMBL; AE003446; AAF46449.1; -. DR HSSP; Q16595; 1DLX. DR FlyBase; FBgn0030092; fh. DR InterPro; IPR001794; Frataxin. DR InterPro; IPR002908; Frataxin_like. DR Pfam; PF01491; Frataxin_Cyay; 1. DR PRINTS; PR00904; FRATAXIN. DR ProDom; PD238818; Frataxin_like; 1. DR PROSITE; PS01344; FRATAXIN_1; 1. DR PROSITE; PS50810; FRATAXIN_2; 1. KW Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 190 FRATAXIN HOMOLOG. SQ SEQUENCE 190 AA; 20921 MW; 8C48332C239F3036 CRC64; MFAGRLMVRS IVGRACLATM GRWSKPQAHA SQVILPSTPA IAAVAIQCEE FTANRRLFSS QIETESTLDG ATYERVCSDT LDALCDYFEE LTENASELQG TDVAYSDGVL TVNLGGQHGT YVINRQTPNK QIWLSSPTSG PKRYDFVGTV AAGRWIYKHS GQSLHELLQQ EIPGILKSQS VDFLRLPYCS // ID FREQ_DROME STANDARD; PRT; 186 AA. AC P37236; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Frequenin (d-FRQ). GN FRQ OR CG5907. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93332694; PubMed=8101711; RA Pongs O., Lindemeier J., Zhu X.R., Theil T., Engelkamp D., RA Krah-Jentgens I., Lambrecht H.-G., Koch K.W., Schwemer G., RA Rivosecchi R., Mallart A., Calceran J., Canal I., Barbas J.A., RA Ferrus A.; RT "Frequenin -- a novel calcium-binding protein that modulates synaptic RT efficacy in the Drosophila nervous system."; RL Neuron 11:15-28(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CA(2+)-DEPENDENT MODULATION OF SYNAPTIC EFFICACY. CC -!- SUBCELLULAR LOCATION: PERIPHERAL MEMBRANE PROTEIN (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: ENRICHED IN SYNAPSES, SUCH AS THE MOTOR NERVE CC ENDINGS AT NEUROMUSCULAR JUNCTIONS. CC -!- MISCELLANEOUS: MAY BIND 3 CALCIUM IONS VIA THE SECOND, THIRD AND CC FOURTH EF-HAND (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE RECOVERIN FAMILY. CC -!- SIMILARITY: CONTAINS 3 EF-HAND DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08064; AAA28539.1; -. DR EMBL; AE003508; AAG22356.1; -. DR HSSP; P36610; 1G8I. DR FlyBase; FBgn0004120; Frq. DR GO; GO:0008021; C:synaptic vesicle; NAS. DR GO; GO:0005509; F:calcium ion binding; IDA. DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activat...; IDA. DR GO; GO:0007269; P:neurotransmitter secretion; IMP. DR GO; GO:0016083; P:synaptic vesicle fusion; NAS. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR001125; Recoverin. DR Pfam; PF00036; efhand; 3. DR PRINTS; PR00450; RECOVERIN. DR ProDom; PD000012; EF-hand; 1. DR SMART; SM00054; EFh; 3. DR PROSITE; PS00018; EF_HAND; 3. KW Lipoprotein; Myristate; Calcium-binding; Repeat. FT INIT_MET 0 0 BY SIMILARITY. FT DOMAIN 35 46 ANCESTRAL CALCIUM SITE 1. FT CA_BIND 72 83 EF-HAND 2 (POTENTIAL). FT CA_BIND 108 119 EF-HAND 3 (POTENTIAL). FT CA_BIND 155 166 EF-HAND 4 (POTENTIAL). FT LIPID 1 1 N-myristoyl glycine (By similarity). SQ SEQUENCE 186 AA; 21537 MW; EE2A9B9FEA4B1CC3 CRC64; GKKSSKLKQD TIDRLTTDTY FTEKEIRQWH KGFLKDCPNG LLTEQGFIKI YKQFFPQGDP SKFASLVFRV FDENNDGSIE FEEFIRALSV TSKGNLDEKL QWAFRLYDVD NDGYITREEM YNIVDAIYQM VGQQPQSEDE NTPQKRVDKI FDQMDKNHDG KLTLEEFREG SKADPRIVQA LSLGGG // ID FRIZ_DROME STANDARD; PRT; 581 AA. AC P18537; Q9VUE0; Q9VUE2; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Frizzled protein precursor (Frizzled-1) (dFz1). GN FZ OR CG17697/CG3646. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM I). RX MEDLINE=89159415; PubMed=2493583; RA Vinson C.R., Conover S., Adler P.N.; RT "A Drosophila tissue polarity locus encodes a protein containing RT seven potential transmembrane domains."; RL Nature 338:263-264(1989). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS I AND II). RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=91060073; PubMed=2174014; RA Adler P.N., Vinson C., Park W.J., Conover S., Klein L.; RT "Molecular structure of frizzled, a Drosophila tissue polarity gene."; RL Genetics 126:401-416(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM I). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP TOPOLOGY. RX MEDLINE=99287588; PubMed=10360843; RA Goo J.H., Ahn Y., Park W.J.; RT "Frizzled-suc2 fusion gene studies in Saccharomyces cerevisiae."; RL DNA Cell Biol. 18:429-434(1999). CC -!- FUNCTION: RECEPTOR FOR WNT PROTEINS. MOST OF FRIZZLED RECEPTORS CC ARE COUPLED TO THE BETA-CATENIN CANONICAL SIGNALING PATHWAY, WHICH CC LEADS TO THE ACTIVATION OF DISHEVELLED PROTEINS, INHIBITION OF CC GSK-3 KINASE, NUCLEAR ACCUMULATION OF BETA-CATENIN AND ACTIVATION CC OF WNT TARGET GENES. A SECOND SIGNALING PATHWAY INVOLVING PKC AND CC CALCIUM FLUXES HAS BEEN SEEN FOR SOME FAMILY MEMBERS, BUT IT IS CC NOT YET CLEAR IF IT REPRESENTS A DISTINCT PATHWAY OR IF IT CAN BE CC INTEGRATED IN THE CANONICAL PATHWAY, AS PKC SEEMS TO BE REQUIRED CC FOR WNT-MEDIATED INACTIVATION OF GSK-3 KINASE. BOTH PATHWAYS SEEM CC TO INVOLVE INTERACTIONS WITH G-PROTEINS. REQUIRED TO COORDINATE CC THE CYTOSKELETONS OF EPIDERMAL CELLS TO PRODUCE A PARALLEL ARRAY CC OF CUTICULAR HAIRS AND BRISTLES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=I; CC IsoId=P18537-1; Sequence=Displayed; CC Name=II; CC IsoId=P18537-2; Sequence=VSP_002013, VSP_002014; CC -!- DOMAIN: LYS-THR-X-X-X-TRP MOTIF IS INVOLVED IN THE ACTIVATION OF CC THE WNT/BETA-CATENIN SIGNALING PATHWAY (BY SIMILARITY). CC -!- DOMAIN: THE FZ DOMAIN IS INVOLVED IN BINDING WITH WNT LIGANDS (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FZ/SMO G-PROTEIN COUPLED RECEPTOR CC FAMILY. CC -!- SIMILARITY: CONTAINS 1 FRIZZLED (FZ) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54648; CAA38460.1; -. DR EMBL; X54649; CAA38460.1; JOINED. DR EMBL; X54650; CAA38460.1; JOINED. DR EMBL; X54651; CAA38460.1; JOINED. DR EMBL; X54648; CAA38461.1; -. DR EMBL; X54649; CAA38461.1; JOINED. DR EMBL; X54650; CAA38461.1; JOINED. DR EMBL; X54652; CAA38461.1; JOINED. DR EMBL; X54646; CAA38458.1; -. DR EMBL; X54647; CAA38459.1; ALT_SEQ. DR EMBL; AE003535; AAF49746.3; -. DR EMBL; AE003535; AAN11810.1; -. DR EMBL; AY051808; AAK93232.1; -. DR PIR; S03540; S03540. DR FlyBase; FBgn0001085; fz. DR GO; GO:0005938; C:cell cortex; IDA. DR GO; GO:0016021; C:integral to membrane; TAS. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0017147; F:Wnt-protein binding; ISS. DR GO; GO:0045198; P:establishment of epithelial cell polarity; IMP. DR GO; GO:0007164; P:establishment of tissue polarity; NAS. DR GO; GO:0016318; P:ommatidial rotation; IMP. DR GO; GO:0016360; P:sensory organ precursor cell fate determina...; IMP. DR GO; GO:0016055; P:Wnt receptor signaling pathway; ISS. DR InterPro; IPR000539; Frizzled. DR InterPro; IPR000024; Fz_domain. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF01534; Frizzled; 1. DR Pfam; PF01392; Fz; 1. DR PRINTS; PR00489; FRIZZLED. DR SMART; SM00063; FRI; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Multigene family; Receptor; G-protein coupled receptor; Transmembrane; KW Developmental protein; Wnt signaling pathway; Glycoprotein; Signal; KW Alternative splicing. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 581 FRIZZLED PROTEIN. FT DOMAIN 19 247 EXTRACELLULAR (PROBABLE). FT TRANSMEM 248 270 1 (PROBABLE). FT DOMAIN 271 280 CYTOPLASMIC (PROBABLE). FT TRANSMEM 281 303 2 (PROBABLE). FT DOMAIN 304 343 EXTRACELLULAR (PROBABLE). FT TRANSMEM 344 364 3 (PROBABLE). FT DOMAIN 365 380 CYTOPLASMIC (PROBABLE). FT TRANSMEM 381 401 4 (PROBABLE). FT DOMAIN 402 421 EXTRACELLULAR (PROBABLE). FT TRANSMEM 422 439 5 (PROBABLE). FT DOMAIN 440 471 CYTOPLASMIC (PROBABLE). FT TRANSMEM 472 492 6 (PROBABLE). FT DOMAIN 493 529 EXTRACELLULAR (PROBABLE). FT TRANSMEM 530 553 7 (PROBABLE). FT DOMAIN 554 581 CYTOPLASMIC (PROBABLE). FT DOMAIN 48 166 FZ. FT SITE 556 561 LYS-THR-X-X-X-TRP MOTIF. FT SITE 579 581 PDZ-BINDING. FT CARBOHYD 67 67 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 167 167 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 406 415 DILSGVCFVG -> MYLWQFHTIN (in isoform II). FT /FTId=VSP_002013. FT VARSPLIC 416 581 Missing (in isoform II). FT /FTId=VSP_002014. SQ SEQUENCE 581 AA; 64847 MW; 486721D84DA0D0A1 CRC64; MWRQILFILP TLIQGVQRYD QSPLDASPYY RSGGGLMASS GTELDGLPHH NRCEPITISI CKNIPYNMTI MPNLIGHTKQ EEAGLEVHQF APLVKIGCSD DLQLFLCSLY VPVCTILERP IPPCRSLCES ARVCEKLMKT YNFNWPENLE CSKFPVHGGE DLCVAENTTS SASTAATPTR SVAKVTTRKH QTGVESPHRN IGFVCPVQLK TPLGMGYELK VGGKDLHDCG APCHAMFFPE RERTVLRYWV GSWAAVCVAS CLFTVLTFLI DSSRFRYPER AIVFLAVCYL VVGCAYVAGL GAGDSVSCRE PFPPPVKLGR LQMMSTITQG HRQTTSCTVL FMALYFCCMA AFAWWSCLAF AWFLAAGLKW GHEAIENKSH LFHLVAWAVP ALQTISVLAL AKVEGDILSG VCFVGQLDTH SLGAFLILPL CIYLSIGALF LLAGFISLFR IRTVMKTDGK RTDKLERLML RIGFFSGLFI LPAVGLLGCL FYEYYNFDEW MIQWHRDICK PFSIPCPAAR APGSPEARPI FQIFMVKYLC SMLVGVTSSV WLYSSKTMVS WRNFVERLQG KEPRTRAQAY V // ID FRU_DROME STANDARD; PRT; 955 AA. AC Q8IN81; O44708; P91618; P91619; Q24004; Q8IN80; Q8IN82; Q8IN83; AC Q9GU18; Q9GU19; Q9GU20; Q9GU21; Q9GU22; Q9VE64; Q9VE65; Q9VE66; AC Q9VE67; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sex determination protein fruitless. GN FRU OR BTB-VI OR CG14307/CG7688/CG7689/CG7690. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS MALE-I AND FEMALE-I), FUNCTION, TISSUE RP SPECIFICITY, AND INTERACTION WITH TRA. RC STRAIN=Oregon-R; RX MEDLINE=97133215; PubMed=8978612; RA Ryner L.C., Goodwin S.F., Castrillon D.H., Anand A., Villella A., RA Baker B.S., Hall J.C., Taylor B.J., Wasserman S.A.; RT "Control of male sexual behavior and sexual orientation in Drosophila RT by the fruitless gene."; RL Cell 87:1079-1089(1996). RN [2] RP SEQUENCE FROM N.A. (ISOFORM FEMALE-A), FUNCTION, AND TISSUE RP SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=96382528; PubMed=8790392; RA Ito H., Fujitani K., Usui K., Shimizu-Nishikawa K., Tanaka S., RA Yamamoto D.; RT "Sexual orientation in Drosophila is altered by the satori mutation in RT the sex-determination gene fruitless that encodes a zinc finger RT protein with a BTB domain."; RL Proc. Natl. Acad. Sci. U.S.A. 93:9687-9692(1996). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS MALE-A; FEMALE-A; MALE-B; FEMALE-B; RP TYPE-C; TYPE-D; MALE-E AND FEMALE-E), FUNCTION, TISSUE SPECIFICITY, RP AND INTERACTION WITH TRA. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=20394292; PubMed=10934470; RA Usui-Aoki K., Ito H., Ui-Tei K., Takahashi K., Lukacsovich T., RA Awano W., Nakata H., Piao Z.F., Nilsson E.E., Tomida J.-Y., RA Yamamoto D.; RT "Formation of the male-specific muscle in female Drosophila by RT ectopic fruitless expression."; RL Nat. Cell Biol. 2:500-506(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE OF 104-218 FROM N.A. RX MEDLINE=95024186; PubMed=7938017; RA Zollman S., Godt D., Prive G.G., Couderc J.-L., Laski F.A.; RT "The BTB domain, found primarily in zinc finger proteins, defines an RT evolutionarily conserved family that includes several developmentally RT regulated genes in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10717-10721(1994). RN [7] RP FUNCTION. RC STRAIN=Canton-S; RX MEDLINE=22323098; PubMed=12435630; RA Dauwalder B., Tsujimoto S., Moss J., Mattox W.; RT "The Drosophila takeout gene is regulated by the somatic sex- RT determination pathway and affects male courtship behavior."; RL Genes Dev. 16:2879-2892(2002). CC -!- FUNCTION: PROBABLY ACTS AS A TRANSCRIPTIONAL REGULATOR. PART OF CC THE SOMATIC SEX DETERMINATION HIERARCHY. VITAL FOR THE DEVELOPMENT CC OF MALES AND FEMALES. CONTROLS THE DEVELOPMENT OF THE MALE CC SPECIFIC ABDOMINAL MUSCLE OF LAWRENCE. PLAYS A ROLE IN MALE CC COURTSHIP BEHAVIOR AND SEXUAL ORIENTATION. ENHANCES MALE-SPECIFIC CC EXPRESSION OF TAKEOUT IN BRAIN-ASSOCIATED FAT BODY. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=11; CC Comment=Sex specific splicing is controlled by tra and tra-2. CC Sex-specific repression of the translation of fru mRNA might be CC mediated by the binding of Tra to the fru mRNA in females; CC Name=Male-A; Synonyms=E; CC IsoId=Q8IN81-1; Sequence=Displayed; CC Name=Female-A; Synonyms=C; CC IsoId=Q8IN81-4; Sequence=VSP_050497; CC Name=Female-B; Synonyms=F; CC IsoId=Q8IN81-7; Sequence=VSP_050497, VSP_050501, VSP_050505; CC Note=Conflict T->A at position 650 (Ref.3, AAG28589); CC Name=Female-E; Synonyms=H; CC IsoId=Q8IN81-10; Sequence=VSP_050497, VSP_050500, VSP_050506; CC Name=Female-I; CC IsoId=Q8IN81-3; Sequence=VSP_050497, VSP_050498, VSP_050501, CC VSP_050505; CC Name=G; CC IsoId=Q8IN81-5; Sequence=VSP_050500, VSP_050506; CC Note=No experimental confirmation available; CC Name=Male-B; Synonyms=B; CC IsoId=Q8IN81-6; Sequence=VSP_050501, VSP_050505; CC Name=Male-E; CC IsoId=Q8IN81-12; Sequence=VSP_050500, VSP_050506; CC Name=Male-I; CC IsoId=Q8IN81-2; Sequence=VSP_050498, VSP_050501, VSP_050505; CC Name=Type-C; Synonyms=D; CC IsoId=Q8IN81-8; Sequence=VSP_050497, VSP_050499, VSP_050504; CC Note=Conflict S->P at position 539 and H->R at position 617 CC (Ref.3, AAG28590); CC Name=Type-D; Synonyms=A; CC IsoId=Q8IN81-9; Sequence=VSP_050497, VSP_050502, VSP_050503; CC -!- TISSUE SPECIFICITY: EXPRESSED IN PARTS OF THE ADULT MALE BRAIN CC ASSOCIATED WITH THE COURTSHIP SONG AND STEPS OF THE MALE CC COURTSHIP. ALSO EXPRESSED IN THE LARVAL AND PUPAL MALE MUSHROOM CC BODY AND OPTIC LOBE. EXPRESSED IN PUPAL FEMALE OPTIC LOBE. CC -!- MISCELLANEOUS: MUTANT MALES EXHIBIT BISEXUAL BEHAVIOR; THEY COURT CC FEMALES BUT ARE BEHAVIORALLY STERILE SO FAIL TO MATE AND THEY CC EXHIBIT VIGOROUS COURTSHIP WITH OTHER FRU MUTANT MALES. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 1 C2H2-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF039231; AAB96677.1; -. DR EMBL; U72492; AAB92662.1; -. DR EMBL; D84437; BAA12663.1; -. DR EMBL; D84438; BAA12664.1; -. DR EMBL; AF220176; AAG28587.1; -. DR EMBL; AF220177; AAG28588.1; -. DR EMBL; AF220178; AAG28589.1; -. DR EMBL; AF220179; AAG28590.1; -. DR EMBL; AF220180; AAG28591.1; -. DR EMBL; AF220181; AAG28592.1; -. DR EMBL; AE003722; AAF55562.2; -. DR EMBL; AE003722; AAF55563.2; -. DR EMBL; AE003722; AAF55564.2; -. DR EMBL; AE003722; AAF55565.2; -. DR EMBL; AE003722; AAN13774.1; -. DR EMBL; AE003722; AAN13775.1; -. DR EMBL; AE003722; AAN13776.1; -. DR EMBL; AE003722; AAN13777.1; -. DR EMBL; U14403; AAA50838.1; -. DR FlyBase; FBgn0004652; fru. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003700; F:transcription factor activity; NAS. DR GO; GO:0016543; P:male courtship behavior (sensu Insecta), or...; NAS. DR GO; GO:0045433; P:male courtship behavior (sensu Insecta), so...; IMP. DR GO; GO:0007517; P:muscle development; IMP. DR GO; GO:0007530; P:sex determination; IMP. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. KW Transcription regulation; Developmental protein; Nuclear protein; KW DNA-binding; Metal-binding; Zinc; Zinc-finger; Alternative splicing. FT DOMAIN 131 196 BTB. FT ZN_FING 918 941 C2H2-TYPE. FT DOMAIN 34 56 HIS-RICH. FT DOMAIN 77 93 PRO-RICH. FT DOMAIN 292 357 ALA-RICH. FT DOMAIN 386 426 ASN-RICH. FT DOMAIN 799 870 ALA/SER-RICH. FT VARSPLIC 1 101 Missing (in isoform Female-I, isoform FT Female-A, isoform Type-D, isoform Type-C, FT isoform Female-B and isoform Female-E). FT /FTId=VSP_050497. FT VARSPLIC 324 336 Missing (in isoform Female-I and isoform FT Male-I). FT /FTId=VSP_050498. FT VARSPLIC 572 766 SAALKLHAEDMSTLLTQHALQAADARDEHNDAKQLQLDQTD FT NIDGRVKCFNIKHDRHPDRELDRNHREHDDDPGVIEEVVVD FT HVREMEAGNEHDPEEMKEAAYHATPPKYRRAVVYAPPHPDE FT EAASGSGSDIYVDGGYNCEYKCKELNMRAIRCSRQQHMMSH FT YSPHHPHHRSLIDCPAEAAYSPPVANNQAYL -> VKKSEA FT FLGSTGNKSMHQMLLHQAVEAQLKSFQLHYQNEGLDSAMHR FT LLAQQQQHQEQQQQHQQQPHHSLGKSQSPAIPSGSAGGSSR FT KSGRFRANWLYQFEWLQYDERANTMFCRHCRKWSGELADIR FT TSFVEGNSNFRLEIVNHHNKCKSHRMCYERELQEQQQHPMP FT SGSAGGSSKRRSPEIITINVGKNSA (in isoform FT Type-C). FT /FTId=VSP_050499. FT VARSPLIC 617 796 RVKCFNIKHDRHPDRELDRNHREHDDDPGVIEEVVVDHVRE FT MEAGNEHDPEEMKEAAYHATPPKYRRAVVYAPPHPDEEAAS FT GSGSDIYVDGGYNCEYKCKELNMRAIRCSRQQHMMSHYSPH FT HPHHRSLIDCPAEAAYSPPVANNQAYLASNGAVQQLDLSTY FT HGHANHQLHQHPPSAT -> SKAWHMRLTFERLSGGCNLHR FT CKLCGKVVTHIRNHYHVHFPGRFECPLCRATYTRSDNLRTH FT CKFKHPMYNPDTRKFDNLMSSSAVGAAATPTASQLAVASQA FT AMAAAAAAAFNAAQQQQQQQQQQQQHQHQQQQQHQQSQQQQ FT QQQQQSQQQLHALAQQHMLQLQPQHHQQQQHNATSE (in FT isoform G, isoform Female-E and isoform FT Male-E). FT /FTId=VSP_050500. FT VARSPLIC 617 789 RVKCFNIKHDRHPDRELDRNHREHDDDPGVIEEVVVDHVRE FT MEAGNEHDPEEMKEAAYHATPPKYRRAVVYAPPHPDEEAAS FT GSGSDIYVDGGYNCEYKCKELNMRAIRCSRQQHMMSHYSPH FT HPHHRSLIDCPAEAAYSPPVANNQAYLASNGAVQQLDLSTY FT HGHANHQLH -> SSARHHLSTPLSTSSSASPPPPPFGMHL FT SAALKREYHPLHYMAAGNGHNGPSALGYGNQGSGNAPNSAG FT GAGSVAGGVGAGGGAGGATGAAGHNSHHTMSYHNMFTPSRD FT PGTMWRCRSCGKEVTNRWHHFHSHTAQRSMCPYCPATYSRI FT DTLRSHLRVKHPDRLLKLNSSI (in isoform FT Female-I, isoform Male-I, isoform Female- FT B and isoform Male-B). FT /FTId=VSP_050501. FT VARSPLIC 617 617 R -> E (in isoform Type-D). FT /FTId=VSP_050502. FT VARSPLIC 618 955 Missing (in isoform Type-D). FT /FTId=VSP_050503. FT VARSPLIC 767 955 Missing (in isoform Type-C). FT /FTId=VSP_050504. FT VARSPLIC 790 955 Missing (in isoform Female-I, isoform FT Male-I, isoform Female-B and isoform FT Male-B). FT /FTId=VSP_050505. FT VARSPLIC 797 955 Missing (in isoform G, isoform Female-E FT and isoform Male-E). FT /FTId=VSP_050506. FT CONFLICT 107 107 C -> S (IN REF. 6). FT CONFLICT 131 131 C -> R (IN REF. 3; BAA12664). FT CONFLICT 212 218 RGLTDNN -> CANQGSI (IN REF. 6). FT CONFLICT 722 723 RA -> QRN (IN REF. 2 AND 3). SQ SEQUENCE 955 AA; 102880 MW; E2A6005D5A7FB7B7 CRC64; MMATSQDYFG NPYALFRGPP TTLRPRESPL GVGHPHGHGH LHSHAHAHGH GHAHSHYAAL DLQTPHKRNI ETDVRAPPPP LPPPPLPLPP ASPRYNTDQG AMDQQFCLRW NNHPTNLTGV LTSLLQREAL CDVTLACEGE TVKAHQTILS ACSPYFETIF LQNQHPHPII YLKDVRYSEM RSLLDFMYKG EVNVGQSSLP MFLKTAESLQ VRGLTDNNNL NYRSDCDKLR DSAASSPTGR GPSNYTGGLG GAGGVADAMR ESRDSLRSRC ERDLRDELTQ RSSSSMSERS SAAAAAAAAA AAVAAAGGNV NAAAVALGLT TPTGGERSPS VGSASAAAAA AAVAAAVAAA ANRSASADGC SDRGSERGTL ERTDSRDDLL QLDYSNKDNN NSNSSSTGGN NNNNNNNNNN SSSNNNNSSS NRERNNSGER ERERERERER DRDRELSTTP VEQLSSSKRR RKNSSSNCDN SLSSSHQDRH YPQDSQANFK SSPVPKTGGS TSESEDAGGR HDSPLSMTTS VHLGGGGGNV GAASALSGLS QSLSIKQELM DAQQQQQHRE HHVALPPDYL PSAALKLHAE DMSTLLTQHA LQAADARDEH NDAKQLQLDQ TDNIDGRVKC FNIKHDRHPD RELDRNHREH DDDPGVIEEV VVDHVREMEA GNEHDPEEMK EAAYHATPPK YRRAVVYAPP HPDEEAASGS GSDIYVDGGY NCEYKCKELN MRAIRCSRQQ HMMSHYSPHH PHHRSLIDCP AEAAYSPPVA NNQAYLASNG AVQQLDLSTY HGHANHQLHQ HPPSATHPSH SQSSPHYPSA SGAGAGAGSV SVSIAGSASG SATSAPASVA TSAVSPQPSS SSTGSTSSAA AVAAAAAAAA NRRDHNIDYS TLFVQLSGTL PTLYRCVSCN KIVSNRWHHA NIHRPQSHEC PVCGQKFTRR DNMKAHCKIK HADIKDRFFS HYVHM // ID FRZ2_DROME STANDARD; PRT; 694 AA. AC Q9VVX3; Q94916; Q9VVX2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Frizzled protein 2 precursor (Frizzled-2) (dFz2). GN FZ2 OR CG9739/CG14083. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND BINDING TO WINGLESS THROUGH FZ DOMAIN. RX MEDLINE=96353971; PubMed=8717036; RA Bhanot P., Brink M., Samos C.H., Hsieh J.C., Wang Y., Macke J.P., RA Andrew D., Nathans J., Nusse R.; RT "A new member of the frizzled family from Drosophila functions as a RT Wingless receptor."; RL Nature 382:225-230(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RECEPTOR FOR WNT PROTEINS. MOST OF FRIZZLED RECEPTORS CC ARE COUPLED TO THE BETA-CATENIN CANONICAL SIGNALING PATHWAY, WHICH CC LEADS TO THE ACTIVATION OF DISHEVELLED PROTEINS, INHIBITION OF CC GSK-3 KINASE, NUCLEAR ACCUMULATION OF BETA-CATENIN AND ACTIVATION CC OF WNT TARGET GENES. A SECOND SIGNALING PATHWAY INVOLVING PKC AND CC CALCIUM FLUXES HAS BEEN SEEN FOR SOME FAMILY MEMBERS, BUT IT IS CC NOT YET CLEAR IF IT REPRESENTS A DISTINCT PATHWAY OR IF IT CAN BE CC INTEGRATED IN THE CANONICAL PATHWAY, AS PKC SEEMS TO BE REQUIRED CC FOR WNT-MEDIATED INACTIVATION OF GSK-3 KINASE. BOTH PATHWAYS SEEM CC TO INVOLVE INTERACTIONS WITH G-PROTEINS. REQUIRED TO COORDINATE CC THE CYTOSKELETONS OF EPIDERMAL CELLS TO PRODUCE A PARALLEL ARRAY CC OF CUTICULAR HAIRS AND BRISTLES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: EXPRESSION STARTS AT STAGE 6 IN ALL CELLS CC BETWEEN 15 AND 70 PER CENT OF EGG LENGTH, INCLUDING THE CC INVAGINATING CELLS OF THE VENTRAL FURROW. STRIPE PATTERN IS CC EMERGING BY EARLY STAGE 8. FROM STAGE 9 AND CONTINUING THROUGHOUT CC EMBRYOGENESIS, EXPRESSION IS SEEN IN THE DEVELOPING CNS. AT STAGE CC 10, EXPRESSED IN 15 STRIPES IN THE PRESUMPTIVE HEAD AND TRUNK CC REGIONS, IN THE POSTERIOR MIDGUT PRIMORDIUM, IN A SUBSET OF CELLS CC OF ANTERIOR MIDGUT INVAGINATION AND IN THE PROCEPHALIC LOBE. AT CC STAGE 12, EXPRESSION DECLINES IN EPIDERMIS AND INCREASES IN THE CC MIDGUT AND VISCERAL MESODERM. AT STAGE 17, ONLY EXPRESSED IN THE CC CNS, HINDGUT AND DORSAL VESSEL. CC -!- DOMAIN: LYS-THR-X-X-X-TRP MOTIF IS INVOLVED IN THE ACTIVATION OF CC THE WNT/BETA-CATENIN SIGNALING PATHWAY (BY SIMILARITY). CC -!- DOMAIN: THE FZ DOMAIN IS INVOLVED IN BINDING WITH WNT LIGANDS. CC -!- SIMILARITY: BELONGS TO THE FZ/SMO G-PROTEIN COUPLED RECEPTOR CC FAMILY. CC -!- SIMILARITY: CONTAINS 1 FRIZZLED (FZ) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U65589; AAC47273.1; -. DR EMBL; AE003518; AAF49185.2; -. DR PIR; S71786; S71786. DR FlyBase; FBgn0016797; fz2. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0017147; F:Wnt-protein binding; IDA. DR GO; GO:0006928; P:cell motility; IMP. DR GO; GO:0007163; P:establishment and/or maintenance of cell po...; ISS. DR GO; GO:0008585; P:female gonad development; IMP. DR GO; GO:0016055; P:Wnt receptor signaling pathway; IDA. DR InterPro; IPR000539; Frizzled. DR InterPro; IPR000024; Fz_domain. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF01534; Frizzled; 1. DR Pfam; PF01392; Fz; 1. DR PRINTS; PR00489; FRIZZLED. DR SMART; SM00063; FRI; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Multigene family; Receptor; G-protein coupled receptor; Transmembrane; KW Developmental protein; Wnt signaling pathway; Glycoprotein; Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 694 FRIZZLED PROTEIN 2. FT DOMAIN 23 315 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 316 336 1 (POTENTIAL). FT DOMAIN 337 352 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 353 373 2 (POTENTIAL). FT DOMAIN 374 397 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 398 418 3 (POTENTIAL). FT DOMAIN 419 439 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 440 460 4 (POTENTIAL). FT DOMAIN 461 482 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 483 503 5 (POTENTIAL). FT DOMAIN 504 534 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 535 555 6 (POTENTIAL). FT DOMAIN 556 584 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 585 605 7 (POTENTIAL). FT DOMAIN 606 694 CYTOPLASMIC (POTENTIAL). FT DOMAIN 187 225 GLY-RICH. FT DOMAIN 59 180 FZ. FT SITE 608 613 LYS-THR-X-X-X-TRP MOTIF. FT SITE 692 694 PDZ-BINDING. FT CARBOHYD 78 78 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 288 288 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 55 55 V -> A (IN REF. 1). FT CONFLICT 417 417 S -> T (IN REF. 1). SQ SEQUENCE 694 AA; 75451 MW; 6C510F13CBAFB096 CRC64; MRHNRLKVLI LGLVLLLTSC RADGPLHSAD HGMGGMGMGG HGLDASPAPG YGVPVIPKDP NLRCEEITIP MCRGIGYNMT SFPNEMNHET QDEAGLEVHQ FWPLVEIKCS PDLKFFLCSM YTPICLEDYH KPLPVCRSVC ERARSGCAPI MQQYSFEWPE RMACEHLPLH GDPDNLCMEQ PSYTEAGSGG SSGGSGGSGS GSGSGGKRKQ GGSGSGGSGA GGSSGSTSTK PCRGRNSKNC QNPQGEKASG KECSCSCRSP LIFLGKEQLL QQQSQMPMMH HPHHWYMNLT VQRIAGVPNC GIPCKGPFFS NDEKDFAGLW IALWSGLCFC STLMTLTTFI IDTERFKYPE RPIVFLSACY FMVAVGYLSR NFLQNEEIAC DGLLLRESST GPHSCTLVFL LTYFFGMASS IWWVILSFTW FLAAGLKWGN EAITKHSQYF HLAAWLIPTV QSVAVLLLSA VDGDPILGIC YVGNLNPDHL KTFVLAPLFV YLVIGTTFLM AGFVSLFRIR SVIKQQGGVG AGVKADKLEK LMIRIGIFSV LYTVPATIVI GCYLYEAAYF EDWIKALACP CAQVKGPGKK PLYSVLMLKY FMALAVGITS GVWIWSGKTL ESWRRFWRRL LGAPDRTGAN QALIKQRPPI PHPYAGSGMG MPVGSAAGSL LATPYTQAGG ASVASTSHHH LHHHVLKQPA ASHV // ID FRZ3_DROME STANDARD; PRT; 581 AA. AC O77438; Q9I7Z7; Q9NIU0; Q9U902; Q9W5D5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Frizzled protein 3 precursor (Frizzled-3) (dFz3). GN FZ3 OR EG:34F3.6 OR CG16785. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RX MEDLINE=99429803; PubMed=10498678; RA Sato A., Kojima T., Ui-Tei K., Miyata Y., Saigo K.; RT "Dfrizzled-3, a new Drosophila Wnt receptor, acting as an attenuator RT of Wingless signaling in wingless hypomorphic mutants."; RL Development 126:4421-4430(1999). RN [2] RP SEQUENCE FROM N.A., AND FUNCTION. RX MEDLINE=20171076; PubMed=10704878; RA Sivasankaran R., Calleja M., Morata G., Basler K.; RT "The Wingless target gene Dfz3 encodes a new member of the Drosophila RT Frizzled family."; RL Mech. Dev. 91:427-431(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RECEPTOR FOR WNT PROTEINS. MOST OF FRIZZLED RECEPTORS CC ARE COUPLED TO THE BETA-CATENIN CANONICAL SIGNALING PATHWAY, WHICH CC LEADS TO THE ACTIVATION OF DISHEVELLED PROTEINS, INHIBITION OF CC GSK-3 KINASE, NUCLEAR ACCUMULATION OF BETA-CATENIN AND ACTIVATION CC OF WNT TARGET GENES. A SECOND SIGNALING PATHWAY INVOLVING PKC AND CC CALCIUM FLUXES HAS BEEN SEEN FOR SOME FAMILY MEMBERS, BUT IT IS CC NOT YET CLEAR IF IT REPRESENTS A DISTINCT PATHWAY OR IF IT CAN BE CC INTEGRATED IN THE CANONICAL PATHWAY, AS PKC SEEMS TO BE REQUIRED CC FOR WNT-MEDIATED INACTIVATION OF GSK-3 KINASE. BOTH PATHWAYS SEEM CC TO INVOLVE INTERACTIONS WITH G-PROTEINS. REQUIRED TO COORDINATE CC THE CYTOSKELETONS OF EPIDERMAL CELLS TO PRODUCE A PARALLEL ARRAY CC OF CUTICULAR HAIRS AND BRISTLES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: WING, LEG AND EYE IMAGINAL DISKS. IN EMBRYOS, CC EXPRESSED IS SEEN IN BRAIN, PROVENTRICULUS, MALPIGHIAN TUBULES, CC ANAL PLATE AND VISCERAL MESODERM OF PARASEGMENT 8. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN EMBRYOS FROM STAGE 11 AND IN CC LARVAE. CC -!- DOMAIN: THE FZ DOMAIN IS INVOLVED IN BINDING WITH WNT LIGANDS (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FZ/SMO G-PROTEIN COUPLED RECEPTOR CC FAMILY. CC -!- SIMILARITY: CONTAINS 1 FRIZZLED (FZ) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB018565; BAA84677.1; -. DR EMBL; AF195242; AAF63250.1; -. DR EMBL; AL031583; CAA20896.1; ALT_SEQ. DR EMBL; AL132792; -; NOT_ANNOTATED_CDS. DR EMBL; AE003418; AAF45547.1; -. DR FlyBase; FBgn0027343; fz3. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0017147; F:Wnt-protein binding; ISS. DR GO; GO:0007163; P:establishment and/or maintenance of cell po...; IMP. DR GO; GO:0016055; P:Wnt receptor signaling pathway; ISS. DR InterPro; IPR000539; Frizzled. DR InterPro; IPR000024; Fz_domain. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF01534; Frizzled; 1. DR Pfam; PF01392; Fz; 1. DR PRINTS; PR00489; FRIZZLED. DR SMART; SM00063; FRI; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Multigene family; Receptor; G-protein coupled receptor; Transmembrane; KW Developmental protein; Wnt signaling pathway; Glycoprotein; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 581 FRIZZLED PROTEIN 3. FT DOMAIN 20 237 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 238 258 1 (POTENTIAL). FT DOMAIN 259 270 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 271 291 2 (POTENTIAL). FT DOMAIN 292 321 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 322 342 3 (POTENTIAL). FT DOMAIN 343 359 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 360 380 4 (POTENTIAL). FT DOMAIN 381 393 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 394 414 5 (POTENTIAL). FT DOMAIN 415 442 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 443 463 6 (POTENTIAL). FT DOMAIN 464 488 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 489 509 7 (POTENTIAL). FT DOMAIN 510 581 CYTOPLASMIC (POTENTIAL). FT DOMAIN 35 156 FZ. FT DOMAIN 403 410 POLY-LEU. FT SITE 579 581 PDZ-BINDING. FT CARBOHYD 54 54 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 206 206 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 56 56 T -> I (IN REF. 1). FT CONFLICT 192 192 A -> V (IN REF. 1). FT CONFLICT 276 276 L -> P (IN REF. 1). FT CONFLICT 304 304 G -> W (IN REF. 4). FT CONFLICT 376 376 A -> V (IN REF. 1). SQ SEQUENCE 581 AA; 63251 MW; 07A8BBFF2A9E3F93 CRC64; MYAASILILH LTWAVATIAA NGAGHNGPVA SGAGPNGLQC QPIAVSACQG LGYNMTALPN LAGHTNQLEA ELQIAKLVPL IESGCSRRAR FLLCSSLFPL CTPDVPRPVA ACKLLCETVR GECMENAPPE LMELWPSFLN CDGLPQPEKH ELCMQIPQEV AVPGGSPSGP PTTGSPGVED HPQTYRFWKS GASPTSDLAG VLCPQNFSGS PFNPEECVPQ CQRDAFHTSS QKKTSETLIL GLSAVCFVLT LFALVTFWAE PTRFGYPERP VLFLCLCYNL FSVCYLERIV FHNQARMHDV ELQGRLMRPG CLLTPPCLAS YITTSYLSLC AASWWLIFAL CFYLSSHKKW SSEALEKRSG LFHVLAWVPP LAPPIAALLL EKVRPSELTG MCYAPGFVEL PALVLLLLGL YFTLRASRSL LSLQQQLQPT LAHHRFGQIR KRFVLFSLLY FAPTTAGVVA ALCERYADSV PSCSTPDDCL SPTPLSAWPA LVRIFFQLVG GTLTGLWVWS RKTCESYRNR LGASGTPTSS LMNQSKAAGA LPKKHLYTSG KSMLPTGGIT PLYAGISFHN VPVYNPNQSR V // ID FRZ4_DROME STANDARD; PRT; 705 AA. AC Q9NBW1; Q9W3S2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Frizzled 4 precursor (Frizzled-4) (dFz4). GN FZ4 OR CG4626. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Xu Y.K., Nusse R.; RT "Dfz4 acts in the Wg pathway."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RECEPTOR FOR WNT PROTEINS. MOST OF FRIZZLED RECEPTORS CC ARE COUPLED TO THE BETA-CATENIN CANONICAL SIGNALING PATHWAY, WHICH CC LEADS TO THE ACTIVATION OF DISHEVELLED PROTEINS, INHIBITION OF CC GSK-3 KINASE, NUCLEAR ACCUMULATION OF BETA-CATENIN AND ACTIVATION CC OF WNT TARGET GENES. A SECOND SIGNALING PATHWAY INVOLVING PKC AND CC CALCIUM FLUXES HAS BEEN SEEN FOR SOME FAMILY MEMBERS, BUT IT IS CC NOT YET CLEAR IF IT REPRESENTS A DISTINCT PATHWAY OR IF IT CAN BE CC INTEGRATED IN THE CANONICAL PATHWAY, AS PKC SEEMS TO BE REQUIRED CC FOR WNT-MEDIATED INACTIVATION OF GSK-3 KINASE. BOTH PATHWAYS SEEM CC TO INVOLVE INTERACTIONS WITH G-PROTEINS. MAY BE INVOLVED IN CC TRANSDUCTION AND INTERCELLULAR TRANSMISSION OF POLARITY CC INFORMATION DURING TISSUE MORPHOGENESIS AND/OR IN DIFFERENTIATED CC TISSUES. REQUIRED TO COORDINATE THE CYTOSKELETONS OF EPIDERMAL CC CELLS TO PRODUCE A PARALLEL ARRAY OF CUTICULAR HAIRS AND BRISTLES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- DOMAIN: THE FZ DOMAIN IS INVOLVED IN BINDING WITH WNT LIGANDS (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FZ/SMO G-PROTEIN COUPLED RECEPTOR CC FAMILY. CC -!- SIMILARITY: CONTAINS 1 FRIZZLED (FZ) DOMAIN. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF241270; AAF81195.1; -. DR EMBL; AE003439; AAF46245.1; ALT_SEQ. DR FlyBase; FBgn0027342; fz4. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0017147; F:Wnt-protein binding; ISS. DR GO; GO:0007163; P:establishment and/or maintenance of cell po...; ISS. DR GO; GO:0016055; P:Wnt receptor signaling pathway; ISS. DR InterPro; IPR000539; Frizzled. DR InterPro; IPR000024; Fz_domain. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF01534; Frizzled; 1. DR Pfam; PF01392; Fz; 1. DR PRINTS; PR00489; FRIZZLED. DR SMART; SM00063; FRI; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Multigene family; Receptor; G-protein coupled receptor; Transmembrane; KW Developmental protein; Wnt signaling pathway; Glycoprotein; Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 705 FRIZZLED 4. FT DOMAIN 23 233 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 234 254 1 (POTENTIAL). FT DOMAIN 255 270 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 271 291 2 (POTENTIAL). FT DOMAIN 292 322 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 323 343 3 (POTENTIAL). FT DOMAIN 344 386 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 387 407 4 (POTENTIAL). FT DOMAIN 408 430 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 431 451 5 (POTENTIAL). FT DOMAIN 452 483 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 484 504 6 (POTENTIAL). FT DOMAIN 505 529 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 530 550 7 (POTENTIAL). FT DOMAIN 551 705 CYTOPLASMIC (POTENTIAL). FT DOMAIN 41 163 FZ. FT DOMAIN 29 36 POLY-SER. FT DOMAIN 646 650 POLY-HIS. FT DOMAIN 651 654 POLY-GLN. FT SITE 703 705 PDZ-BINDING. FT CARBOHYD 60 60 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 306 306 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 317 317 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 423 423 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 705 AA; 77489 MW; 0188DFCE57BB626F CRC64; MKPTCILCLL VVILLHPRIS KSSTSGNPSA SSSSSSPPEI PAFRQCETIR IEMCRKIGYN ETSMPNLVGN EMQTDVEYTL QTFAPLIEYD CSSQLKLFLC AAYVPMCTPK APVHAIGPCR SLCESVRIRC HPVLQGFGFP WPPALDCDKF PRENNHETMC MEGPGELHQP QQEQDLYGLP GQGIPGGLGG KLPMDCSGLA KSHLYVRLPR SGRCAPLCEA DILFTPAEKH LAEIWVSTWA YAALGLALVA TVCLLASDGS RLASAKWSRL LSPLIWCHNM VTLGWAVRFM VGRTGTACGT DPQAPNESLL TVDGLSNASC ASVFLMRYYF GMAACAWWAV LCLGWHRDIR RHSPDSKGHV VIPSNFGGSP AKRNSAKTAQ QDLTQNNFVC FVAWGLPAFQ TSAVIVARFV DADELLGACF VGNQSDKALQ ILVATPVFCY WIFGSMNLIS GYLVHCRTKE ILRNSNALSV QQQLQQLSAH SSSGIGIFLF IYGLACAMLL LAVIYEFANI DVWLGSGDTN TPLWPFLLRA FMELMLGICC FAWVLGPSIS TLYKRQVSNG KMVKHTSAGA ATGHLDGHSS SRGSHAACNS TVVSYHSVRT SMASVPLPPS PYKLKTSPGT GSISLNQMSN YSLGRSVHHQ QRHSPHHHHH QQQQHHQFHP HHNHQHHSTS SHRLYYPPGS YASQKYSQHG SYYPHLQQYG NETLL // ID FSH_DROME STANDARD; PRT; 2038 AA. AC P13709; P13710; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Female sterile homeotic protein (Fragile-chorion membrane protein). GN FS(1)H OR FSH. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89276730; PubMed=2567251; RA Haynes S.R., Mozer B.A., Bhatia-Dey N., Dawid I.B.; RT "The Drosophila fsh locus, a maternal effect homeotic gene, encodes RT apparent membrane proteins."; RL Dev. Biol. 134:246-257(1989). CC -!- FUNCTION: REQUIRED MATERNALLY FOR PROPER EXPRESSION OF OTHER CC HOMEOTIC GENES INVOLVED IN PATTERN FORMATION, SUCH AS UBX. CC -!- SIMILARITY: HIGH, TO HUMAN RING3 PROTEIN. CC -!- SIMILARITY: CONTAINS 2 BROMODOMAINS. CC -!- SIMILARITY: CONTAINS 1 ET DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23221; AAA28540.1; -. DR EMBL; M23222; AAA28541.1; ALT_TERM. DR EMBL; M15762; AAA70424.1; -. DR EMBL; M15763; AAA70423.1; -. DR EMBL; M15764; AAA70422.1; -. DR PIR; A43742; A43742. DR HSSP; Q92831; 1B91. DR FlyBase; FBgn0004656; fs(1)h. DR InterPro; IPR001487; Bromodomain. DR Pfam; PF00439; bromodomain; 2. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 2. DR PROSITE; PS50014; BROMODOMAIN_2; 2. KW Developmental protein; Bromodomain; Transmembrane; Repeat. FT DOMAIN 51 123 BROMODOMAIN 1. FT DOMAIN 495 567 BROMODOMAIN 2. FT DOMAIN 945 1106 ET DOMAIN. FT TRANSMEM 330 350 POTENTIAL. FT TRANSMEM 451 471 POTENTIAL. FT TRANSMEM 750 770 POTENTIAL. FT TRANSMEM 790 810 POTENTIAL. FT TRANSMEM 816 830 POTENTIAL. FT TRANSMEM 874 894 POTENTIAL. FT TRANSMEM 1731 1751 POTENTIAL. FT TRANSMEM 1939 1959 POTENTIAL. FT VARIANT 909 909 G -> A. FT VARIANT 1022 1022 H -> RKPYY. SQ SEQUENCE 2038 AA; 205332 MW; 849E0706D50A0098 CRC64; MSSSEPPPRY EPPVEPVNGI VQPPVIPPAE RPGRNTNQLQ YLIKTVMKVI WKHHFSWPFQ QPVDAKKLNL PDYHKIIKQP MDMGTIKKRL ENNYYWSAKE TIQDFNTMFN NCYVYNKPGE DVVVMAQTLE KVFLQKIESM PKEELELEPV TAKGGKKKQR APATPKSSSG GAGASTGSGT SSAAVTSGPG SGSTKVSVAA SSAQQSGLQG ATGAGGGSSS TPGTQPGSGA GGAIAARPVS AMGGTVSSTA GGAPSIPPIS TMPPHTVPGS TNTTTTAMAG GVGGPGAAGA NPNAAALMAS LLNAGQTGAY PGAPGQTAVN SSSLLDGSTA AVAAAAAAAA AAAAAAGGAA GAAGGAGTIP AVAVNAANAV QAYVNAGVSV GVDAVIPPQQ PAKIKKGVKR KADTTTPTAN AFESPYTQMD SKSAKIATRR ESNRQDLTFQ GSGYNMSPLG VSGVPGLGGL VAGGVAGVAV AKNKEKLSDA LKSCNEILKE LFSKKHSGYA WPFYKPVDAE MLGLHDYHDI IKKPMDLGTV KRKMDNREYK SAPEFAADVR LIFTNCYKYN PPDHDVVAMG RKLQDVFEMR YANIPDEPVA NAAHHHGHGH GHGHGHGHGH GHGHGHGHGH GYGGSSSLKH DASDSSSEDS SDTENESNSD EERSARLKML ESKLLGLQEE IRKLSEEASA KKKAKKKLKE KKKSIGGGSG SGSASHHCHA TGGGANAGGA GGPGSGGHGS VSVPGGVGSL GPGGAGGANL NALLGGSLVG HGGAAVAGGV PNVGALHSQV HDVAMAFSQM AGGGAAAGAG FGAGVTAAGA SSGGKAGTLA GALAAGAAAG AGGTTAGSGS SKGAKSKGGR GAKGSGAGGV GASNNAAAGN AAGGAAGAAA GAGSVGGVGG AGAAGGGNAS KRAKGSSSGG AGGGVGGANA SAGGAGARGS SKKKPSQVMN FDSEEEDTAK PMSYDEKRQL SLDINKLPGD KLGRVVHIIQ NREPSLRDSN PDEIEIDFET LKPSTLRELE SYVASCLRKK THKKPSGKSK DEQMAEKKQE LEKRLQDVTG QLGASKKTAK KDESASSKVE AVQPANPVSS SSSSSDSSSS SSSDSSSSDS SDSEAGDGDE RPPRKKKSRD SNGSNVNNPS INVVMGGNLP SGALSPTTML MGLDHVVNSN TPTSQMSNML GNANPLTAAA MLNNNNKTSL PGSNFGGAPA PGNMMHAGAG VPVAGAAVSA STGQQHNKNG PNDLSKVQPG GPINAALPPH SFAGGTATVA TSQSSGGIRI ASNLHKPSGL GGGDLGEHHA ALAAALTSGI NSTGTAGGGI NNNGGSNNNA NPLGGSHGDA MVNASLASLA SGLKQIPQFD DPVEQSLASL EFSAGSTGKS GLTDNFLMQQ HLMQPAGPQQ QQQQQQQQPF GHQQQQQQQQ QQQQQQQQQH MDYVTELLSK GAENVGGMNG NHLLNFNLDM AAAYQQKHPQ QQQQQAHNNG FNVADFGMAG FDGLNMTAAS FLDLEPSLQQ QQMQQMQLQQ QHHQQQQQQT HQQQQQHQQQ HHQQQQQQLT QQQLQQQQQQ QQQQQHLQQQ QHQQQHHQAA NKLLIIPKPI ESMMPSPPDK QQLQQHQKVL PPQQSPSDMK LHPNAAAAAA VASAQAKLVQ TFKANEQNLK NASSWSSLAS ANSPQSHTSS SSSSSKAKPA MDSFQQFRNK AKERDRLKLL EAAEKEKKNQ KEAAEKEQQR KHHKSSSSSL TSAAVAQAAA IAAATAAAAV TLGAAAAAAL ASSASNPSGG SSSGGAGSTS QQAITGDRDR DRDRERERER SGSGGGQSGN GNNSSNSANS NGPGSAGSGG SGGGGGSGPA SAGGPNSGGG GTANSNSGGG GGGGGPALLN AGSNSNSGVG SGGAASSNSN SSVGGIVGSG GPGSNSQGSS GGGGGGPASG GGMGSGAIDY GQQVAVLTQV AANAQAQHVA AAVAAQAILA ASPLGAMESG RKSVHDAQPQ ISRVEDIKAS PGGQGQSSPA QQSPQDRAAA KRAEQRRAEQ ERRRREALAG QIDMNMQSDL MAAFEETL // ID FSYA_DROME STANDARD; PRT; 696 AA. AC P25028; Q8T057; Q9W4W0; Q9W4W1; DT 01-MAY-1992 (Rel. 22, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitosis initiation protein fs(1)Ya. GN FS(1)YA OR EG:95B7.4 OR CG2707. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=91098653; PubMed=1986869; RA Lin H., Wolfner M.F.; RT "The Drosophila maternal-effect gene fs(1)Ya encodes a cell cycle- RT dependent nuclear envelope component required for embryonic RT mitosis."; RL Cell 64:49-62(1991). RN [2] RP REVISIONS. RA Liu J., Wolfner M.F.; RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CELL CYCLE-DEPENDENT NUCLEAR ENVELOPE COMPONENT CC REQUIRED FOR EMBRYONIC MITOSIS. CC -!- SUBCELLULAR LOCATION: IN THE NUCLEAR ENVELOPE DURING INTERPHASE TO CC METAPHASE, AND IN THE NUCLEOPLASM AND CYTOPLASM DURING ANAPHASE CC AND TELOPHASE. CC -!- DEVELOPMENTAL STAGE: MATERNAL PROTEIN SYNTHESIZED DURING CC POSTOOGENIC MATURATION AND PERSISTING THROUGHOUT EMBRYOGENESIS. CC -!- MISCELLANEOUS: THE OPA REPEAT-CONTAINING AND THE SER/THR-RICH CC REGIONS MIGHT BE INVOLVED IN PROTEIN-PROTEIN INTERACTIONS WITH THE CC MAYOR PROTEIN-RICH LAYER OF THE NUCLEAR ENVELOPE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M38442; AAA65184.1; -. DR EMBL; AE003425; AAF45816.2; -. DR EMBL; AL021728; CAA16819.1; -. DR EMBL; AY069542; AAL39687.1; -. DR PIR; A38436; A38436. DR PIR; T13648; T13648. DR FlyBase; FBgn0000927; fs(1)Ya. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005635; C:nuclear membrane; IDA. DR GO; GO:0006333; P:chromatin assembly/disassembly; IMP. DR GO; GO:0030261; P:chromosome condensation; IMP. DR GO; GO:0007067; P:mitosis; IMP. DR GO; GO:0007344; P:pronuclear fusion; IMP. DR InterPro; IPR007087; Znf_C2H2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; UNKNOWN_1. KW Cell cycle; Mitosis; Nuclear protein; Phosphorylation. FT DOMAIN 270 281 GLN-RICH (OPA-REPEAT). FT DOMAIN 512 520 NUCLEAR LOCALIZATION SIGNAL (PROBABLE). FT DOMAIN 534 538 NUCLEAR LOCALIZATION SIGNAL (PROBABLE). FT DOMAIN 448 696 RICH IN CHARGED AA. FT CONFLICT 270 270 MISSING (IN REF. 5). FT CONFLICT 412 412 K -> E (IN REF. 5). FT CONFLICT 673 673 L -> P (IN REF. 1). SQ SEQUENCE 696 AA; 77725 MW; C938FFFB3D9A5481 CRC64; MSFSNVLIMR QPDEGKCHIC KRVFCCGKCR QKHQFKAHAI AVREPLGLRS AGGGIIEHRH QMESGATTIY VFCPICERRP LLLREEMHGE LLAHIETCHL PLRCRKCQRN YTRVDDLREF SKCVDQQQSC TDVTGATETS KATLKKAANS TAISTQTSPS VTPISLINMR WKAKSRVTHE EFISDSVSSI RNLSSFSNSS IRRSIGQLGV NPSETMEKGK VIRSTSTPLH VESVFAKPKE PITFNASTGG HVSSIYHEEP SPTPESNPVQ QQQQQQQPLQ QRAWKMGARN KMSAATPLRQ VMSKSIQKAF VEHGGMMVHQ PPSAVVQRRV RLDLSEHSSH EAAGSSALDL RLSPAMRRTQ SESSASEVNS GSSSSYSTSR NADLCKRQFL LSAQKLTTES IIITRTNSSS QKTSSTVYNS CESVEIIRST SESAEVCHVP AITPIRVTGA GINKKQIKFE TPPKSSQQMR SNGEGDETKD QFFTPEPGTP EIPERRHRQA IVPRQLSGEF SPKKDKPKEK GLAVMALISP PLQQPRVRPP LRECRQQRVY SGVQDVGEPE VVDAEEEDEV FRPTNASTCN DKKLEAPNSG RLWSLMSSMM RLPASLRGER EKDRDRDRDS DKENAGSGSL IRRCASIAGS LVRPSARDSS MEDQQCLKRK RTQTLDSQYC SPLSPSSSSK RYRIRPREPI ERMRRQ // ID FTF1_DROME STANDARD; PRT; 1043 AA. AC P33244; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Nuclear hormone receptor FTZ-F1 (FTZ-F1 alpha). GN FTZ-F1 OR NR5A3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=91227912; PubMed=1709303; RA Lavorgna G., Ueda H., Clos J., Wu C.; RT "FTZ-F1, a steroid hormone receptor-like protein implicated in the RT activation of fushi tarazu."; RL Science 252:848-851(1991). RN [2] RP CHARACTERIZATION, AND SUBUNITS. RX MEDLINE=94217714; PubMed=8164672; RA Ohno C.K., Ueda H., Petkovich M.; RT "The Drosophila nuclear receptors FTZ-F1 alpha and FTZ-F1 beta RT compete as monomers for binding to a site in the fushi tarazu gene."; RL Mol. Cell. Biol. 14:3166-3175(1994). RN [3] RP CHARACTERIZATION, AND MUTAGENESIS. RX MEDLINE=93078768; PubMed=1448096; RA Ueda H., Sun G.-C., Murata T., Hirose S.; RT "A novel DNA-binding motif abuts the zinc finger domain of insect RT nuclear hormone receptor FTZ-F1 and mouse embryonal long terminal RT repeat-binding protein."; RL Mol. Cell. Biol. 12:5667-5672(1992). RN [4] RP CHARACTERIZATION. RX MEDLINE=97172279; PubMed=9020363; RA Guichet A., Copeland J.W.R., Erdelyi M., Hlousek D., Zavorszky P., RA Ho J., Brown S., Percival-Smith A., Krause H.M., Ephrussi A.; RT "The nuclear receptor homologue Ftz-F1 and the homeodomain protein RT Ftz are mutually dependent cofactors."; RL Nature 385:548-552(1997). RN [5] RP CHARACTERIZATION. RX MEDLINE=97172280; PubMed=9020364; RA Yu Y., Li W., Su K., Yussa M., Han W., Perrimon N., Pick L.; RT "The nuclear hormone receptor Ftz-F1 is a cofactor for the Drosophila RT homeodomain protein Ftz."; RL Nature 385:552-555(1997). CC -!- FUNCTION: ACTS AS A COFACTOR TO FUSHI TARAZU (FTZ). FACILITATES CC THE BINDING OF FTZ TO DNA. BINDS THE SEQUENCE ELEMENT 5'- CC YCYYGGYCR-3' IN THE ZEBRA ELEMENT OF FTZ. PROBABLY ALSO FUNCTION CC AS A RECEPTOR FOR A YET UNKNOWN LIGAND. CC -!- SUBUNIT: MONOMER; FORMS A COMPLEX WITH FTZ. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSION IN THE PARASEGMENTAL PRIMORDIA CC OF THE EMBRYONIC BLASTODERM. CC -!- DEVELOPMENTAL STAGE: FIRST APPEARS IN BLASTODERM EMBRYOS. IT IS CC ABSENT IN SUBSEQUENT EMBRYO STAGES, AND THEN REAPPEARS IN LATE CC EMBRYOGENESIS TO BE FOUND IN LARVAE, PUPAE AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR5 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63711; AAA28542.1; -. DR PIR; T13733; T13733. DR HSSP; P19793; 2NLL. DR TRANSFAC; T00296; -. DR FlyBase; FBgn0001078; ftz-f1. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Activator. FT DOMAIN 29 47 GLN-RICH (OPA-REPEAT). FT DOMAIN 157 171 POLY-ASN. FT DOMAIN 361 367 POLY-GLN (OPA-REPEAT). FT DOMAIN 414 497 GLY-RICH. FT DNA_BIND 510 575 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 510 530 C4-TYPE. FT ZN_FING 546 570 C4-TYPE. FT DOMAIN 688 740 GLY-RICH. FT DOMAIN 837 879 LIGAND-BINDING (POTENTIAL). FT MUTAGEN 565 565 C->S: 100-FOLD LESS BINDING. FT MUTAGEN 581 581 R->Q: 100-FOLD LESS BINDING. FT MUTAGEN 584 584 R->Q: 100-FOLD LESS BINDING. FT MUTAGEN 585 585 M->I: 10-FOLD LESS BINDING. FT MUTAGEN 586 586 R->Q: 10-FOLD LESS BINDING. FT MUTAGEN 587 588 GG->AA: NO BINDING. FT MUTAGEN 589 589 R->Q: 10-FOLD LESS REDUCED BINDING. FT MUTAGEN 591 591 K->Q: NO EFFECT ON BINDING. SQ SEQUENCE 1043 AA; 110234 MW; 0C4539F944921617 CRC64; MDTFNVPMLA ESSNTNYATE ATSNHHHLQH QHQQQHSHQQ QQQQQQQLLM PHHHKDQMLA AGSSPMLPFY SHLQLQQKDA TATIGPAAAA AAVEAATTSA NADNFSSLQT IDASQLDGGI SLSGLCDRFF VASPNPHSNS NMTLMGTATA ATTTTTNNNN NNNTNNNNNN NVEAKTVRPS NGNSVIIESV TMPSFANILF PTHRSANECI DPALLQKNPQ NPNGNNSSII VPPVEYHQLK PLEVNSSTSV STSNFLSSTT AQLLDFEVQV GKDDGHISTT TTTGPGSGSA SGSGSGSGSG SGSIASTIGT ATPTTTTSMS NTANPTRSSL HSIEELAASS CAPRAASPNS NHTSSASTTP QQQQQQQHHM QSGNHSGSNL SSDDESMSED EFGLEIDDNG GYQDTTSSHS QQSGGGGGGG GGNLLNGSSG GSSAGGGYML LPQAASSSGN NGNPNAGHMS SGSVGNGSGG AGNGGAGGNS GPGNPMGGTS ATPGHGGEVI DFKHLFEELC PVCGDKVSGY HYGLLTCESC KGFFKRTVQN KKVYTCVAER SCHIDKTQRK RCPYCRFQKC LEVGMKLEAV RADRMRGGRN KFGPMYKRDR ARKLQVMRQR QLALQALRNS MGPDIKPTPI SPGYQQAYPN MNIKQEIQIP QVSSLTQSPD SSPSPIAIAL GQVNASTGGV IATPMNAGTG GSGGGGLNGP SSVGNGNSSN GSSNGNNNSS TGNGTSGGGG GNNAGGGGGG TNSNDGLHRN GGNDSSSCHE AGIGSLQNTA DSKLCFDSGT HPSSTADALI EPLRVSPMIR EFVQSIDDRE WQTQLFALLQ KQTYNQVEVD LFELLMCKVL DQNLFSQVDW ARNTVFFKDL KVDDQMKLLQ HSWSDMLVLD HLHHRIHNGL PDETQLNNGQ VFNLMSLGLL GVPQPGDYFN ELQNKLQDLK FDMGDYVCMK FLILLNPSVR GIVNRKTVSE GHDNVQAALL DYTLTCYPSV NDKFRGLVNI LPEIHAMAVR GEDHLITCTP STVPAVRPPK RCSWRCCTPS ARDRGRENVT RNT // ID FTFB_DROME STANDARD; PRT; 808 AA. AC Q05192; Q9VID8; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nuclear hormone receptor FTZ-F1 beta (dHR39). GN HR39 OR FTZ-F1-BETA OR FTZF1-BETA OR NR5-BETA-1 OR CG4059. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=93183764; PubMed=8382937; RA Ohno C.K., Petkovich M.; RT "FTZ-F1 beta, a novel member of the Drosophila nuclear receptor RT family."; RL Mech. Dev. 40:13-24(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC TISSUE=Embryo; RX MEDLINE=93241944; PubMed=8479913; RA Ayer S., Walker N., Mosammaparast M., Nelson J.P., Shilo B.-Z., RA Benyajati C.; RT "Activation and repression of Drosophila alcohol dehydrogenase distal RT transcription by two steroid hormone receptor superfamily members RT binding to a common response element."; RL Nucleic Acids Res. 21:1619-1627(1993). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP CHARACTERIZATION, AND SUBUNITS. RX MEDLINE=94217714; PubMed=8164672; RA Ohno C.K., Ueda H., Petkovich M.; RT "The Drosophila nuclear receptors FTZ-F1 alpha and FTZ-F1 beta RT compete as monomers for binding to a site in the fushi tarazu gene."; RL Mol. Cell. Biol. 14:3166-3175(1994). CC -!- FUNCTION: ACTS AS A COFACTOR TO FUSHI TARAZU (FTZ). FACILITATES CC THE BINDING OF FTZ TO DNA. BINDS THE SEQUENCE ELEMENT 5'- CC YCYYGGYCR-3' IN THE ZEBRA ELEMENT OF FTZ. PROBABLY ALSO FUNCTION CC AS A RECEPTOR FOR A YET UNKNOWN LIGAND (BY SIMILARITY). CC -!- SUBUNIT: MONOMER; FORMS A COMPLEX WITH FTZ (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q05192-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q05192-2; Sequence=VSP_003718, VSP_003719; CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR5 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L06423; AAA28543.1; -. DR EMBL; L07551; AAA28464.1; -. DR EMBL; L07549; AAA28462.1; -. DR EMBL; L07550; AAA28463.1; -. DR EMBL; AE003669; AAF53984.1; -. DR PIR; S33708; S33708. DR HSSP; P06536; 1GDC. DR TRANSFAC; T02771; -. DR FlyBase; FBgn0010229; Hr39. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; IDA. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Activator; Alternative splicing. FT DOMAIN 36 39 POLY-THR. FT DNA_BIND 376 441 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 376 396 C4-TYPE. FT ZN_FING 412 436 C4-TYPE. FT DOMAIN 478 488 POLY-ALA. FT DOMAIN 576 585 POLY-SER. FT DOMAIN 621 663 LIGAND-BINDING (POTENTIAL). FT VARSPLIC 696 698 TCI -> VSL (in isoform Short). FT /FTId=VSP_003718. FT VARSPLIC 699 808 Missing (in isoform Short). FT /FTId=VSP_003719. FT CONFLICT 185 185 G -> E (IN REF. 3). FT CONFLICT 203 203 V -> L (IN REF. 1). FT CONFLICT 389 389 G -> F (IN REF. 2). FT CONFLICT 763 763 P -> Q (IN REF. 2). SQ SEQUENCE 808 AA; 87241 MW; 96235A940FDE5E4B CRC64; MPNMSSIKAE QQSGPLGGSS GYQVPVNMCT TTVANTTTTL GSSAGGATGS RHNVSVTNIK CELDELPSPN GNMVPVIANY VHGSLRIPLS GHSNHRESDS EEELASIENL KVRRRTAADK NGPRPMSWEG ELSDTEVNGG EELMEMEPTI KSEVVPAVAP PQPVCALQPI KTELENIAGE MQIQGKCYPQ SNTQHHAATK LKVAPTQSDP INLKFEPPLG DNSPLLAARS KSSSGGHLPL PTNPSPDSAI HSVYTHSSPS QSPLTSRHAP YTPSLSRNNS DASHSSCYSY SSEFSPTHSP IQARHAPPAG TLYGNHHGIY RQMKVEASST VPSSGQEAQN LSMDSASSNL DTVGLGSSHP ASPAGISRQQ LINSPCPICG DKISGFHYGI FSCESCKGFF KRTVQNRKNY VCVRGGPCQV SISTRKKCPA CRFEKCLQKG MKLEAIREDR TRGGRSTYQC SYTLPNSMLS PLLSPDQAAA AAAAAAVASQ QQPHQRLHQL NGFGGVPIPC STSLPASPSL AGTSVKSEEM AETGKQSLRT GSVPPLLQEI MDVEHLWQYT DAELARINQP LSAFASGSSS SSSSSGTSSG AHAQLTNPLL ASAGLSSNGE NANPDLIAHL CNVADHRLYK IVKWCKSLPL FKNISIDDQI CLLINSWCEL LLFSCCFRSI DTPGEIKMSQ GRKITLSQAK SNGLQTCIER MLNLTDHLRR LRVDRYEYVA MKVIVLLQSD TTELQEAVKV RECQEKALQS LQAYTLAHYP DTPSKFGELL LRIPDLQRTC QLGKEMLTIK TRDGADFNLL MELLRGEH // ID FTN_DROME STANDARD; PRT; 182 AA. AC P35554; Q9VW65; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Flightin (Muscle protein 27). GN FLN OR FTN OR MP27 OR CG7445. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Flight muscle; RX MEDLINE=93252994; PubMed=8486738; RA Vigoreaux J.O., Saide J.D., Valgeirsdottir K., Pardue M.L.; RT "Flightin, a novel myofibrillar protein of Drosophila RT stretch-activated muscles."; RL J. Cell Biol. 121:587-598(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: POSSIBLY INVOLVED IN THE REGULATION OF FLIGHT MUSCLES CC CONTRACTION, POSSIBLY BY MODULATING ACTIN-MYOSIN INTERACTION. CC -!- TISSUE SPECIFICITY: FOUND ONLY IN INDIRECT FLIGHT MUSCLES (IFM). CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN LATE PUPAL AND ADULT STAGES. CC -!- PTM: ISOFORMS OF FLIGHTIN ARE THOUGHT TO BE PRODUCED BY CC POSTTRANSLATIONAL MODIFICATIONS, POSSIBLY BY PHOSPHORYLATION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z18858; CAA79309.1; -. DR EMBL; AE003515; AAF49084.1; -. DR EMBL; AY060802; AAL28350.1; -. DR PIR; A46436; A46436. DR FlyBase; FBgn0005633; fln. DR GO; GO:0005863; C:striated muscle thick filament; IDA. KW Muscle protein; Phosphorylation. FT DOMAIN 1 65 ASP/GLU-RICH (ACIDIC). FT DOMAIN 66 70 POLY-PRO. FT DOMAIN 71 182 ARG/LYS-RICH (BASIC). SQ SEQUENCE 182 AA; 20656 MW; 4855356B0FD24F1E CRC64; MADEEDPWGF DDGGEEEKAA STQAGTPAPP SKAPSVASDH KADSVVAGTP ANEEAAPEEV EEIKAPPPPP EDDGYRKPVQ LYRHWVRPKF LQYKYMYNYR TNYYDDVIDY IDKKQTGVAR EIPRPQTWAE RVLRTRNISG SDIDSYAPAK RDKQLIQTLA ASIRTYNYHT KAYINQRYAS VL // ID FUR1_DROME STANDARD; PRT; 1269 AA. AC P26016; Q05817; Q27436; DT 01-MAY-1992 (Rel. 22, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Furin-like protease 1, isoforms 1/1-X/2 precursor (EC 3.4.21.75) DE (Furin 1) (Kex2-like endoprotease 1) (dKLIP-1). GN FUR1 OR CG10772. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=92008605; PubMed=1915835; RA Roebroek A.J.M., Pauli I.G.L., Zhang Y., van de Ven W.J.M.; RT "cDNA sequence of a Drosophila melanogaster gene, Dfur1, encoding a RT protein structurally related to the subtilisin-like proprotein RT processing enzyme furin."; RL FEBS Lett. 289:133-137(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1-X AND 2), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Tuebingen, and Oregon-R; TISSUE=Embryo; RX MEDLINE=93259127; PubMed=8491178; RA Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Bogaert T., RA Van de Ven W.J.M.; RT "Generation of structural and functional diversity in furin-like RT proteins in Drosophila melanogaster by alternative splicing of the RT DFur1 gene."; RL EMBO J. 12:1853-1870(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: FURIN IS LIKELY TO REPRESENT THE UBIQUITOUS ENDOPROTEASE CC ACTIVITY WITHIN CONSTITUTIVE SECRETORY PATHWAYS AND CAPABLE OF CC CLEAVAGE AT THE RX(K/R)R CONSENSUS MOTIF (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RELEASE OF MATURE PROTEINS FROM THEIR CC PROPROTEINS BY CLEAVAGE OF ARG-XAA-YAA-ARG-|-ZAA BONDS, WHERE XAA CC CAN BE ANY AMINO ACID AND YAA IS ARG OR LYS. RELEASES ALBUMIN, CC COMPLEMENT COMPONENT C3 AND VON WILLEBRAND FACTOR FROM THEIR CC RESPECTIVE PRECURSORS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. GOLGI. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1-X; Synonyms=B; CC IsoId=P26016-1; Sequence=Displayed; CC Name=1; Synonyms=F; CC IsoId=P26016-2; Sequence=VSP_005424, VSP_008042; CC Name=2; Synonyms=C, D, E; CC IsoId=P26016-3; Sequence=VSP_005424; CC Name=1-CRR; Synonyms=A; CC IsoId=P30430-1; Sequence=External; CC -!- TISSUE SPECIFICITY: IN ADULTS, ISOFORM 1-X IS EXPRESSED IN CNS, CC FAT BODY AND FEMALE REPRODUCTIVE TISSUES, AND IN EMBRYOS, IN CNS, CC TRACHEAL PITS, HINDGUT, POSTERIOR SPIRACLES AND ANAL PADS. CC -!- DEVELOPMENTAL STAGE: ISOFORMS 1-X AND 2 ARE EXPRESSED IN EMBRYOS, CC LARVAE, PUPAE AND ADULTS. HIGHEST EXPRESSION IS IN LATE EMBRYOS. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S8. FURIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X59384; CAA42027.1; -. DR EMBL; L12370; AAA28546.1; -. DR EMBL; L12369; AAA28546.1; JOINED. DR EMBL; L12370; AAA28547.1; -. DR EMBL; L12369; AAA28547.1; JOINED. DR EMBL; L12375; AAA28550.1; -. DR EMBL; L12376; AAA28549.1; -. DR EMBL; AE003751; AAF56463.2; -. DR EMBL; AE003751; AAF56464.1; -. DR EMBL; AY069590; AAL39735.1; -. DR PIR; S17546; S17546. DR PIR; S35366; S35366. DR MEROPS; S08.048; -. DR FlyBase; FBgn0004509; Fur1. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0004276; F:furin activity; IDA. DR InterPro; IPR000209; Peptidase_S8. DR InterPro; IPR002884; Peptidase_S8B. DR InterPro; IPR009020; Protease_inhib. DR Pfam; PF01483; P_proprotein; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR ProDom; PD000717; P_domain; 1. DR PROSITE; PS00136; SUBTILASE_ASP; 1. DR PROSITE; PS00137; SUBTILASE_HIS; 1. DR PROSITE; PS00138; SUBTILASE_SER; 1. KW Hydrolase; Serine protease; Glycoprotein; Signal; Transmembrane; KW Multigene family; Zymogen; Alternative splicing; Golgi stack. FT SIGNAL 1 ? POTENTIAL. FT PROPEP ? 309 POTENTIAL. FT CHAIN 310 1269 FURIN-LIKE PROTEASE 1, ISOFORMS 1/1-X/2. FT DOMAIN 310 655 SERINE PROTEASE. FT ACT_SITE 372 372 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 413 413 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 587 587 CHARGE RELAY SYSTEM (BY SIMILARITY). FT TRANSMEM 119 139 POTENTIAL. FT TRANSMEM 581 601 POTENTIAL. FT TRANSMEM 1082 1102 POTENTIAL. FT TRANSMEM 1233 1253 POTENTIAL. FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 18 18 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 28 28 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 108 108 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 333 333 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 426 426 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 606 606 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 727 727 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 814 814 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 857 857 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 897 897 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 908 908 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 994 994 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 776 1152 Missing (in isoform 1 and isoform 2). FT /FTId=VSP_005424. FT VARSPLIC 1208 1208 Q -> QQYPFPFQ (in isoform 1). FT /FTId=VSP_008042. SQ SEQUENCE 1269 AA; 138627 MW; 594E641CFB024C82 CRC64; MKNDVVRWSR QPTSNTTNSS SSSRSDSNST HKHRSKSNKL NARQLGSNAA RSCQQRSSVA TTLEDEQQTI IECDIGNFNF DCNLFKTSFL TQHKQKRSGK SSSKSKSNRS RPLAKTKAVF LLALQFSAVV FLCNINVGFV AGSVATAASS AGGSSPAAPS SAPSSPPTVA VPPPPPPSSA LKVDPNGQSP VLPPYVLDYE TGGKAKLTPN NGKFGQSGSS GSNNNHIVGH YTHTWAVHIP NGDNGMADAV AKDHGFVNLG KIFDDHYHFA HHKVSKRSLS PATHHQTRLD DDDRVHWAKQ QRAKSRSKRD FIRMRPSRTS SRAMSMVDAM SFNDSKWPQM WYLNRGGGLD MNVIPAWKMG ITGKGVVVTI LDDGLESDHP DIQDNYDPKA SYDVNSHDDD PMPHYDMTDS NRHGTRCAGE VAATANNSFC AVGIAYGASV GGVRMLDGDV TDAVEARSLS LNPQHIDIYS ASWGPDDDGK TVDGPGELAS RAFIEGTTKG RGGKGSIFIW ASGNGGREQD NCNCDGYTNS IWTLSISSAT EEGHVPWYSE KCSSTLATTY SSGGQGEKQV VTTDLHHSCT VSHTGTSASA PLAAGIAALV LQSNQNLTWR DLQHIVVRTA KPANLKDPSW SRNGVGRRVS HSFGYGLMDA AEMVRVARNW KAVPEQQRCE INAPHVDKVI PPRTHITLQL TVNHCRSVNY LEHVQAKITL TSQRRGDIQL FLRSPANTSV TLLTPRIHDN SRSGFNQWPF MSVHTWGESP QGNWQLEIHN EGRYMGHALL REWSLIFYGT TQSIGPNDPI SVPKPSGSEA TTPNSSSTTS NLHQAYSPQY PRIPPNNFGS SPSGGSKLPL GKVPPPNKSS YVTNNPLLNS APPKQGYQQI SATYGVILGK ANGKSNNNSK EKTNNKGNKS NNGNKGKSGG SSGNRKEQTT QSTIIQTSTS KNKYYRISQQ QQQKNNKQDR NGVQTQRPKA NSGEKSYDEK SRKVVGEITT NSGNGSIKAA KQVKESTTTS SNSRIPKLFE RYEKIQAIFP ELEPYENSSP KGKPKQAKQG KQFEVDLFKP TNGGNSRQGN TKKSPSVPPP SQTMATLSIL PILPAGGSSF LPDQKILKKQ QLLMAAAGVM APAQVEVEME EVHATPDYEA RKDQRKEVNG PNAQITQWDM IFYGTETPAQ PDDVANPSQS NQFNLYGNDM AHNDVEYDST GQWRNMQQVG EVGMTRDHSN TAACLKWSDR KCLGLSLLFF MIMQVFFLNF KHANDNNNKN KNNIIKCIR // ID FUR2_DROME STANDARD; PRT; 1679 AA. AC P30432; Q24301; DT 01-APR-1993 (Rel. 25, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Furin-like protease 2 precursor (EC 3.4.21.75) (Furin 2). GN FUR2 OR CG18734/CG4235. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, Tuebingen, and Iso-1; RX MEDLINE=92381036; PubMed=1512259; RA Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Kurzik-Dumke U., RA Rentrop M., Gateff E.A.F., Leunissen J.A.M., van de Ven W.J.M.; RT "Cloning and functional expression of Dfurin2, a subtilisin-like RT proprotein processing enzyme of Drosophila melanogaster with multiple RT repeats of a cysteine motif."; RL J. Biol. Chem. 267:17208-17215(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1; RX MEDLINE=95186060; PubMed=7880443; RA Roebroek A.J.M., Ayoubi T.A.Y., Creemers J.W.M., Pauli I.G.L., RA van de Ven W.J.M.; RT "The Dfur2 gene of Drosophila melanogaster: genetic organization, RT expression during embryogenesis, and pro-protein processing activity RT of its translational product Dfurin2."; RL DNA Cell Biol. 14:223-234(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: FURIN IS LIKELY TO REPRESENT THE UBIQUITOUS ENDOPROTEASE CC ACTIVITY WITHIN CONSTITUTIVE SECRETORY PATHWAYS AND CAPABLE OF CC CLEAVAGE AT THE RX(K/R)R CONSENSUS MOTIF (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RELEASE OF MATURE PROTEINS FROM THEIR CC PROPROTEINS BY CLEAVAGE OF ARG-XAA-YAA-ARG-|-ZAA BONDS, WHERE XAA CC CAN BE ANY AMINO ACID AND YAA IS ARG OR LYS. RELEASES ALBUMIN, CC COMPLEMENT COMPONENT C3 AND VON WILLEBRAND FACTOR FROM THEIR CC RESPECTIVE PRECURSORS. CC -!- TISSUE SPECIFICITY: TRANSIENT EXPRESSION IN A SUBSET OF CENTRAL CC NERVOUS SYSTEM NEURONS DURING EMBRYONIC STAGES 12-13. EXPRESSION CC IN DEVELOPING TRACHEAL TREE FROM STAGE 13 TO END OF EMBRYONIC CC DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S8. FURIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M94375; AAA28551.1; -. DR EMBL; L33831; AAA69860.1; -. DR EMBL; AE003502; AAF48598.1; -. DR PIR; A43434; A43434. DR HSSP; Q99405; 1MPT. DR MEROPS; S08.049; -. DR FlyBase; FBgn0004598; Fur2. DR GO; GO:0004276; F:furin activity; IDA. DR InterPro; IPR006212; Furin_repeat. DR InterPro; IPR009030; Grow_fac_recep. DR InterPro; IPR000209; Peptidase_S8. DR InterPro; IPR002884; Peptidase_S8B. DR InterPro; IPR009020; Protease_inhib. DR Pfam; PF00082; Peptidase_S8; 1. DR Pfam; PF01483; P_proprotein; 2. DR PRINTS; PR00723; SUBTILISIN. DR ProDom; PD000717; P_domain; 1. DR SMART; SM00261; FU; 10. DR PROSITE; PS00136; SUBTILASE_ASP; 1. DR PROSITE; PS00137; SUBTILASE_HIS; 1. DR PROSITE; PS00138; SUBTILASE_SER; 1. KW Hydrolase; Serine protease; Glycoprotein; Signal; Transmembrane; KW Multigene family; Zymogen; Repeat. FT SIGNAL 1 ? POTENTIAL. FT PROPEP ? 318 POTENTIAL. FT CHAIN 319 1679 FURIN-LIKE PROTEASE 2. FT ACT_SITE 417 417 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 456 456 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 637 637 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DOMAIN 961 1443 10 X TANDEM REPEATS, CYS-RICH. FT REPEAT 961 1006 1. FT REPEAT 1007 1056 2. FT REPEAT 1057 1103 3. FT REPEAT 1104 1152 4. FT REPEAT 1153 1204 5. FT REPEAT 1205 1253 6. FT REPEAT 1254 1298 7. FT REPEAT 1299 1345 8. FT REPEAT 1346 1392 9. FT REPEAT 1393 1443 10. FT TRANSMEM 1512 1532 POTENTIAL. FT DOMAIN 1533 1679 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 3 3 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 109 109 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 130 130 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 205 205 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 442 442 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 480 480 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 927 927 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1060 1060 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1181 1181 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1274 1274 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1277 1277 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1439 1439 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 152 153 MISSING (IN REF. 1). FT CONFLICT 177 177 V -> F (IN REF. 1). FT CONFLICT 213 213 V -> VDQL (IN REF. 1). SQ SEQUENCE 1679 AA; 183369 MW; 3F9E749F0B021CF6 CRC64; MSNTTRSSRV TIGRIGTTPQ ITDPWSSGLE KQRPSRCGGP KSLAEPTYRK IGRRKMMLHM RVHDPGTTVT QRAKETATAK LNRIYLCTFN RMAQSCIYFV LFLVILSPNT SCALRSSAGE TQNYVGILSN DSATTTYDVS SLHSSRRTNP PSSSSSSSSN VDVDYRNDRE LHKVDLVGLG GERAGQAETI SGGKYDYNYE NTHTNASAKD EIVERQSNSL DFDGVDMFGA FSIPEEAIYT NEFAVNIPAG KQMADVIATK HGFINRGQIG SLDNYYLFQH HHVSKRSLRS SRKHQGALKS ENEVKWMQQQ HEKVRRKRDG PYQDLPTYSP YNLLRQHGGY VVDPNPHLSF SPESISLASH SQRMEYRDVS SHFIFPDPLF KEQWYLNGGA KDGLDMNVGP AWQKGYTGKG VVVSILDDGI QTNHPDLAQN YDPEASFDIN GNDSDPTPQD NGDNKHGTRC AGEVAAVAFN NFCGVGVAYN ASIGGVRMLD GKVNDVVEAQ ALSLNPSHID IYSASWGPED DGSTVDGPGP LARRAFIYGV TSGRQGKGSI FVWASGNGGR YTDSCNCDGY TNSIFTLSIS SATQAGFKPW YLEECSSTLA TTYSSGTPGH DKSVATVDMD GSLRPDHICT VEHTGTSASA PLAAGICALA LEANPELTWR DMQYLVVYTS RPAPLEKENG WTLNGVKRKY SHKFGYGLMD AGAMVSLAEQ WTSVPPQHIC KSRENNEDRK IDGAYGSTLS THMDVNGCAG TINEVRYLEH VQCRITLRFF PRGNLRILLT SPMGTTSTLL FERPRDIVKS NFDDWPFLSV HFWGEKAEGR WTLQVINGGR RRVNQPGILS KWQLIFYGTS TQPMRLKSEL LNSSPQLRSP SSSNPFLFPS ASNIGQPANE GGNFNTDSFA SYLNYQNIFS SAGSDPEPAT ATLDGQNVTA AIAGGSSAES LGFTASAAQL VAAPETRDGD KKILHSCDAE CDSSGCYGRG PTQCVACSHY RLDNTCVSRC PPRSFPNQVG ICWPCHDTCE TCAGAGPDSC LTCAPAHLHV IDLAVCLQFC PDGYFENSRN RTCVPCEPNC ASCQDHPEYC TSCDHHLVMH EHKCYSACPL DTYETEDNKC AFCHSTCATC NGPTDQDCIT CRSSRYAWQN KCLISCPDGF YADKKRLECM PCQEGCKTCT SNGVCSECLQ NWTLNKRDKC IVSGSEGCSE SEFYSQVEGQ CRPCHASCGS CNGPADTSCT SCPPNRLLEQ SRCVSGCREG FFVEAGSLCS PCLHTCSQCV SRTNCSNCSK GLELQNGECR TTCADGYYSD RGICAKCYLS CHTCSGPRRN QCVQCPAGWQ LAAGECHPEC PEGFYKSDFG CQKCHHYCKT CNDAGPLACT SCPPHSMLDG GLCMECLSSQ YYDTTSATCK TCHDSCRSCF GPGQFSCKGC VPPLHLDQLN SQCVSCCQNQ TLAEKTSSAA CCNCDGETGE CKATSTGGKR RTVVGSGSAY KSSESKHGSF ENDGNAREFV LRLDSPLTAI TAIAVAICLL IITIFSIIFA VLQRNSNHVS RNSVRYRKIA NTSSGRRKNL SAKPTSDARF IFNIGEDDDT DGDNSDDELD GNVGTDINNR IVYDRKGNDH GHEFYIESTN DIDAIEFHCN GAGAQKAETQ LQRCNANGDD DDILHYDRHT NAERKNHPSS TTSRTNIRS // ID FURC_DROME STANDARD; PRT; 1101 AA. AC P30430; Q27235; Q9VBR5; DT 01-APR-1993 (Rel. 25, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Furin-like protease 1, isoform 1-CRR precursor (EC 3.4.21.75) (Furin DE 1) (Kex2-like endoprotease 1) (dKLIP-1). GN FUR1 OR CG10772. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=92185516; PubMed=1545235; RA Hayflick J.S., Wolfgang W.J., Forte M.A., Thomas G.; RT "A unique Kex2-like endoprotease from Drosophila melanogaster is RT expressed in the central nervous system during early embryogenesis."; RL J. Neurosci. 12:705-717(1992). RN [2] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Tuebingen, and Oregon-R; TISSUE=Embryo; RX MEDLINE=93259127; PubMed=8491178; RA Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Bogaert T., RA Van de Ven W.J.M.; RT "Generation of structural and functional diversity in furin-like RT proteins in Drosophila melanogaster by alternative splicing of the RT DFur1 gene."; RL EMBO J. 12:1853-1870(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: FURIN IS LIKELY TO REPRESENT THE UBIQUITOUS ENDOPROTEASE CC ACTIVITY WITHIN CONSTITUTIVE SECRETORY PATHWAYS AND CAPABLE OF CC CLEAVAGE AT THE RX(K/R)R CONSENSUS MOTIF (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RELEASE OF MATURE PROTEINS FROM THEIR CC PROPROTEINS BY CLEAVAGE OF ARG-XAA-YAA-ARG-|-ZAA BONDS, WHERE XAA CC CAN BE ANY AMINO ACID AND YAA IS ARG OR LYS. RELEASES ALBUMIN, CC COMPLEMENT COMPONENT C3 AND VON WILLEBRAND FACTOR FROM THEIR CC RESPECTIVE PRECURSORS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. GOLGI. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1-CRR; Synonyms=A; CC IsoId=P30430-1; Sequence=Displayed; CC Name=1; Synonyms=F; CC IsoId=P26016-2; Sequence=External; CC Name=1-X; Synonyms=B; CC IsoId=P26016-1; Sequence=External; CC Name=2; Synonyms=C, D, E; CC IsoId=P26016-3; Sequence=External; CC -!- TISSUE SPECIFICITY: IN ADULTS, ISOFORM 1-CRR IS EXPRESSED IN CNS, CC FAT BODY, AND FEMALE REPRODUCTIVE TISSUES, AND IN EMBRYOS, IN ANAL CC PADS, HINDGUT, DEVELOPING ANTENNOMAXILLARY COMPLEX, OENOCYTES, CC CLIPEOLABRUM, PHARYNX, TRACHEA, CNS AND DEVELOPING POSTERIOR CC SPIRACLES. CC -!- DEVELOPMENTAL STAGE: ISOFORM 1-CRR IS EXPRESSED IN EMBRYOS, CC LARVAE, PUPAE AND ADULTS. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S8. FURIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81431; AAA28467.1; -. DR EMBL; L12370; AAA28545.1; -. DR EMBL; L12369; AAA28545.1; JOINED. DR EMBL; L12372; AAA28548.1; -. DR EMBL; AE003751; AAN14051.1; -. DR MEROPS; S08.048; -. DR FlyBase; FBgn0004509; Fur1. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0004276; F:furin activity; IDA. DR InterPro; IPR006212; Furin_repeat. DR InterPro; IPR000209; Peptidase_S8. DR InterPro; IPR002884; Peptidase_S8B. DR InterPro; IPR009020; Protease_inhib. DR Pfam; PF01483; P_proprotein; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR ProDom; PD000717; P_domain; 1. DR SMART; SM00261; FU; 2. DR PROSITE; PS00136; SUBTILASE_ASP; 1. DR PROSITE; PS00137; SUBTILASE_HIS; 1. DR PROSITE; PS00138; SUBTILASE_SER; 1. KW Hydrolase; Serine protease; Glycoprotein; Signal; Transmembrane; KW Multigene family; Zymogen; Alternative splicing; Golgi stack. FT SIGNAL 1 ? POTENTIAL. FT PROPEP ? 309 POTENTIAL. FT CHAIN 310 1101 FURIN-LIKE PROTEASE 1, ISOFORM 1-CRR. FT DOMAIN 310 655 CATALYTIC. FT ACT_SITE 372 372 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 413 413 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 587 587 CHARGE RELAY SYSTEM (BY SIMILARITY). FT TRANSMEM 119 139 POTENTIAL. FT TRANSMEM 1014 1034 POTENTIAL. FT DOMAIN 847 982 CYS-RICH. FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 18 18 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 28 28 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 108 108 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 333 333 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 426 426 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 606 606 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 727 727 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 859 859 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 978 978 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 1014 1014 T -> I (IN REF. 1). SQ SEQUENCE 1101 AA; 120993 MW; 90DC38E2CACB71A0 CRC64; MKNDVVRWSR QPTSNTTNSS SSSRSDSNST HKHRSKSNKL NARQLGSNAA RSCQQRSSVA TTLEDEQQTI IECDIGNFNF DCNLFKTSFL TQHKQKRSGK SSSKSKSNRS RPLAKTKAVF LLALQFSAVV FLCNINVGFV AGSVATAASS AGGSSPAAPS SAPSSPPTVA VPPPPPPSSA LKVDPNGQSP VLPPYVLDYE TGGKAKLTPN NGKFGQSGSS GSNNNHIVGH YTHTWAVHIP NGDNGMADAV AKDHGFVNLG KIFDDHYHFA HHKVSKRSLS PATHHQTRLD DDDRVHWAKQ QRAKSRSKRD FIRMRPSRTS SRAMSMVDAM SFNDSKWPQM WYLNRGGGLD MNVIPAWKMG ITGKGVVVTI LDDGLESDHP DIQDNYDPKA SYDVNSHDDD PMPHYDMTDS NRHGTRCAGE VAATANNSFC AVGIAYGASV GGVRMLDGDV TDAVEARSLS LNPQHIDIYS ASWGPDDDGK TVDGPGELAS RAFIEGTTKG RGGKGSIFIW ASGNGGREQD NCNCDGYTNS IWTLSISSAT EEGHVPWYSE KCSSTLATTY SSGGQGEKQV VTTDLHHSCT VSHTGTSASA PLAAGIAALV LQSNQNLTWR DLQHIVVRTA KPANLKDPSW SRNGVGRRVS HSFGYGLMDA AEMVRVARNW KAVPEQQRCE INAPHVDKVI PPRTHITLQL TVNHCRSVNY LEHVQAKITL TSQRRGDIQL FLRSPANTSV TLLTPRIHDN SRSGFNQWPF MSVHTWGESP QGNWQLEIHN EGRYMAQITQ WDMIFYGTET PAQPDDVANP SQSNQFNLYG NDMAHNDVEY DSTGQWRNMQ QVGEVGMTRD HSNTAACLKW SDRKCLECND SAYMFEDQCY DVCPVHTYPL DKFQAEEDEQ DDEVTRGPVN PYSSSPMDHS LLMSNSLDDK QDPLQAEDRR RRSSLTQLVE VPSRVCAACD RSCLECYGAL ASQCSTCSPG SQLRKILNET FCYAYVVRST GMASVVDISK MDDRDTQQYM TGTTVLLLVS VIFTLMGVAV AGGIVYHRRA MARSNELYSR VSLVPGDESD SDEDELFTAH FPARKSGVNI YRDEAPSEKI FEEDEISHLV P // ID FUSE_DROME STANDARD; PRT; 805 AA. AC P23647; Q26346; Q26347; Q27412; Q9VWR7; DT 01-NOV-1991 (Rel. 20, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine-protein kinase fused (EC 2.7.1.-). GN FU OR CG6551. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Embryo, Ovary, and Pupae; RX MEDLINE=94206843; PubMed=8155575; RA Thermond P., Busson D., Guillemet E., Limbourg-Bouchon B., Preat T., RA Terracol R., Tricoire H., Lamour-Isnard C.; RT "Molecular organisation and expression pattern of the segment polarity RT gene fused of Drosophila melanogaster."; RL Mech. Dev. 44:65-80(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-155 FROM N.A., AND MUTAGENESIS. RX MEDLINE=94140077; PubMed=8307322; RA Preat T., Therond P., Limbourg-Bouchon B., Pham A., Tricoire H., RA Busson D., Lamour-Isnard C.; RT "Segmental polarity in Drosophila melanogaster: genetic dissection of RT fused in a Suppressor of fused background reveals interaction with RT costal-2."; RL Genetics 135:1047-1062(1993). RN [4] RP SEQUENCE OF 1-273 FROM N.A., AND FUNCTION. RX MEDLINE=90370097; PubMed=2168522; RA Preat T., Therond P., Lamour-Isnard C., Limbourg-Bouchon B., RA Tricoire H., Erk I., Mariol M.-C., Busson D.; RT "A putative serine/threonine protein kinase encoded by the segment- RT polarity fused gene of Drosophila."; RL Nature 347:87-89(1990). CC -!- FUNCTION: PROBABLE SERINE/THREONINE-PROTEIN KINASE; MATERNALLY CC REQUIRED FOR CORRECT PATTERNING IN THE POSTERIOR PART OF EACH CC EMBRYONIC METAMERE. MAY BE INVOLVED IN CONTROL OF CELL DIVISION CC DURING METAMORPHOSIS AND OVARIAN DEVELOPMENT. MAY INTERACT WITH CC COSTAL-2. CC -!- TISSUE SPECIFICITY: EXPRESSED IN ALL IMAGINAL DISKS, HIGHER LEVEL CC IN WING DISK. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY, CC LOW EXPRESSION IS PRESENT IN MALES, LARVAE AND PUPAE. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X80468; CAA56640.1; -. DR EMBL; L34782; AAA28552.1; -. DR EMBL; AE003509; AAF48871.1; -. DR EMBL; S69165; AAB29840.1; -. DR EMBL; S69166; AAB29841.1; -. DR EMBL; X55759; CAA39285.1; -. DR PIR; S11380; S11380. DR HSSP; Q00534; 1BI8. DR FlyBase; FBgn0001079; fu. DR GO; GO:0007293; P:egg chamber formation (sensu Insecta); IMP. DR GO; GO:0007367; P:segment polarity determination; IMP. DR GO; GO:0007224; P:smoothened signaling pathway; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Segmentation polarity protein; Developmental protein; Transferase; KW Serine/threonine-protein kinase; ATP-binding. FT DOMAIN 4 254 PROTEIN KINASE. FT NP_BIND 10 18 ATP (BY SIMILARITY). FT BINDING 33 33 ATP (BY SIMILARITY). FT ACT_SITE 149 149 BY SIMILARITY. FT MUTAGEN 139 141 MISSING: IN FU-62. FT MUTAGEN 147 147 A->T: IN FU-H63. FT CONFLICT 9 9 L -> M (IN REF. 2). FT CONFLICT 15 15 F -> L (IN REF. 1). FT CONFLICT 37 37 K -> KVSGAGQVIKQQVHTTSSHHIHVLQ (IN REF. FT 4). FT CONFLICT 174 175 EQ -> DE (IN REF. 1 AND 4). FT CONFLICT 225 225 S -> C (IN REF. 1 AND 4). FT CONFLICT 326 326 E -> D (IN REF. 1). FT CONFLICT 397 397 G -> V (IN REF. 1). FT CONFLICT 708 708 G -> S (IN REF. 1). FT CONFLICT 744 744 R -> G (IN REF. 1). SQ SEQUENCE 805 AA; 90347 MW; A7804E2749B79D0C CRC64; MNRYAVSSLV GQGSFGCVYK ATRKDDSKVV AIKVISKRGR ATKELKNLRR ECDIQARLKH PHVIEMIESF ESKTDLFVVT EFALMDLHRY LSYNGAMGEE PARRVTGHLV SALYYLHSNR ILHRDLKPQN VLLDKNMHAK LCDFGLARNM TLGTHVLTSI KGTPLYMAPE LLAEQPYDHH ADMWSLGCIA YESMAGQPPF CASSILHLVK MIKHEDVKWP STLTSECRSF LQGLLEKDPG LRISWTQLLC HPFVEGRIFI AETQAEAAKE SPFTNPEAKV KSSKQSDPEV GDLDEALAAL DFGESRQENL TTSRDSINAI APSDVEHLET DVEDNMQRVV VPFADLSYRD LSGVRAMPMV HQPVINSHTC FVSGNSNMIL NHMNDNFDFQ ASLRGGGVAA KPIVAPTVRQ SRSKDLEKRK LSQNLDNFSV RLGHSVDHEA QRKATEIATQ EKHNQENKPP AEAISYANSQ PPQQQPQQLK HSMHSTNEEK LSSDNTPPCL LPGWDSCDES QSPPIENDEW LAFLNRSVQE LLDGELDSLK QHNLVSIIVA PLRNSKAIPR VLKSVAQLLS LPFVLVDPVL IVDLELIRNV YVDVKLVPNL MYACKLLLSH KQLSDSAASA PLTTGSLSRT LRSIPELTVE ELETACSLYE LVCHLVHLQQ QFLTQFCDAV AILAASDLFL NFLTHDFRQS DSDAASVRLA GCMLALMGCV LRELPENAEL VERIVFNPRL NFVSLLQSRH HLLRQRSCQL LRLLARFSLR GVQRIWNGEL RFALQQLSEH HSYPALRGEA AQTLDEISHF TFFVT // ID FUT8_DROME STANDARD; PRT; 619 AA. AC Q9VYV5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-(1,6)-fucosyltransferase (EC 2.4.1.68) (Glycoprotein 6-alpha-L- DE fucosyltransferase) (GDP-fucose--glycoprotein fucosyltransferase) DE (GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase) DE (alpha1-6FucT). GN FUCT6 OR CG2448. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Petit D., Picaud F., Dupuy F., Germot A., Julien R., Maftah A.; RT "Core a3- and a6-fucosyltransferases in Drosophila: characterization RT and origin of diversity."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP HOMOLOGY. RX MEDLINE=21671316; PubMed=11698403; RA Roos C., Kolmer M., Mattila P., Renkonen R.; RT "Composition of Drosophila melanogaster proteome involved in RT fucosylated glycan metabolism."; RL J. Biol. Chem. 277:3168-3175(2002). CC -!- FUNCTION: CATALYZES THE ADDITION OF FUCOSE IN ALPHA 1-6 LINKAGE TO CC THE FIRST GLCNAC RESIDUE, NEXT TO THE PEPTIDE CHAINS IN N-GLYCANS CC (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: GDP-L-FUCOSE + N(4)-{N-ACETYL-BETA-D- CC GLUCOSAMINYL-(1->2)-ALPHA-D-MANNOSYL-(1->3)-[N-ACETYL-BETA-D- CC GLUCOSAMINYL-(1->2)-ALPHA-D-MANNOSYL-(1->6)]-BETA-D-MANNOSYL- CC (1->4)-N-ACETYL-BETA-D-GLUCOSAMINYL-(1->4)-N-ACETYL-BETA-D- CC GLUCOSAMINYL}ASPARAGINE = GDP + N(4)-{N-ACETYL-BETA-D- CC GLUCOSAMINYL-(1->2)-ALPHA-D-MANNOSYL-(1->3)-[N-ACETYL-BETA-D- CC GLUCOSAMINYL-(1->2)-ALPHA-D-MANNOSYL-(1->6)]-BETA-D-MANNOSYL- CC (1->4)-N-ACETYL-BETA-D-GLUCOSAMINYL-(1->4)-[ALPHA-L-FUCOSYL- CC (1->6)]-N-ACETYL-BETA-D-GLUCOSAMINYL}ASPARAGINE. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. MEMBRANE-BOUND CC FORM IN TRANS CISTERNAE OF GOLGI (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 23. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF441264; AAN63649.1; -. DR EMBL; AE003487; AAF48079.1; -. DR EMBL; AY051451; AAK92875.1; -. DR FlyBase; FBgn0030327; FucT6. DR GO; GO:0030173; C:integral to Golgi membrane; ISS. DR GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase a...; ISS. DR GO; GO:0006486; P:protein amino acid glycosylation; ISS. DR InterPro; IPR001452; SH3. DR Pfam; PF00018; SH3; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS50002; SH3; FALSE_NEG. KW Transferase; Glycosyltransferase; Transmembrane; Signal-anchor; KW Golgi stack; SH3 domain. FT DOMAIN 1 17 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 18 38 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 39 619 LUMENAL, CATALYTIC (POTENTIAL). FT DOMAIN 548 609 SH3. FT SITE 345 351 SH3-BINDING (POTENTIAL). FT SITE 411 412 IMPORTANT FOR DONOR SUBSTRATE BINDING (BY FT SIMILARITY). SQ SEQUENCE 619 AA; 70205 MW; 691BFD9B5C6557DE CRC64; MLLVRQLFGA SANSWARALI IFVLAWIGLV YVFVVKLTNT QGQQAAGESE LNARRISQAL QMLEHTRQRN EELKQLIDEL MSDQLDKQSA MKLVQRLEND ALNPKLAPEV AGPEPESMFE SAPADLRGWN NVAEGAPNDL EAGVPDHGEF EPSLEYEFTR RRIQTNIGEI WNFFSSELGK VRKAVAAGHA SADLEESINQ VLLQGAEHKR SLLSDMERMR QSDGYEAWRH KEARDLSDLV QRRLHHLQNP SDCQNARKLV CKLNKGCGYG CQLHHVVYCF IVAYATERTL ILKSRGWRYH KGGWEEVFQP VSNSCHDAGT ANTYNWPGKP NTQVLVLPII DSLMPRPPYL PLAVPEDLAP RLKRLHGDPI VWWVGQFLKY LLRPQPTTRD FLTSGMRNLG WERPIVGVHV RRTDKVGTEA ACHSVEEYMT YVEDYYRTLE VNGSTVARRI FLASDDAQVI EEARRKYPQY QIIGDPEVAR MASVSTRYTD TALNGIILDI HLLSMSDHLV CTFSSQVCRV AYEIMQTMYP DAAHRFKSLD DIYYYGGQNA HNRRVVIAHK PRTHEDLQLR VGDLVSVAGN HWDGNSKGKN TRTNQGGLFP SFKVEEKVDT AKLPLYAGI // ID FUTA_DROME STANDARD; PRT; 503 AA. AC Q9VUL9; Q8SYT5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glycoprotein 3-alpha-L-fucosyltransferase A (EC 2.4.1.214) (Core DE alpha-(1,3)-fucosyltransferase). GN FUCTA OR CG6869. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC STRAIN=Canton-S; RX MEDLINE=21359431; PubMed=11382750; RA Fabini G., Freilinger A., Altmann F., Wilson I.B.H.; RT "Identification of core alpha1,3-fucosylated glycans and cloning of RT the requisite fucosyltransferase cDNA from Drosophila melanogaster: RT Potential basis of the neural anti-horseradish peroxidase epitope."; RL J. Biol. Chem. 276:28058-28067(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CATALYZES ALPHA-1,3 GLYCOSIDIC LINKAGES. CC -!- CATALYTIC ACTIVITY: GDP-L-FUCOSE + N(4)-{N-ACETYL-BETA-D- CC GLUCOSAMINYL-(1->2)-ALPHA-D-MANNOSYL-(1->3)-[N-ACETYL-BETA-D- CC GLUCOSAMINYL-(1->2)-ALPHA-D-MANNOSYL-(1->6)]-BETA-D-MANNOSYL- CC (1->4)-N-ACETYL-BETA-D-GLUCOSAMINYL-(1->4)-N-ACETYL-BETA-D- CC GLUCOSAMINYL}ASPARAGINE = GDP + N(4)-{N-ACETYL-BETA-D- CC GLUCOSAMINYL-(1->2)-ALPHA-D-MANNOSYL-(1->3)-[N-ACETYL-BETA-D- CC GLUCOSAMINYL-(1->2)-ALPHA-D-MANNOSYL-(1->6)]-BETA-D-MANNOSYL- CC (1->4)-N-ACETYL-BETA-D-GLUCOSAMINYL-(1->4)-[ALPHA-L-FUCOSYL- CC (1->3)]-N-ACETYL-BETA-D-GLUCOSAMINYL}ASPARAGINE. CC -!- COFACTOR: MANGANESE. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. MEMBRANE-BOUND CC FORM IN TRANS CISTERNAE OF GOLGI (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 10. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 112. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ302045; CAC41641.1; -. DR EMBL; AE003532; AAF49657.2; -. DR EMBL; AY071324; AAL48946.1; ALT_FRAME. DR FlyBase; FBgn0036485; FucTA. DR GO; GO:0000138; C:Golgi trans cisterna; ISS. DR GO; GO:0018392; F:glycoprotein 3-alpha-L-fucosyltransferase a...; IDA. DR GO; GO:0006486; P:protein amino acid glycosylation; IDA. DR InterPro; IPR001503; Glyco_trans_10. DR Pfam; PF00852; Glyco_transf_10; 1. KW Transferase; Glycosyltransferase; Glycoprotein; Transmembrane; KW Signal-anchor; Golgi stack. FT DOMAIN 1 10 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 11 28 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 29 503 LUMENAL, CATALYTIC (POTENTIAL). FT CARBOHYD 262 262 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 295 295 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 299 299 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 53 53 H -> Y (IN REF. 1). SQ SEQUENCE 503 AA; 59159 MW; D9DA06078E6010C2 CRC64; MRRPKISLKK YFYLTLICAL LLIFGFSLKE REIWKTLSPR SSQITTQQQQ HQHLHQLQSM DEEHPMATSS TPPPIAATLL PEVADNLVEE PEQTVLEEEE SEADRLQEPP AEKAWFFKNG EYYPKPAKTY SNRKARKRHA PRLLPHQDPY SDRIINQLMY VPHNYEEIKS SGKLKTILLY NGLGPWNVKK GRDVFLKAKC PVDTCELTAN RDLASTADMI LYKDHYIPTG IRRPSNSKQV SMLYYLECPY HTQNVKVPDA INWTATYRRD STIVAPYEKW QYYDTKVQQQ EQDINYSVNK TKKVAWFVSN CGARNGRLQY AHELQKYIEV DIYGACGNFK CSRSTADKCF EILDNDYKFY LAFENSNCKD YITEKFFVNA LNRRVLPIVM GARPEDYEVS APRRSYIHVD EFSSPKELAE YLRILDHDDE LYNSYFKWKG TGEFINTYYW CRVCATLHNE EQLRKPRWYT DLNDWWRGPG VCTTRSWRNF KARKDVISDS SDD // ID FUTB_DROME STANDARD; PRT; 443 AA. AC Q9VLC1; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-(1,3)-fucosyltransferase B (EC 2.4.1.-) (Galactoside 3-L- DE fucosyltransferase). GN FUCTB OR CG4435. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=21359431; PubMed=11382750; RA Fabini G., Freilinger A., Altmann F., Wilson I.B.H.; RT "Identification of core alpha1,3-fucosylated glycans and cloning of RT the requisite fucosyltransferase cDNA from Drosophila melanogaster: RT Potential basis of the neural anti-horseradish peroxidase epitope."; RL J. Biol. Chem. 276:28058-28067(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. MEMBRANE-BOUND CC FORM IN TRANS CISTERNAE OF GOLGI (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 10. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ302046; CAC41642.1; -. DR EMBL; AE003624; AAF52773.1; -. DR FlyBase; FBgn0032117; FucTB. DR InterPro; IPR001503; Glyco_trans_10. DR Pfam; PF00852; Glyco_transf_10; 1. KW Transferase; Glycosyltransferase; Glycoprotein; Transmembrane; KW Signal-anchor; Golgi stack. FT DOMAIN 1 6 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 7 27 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 28 443 LUMENAL, CATALYTIC (POTENTIAL). FT CARBOHYD 278 278 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 436 436 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 439 439 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 214 214 R -> SL (IN REF. 1). FT CONFLICT 408 408 V -> I (IN REF. 1). FT CONFLICT 416 416 D -> N (IN REF. 1). SQ SEQUENCE 443 AA; 51756 MW; C8FDA2CD22BFE118 CRC64; MRLAQRYGIA LVALLMVGAT VLFFWSENII NYENIKFNSP VELVWWSRDM SWNYDVQRQC GIHTCRITNK RSRRPWARGV LFYGSNIKTG DFPLPRNEHQ IWALLHEESP RNTPFVSNKE FLRHFHFTST FSRYSNLPLT TMYLPSGEAL TSKDYYVTFD GKSKYGYRPS TSVVFLQSDC DTMSGREDYV KELMKHLPID SYGSCLRNRD LPERQKDYLN NLYSPELLRF LSEYKFMIAI ENAACPDYIT EKFWRPLIMG VIPIYFGSPT IKDWEPNNKS AIFVNDFQNP QALVEYLNKL ADNKKLYNSY RQHKLNRRNP ISNKKLLHNL VTRQYHIGDS SPGASLFEKF ECAVCYHVIN TARNVKADLR HYNCPLEPVY AKMEGQKIPQ NVADWRAAME VGQCQAKVLD EFFRRDIGFN DAEFDAELNR RIEGNNCSNS SNT // ID FUTC_DROME STANDARD; PRT; 425 AA. AC P83088; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-(1,3)-fucosyltransferase C (EC 2.4.1.-) (Galactoside 3-L- DE fucosyltransferase). GN FUCTC OR CG40305. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=21359431; PubMed=11382750; RA Fabini G., Freilinger A., Altmann F., Wilson I.B.H.; RT "Identification of core alpha1,3-fucosylated glycans and cloning of RT the requisite fucosyltransferase cDNA from Drosophila melanogaster: RT Potential basis of the neural anti-horseradish peroxidase epitope."; RL J. Biol. Chem. 276:28058-28067(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. MEMBRANE-BOUND CC FORM IN TRANS CISTERNAE OF GOLGI (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 10. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ302047; CAC41643.1; -. DR FlyBase; FBgn0044872; FucTC. DR InterPro; IPR001503; Glyco_trans_10. DR Pfam; PF00852; Glyco_transf_10; 1. KW Transferase; Glycosyltransferase; Glycoprotein; Transmembrane; KW Signal-anchor; Golgi stack. FT DOMAIN 1 37 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 38 58 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 59 425 LUMENAL, CATALYTIC (POTENTIAL). FT CARBOHYD 187 187 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 230 230 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 425 AA; 49130 MW; 0E037B103ACF2EC1 CRC64; MYLGRVHCSF EVPGLLSGRV GHMSMAVRSV RLACGPRGAL LLLLLVLLGV LVVLHKVTQS PLLNQNKILQ DHLRGQHERY IQSTRTILLW TEFFGDSRWK LSWDTLGPQE LRDELHCPVY QCEISNQNAF LPAVELYDAI VFHAAEMFPL LRPVPSQRSP HQVYVFALME PPGETKHRLD DEQGFYNLTM TYRIDSDVFW PYGQLLDITA DAVVAPSVKP PWRKPPVAFN DSLVWDLWSG KTKTAAWFVS HCETLSKREV LANRLQEFFE VDIYGNCGTL SCTRGDPHCA EMLDTDYFFY LAFENSLCDD YVTEKLFDAL ERTVIPVVFG GADYSRILPP HSYVDANRFM SVEGLAQYMK LVVADPDLYV SYFWWRSHYR LTYSSPFCDL CARLHDPSFG HKTQFYHDIQ SWWFNSCRLQ SRIRL // ID G02A_DROME STANDARD; PRT; 414 AA. AC Q9W594; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 2a. GN GR2A OR EG:BACN32G11.1 OR CG18531. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY I. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003420; AAF45624.2; -. DR EMBL; AL035632; CAB38469.1; ALT_INIT. DR FlyBase; FBgn0027796; Gr2a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 44 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 45 65 1 (POTENTIAL). FT DOMAIN 66 86 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 87 107 2 (POTENTIAL). FT DOMAIN 108 149 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 150 170 3 (POTENTIAL). FT DOMAIN 171 177 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 178 198 4 (POTENTIAL). FT DOMAIN 199 254 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 255 275 5 (POTENTIAL). FT DOMAIN 276 304 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 305 325 6 (POTENTIAL). FT DOMAIN 326 381 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 382 402 7 (POTENTIAL). FT DOMAIN 403 414 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 199 199 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 349 349 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 414 AA; 47005 MW; 4DA6E5F3983703A5 CRC64; MEFGMDTLRA LEPLHRACQV CNLWPWRLAP PPDSEGILLR RSRWLELYGW TVLIAATSFT VYGLFQESSV EEKQDSESTI SSIGHTVDFI QLVGMRVAHL AALLEALWQR QAQRGFFAEL GEIDRLLSKA LRVDVEAMRI NMRRQTSRRA VWILWGYAVS QLLILGAKLL SRGDRFPIYW ISYLLPLLVC GLRYFQIFNA TQLVRQRLDV LLVALQQLQL HQKGPAVDTV LEEQEDLEEA AMDRLIAVRL VYQRVWALVA LLNRCYGLSM LMQVGNDFLA ITSNCYWMFL NFRQSAASPF DILQIVASGV WSAPHLGNVL VLSLLCDRTA QCASRLALCL HQVSVDLRNE SHNALITQFS LQLLHQRLHF SAAGFFNVDC TLLYTIVGAT TTYLIILIQF HMSESTIGSD SNGQ // ID G05A_DROME STANDARD; PRT; 444 AA. AC Q9W497; Q95NT7; Q95NX8; Q95NY8; Q95NZ9; Q95P00; Q95YH9; Q95YI0; AC Q95YI1; Q95YN5; Q95YN6; Q95YN7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Gustatory receptor for trehalose (Trehalose receptor). GN TRE OR GR5A OR GRLU.7 OR CG15779. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND VARIANTS. RC STRAIN=AK07, AK10, AK13, AK17, AK19, AK41, Canton-S, EP(X)496, HG84, RC Oregon-R, Shanghai, Singapore, Tananarive, w cv, and w cx; RX MEDLINE=21450540; PubMed=11566105; RA Ueno K., Ohta M., Morita H., Mikuni Y., Nakajima S., Yamamoto K., RA Isono K.; RT "Trehalose sensitivity in Drosophila correlates with mutations in and RT expression of the gustatory receptor gene Gr5a."; RL Curr. Biol. 11:1451-1455(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=21580278; PubMed=11704765; RA Dahanukar A., Foster K., van der Goes van Naters W.M., Carlson J.R.; RT "A Gr receptor is required for response to the sugar trehalose in RT taste neurons of Drosophila."; RL Nat. Neurosci. 4:1182-1186(2001). CC -!- FUNCTION: TASTE RECEPTOR SENSITIVE TO TREHALOSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN LABELLAR CHEMOSENSORY NEURONS. CC -!- MISCELLANEOUS: MUTANTS EXHIBIT TREHALOSE-SPECIFIC PHYSIOLOGICAL CC AND BEHAVIORAL DEFECTS (REDUCED RESPONSE BY CHEMOSENSORY NEURONS CC OF THE LABELLAR TASTE HAIRS). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003435; AAF46060.1; -. DR EMBL; AB066619; BAB68243.1; -. DR EMBL; AB066620; BAB68244.1; -. DR EMBL; AB066621; BAB68245.1; -. DR EMBL; AB066622; BAB68246.1; -. DR EMBL; AB066623; BAB68247.1; -. DR EMBL; AB066624; BAB68248.1; -. DR EMBL; AB066625; BAB68249.1; -. DR EMBL; AB066626; BAB68250.1; -. DR EMBL; AB066627; BAB68251.1; -. DR EMBL; AB066628; BAB68252.1; -. DR EMBL; AB066629; BAB68253.1; -. DR EMBL; AB066630; BAB68254.1; -. DR EMBL; AB066631; BAB68255.1; -. DR EMBL; AB066632; BAB68256.1; -. DR EMBL; AB066633; BAB68257.1; -. DR EMBL; AB066634; BAB68258.1; -. DR EMBL; AB066635; BAB68259.1; -. DR EMBL; AB066636; BAB68260.1; -. DR EMBL; AB066637; BAB68261.1; -. DR EMBL; AB066638; BAB68262.1; -. DR EMBL; AB066639; BAB68263.1; -. DR EMBL; AB066640; BAB68264.1; -. DR EMBL; AB066641; BAB68265.1; -. DR EMBL; AB066642; BAB68266.1; -. DR EMBL; AB066643; BAB68267.1; -. DR FlyBase; FBgn0003747; Tre. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; IMP. DR GO; GO:0001582; P:sweet taste perception; IMP. DR InterPro; IPR000276; GPCR_Rhodpsn. KW Receptor; G-protein coupled receptor; Glycoprotein; Transmembrane; KW Polymorphism; Multigene family. FT DOMAIN 1 56 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 57 77 1 (POTENTIAL). FT DOMAIN 78 178 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 179 199 2 (POTENTIAL). FT DOMAIN 200 214 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 215 235 3 (POTENTIAL). FT DOMAIN 236 240 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 241 261 4 (POTENTIAL). FT DOMAIN 262 305 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 306 326 5 (POTENTIAL). FT DOMAIN 327 338 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 339 359 6 (POTENTIAL). FT DOMAIN 360 410 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 411 431 7 (POTENTIAL). FT DOMAIN 432 444 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 269 269 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 406 406 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 19 19 V -> I (IN STRAINS AK07, AK10, AK13, FT AK19, AK41, HG84, OREGON-R, SHANGHAI, FT SINGAPORE, TANANARIVE AND W CV). FT VARIANT 23 23 M -> I (IN STRAIN OREGON-R). FT VARIANT 73 73 C -> S (IN STRAIN SINGAPORE). FT VARIANT 164 164 T -> A (IN STRAIN SINGAPORE). FT VARIANT 216 216 L -> H (IN STRAINS AK10, TANANARIVE FT AND W CV). FT VARIANT 218 218 A -> T (IN STRAINS AK07, AK10, AK13, FT OREGON-R, SHANGHAI, SINGAPORE, TANANARIVE FT AND W CV; DECREASED SENSITIVITY TO FT TREHALOSE). FT CONFLICT 25 36 LKNLKSGLEQIR -> MSTFILITFYNP (IN REF. 2). SQ SEQUENCE 444 AA; 51155 MW; D23CA15EC08B6C05 CRC64; MRQLKGRNRC NRAVRHLKVQ GKMWLKNLKS GLEQIRESQV RGTRKNFLHD GSFHEAVAPV LAVAQCFCLM PVCGISAPTY RGLSFNRRSW RFWYSSLYLC STSVDLAFSI RRVAHSVLDV RSVEPIVFHV SILIASWQFL NLAQLWPGLM RHWAAVERRL PGYTCCLQRA RPARRLKLVA FVLLVVSLME HLLSIISVVY YDFCPRRSDP VESYLLGASA QLFEVFPYSN WLAWLGKIQN VLLTFGWSYM DIFLMMLGMG LSEMLARLNR SLEQQVRQPM PEAYWTWSRT LYRSIVELIR EVDDAVSGIM LISFGSNLYF ICLQLLKSIN TMPSSAHAVY FYFSLLFLLS RSTAVLLFVS AINDQAREPL RLLRLVPLKG YHPEVFRFAA ELASDQVALT GLKFFNVTRK LFLAMAGTVA TYELVLIQFH EDKKTWDCSP FNLD // ID G08A_DROME STANDARD; PRT; 385 AA. AC Q9W367; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 8a. GN GR8A OR CG15371. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003446; AAF46468.3; -. DR FlyBase; FBgn0030108; Gr8a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 38 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 39 59 1 (POTENTIAL). FT DOMAIN 60 69 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 70 90 2 (POTENTIAL). FT DOMAIN 91 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 152 3 (POTENTIAL). FT DOMAIN 153 154 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 155 175 4 (POTENTIAL). FT DOMAIN 176 248 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 249 269 5 (POTENTIAL). FT DOMAIN 270 284 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 285 305 6 (POTENTIAL). FT DOMAIN 306 347 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 348 372 7 (POTENTIAL). FT DOMAIN 373 385 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 248 248 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 334 334 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 385 AA; 44484 MW; 0ED98019E80390C0 CRC64; MSGHLGRVLQ FHLRLYQVLG FHGLPLPGDG NPARTRRRLM AWSLFLLISL SALVLACLFS GEEFLYRGDM FGCANDALKY VFAELGVLAI YLETLSSQRH LANFWWLHFK LGGQKTGLVS LRSEFQQFCR YLIFLYAMMA AEVAIHLGLW QFQALTQHML LFWSTYEPLV WLTYLRNLQF VLHLELLREQ LTGLEREMGL LAEYSRFASE TGRSFPGFES FLRRRLVQKQ RIYSHVYDML KCFQGAFNFS ILAVLLTINI RIAVDCYFMY YSIYNNVINN DYYLIVPALL EIPAFIYASQ SCMVVVPRIA HQLHNIVTDS GCCSCPDLSL QIQNFSLQLL HQPIRIDCLG LTILDCSLLT RMACSVGTYM IYSIQFIPKF SNTYM // ID G10A_DROME STANDARD; PRT; 408 AA. AC P58950; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 10a. GN GR10A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [3] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003486; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0045502; Gr10a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 20 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 21 38 1 (POTENTIAL). FT DOMAIN 39 48 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 49 69 2 (POTENTIAL). FT DOMAIN 70 86 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 87 107 3 (POTENTIAL). FT DOMAIN 108 144 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 145 165 4 (POTENTIAL). FT DOMAIN 166 270 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 271 291 5 (POTENTIAL). FT DOMAIN 292 304 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 305 325 6 (POTENTIAL). FT DOMAIN 326 381 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 382 402 7 (POTENTIAL). FT DOMAIN 403 408 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 192 192 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 205 205 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 408 AA; 48391 MW; 63FEBB27DDE856AD CRC64; MTSPDERKSF WERHEFKFYR YGHVYALIYG QVVIDYVPQR ALKRGVKVLL IAYGHLFSML LIVVLPGYFC YHFRTLTDTL DRRLQLLFYV SFTNTAIKYA TVIVTYVANT VHFEAINQRC TMQRTHLEFE FKNAPQEPKR PFEFFMYFKF CLINLMMMIQ VCGIFAQYGE VGKGSVSQVR VHFAIYAFVL WNYTENMADY CYFINGSVLK YYRQFNLQLG SLRDEMDGLR PGGMLLHHCC ELSDRLEELR RRCREIHDLQ RESFRMHQFQ LIGLMLSTLI NNLTNFYTLF HMLAKQSLEE VSYPVVVGSV YATGFYIDTY IVALINEHIK LELEAVALTM RRFAEPREMD ERLTREIEHL SLELLNYQPP MLCGLLHLDR RLVYLIAVTA FSYFITLVQF DLYLRKKS // ID G10B_DROME STANDARD; PRT; 373 AA. AC Q9VYZ2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 10b. GN GR10B OR CG12622. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003486; AAF48041.1; -. DR FlyBase; FBgn0030297; Gr10b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 8 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 9 29 1 (POTENTIAL). FT DOMAIN 30 82 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 83 103 2 (POTENTIAL). FT DOMAIN 104 132 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 133 153 3 (POTENTIAL). FT DOMAIN 154 170 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 171 191 4 (POTENTIAL). FT DOMAIN 192 230 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 231 251 5 (POTENTIAL). FT DOMAIN 252 273 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 274 294 6 (POTENTIAL). FT DOMAIN 295 350 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 351 371 7 (POTENTIAL). FT DOMAIN 372 373 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 192 192 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 373 AA; 44030 MW; 57CF481BF6139B14 CRC64; MRVGKLCRLA LRFWMGLILV LGFSSHYYNP TRRRLVYSRI LQTYDWLLMV INLGAFYLYY RYAMTYFLEG MFRRQGFVNQ VSTCNVFQQL LMAVTGTWLH FLFERHVCQT YNELSRILKH DLKLKEHSRF YCLAFLAKVY NFFHNFNFAL SAIMHWGLRP FNVWDLLANL YFVYNSLARD AILVAYVLLL LNLSEALRLN GQQEHDTYSD LMKQLRRRER LLRIGRRVHR MFAWLVAIAL IYLVFFNTAT IYLGYTMFIQ KHDALGLRGR GLKMLLTVVS FLVILWDVVL LQVICEKLLA EENKICDCPE DVASSRTTYR QWEMSALRRA ITRSSPENNV LGMFRMDMRC AFALISCSLS YGIIIIQIGY IPG // ID G21A_DROME STANDARD; PRT; 447 AA. AC Q9VPT1; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 21a. GN GR21A OR GR21D.1 OR CG13948. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003588; AAF51461.1; ALT_SEQ. DR FlyBase; FBgn0041250; Gr21a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 107 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 108 128 1 (POTENTIAL). FT DOMAIN 129 146 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 147 167 2 (POTENTIAL). FT DOMAIN 168 199 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 200 220 3 (POTENTIAL). FT DOMAIN 221 230 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 231 251 4 (POTENTIAL). FT DOMAIN 252 305 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 306 326 5 (POTENTIAL). FT DOMAIN 327 338 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 339 359 6 (POTENTIAL). FT DOMAIN 360 415 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 416 436 7 (POTENTIAL). FT DOMAIN 437 447 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 378 378 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 447 AA; 51907 MW; D8B3356422E731DE CRC64; MSFWAVSRGL TPPSKVVPML NPNQRQFLED EVRYREKLKL MARGDAMEEV YVRKQETVDD PLELDKHDSF YQTTKSLLVL FQIMGVMPIH RNPPEKNLPR TGYSWGSKQV MWAIFIYSCQ TTIVVLVLRE RVKKFVTSPD KRFDEAIYNV IFISLLFTNF LLPVASWRHG PQVAIFKNMW TNYQYKFFKT TGSPIVFPNL YPLTWSLCVF SWLLSIAINL SQYFLQPDFR LWYTFAYYPI IAMLNCFCSL WYINCNAFGT ASRALSDALQ TTIRGEKPAQ KLTEYRHLWV DLSHMMQQLG RAYSNMYGMY CLVIFFTTII ATYGSISEII DHGATYKEVG LFVIVFYCMG LLYIICNEAH YASRKVGLDF QTKLLNINLT AVDAATQKEV EMLLVAINKN PPIMNLDGYA NINRELITTN ISFMATYLVV LLQFKITEQR RIGQQQA // ID G22A_DROME STANDARD; PRT; 394 AA. AC P58951; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 22a. GN GR22A OR CG31662. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY III. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003585; AAN10464.1; -. DR FlyBase; FBgn0045501; Gr22a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Multigene family. FT DOMAIN 1 16 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 17 37 1 (POTENTIAL). FT DOMAIN 38 47 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 48 68 2 (POTENTIAL). FT DOMAIN 69 148 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 149 169 3 (POTENTIAL). FT DOMAIN 170 170 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 171 191 4 (POTENTIAL). FT DOMAIN 192 256 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 257 277 5 (POTENTIAL). FT DOMAIN 278 281 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 282 302 6 (POTENTIAL). FT DOMAIN 303 361 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 362 382 7 (POTENTIAL). FT DOMAIN 383 394 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 394 AA; 46131 MW; F9A06A7362314209 CRC64; MSQPKRIHRI CKGLARFTIR ATLYGSWVLG LFPFTFDSRK RRLNRSKWLL AYGLVLNLTL LVLSMLPSTD DHNSVKVEVF QRNPLVKQVE ELVEVISLIT TLVTHLRTFS RSSELVEILN ELLVLDKNHF SKLMLSECHT FNRYVIEKGL VIILEIGSSL VLYFGIPNSK IVVYEAVCIY IVQLEVLMVV MHFHLAVIYI YRYLWIINGQ LLDMASRLRR GDSVDPDRIQ LLLWLYSRLL DLNHRLTAIY DIQVTLFMAT LFSVNIIVGH VLVICWINIT RFSLLVIFLL FPQALIINFW DLWQGIAFCD LAESTGKKTS MILKLFNDME NMDQETERRV TEFTLFCSHR RLKVCHLGLL DINYEMGFRM IITNILYVVF LVQFDYMNLK FKTD // ID G22C_DROME STANDARD; PRT; 385 AA. AC P58952; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 22c. GN GR22C OR CG31929. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: TASTE BRISTLES IN THE FORELEG AND LABIAL CC PALPS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY III. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003585; AAN10463.1; -. DR FlyBase; FBgn0045499; Gr22c. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 11 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 12 32 1 (POTENTIAL). FT DOMAIN 33 45 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 46 66 2 (POTENTIAL). FT DOMAIN 67 86 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 87 107 3 (POTENTIAL). FT DOMAIN 108 144 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 145 165 4 (POTENTIAL). FT DOMAIN 166 250 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 251 271 5 (POTENTIAL). FT DOMAIN 272 279 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 280 300 6 (POTENTIAL). FT DOMAIN 301 362 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 363 383 7 (POTENTIAL). FT DOMAIN 384 385 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 166 166 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 385 AA; 44593 MW; 4F649AE08DCD7F5B CRC64; MFASRSDLQS RLCWIILKAT LYSSWFLGVF PYRFDSRNGQ LKRSRFLLFY GLILNFFLLL KMVCSGGQKL GIPEAFARNS VLENTHYTTG MLAVFSCVVI HFLNFWGSTR VQDLANELLV LEYQQFASLN ETKCPKFNSF VIQKWLSVIG LLLSYLSIAY GLPGNNFSVE MVLINSLVQF SFNCNIMHYY IGVLLIYRYL WLINGQLLEM VTNLKLDCSV DSSRIRKYLS LYRRLLELKG YMVATYEYHM TLVLTTGLAS NFLAIYSWIV LDISMNINFI YLLIFPLFLL VNVWNLWLSI AASDLAENAG KSTQTVLKLF ADLEVKDIEL ERSVSVNEFA LLCGHCQFNF HVCGLFTINY KMGFQMIITS FLYLIYMIQF DFMNL // ID G22E_DROME STANDARD; PRT; 389 AA. AC P58953; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 22e. GN GR22E OR CG31936. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: TASTE BRISTLES ON THE LABIAL PALP, LABRAL AND CC CIBARIAL SENSE ORGANS, CHEMOSENSORY BRISTLES ON THE LEG AND CC ANTERIOR WING MARGIN. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY III. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003585; AAN10462.1; -. DR FlyBase; FBgn0045497; Gr22e. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 14 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 15 35 1 (POTENTIAL). FT DOMAIN 36 46 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 47 67 2 (POTENTIAL). FT DOMAIN 68 142 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 143 163 3 (POTENTIAL). FT DOMAIN 164 170 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 171 191 4 (POTENTIAL). FT DOMAIN 192 254 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 255 275 5 (POTENTIAL). FT DOMAIN 276 287 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 288 308 6 (POTENTIAL). FT DOMAIN 309 366 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 367 387 7 (POTENTIAL). FT DOMAIN 388 389 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 131 131 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 389 AA; 45560 MW; 502436D60B411099 CRC64; MFRPSGSGYR QKWTGLTLKG ALYGSWILGV FPFAYDSWTR TLRRSKWLIA YGFVLNAAFI LLVVTNDTES ETPLRMEVFH RNALAEQING IHDIQSLSMV SIMLLRSFWK SGDIERTLNE LEDLQHRYFR NYSLEECISF DRFVLYKGFS VVLELVSMLV LELGMSPNYS AQFFIGLGSL CLMLLAVLLG ASHFHLAVVF VYRYVWIVNR ELLKLVNKMA IGETVESERM DLLLYLYHRL LDLGQRLASI YDYQMVMVMV SFLIANVLGI YFFIIYSISL NKSLDFKILV FVQALVINML DFWLNVEICE LAERTGRQTS TILKLFNDIE NIDEKLERSI TDFALFCSHR RLRFHHCGLF YVNYEMGFRM AITSFLYLLF LIQFDYWNL // ID G22F_DROME STANDARD; PRT; 378 AA. AC P58954; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 22f. GN GR22F OR CG31932. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: TASTE BRISTLES IN THE FORELEG AND LABIAL CC PALPS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY III. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003585; AAN10461.1; ALT_INIT. DR FlyBase; FBgn0041249; Gr22f. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Multigene family. FT DOMAIN 1 13 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 14 34 1 (POTENTIAL). FT DOMAIN 35 48 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 49 69 2 (POTENTIAL). FT DOMAIN 70 88 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 89 109 3 (POTENTIAL). FT DOMAIN 110 143 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 144 164 4 (POTENTIAL). FT DOMAIN 165 178 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 179 199 5 (POTENTIAL). FT DOMAIN 200 245 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 246 266 6 (POTENTIAL). FT DOMAIN 267 354 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 355 375 7 (POTENTIAL). FT DOMAIN 376 378 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 378 AA; 44421 MW; 4EF9CCA17C3F1334 CRC64; MKMFQPRRGF SCHLAWFMLQ TTLYASWLLG LFPFTFDSRR KQLKRSRWLL LYGFVLHSLA MCLAMSSHLA SKQRRKYNAF ERNPLLEKIY MQFQVTTFFT ISVLLLMNVW KSNTVRKIAN ELLTLEGQVK DLLTLKNCPN FNCFVIKKHV AAIGQFVISI YFCLCQENSY PKILKILCCL PSVGLQLIIM HFHTEIILVY RYVWLVNETL EDSHHLSSSR IHALASLYDR LLKLSELVVA CNDLQLILML IIYLIGNTVQ IFFLIVLGVS MNKRYIYLVA SPQLIINFWD FWLNIVVCDL AGKCGDQTSK VLKLFTDLEH DDEELERSLN EFAWLCTHRK FRFQLCGLFS INHNMGFQMI ITSFLYLVYL LQFDFMNL // ID G23L_DROME STANDARD; PRT; 383 AA. AC Q9VQE7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 23a, long isoform. GN GR23A OR GR23A.1 OR CG15396. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9VQE7-1; Sequence=Displayed; CC Name=Short; CC IsoId=P83292-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS AND LABRAL SENSE ORGAN. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY IV. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003582; AAF51227.2; -. DR FlyBase; FBgn0041248; Gr23a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Multigene family; Alternative splicing. FT DOMAIN 1 26 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 27 47 1 (POTENTIAL). FT DOMAIN 48 54 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 55 75 2 (POTENTIAL). FT DOMAIN 76 77 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 78 98 3 (POTENTIAL). FT DOMAIN 99 153 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 154 174 4 (POTENTIAL). FT DOMAIN 175 246 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 247 267 5 (POTENTIAL). FT DOMAIN 268 274 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 275 295 6 (POTENTIAL). FT DOMAIN 296 352 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 353 373 7 (POTENTIAL). FT DOMAIN 374 383 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 383 AA; 43398 MW; E50394ABA1CFD973 CRC64; MVMVQSVSVY KANMKTLECL TRRFLEVIFS VLALVPLPPI SQLGWLFLSL AIRCCWIVYF IYLLDVAISF SWVAIENVGN AVGTMLFVGN SVLGFALLLE SVLKQKTHSQ LEDLRVQTEL QLQRLGMFGR SRHAAYLLPL IGVQFTCDLV RLATNFGETV SPVFCISLPL MWLLRYRYVQ LVQHVMDLNQ RSIHLRRSLL SMASGNDLWQ PYGVQECLQL QTLRTTYERI FECYETFSDC YGWGMLGLHL LTSFQFVTNA YWMIMGIYDG GNVRSLIFNG ATGIDFGTPI ATLFWHGDSG AENGRQIGCL ISKLVKPQGS KLYNDLVSEF SLQTLHQRFV VTAKDFFSLN LHLLSSMFAA VVTYLVILIQ FMFAERSSTR GSG // ID G23S_DROME STANDARD; PRT; 374 AA. AC P83292; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 23a, short isoform. GN GR23A OR GR23A.1 OR CG15396. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Short; CC IsoId=P83292-1; Sequence=Displayed; CC Name=Long; CC IsoId=Q9VQE7-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS AND LABRAL SENSE ORGAN. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY IV. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003582; AAO41162.1; -. DR FlyBase; FBgn0041248; Gr23a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Multigene family; Alternative splicing. FT DOMAIN 1 6 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 7 27 1 (POTENTIAL). FT DOMAIN 28 36 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 37 57 2 (POTENTIAL). FT DOMAIN 58 72 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 73 93 3 (POTENTIAL). FT DOMAIN 94 112 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 113 133 4 (POTENTIAL). FT DOMAIN 134 226 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 227 247 5 (POTENTIAL). FT DOMAIN 248 263 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 264 284 6 (POTENTIAL). FT DOMAIN 285 343 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 344 364 7 (POTENTIAL). FT DOMAIN 365 374 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 374 AA; 43587 MW; 11FEE5851BD3319D CRC64; MFPPTRVQAS SRVVLKIFHF ILVAFSLRSR RLSRLVLWLQ FLGWLTWFIS MWTQSVIYAQ TIDCTLDCSL RHILTFFQTV SHAFIVVTSF LDGFRIKQDQ LDEPIAFEDS DPWLAFTVLA MLVPTLGVEY LVCSNAPEYA FRIRIYHLKT LPSFLALQVQ IISFILEVMK VNIRVRQTKL QLLILARELS CRWPQRKQKP QFSDQQAHRV KDLKRRYNDL HYLFVRINGY FGGSLLTIII VHFAIFVSNS YWLFVDIRTR PWRIYAILLN LGFIFNVALQ MAAACWHCQQ SYNLGRQIGC LISKLVKPQG SKLYNDLVSE FSLQTLHQRF VVTAKDFFSL NLHLLSSMFA AVVTYLVILI QFMFAERSST RGSG // ID G28A_DROME STANDARD; PRT; 450 AA. AC Q9VM09; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 28a. GN GR28A OR CG13787. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [3] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY V. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003617; AAF52519.1; ALT_SEQ. DR FlyBase; FBgn0041247; Gr28a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 47 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 48 68 1 (POTENTIAL). FT DOMAIN 69 87 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 88 108 2 (POTENTIAL). FT DOMAIN 109 138 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 139 159 3 (POTENTIAL). FT DOMAIN 160 171 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 172 192 4 (POTENTIAL). FT DOMAIN 193 292 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 293 313 5 (POTENTIAL). FT DOMAIN 314 329 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 330 350 6 (POTENTIAL). FT DOMAIN 351 407 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 408 424 7 (POTENTIAL). FT DOMAIN 425 450 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 371 371 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 450 AA; 51856 MW; 9FCB2B611D94258F CRC64; MAFKLWERFS QADNVFQALR PLTFISLLGL APFRLNLNPR KEVQTSKFSF FAGIVHFLFF VLCFGISVKE GDSIIGYFFQ TNITRFSDGT LRLTGILAMS TIFGFAMFKR QRLVSIIQNN IVVDEIFVRL GMKLDYRRIL LSSFLISLGM LLFNVIYLCV SYSLLVSATI SPSFVTFTTF ALPHINISLM VFKFLCTTDL ARSRFSMLNE ILQDILDAHI EQLSALELSP MHSVVNHRRY SHRLRNLIST PMKRYSVTSV IRLNPEYAIK QVSNIHNLLC DICQTIEEYF TYPLLGIIAI SFLFILFDDF YILEAILNPK RLDVFEADEF FAFFLMQLIW YIVIIVLIVE GSSRTILHSS YTAAIVHKIL NITDDPELRD RLFRLSLQLS HRKVLFTAAG LFRLDRTLIF TITGAATCYL IILIQFRFTH HMDDTSSNST NNLHSIHLGD // ID G28B_DROME STANDARD; PRT; 470 AA. AC Q9VM08; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 28b. GN GR28B OR CG13788. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [3] RP CONCEPTUAL TRANSLATION, AND ALTERNATIVE SPLICING. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=C; CC IsoId=Q9VM08-1; Sequence=Displayed; CC Name=A; CC IsoId=Q9VM08-2; Sequence=VSP_002015, VSP_002019; CC Name=B; CC IsoId=Q9VM08-3; Sequence=VSP_002017, VSP_002020; CC Name=D; CC IsoId=Q9VM08-4; Sequence=VSP_002018, VSP_002021; CC Name=E; CC IsoId=Q9VM08-5; Sequence=VSP_002016, VSP_002022; CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY V. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003617; AAF52520.1; ALT_SEQ. DR FlyBase; FBgn0045495; Gr28b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family; Alternative splicing. FT DOMAIN 1 76 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 77 97 1 (POTENTIAL). FT DOMAIN 98 119 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 120 140 2 (POTENTIAL). FT DOMAIN 141 175 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 176 196 3 (POTENTIAL). FT DOMAIN 197 204 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 205 225 4 (POTENTIAL). FT DOMAIN 226 309 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 310 330 5 (POTENTIAL). FT DOMAIN 331 346 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 347 367 6 (POTENTIAL). FT DOMAIN 368 423 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 424 444 7 (POTENTIAL). FT DOMAIN 445 470 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 388 388 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 412 412 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 18 Missing (in isoform A). FT /FTId=VSP_002015. FT VARSPLIC 1 23 Missing (in isoform E). FT /FTId=VSP_002016. FT VARSPLIC 1 27 Missing (in isoform B). FT /FTId=VSP_002017. FT VARSPLIC 1 30 Missing (in isoform D). FT /FTId=VSP_002018. FT VARSPLIC 19 240 EVTPGLCQPLRRRFRRFVTAKQLYECLRPVFHVTYIHGLTS FT FYISCDTKTGKKAIKKTIFGYINGIMHIAMFVFAYSLTIYN FT NCESVASYFFRSRITYFGDLMQIVSGFIGVTVIYLTAFVPN FT HRLERCLQKFHTMDVQLQTVGVKIMYSKVLRFSYMVLISMF FT LVNVLFTGGTFSVLYSSEVAPTMALHFTFLIQHTVIAIAIA FT LFSCFTYLVEMRLVMVN -> MIRCGLDIFRGCRGRFRYWL FT SARDCYDSISLMVAIAFALGITPFLVRRNALGENSLEQSWY FT GFLNAIFRWLLLAYCYSYINLRNESLIGYFMRNHVSQISTR FT VHDVGGIIAAVFTFILPLLLRKYFLKSVKNMVQVDTQLERL FT RSPVNFNTVVGQVVLVILAVVLLDTVLLTTGLVCLAKMEVY FT ASWQLTFIFVYELLAISITICMFCLMTRTVQRRITCLH FT (in isoform A). FT /FTId=VSP_002019. FT VARSPLIC 28 241 LRRRFRRFVTAKQLYECLRPVFHVTYIHGLTSFYISCDTKT FT GKKAIKKTIFGYINGIMHIAMFVFAYSLTIYNNCESVASYF FT FRSRITYFGDLMQIVSGFIGVTVIYLTAFVPNHRLERCLQK FT FHTMDVQLQTVGVKIMYSKVLRFSYMVLISMFLVNVLFTGG FT TFSVLYSSEVAPTMALHFTFLIQHTVIAIAIALFSCFTYLV FT EMRLVMVNK -> MSALRRVRKYFISSQVYEAHVVRRKMGE FT SYLKMSCFGVFNIFIYICLCGFCYISSLRQGESIVGYFFRT FT EISTIGDRLQIFNGLIAGAVIYTSAILKRCKLLGTLTILHS FT LDTNFSNIGVRVKYSRIFRYSLLVLIFKLLILGVYFVGVFR FT LLVSLDVTPSFCVCMTFFLQHSVVSIAICLFCVIAFSFERR FT LSIINA (in isoform B). FT /FTId=VSP_002020. FT VARSPLIC 31 241 RFRRFVTAKQLYECLRPVFHVTYIHGLTSFYISCDTKTGKK FT AIKKTIFGYINGIMHIAMFVFAYSLTIYNNCESVASYFFRS FT RITYFGDLMQIVSGFIGVTVIYLTAFVPNHRLERCLQKFHT FT MDVQLQTVGVKIMYSKVLRFSYMVLISMFLVNVLFTGGTFS FT VLYSSEVAPTMALHFTFLIQHTVIAIAIALFSCFTYLVEMR FT LVMVNK -> MSFYFCEIFKPRDAFGAEQTLLLYTYLLGLT FT PFRLRGQAGERQFHLSKIGYLNAFLQLSFFSYCFLAALIEQ FT QSIVGYFFKSEISQMGDSLQKFIGMTGMSILFLCSSIRVRL FT LIHIWDRISYIDDRFLNLGVCFNYPAIMRLRLLQIFLINGV FT QLGYLISSNWMLLGNDVRPIYTAIVAFYVPQIFLLSIVMLF FT NATLHRLWQHFTVLNQ (in isoform D). FT /FTId=VSP_002021. FT VARSPLIC 24 241 LCQPLRRRFRRFVTAKQLYECLRPVFHVTYIHGLTSFYISC FT DTKTGKKAIKKTIFGYINGIMHIAMFVFAYSLTIYNNCESV FT ASYFFRSRITYFGDLMQIVSGFIGVTVIYLTAFVPNHRLER FT CLQKFHTMDVQLQTVGVKIMYSKVLRFSYMVLISMFLVNVL FT FTGGTFSVLYSSEVAPTMALHFTFLIQHTVIAIAIALFSCF FT TYLVEMRLVMVNK -> MWLLRRSVGKSGNRPHDVYTCYRL FT TIFMALCLGIVPYYVSISSEGRGKLTSSYIGYINIIIRMAI FT YMVNSFYGAVNRDTLMSNFFLTDISNVIDALQKINGMLGIF FT AILLISLLNRKELLKLLATFDRLETEAFPRVGVAMHQVAAN FT KKMNRLVIILVGSMVAYITCSFLMISLRDTTTFSISAVISF FT FSPHFIVCAVSFLAGNVMIKLRIYLSALNE (in FT isoform E). FT /FTId=VSP_002022. SQ SEQUENCE 470 AA; 53598 MW; 485C2FE5B98D2712 CRC64; MDIEMAKEPV NPTDTPDIEV TPGLCQPLRR RFRRFVTAKQ LYECLRPVFH VTYIHGLTSF YISCDTKTGK KAIKKTIFGY INGIMHIAMF VFAYSLTIYN NCESVASYFF RSRITYFGDL MQIVSGFIGV TVIYLTAFVP NHRLERCLQK FHTMDVQLQT VGVKIMYSKV LRFSYMVLIS MFLVNVLFTG GTFSVLYSSE VAPTMALHFT FLIQHTVIAI AIALFSCFTY LVEMRLVMVN KVLKNLAHQW DTRSLKAVNQ KQRSLQCLDS FSMYTIVTKD PAEIIQESME IHHLICEAAA TANKYFTYQL LTIISIAFLI IVFDAYYVLE TLLGKSKRES KFKTVEFVTF FSCQMILYLI AIISIVEGSN RAIKKSEKTG GIVHSLLNKT KSAEVKEKLQ QFSMQLMHLK INFTAAGLFN IDRTLYFTIS GALTTYLIIL LQFTSNSPNN GYGNGSSCCE TFNNMTNHTL // ID G32A_DROME STANDARD; PRT; 418 AA. AC Q9VKJ7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 32a. GN GR32A OR GR32D.1 OR CG14916. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003631; AAF53071.2; -. DR FlyBase; FBgn0041246; Gr32a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 57 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 58 78 1 (POTENTIAL). FT DOMAIN 79 84 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 85 105 2 (POTENTIAL). FT DOMAIN 106 137 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 138 158 3 (POTENTIAL). FT DOMAIN 159 171 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 172 192 4 (POTENTIAL). FT DOMAIN 193 274 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 275 295 5 (POTENTIAL). FT DOMAIN 296 305 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 306 326 6 (POTENTIAL). FT DOMAIN 327 371 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 372 392 7 (POTENTIAL). FT DOMAIN 393 394 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 108 108 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 133 133 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 338 338 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 418 AA; 47879 MW; 7998589B77315E19 CRC64; MPARNHDHPV FEDIRTILSV LKASGLMPIY EQVSDYEVGP PTKTNEFYSF FVRGVVHALT IFNVYSLFTP ISAQLFFSYR ETDNVNQWIE LLLCILTYTL TVFVCAHNTT SMLRIMNEIL QLDEEVRRQF GANLSQNFGF LVKFLVGITA CQAYIIVLKI YAVQGEITPT SYILLAFYGI QNGLTATYIV FASALLRIVY IRFHFINQLL NGYTYGQQHR RKEGGARARR QRGDVNPNVN PALMEHFPED SLFIYRMHNK LLRIYKGIND CCNLILVSFL GYSFYTVTTN CYNLFVQITG KGMVSPNILQ WCFAWLCLHV SLLALLSRSC GLTTTEANAT SQILARVYAK SKEYQNIIDK FLTKSIKQEV QFTAYGFFAI DNSTLFKIFS AVTTYLVILI QFKQLEDSKV EDPVPEQT // ID G33A_DROME STANDARD; PRT; 482 AA. AC Q9VKA5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 33a. GN GR33A OR CG17213. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003635; AAF53173.3; -. DR FlyBase; FBgn0032416; Gr33a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 41 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 42 62 1 (POTENTIAL). FT DOMAIN 63 75 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 76 96 2 (POTENTIAL). FT DOMAIN 97 135 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 136 156 3 (POTENTIAL). FT DOMAIN 157 165 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 166 186 4 (POTENTIAL). FT DOMAIN 187 326 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 327 347 5 (POTENTIAL). FT DOMAIN 348 364 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 365 385 6 (POTENTIAL). FT DOMAIN 386 448 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 449 469 7 (POTENTIAL). FT DOMAIN 470 482 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 291 291 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 300 300 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 393 393 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 482 AA; 55426 MW; 2743FD2F60A64F9B CRC64; MIQIMNWFSM VKIKKMLVIG LIPLNRQQSE TNFILDYAMM CIVPIFYVAC YLLINLSHII GLCLLDSCNS VCKLSSHLFM HLGAFLYLTI TLLSLYRRKE FFQQFDARLN DIDAVIQKCQ RVAEMDKVKV TAVKHSVAYH FTWLFLFCVF TFALYYDVRS LYLTFGNLAF IPFMVSSFPY LAGSIIQGEF IYHVSVISQR FEQINMLLEK INQEARHRHA PLTVFDIESE GKKERKTVTP ITVMDGRTTT GFGNENKFAG EMKRQEGQQK NDDDDLDTSN DEDEDDFDYD NATIAENTGN TSEANLPDLF KLHDKILALS VITNGEFGPQ CVPYMAACFV VSIFGIFLET KVNFIVGGKS RLLDYMTYLY VIWSFTTMMV AYIVLRLCCN ANNHSKQSAM IVHEIMQKKP AFMLSNDLFY NKMKSFTLQF LHWEGFFQFN GVGLFALDYT FIFSTVSAAT SYLIVLLQFD MTAILRNEGL MS // ID G36A_DROME STANDARD; PRT; 391 AA. AC P58955; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 36a. GN GR36A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [3] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY VI. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003654; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0045487; Gr36a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Multigene family. FT DOMAIN 1 3 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 4 24 1 (POTENTIAL). FT DOMAIN 25 38 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 39 59 2 (POTENTIAL). FT DOMAIN 60 73 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 74 94 3 (POTENTIAL). FT DOMAIN 95 126 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 127 147 4 (POTENTIAL). FT DOMAIN 148 165 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 166 186 5 (POTENTIAL). FT DOMAIN 187 247 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 248 268 6 (POTENTIAL). FT DOMAIN 269 290 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 291 311 7 (POTENTIAL). FT DOMAIN 312 391 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 391 AA; 45372 MW; 944EC01231A74275 CRC64; MFDWVGLLLK VLYYYGQIIG LINFEIDWQR GRVVAAQRGI LFAIAINVLI CMVLLLQISK KFNLDVYFGR ANQLHQYVII VMVSLRMASG ISAILNRWRQ RAQLMRLVEC VLRLFLKKPH VKQMSRWAIL VKFSVGVVSN FLQMAISMES LDRLGFNEFV GMASDFWMSA IINMAISQHY LVILFVRAYY HLLKTEVRQA IHESQMLSEI YPRRAAFMTK CCYLADRIDN IAKLQNQLQS IVTQLNQVFG IQGIMVYGGY YIFSVATTYI TYSLAINGIE ELHLSVRAAA LVFSWFLFYY TSAILNLFVM LKLFDDHKEM ERILEERTLF TSALDVRLEQ SFESIQLQLI RNPLKIEVLD IFTITRSSSA AMIGSIITNS IFLIQYDMEY F // ID G391_DROME STANDARD; PRT; 372 AA. AC P58956; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 39a, isoform a. GN GR39A OR GR39D.2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=a; CC IsoId=P58956-1; Sequence=Displayed; CC Name=b; CC IsoId=P58957-1; Sequence=External; CC Name=c; CC IsoId=P58958-1; Sequence=External; CC Name=d; CC IsoId=P58959-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003670; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041244; Gr39a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family; Alternative splicing. FT DOMAIN 1 32 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 33 53 1 (POTENTIAL). FT DOMAIN 54 59 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 60 80 2 (POTENTIAL). FT DOMAIN 81 122 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 123 143 3 (POTENTIAL). FT DOMAIN 144 147 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 148 168 4 (POTENTIAL). FT DOMAIN 169 224 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 225 245 5 (POTENTIAL). FT DOMAIN 246 265 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 266 286 6 (POTENTIAL). FT DOMAIN 287 348 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 349 368 7 (POTENTIAL). FT DOMAIN 369 369 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 295 295 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 372 AA; 42820 MW; 25D7A1C1742E1295 CRC64; MGTRNRKLLF FLHYQRYLGL TNLDFSKSLH IYWLHGTWSS TAIQIVVVGV FMAALLGALA ESLYYMETKS QTGNTFDNAV ILTTSVTQLL ANLWLRSQQK SQVNLLQRLS QVVELLQFEP YAVPQFRWLY RIWLLVCLIY GAMVTHFGIN WLTTMQISRV LTLIGFVYRC VLANFQFTCY TGMVVILKKL LQVQVKQLEH LVSTTTISMA GVAGCLRTHD EILLLGQREL IAVYGGVILF LFIYQVMQCI LIFYISNLEG FHSSNDLVLI FCWLAPMLFY LILPLVVNDI HNQANKTAKM LTKVPRTGTG LDRMIEKFLL KNLRQKPILT AYGFFALDKS TLFKLFTAIF TYMVILVQFK EMENSTKSIN KF // ID G392_DROME STANDARD; PRT; 381 AA. AC P58957; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 39a, isoform b. GN GR39A OR GR39D.2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=b; CC IsoId=P58957-1; Sequence=Displayed; CC Name=a; CC IsoId=P58956-1; Sequence=External; CC Name=c; CC IsoId=P58958-1; Sequence=External; CC Name=d; CC IsoId=P58959-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003670; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041244; Gr39a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family; Alternative splicing. FT DOMAIN 1 37 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 38 58 1 (POTENTIAL). FT DOMAIN 59 79 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 80 100 2 (POTENTIAL). FT DOMAIN 101 129 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 130 150 3 (POTENTIAL). FT DOMAIN 151 171 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 172 192 4 (POTENTIAL). FT DOMAIN 193 239 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 240 260 5 (POTENTIAL). FT DOMAIN 261 271 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 272 292 6 (POTENTIAL). FT DOMAIN 293 350 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 351 371 7 (POTENTIAL). FT DOMAIN 372 381 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 195 195 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 304 304 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 381 AA; 44517 MW; 20DF5B0D111FB171 CRC64; MDFQPGELCA YYRLCRYLGI FCIDYNPTKK KFRLRRSVLC YIVHFALQAY LVGCISVMVT YWRRCFKSEL TTTGNHFDRL VMVIALGILV VQNAWLIWLQ APHLRIVRQI EFYRRNHLAN VRLLLPKRLL WLIIATNVVY MANFIKTCIF EWLTDASRLF VITSLGFPLR YLVTSFTMGT YFCMVHIVRL VLDWNQSQIN AIIDESADLK MTSPNRLRLR VCLEMHDRLM LLCNDEISLV YGFIAWLSWM FASLDVTGVI YLTMVIQTKK SIVLKLITNV VWLSPTFMTC AASFMSNRVT IQANKTAKML TKVPRTGTGL DRMIEKFLLK NLRQKPILTA YGFFALDKST LFKLFTAIFT YMVILVQFKE MENSTKSINK F // ID G393_DROME STANDARD; PRT; 381 AA. AC P58958; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 39a, isoform c. GN GR39A OR GR39D.2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=c; CC IsoId=P58958-1; Sequence=Displayed; CC Name=a; CC IsoId=P58956-1; Sequence=External; CC Name=b; CC IsoId=P58957-1; Sequence=External; CC Name=d; CC IsoId=P58959-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS AND ADULT THORAX AND ABDOMEN. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003670; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041244; Gr39a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family; Alternative splicing. FT DOMAIN 1 43 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 44 64 1 (POTENTIAL). FT DOMAIN 65 78 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 79 101 2 (POTENTIAL). FT DOMAIN 102 128 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 129 149 3 (POTENTIAL). FT DOMAIN 150 172 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 173 193 4 (POTENTIAL). FT DOMAIN 194 234 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 235 255 5 (POTENTIAL). FT DOMAIN 256 273 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 274 294 6 (POTENTIAL). FT DOMAIN 295 350 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 351 371 7 (POTENTIAL). FT DOMAIN 372 381 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 36 36 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 304 304 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 381 AA; 44590 MW; 66A5C636B606728F CRC64; MKRNAFEELR VQLRTLKWLG VLRFTIDFNK CLVRENASEE RSAWLYLIGV VGITCSLIVY STYFPSHFIM GKHNTTGNCY ALINIRSCSI VTMLIYTQLY IQRFRFVALL QSILRFNQIS GSHREEGRFA FYYYTHLSLL IICMLNYAYG YWTAGVRLTT IPIYLLQYGF SYLFLGQVVV LFACIQQILL SILKYYNQVV LKNIKSSKES REFYYNFCKY NQVIWLSYTE INHCFGLLLL LVTGLILLIT PSGPFYLVST IFEGRFRQNW QFSLMSFTAI LWSLPWIVLL VLAMGRNDVQ KEANKTAKML TKVPRTGTGL DRMIEKFLLK NLRQKPILTA YGFFALDKST LFKLFTAIFT YMVILVQFKE MENSTKSINK F // ID G394_DROME STANDARD; PRT; 371 AA. AC P58959; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 39a, isoform d. GN GR39A OR GR39D.2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=d; CC IsoId=P58959-1; Sequence=Displayed; CC Name=a; CC IsoId=P58956-1; Sequence=External; CC Name=b; CC IsoId=P58957-1; Sequence=External; CC Name=c; CC IsoId=P58958-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS, AND ADULT THORAX AND WING. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003670; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041244; Gr39a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family; Alternative splicing. FT DOMAIN 1 41 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 42 62 1 (POTENTIAL). FT DOMAIN 63 80 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 81 101 2 (POTENTIAL). FT DOMAIN 102 127 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 128 148 3 (POTENTIAL). FT DOMAIN 149 161 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 162 182 4 (POTENTIAL). FT DOMAIN 183 228 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 229 249 5 (POTENTIAL). FT DOMAIN 250 263 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 264 284 6 (POTENTIAL). FT DOMAIN 285 340 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 341 361 7 (POTENTIAL). FT DOMAIN 362 371 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 294 294 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 371 AA; 42447 MW; 97BF69BB6AFC9A69 CRC64; MSKVCRDLRI YLRLLHIMGM MCWHFDSDHC QLVATSGSER YAVVYAGCIL VSTTAGFIFA LLHPSRFHIA IYNQTGNFYE AVIFRSTCVV LFLVYVILYA WRHRYRDLVQ HILRLNRRCA SSCTNQQFLH NIILYGMLTI LCFGNYLHGY TRAGLATLPL ALCMLVYIFA FLVLCLLLMF FVSLKQVMTA GLIHYNQQLC QGDLISGLRG RQQILKLCGG ELNECFGLLM LPIVALVLLM APSGPFFLIS TVLEGKFRPD ECLIMLLTSS TWDTPWMIML VLMLRTNGIS EEANKTAKML TKVPRTGTGL DRMIEKFLLK NLRQKPILTA YGFFALDKST LFKLFTAIFT YMVILVQFKE MENSTKSINK F // ID G39B_DROME STANDARD; PRT; 369 AA. AC P58960; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 39b. GN GR39B OR GR39D.1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003670; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041245; Gr39b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 32 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 33 53 1 (POTENTIAL). FT DOMAIN 54 59 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 60 80 2 (POTENTIAL). FT DOMAIN 81 122 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 123 143 3 (POTENTIAL). FT DOMAIN 144 147 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 148 168 4 (POTENTIAL). FT DOMAIN 169 224 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 225 245 5 (POTENTIAL). FT DOMAIN 246 265 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 266 286 6 (POTENTIAL). FT DOMAIN 287 348 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 349 368 7 (POTENTIAL). FT DOMAIN 369 369 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 196 196 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 305 305 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 369 AA; 42334 MW; C31B3E88B0721758 CRC64; MLYSFHPYLK YFALLGLVPW SESCAQSKFV QKVYSAILII LNAVHFGISI YFPQSAELFL SLMVNVIVFV ARIVCVTVII LQVMVHYDDY FRFCREMKYL GLRLQCELKI HVGRLKWQSY AKILALGIGF LVTVLPSIYV ALSGSLLYFW SSLLSILIIR MQFVLVLLNV ELLGHHVSLL GIRLQNVLEC HLMGANCTLD GNANRLCSLE FLLALKQSHM QLHYLFTHFN DLFGWSILGT YVVLFSDSTV NIYWTQQVLV EVYEYKYLYA TFSVFVPSFF NILVFCRCGE FCQRQSVLIG SYLRNLSCHP SIGRETSYKD LLMEFILQVE QNVLAINAEG FMSTDNSLLM SILAAKVTYL IVLMQFSSV // ID G3P1_DROME STANDARD; PRT; 332 AA. AC P07486; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase I (EC 1.2.1.12) (GAPDH I). GN GAPDH1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85234524; PubMed=2989282; RA Tso J.Y., Sun X.-H., Wu R.; RT "Structure of two unlinked Drosophila melanogaster glyceraldehyde-3- RT phosphate dehydrogenase genes."; RL J. Biol. Chem. 260:8220-8228(1985). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + PHOSPHATE + CC NAD(+) = 3-PHOSPHO-D-GLYCEROYL PHOSPHATE + NADH. CC -!- PATHWAY: SECOND PHASE OF GLYCOLYSIS; FIRST STEP. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11254; AAA28560.1; -. DR PIR; A22366; A22366. DR HSSP; P56649; 1DSS. DR FlyBase; FBgn0001091; Gapdh1. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IDA. DR GO; GO:0006096; P:glycolysis; IEP. DR InterPro; IPR000173; GAP_dhdrogenase. DR InterPro; IPR006424; GAPDH-I. DR Pfam; PF00044; gpdh; 1. DR Pfam; PF02800; gpdh_C; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD; Multigene family. FT BINDING 149 149 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 176 176 ACTIVATES THIOL GROUP DURING CATALYSIS. SQ SEQUENCE 332 AA; 35316 MW; 320E44AC5DFC6E42 CRC64; MSKIGINGFG RIGRLVLRAA IDKGASVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVAAE GGFLVVNGQK ITVFSERDPA NINWASAGAE YVVESTGVFT TIDKASTHLK GGAKKVIISA PSADAPMFVC GVNLDAYSPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA TQKTVDGPSG KLWRDGRGAA QNIIPAATGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV DLTVRLGKGA TYDEIKAKVE EASKGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KD // ID G3P2_DROME STANDARD; PRT; 332 AA. AC P07487; Q9VXM7; DT 01-APR-1988 (Rel. 07, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase II (EC 1.2.1.12) (GAPDH II). GN GAPDH2 OR CG8893. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85234524; PubMed=2989282; RA Tso J.Y., Sun X.-H., Wu R.; RT "Structure of two unlinked Drosophila melanogaster glyceraldehyde-3- RT phosphate dehydrogenase genes."; RL J. Biol. Chem. 260:8220-8228(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + PHOSPHATE + CC NAD(+) = 3-PHOSPHO-D-GLYCEROYL PHOSPHATE + NADH. CC -!- PATHWAY: SECOND PHASE OF GLYCOLYSIS; FIRST STEP. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11255; AAA28561.1; -. DR EMBL; AE003500; AAF48531.1; -. DR PIR; B22366; B22366. DR HSSP; P56649; 1SZJ. DR FlyBase; FBgn0001092; Gapdh2. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IDA. DR GO; GO:0006096; P:glycolysis; IEP. DR InterPro; IPR000173; GAP_dhdrogenase. DR InterPro; IPR006424; GAPDH-I. DR Pfam; PF00044; gpdh; 1. DR Pfam; PF02800; gpdh_C; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD; Multigene family. FT BINDING 149 149 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 176 176 ACTIVATES THIOL GROUP DURING CATALYSIS. FT CONFLICT 38 38 N -> K (IN REF. 1). SQ SEQUENCE 332 AA; 35369 MW; 5D5D274B8D3B4839 CRC64; MSKIGINGFG RIGRLVLRAA IDKGANVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVAAE GGFLVVNGQK ITVFSERDPA NINWASAGAE YIVESTGVFT TIDKASTHLK GGAKKVIISA PSADAPMFVC GVNLDAYKPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA TQKTVDGPSG KLWRDGRGAA QNIIPASTGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV DLTVRLGKGA SYDEIKAKVQ EAANGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KD // ID G43A_DROME STANDARD; PRT; 449 AA. AC Q9V4K2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 43a. GN GR43A OR GR43.1 OR CG1712. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS AND IN THE ADULT HEAD, ABDOMEN, LEG AND WING. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003841; AAF59268.2; -. DR FlyBase; FBgn0041243; Gr43a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 2 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 3 23 1 (POTENTIAL). FT DOMAIN 24 33 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 34 54 2 (POTENTIAL). FT DOMAIN 55 81 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 82 102 3 (POTENTIAL). FT DOMAIN 103 131 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 132 152 4 (POTENTIAL). FT DOMAIN 153 171 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 172 192 5 (POTENTIAL). FT DOMAIN 193 317 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 318 338 6 (POTENTIAL). FT DOMAIN 339 424 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 425 445 7 (POTENTIAL). FT DOMAIN 446 449 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 423 423 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 449 AA; 49943 MW; F8BB6BBD61CE7EAC CRC64; MEISQPSIGI FYISKVLALA PYATVRNSKG RVEIGRSWLF TVYSATLTVV MVFLTYRGLL FDANSEIPVR MKSATSKVVT ALDVSVVVMA IVSGVYCGLF SLNDTLELND RLNKIDNTLN AYNNFRRDRW RALGMAAVSL LAISILVGLD VGTWMRIAQD MNIAQSDTEL NVHWYIPFYS LYFILTGLQV NIANTAYGLG RRFGRLNRML SSSFLAENNA TSAIKPQKVS TVKNVSVNRP AMPSALHASL TKLNGETLPS EAAGDKAAAR SLILNVELLK LGYFPAKNKG LLLKSLADSH ESLGKCVHLL SNSFGIAVLF ILVSCLLHLV ATAYFLFLEL LSKRDNGYLW VQMLWICFHF LRLLMVVEPC HLAARESRKT IQIVCEIERK VHEPILAEAV KKFWQQLLVV DADFSACGLC RVNRTILTSF ASAIATYLVI LIQFQRTNG // ID G43B_DROME STANDARD; PRT; 430 AA. AC Q9V4Q0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 43b. GN GR43B OR CG1339. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003840; AAF59215.4; -. DR FlyBase; FBgn0033202; Gr43b. DR GO; GO:0016021; C:integral to membrane; ISS. DR GO; GO:0008527; F:taste receptor activity; ISS. DR GO; GO:0007607; P:taste; ISS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 31 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 32 52 1 (POTENTIAL). FT DOMAIN 53 79 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 80 100 2 (POTENTIAL). FT DOMAIN 101 110 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 111 131 3 (POTENTIAL). FT DOMAIN 132 168 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 169 189 4 (POTENTIAL). FT DOMAIN 190 277 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 278 298 5 (POTENTIAL). FT DOMAIN 299 306 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 307 327 6 (POTENTIAL). FT DOMAIN 328 396 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 397 417 7 (POTENTIAL). FT DOMAIN 418 430 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 270 270 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 430 AA; 50620 MW; 100D976FC0F3323C CRC64; MSTGSHSPEA MWSATNFRRH QRKPNQVLHR WFFKGSAWII YAIACGLHFF KLHYNERTNQ VEESQYHRIW SKIVVVLKVI LLASPYLQYF VLGLGIYIHI TLVQDSKAQN FLMSLIVLGI VIGVLRRLLI FLHLKRDRRF LKHTVNEILH ITSALEQKFG MEYKCDSTLL VVYLAKLWIL TVMLDSLWYK PYFLSSIFLY WVLLEYCFAG YFIYQLILLS WYHTIILFLQ RFIEDHANRL DIELHYHRRL IPLFELHLRI NNLHKHVRDN VSWLSTSVYL MIFTCIFNAE LLIECSLFAG DELENKIYII TDGCLGPVCV PILYVLILGM CTDRFRDAEV QLQQLFVIVQ GLYMRKVRPH LLIAMVLENE HTSLIIHQKL KPLENMIILD ITCDREFVMD YIVTVILTAL SLVQYTISTG GNISECVTHK // ID G47B_DROME STANDARD; PRT; 408 AA. AC P58961; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 47b. GN GR47B. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003486; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041241; Gr47b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 20 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 21 38 1 (POTENTIAL). FT DOMAIN 39 48 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 49 69 2 (POTENTIAL). FT DOMAIN 70 86 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 87 107 3 (POTENTIAL). FT DOMAIN 108 144 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 145 165 4 (POTENTIAL). FT DOMAIN 166 270 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 271 291 5 (POTENTIAL). FT DOMAIN 292 304 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 305 325 6 (POTENTIAL). FT DOMAIN 326 381 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 382 402 7 (POTENTIAL). FT DOMAIN 403 408 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 192 192 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 205 205 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 408 AA; 48391 MW; 63FEBB27DDE856AD CRC64; MTSPDERKSF WERHEFKFYR YGHVYALIYG QVVIDYVPQR ALKRGVKVLL IAYGHLFSML LIVVLPGYFC YHFRTLTDTL DRRLQLLFYV SFTNTAIKYA TVIVTYVANT VHFEAINQRC TMQRTHLEFE FKNAPQEPKR PFEFFMYFKF CLINLMMMIQ VCGIFAQYGE VGKGSVSQVR VHFAIYAFVL WNYTENMADY CYFINGSVLK YYRQFNLQLG SLRDEMDGLR PGGMLLHHCC ELSDRLEELR RRCREIHDLQ RESFRMHQFQ LIGLMLSTLI NNLTNFYTLF HMLAKQSLEE VSYPVVVGSV YATGFYIDTY IVALINEHIK LELEAVALTM RRFAEPREMD ERLTREIEHL SLELLNYQPP MLCGLLHLDR RLVYLIAVTA FSYFITLVQF DLYLRKKS // ID G58A_DROME STANDARD; PRT; 395 AA. AC P58962; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 58a. GN GR58A OR GR58A.1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY VII. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003585; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041239; Gr58a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 32 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 33 53 1 (POTENTIAL). FT DOMAIN 54 72 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 73 93 2 (POTENTIAL). FT DOMAIN 94 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 152 3 (POTENTIAL). FT DOMAIN 153 169 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 170 190 4 (POTENTIAL). FT DOMAIN 191 250 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 251 271 5 (POTENTIAL). FT DOMAIN 272 288 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 289 309 6 (POTENTIAL). FT DOMAIN 310 366 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 367 387 7 (POTENTIAL). FT DOMAIN 388 395 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 117 117 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 224 224 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 395 AA; 46262 MW; B68A0E8263A10A4C CRC64; MLLKFMYIYG IGCGLMPAPL KKGQFLLGYK QRWYLIYTAC LHGGLLTVLP FTFPHYMYDD SYMSSNPVLK WTFNLTNITR IMAMFSGVLL MWFRRKRILN LGENLILHCL KCKTLDNRSK KYSKLRKRVR NVLFQMLLVA NLSILLGALI LFRIHSVQRI SKTAMIVAHI TQFIYVVFMM TGICVILLVL HWQSERLQIA LKDLCSFLNH EERNSLTLSE NKANRSLGKL AKLFKLFAEN QRLVREVFRT FDLPIALLLL KMFVTNVNLV YHGVQFGNDT IETSSYTRIV GQWVVISHYW SAVLLMNVVD DVTRRSDLKM GDLLREFSHL ELVKRDFHLQ LELFSDHLRC HPSTYKVCGL FIFNKQTSLA YFFYVLVQVL VLVQFDLKNK VEKRN // ID G58B_DROME STANDARD; PRT; 408 AA. AC Q9W2B1; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 58b. GN GR58B OR GR58A.2 OR CG13495. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS, LABRAL SENSE ORGAN AND THORAX. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY VII. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003455; AAF46781.1; ALT_SEQ. DR FlyBase; FBgn0041238; Gr58b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 44 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 45 65 1 (POTENTIAL). FT DOMAIN 66 82 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 83 103 2 (POTENTIAL). FT DOMAIN 104 150 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 151 171 3 (POTENTIAL). FT DOMAIN 172 193 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 194 214 4 (POTENTIAL). FT DOMAIN 215 245 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 246 266 5 (POTENTIAL). FT DOMAIN 267 284 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 285 305 6 (POTENTIAL). FT DOMAIN 306 364 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 365 385 7 (POTENTIAL). FT DOMAIN 386 401 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 316 316 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 404 404 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 408 AA; 47852 MW; C17EF201453EB7BB CRC64; MLHPKLGRVM NVVYYHSVVF ALMSTTLRIR SCRKCLRLEK VSRTYTIYSF FVGIFLFLNL YFMVPRIMED GYMKYNIVLQ WNFFVMLFLR AIAVVSCYGT LWLKRHKIIQ LYKYSLIYWK RFGHITRAIV DKKELLDLQE SLARIMIRKI ILLYSAFLCS TVLQYQLLSV INPQIFLAFC ARLTHFLHFL CVKMGFFGVL VLLNHQFLVI HLAINALHGR KARKKWKALR SVAAMHLKTL RLARRIFDMF DIANATVFIN MFMTAINILY HAVQYSNSSI KSNGWGILFG NGLIVFNFWG TMALMEMLDS VVTSCNNTGQ QLRQLSDLPK VGPKMQRELD VFTMQLRQNR LVYKICGIVE LDKPACLSYI GSILSNVIIL MQFDLRRQRQ PINDRQYLIH LMKNKTKV // ID G59C_DROME STANDARD; PRT; 397 AA. AC Q9W1U5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 59c. GN GR59C OR GR59D.2 OR CG30186/CG13543. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY VI. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003459; AAF46958.3; -. DR FlyBase; FBgn0041235; Gr59c. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 3 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 4 24 1 (POTENTIAL). FT DOMAIN 25 39 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 40 60 2 (POTENTIAL). FT DOMAIN 61 75 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 76 96 3 (POTENTIAL). FT DOMAIN 97 166 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 167 187 4 (POTENTIAL). FT DOMAIN 188 259 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 260 280 5 (POTENTIAL). FT DOMAIN 281 284 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 285 305 6 (POTENTIAL). FT DOMAIN 306 372 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 373 393 7 (POTENTIAL). FT DOMAIN 394 397 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 61 61 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 397 AA; 46164 MW; 60CEFC8AC46F9D0E CRC64; MVDLVKTILL IAYWYGLAVG VSNFEVDWLT GEAIATRRTT IYAAVHNASL ITLLILFNLG NNSLKSEFIS ARYLHEYFFM LMTAVRISAV LLSLITRWYQ RSRFIRIWNQ ILALVRDRPQ VVRGRWYRRS IILKFVFCVL SDSLHTISDV SAQRKRITAD LIVKLSLLAT LTTIFNMIVC QYYLAMVQVI GLYKILLQDL RCLVRQAECI CSIRNRRGGV YSIQCCSLAD QLDLIAERHY FLKDRLDEMS DLFQIQSLSM SLVYFFSTMG SIYFSVCSIL YSSTGFGSTY WGLLLIVLST ASFYMDNWLS VNIGFHIRDQ QDELFRVLAD RTLFYRELDN RLEAAFENFQ LQLASNRHEF YVMGLFKMER GRLIAMLSSV ITHTMVLVQW EIQNDES // ID G59D_DROME STANDARD; PRT; 390 AA. AC P58985; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 59d. GN GR59D OR GR59D.1 OR CG30330/CG13543. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [5] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY VI. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003459; AAM68236.2; ALT_SEQ. DR FlyBase; FBgn0041236; Gr59d. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 38 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 39 59 1 (POTENTIAL). FT DOMAIN 60 75 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 76 96 2 (POTENTIAL). FT DOMAIN 97 128 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 129 149 3 (POTENTIAL). FT DOMAIN 150 156 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 157 177 4 (POTENTIAL). FT DOMAIN 178 252 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 253 273 5 (POTENTIAL). FT DOMAIN 274 283 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 284 304 6 (POTENTIAL). FT DOMAIN 305 366 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 367 383 7 (POTENTIAL). FT DOMAIN 384 390 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 243 243 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 390 AA; 44823 MW; 6FA7D30716A6FC8D CRC64; MADLLKLCLR IAYAYGRLTG VINFKIDLKT GQALVTRGAT LISVSTHLLI FALLLYQTMR KSVVNVMWKY ANSLHEYVFL VIAGFRVVCV FLELVSRWSQ RRTFVRLFNS FRRLYQRNPD IIQYCRRSIV SKFFCVTMTE TLHIIVTLAM MRNRLSIALA LRIWAVLSLT AIINVIITQY YVATACVRGR YALLNKDLQA IVTESQSLVP NGGGVFVTKC CYLADRLERI AKSQSDLQEL VENLSTAYEG EVVCLVITYY LNMLGTSYLL FSISKYGNFG NNLLVIITLC GIVYFVFYVV DCWINAFNVF YLLDAHDKMV KLLNKRTLFQ PGLDHRLEMV FENFALNLVR NPLKLHMYGL FEFGRGTSFA VFNSLLTHSL LLIQYDVQNF // ID G59E_DROME STANDARD; PRT; 399 AA. AC Q9W1N6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 59e. GN GR59E OR GR59E.2 OR CG33151/CG30181/CG15872. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT LABELLAR CHEMOSENSORY CC NEURONS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY VIII. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003461; AAF47021.2; -. DR FlyBase; FBgn0041233; Gr59e. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 2. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Multigene family. FT DOMAIN 1 33 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 34 54 1 (POTENTIAL). FT DOMAIN 55 65 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 66 86 2 (POTENTIAL). FT DOMAIN 87 120 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 121 141 3 (POTENTIAL). FT DOMAIN 142 206 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 207 227 4 (POTENTIAL). FT DOMAIN 228 250 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 251 271 5 (POTENTIAL). FT DOMAIN 272 282 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 283 303 6 (POTENTIAL). FT DOMAIN 304 361 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 362 382 7 (POTENTIAL). FT DOMAIN 383 399 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 399 AA; 45796 MW; 23BD9050493196B9 CRC64; MDSSYWENLL LTINRFLGVY PSGRVGVLRW LHTLWSLFLL MYIWTGSIVK CLEFTVEIPT IEKLLYLMEF PGNMATIAIL VYYAVLNRPL AHGAELQIER IITGLKGKAK RLVYKRHGQR TLHLMATTLV FHGLCVLVDV VNYDFEFWTT WSSNSVYNLP GLMMSLGVLQ YAQPVHFLWL VMDQMRMCLK ELKLLQRPPQ GSTKLDACYE SAFAVLVDAG GGSALMIEEM RYTCNLIEQV HSQFLLRFGL YLVLNLLNSL VSICVELYLI FNFFETPLWE ESVLLVYRLL WLAMHGGRIW FILSVNEQIL EQKCNLCQLL NELEVCSSRL QRTINRFLLQ LQRSIDQPLE ACGIVTLDTR SLGGFIGVLM AIVIFLIQIG LGNKSLMGVA LNRSNWVYV // ID G59F_DROME STANDARD; PRT; 406 AA. AC Q9W1N5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 59f. GN GR59F OR GR59E.1 OR CG30185/CG5365. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=20175760; PubMed=10710312; RA Clyne P.J., Warr C.G., Carlson J.R.; RT "Candidate taste receptors in Drosophila."; RL Science 287:1830-1834(2000). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [5] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT ABDOMEN AND WING. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY VIII. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003461; AAF47022.2; ALT_SEQ. DR FlyBase; FBgn0041234; Gr59f. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 36 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 37 57 1 (POTENTIAL). FT DOMAIN 58 69 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 70 90 2 (POTENTIAL). FT DOMAIN 91 99 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 100 120 3 (POTENTIAL). FT DOMAIN 121 154 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 155 175 4 (POTENTIAL). FT DOMAIN 176 189 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 190 210 5 (POTENTIAL). FT DOMAIN 211 259 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 260 280 6 (POTENTIAL). FT DOMAIN 281 364 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 365 385 7 (POTENTIAL). FT DOMAIN 386 406 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 315 315 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 406 AA; 47559 MW; 7548A5A2F2465614 CRC64; MRSSATKGAK LKNSPRERLS SFNPQYAERY KELYRTLFWL LLISVLANTA PITILPGCPN RFYRLVHLSW MILWYGLFVL GSYWEFVLVT TQRVSLDRYL NAIESAIYVV HIFSIMLLTW QCRNWAPKLM TNIVTSDLNR AYTIDCNRTK RFIRLQLFLV GIFACLAIFF NIWTHKFVVY RSILSINSYV MPNIISSISF AQYYLLLQGI AWRQRRLTEG LERELTHLHS PRISEVQKIR MHHANLIDFT KAVNRTFQYS ILLLFVGCFL NFNLVLFLVY QGIENPSMAD FTKWVCMLLW LAMHVGKVCS ILHFNQSIQN EHSTCLTLLS RVSYARKDIQ DTITHFIIQM RTNVRQHVVC GVINLDLKFL TTLLVASADF FIFLLQYDVT YEALSKSVQG NVTRYK // ID G63A_DROME STANDARD; PRT; 512 AA. AC Q9VZL7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 63a. GN GR63A OR CG14979. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003479; AAF47803.1; -. DR FlyBase; FBgn0035468; Gr63a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 129 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 130 150 1 (POTENTIAL). FT DOMAIN 151 166 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 167 187 2 (POTENTIAL). FT DOMAIN 188 222 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 223 243 3 (POTENTIAL). FT DOMAIN 244 252 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 253 273 4 (POTENTIAL). FT DOMAIN 274 324 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 325 345 5 (POTENTIAL). FT DOMAIN 346 350 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 351 371 6 (POTENTIAL). FT DOMAIN 372 436 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 437 457 7 (POTENTIAL). FT DOMAIN 458 512 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 431 431 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 512 AA; 57465 MW; B98BD94D6D4BFFF6 CRC64; MRPSGEKVVK GHGQGNSGHS LSGMANYYRR KKGDAVFLNA KPLNSANAQA YLYGVRKYSI GLAERLDADY EAPPLDRKKS SDSTASNNPE FKPSVFYRNI DPINWFLRII GVLPIVRHGP ARAKFEMNSA SFIYSVVFFV LLACYVGYVA NNRIHIVRSL SGPFEEAVIA YLFLVNILPI MIIPILWYEA RKIAKLFNDW DDFEVLYYQI SGHSLPLKLR QKAVYIAIVL PILSVLSVVI THVTMSDLNI NQVVPYCILD NLTAMLGAWW FLICEAMSIT AHLLAERFQK ALKHIGPAAM VADYRVLWLR LSKLTRDTGN ALCYTFVFMS LYLFFIITLS IYGLMSQLSE GFGIKDIGLT ITALWNIGLL FYICDEAHYA SVNVRTNFQK KLLMVELNWM NSDAQTEINM FLRATEMNPS TINCGGFFDV NRTLFKGLLT TMVTYLVVLL QFQISIPTDK GDSEGANNIT VVDFVMDSLD NDMSLMGAST LSTTTVGTTL PPPIMKLKGR KG // ID G64A_DROME STANDARD; PRT; 456 AA. AC P83293; Q9VZJ7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 64a. GN GR64A OR CG32261/CG14986. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003480; AAN11576.1; -. DR FlyBase; FBgn0045479; Gr64a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 61 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 62 82 1 (POTENTIAL). FT DOMAIN 83 95 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 96 116 2 (POTENTIAL). FT DOMAIN 117 128 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 129 149 3 (POTENTIAL). FT DOMAIN 150 185 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 186 206 4 (POTENTIAL). FT DOMAIN 207 238 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 239 259 5 (POTENTIAL). FT DOMAIN 260 321 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 322 342 6 (POTENTIAL). FT DOMAIN 343 351 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 352 372 7 (POTENTIAL). FT DOMAIN 373 456 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 52 52 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 217 217 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 456 AA; 52822 MW; 5466974C73495D6C CRC64; MKGPNLNFRK TPSKDNGVKQ VESLARPETP PPKFVEDSNL EFNVLASEKL PNYTNLDLFH RAVFPFMFLA QCVAIMPLVG IRESNPRRVR FAYKSIPMFV TLIFMIATSI LFLSMFTHLL KIGITAKNFV GLVFFGCVLS AYVVFIRLAK KWPAVVRIWT RTEIPFTKPP YEIPKRNLSR RVQLAALAII GLSLGEHALY QVSAILSYTR RIQMCANITT VPSFNNYMQT NYDYVFQLLP YSPIIAVLIL LINGACTFVW NYMDLFIMMI SKGLSYRFEQ ITTRIRKLEH EEVCESVFIQ IREHYVKMCE LLEFVDSAMS SLILLSCVNN LYFVCYQLLN VFNKLRWPIN YIYFWYSLLY LIGRTAFVFL TAADINEESK RGLGVLRRVS SRSWCVEVER LIFQMTTQTV ALSGKKFYFL TRRLLFGMAG TIVTYELVLL QFDEPNRRKG LQPLCA // ID G64B_DROME STANDARD; PRT; 406 AA. AC P83294; Q9VZJ7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 64b. GN GR64B OR CG32257/CG14986. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003480; AAN11577.1; -. DR FlyBase; FBgn0045478; Gr64b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 47 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 48 68 1 (POTENTIAL). FT DOMAIN 69 79 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 80 100 2 (POTENTIAL). FT DOMAIN 101 130 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 131 151 3 (POTENTIAL). FT DOMAIN 152 183 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 184 204 4 (POTENTIAL). FT DOMAIN 205 265 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 266 286 5 (POTENTIAL). FT DOMAIN 287 290 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 291 311 6 (POTENTIAL). FT DOMAIN 312 370 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 371 391 7 (POTENTIAL). FT DOMAIN 392 406 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 355 355 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 406 AA; 47488 MW; F6A37DD9E1E58B88 CRC64; MPQGETFHRA VSNVLFISQI YGLLPVSNVR ALDVADIRFR WCSPRILYSL LIGILNLSEF GAVINYVIKV TINFHTSSTL SLYIVCLLEH LFFWRLAIQW PRIMRTWHGV EQLFLRVPYR FYGEYRIKRR IYIVFTIVMS SALVEHCLLL GNSFHLSNME RTQCKINVTY FESIYKWERP HLYMILPYHF WMLPILEWVN QTIAYPRSFT DCFIMCIGIG LAARFHQLYR RIAAVHRKVM PAVFWTEVRE HYLALKRLVH LLDAAIAPLV LLAFGNNMSF ICFQLFNSFK NIGVDFLVML AFWYSLGFAV VRTLLTIFVA SSINDYERKI VTALRDVPSR AWSIEVQRFS EQLGNDTTAL SGSGFFYLTR SLVLAMGTTI ITYELMISDV INQGSIRQKT QYCREY // ID G64C_DROME STANDARD; PRT; 419 AA. AC P83295; Q9VZJ7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 64c. GN GR64C OR CG32256/CG14986. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003480; AAF47824.2; -. DR FlyBase; FBgn0045477; Gr64c. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Multigene family. FT DOMAIN 1 15 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 16 36 1 (POTENTIAL). FT DOMAIN 37 48 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 49 69 2 (POTENTIAL). FT DOMAIN 70 82 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 83 103 3 (POTENTIAL). FT DOMAIN 104 139 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 140 160 4 (POTENTIAL). FT DOMAIN 161 204 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 205 225 5 (POTENTIAL). FT DOMAIN 226 305 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 306 326 6 (POTENTIAL). FT DOMAIN 327 377 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 378 398 7 (POTENTIAL). FT DOMAIN 399 419 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 419 AA; 48889 MW; 494F0D787DC314FB CRC64; MQQSGQKGTR NTLQHAIGPV LVIAQFFGVL PVAGVWPSCR PERVRFRWIS LSLLAALILF VFSIVDCALS SKVVFDHGLK IYTIGSLSFS VICIFCFGVF LLLSRRWPYI IRRTAECEQI FLEPEYDCSY GRGYSSRLRL WGVCMLVAAL CEHSTYVGSA LYNNHLAIVE CKLDANFWQN YFQRERQQLF LIMHFTAWWI PFIEWTTLSM TFVWNFVDIF LILICRGMQM RFQQMHWRIR QHVRQQMPNE FWQRIRCDLL DLSDLLGIYD KELSGLIVLS CAHNMYFVCV QIYHSFQSKG NYADELYFWF CLSYVIIRVL NMMFAASSIP QEAKEISYTL YEIPTEFWCV ELRRLNEIFL SDHFALSGKG YFLLTRRLIF AMAATLMVYE LVLINQMAGS EVQKSFCEGG VGSSKSIFS // ID G64D_DROME STANDARD; PRT; 429 AA. AC Q9VZJ6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 64d. GN GR64D OR CG14987. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). RN [4] RP CONCEPTUAL TRANSLATION. RA Robertson H.; RL Unpublished observations (NOV-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY II. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003480; AAF47825.3; ALT_SEQ. DR FlyBase; FBgn0035486; Gr64d. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 23 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 24 44 1 (POTENTIAL). FT DOMAIN 45 57 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 58 78 2 (POTENTIAL). FT DOMAIN 79 89 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 90 110 3 (POTENTIAL). FT DOMAIN 111 150 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 151 171 4 (POTENTIAL). FT DOMAIN 172 205 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 206 226 5 (POTENTIAL). FT DOMAIN 227 314 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 315 335 6 (POTENTIAL). FT DOMAIN 336 386 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 387 407 7 (POTENTIAL). FT DOMAIN 408 429 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 370 370 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 429 AA; 50228 MW; 8358E6C0D60D5462 CRC64; MLRSHLSVHG LQMERSVQEN TLHYTIGHVL IIARIFGVLP LAGINPNGKP ENVRFRWFSP YILFFVVAFT FVIADFMLST KIVLNDGLQL YTMGSLSFSV ICIFCFGSFI KLSRRWPHII RETALCERIF LKPCYANQEG LNFTRFLRRW ALILLVAALC EHLTYVGSAA WSNYVQIRDC NLKVGFVENY FLRERQELFS VFEYRAWMVF FIEWNTMAMT FVWNFGDIFL FLMCRGLKIR FQQLHWRIRQ NLGKPMAKEF WQEIRSDFLD LDSLLKLYDK ELSGLILVCC AHNMYFICVQ VYHSFQVKGA FMDELYFWFC LLYVISRLMN MMLAASSIPQ EIKDISNTLY EVRSSPWCDE LGRLSEMLRN ETFALSGMGY FYVTRRLIFA MAGALMGYEL VLFRQMQGAV VQKSICSRGP GSSMSIFFS // ID G64E_DROME STANDARD; PRT; 451 AA. AC P83296; Q8IRC5; Q9VZJ5; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable gustatory receptor 64e. GN GR64E OR CG32258/CG14988. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003480; AAN11578.2; -. DR EMBL; BT003632; AAO39636.1; -. DR FlyBase; FBgn0045476; Gr64e. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Receptor; G-protein coupled receptor; Transmembrane; Multigene family. FT DOMAIN 1 100 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 101 121 1 (POTENTIAL). FT DOMAIN 122 130 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 131 151 2 (POTENTIAL). FT DOMAIN 152 183 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 184 204 3 (POTENTIAL). FT DOMAIN 205 223 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 224 244 4 (POTENTIAL). FT DOMAIN 245 250 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 251 271 5 (POTENTIAL). FT DOMAIN 272 344 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 345 365 6 (POTENTIAL). FT DOMAIN 366 420 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 421 441 7 (POTENTIAL). FT DOMAIN 442 446 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 451 AA; 52529 MW; 0C2471D9EA0B99BE CRC64; MARTTGDPAK RRRCMSRIKF WRRSRVGSEV VEKDTKRFKL SLIKAWLLRI RQEDYKYSGS FQEAIKPVLI IAQIFALMPV RKVSSKFAED LTFTWFSVRS YYALVTILFF GVSSGYMVAF VTSVSFNFDS VETLVFYLSI FLISLSFFQL ARKWPEIAQS WQLVEAKLPP LKLPKERRSL AQHINMITIV ATTCSLVEHI MSMLSMGYYV NSCPRWPDRP IDSFLYLSFS SVFYFVDYTR FLGIVGKVVN VLSTFAWNFN DIFVMAVSVA LAARFRQLND YMMREARLPT TVDYWMQCRI NFRNLCKLCE EVDDAISTIT LLCFSNNLYF ICGKILKSMQ AKPSIWHALY FWFSLVYLLG RTLILSLYSS SINDESKRPL VIFRLVPREY WCDELKRFSE EVQMDNVALT GMKFFRLTRG VVISVAGTIV TYELILLQFN GEEKVPGCFE N // ID G64F_DROME STANDARD; PRT; 449 AA. AC P83297; Q9VZJ5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 64f. GN GR64F OR CG32255/CG14988. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003480; AAF47826.2; -. DR FlyBase; FBgn0052255; Gr64f. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Multigene family. FT DOMAIN 1 97 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 98 118 1 (POTENTIAL). FT DOMAIN 119 126 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 127 147 2 (POTENTIAL). FT DOMAIN 148 179 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 180 200 3 (POTENTIAL). FT DOMAIN 201 245 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 246 266 4 (POTENTIAL). FT DOMAIN 267 310 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 311 331 5 (POTENTIAL). FT DOMAIN 332 333 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 334 354 6 (POTENTIAL). FT DOMAIN 355 415 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 416 436 7 (POTENTIAL). FT DOMAIN 437 449 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 449 AA; 52190 MW; 109D965C6E03BA44 CRC64; MKILPKLERK LRRLKKRVTR TSLFRKLDLV HERLDMVLDQ TELSRSDKEA FLSDGSFHQA VGRVLLVAEF FAMMPVKGVT GKHPSDLSFS WRNIRTCFSL LFIASSLANF GLSLFKVLNN PISFNSIKPI IFRGSVLLVL IVALNLARQW PQLMMYWHTV EKDLPQYKTQ LTKWKMGHTI SMVMLLGMML SFAEHILSMV SAINYASFCN RTADPIQNYF LRTNDEIFFV TSYSTTLALW GKFQNVFSTF IWNYMDLFVM IVSIGLASKF RQLNDDLRNF KGMNMAPSYW SERRIQYRNI CILCDKMDDA ISLITMVSFS NNLYFICVQL LRSLNTMPSV AHAVYFYFSL IFLIGRTLAV SLYSSSVHDE SRLTLRYLRC VPKESWCPEV KRFTEEVISD EVALTGMKFF HLTRKLVLSV AGTIVTYELV LIQFHEDNDL WDCDQSYYS // ID G66A_DROME STANDARD; PRT; 498 AA. AC Q9VSH2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 66a. GN GR66A OR CG7189. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: TASTE HAIRS IN LABIAL PALPS, LABRAL AND CC CIBARIAL SENSE ORGANS AND FORELEGS. CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY V. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003556; AAF50447.1; -. DR FlyBase; FBgn0035870; Gr66a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 49 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 50 70 1 (POTENTIAL). FT DOMAIN 71 83 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 84 104 2 (POTENTIAL). FT DOMAIN 105 147 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 148 168 3 (POTENTIAL). FT DOMAIN 169 177 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 178 198 4 (POTENTIAL). FT DOMAIN 199 316 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 317 337 5 (POTENTIAL). FT DOMAIN 338 353 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 354 374 6 (POTENTIAL). FT DOMAIN 375 431 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 432 452 7 (POTENTIAL). FT DOMAIN 453 498 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 139 139 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 414 414 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 498 AA; 56323 MW; D5DD7D4F667B3086 CRC64; MDNMAQAEDA VQPLLQQFQQ LFFISKIAGI LPQDLEKFRS RNLLEKSRNG MIYMLSTLIL YVVLYNILIY SFGEEDRSLK ASQSTLTFVI GLFLTYIGLI MMVSDQLTAL RNQGRIGELY ERIRLVDERL YKEGCVMDNS TIGRRIRIML IMTVIFELSI LVSTYVKLVD YSQWMSLLWI VSAIPTFINT LDKIWFAVSL YALKERFEAI NATLEELVDT HEKHKLWLRG NQEVPPPLDS SQPPQYDSNL EYLYKELGAI DAASRKPPPP PLATNMVHES ELGNAAKVEE KLNNLCQVHD EICEIGKALN ELWSYPILSL MAYGFLIFTA QLYFLYCATQ YQSIPSLFRS AKNPFITVIV LSYTSGKCVY LIYLSWKTSQ ASKRTGISLH KCGVVADDNL LYEIVNHLSL KLLNHSVDFS ACGFFTLDME TLYGVSGGIT SYLIILIQFN LAAQQAKEAI QTFNSLNDTA GLVGAATDMD NISSTLRDFV TTTMTPAV // ID G68A_DROME STANDARD; PRT; 389 AA. AC Q9VTN0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative gustatory receptor 68a. GN GR68A OR GR68D.1 OR CG7303. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21407712; PubMed=11516643; RA Dunipace L., Meister S., McNealy C., Amrein H.; RT "Spatially restricted expression of candidate taste receptors in the RT Drosophila gustatory system."; RL Curr. Biol. 11:822-835(2001). CC -!- FUNCTION: PROBABLE ROLE IN THE GUSTATORY RESPONSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-TR OF G-PROTEIN COUPLED CC RECEPTORS. SUBFAMILY I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003543; AAF50017.2; -. DR FlyBase; FBgn0041231; Gr68a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; NAS. DR GO; GO:0007607; P:taste; NAS. KW Hypothetical protein; Receptor; G-protein coupled receptor; KW Transmembrane; Glycoprotein; Multigene family. FT DOMAIN 1 42 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 43 63 1 (POTENTIAL). FT DOMAIN 64 82 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 83 103 2 (POTENTIAL). FT DOMAIN 104 133 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 134 154 3 (POTENTIAL). FT DOMAIN 155 164 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 165 185 4 (POTENTIAL). FT DOMAIN 186 236 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 237 257 5 (POTENTIAL). FT DOMAIN 258 281 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 282 302 6 (POTENTIAL). FT DOMAIN 303 352 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 353 373 7 (POTENTIAL). FT DOMAIN 374 389 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 133 133 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 311 311 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 389 AA; 43779 MW; 59A55E4895BDEC3B CRC64; MKIYQDIYPI SKPSQIFAIL PFYSGDVDDG FRFGGLGRWY GRLVALIILI GSLTLGEDVL FASKEYRLVA SAQGDTEEIN RTIETLLCII SYTMVVLSSV QNASRHFRTL HDIAKIDEYL LANGFRETYS CRNLTILVTS AAGGVLAVAF YYIHYRSGIG AKRQIILLLI YFLQLLYSTL LALYLRTLMM NLAQRIGFLN QKLDTFNLQD CGHMENWREL SNLIEVLCKF RYITENINCV AGVSLLFYFG FSFYTVTNQS YLAFATLTAG SLSSKTEVAD TIGLSCIWVL AETITMIVIC SACDGLASEV NGTAQILARI YGKSKQFQNL IDKFLTKSIK QDLQFTAYGF FSIDNSTLFK IFSAVTTYLV ILIQFKQLED SKVEDISQA // ID G6PD_DROME STANDARD; PRT; 524 AA. AC P12646; Q27574; Q27872; Q27879; Q27881; Q9VWE2; Q9VWE3; DT 01-OCT-1989 (Rel. 12, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (G6PD) DE (Zwischenferment). GN ZW OR G6PD OR CG12529. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88255872; PubMed=2838391; RA Fouts D., Ganguly R., Gutierrez A.G., Lucchesi J.C., Manning J.E.; RT "Nucleotide sequence of the Drosophila glucose-6-phosphate RT dehydrogenase gene and comparison with the homologous human gene."; RL Gene 63:261-275(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=F23.3, F24.1, MT41, MT68, Z3, Z5, Z11, Z16, Z21, Z27, Z41, Z42, RC Z55, Z62, Z64, and Z74; RX MEDLINE=97070821; PubMed=8913747; RA Eanes W.F., Kirchner M., Yoon J., Biermann C.H., Wang I.N., RA McCartney M.A., Verrelli B.C.; RT "Historical selection, amino acid polymorphism and lineage-specific RT divergence at the G6pd locus in Drosophila melanogaster and D. RT simulans."; RL Genetics 144:1027-1041(1996). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: D-GLUCOSE 6-PHOSPHATE + NADP(+) = D-GLUCONO- CC 1,5-LACTONE 6-PHOSPHATE + NADPH. CC -!- PATHWAY: PENTOSE PHOSPHATE PATHWAY; FIRST STEP. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P12646-1; Sequence=Displayed; CC Name=Short; CC IsoId=P12646-2; Sequence=VSP_001593; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE GLUCOSE-6-PHOSPHATE DEHYDROGENASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M26674; AAA51463.1; -. DR EMBL; M26673; AAA51463.1; JOINED. DR EMBL; U42738; AAB02801.1; -. DR EMBL; U42739; AAB02802.1; -. DR EMBL; U42740; AAB02803.1; -. DR EMBL; U42741; AAB02804.1; -. DR EMBL; U42742; AAB02805.1; -. DR EMBL; U42743; AAB02806.1; -. DR EMBL; U42744; AAB02807.1; -. DR EMBL; U42745; AAB02808.1; -. DR EMBL; U42746; AAB02809.1; -. DR EMBL; U42747; AAB02810.1; -. DR EMBL; U42748; AAB02811.1; -. DR EMBL; U42749; AAB02812.1; -. DR EMBL; U43165; AAA99071.1; -. DR EMBL; U43166; AAA99072.1; -. DR EMBL; U43167; AAA99073.1; -. DR EMBL; U44721; AAA99092.1; -. DR EMBL; U45985; AAA99107.1; -. DR EMBL; AE003512; AAF48999.1; -. DR EMBL; AE003512; AAF49000.1; -. DR EMBL; AY052079; AAK93503.1; -. DR PIR; A47740; A47740. DR PIR; JT0272; DEFFG6. DR HSSP; P11411; 1DPG. DR FlyBase; FBgn0004057; Zw. DR InterPro; IPR001282; G6PD. DR Pfam; PF00479; G6PD; 1. DR Pfam; PF02781; G6PD_C; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR ProDom; PD001129; G6PD; 1. DR TIGRFAMs; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. KW Oxidoreductase; NADP; Glucose metabolism; Polymorphism; KW Alternative splicing. FT ACT_SITE 209 209 BY SIMILARITY. FT VARSPLIC 1 7 Missing (in isoform Short). FT /FTId=VSP_001593. FT VARIANT 32 32 G -> C (IN STRAINS F24.1, MT32 AND MT68). FT VARIANT 80 80 T -> N (IN STRAIN Z74). FT VARIANT 382 382 L -> P (IN STRAINS F23.3, MT41, Z3, Z5, FT Z11, Z16, Z21, Z27, Z42, Z55, Z64, Z74 FT AND BERKELEY). FT CONFLICT 185 186 QA -> AG (IN REF. 1). FT CONFLICT 214 214 N -> K (IN REF. 1). FT CONFLICT 344 346 LGV -> ARS (IN REF. 1). FT CONFLICT 461 465 DELRE -> AAAQ (IN REF. 1). SQ SEQUENCE 524 AA; 60431 MW; ABF81B763A82F1FD CRC64; MATQKEDHTA LDLIIKSLKS PTMVCEGTHF DGKIPHTFVI FGASGDLAKK KIYPTLWWLY RDDLLPKPTK FCGYARSMLT VDSIKEQCLP YMKVQPHEQK KYEEFWALNE YVSGRYDGRT GFELLNQQLE IMENKNKANR IFYLALPPSV FEEVTVNIKQ ICMSVCGWNR VIIEKPFGRD DASSQALSDH LAGLFQEDQL YRIDHYLGKE MVQNLMTIRF GNKILSSTWN RENIASVLIT FKEPFGTQGR GGYFDEFGII RDVMQNHLLQ ILSLVAMEKP VSCHPDDIRD EKVKVLKSIE ALTLDDMVLG QYLGNPQGTN DDARTGYVED PTVSNDSNTP TYALGVLKIN NERWQGVPFI LRCGKALNER KAEVRIQYQD VLGDIFEGNT KRNELVIRVQ PGEALYFKMM TKSPGITFDI EETELDLTYE HRYKDSYLPD AYERLILDVF CGSQMHFVRS DELREAWRIF TPILHQIEKE HIRPITYQYG SRGPKEADRK CEENNFKYSG SYKWHGGKAA TSNH // ID G6PI_DROME STANDARD; PRT; 558 AA. AC P52029; Q27868; Q27870; Q9V4Z8; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glucose-6-phosphate isomerase (EC 5.3.1.9) (GPI) (Phosphoglucose DE isomerase) (PGI) (Phosphohexose isomerase) (PHI). GN PGI OR CG8251. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND VARIANTS TYR-184; ILE-329 AND ALA-471. RC STRAIN=AF-F, AF-S, F1-F, F1-1S, FL-2S, FR-F, FR-S, JA-F, JA-S, LW8, RC LW15, MW13, MW17, MW18, WA-F, WA-S, ZW20, ZW29, ZW34, ZW53, and ZW56; RA McDonald J.H., Kreitman M.E.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: D-GLUCOSE 6-PHOSPHATE = D-FRUCTOSE 6- CC PHOSPHATE. CC -!- PATHWAY: INVOLVED IN GLYCOLYSIS AND IN GLUCONEOGENESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GPI FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L27539; AAA28789.1; -. DR EMBL; L27540; AAA28790.1; -. DR EMBL; L27541; AAA28791.1; -. DR EMBL; L27542; AAA28792.1; -. DR EMBL; L27543; AAA28793.1; -. DR EMBL; L27544; AAA28794.1; -. DR EMBL; L27545; AAA28795.1; -. DR EMBL; L27546; AAA28796.1; -. DR EMBL; L27553; AAA28803.1; -. DR EMBL; L27554; AAA28804.1; -. DR EMBL; L27555; AAA28805.1; -. DR EMBL; U20566; AAA63671.1; -. DR EMBL; U20567; AAA63672.1; -. DR EMBL; U20568; AAA63673.1; -. DR EMBL; U20569; AAA63674.1; -. DR EMBL; U20570; AAA63675.1; -. DR EMBL; U20571; AAA63676.1; -. DR EMBL; U20572; AAA63677.1; -. DR EMBL; U20573; AAA63678.1; -. DR EMBL; U20574; AAA63679.1; -. DR EMBL; U20575; AAA63680.1; -. DR EMBL; AE003835; AAM71090.1; -. DR EMBL; AY051468; AAK92892.1; -. DR HSSP; Q9N1E2; 1HOX. DR FlyBase; FBgn0003074; Pgi. DR InterPro; IPR001672; G6P_Isomerase. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. KW Isomerase; Gluconeogenesis; Glycolysis; Polymorphism. FT ACT_SITE 393 393 BY SIMILARITY. FT ACT_SITE 523 523 BY SIMILARITY. FT VARIANT 184 184 H -> Y (IN STRAIN LW15). FT VARIANT 329 329 V -> I (IN STRAINS AF-F, F1-F, F1-1S, JA- FT F, LW8, MW18 AND ZW20). FT VARIANT 471 471 V -> A (IN STRAIN JA-S). SQ SEQUENCE 558 AA; 62339 MW; 8DD54FCFCCBD1488 CRC64; MAGPLPPLNQ EAAFQKLQEY YDSKGKDLNI KDLFVKDSKR FSKYSLRLHT QNDGEILLDY SKNRINDEVW DLLLTLAKVR RVNAARDAMF SGQHINITEN RAVLHTALRN RGTDPVLVDD KDVMPDVRAE LAHMKEFTNM VISGVWRGCT GKQITDVVNI GIGGSDLGPL MVTEALKPYG KGLHSHFVSN IDGTHLAEVL KKVNYETTLF IVASKTFTTQ ETITNATSAK TWLLEHSKEP ESVAKHFVAL STNKEKVTEF GIDSTNMFGF WDWVGGRYSL WSAIGLSICL SIGFENFEQL LDGAHFMDNH FKTTPFEKNA PVILALLGVW YSNFFKAETH ALLPYDQYLH RFAAYFQQGD MESNGKFVSK SGKPVKYSTG PIVWGEPGTN GQHAFYQLIH QGTRLIPCDF IAPAQTHNPI AGGKHHKILL SNFLAQTEAL MAGKTVDEAR TELSKAGLCG NELDNLLPHK VFVGNRPTNS IVVKKVSPFT LGALIALYEH KIFVQGIIWD INSFDQWGVE LGKQLAKAIE PELDHCNEVS THDSSTNGLI NFIKANWK // ID GAB3_DROME STANDARD; PRT; 496 AA. AC Q08832; Q9VXL8; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Gamma-aminobutyric-acid receptor beta-like subunit precursor (GABA(A) DE receptor). GN LCCH3 OR CG17336. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93290631; PubMed=7685594; RA Henderson J.E., Soderlund D.M., Knipple D.C.; RT "Characterization of a putative gamma-aminobutyric acid (GABA) RT receptor beta subunit gene from Drosophila melanogaster."; RL Biochem. Biophys. Res. Commun. 193:474-482(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: GABA, AN INHIBITORY NEUROTRANSMITTER, MEDIATES NEURONAL CC INHIBITION BY BINDING TO THE GABA RECEPTOR AND OPENING AN INTEGRAL CC CHLORIDE CHANNEL (BY SIMILARITY). CC -!- SUBUNIT: GENERALLY PENTAMERIC. THERE ARE FIVE TYPES OF GABA(A) CC RECEPTOR CHAINS: ALPHA, BETA, GAMMA, DELTA, AND RHO. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNEL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L17436; AAA28559.1; -. DR EMBL; S62717; AAB27090.1; -. DR EMBL; AE003500; AAF48540.1; -. DR EMBL; AY060660; AAL28208.1; -. DR PIR; JN0603; JN0603. DR FlyBase; FBgn0010240; Lcch3. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0004890; F:GABA-A receptor activity; IDA. DR InterPro; IPR006029; Neu_channel_memb. DR InterPro; IPR006202; Neur_chan_LBD. DR InterPro; IPR006201; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Chloride channel. FT SIGNAL 1 20 OR 27 (POTENTIAL). FT CHAIN 21 496 GAMMA-AMINOBUTYRIC-ACID RECEPTOR BETA- FT LIKE SUBUNIT. FT DOMAIN 21 258 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 259 280 POTENTIAL. FT TRANSMEM 285 306 POTENTIAL. FT TRANSMEM 318 342 POTENTIAL. FT DOMAIN 343 472 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 473 494 POTENTIAL. FT CARBOHYD 39 39 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 189 189 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 176 190 BY SIMILARITY. FT CONFLICT 12 12 G -> S (IN REF. 1). SQ SEQUENCE 496 AA; 56597 MW; 62C9A9E97E8DF681 CRC64; MTCFTRVGVS CGLFFFLLGA QLQLIRCIRK DVLAGRLENV TQTISNILQG YDIRLRPNFG GEPLHVGMDL TIASFDAISE VNMDYTITMY LNQYWRDERL AFNIFGQYFD DENDDGISDV LTLSGDFAEK IWVPDTFFAN DKNSFLHDVT ERNKLVRLGG DGAVTYGMRF TTTLACMMDL HYYPLDSQNC TVEIESYGYT VSDVVMYWKP TPVRGVEDAE LPQFTIIGYE TNDRKERLAT GVYQRLSLSF KLQRNIGYFV FQTYLPSILI VMLSWVSFWI NHEATSARVA LGITTVLTMT TISTGVRSSL PRISYVKAID IYLVMCFVFV FAALLEYAAV NYTYWGKRAK KKIKKVKECC PGKIGKSERS ETCSTTEDII ELQDVRMSPI PSLRRGTYNA TLDSIGTETM NLGKFPPSFR ITRNYGTGHS QLRRRAQRGI STRPRMLHAL KRGASAIKAT IPKIKDVNII DKYSRMIFPI SFLAFNLGYW LFYILE // ID GAB_DROME STANDARD; PRT; 606 AA. AC P25123; Q24561; Q26302; Q9VSV0; DT 01-MAY-1992 (Rel. 22, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Gamma-aminobutyric-acid receptor beta subunit precursor (GABA(A) DE receptor) (Cyclodiene resistance protein). GN RDL OR CG10537. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91334435; PubMed=1651498; RA Ffrench-Constant R.H., Mortlock D.P., Shaffer C.D., RA Macintyre R.J., Roush R.T.; RT "Molecular cloning and transformation of cyclodiene resistance in RT Drosophila: an invertebrate gamma-aminobutyric acid subtype A RT receptor locus."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7209-7213(1991). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=94286578; PubMed=8016117; RA Chen R., Belelli D., Reyes A., Lambert J.J., Peters J.A., Lan N.C.; RT "Cloning and functional expression of a Drosophila gamma-aminobutyric RT acid receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6069-6073(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 70-113 FROM N.A. RX MEDLINE=93260477; PubMed=7684073; RA Ffrench-Constant R.H., Rocheleau T.A.; RT "Drosophila gamma-aminobutyric acid receptor gene Rdl shows extensive RT alternative splicing."; RL J. Neurochem. 60:2323-2326(1993). RN [5] RP RNA EDITING. RX MEDLINE=22789647; PubMed=12907802; RA Hoopengardner B., Bhalla T., Staber C., Reenan R.; RT "Nervous system targets of RNA editing identified by comparative RT genomics."; RL Science 301:832-836(2003). CC -!- FUNCTION: GABA, AN INHIBITORY NEUROTRANSMITTER, MEDIATES NEURONAL CC INHIBITION BY BINDING TO THE GABA RECEPTOR AND OPENING AN INTEGRAL CC CHLORIDE CHANNEL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- MISCELLANEOUS: RESISTANCE IS THOUGHT TO BE DUE TO INSENSITIVITY OF CC THE CYCLODIENE/PICROTOXININ BINDING SITE ON THE GABA(A) RECEPTOR- CC CHLORIDE IONOPHORE COMPLEX. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNEL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M69057; AAA28556.1; -. DR EMBL; U02042; AAA19249.1; -. DR EMBL; AE003553; AAF50311.1; -. DR EMBL; S61113; AAB26669.1; -. DR FlyBase; FBgn0004244; Rdl. DR InterPro; IPR006029; Neu_channel_memb. DR InterPro; IPR006202; Neur_chan_LBD. DR InterPro; IPR006201; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; RNA editing; Chloride channel. FT SIGNAL 1 44 POTENTIAL. FT CHAIN 45 606 GAMMA-AMINOBUTYRIC-ACID RECEPTOR BETA FT SUBUNIT. FT DOMAIN 45 268 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 269 291 POTENTIAL. FT TRANSMEM 297 316 POTENTIAL. FT TRANSMEM 333 356 POTENTIAL. FT DOMAIN 357 568 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 569 590 POTENTIAL. FT CARBOHYD 58 58 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 253 253 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 185 199 BY SIMILARITY. FT DOMAIN 499 535 GLY-RICH. FT VARIANT 122 122 R -> G (partial, due to RNA editing). FT VARIANT 283 283 I -> V (partial, due to RNA editing). FT VARIANT 294 294 N -> D (partial, due to RNA editing). FT VARIANT 360 360 M -> V (partial, due to RNA editing). FT CONFLICT 38 38 H -> N (IN REF. 2). FT CONFLICT 68 68 V -> I (IN REF. 2). FT CONFLICT 97 97 L -> V (IN REF. 1). FT CONFLICT 101 101 K -> L (IN REF. 1). FT CONFLICT 216 222 KWNEGPN -> FWRDGLS (IN REF. 1). FT CONFLICT 226 226 V -> M (IN REF. 1). FT CONFLICT 231 231 S -> E (IN REF. 1). FT CONFLICT 236 236 K -> R (IN REF. 1). FT CONFLICT 245 245 M -> T (IN REF. 1). FT CONFLICT 248 248 S -> N (IN REF. 1). FT CONFLICT 428 428 G -> R (IN REF. 2). SQ SEQUENCE 606 AA; 65656 MW; 25BDDCB03DAD54F8 CRC64; MSDSKMDKLA RMAPLPRTPL LTIWLAINMA LIAQETGHKR IHTVQAATGG GSMLGDVNIS AILDSFSVSY DKRVRPNYGG PPVEVGVTMY VLSISSLSEV KMDFTLDFYF RQFWTDPRLA YRKRPGVETL SVGSEFIKNI WVPDTFFVNE KQSYFHIATT SNEFIRVHHS GSITRSIRLT ITASCPMNLQ YFPMDRQLCH IEIESFGYTM RDIRYKWNEG PNSVGVSSEV SLPQFKVLGH RQRAMEISLT TGNYSRLACE IQFVRSMGYY LIQIYIPSGL IVIISWVSFW LNRNATPARV ALGVTTVLTM TTLMSSTNAA LPKISYVKSI DVYLGTCFVM VFASLLEYAT VGYMAKRIQM RKQRFMAIQK IAEQKKQQLD GANQQQANPN PNANVGGPGG VGVGPGGPGG PGGGVNVGVG MGMGPEHGHG HGHHAHSHGH PHAPKQTVSN RPIGFSNIQQ NVGTRGCSIV GPLFQEVRFK VHDPKAHSKG GTLENTVNGG RGGPQSHGPG PGQGGGPPGG GGGGGGGGGP PEGGGDPEAA VPAHLLHPGK VKKDINKLLG ITPSDIDKYS RIVFPVCFVC FNLMYWIIYL HVSDVVADDL VLLGEE // ID GAG2_DROME STANDARD; PRT; 414 AA. AC P20828; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Retrovirus-related Gag polyprotein from transposon 297. GN GAG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86108354; PubMed=2417839; RA Inouye S., Yuki S., Saigo K.; RT "Complete nucleotide sequence and genome organization of a Drosophila RT transposable genetic element, 297."; RL Eur. J. Biochem. 154:417-425(1986). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03431; CAA27159.1; -. DR PIR; A24872; A24872. DR FlyBase; FBgn0044338; 297\gag. KW Core protein; Polyprotein; Transposable element. SQ SEQUENCE 414 AA; 49250 MW; 7393C9CEEB864148 CRC64; MSQPIIALSD INLAEARRQL KDIMPFKGDP ETLHTFISRV DYVISLYQTN DVRQQRILLG AIERNLDGQI TRSLGLPNVE DWPTLKARLI AEFKIQTPNY KLLENFRETP YRGSLRAFCE EAERRRQLLI SKLHLEGNQS DFLIYIQGIK ESIKILIRKL PIQLFTILAH HDITDLRSLI TIAQNEGIYE EHINFEFYEK PEYRNKNSNS NQNSKTQKFN TNVQTQNRPS YSQYSQPFQP NFNQYIQPFR PSYTQQITNN PPMWHAPNYF RPNQYINPQP IIQKNHFQQY PNKAQFPQTT HFRGNTYPRL QQPSTYKNTN FPITKRLRPS DSEQTKMSID EIRFQDAHEF EQVQPNYYEQ QYFNQNQYNP YQNHSFINEG QQQVQFVQIN NKQNQNNSEL NENFRLTVPE NTNT // ID GAGA_DROME STANDARD; PRT; 519 AA. AC Q08605; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor GAGA (Trithorax-like protein). GN TRL OR TFGAGA OR GAGA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 393-405 AND 498-518. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94067157; PubMed=7504178; RA Soeller W.C., Oh C.E., Kornberg T.B.; RT "Isolation of cDNAs encoding the Drosophila GAGA transcription RT factor."; RL Mol. Cell. Biol. 13:7961-7970(1993). RN [2] RP STRUCTURE BY NMR OF 319-372. RX MEDLINE=97185912; PubMed=9033593; RA Omichinski J.G., Pedone P.V., Felsenfeld G., Gronenborn A.M., RA Clore G.M.; RT "The solution structure of a specific GAGA factor-DNA complex reveals RT a modular binding mode."; RL Nat. Struct. Biol. 4:122-132(1997). CC -!- FUNCTION: PUTATIVE TRANSCRIPTIONAL ACTIVATOR THAT BINDS TO THE CC PROXIMAL REGION OF THE ENGRAILED PROMOTER. MAY ACTIVATE AS WELL CC KRUEPPEL, EVE, FTZ AND UBX. THE 5'-GAGAG-3' PENTAMER MAY FORM A CC CORE RECOGNITION SEQUENCE WERE GAGA BINDS ACTING AS AN CC ANTIREPRESSOR. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED DURING EMBRYOGENESIS WITH HIGHER CC LEVELS FOUND FROM 9-12 HOURS AFTER EGG LAYING. LOW LEVELS ARE CC FOUND IN LARVAE AND IN ADULTS. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L22205; AAA16072.1; -. DR PIR; A54590; A54590. DR PDB; 1YUI; 31-DEC-97. DR PDB; 1YUJ; 31-DEC-97. DR TRANSFAC; T00301; -. DR FlyBase; FBgn0013263; Trl. DR GO; GO:0005721; C:centric heterochromatin; IDA. DR GO; GO:0005717; C:chromatin; NAS. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003704; F:specific RNA polymerase II transcription fa...; IMP. DR GO; GO:0006325; P:establishment and/or maintenance of chromat...; NAS. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. KW Transcription regulation; Activator; DNA-binding; Nuclear protein; KW Zinc-finger; Metal-binding; 3D-structure. FT DOMAIN 34 99 BTB. FT DOMAIN 446 459 GLN-RICH. FT DOMAIN 485 498 GLN-RICH. FT DOMAIN 512 519 GLN-RICH. FT ZN_FING 343 366 C2H2-TYPE. FT HELIX 334 337 FT TURN 338 338 FT STRAND 343 344 FT TURN 346 348 FT STRAND 351 352 FT HELIX 355 365 FT TURN 366 368 SQ SEQUENCE 519 AA; 54829 MW; B6EA2F36BFD6DD0E CRC64; MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQ TVTKDDYTTH SIQLQHMIPQ HHDQDQLIAT IATAPQQTVH AQVVEDIHHQ GQILQATTQT NAAGQQQTIV TTDAAKHDQA VIQAFLPARK RKPRVKKMSP TAPKISKVEG MDTIMGTPTS SHGSGSVQQV LGENGAEGQL LSSTPIIKSE GQKVETILTM DPNNMIPVTS ANAATGEITP AQGATGSSGG NTSGVLSTPK AKRAKHPPGT EKPRSRSQSE QPATCPICYA VIRQSRNLRR HLELRHFAKP GVKKEKKSKS GNDTTLDSSM EMNTTAEGDN TVGSDGAGGA GSAGGQSSGT TPTRVISNAP QAAGAPAILA QGVLPQQQQQ QQLQQQHQQH LTATLAGGGQ AYIKHEGGGG GGTGQQQQQQ AAQQQGMQNV IHIVGDQVFI PQQQQPQPQ // ID GAGJ_DROME STANDARD; PRT; 568 AA. AC P21330; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Nucleic-acid-binding protein (Mobile element jockey) (ORF1). GN GAG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89108009; PubMed=2463954; RA Priimaegi A.F., Mizrokhi L.J., Ilyin Y.V.; RT "The Drosophila mobile element jockey belongs to LINEs and contains RT coding sequences homologous to some retroviral proteins."; RL Gene 70:253-262(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87303653; PubMed=3040362; RA Mizrokhi L.J., Priimaegi A.F., Ilyin Y.V.; RT "Drosophila mobile element jockey is a retroposon and encodes the RT GAG-specific protein sequence characteristic for retroviruses."; RL Dokl. Akad. Nauk SSSR 294:1235-1239(1987). CC -!- FUNCTION: STRONGLY BASIC PROTEIN THAT BINDS DIRECTLY TO CC RETROVIRAL RNA AND MAY BE INVOLVED IN ITS PACKAGING AND CC IN THE REVERSE TRANSCRIPTION PROCESS. CC -!- SIMILARITY: STRONG TO THE EQUIVALENT PROTEIN OF DROSOPHILA CC FUNEBRIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22874; AAA28674.1; ALT_INIT. DR EMBL; M38643; AAA28939.1; ALT_INIT. DR PIR; JT0395; JT0395. DR FlyBase; FBgn0020297; jockey\gag. DR InterPro; IPR006579; Pre_C2HC. DR InterPro; IPR001878; Znf_CCHC. DR SMART; SM00596; PRE_C2HC; 1. DR SMART; SM00343; ZnF_C2HC; 1. KW Transposable element; Zinc-finger. FT DOMAIN 390 444 THREE ZINC-FINGER-LIKE REGIONS. FT ZN_FING 390 403 POTENTIAL. FT ZN_FING 403 423 POTENTIAL. FT ZN_FING 430 444 POTENTIAL. SQ SEQUENCE 568 AA; 62878 MW; DE0E4834A24C759A CRC64; MENSFAQSRP SNGCDKFEKM RKVAGVEPGE LRSQLRASCA VVSPNLEGMP TQSAVSSLMV TISSNTNASV TCTISNVQAN MICTPTYTDC TTVTTSICPT TPYDNGLPTP LSSLPNKPSK ANCPFQAHDR TVNRKRKGVS QPPLPILTPS PSRKTKRQAT MPLNEEASTS TAAALNNNRF ALLSAEAENM EQDVSDADSD IEDSAARDGG GQSAKYSKPP AICVPSVSDP VTLERALNLS TGSSNYYIRI SRFGVSRIYT ANPDAFRTAV KELNKLNCQF WHHQLKEEKP YRVVLKGIHA NVPSSQIEQA FSDHGYEVLN IYCPRKSDWK NIQVNEDDNE ATKNFKTRQN LFYINLKQGP NVKESLKITR LGRYRVTVER ATRRKELLQC QRCQIFGHSK NYCAQDPICG KCSGPHMTGF ALCISDVCLC INCGGDHVST DKSCPVRAEK AKKLKPRSRL PMTNNIATLK PPQRSSSGYI PAEALRTNIS YADIARRNTT QSRARATVQA EVIPTSDNSL NNKFMTLDNS IRAINTRMDE LFKLIHETVE ANKAFRELVQ VLITRIPK // ID GAGO_DROME STANDARD; PRT; 417 AA. AC Q8I7Q0; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Retrovirus-related Gag polyprotein from transposon opus. GN GAG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426070; PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J.W., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster RT euchromatin: a genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY180918; AAN87270.1; -. DR FlyBase; FBgn0025876; opus\gag. KW Core protein; Polyprotein; Transposable element. SQ SEQUENCE 417 AA; 47195 MW; EF2F39E4EAD0C818 CRC64; MEETLRALSE SLNALTNVVT GIKEDIKKNN DRLAILEQER GNADPTVDQP QPLVRARTEY ELREISVLPD CVKELQAFEG RQEAYLSWIN RAQSILTEYD LIKTRPLYRA IVLHIRQKIR GHADMALAAY GVQDDDWDDI KRVLALHYAD KRDLRTLEHE LGAMCQGSRP LDRFYMDVNG HLSLILNNLK ARNHPREVVN ALIETYRDKA LDVFIRGVGR DCSKHLLVRS PKNLPEAYSF CMGLQNVMSR NFTAQNYQPS GAPRFAGPYQ HQARPPFRTP FSPGSGRFSQ NSYRTQGPRQ AIKMESNRSG QSYQSGYSGR QEEGSGIKRM SEGNNPFQKA QRLYHMELAP PPLAPAASGD NQGRSHEGYY DDESQAVERS NNYPPQKNVE GVTDAPHNLE TEGGANFMTN ASPVYRT // ID GAGY_DROME STANDARD; PRT; 451 AA. AC P10405; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Retrovirus-related GAG polyprotein (Transposon gypsy). GN GAG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87064379; PubMed=3023871; RA Marlor R.L., Parkhurst S.M., Corces V.G.; RT "The Drosophila melanogaster gypsy transposable element encodes RT putative gene products homologous to retroviral proteins."; RL Mol. Cell. Biol. 6:1129-1134(1986). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12927; AAA70218.1; -. DR EMBL; AF033821; AAC82603.1; -. DR PIR; A25666; FOFFGY. DR FlyBase; FBgn0014965; gypsy\gag. KW Core protein; Polyprotein; Transposable element. SQ SEQUENCE 451 AA; 50675 MW; FEBEDED61460DF2B CRC64; MSWAHNYRKV KVEYESEDSW EEEQVGQALG RPLDSATVDI TMDPNQIQAL IDNAVRQALS QQQSQFQTQL NSLAARVQSL QVEAPQIKIY EKVSVNPDVR CDIPLDIIKS VPEFSGTQDE YVAWRQSAIY AYELFKPYNG SSAHYQAVAI LRNKIRGAAG ALLVSHNTVL NFDAILARLD CTYSDKTSLR LLRQGLEMVR QGDLPLMQYY DEVEKKLTLV TNKIVMTHEQ EGADLLNAEV RADALHAFIS GLKKALRAVV FPAQPKDLPS ALALAREAEA SIERSMFANS YAKAVEERAH SGANGKSRFQ GKPNKEEQGQ DRNPHFTKRP KNNGQTNKDT QAQAPQPMEV DSSSRFRQRT EHYQNHPNES NAFKRRNSSE RSTGPRRQRL NNVVQEAPKQ KDPKEEYEKT AKAAVEEIDS ENEYAPSDDS LNFLGGAPGC RSLNDGWLGE P // ID GAP1_DROME STANDARD; PRT; 1165 AA. AC P48423; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE GTPase-activating protein (Ras GTPase-activating protein). GN GAP1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92191280; PubMed=1547500; RA Gaul U., Mardon G., Rubin G.M.; RT "A putative Ras GTPase activating protein acts as a negative RT regulator of signaling by the Sevenless receptor tyrosine kinase."; RL Cell 68:1007-1019(1992). CC -!- FUNCTION: INHIBITORY REGULATOR OF THE RAS-CYCLIC AMP PATHWAY. MAY CC FUNCTION AS A NEGATIVE REGULATOR OF RAS1 IN THE SEV SIGNALING CC PATHWAY. CC -!- SIMILARITY: CONTAINS 2 C2 DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RAS-GAP DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86655; AAA28595.1; -. DR PIR; A42142; S27809. DR HSSP; Q06187; 1BWN. DR FlyBase; FBgn0004390; Gap1. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0005099; F:Ras GTPase activator activity; IMP. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR GO; GO:0007067; P:mitosis; IMP. DR GO; GO:0046580; P:negative regulation of RAS protein signal t...; NAS. DR GO; GO:0007265; P:RAS protein signal transduction; IMP. DR GO; GO:0007062; P:sister chromatid cohesion; IMP. DR InterPro; IPR001562; BTK. DR InterPro; IPR000008; C2. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR001849; PH. DR InterPro; IPR001936; RasGAP. DR InterPro; IPR008936; Rho_GAP. DR Pfam; PF00779; BTK; 1. DR Pfam; PF00168; C2; 2. DR Pfam; PF00169; PH; 1. DR Pfam; PF00616; RasGAP; 1. DR SMART; SM00107; BTK; 1. DR SMART; SM00239; C2; 2. DR SMART; SM00233; PH; 1. DR SMART; SM00323; RasGAP; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS00499; C2_DOMAIN_1; FALSE_NEG. DR PROSITE; PS50004; C2_DOMAIN_2; 2. DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1. DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1. KW GTPase activation; Repeat. FT DOMAIN 30 132 C2 DOMAIN 1. FT DOMAIN 281 401 C2 DOMAIN 2. FT DOMAIN 504 698 RAS-GAP. FT DOMAIN 762 862 PH. FT DOMAIN 221 226 POLY-ALA. FT DOMAIN 227 230 POLY-SER. FT DOMAIN 750 754 POLY-ALA. FT DOMAIN 1034 1052 POLY-GLN. FT DOMAIN 1096 1100 POLY-GLN. FT DOMAIN 1103 1113 POLY-GLN. FT DOMAIN 1124 1131 POLY-ASN. FT DOMAIN 1136 1142 POLY-SER. SQ SEQUENCE 1165 AA; 132259 MW; 58904F5EBF2435DB CRC64; MLLNKKRYMF DERDDNNINS PVAVEPSSNN NKMADTREVR IEEQLKVKIG EAKNLSSRNA ANTSCSTQGT RDVYCTIALD QEEICRTPTI ERTLTPFFGE EHQFKIPRRF RYLTIYLWDR DMKQDKPIGK IAIKREELHM YNHKDHWFSL RPVDQDSEVQ GMVNVEVAFT EAQQTQSLSE GIDLGQHTLR HHQNLPHHSH QQRAHLNDYK ENSELSNIQR ASAAAASSSS AAMTLKTRAA GLFGHVHHPP SQTQHFPIIN TTSTSSDQLS NWKSHGRFVG VTIKVPACVD LAKKQGTCDP FVVCTAHYSN KHQVTRRTKQ RKKTVDPEFD EAMYFDLHID ADAGSTNTTG SNKSAGSLES SANKGYSIYP VGGADLVEIV VSVWHDAHGA MSDKVFLGEV RLPMLNKQEQ QAVNPSAWYY LQPRSMTHSS RSLNATPRSC ATPPGTRLSV DSTIGSLRLN LNYTADHVFP LATYDDLMNL LLESVDQRPI TVSAVSILGE LVSGKTEVAQ PLVRLFTHTE RIAPIIKALA DHEISHLTDP TTIFRGNTLV SKMMDEAMRL SGLHYLHQTL RPVLSQIVAE KKPCEIDPSK IKDRSAVDTN LHNLQDYVER VFEAITKSAD RCPKVLCQIF HDLRECAGEH FPSNREVRYS VVSGFIFLRF FAPAILGPKL FDLTTERLDA QTSRTLTLIS KTIQSLGNLV SSRSSQQTCK EEFTVELYKK FCTEQHVDAV KHFLEVISTP SHASSSVHPA AAAATPLEPV LLKEGEGLMT KYPTSRKRFG RQFKQRHFRL TTHSLSYAKS KGKQPICDIP LQEIASVEQL KDKSFKMQNC FKIVHNDRSL IVQTTNCVEE REWFDLLHKI CLMNSIRMQY FHPSAFVSGF YSCCGRSDEN SPGCKKVLDK TMDYFQMDLV TALDPALDLQ RIHTLIMSNM SVLESLLDPL TYHQSLSQTQ HQQHNPLVPL ATDLQKHSPQ AFAEFKRTIE KLREKAYAID RDHRDYKQGI TRQLKYGSRQ APIGDDNYWH MMRAAGQLNQ QHHQQQQHQQ QQQQQQQQQL QQFQPQPVLP QMQNVRAYPY QPATSNMNAY CLHNMQYQQQ RLPFHQQQQQ HHQQLQQQQS QFQPLRSHQL QRHNNNLNNN NCGNGSSSSP SSTTSSVVAA PPSTTSSSQP APPIY // ID GAS8_DROME STANDARD; PRT; 479 AA. AC Q8MT08; Q8T9R5; Q9W4R6; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Growth-arrest-specific protein 8 homolog. GN GAS8 OR CG14271. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21839108; PubMed=11751847; RA Yeh S.-D., Chen Y.-J., Chang A.C.Y., Ray R., She B.-R., Lee W.-S., RA Chiang H.-S., Cohen S.N., Lin-Chao S.; RT "Isolation and properties of Gas8, a growth arrest-specific gene RT regulated during male gametogenesis to produce a protein associated RT with the sperm motility apparatus."; RL J. Biol. Chem. 277:6311-6317(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLE CYTOSKELETAL LINKER WHICH MAY BE INVOLVED IN CC THE SPERMATOZOA FLAGELLUM CELL MOTILITY (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE GAS8 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF468957; AAL79828.1; ALT_INIT. DR EMBL; AE003427; AAF45877.3; -. DR EMBL; AY118453; AAM49822.1; -. DR FlyBase; FBgn0029667; Gas8. DR GO; GO:0005737; C:cytoplasm; NAS. DR GO; GO:0030317; P:sperm motility; ISS. KW Cytoskeleton; Microtubule; Flagellum; Coiled coil. FT DOMAIN 28 93 COILED COIL (POTENTIAL). FT DOMAIN 117 170 COILED COIL (POTENTIAL). FT DOMAIN 210 347 COILED COIL (POTENTIAL). SQ SEQUENCE 479 AA; 57168 MW; 4C4EC1E487A0AFEE CRC64; MPPKGKKGKK GKKLPVLIDG VDTSAMTRDQ LEAFALRLKA EMDREREERN YFQLERDKIR TFWEITRQQL DETRYELQQK DKEIEATQDL ADIDTKHVMQ QMKHLQFENH NRLGEVRAEA MTQLKLAQEH HVLQENELQR DKRQLRRMLR ERMEMSEMQL RQMEAHFNEK LLEQRITFER ERKDNEMLHE EKMIEQKAKL DLFYGTQMFE VEERKNQQIK DLQDHHDLAF NDMKNYYNDI TLNNLALIGS MKEQLEHLRK QAERSDRIAA DTAAENRRLK EPLEHANIQL NEYRRKLEFY ERDKQQLSRL KTRNTRLEKK VKGLTWEAET LILRNDSLVA EREGLKERFN DVIVELQQKT GLKNVLLERK IAALMREDEK RSIVLHETIA TCAPNFAEKL TSLDERVGNI IDEKNKIILD LRYEVTKARK AHDDLLETYE CKLKQYGVPT DELGFKPIRN RDQQQLYVCG PAGIITENK // ID GATC_DROME STANDARD; PRT; 486 AA. AC P91623; Q9VHV4; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GATA-binding factor-C (Transcription factor GATA-C) (dGATA-C) (Grain DE protein). GN GRN OR GATA-C OR CG9656. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96027621; PubMed=7559649; RA Lin W.H., Huang L.H., Yeh J.Y., Hoheisel J., Lehrach H., Sun Y.H., RA Tsai S.F.; RT "Expression of a Drosophila GATA transcription factor in multiple RT tissues in the developing embryos. Identification of homozygous RT lethal mutants with P-element insertion at the promoter region."; RL J. Biol. Chem. 270:25150-25158(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTION FACTOR THAT IS VITAL TO THE DEVELOPMENT OF CC MULTIPLE ORGAN SYSTEMS. BINDS TO THE CORE CONSENSUS SEQUENCE 5'- CC WGATAR-3'. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 2 GATA-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D50542; BAA09102.1; -. DR EMBL; AE003677; AAF54195.1; -. DR PIR; A57601; A57601. DR HSSP; P17679; 1GNF. DR FlyBase; FBgn0001138; grn. DR GO; GO:0009888; P:histogenesis; IMP. DR InterPro; IPR000679; Znf_GATA. DR Pfam; PF00320; GATA; 2. DR PRINTS; PR00619; GATAZNFINGER. DR SMART; SM00401; ZnF_GATA; 2. DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2. DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2. KW Transcription regulation; DNA-binding; Zinc-finger; Nuclear protein. FT ZN_FING 261 285 GATA-TYPE 1. FT ZN_FING 321 345 GATA-TYPE 2. FT DOMAIN 21 24 POLY-GLY. FT DOMAIN 73 79 POLY-GLY. FT DOMAIN 326 330 POLY-THR. FT DOMAIN 375 380 POLY-LYS. SQ SEQUENCE 486 AA; 50634 MW; 0A5E6EBD070C7E38 CRC64; MDMTSTAEAA ARSWYDSPRL GGGGSSGGGN GGGVSPQTNG LGSAGSSLAH SHHSLSSGAS SAGSSVGVGS ALGGGGGSGL DTSDMSAFYA LESNGHHRRY YPSYHQHTSR MPSTHASPQV CRPHFHTPLS PWLTSEHKSF APASAWSMGQ FACPQEPQVE HKLGQMGQSH QTTAAGQHSF PFPPTPPKDS TPDSVQTGPS EYQAVMNAFM HQQATGSTSL TDASCALDIK PSIQNGSASG SSGSGTTHTS TPKQREEGRE CVNCGATSTP LWRRDGTGHY LCNACGLYYK MNGQNRPLIK PKRRLTLQSL QSAAKRAGTS CANCKTTTTT LWRRNASGEP VCNACGLYYK LHNVNRPLTM KKEGIQTRNR KLSSKSKKKK GLGGGCLPIG GHLGMGDFKP LDPSKGFGGG FSASMAQHGH LSSGLHPAHA HMHGSWYTGG MGALGASSGL QGGFSTAGSL SGAVVPHSQP YHLGLSSMGT WRTDYT // ID GB01_DROME STANDARD; PRT; 354 AA. AC P16378; P16377; P16707; Q9V5L5; Q9V5L6; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein G(O), alpha subunit 47A. GN G-O-ALPHA-47A OR G-OA47A OR CG2204. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING. RX MEDLINE=90036957; PubMed=2509464; RA Thambi N.C., Quan F., Wolfgang W.J., Spiegel A., Forte M.; RT "Immunological and molecular characterization of Go alpha-like RT proteins in the Drosophila central nervous system."; RL J. Biol. Chem. 264:18552-18560(1989). RN [2] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING. RC TISSUE=Head; RX MEDLINE=90036955; PubMed=2509462; RA Yoon J., Shortridge R.D., Bloomquist B.T., Schneuwly S., Perdew M.H., RA Pak W.L.; RT "Molecular characterization of Drosophila gene encoding G0 alpha RT subunit homolog."; RL J. Biol. Chem. 264:18536-18543(1989). RN [3] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP ALTERNATIVE SPLICING. RX MEDLINE=90036956; PubMed=2509463; RA de Sousa S.M., Hoveland L.L., Yarfitz S., Hurley J.B.; RT "The Drosophila Go alpha-like G protein gene produces multiple RT transcripts and is expressed in the nervous system and in ovaries."; RL J. Biol. Chem. 264:18544-18551(1989). RN [4] RP SEQUENCE FROM N.A. (ISOFORM G-OA47A-2), AND TISSUE SPECIFICITY. RX MEDLINE=92096479; PubMed=2519611; RA Schmidt C.J., Garen-Fazio S., Chow Y.K., Neer E.J.; RT "Neuronal expression of a newly identified Drosophila melanogaster G RT protein alpha 0 subunit."; RL Cell Regul. 1:125-134(1989). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS G-OA47A-1 AND G-OA4A-2). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. CC -!- FUNCTION: THE G(O) PROTEIN FUNCTION IS NOT CLEAR. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA AND CC GAMMA). THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING CC SITE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=G-OA47A-1; CC IsoId=P16378-1; Sequence=Displayed; CC Name=G-OA47A-2; CC IsoId=P16378-2; Sequence=VSP_001830; CC -!- TISSUE SPECIFICITY: EXPRESSED PRIMARILY IN NEURONAL CELL BODIES IN CC THE BRAIN, OPTIC LOBE, AND THORACIC AND ABDOMINAL GANGLIA. ALSO CC EXPRESSED IN ANTENNA, OOCYTES AND OVARIAN NURSE CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, HIGHEST CC LEVEL IN ADULTS. CC -!- SIMILARITY: BELONGS TO THE G-ALPHA FAMILY. SUBFAMILY 1 CC (G(I/O/T/Z)). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M29731; AAA28580.1; -. DR EMBL; M29732; AAA28581.1; -. DR EMBL; M31203; AAA28586.1; -. DR EMBL; M29601; AAA28586.1; JOINED. DR EMBL; M31198; AAA28586.1; JOINED. DR EMBL; M31199; AAA28586.1; JOINED. DR EMBL; M31200; AAA28586.1; JOINED. DR EMBL; M31201; AAA28586.1; JOINED. DR EMBL; M31202; AAA28586.1; JOINED. DR EMBL; M29602; AAA28587.1; -. DR EMBL; M30151; AAA28584.1; -. DR EMBL; M30152; AAA28585.1; -. DR EMBL; M31129; AAA28583.1; -. DR EMBL; M86660; AAA28577.1; -. DR EMBL; AE003829; AAF58789.1; -. DR EMBL; AE003829; AAM68759.1; -. DR PIR; A34304; RGFFO1. DR PIR; B34304; RGFFO2. DR HSSP; P04896; 1AZT. DR FlyBase; FBgn0001122; G-o-alpha-47A. DR InterPro; IPR001019; Gprotein_alpha. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR ProDom; PD000281; Gprotein_alpha; 1. DR SMART; SM00275; G_alpha; 1. KW GTP-binding; Transducer; Multigene family; ADP-ribosylation; KW Alternative splicing. FT NP_BIND 40 47 GTP (BY SIMILARITY). FT NP_BIND 201 205 GTP (BY SIMILARITY). FT NP_BIND 270 273 GTP (BY SIMILARITY). FT MOD_RES 179 179 ADP-RIBOSYL[1] (BY ACTION OF CTX). FT MOD_RES 351 351 ADP-RIBOSYL[1] (BY ACTION OF IAP). FT VARSPLIC 4 21 AQSAEERAAAARSRLIER -> TTSAEERAAIQRSKQIEK FT (in isoform G-OA47A-2). FT /FTId=VSP_001830. FT CONFLICT 88 88 M -> I (IN REF. 3; AAA28585). SQ SEQUENCE 354 AA; 40476 MW; 3C5DA142B4CF7DD2 CRC64; MGCAQSAEER AAAARSRLIE RNLKEDGIQA AKDIKLLLLG AGESGKSTIV KQMKIIHESG FTAEDFKQYR PVVYSNTIQS LVAILRAMPT LSIQYSNNER ESDAKMVFDV CQRMHDTEPF SEELLAAMKR LWQDAGVQEC FSRSNEYQLN DSAKYFLDDL DRLGAKDYQP TEQDILRTRV KTTGIVEVHF SFKNLNFKLF DVGGQRSERK KWIHCFEDVT AIIFCVAMSE YDQVLHEDET TNRMQESLKL FDSICNNKWF TDTSIILFLN KKDLFEEKIR KSPLTICFPE YTGGQEYGEA AAYIQAQFEA KNKSTSKEIY CHMTCATDTN NIQFVFDAVT DVIIANNLRG CGLY // ID GBAF_DROME STANDARD; PRT; 399 AA. AC Q05337; Q9VV88; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein G(F), alpha subunit. GN G-ALPHA-73B OR G-A73B OR CG12232. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=93248264; PubMed=7683429; RA Quan F., Wolfgang W.J., Forte M.; RT "A Drosophila G-protein alpha subunit, Gf alpha, expressed in a RT spatially and temporally restricted pattern during Drosophila RT development."; RL Proc. Natl. Acad. Sci. U.S.A. 90:4236-4240(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA AND CC GAMMA). THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING CC SITE. CC -!- TISSUE SPECIFICITY: DURING EMBRYOGENESIS, EXPRESSED PRIMARILY CC IN THE DEVELOPING GUT AND TRANSIENTLY IN THE AMNIOSEROSA. CC -!- DEVELOPMENTAL STAGE: EXPRESSED PRIMARILY DURING EMBRYONIC, LARVAL CC AND EARLY PUPAL DEVELOPMENT AND AT LOW LEVELS IN LATE PUPAE AND CC ADULTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L09700; AAA28569.1; -. DR EMBL; AE003526; AAF49429.2; -. DR PIR; A47460; A47460. DR HSSP; P04896; 1AZT. DR FlyBase; FBgn0010223; G-alpha-73B. DR InterPro; IPR001019; Gprotein_alpha. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR ProDom; PD000281; Gprotein_alpha; 1. DR SMART; SM00275; G_alpha; 1. KW GTP-binding; Transducer; Multigene family. FT NP_BIND 54 61 GTP (BY SIMILARITY). FT NP_BIND 221 225 GTP (BY SIMILARITY). FT NP_BIND 290 293 GTP (BY SIMILARITY). SQ SEQUENCE 399 AA; 46206 MW; 5A20427306C2F6D4 CRC64; MKLRLLRCLR QQPAKPAAVM THKEDQYPVS LDHHVLKDMA KGVRDTTVKI LLLGTAESGK TTIIKQMRIL HINGFTDDER REKIPEIYQN IHESILQLVG QMGVLGIDFG SCTSERSADY ILSLPGSAPE YMNEEYCDHV TTLWNDVGIR ACYDRSNEFP LLDSAKYFLD NFVRISDAEY IPSTEDILHS RKITTGISQI TFRVPIPKSM GGGEQQFQMY DVGGQRDQRN KWIQVFEGIQ AVLFLISCSE FDQNLREDPS QNRLQEALKL FRAVWQNRFL ASAGLIVFLN KYDIMERKIR AGKHIVDYFP EYEDFCKRPQ QDNCFGESDW TKMFIKQKLV DITQEPFKRH SRNQVDLGTS ERECYYHFTV ATDTRCIRDV FCDVQKMILS ENVSSMGLF // ID GBAL_DROME STANDARD; PRT; 457 AA. AC P25157; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein, alpha subunit homolog (Protein DE concertina). GN CTA OR CTR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91105860; PubMed=1899050; RA Parks S., Wieschaus E.; RT "The Drosophila gastrulation gene concertina encodes a G alpha-like RT protein."; RL Cell 64:447-458(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). CC -!- FUNCTION: MAY PLAY A ROLE IN A SIGNAL TRANSDUCTION PATHWAY USED CC DURING GASTRULATION. REQUIRED SPECIFICALLY FOR THE VENTRAL FURROW CC AND POSTERIOR MIDGUT INVAGINATIONS, WHERE IT IS NECESSARY FOR CC COORDINATING CELL SHAPE CHANGES. CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA AND CC GAMMA). THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING CC SITE. CC -!- TISSUE SPECIFICITY: DISTRIBUTED UNIFORMLY. CC -!- DEVELOPMENTAL STAGE: GASTRULATION. CC -!- SIMILARITY: BELONGS TO THE G-ALPHA FAMILY. SUBFAMILY 4 (G(12)). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M94285; AAA82939.1; -. DR PIR; A38567; A38567. DR HSSP; P04896; 1AZT. DR FlyBase; FBgn0000384; cta. DR GO; GO:0005834; C:heterotrimeric G-protein complex; NAS. DR GO; GO:0016476; P:shape changes of embryonic cells; NAS. DR InterPro; IPR001019; Gprotein_alpha. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR ProDom; PD000281; Gprotein_alpha; 1. DR SMART; SM00275; G_alpha; 1. KW GTP-binding; Transducer; Multigene family; Gastrulation. FT NP_BIND 139 146 GTP (BY SIMILARITY). FT NP_BIND 299 303 GTP (BY SIMILARITY). FT NP_BIND 369 372 GTP (BY SIMILARITY). SQ SEQUENCE 457 AA; 52753 MW; D204415C4BC2CEC7 CRC64; MSGITLTKLT QERISIPNNN VITNGVENNI DSDTLSGTLT HLMEEHRTRV GAVTGPEAAT TSTDGLISNG AERLRLQGSR LQTSRFACFR CCGNIITYLV RLRSTPEELE QRYKSKEIDK FLEKEKHTFR RQVKLLLLGA GESGKSTFLK QMRIIHGVNF DYELLLEYQS VIYQNVIRGM QVLLDAREKL NIAWGSDGRE QDAYDAKLME CNSLDVPKFM EYAPPISRLW QDRGIRRAFE RRREFQISDS VSYFLDEIQR LATPDYVPTH KDILHCRKAT KGVYEFCVKV QNIPFVFVDV GGQRTQRQKW TRCFDSSVTS IIFLVSSSEF DQVLAEDRKT NRLEESKNIF DTIVNNATFK GISIILFLNK TDLLEQKVCN PETDIRWYYP HFNGNPHSVL DVQNFILQMF MSVRRSSSIS RIYHHFTTAI DTRNINVVFN SVKDTILQRN LNALMLQ // ID GBAS_DROME STANDARD; PRT; 385 AA. AC P20354; P20355; Q9W1F9; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein G(S), alpha subunit (Adenylate DE cyclase-stimulating G alpha protein). GN G-S-ALPHA-60A OR G-SA60A OR CG2835. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RX MEDLINE=89264611; PubMed=2498884; RA Quan F., Wolfgang W.J., Forte M.A.; RT "The Drosophila gene coding for the alpha subunit of a stimulatory G RT protein is preferentially expressed in the nervous system."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4321-4325(1989). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=90158605; PubMed=2106072; RA Quan F., Forte M.A.; RT "Two forms of Drosophila melanogaster Gs alpha are produced by RT alternate splicing involving an unusual splice site."; RL Mol. Cell. Biol. 10:910-917(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. CC -!- FUNCTION: THE G(S) PROTEIN IS INVOLVED IN HORMONAL REGULATION OF CC ADENYLATE CYCLASE: IT ACTIVATES THE CYCLASE. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA AND CC GAMMA). THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING CC SITE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P20354-1; Sequence=Displayed; CC Name=Short; CC IsoId=P20354-2; Sequence=VSP_001831; CC -!- TISSUE SPECIFICITY: PREFERENTIALLY EXPRESSED IN THE NERVOUS SYSTEM CC AND IN THE EYES. CC -!- SIMILARITY: BELONGS TO THE G-ALPHA FAMILY. SUBFAMILY 2 (G(S)). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23233; AAA28917.1; -. DR EMBL; M33998; AAA28578.1; -. DR EMBL; M33997; AAA28578.1; JOINED. DR EMBL; M33998; AAA28579.1; -. DR EMBL; M33997; AAA28579.1; JOINED. DR EMBL; AE003462; AAF47107.2; -. DR EMBL; AE003462; AAM68282.2; -. DR EMBL; AY058572; AAL13801.1; -. DR PIR; A34754; RGFFAL. DR PIR; B34754; RGFFAS. DR HSSP; P04896; 1AZT. DR FlyBase; FBgn0001123; G-s-alpha-60A. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0002165; P:larval/pupal development (sensu Insecta); NAS. DR GO; GO:0007611; P:learning and/or memory; NAS. DR GO; GO:0008341; P:response to cocaine (sensu Insecta); NAS. DR GO; GO:0007632; P:visual behavior; NAS. DR GO; GO:0007476; P:wing morphogenesis; IMP. DR InterPro; IPR001019; Gprotein_alpha. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR ProDom; PD000281; Gprotein_alpha; 1. DR SMART; SM00275; G_alpha; 1. KW GTP-binding; Transducer; Multigene family; Palmitate; Lipoprotein; KW Alternative splicing. FT LIPID 3 3 S-palmitoyl cysteine (By similarity). FT NP_BIND 50 57 GTP (BY SIMILARITY). FT NP_BIND 211 215 GTP (BY SIMILARITY). FT NP_BIND 280 283 GTP (BY SIMILARITY). FT VARSPLIC 310 313 IDTG -> S (in isoform Short). FT /FTId=VSP_001831. SQ SEQUENCE 385 AA; 44999 MW; CC9F004F314AC48F CRC64; MGCFGSPTSK QSDVNSEDSK SQKRRSDAIS RQLQKDKQLY RATHRLLLLG AGESGKSTIV KQMRILHVDG FSDSEKKQKI DDIKKNIRDA ILTITGAMST LNPPVALEKK ENEPRVEYIQ DYASSPDFNY PPEFYEHTEE LWKDKGVLQT YERSNEYQLI DCAKYFLDRV STIKNPNYTP NEQDILRCRV LTSGIFETRF QVDKVNFHMF DVGGQRDERR KWIQCFNDVT AIIFVTACSS YNMVLREDPT QNRLRESLDL FKSIWNNRWL RTISIILFLN KQDLLAEKIK AGKSKLSEYF SEFNKYQTPI DTGDAIMESN DDPEVIRAKY FIRDEFLRIS TASGDGKHYC YPHFTCAVDT ENIKRVFNDC RDIIQRMHLR QYELL // ID GBB1_DROME STANDARD; PRT; 340 AA. AC P26308; Q9VXM8; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein beta subunit 1. GN G-BETA-13F OR GB13F OR CG10545. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89017152; PubMed=3140235; RA Yarfitz S., Provost N.M., Hurley J.B.; RT "Cloning of a Drosophila melanogaster guanine nucleotide regulatory RT protein beta-subunit gene and characterization of its expression RT during development."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7134-7138(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS A MODULATOR OR TRANSDUCER IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. THE BETA AND GAMMA CHAINS ARE REQUIRED FOR THE CC GTPASE ACTIVITY, FOR REPLACEMENT OF GDP BY GTP, AND FOR G PROTEIN- CC EFFECTOR INTERACTION. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS, ALPHA, BETA AND CC GAMMA. CC -!- SIMILARITY: CONTAINS 7 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22567; AAB59247.1; -. DR EMBL; AE003500; AAF48530.1; -. DR EMBL; AY058566; AAL13795.1; -. DR PIR; A40489; RGFFBH. DR HSSP; P04901; 1TBG. DR FlyBase; FBgn0001105; G-beta-13F. DR InterPro; IPR001632; Gprotein_B. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00319; GPROTEINB. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 4. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Transducer; Repeat; WD repeat; Multigene family. FT REPEAT 53 83 WD 1. FT REPEAT 95 125 WD 2. FT REPEAT 141 170 WD 3. FT REPEAT 182 212 WD 4. FT REPEAT 224 254 WD 5. FT REPEAT 268 298 WD 6. FT REPEAT 310 340 WD 7. SQ SEQUENCE 340 AA; 37133 MW; 5A4B70DCB0A1C32C CRC64; MNELDSLRQE AESLKNAIRD ARKAACDTSL LQAATSLEPI GRIQMRTRRT LRGHLAKIYA MHWGNDSRNL VSASQDGKLI VWDSHTTNKV HAIPLRSSWV MTCAYAPSGS YVACGGLDNM CSIYNLKTRE GNVRVSRELP GHGGYLSCCR FLDDNQIVTS SGDMSCGLWD IETGLQVTSF LGHTGDVMAL SLAPQCKTFV SGACDASAKL WDIREGVCKQ TFPGHESDIN AVTFFPNGQA FATGSDDATC RLFDIRADQE LAMYSHDNII CGITSVAFSK SGRLLLAGYD DFNCNVWDTM KAERSGILAG HDNRVSCLGV TENGMAVATG SWDSFLRVWN // ID GBB2_DROME STANDARD; PRT; 346 AA. AC P29829; DT 01-APR-1993 (Rel. 25, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein beta subunit 2. GN GBE OR GB76C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye; RX MEDLINE=92000689; PubMed=1910788; RA Yarfitz S., Niemi G.A., McConnell J.L., Fitch C.L., Hurley J.B.; RT "A G beta protein in the Drosophila compound eye is different from RT that in the brain."; RL Neuron 7:429-438(1991). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS A MODULATOR OR TRANSDUCER IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. THE BETA AND GAMMA CHAINS ARE REQUIRED FOR THE CC GTPASE ACTIVITY, FOR REPLACEMENT OF GDP BY GTP, AND FOR G PROTEIN- CC EFFECTOR INTERACTION. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS, ALPHA, BETA AND CC GAMMA. CC -!- TISSUE SPECIFICITY: IN THE DROSOPHILA COMPOUND EYE. CC -!- SIMILARITY: CONTAINS 7 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M76593; AAA73103.1; -. DR HSSP; P04901; 1TBG. DR FlyBase; FBgn0004623; G-beta-76C. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0003927; F:heterotrimeric G-protein GTPase activity; IMP. DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007202; P:phospholipase C activation; IMP. DR GO; GO:0007602; P:phototransduction; IMP. DR GO; GO:0016056; P:rhodopsin mediated signaling; IMP. DR InterPro; IPR001632; Gprotein_B. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00319; GPROTEINB. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 4. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 4. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Transducer; Repeat; WD repeat; Multigene family; Vision. FT REPEAT 57 87 WD 1. FT REPEAT 99 129 WD 2. FT REPEAT 147 176 WD 3. FT REPEAT 188 218 WD 4. FT REPEAT 230 260 WD 5. FT REPEAT 274 304 WD 6. FT REPEAT 316 345 WD 7. SQ SEQUENCE 346 AA; 38375 MW; 7C9F88EFF0092346 CRC64; MPKIDPETQK LYDEINGMIQ KFKDDQKSKA DCTLADKCGD MGDVPKIRFS SKKILKGHIN KVNSVHFAGD SRHCVTGSLD GKLIIWDTWT ANKVQIIPLR SAWVMTVAFS PSGNFEACGG MDNQCTVYDV NNRDAPGVAK MVKELMGYEG FLSSCRFLDD GHLITGSGDM KICHWDLEKG VKTMDFNGHA GDIAGLSLSP DMKTYITGSV DKTAKLWDVR EEGHKQMFFG HDMDVSSVCY HPSGFGFASC SEDQTARMYD LRADQQIAQY EPPQKNTGFT SCALSTSGRY LMCGGIEGNV HSWDTMKQRH TGTLSGHENR ITCISLCPNG MCLASTSWDQ QVRLWL // ID GBG1_DROME STANDARD; PRT; 70 AA. AC P38040; Q9V4Z3; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein gamma-1 subunit. GN G-GAMMA-1 OR CG8261. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92210579; PubMed=1372898; RA Ray K., Ganguly R.; RT "The Drosophila G protein gamma subunit gene (D-G gamma 1) produces RT three developmentally regulated transcripts and is predominantly RT expressed in the central nervous system."; RL J. Biol. Chem. 267:6086-6092(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE BETA AND GAMMA CHAINS ARE REQUIRED FOR THE GTPASE CC ACTIVITY, FOR REPLACEMENT OF GDP BY GTP, AND FOR G PROTEIN- CC EFFECTOR INTERACTION. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS, ALPHA, BETA AND CC GAMMA. CC -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN THE CENTRAL NERVOUS CC SYSTEM. CC -!- SIMILARITY: BELONGS TO THE G PROTEIN GAMMA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M85042; AAA28570.1; -. DR EMBL; AE003835; AAM71086.1; -. DR PIR; A42155; A42155. DR FlyBase; FBgn0004921; G-gamma-1. DR GO; GO:0005834; C:heterotrimeric G-protein complex; NAS. DR GO; GO:0003927; F:heterotrimeric G-protein GTPase activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR InterPro; IPR001770; G-gamma. DR Pfam; PF00631; G-gamma; 1. DR ProDom; PD003783; G-gamma; 1. DR SMART; SM00224; GGL; 1. DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1. KW Transducer; Prenylation; Lipoprotein. FT LIPID 67 67 S-geranylgeranyl cysteine FT (By similarity). FT PROPEP 68 70 REMOVED IN MATURE FORM (BY SIMILARITY). SQ SEQUENCE 70 AA; 8130 MW; 1CD46E3BBF8FE4F3 CRC64; MDVMSSSLQQ QRVVVEQLRR EAAIDRQTIS ESCAKMMKYI TEHEQEDYLL TGFTSQKVNP FREKSSCTVL // ID GBGE_DROME STANDARD; PRT; 72 AA. AC Q9NFZ3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein gamma-e subunit. GN G-GAMMA-30A OR CG18511. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye; RX MEDLINE=20076421; PubMed=10608815; RA Schulz S., Huber A., Schwab K., Paulsen R.; RT "A novel Ggamma isolated from Drosophila constitutes a visual G RT protein gamma subunit of the fly compound eye."; RL J. Biol. Chem. 274:37605-37610(1999). CC -!- FUNCTION: THE BETA AND GAMMA CHAINS ARE REQUIRED FOR THE GTPASE CC ACTIVITY, FOR REPLACEMENT OF GDP BY GTP, AND FOR G PROTEIN- CC EFFECTOR INTERACTION. THIS SUBUNIT FUNCTIONS IN VISUAL CC TRANSDUCTION IN THE COMPOUND EYE. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS, ALPHA, BETA AND CC GAMMA. CC -!- SIMILARITY: BELONGS TO THE G PROTEIN GAMMA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ250440; CAB70093.1; -. DR FlyBase; FBgn0028433; G-gamma-30A. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IPI. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0003927; F:heterotrimeric G-protein GTPase activity; IPI. DR GO; GO:0007602; P:phototransduction; IPI. DR InterPro; IPR001770; G-gamma. DR Pfam; PF00631; G-gamma; 1. DR PRINTS; PR00321; GPROTEING. DR ProDom; PD003783; G-gamma; 1. DR SMART; SM00224; GGL; 1. DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1. KW Transducer; Prenylation; Lipoprotein; Vision. FT LIPID 69 69 S-geranylgeranyl cysteine FT (By similarity). FT PROPEP 70 72 REMOVED IN MATURE FORM (BY SIMILARITY). SQ SEQUENCE 72 AA; 8398 MW; B0FC6DC9170EDA70 CRC64; MDPSALQNMD RDALKKQIEN MKYQASMERW PLSKSIAEMR SFIEENEKND PLINAPDKKN NPWAEKGKCV IM // ID GBI5_DROME STANDARD; PRT; 355 AA. AC P20353; Q9VS04; DT 01-FEB-1991 (Rel. 17, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein G(i), alpha subunit 65A. GN G-I-ALPHA-65A OR G-OA65C OR CG10060. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88298893; PubMed=3136172; RA Provost N.M., Somers D.E., Hurley J.B.; RT "A Drosophila melanogaster G protein alpha subunit gene is expressed RT primarily in embryos and pupae."; RL J. Biol. Chem. 263:12070-12076(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. CC -!- FUNCTION: THE G(O) PROTEIN FUNCTION IS NOT CLEAR. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA AND CC GAMMA). THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING CC SITE. CC -!- TISSUE SPECIFICITY: EXPRESSED PRIMARILY IN EMBRYOS AND PUPAE. CC -!- SIMILARITY: BELONGS TO THE G-ALPHA FAMILY. SUBFAMILY 1 CC (G(I/O/T/Z)). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23093; -; NOT_ANNOTATED_CDS. DR EMBL; M23094; AAA28565.1; -. DR EMBL; AE003560; AAF50626.1; -. DR EMBL; AY051670; AAK93094.1; -. DR PIR; A31076; RGFFA. DR HSSP; P10824; 1AS3. DR FlyBase; FBgn0001104; G-i-alpha-65A. DR InterPro; IPR001019; Gprotein_alpha. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR ProDom; PD000281; Gprotein_alpha; 1. DR SMART; SM00275; G_alpha; 1. KW GTP-binding; Transducer; Multigene family; ADP-ribosylation. FT NP_BIND 41 48 GTP (BY SIMILARITY). FT NP_BIND 201 205 GTP (BY SIMILARITY). FT NP_BIND 270 273 GTP (BY SIMILARITY). FT MOD_RES 179 179 ADP-RIBOSYL[1] (BY ACTION OF CTX). FT CONFLICT 140 140 S -> T (IN REF. 1). SQ SEQUENCE 355 AA; 40595 MW; 69DF15754EB22F9D CRC64; MGCAVSTARD KEAIERSKNI DRALRAEGER AASEVKLLLL GAGESGKSTI VKQMKIIHDT GYSQEECEEY RRVVFSNTVQ SLMVIIRAMG RLKIEFADPS RTDIARQFFT HASAADEGIL LPEIVLLMKK LWADGGVQQS FARSREYQLN DSAGYYLNSL DRIAQPNYIP TQQDVLRTRV KTTGIIETHF SCKQLHFKLF DVGGQRSERK KWIHCFEGVT AIIFCVALSG YDLVLAEDEE MNRMIESLKL FDSICNSKWF VETSIILFLN KKDLFEEKIK RSPLTICFPE YTGTNTFEEA ANYIRMKFEN LNKRKDQKEI YTHLTCATDT NNVKFVFDAV TDVIIKNNLK QIGLF // ID GBLP_DROME STANDARD; PRT; 318 AA. AC O18640; Q9VLW5; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein beta subunit-like protein DE (Receptor of activated protein kinase C homolog). GN RACK1 OR CG7111. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=97441085; PubMed=9296523; RA Vani K., Yang G., Mohler J.; RT "Isolation and cloning of a Drosophila homolog to the mammalian RACK1 RT gene, implicated in PKC-mediated signalling."; RL Biochim. Biophys. Acta 1358:67-71(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: HIGHEST EXPRESSION IN THE MESODERMAL AND CC ENDODERMAL LINEAGES. CC -!- SIMILARITY: CONTAINS 7 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96491; AAB72148.1; -. DR EMBL; AE003619; AAF52566.1; -. DR FlyBase; FBgn0020618; Rack1. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 5. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 4. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Repeat; WD repeat. FT REPEAT 13 44 WD 1. FT REPEAT 62 92 WD 2. FT REPEAT 104 134 WD 3. FT REPEAT 147 179 WD 4. FT REPEAT 191 221 WD 5. FT REPEAT 232 261 WD 6. FT REPEAT 282 312 WD 7. FT CONFLICT 104 104 G -> R (IN REF. 1). SQ SEQUENCE 318 AA; 35618 MW; 202930BE51AEE822 CRC64; MSETLQLRGT LIGHNGWVTQ IATNPKDPDT IISASRDKTL IVWKLTRDED TNYGYPQKRL YGHSHFISDV VLSSDGNYAL SGSWDQTLRL WDLAAGKTTR RFEGHTKDVL SVAFSADNRQ IVSGSRDKTI KLWNTLAECK FTIQEDGHTD WVSCVRFSPN HSNPIIVSCG WDRTVKVWNL ANCKLKNNHH GHNGYLNTVT VSPDGSLCTS GGKDSKALLW DLNDGKNLYT LEHNDIINAL CFSPNRYWLC VAYGPSIKIW DLACKKTVEE LRPEVVSPTS KADQPQCLSL AWSTDGQTLF AGYSDNTIRV WQVSVSAH // ID GBQ_DROME STANDARD; PRT; 353 AA. AC P23625; P54400; Q9V6E2; DT 01-NOV-1991 (Rel. 20, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Guanine nucleotide-binding protein G(q), alpha subunit (dGQalpha). GN G-ALPHA-49B OR G-A49B OR DGQ OR CG17759. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RX MEDLINE=91097801; PubMed=2125225; RA Lee Y.-J., Dobbs M.B., Verardi M.L., Hyde D.R.; RT "Dgq: a Drosophila gene encoding a visual system-specific G alpha RT molecule."; RL Neuron 5:889-898(1990). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Appendages; RX MEDLINE=96102136; PubMed=8524786; RA Talluri S., Bhatt A., Smith D.P.; RT "Identification of a Drosophila G protein alpha subunit (dGq alpha-3) RT expressed in chemosensory cells and central neurons."; RL Proc. Natl. Acad. Sci. U.S.A. 92:11475-11479(1995). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. COULD BE THE TRANSDUCIN ANALOG, AN AMPLIFIER CC AND ONE OF THE TRANSDUCERS OF A VISUAL IMPULSE THAT PERFORMS THE CC COUPLING BETWEEN OPSIN AND CGMP-PHOSPHODIESTERASE. COULD MEDIATE A CC SUBSET OF OLFACTORY AND GUSTATORY RESPONSES. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=1; CC IsoId=P23625-1; Sequence=Displayed; CC Name=2; CC IsoId=P23625-2; Sequence=VSP_001835, VSP_001836; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: ISOFORM 1 IS EXPRESSED ONLY IN THE RETINA AND CC OCELLUS OF THE ADULT HEAD. ISOFORM 2 IS EXPRESSED IN CHEMOSENSORY CC CELLS OF THE OLFACTORY AND TASTE STRUCTURES, INCLUDING A SUBSET OF CC OLFACTORY AND GUSTATORY NEURONS, AND IN CELLS OF THE CENTRAL CC NERVOUS SYSTEM, INCLUDING NEURONS IN THE LAMINA GANGLIONARIS. CC -!- SIMILARITY: BELONGS TO THE G-ALPHA FAMILY. SUBFAMILY 3 (G(Q)). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M58016; AAA28460.1; -. DR EMBL; U31092; AAC46943.1; -. DR EMBL; AE003821; AAM68632.1; -. DR HSSP; P10824; 1BOF. DR FlyBase; FBgn0004435; G-alpha-49B. DR GO; GO:0016027; C:inaD signaling complex; IDA. DR GO; GO:0003927; F:heterotrimeric G-protein GTPase activity; IMP. DR GO; GO:0007202; P:phospholipase C activation; IGI. DR GO; GO:0007602; P:phototransduction; IEP. DR GO; GO:0016056; P:rhodopsin mediated signaling; IMP. DR InterPro; IPR001019; Gprotein_alpha. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR ProDom; PD000281; Gprotein_alpha; 1. DR SMART; SM00275; G_alpha; 1. KW GTP-binding; Transducer; Multigene family; ADP-ribosylation; KW Palmitate; Lipoprotein; Vision; Alternative splicing. FT LIPID 3 3 S-palmitoyl cysteine (By similarity). FT LIPID 4 4 S-palmitoyl cysteine (By similarity). FT NP_BIND 40 47 GTP (BY SIMILARITY). FT NP_BIND 199 203 GTP (BY SIMILARITY). FT NP_BIND 268 271 GTP (BY SIMILARITY). FT MOD_RES 177 177 ADP-RIBOSYL[1] (BY ACTION OF CTX) FT (BY SIMILARITY). FT VARSPLIC 156 194 SDLARIEQADYLPTEQDILRARVPTTGILEYPFDLDGIV FT -> KDLDRVAQPAYLPTEQDILRVRVPTTGIIEYPFDLEEI FT R (in isoform 2). FT /FTId=VSP_001835. FT VARSPLIC 293 353 KQDHAAAKQFVLKKYLACNPDPERQCYSHFTTATDTENIKL FT VFCAVKDTIMQNALKEFNLG -> QRDAITAREFILRMFVD FT LNPDSEKIIYSHFTCATDTENIRFVFAAVKDTILQSNLKEY FT NLV (in isoform 2). FT /FTId=VSP_001836. SQ SEQUENCE 353 AA; 41295 MW; A742A7C9CB23FD19 CRC64; MECCLSEEAK EQKRINQEIE KQLRRDKRDA RRELKLLLLG TGESGKSTFI KQMRIIHGSG YSDEDKRGYI KLVFQNIFMA MQSMIKAMDM LKISYGQGEH SELADLVMSI DYETVTTFED PYLNAIKTLW DDAGIQECYD RRREYQLTDS AKYYLSDLAR IEQADYLPTE QDILRARVPT TGILEYPFDL DGIVFRMVDV GGQRSERRKW IHCFENVTSI IFLVALSEYD QILFESDNEN RMEESKALFR TIITYPWFQN SSVILFLNKK DLLEEKIMYS HLVDYFPEYD GPKQDHAAAK QFVLKKYLAC NPDPERQCYS HFTTATDTEN IKLVFCAVKD TIMQNALKEF NLG // ID GCH1_DROME STANDARD; PRT; 324 AA. AC P48596; Q960S4; Q9W2J9; Q9W2K1; Q9Y0C8; DT 01-FEB-1996 (Rel. 33, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GTP cyclohydrolase I (EC 3.5.4.16) (GTP-CH-I) (Punch protein). GN PU OR CG9441. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS B AND C), FUNCTION, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RC TISSUE=Head; RX MEDLINE=94086535; PubMed=8262960; RA McLean J.R., Krishnakumar S., O'Donnell J.M.; RT "Multiple mRNAs from the Punch locus of Drosophila melanogaster RT encode isoforms of GTP cyclohydrolase I with distinct N-terminal RT domains."; RL J. Biol. Chem. 268:27191-27197(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORM A). RC TISSUE=Embryo; RA Xu D., Neckameyer W., O'Donnell J.; RT "Differential regulation of Drosophila GTP cyclohydrolase I isoforms RT and their interaction with tyrosine hydroxylase."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ISOFORM B IS REQUIRED FOR EYE PIGMENT PRODUCTION, CC ISOFORM C MAY BE REQUIRED FOR NORMAL EMBRYONIC DEVELOPMENT AND CC SEGMENT PATTERN FORMATION. CC -!- CATALYTIC ACTIVITY: GTP + 2 H(2)O = FORMATE + 2-AMINO-4-HYDROXY-6- CC (ERYTHRO-1,2,3-TRIHYDROXYPROPYL)DIHYDROPTERIDINE TRIPHOSPHATE. CC -!- PATHWAY: TETRAHYDROBIOPTERIN BIOSYNTHESIS; FIRST STEP. CC -!- SUBUNIT: HOMOPOLYMER (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; Synonyms=C; CC IsoId=P48596-1; Sequence=Displayed; CC Name=B; CC IsoId=P48596-2; Sequence=VSP_001616; CC Name=C; CC IsoId=P48596-3; Sequence=VSP_001615; CC -!- TISSUE SPECIFICITY: ISOFORM B IS EXPRESSED ALMOST EXCLUSIVELY IN CC ADULT HEADS. CC -!- DEVELOPMENTAL STAGE: ISOFORM C IS EXPRESSED IN EMBRYOS, LARVAE AND CC ADULTS. CC -!- SIMILARITY: BELONGS TO THE GTP CYCLOHYDROLASE I FAMILY. CC -!- CAUTION: REF.1 AND REF.2 SEQUENCES DIFFER FROM THAT SHOWN DUE TO CC FRAMESHIFTS IN POSITIONS 27, 75, 266 AND 271. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U01118; AAC04308.1; ALT_FRAME. DR EMBL; U01119; AAC04309.1; ALT_FRAME. DR EMBL; AF159422; AAD44334.1; ALT_FRAME. DR EMBL; AE003453; AAF46690.1; -. DR EMBL; AE003453; AAF46692.1; -. DR EMBL; AE003453; AAM70858.1; -. DR EMBL; AY051890; AAK93314.1; -. DR HSSP; P27511; 1A8R. DR FlyBase; FBgn0003162; Pu. DR GO; GO:0006727; P:ommochrome biosynthesis; IMP. DR InterPro; IPR001474; GTP_cyclohydroI. DR Pfam; PF01227; GTP_cyclohydroI; 1. DR ProDom; PD003330; GTP_cyclohydroI; 1. DR TIGRFAMs; TIGR00063; folE; 1. DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1. DR PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1. KW Tetrahydrobiopterin biosynthesis; Hydrolase; Allosteric enzyme; KW Alternative splicing. FT DISULFID 214 285 BY SIMILARITY. FT VARSPLIC 102 117 Missing (in isoform C). FT /FTId=VSP_001615. FT VARSPLIC 1 117 MSFTRQLSEMSASELNDAIDDTNFPQAHILSRGRNNSVCST FT SSTSGTSSLADRQQNQAEEATAIAGTPVEEVAPAPALVPLA FT GNQRPRLILKTNGSSPDSDGTQPKTPLTPRTSTTP -> MK FT PQTSEQNGSGQNGEGAADAVAVATIPTGEASAASATSGTDL FT TVSKNSQQLKLEMLNLELASNGS (in isoform B). FT /FTId=VSP_001616. SQ SEQUENCE 324 AA; 35541 MW; 712A0045F2C12D6A CRC64; MSFTRQLSEM SASELNDAID DTNFPQAHIL SRGRNNSVCS TSSTSGTSSL ADRQQNQAEE ATAIAGTPVE EVAPAPALVP LAGNQRPRLI LKTNGSSPDS DGTQPKTPLT PRTSTTPGHE KCTFHHDLEL DHKPPTREAL LPDMARSYRL LLGGLGENPD RQGLIKTPER AAKAMLYFTK GYDQSLEDVL NGAVFDEDHD EMVVVKDIEM FSMCEHHLVP FYGKVSIGYL PCNKILGLSK LARIVEIFSR RLQVQERLTK QIAVAVTQAV QPAGVAVVVE GVHMCMVMRG VQKINSKTVT STMLGVFRDD PKTREEFLNL VNSK // ID GCL1_DROME STANDARD; PRT; 569 AA. AC Q01820; Q9V4X5; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Germ cell-less protein. GN GCL OR CG8411. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92370679; PubMed=1380406; RA Jongens T.A., Hay B., Jan L.Y., Jan Y.N.; RT "The germ cell-less gene product: a posteriorly localized component RT necessary for germ cell development in Drosophila."; RL Cell 70:569-584(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR THE SPECIFICATION OF POLE CELLS AND GERM CC CELL FORMATION. MOTHERS WITH REDUCED GLC FUNCTION GIVE RISE TO CC STERILE ADULT PROGENY THAT LACK GERM CELLS. CC -!- SUBCELLULAR LOCATION: POLE PLASM. CC -!- DEVELOPMENTAL STAGE: OOGENESIS AND EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97933; AAA28566.1; -. DR EMBL; AE003836; AAF59048.1; -. DR EMBL; AY061319; AAL28867.1; -. DR PIR; A43317; A43317. DR FlyBase; FBgn0005695; gcl. DR GO; GO:0005643; C:nuclear pore; IDA. DR GO; GO:0016480; P:negative regulation of transcription from P...; IMP. DR GO; GO:0007278; P:pole cell fate determination; IDA. DR InterPro; IPR000210; BTB_POZ. DR Pfam; PF00651; BTB; 1. DR SMART; SM00225; BTB; 1. DR PROSITE; PS50097; BTB; 1. KW Developmental protein. FT DOMAIN 66 136 BTB. SQ SEQUENCE 569 AA; 65152 MW; A91A670C4B5F83A4 CRC64; MGQIVGSMHM NVAEVFSNRR KRKRSTDSSL GKDDPAQLDT TQPKKKKLLT TTQYIYKALF KEEKNSDVAV MALDKVWHLH KVYLSQSPYF YTMFNGTWRE AQQNFIQITI LDDRITVASL DAVFGSMYSD EIEIESADVI SVLATATLFH LDGIIDKCAE VMVDNISPET AIQYYEAACQ YGVVGVKKST FQWFQINLLS IYSKQPNLLR HISIELMSAL TASPDLYVMQ TEFSLYTLLR TWMFLRLHPD YDPEDPVQRA EALKTQELLV NAGVETHAPS GDVVQWTYFT SRSEERSFLA TPEGQPYVKV FQKLRTQYLT NHYMDLKIIY NDNIIPKEWL YRHIHNHWDA LLRIDHGQED CSPQQLDDEQ FFENCMRCGR MLLEPGYQKW RWTGFNFGMD LILIMDSRRL NIRRHHRHEH ERVLSLQTKR KFMVRTTVTS INAQRQAVFT QTSEICSLSL EKNEEVPLMV LDPKLVHPLL ISINMLVVMP PNQSFKEIVP LSEEATTSLS IPISEIGANS DRPLSPSSAD DSAVFIGDSE PSTPSSPAPR PRIAWSASET GAICGQLAC // ID GCM2_DROME STANDARD; PRT; 613 AA. AC Q9VLA2; Q8N012; Q8WST6; Q9NCQ2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor glial cells missing 2 (Glide2 protein). GN GCM2 OR CG3858. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=21423447; PubMed=11532931; RA Kammerer M., Giangrande A.; RT "Glide2, a second glial promoting factor in Drosophila melanogaster."; RL EMBO J. 20:4664-4673(2001). RN [2] RP SEQUENCE FROM N.A. (ISOFORM A). RA Hosoya T., Iwasaki Y., Osato M., Higashi-Takizawa C., Akiyama-Oda Y., RA Ikenaka K., Hiromi Y., Hotta Y.; RT "Binary cell-fate decisions in Drosophila neurogenesis and RT hematopoiesis regulated by Gcm-motif transcription factors."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=22157281; PubMed=12167411; RA Alfonso T.B., Jones B.W.; RT "gcm2 promotes glial cell differentiation and is required with glial RT cells missing for macrophage development in Drosophila."; RL Dev. Biol. 248:369-383(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: TRANSCRIPTION FACTOR WITH A MINOR ROLE PROMOTING GLIAL CC CELL DIFFERENTIATION AND A MORE SIGNIFICANT ROLE IN HEMATOCYTE CC DIFFERENTIATION. GCM2, TOGETHER WITH GCM, IS REQUIRED FOR THE CC PROLIFERATION OF PLASMATOCYTE PRECURSORS, THE EXPRESSION OF CC CROQUEMORT PROTEIN, AND THE ABILITY OF PLASMATOCYTES TO CONVERT CC INTO MACROPHAGES. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=Q9VLA2-1; Sequence=Displayed; CC Name=A; CC IsoId=Q9VLA2-2; Sequence=VSP_008080; CC -!- TISSUE SPECIFICITY: EXPRESSED IN GLIAL LINEAGES WITHIN EMBRYONIC CC PROCEPHALIC MESODERM. EXPRESSION IS HIGHEST IN HEMOCYTE PRIMORDIA CC AND LONGITUDINAL AND NERVE ROOT GANGLIA. CC -!- DEVELOPMENTAL STAGE: FIRST APPEARS IN EMBRYOS, LEVELS DECREASE IN CC LARVAE AND PEAK AGAIN IN 1 DAY OLD PUPAE. NO EXPRESSION IS FOUND CC IN ADULTS. CC -!- SIMILARITY: CONTAINS 1 GCM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF184664; AAF74349.1; -. DR EMBL; AB056467; BAB83120.1; -. DR EMBL; AF461416; AAM22408.1; -. DR EMBL; AE003625; AAF52793.2; -. DR FlyBase; FBgn0019809; gcm2. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003700; F:transcription factor activity; IDA. DR GO; GO:0010001; P:glial cell differentiation; IMP. DR GO; GO:0042387; P:plasmatocyte differentiation; IEP. DR InterPro; IPR003902; GCM_motif. DR Pfam; PF03615; GCM; 1. DR PROSITE; PS50807; GCM; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW Developmental protein; Alternative splicing. FT DOMAIN 72 231 GCM. FT DOMAIN 570 600 HIS/PRO-RICH. FT VARSPLIC 1 11 MQLIIYKILY R -> MVVI (in isoform A). FT /FTId=VSP_008080. FT CONFLICT 39 39 S -> N (IN REF. 2). FT CONFLICT 44 44 S -> P (IN REF. 2 AND 3). FT CONFLICT 48 48 G -> C (IN REF. 2). FT CONFLICT 57 57 G -> V (IN REF. 3). FT CONFLICT 67 67 T -> A (IN REF. 2). FT CONFLICT 295 295 A -> T (IN REF. 3). FT CONFLICT 308 308 S -> N (IN REF. 2). FT CONFLICT 440 440 G -> S (IN REF. 3). FT CONFLICT 496 496 Q -> E (IN REF. 3). FT CONFLICT 550 550 S -> N (IN REF. 2). FT CONFLICT 571 571 T -> A (IN REF. 2 AND 3). SQ SEQUENCE 613 AA; 66667 MW; B9C9CEE82E1663D7 CRC64; MQLIIYKILY RNGYSFKTQQ LLTQQPDHSQ LTQFVQPQSQ STHSVHPGPS PGQQQAGGSM TMPSSSTGKG KREWDINDAI VPHVPDQEFD EFNEWSDGHV RHIYSLHNEE AKKHISGWAM RNTNNHNVNI LKKSCLGVLV CSQHCTLPNG SKINLRPAIC DKARRKQEGK ACPNKSCRGG RLEIKPCRGH CGYPVTHFWR HSGNAIFFQA KGVHDHLRPD PKNSSVSKRA FGRVPLAGKS ANGSVAKKSV IAGLVKQAKQ QHSLISKVLK RPAVSNPLAH TALDIYQYNA CGKCAGYSHC TCSYLDDSTT ARSHQLSQSS NYGTNSWPLS GSESSAPCET AANVFTVNHQ HITYNYPIYH ATPAAATAAP SKSPSLPYAC SISELAAYQQ SSSGNSFAMG VPVHGHTQCQ AVAYDSSPQL ATPEPEFINY SQIKHLGGGG GQEEISCKAE PGPTIKYNAT VETQPYVEDN YDYYYSPKAE YEMQQHHHQQ QQSHQQFGGN QTAGHHYYES SSGYNGVSYF DTGTTTAPGN TATGNGLEVG YGGYYDHYTS YEQQMAVAGG FATAGGSTAP TVAAPPGHPP PPPPPPTLTY HHHHHHHLHH PAAATGLAPS VTH // ID GCM_DROME STANDARD; PRT; 504 AA. AC Q27403; Q9VLA5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor glial cells missing (Glide protein). GN GCM OR CG12245. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96016097; PubMed=7553844; RA Hosoya T., Takizawa K., Nitta K., Hotta Y.; RT "Glial cells missing: a binary switch between neuronal and glial RT determination in Drosophila."; RL Cell 82:1025-1036(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96016096; PubMed=7553843; RA Jones B.W., Fetter R.D., Tear G., Goodman C.S.; RT "Glial cells missing: a genetic switch that controls glial versus RT neuronal fate."; RL Cell 82:1013-1023(1995). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=98022869; PubMed=9356176; RA Bernardoni R., Vivancos V., Giangrande A.; RT "Glide/gcm is expressed and required in the scavenger cell lineage."; RL Dev. Biol. 191:118-130(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTION FACTOR THAT INDUCES GLIOGENESIS. IT CC DETERMINES THE CHOICE BETWEEN GLIAL AND NEURONAL FATES. ALSO HAS A CC ROLE IN THE DIFFERENTIATION OF THE PLASMATOCYTE/MACROPHAGE LINEAGE CC OF HEMOCYTES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 GCM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D64040; BAA10905.1; -. DR EMBL; U34039; AAC46912.1; -. DR EMBL; U81164; AAC47808.1; -. DR EMBL; AE003625; AAF52790.1; -. DR PIR; A57215; A57215. DR TRANSFAC; T02302; -. DR FlyBase; FBgn0014179; gcm. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0007403; P:glial cell fate determination; IMP. DR GO; GO:0007516; P:hemocyte development; NAS. DR InterPro; IPR003902; GCM_motif. DR Pfam; PF03615; GCM; 1. DR PROSITE; PS50807; GCM; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW Developmental protein. FT DOMAIN 32 188 GCM. FT CONFLICT 413 413 I -> F (IN REF. 4). SQ SEQUENCE 504 AA; 56168 MW; 07D7DC22C4944C4F CRC64; MVLNGMPITM PVPMPVPMPV PSPPATKSRV AIDWDINDSK MPSVGEFDDF NDWSNGHCRL IYSVQSDEAR KHASGWAMRN TNNHNVNILK KSCLGVLLCS AKCKLPNGAS VHLRPAICDK ARRKQQGKQC PNRNCNGRLE IQACRGHCGY PVTHFWRRDG NGIYFQAKGT HDHPRPEAKG STEARRLLAG GRRVRSLAVM LARESALSDK LSSLRPTKRQ AKTQSIQESK RRRMGASDVL ETKQELVVPP TTYLPTSTPT HSTNFNQSQG SYVPAGQGSV ISQWNREIHY ETEDPCYANG MYSYDMLHSP LSAHSSTGSY YQENKPQQLQ HSQYQQQLSP QQHVPVSYDP SQPISSSLQC GMPSYEICDD TSSLTSSSGY CSEDYGYYNG YLPNSLDVSN GSQSQNLSQD ASIYTTSSEI FSVFESTLNG GGTSGVDLIY DEATAYQQHQ QQGTFPHLTN YQQEPQDQMQ SADYYYSNTG VDNSWNIQMD ATYHPVNSTD PIYC // ID GCP2_DROME STANDARD; PRT; 852 AA. AC Q9XYP7; Q95RT7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gamma-tubulin complex component 2 homolog (Gamma ring complex protein DE 84) (dGrip84) (d84p). GN GRIP84 OR CG3917. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 2), AND SEQUENCE OF 39-56; 95-106; RP 166-173; 237-248; 340-347; 358-370; 391-396; 406-412; 418-435; RP 438-444; 515-519 AND 570-588. RX MEDLINE=99156983; PubMed=10037793; RA Oegema K., Wiese O.C., Martin O., Milligan R.A., Iwamatsu A., RA Mitchison T.J., Zheng Y.; RT "Characterization of two related Drosophila gamma-tubulin complexes RT that differ in their ability to nucleate microtubules."; RL J. Cell Biol. 144:721-733(1999). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 291-852 FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBUNIT: GAMMA-TUBULIN SMALL COMPLEX (GAMMMA TUSC) IS A CC HETEROTETRAMERIC COMPLEX WHICH CONTAINS TWO MOLECULES OF GAMMA- CC TUBULIN, AND ONE MOLECULE EACH OF DGRIP84 AND DGRIP91. THE GAMMA- CC TUBULIN IN THIS COMPLEX BINDS PREFERENTIALLY TO GDP OVER GTP. CC -!- SUBCELLULAR LOCATION: CENTROSOME (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9XYP7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9XYP7-2; Sequence=VSP_001619; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE GCP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF118379; AAD27816.1; -. DR EMBL; AE003512; AAF48971.1; -. DR EMBL; AY061148; AAL28696.1; ALT_INIT. DR FlyBase; FBgn0026430; Grip84. DR GO; GO:0008275; C:gamma-tubulin small complex; IDA. DR GO; GO:0007020; P:microtubule nucleation; IDA. DR InterPro; IPR007259; Spc97_Spc98. DR Pfam; PF04130; Spc97_Spc98; 1. KW Microtubule; Alternative splicing. FT DOMAIN 18 27 POLY-SER. FT VARSPLIC 747 779 Missing (in isoform 2). FT /FTId=VSP_001619. FT CONFLICT 171 171 H -> S (IN REF. 1; AA SEQUENCE). SQ SEQUENCE 852 AA; 98504 MW; 38BE28083FE3E92B CRC64; MYALLVFVER YSECKPVSES SSSTSLSAMG LPHGNKTSDV NSAAGSVPTT LAIASTSTIL TTSQNVSGST RLSLTQSQDF PTSTPVNCKK ATESDTTPVV FVRRGPMDRN RGAGKDERND LSVIKERVLN AVSDQSLSGY RSVTNKTGNS PKSMPNDLVT LTDVPDEYRT HLLWEYYKVD GDKVPRAEIA AMPLLSQESM LLDELLHCLT GIRESLLVPQ KPIISAVGLA KYDTDFDIHT HLDRSLTHQV REILPLASYF MGVQKIIAAT DGLGQVMNSL NEALQELTHD FYLIIVQAEQ ELRHNRLTLQ KLLYYLQPTM WVMHEVWSSL VIIQLSDSRD AEVLTYLHER IKRLEGNKDA QQLIIGLVRK AAKPYMRMLQ MWIQKGVIVD RHREFLVVDN EVIHRDELPE HYSDDYWERR YTLRDEQIPS FLAKYSDKIL RTGKYLNVIR QCGKRVMPTQ EMNLEFDPTS ERHVSVINDA YYFAARMLLD VLLTENDLMG HLQSVKRYLL LNQGDFTMQF MDACEDELTK NVDHVLPMTL ENLLGLTLRI SSARNDPYKD DLHCELLPYD LVTQMSKIMK KEENWQAQPR LDLSGLECFA FTYEVKWPCS LVLNHISISK YQMLFRQLFY CKHVERQLCK IWKENSIARQ FEPQAASLYR AAFTLRQRMM NAIQNLEYYM MIEIIEPNWH IFIEKMKTVE NVDNVLRLHQ DFLDSCLKNC MLTESSHLNR SIFKLCKICL KYCEFIQITQ RYFQDAELRS MVRDSADSSE SEQESLHCPQ IETPLDPTDT FSERVRRFDL EFTQLLISFL KQINSMAKKN TADCFMNLVH RINFNAFYTD QMDKMCVEDA IG // ID GCP3_DROME STANDARD; PRT; 917 AA. AC Q9XYP8; Q9VY94; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gamma-tubulin complex component 3 homolog (Gamma ring complex protein DE 91) (dGrip91) (d91p). GN L(1)DD4 OR CG10988. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 24-36; 85-90; 202-227; 250-257; RP 277-302; 541-548; 616-626; 664-671; 799-804; 810-817 AND 863-880. RX MEDLINE=99156983; PubMed=10037793; RA Oegema K., Wiese C., Martin O.C., Milligan R.A., Iwamatsu A., RA Mitchison T.J., Zheng Y.; RT "Characterization of two related Drosophila gamma-tubulin complexes RT that differ in their ability to nucleate microtubules."; RL J. Cell Biol. 144:721-733(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBUNIT: GAMMA-TUBULIN SMALL COMPLEX (GAMMMA TUSC) IS A CC HETEROTETRAMERIC COMPLEX WHICH CONTAINS TWO MOLECULES OF GAMMA- CC TUBULIN, AND ONE MOLECULE EACH OF DGRIP84 AND DGRIP91. THE GAMMA- CC TUBULIN IN THIS COMPLEX BINDS PREFERENTIALLY TO GDP OVER GTP. CC -!- SUBCELLULAR LOCATION: CENTROSOME (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE GCP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF118380; AAD27817.1; -. DR EMBL; AE003493; AAF48309.1; -. DR EMBL; AY069292; AAL39437.1; -. DR FlyBase; FBgn0001612; l(1)dd4. DR GO; GO:0008275; C:gamma-tubulin small complex; IDA. DR GO; GO:0007020; P:microtubule nucleation; IDA. DR InterPro; IPR007259; Spc97_Spc98. DR Pfam; PF04130; Spc97_Spc98; 1. KW Microtubule. FT CONFLICT 79 79 N -> Y (IN REF. 1). FT CONFLICT 118 118 M -> I (IN REF. 1). FT CONFLICT 413 413 L -> F (IN REF. 1). FT CONFLICT 479 479 L -> F (IN REF. 1). FT CONFLICT 583 583 G -> A (IN REF. 1). SQ SEQUENCE 917 AA; 103706 MW; 6AEE88C211D256BB CRC64; MSQDRIAGID VATNSTDISN IINEMIICIK GKQMPEVHEK AMDHLSKMIA ANSRVIRDSN MLTERECVQK IMKLLSARNK KEEGKTVSDH FNELYRKLTL TKCDPHMRHS LMTHLLTMTD NSDAEKAVAS EDPRTQCDNL TQILVSRLNS ISSSIASLNE MGVVNGNGVG AAAVTGAAAV TGAAAVTGAA AVTGAAASHS YDATQSSIGL RKQSLPNYLD ATKMLPESRH DIVMSAIYSF TGVQGKYLKK DVVTGRFKLD QQNIKFLTTG QAGMLLRLSE LGYYHDRVVK FSDVSTGFNA IGSMGQALIS KLKEELANFH GQVAMLHDEM QRFRQASVNG IANKGKKDSG PDAGDEMTLF KLLAWYIKPL HRMQWLTKIA DACQVKKGGD LASTVYDFLD NGNDMVNKLV EDLLTAICGP LVRMISKWIL EGGISDMHRE FFVKSIKDVG VDRLWHDKFR LRLPMLPKFV PMDMANKILM TGKSINFLRE ICEEQGMMKE RDELMKVMES SASQIFSYTP DTSWHAAVET CYQQTSKHVL DIMVGPHKLL DHLHGMRRYL LLGQGDFISI LIENMKNELE RPGLDIYAND LTSMLDSALR CTNAQYDDPD ILNHLDVIVQ RPFNGDIGWN IISLQYIVHG PLAAMLESTM PTYKVLFKPL WRMKHMEFVL SMKIWKEQMG NAKALRTMKS EIGKASHRLN LFTSEIMHFI HQMQYYVLFE VIECNWVELQ KKMQKATTLD EILEAHEKFL QTILVGCFVS NKASVEHSLE VVYENIIELE KWQSSFYKDC FKELNARKEL SKIVEKSEKK GVYGLTNKMI LQRDQEAKIF AEKMDIACRG LEVIATDYEK AVSTFLMSLN SSDDPNLQLF GTRLDFNEYY KKRDTNLSKP LTFEHMRMSN VFAVNSRFVI CTPSTQE // ID GCP4_DROME STANDARD; PRT; 650 AA. AC Q9VKU7; Q9U1J7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gamma-tubulin complex component 4 homolog (Gamma ring complex protein DE 75) (dGrip75). GN GRIP75 OR 75P OR CG6176. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20029771; PubMed=10562286; RA Fava F., Raynaud-Messina B., Leung-Tack J., Mazzolini L., Li M., RA Guillemot J.C., Cachot D., Tollon Y., Ferrara P., Wright M.; RT "Human 76p: a new protein member of the gamma-tubulin associated RT protein family."; RL J. Cell Biol. 147:857-868(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: GAMMA-TUBULIN COMPLEX IS NECESSARY FOR MICROTUBLULE CC NUCLEATION AT THE CENTROSOME (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CENTROSOME (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE GCP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003628; AAF52962.2; -. DR EMBL; AJ249678; CAB62508.1; -. DR FlyBase; FBgn0026431; Grip75. DR GO; GO:0008274; C:gamma-tubulin ring complex; ISS. DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS. DR GO; GO:0007020; P:microtubule nucleation; ISS. DR InterPro; IPR007259; Spc97_Spc98. DR Pfam; PF04130; Spc97_Spc98; 1. KW Microtubule. SQ SEQUENCE 650 AA; 74979 MW; 515D8B36A80D08BE CRC64; MIHDLLLACR SHNPEQLGIK AFNETTVIDQ FIHPCEREIF MDIIKIIKVY QEVEQFTHSS GRKSDTHGEL PDSLHGYYLL NLAKGIEMAL EEYYAEIGRL EKYCLGNERN SLSYVYNALY AKFPLLVFMR NLITEIHVLN LRGCVLLHNL HQQCEHGDIQ LEKAIKIIMK PVKNAFFSSL AHWLLFGVID DVHSEFFIKF TPTDAVDGSS FSKSATCSLL SAEKNPEDYI WQYEVNMSQL PGFFSIVLAE KVLFVGQTVL VFKMGRNVKV KNKTDPLAAK LAELDSDDIY QLWSGRESEF FKMVVDLSNE DTINVFRLEK VIIDIKNYVS ARLSEIAVNE VDLERQMGLI KDFFLLGRGE FYLEFCSQMV GTMETYREER FKNVTRSFEL AATVTGITDD LDKFSLICQR STSEPDDTSD FNFLQGLSLK YEYEWPLNLL FSPTTIERYN NIFRFLLIIR TYQYEIQRVW AKQTWRAKSA KDVPPNNKII TLRNYLMFFL NNMQYYIQVD VLESQFGILM NVIKSRSDFE VIQRAHTVFL ANVLSHCFLL NESETQLNVT GSQNRNPIYG TLLKLFGICE KFAHMTQTKD PSDDLEDEVD QLNESFGVQI ASLIQLLVDV KSASCLGPLS QLLLRLDFNC WFSASHNTSA // ID GCSH_DROME STANDARD; PRT; 165 AA. AC Q9U616; Q9VP59; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glycine cleavage system H protein, mitochondrial precursor (Pumpless DE protein). GN PPL OR CG7758. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20025927; PubMed=10556053; RA Zinke I., Kirchner C., Chao L.C., Tetzlaff M.T., Pankratz M.J.; RT "Suppression of food intake and growth by amino acids in Drosophila: RT the role of pumpless, a fat body expressed gene with homology to RT vertebrate glycine cleavage system."; RL Development 126:5275-5284(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE GLYCINE CLEAVAGE SYSTEM CATALYZES THE DEGRADATION OF CC GLYCINE. THE H PROTEIN SHUTTLES THE METHYLAMINE GROUP OF GLYCINE CC FROM THE P PROTEIN TO THE T PROTEIN (BY SIMILARITY). CC -!- COFACTOR: THE H CHAIN CONTAINS A COVALENTLY-BOUND LIPOYL COFACTOR CC (BY SIMILARITY). CC -!- SUBUNIT: THE GLYCINE CLEAVAGE SYSTEM IS COMPOSED OF FOUR PROTEINS: CC P, T, L AND H (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GCVH FAMILY. CC -!- SIMILARITY: CONTAINS 1 LIPOYL-BINDING DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF203725; AAF13277.1; -. DR EMBL; AE003594; AAF51697.3; -. DR EMBL; AY075433; AAL68248.1; -. DR HSSP; P16048; 1HTP. DR FlyBase; FBgn0027945; ppl. DR InterPro; IPR002930; GCV_H. DR InterPro; IPR003016; Lipoyl_BS. DR Pfam; PF01597; GCV_H; 1. DR TIGRFAMs; TIGR00527; gcvH; 1. DR PROSITE; PS00189; LIPOYL; 1. KW Mitochondrion; Transit peptide; Lipoyl. FT TRANSIT 1 ? MITOCHONDRION (BY SIMILARITY). FT CHAIN ? 165 GLYCINE CLEAVAGE SYSTEM H PROTEIN. FT BINDING 98 98 LIPOYL (BY SIMILARITY). SQ SEQUENCE 165 AA; 18002 MW; CCEBD650304D359E CRC64; MVFITKFARI GLQAARQLSV TPLGAVQARA IHLTSLLAKE RRYTNKHEWV EVVSGSNAIV GISSYAQEAL GDVVFAQLPE PGTELKQDDE CGALESVKAA SEVYSPVSGK VIEKNAEVED TPALVNSSCY EKGWLFKVDL KNPKELEALM TEDQYKAFLS SSGDH // ID GDLO_DROME STANDARD; PRT; 39 AA. AC Q9U5V6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gonadal protein gdl-ORF39. GN GDL-ORF39. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo, Ovary, and Testis; RX MEDLINE=91115092; PubMed=1899227; RA Schulz R.A., Butler B.A.; RT "Overlapping genes of Drosophila melanogaster: organization of the RT z600-gonadal-Eip28/29 gene cluster."; RL Genes Dev. 3:232-243(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP CHARACTERIZATION. RX MEDLINE=90353183; PubMed=2117521; RA Schulz R.A., Miksch J.L., Xie X.L., Cornish J.A., Galewsky S.; RT "Expression of the Drosophila gonadal gene: alternative promoters RT control the germ-line expression of monocistronic and bicistronic RT gene transcripts."; RL Development 108:613-622(1990). CC -!- TISSUE SPECIFICITY: IN BUNDLES OF MATURING SPERM OF LARVAL, PUPAL CC AND ADULT MALES. CC -!- DEVELOPMENTAL STAGE: DURING SPERMATOGENESIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58286; CAB58350.1; -. DR EMBL; AE003530; AAO41249.1; -. DR PIR; S22880; S22880. DR FlyBase; FBgn0028377; gdl-ORF39. SQ SEQUENCE 39 AA; 4203 MW; B9F3A4D7C2755D3E CRC64; MWAAKLIVVT LLLLQFAALA LSCSCGEEAK LECGCTKHH // ID GDL_DROME STANDARD; PRT; 194 AA. AC P22468; Q9U5V5; Q9VUP2; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gonadal protein gdl. GN GDL OR CG7268. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo, Ovary, and Testis; RX MEDLINE=89232719; PubMed=2497054; RA Schulz R.A., Butler B.A.; RT "Overlapping genes of Drosophila melanogaster: organization of the RT z600-gonadal-Eip28/29 gene cluster."; RL Genes Dev. 3:232-242(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP CHARACTERIZATION. RX MEDLINE=90353183; PubMed=2117521; RA Schulz R.A., Miksch J.L., Xie X.L., Cornish J.A., Galewsky S.; RT "Expression of the Drosophila gonadal gene: alternative promoters RT control the germ-line expression of monocistronic and bicistronic RT gene transcripts."; RL Development 108:613-622(1990). CC -!- TISSUE SPECIFICITY: IN STAGE 6-14 EGG CHAMBER NURSE CELLS AND CC OOCYTES OF ADULT FEMALES AND SPERMATOCYTE CYSTS AND BUNDLES OF CC MATURING SPERM OF LARVAL, PUPAL AND ADULT MALES. CC -!- DEVELOPMENTAL STAGE: DURING OOGENESIS AND SPERMATOGENESIS. CC -!- SIMILARITY: BELONGS TO THE GONADAL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58286; CAB58351.1; -. DR EMBL; AE003530; AAF49633.1; -. DR PIR; S22881; S22881. DR FlyBase; FBgn0001099; gdl. FT CONFLICT 21 21 Y -> H (IN REF. 1). FT CONFLICT 162 163 GF -> V (IN REF. 1). FT CONFLICT 185 188 LSRL -> FTAV (IN REF. 1). SQ SEQUENCE 194 AA; 22653 MW; 48BAF262DEE891C0 CRC64; MADIPATSEG SANTSEAVVE YQQPTPEFLQ RKIYFLVDQL RTYHSELPEN LQTRISYDLL TELANCVLND GIFVIVKALM ELQHETERHL IKIRMQAENE YEIEVAEWRS KIKDPEELRH ILGLMKIKHT KKLHESDTKI IEILDQKVND QQSTLQKAGV PGFYVTENPK EIKIQMFLLD FILRLSRLKY EPGK // ID GD_DROME STANDARD; PRT; 528 AA. AC O62589; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine protease gd precursor (EC 3.4.21.-) (Gastrulation defective DE protein). GN GD OR CG1505. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Embryo; RX MEDLINE=98284015; PubMed=9618496; RA Konrad K.D., Goralski T.J., Mahowald A.P., Marsh J.L.; RT "The gastrulation defective gene of Drosophila melanogaster is a RT member of the serine protease superfamily."; RL Proc. Natl. Acad. Sci. U.S.A. 95:6819-6824(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PART OF A CASCADE THAT ACTIVATES THE SPZ LIGAND FOR THE CC TL RECEPTOR IN THE VENTRAL REGION OF THE EGG. GD ACTS EARLY TO CC ESTABLISH A LOCALIZED COMPLEX INVOLVING OTHER PUTATIVE PROTEASES CC (EA, SNK AND NDL) THAT LEAD TO LOCALIZED ACTIVATION OF SPZ. LOSS CC OF GD FUNCTION RESULTS IN A DORSALIZED EMBRYO. CC -!- DEVELOPMENTAL STAGE: OVARY AND EARLY EMBRYO. EXPRESSION BEGINS IN CC PREVITELLOGENIC STAGES AND IS SEEN IN GERM LINE-DERIVED NURSE CC CELLS OF THE GERMARIUM. EXPRESSION CONTINUES THROUGHOUT OOGENESIS CC WITH TRANSCRIPTS FROM THE NURSE CELLS ACCUMULATING IN THE OOCYTES. CC MOST ABUNDANT IN THE OVARIES, THE LEVEL OF PROTEIN DECREASES FROM CC THE MOMENT OF EGG LAYING AND IS ESSENTIALLY GONE BY 4HR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF056311; AAC13558.1; -. DR EMBL; AE003487; AAF48122.1; -. DR EMBL; U09808; AAC24235.1; -. DR HSSP; P00752; 1HIA. DR FlyBase; FBgn0000808; gd. DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS. DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP. DR GO; GO:0016485; P:protein processing; IGI. DR GO; GO:0008063; P:Tl signaling pathway; IGI. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR Pfam; PF00089; trypsin; 1. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; FALSE_NEG. DR PROSITE; PS00135; TRYPSIN_SER; FALSE_NEG. KW Hydrolase; Serine protease; Glycoprotein; Developmental protein; KW Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 528 SERINE PROTEASE GD. FT DOMAIN 243 528 SERINE PROTEASE. FT ACT_SITE 292 292 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 347 347 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 468 468 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 277 293 BY SIMILARITY. FT DISULFID 429 446 BY SIMILARITY. FT CARBOHYD 269 269 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 394 394 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 442 442 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 528 AA; 59084 MW; 31E3BEBBC5AE07A8 CRC64; MRLHLAAILI LCIEHVTKAV AQGMPISPCP KVFQYRFDGS EWFGLMAVRS PDGHQPLHIR VTLSMRGKPT TNYLGEIELL TRGKFTHNAP VLYKIRFPKH HFPPKLLLMS ANNHVICFGS GEHSIFMTQI QLEHIRKLSF IPDKKSSLLL DPEEEEVRKT DDKPPSTPHI QFKKKPFAQA PKEICGRIDR DLDFHLSQRT ESLHVAIGEP KSSDGITSPV FVDDDEDDVL EHQFVDESEA EAIESDSADS LPSITRGSWP WLAAIYVNNL TSLDFQCGGS LVSARVVISS AHCFKLFNKR YTSNEVLVFL GRHNLKNWNE EGSLAAPVDG IYIHPDFNSQ LSSYDADIAV IILKDEVRFN TFIRPACLWS GSSKTEYIVG ERGIVIGWSF DRTNRTRDQK LSSELPGKKS TDASAPKVVK APIVGNAECF RANAHFRSLS SNRTFCAGIQ AEERDTHQSG ASIYTGISGA GLFIRRNNRW MLRGTVSAAL PAVETPDAES SHKLCCKNQY IIYADVAKFL DWITAFVI // ID GELS_DROME STANDARD; PRT; 798 AA. AC Q07171; Q8MRF9; Q9VMZ1; Q9VMZ2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gelsolin precursor. GN GEL OR CG1106. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=93240523; PubMed=8386771; RA Heintzelman M.B., Frankel S.A., Artavanis-Tsakonas S., Mooseker M.S.; RT "Cloning of a secretory gelsolin from Drosophila melanogaster."; RL J. Mol. Biol. 230:709-716(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX MEDLINE=94230568; PubMed=8175883; RA Stella M.C., Schauerte H., Straub K.L., Leptin M.; RT "Identification of secreted and cytosolic gelsolin in Drosophila."; RL J. Cell Biol. 125:607-616(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; RA Misra S., Crosby M.A., Matthews B.B., Bayraktaroglu L., Campbell K., RA Hradecky P., Huang Y., Kaminker J.S., Prochnik S.E., Smith C.D., RA Tupy J.L., Bergman C.M., Berman B.P., Carlson J.W., Celniker S.E., RA Clamp M.E., Drysdale R.A., Emmert D., Frise E., de Grey A.D.N.J., RA Harris N.L., Kronmiller B., Marshall B., Millburn G.H., Richter J., RA Russo S., Searle S.M.J., Smith E., Shu S., Smutniak F., RA Whitfield E.J., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Mungall C.J., Lewis S.E.; RT "Annotation of Drosophila melanogaster genome."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 169-737 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CALCIUM-REGULATED, ACTIN-MODULATING PROTEIN THAT BINDS CC TO THE PLUS (OR BARBED) ENDS OF ACTIN MONOMERS OR FILAMENTS, CC PREVENTING MONOMER EXCHANGE (END-BLOCKING OR CAPPING). IT CAN CC PROMOTE THE ASSEMBLY OF MONOMERS INTO FILAMENTS (NUCLEATION) AS CC WELL AS SEVER FILAMENTS ALREADY FORMED. CC -!- SUBUNIT: BINDS TO ACTIN AND TO FIBRONECTIN. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (ISOFORM 2); SECRETED (ISOFORM CC 1). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=B, C, D, F, Secreted; CC IsoId=Q07171-1; Sequence=Displayed; CC Name=2; Synonyms=A, Cytoplasmic; CC IsoId=Q07171-2; Sequence=VSP_007010; CC Name=3; Synonyms=E; CC IsoId=Q07171-3; Sequence=VSP_007011; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: ISOFORMS 1 AND 2 ARE UBIQUITOUSLY EXPRESSED IN CC EARLY EMBRYO. ISOFORM 1 IS EXPRESSED IN THE FAT BODY, AND IS CC ABUNDANT IN HEMOLYMPH. ISOFORM 2 IS EXPRESSED IN PARTS OF THE GUT. CC -!- SIMILARITY: BELONGS TO THE VILLIN/GELSOLIN FAMILY. CC -!- SIMILARITY: CONTAINS 6 GELSOLIN-LIKE REPEATS. CC -!- CAUTION: LACKS ONE OF THE CYSTEINES TO MAKE THE DISULFIDE BRIDGE CC IN ISOFORM 1. IT IS REPLACED BY VAL-233. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08794; AAA28568.1; ALT_INIT. DR EMBL; X75629; CAA53294.1; -. DR EMBL; X75630; CAA53295.1; ALT_INIT. DR EMBL; AE003607; AAF52162.2; -. DR EMBL; AE003607; AAF52163.1; -. DR EMBL; AY119662; AAM50316.1; ALT_SEQ. DR HSSP; P02640; 2VIL. DR FlyBase; FBgn0010225; Gel. DR GO; GO:0005884; C:actin filament; IDA. DR GO; GO:0005829; C:cytosol; IEP. DR GO; GO:0005576; C:extracellular; IEP. DR GO; GO:0003789; F:actin filament severing activity; ISS. DR GO; GO:0030041; P:actin filament polymerization; ISS. DR InterPro; IPR007122; Gelsolin. DR InterPro; IPR007123; Gelsoln. DR Pfam; PF00626; Gelsolin; 5. DR PRINTS; PR00597; GELSOLIN. DR SMART; SM00262; GEL; 6. KW Cytoskeleton; Actin-binding; Repeat; Calcium; Alternative splicing; KW Signal; Phosphorylation. FT SIGNAL 1 28 POTENTIAL. FT CHAIN 29 798 GELSOLIN. FT DOMAIN 57 181 ACTIN-SEVERING (POTENTIAL). FT DOMAIN 451 792 ACTIN-BINDING, CA-SENSITIVE (POTENTIAL). FT REPEAT 78 131 GELSOLIN-LIKE 1. FT REPEAT 203 243 GELSOLIN-LIKE 2. FT REPEAT 322 365 GELSOLIN-LIKE 3. FT REPEAT 474 524 GELSOLIN-LIKE 4. FT REPEAT 583 625 GELSOLIN-LIKE 5. FT REPEAT 689 730 GELSOLIN-LIKE 6. FT MOD_RES 90 90 PHOSPHORYLATION (BY SRC) (PROBABLE). FT MOD_RES 612 612 PHOSPHORYLATION (BY SRC) (PROBABLE). FT MOD_RES 662 662 PHOSPHORYLATION (BY SRC) (PROBABLE). FT SITE 128 131 ACTIN-ACTIN INTERFILAMENT CONTACT FT POINT (BY SIMILARITY). FT SITE 167 174 POLYPHOSPHOINOSITIDE BINDING (BY FT SIMILARITY). FT SITE 193 201 POLYPHOSPHOINOSITIDE BINDING (BY FT SIMILARITY). FT VARSPLIC 1 1 M -> MGLPLDENSRDLIRSFHTLCLNLEEQLPLFELETNA FT TTKIKANTKDRVPKHIGHIRYLRLTDTYRNNKQSSSEPSVV FT DQRRGRLEM (in isoform 3). FT /FTId=VSP_007011. FT VARSPLIC 1 58 Missing (in isoform 2). FT /FTId=VSP_007010. FT CONFLICT 498 498 N -> S (IN REF. 2). FT CONFLICT 646 646 G -> S (IN REF. 2). SQ SEQUENCE 798 AA; 88374 MW; 79828666DC0965CC CRC64; MDASGAATMA VLSSLLVFLA LSSSLCSAGT LNARPAFPVQ SGEIQPSGQN SKQAARRVMH PSFANAGRTP GLEIWRIENF EPVIYPKTNY GKFYTGDSFI VLNTIENKKD KKLSWDVHFW LGLETSTDEA GAAAILTVQL DDLLNGGPVQ HREVQDHESQ LFLSYFKNGI RYEQGGVGTG FKHVETNAQG ETRLFQVKGK RNVRVRQVNL SVSSMNTGDC FILDAGSDIY VYVGSQAKRV EKLKAISAAN QIRDQDHNGR ARVQIVDDFS TDADKQHFFD VLGSGSADQV PDESTADEDS AFERTDAAAV SLYKVSDASG KLKVDIIGQK PLTQAMLDTR ECFILDTGSG IFVWVGKGAT QKEKTDAMAK AQEFLRTKKY PAWTQIHRIV EGSESAPFKQ YFDTWRDAGM SHSRLIRSAL GIGSDELLND DEIDSVVTQL KKSGGRAFGF MPDHGQNVIE TITQYVAKPG SDEIVVSTVP FDEKLPLLGF ASYVLTYNYE ANNGDTGSLT YVWHGVKASA AARKRAFEEG LVGSKDGLLV QTNQGHEPRH FYKIFKGKLL TSFTALPVTA QLFRIRGTVE SDVHASEVAA DSSSLASSDA FVLHSGKSHK IYIWNGLGAS AFEKQAAVDR FSDYWDDVEL EQVEEGAEPD EFWEELNGEG QYDRSLGDDG APLLESRLFH CHLSSGGFLK VEEVAQYEQE DLDSDDIMLL DAGDEIYLWV GYGVSEEENG KLLDTAKLYF NLEPTARSFD TVSIIRVPQG KEPRVFKRMF PNWDDNYWQN QPSYEDMKQL VIDANNEV // ID GIAN_DROME STANDARD; PRT; 448 AA. AC P39572; Q9V3N3; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Giant protein. GN GT OR EG:BACH7M4.5 OR CG7952. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=92249218; PubMed=1576969; RA Capovilla M., Eldon E.D., Pirrotta V.; RT "The giant gene of Drosophila encodes a b-ZIP DNA-binding protein RT that regulates the expression of other segmentation gap genes."; RL Development 114:99-112(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- FUNCTION: REPRESSES THE EXPRESSION OF BOTH THE KRUEPPEL AND KNIRPS CC SEGMENTATION GAP GENES. BINDS, IN VITRO, TO THE KRUEPPEL CC REGULATORY ELEMENTS CD1 AND CD2. IT IS REQUIRED IN THE EARLY CC EMBRYO FOR THE DEVELOPMENT OF PORTIONS OF THE HEAD AND ABDOMEN. CC -!- SUBUNIT: HOMODIMER OR HETERODIMER (PROBABLE). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: PHOSPHORYLATED AT MULTIPLE SITES. CC -!- SIMILARITY: BELONGS TO THE BZIP FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1, MET-3, MET-8 OR MET-23 CC IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61148; CAA43456.1; -. DR EMBL; AE003424; AAF45780.1; -. DR EMBL; AL133504; CAB63520.1; -. DR PIR; S17370; S17370. DR FlyBase; FBgn0001150; gt. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR InterPro; IPR004827; TF_bZIP. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW Transcription regulation; Repressor; DNA-binding; Nuclear protein; KW Phosphorylation; Developmental protein. FT DOMAIN 24 41 HIS-RICH. FT DOMAIN 74 91 POLY-GLN. FT DOMAIN 144 160 POLY-GLN. FT DOMAIN 198 210 POLY-ALA. FT DNA_BIND 390 408 BASIC MOTIF. FT DOMAIN 412 433 LEUCINE-ZIPPER. FT CONFLICT 234 234 L -> Q (IN REF. 1). SQ SEQUENCE 448 AA; 49169 MW; 98EB75D082129439 CRC64; MLMHEKLMAG QFFDLKTDRK PLMHHHQYQH HQQQPLHHLP HSQLPVQGSL GLPKMDLYTA YAYQQQLLGA ALSQQQQQQQ QQQQHQQLQQ QHTSSAEVLD LSRRCDSVET PRKTPSPYQT SYSYGSGSPS ASPTSNLLYA AQMQQQQHQQ QQQQQQQQQQ LASLYPAFYY SNIKQEQATP TAAPPKVTPT ANLLQTFAAA SAAAAAAAAA SSTNSPRPAS NASTMQIDVL ENPLSPAVEA TTPTTSSSGE AGKNTRPFKA FPRDPLVIAA NFAATDVLLD NPRVERYTEY RKRVLEQIRS SNGGSRTVTN PKMRRTNSRS GSVNEGSSSN NNSESEDRAA AEESSDCDSQ AGNFESKSAT SSSSNLANAT AANSGISSGS QVKDAAYYER RRKNNAAAKK SRDRRRIKED EIAIRAAYLE RQNIELLCQI DALKVQLAAF TSAKVTTA // ID GIL_DROME STANDARD; PRT; 444 AA. AC Q00805; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Giant-lens protein precursor (Argos protein). GN ARGOS OR AOS OR GIL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92331605; PubMed=1628618; RA Kretzschmar D., Brunner A., Wiersdorff V., Pflugfelder G.O., RA Heisenberg M., Schneuwly S.; RT "Giant lens, a gene involved in cell determination and axon guidance RT in the visual system of Drosophila melanogaster."; RL EMBO J. 11:2531-2539(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92298394; PubMed=1606617; RA Freeman M., Klambt C., Goodman C.S., Rubin G.M.; RT "The argos gene encodes a diffusible factor that regulates cell fate RT decisions in the Drosophila eye."; RL Cell 69:963-975(1992). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=93162369; PubMed=1286772; RA Okano H., Hayashi S., Tanimura T., Sawamoto K., Yoshikawa S., RA Watanabe J., Iwasaki M., Hirose S., Mikoshiba K., Montell C.; RT "Regulation of Drosophila neural development by a putative secreted RT protein."; RL Differentiation 52:1-11(1992). CC -!- FUNCTION: REGULATES CELL DETERMINATION AND AXON GUIDANCE IN THE CC DROSOPHILA EYE. ANTAGONIST FOR THE EGFR RECEPTOR (GURKEN). CC -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65161; CAA46279.1; -. DR EMBL; M91381; AAA28379.1; -. DR EMBL; S55367; AAB25390.1; -. DR PIR; S22699; S22699. DR FlyBase; FBgn0004569; argos. DR GO; GO:0048019; F:receptor antagonist activity; NAS. DR InterPro; IPR006209; EGF_like. DR PROSITE; PS00022; EGF_1; FALSE_NEG. DR PROSITE; PS01186; EGF_2; FALSE_NEG. KW Developmental protein; Vision; Signal; EGF-like domain. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 444 GIANT-LENS PROTEIN. FT DOMAIN 366 414 EGF-LIKE. FT DISULFID 370 384 BY SIMILARITY. FT DISULFID 378 405 BY SIMILARITY. FT DISULFID 407 413 BY SIMILARITY. FT CARBOHYD 333 333 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 444 AA; 50008 MW; 80E6727D48B0D19F CRC64; MPTTLMLLPC MLLLLLTAAA VAVGGTRLPL EVFEITPTTS TADKHKSLQY TVVYDAKDIS GAAAATGVAS STVKPATEQL TVVSISSTAA AEKDLAESRR HARQMLQKQQ QHRSIIGGKH GDRDVRILYQ VGDSEEDLPV CAPNAVCSKI DLYETPWIER QCRCPESNRM PNNVIIHHHS HSSGSVDSLK YRNYYEREKM MQHKRMLLGE FQDKKFESLH MKKLMQKLGA VYEDDLDHLD QSPDYNDALP YAEVQDNEFP RGSAHMRHSG HRGSKEPATT FIGGCPSSLG VEDGHTIADK TRHYKMCQPV HKLPVCKHFR DYTWTLTTAA ELNVTEQIVH CRCPRNSVTY LTKREPIGND SPGYRYLFAC SPLTRLRCQR KQPCKLFTVR KRQEFLDEVN INSLCQCPKG HRCPSHHTQS GVIAGESFLE DNIQTYSGYC MAND // ID GLAS_DROME STANDARD; PRT; 604 AA. AC P13360; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glass protein. GN GL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89365138; PubMed=2770860; RA Moses K., Ellis M.C., Rubin G.M.; RT "The glass gene encodes a zinc-finger protein required by Drosophila RT photoreceptor cells."; RL Nature 340:531-536(1989). CC -!- FUNCTION: GLASS IS PROBABLY A TRANSCRIPTION FACTOR REQUIRED FOR CC GENE EXPRESSION SPECIFIC TO PHOTORECEPTOR CELLS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 5 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15400; CAA33450.1; -. DR PIR; S05447; S05447. DR HSSP; P08046; 1A1I. DR TRANSFAC; T00329; -. DR FlyBase; FBgn0004618; gl. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007459; P:photoreceptor fate commitment (sensu Drosop...; IMP. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 5. DR ProDom; PD000003; Znf_C2H2; 2. DR SMART; SM00355; ZnF_C2H2; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. KW Transcription regulation; Zinc-finger; Metal-binding; DNA-binding; KW Repeat; Vision; Nuclear protein. FT ZN_FING 437 459 C2H2-TYPE 1. FT ZN_FING 465 487 C2H2-TYPE 2. FT ZN_FING 493 515 C2H2-TYPE 3. FT ZN_FING 521 543 C2H2-TYPE 4. FT ZN_FING 549 571 C2H2-TYPE 5. FT VARIANT 60 60 E -> Q. FT VARIANT 361 362 PM -> SL. FT VARIANT 377 377 S -> T. SQ SEQUENCE 604 AA; 62528 MW; 82B947C78366C071 CRC64; MGLLYKGSKL LNTILDSLED QEGGAMYISC DVSNGGPVEP ETGYVPNNPL FGLALDSPQE ECAASCVGCL SCQGSTALPI SSLTSSDFDC GGCFDPTIGV GVGIGGGHIQ ISTTPPASSG NGSSNNGAGG GSSGNHGYWS TDEMASTFPG LPPLDIDPLP SLFPFSPCGA SYNFAAGNPH QAASLSYTVH PHQMLISPNS HNHGQMHSQH QQHQHQQSQV QASHVGNSLL QSSGGNNIGS NGSAGGVANA ASCYYETSAG TAAPPPPPAA AMYPSMSVNV SMNMTMHHGY GAGDAGGVPM QCSQMNWTPP SNSTSAAAAA AAVNVLYPPL LSPGHYPASA TYSFTADFRA PAPTGLGALP PMTVGEKESP SPPANSSLAG YYPTGVGNQG YTPPHKSPTS YQAAALGLSL SAFEDEEDSN EDLDGDEGSS GGEMKPNLCR LCGKTYARPS TLKTHLRTHS GERPYRCPDC NKSFSQAANL TAHVRTHTGQ KPFRCPICDR RFSQSSSVTT HMRTHSGERP YRCSSCKKSF SDSSTLTKHL RIHSGEKPYQ CKLCLLRFSQ SGNLNRHMRV HGNNNSSNGS NGATGVGGES STGSGVGGGN SLLT // ID GLK1_DROME STANDARD; PRT; 991 AA. AC Q03445; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glutamate receptor I precursor (dGLUR-I) (Kainate-selective DE glutamate receptor). GN GLU-RI. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93066263; PubMed=1359540; RA Ultsch A., Schuster C.M., Laube B., Schloss P., Schmitt B., Betz H.; RT "Glutamate receptors of Drosophila melanogaster: cloning of a RT kainate-selective subunit expressed in the central nervous system."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10484-10488(1992). CC -!- FUNCTION: L-GLUTAMATE ACTS AS AN EXCITATORY NEUROTRANSMITTER AT CC MANY SYNAPSES IN THE CENTRAL NERVOUS SYSTEM. THE POSTSYNAPTIC CC ACTIONS OF GLU ARE MEDIATED BY A VARIETY OF RECEPTORS THAT ARE CC NAMED ACCORDING TO THEIR SELECTIVE AGONISTS (BY SIMILARITY). CC -!- SUBUNIT: FORMS HOMOOLIGOMERIC CHANNELS WHICH ARE ACTIVATED BY CC KAINATE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CENTRAL NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: NO EXPRESSION IS SEEN IN EARLY EMBRYOGENESIS, CC WHEREAS HIGH EXPRESSION OCCURS IN LATE EMBRYOS. DURING LARVAL CC DEVELOPMENT, EXPRESSION DECREASES TO UNDETECTABLE LEVELS IN LATE CC LARVAE, RESUMES AT THE EARLY PUPAL STAGE AND GRADUALLY INCREASES CC IN LATE PUPAE AND EARLY ADULT FLIES. HIGH LEVELS OF EXPRESSION CC COINCIDE WITH MAJOR STAGES OF NEUROGENESIS. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNEL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97192; AAA28575.1; -. DR HSSP; P19491; 1GR2. DR FlyBase; FBgn0004619; Glu-RI. DR GO; GO:0004971; F:alpha-amino-3-hydroxy-5-methyl-4-isoxazole ...; IDA. DR InterPro; IPR001828; ANF_receptor. DR InterPro; IPR001320; Ion_glu_receptor. DR InterPro; IPR001622; K+channel_pore. DR InterPro; IPR001311; SBP/glu_receptor. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00060; lig_chan; 1. DR SMART; SM00079; PBPe; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Transmembrane; KW Signal; Glycoprotein. FT SIGNAL 1 27 POTENTIAL. FT CHAIN 28 991 GLUTAMATE RECEPTOR I. FT DOMAIN 28 611 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 612 632 POTENTIAL. FT TRANSMEM 711 731 POTENTIAL. FT TRANSMEM 896 916 POTENTIAL. FT DOMAIN 28 32 POLY-GLN. FT DOMAIN 367 371 POLY-SER. FT CARBOHYD 67 67 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 195 195 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 208 208 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 281 281 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 376 376 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 385 385 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 426 426 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 437 437 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 477 477 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 991 AA; 111655 MW; F81D5D6D614D0D2C CRC64; MHSRLKFLAY LHFICASSIF WPEFSSAQQQ QQTVSLTEKI PLGAIFEQGT DDVQSAFKYA LLNHNLNVSS RRFELQAYVD VINTADAFKL SRLICNQFSR GVYSMLGAVS PDSFDTLHSY SNTFQMPFVT PWFPEKVLAP SSGLLDFAIS MRPDYHQAII DTIQYYGWQS IIYLYDSHDG LLRLQQIYQE LKPGNETFRV QMVKRIANVT MAIEFLHTLE DLGRFSKKRI VLDCPAEMAK EIIVQHVRDI KLGRRTYHYL LSGLVMDNHW PSDVVEFGAI NITGFRIVDS NRRAVRDFHD NRKRLEPSAK AKARTQGGPN SLPPISAQAA LMYDAVFVLV EAFNRILRKK PDQFRSNHLQ RRSHGGSSSS SATGTNESSA LLDCNTSKGW VTPWEQGEKI SRVLRKVEID GLSGEIRFDE DGRRINYTLH VVEMSVNSTL QQVAEWRDDA GLLPLHSHNY ASSSRSASAS TGDYDRNHTY IVSSLLEEPY LSLKQYTYGE SLVGNDRFEG YCKDLADMLA AQLGIKYEIR LVQDGNYGAE NQYAPGGWDG MVGELIRKEA DIAISAMTIT AERERVIDFS KPFMTLGISI MIKKPVKQTP GVFSFLNPLS QEIWISVILS YVGVSFVLYF VTRFPPYEWR IVRRPQADST AQQPPGIIGG ATLSEPQAHV PPVPPNEFTM LNSFWYSLAA FMQQGCDITP PSIAGRIAAA VWWFFTIILI SSYTANLAAF LTVERMVAPI KTPEDLAMQT DVNYGTLLHG STWEFFRRSQ IGLHNKMWEY MNANQHHSVH TYDEGIRRVR QSKGKYALLV ESPKNEYVNA RPPCDTMKVG RNIDTKGFGV ATPIGSPLRK RLNEAVLTLK ENGELLRIRN KWWFDKTECN LDQETSTPNE LSLSNVAGIY YILIGGLLLA VIVAIVEFFC RNKTPQLKSP GSNGSAGGVP GMLGSSTYQR DSLSDAIMHS QAKLAMQASS EYDERLVGVE LASNVRYQYS M // ID GLN1_DROME STANDARD; PRT; 399 AA. AC P20477; DT 01-FEB-1991 (Rel. 17, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Glutamine synthetase 1, mitochondrial precursor (EC 6.3.1.2) DE (Glutamate--ammonia ligase 1). GN GS1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90204539; PubMed=1969491; RA Caizzi R., Bozzetti M.P., Caggese C., Ritossa F.; RT "Homologous nuclear genes encode cytoplasmic and mitochondrial RT glutamine synthetase in Drosophila melanogaster."; RL J. Mol. Biol. 212:17-26(1990). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + NH(3) = ADP + PHOSPHATE + CC L-GLUTAMINE. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE GLUTAMINE SYNTHETASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52760; CAA36971.1; -. DR FlyBase; FBgn0001142; Gs1. DR GO; GO:0005739; C:mitochondrion; IDA. DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA. DR InterPro; IPR008147; Gln_synt_beta. DR InterPro; IPR008146; Gln_synt_C. DR Pfam; PF00120; gln-synt; 1. DR Pfam; PF03951; gln-synt_N; 1. DR ProDom; PD001057; Gln_synt_C; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. KW Ligase; Multigene family; Mitochondrion; Transit peptide. FT TRANSIT 1 27 MITOCHONDRION (POTENTIAL). FT CHAIN 28 399 GLUTAMINE SYNTHETASE 1. SQ SEQUENCE 399 AA; 44601 MW; 1A24628028268827 CRC64; MALRVAGLFL KKELVAPATQ QLRLLRTGNT TRSQFLANSP NTALDKSILQ RYRNLETPAN RVQATYLWID GTGENIRLKD RVLDKVPSSV EDLPDWQYDG SSTYQAHGEN SDTTLKPRAI YRDPFKPGKN DVIVLCDTYS ADGKPTASNK RAAFQAAIDL ISDQEPWFGI EQEYTLLRRG RTSFGWPENG FPAPQGPYYC GVGADRVYAR DLVEAHVVAC LYAGIDFAGT NAEVMPAQWE FQIGPAGIKA CDDLWVSRYI LQRIAEEYGV VVTFDPKPME GQWNGAGRHT NFSTKEMRAD GGIKAIEEPI EKLSKRHERH IKAYYPKEGK DNERRLVGRL ETSSIDKFSW GVANRAVSVR VPRGVATAGK GYLEDRRPSS NCDPYAVCNA IVQTCLLNE // ID GLN2_DROME STANDARD; PRT; 365 AA. AC P20478; DT 01-FEB-1991 (Rel. 17, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Glutamine synthetase 2, cytoplasmic (EC 6.3.1.2) (Glutamate--ammonia DE ligase 2). GN GS2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90204539; PubMed=1969491; RA Caizzi R., Bozzetti M.P., Caggese C., Ritossa F.; RT "Homologous nuclear genes encode cytoplasmic and mitochondrial RT glutamine synthetase in Drosophila melanogaster."; RL J. Mol. Biol. 212:17-26(1990). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + NH(3) = ADP + PHOSPHATE + CC L-GLUTAMINE. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GLUTAMINE SYNTHETASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52759; CAA36970.1; -. DR FlyBase; FBgn0001145; Gs2. DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA. DR InterPro; IPR008147; Gln_synt_beta. DR InterPro; IPR008146; Gln_synt_C. DR Pfam; PF00120; gln-synt; 1. DR Pfam; PF03951; gln-synt_N; 1. DR ProDom; PD001057; Gln_synt_C; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. KW Ligase; Multigene family. SQ SEQUENCE 365 AA; 40874 MW; 5DB3207314B1D43E CRC64; MSARILEDSP NARINKTILD RYLSLPLQEN IVQATYVWID GTGEDLRCKD RTLDFIPQSP KELPVWNYDG SSCYQAEGSN SDTYLYPVAI YKDPFRRGNN ILVMCDTYKF DGTPTDTNKR KTCLEVANKC AAEEPWFGIE QEYTSDFDGH HWAGQEWFPD PGPYYCGVGA NKSSPRHLDA HYAPCLYAGT QGVPTNAEVM PAQWEFQVGP CEGISIGHDL WMARFLLHRI SEEFGIVSTL DPKPMPGDWN GAGAHTNVST KAMREDGGIR DIEKAVAKLS KCHERHIRAY DPKQGQDNAR RLTGKHETSS INDFSAGVAN RGCSIRIPRG VNDDGKGYFE DRCPSSNCDP YSVVEAILRT ICLDE // ID GLT_DROME STANDARD; PRT; 1023 AA. AC P33438; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glutactin precursor. GN GLT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., PARTIAL SEQUENCE, AND SULFATION. RC STRAIN=Oregon-R; RX MEDLINE=90214632; PubMed=2108864; RA Olson P.F., Fessler L.I., Nelson R.E., Sterne R.E., Campbell A.G., RA Fessler J.H.; RT "Glutactin, a novel Drosophila basement membrane-related glycoprotein RT with sequence similarity to serine esterases."; RL EMBO J. 9:1219-1227(1990). CC -!- FUNCTION: NOT KNOWN. BINDS CALCIUM IONS. CC -!- SUBCELLULAR LOCATION: BASEMENT MEMBRANES. CC -!- PTM: EXTENSIVELY O-GLYCOSYLATED AND ALSO N-GLYCOSYLATED. CC -!- PTM: ABOUT FOUR TYROSINES ARE SULFATED. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE TYPE-B CC CARBOXYLESTERASE/LIPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53286; CAA37380.1; -. DR PIR; S12519; S12519. DR HSSP; P21836; 1MAA. DR FlyBase; FBgn0001114; Glt. DR GO; GO:0005604; C:basement membrane; IDA. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00135; COesterase; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. KW Glycoprotein; Sulfation; Calcium-binding; Signal. FT SIGNAL 1 17 FT CHAIN 18 1023 GLUTACTIN. FT DOMAIN 603 615 POLY-THR. FT DOMAIN 616 1023 GLU/GLN-RICH. FT MOD_RES 26 26 SULFATION (POTENTIAL). FT MOD_RES 29 29 SULFATION (POTENTIAL). FT MOD_RES 182 182 SULFATION (POTENTIAL). FT MOD_RES 559 559 SULFATION (POTENTIAL). FT MOD_RES 645 645 SULFATION (POTENTIAL). FT MOD_RES 727 727 SULFATION (POTENTIAL). FT MOD_RES 836 836 SULFATION (POTENTIAL). FT MOD_RES 862 862 SULFATION (POTENTIAL). FT MOD_RES 865 865 SULFATION (POTENTIAL). FT MOD_RES 868 868 SULFATION (POTENTIAL). FT MOD_RES 919 919 SULFATION (POTENTIAL). FT MOD_RES 925 925 SULFATION (POTENTIAL). FT MOD_RES 978 978 SULFATION (POTENTIAL). FT MOD_RES 981 981 SULFATION (POTENTIAL). FT MOD_RES 1003 1003 SULFATION (POTENTIAL). FT CARBOHYD 115 115 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 368 368 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 402 402 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 810 810 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 123 145 BY SIMILARITY. FT DISULFID 298 316 BY SIMILARITY. SQ SEQUENCE 1023 AA; 118412 MW; 3638CF79AB860E8C CRC64; MKPLLLVLAL CGAQVHAHSV GLRPDYNDYS DEDTRRDWLP EPLKPVPWQS ETRYAQPQEA VVQAPEVGQI LGISGHKTIA NRPVNAFLGI RYGTVGGGLA RFQAAQPIGY QGRVNATVQS PNCAQFPELD RLRLSESRGE NVDDCLTLDI YAPEGANQLP VLVFVHGEML FDGGSEEAQP DYVLEKDVLL VSINYRLAPF GFLSALTDEL PGNVALSDLQ LALEWLQRNV VHFGGNAGQV TLVGQAGGAT LAHALSLSGR AGNLFQQLIL QSGTALNPYL IDNQPLDTLS TFARLARCPP PSINPSAQGL KPLYDCLARL PTSQLVAAFE QLLLQNEHLG LTQLGGFKLV VGDPLGFLPS HPASLATNSS LALPMIIGAT KDASAFIVSR IYDQLARLQS RNVSDYIDVV LRHTAPPSEH RLWKQWALRE IFTPIQEQTA SLQTVAPGLL ELSNYILYRA PVINSISQSY RSVPAYLYTF DYRGEHHRFG HLSNPLPFGV DASLSDDSVY LFPYPPEASR LNPLDRSLSR ALVTMWVNFA TTGVPNPSSG VWPQATSEYG PFLRFTNNQQ SPLELDPHFG EGIYLPNYRV IYKPTTNFSP PITTTTTTTT TTTTTSRPYA YNPYANWQNR PSQQHPNWHP ADPEYVRAQE ARQQEFIRER EQRRREQQLR DQQRYPQQEP REQQDERIRQ QREQEERLRQ QREQEERLRQ QRELEERIRQ QQEREQYERE QQEREQRERE ELERQQRERE QQQPEQQPEY NPEPVNPWGY PVQEPQPDDN PEDGRLPYPS YEQYGPEGNE NLPETDANRN FSEEDREQQQ QEQLRREQQE QQEREYQLQL EREQQEREQQ ERGQQEPGPE EYPSYEEYSR ALQEKNAERD RIYAEEQERE RQQQETLLQE NQQHPEQSLP EEQPTHPNYD GDRSYAEEQE REQQRRDQVE QEREEQPDED QGEEYERLPD EEEAAEQDVL KVEDFPSYEA YLEAATKLRE EQEEQEKLEE ERYRAQQEEE DRIQAERERN SRN // ID GMDS_DROME STANDARD; PRT; 395 AA. AC Q9VMW9; Q8T3U5; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable GDP-mannose 4,6 dehydratase (EC 4.2.1.47) (GDP-D-mannose DE dehydratase) (Dm-gmd). GN GMD OR CG8890. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP HOMOLOGY. RX MEDLINE=21671316; PubMed=11698403; RA Roos C., Kolmer M., Mattila P., Renkonen R.; RT "Composition of Drosophila melanogaster proteome involved in RT fucosylated glycan metabolism."; RL J. Biol. Chem. 277:3168-3175(2002). CC -!- FUNCTION: CONVERSION OF GDP-D-MANNOSE TO GDP-4-KETO-6-D- CC DEOXYMANNOSE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: GDP-MANNOSE = GDP-4-DEHYDRO-6-DEOXY-D-MANNOSE CC + H(2)O. CC -!- COFACTOR: NADP(+) (BY SIMILARITY). CC -!- PATHWAY: CONVERSION OF GDP-MANNOSE TO GDP-FUCOSE; FIRST STEP. CC -!- SIMILARITY: BELONGS TO THE GDP-MANNOSE 4,6-DEHYDRATASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003608; AAF52189.2; -. DR EMBL; AY089519; AAL90257.1; -. DR HSSP; P32054; 1DB3. DR FlyBase; FBgn0031661; Gmd. DR InterPro; IPR006368; GDP_mann_dehyd. DR TIGRFAMs; TIGR01472; gmd; 1. KW Lyase; NADP. FT CONFLICT 333 333 N -> S (IN REF. 3). SQ SEQUENCE 395 AA; 44783 MW; 533E1B41E69ED36D CRC64; MLNTRLIAMS TSDGAPETKK QRPESSSNGS KDQNGTEAGA EGDSRDKVAL ITGITGQDGS YLAEFLLKKD YEVHGIIRRA STFNTTRIEH LYADPKAHKG GRMKLHYGDM TDSSSLVKII NMVKPTEIYN LAAQSHVKVS FDLSEYTAEV DAVGTLRILD AIRTCGMEKN VRFYQASTSE LYGKVVETPQ NEQTPFYPRS PYACAKMYGF WIVINYREAY NMYACNGILF NHESPRRGEN FVTRKITRSV AKIYHKQMEY FELGNLDSKR DWGHASDYVE AMWMMLQRES PSDYVIATGE THSVREFVEA AFKHIDREIT WKGKGVDEVG VENGTGIVRV RINPKYFRPT EVDLLQGDAS KANRELNWTP KVTFVELVSD MMKADIELMR KNPIA // ID GOLI_DROME STANDARD; PRT; 284 AA. AC Q06003; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Goliath protein (G1 protein). GN GOL OR G1 OR GL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=93216124; PubMed=8462875; RA Bouchard M.L., Cote S.; RT "The Drosophila melanogaster developmental gene g1 encodes a variant RT zinc-finger-motif protein."; RL Gene 125:205-209(1993). CC -!- FUNCTION: REGULATION OF GENE EXPRESSION DURING MESODERM FORMATION. CC PUTATIVE ROLE AS TRANSCRIPTION FACTOR. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: VISCERAL MESODERM AND PRIMORDIA OF SOMATIC CC MUSCULATURE. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97204; AAA28582.1; -. DR PIR; JC1495; JC1495. DR FlyBase; FBgn0004919; gol. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW Developmental protein; Zinc-finger; Transcription regulation; KW DNA-binding; Nuclear protein. FT ZN_FING 126 167 RING-TYPE. FT DOMAIN 208 259 GLN/PRO/SER-RICH. SQ SEQUENCE 284 AA; 31973 MW; ECEE2D5EEDBA1E2B CRC64; MQLEKMQIKG KTRNIAAVIT YQNIGQDLSL TLDKGYNVTI SIIEGRRGVR TISSLNRTSV LFVSISFIVD DILCWLIFYY IQRFRYMQAK DQQSRNLCSV TKKAIMKIPT KTGKFSDEKD LDSDCCAICI EAYKPTDTIR ILPCKHEFHK NCIDPWLIEH RTCPMCKLDV LKFYGYVVGD QIYQTPSPQH TAPIASIEEV PVIVVAVPHG PQPLQPLQAS NMSSFAPSHY FQSSRSPSSS VQQQLAPLTY QPHPQQAASE RGRRNSAPAT MPHAITASHQ VTDV // ID GPDA_DROME STANDARD; PRT; 363 AA. AC P13706; Q27590; Q27925; Q95077; Q9VML0; DT 01-JAN-1990 (Rel. 13, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic (EC 1.1.1.8) DE (GPD-C) (GPDH-C). GN GPDH OR CG9042. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; RX MEDLINE=89296935; PubMed=2500660; RA von Kalm L., Weaver J., Demarco J., Macintyre R.J., Sullivan D.T.; RT "Structural characterization of the alpha-glycerol-3-phosphate RT dehydrogenase-encoding gene of Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5020-5024(1989). RN [2] RP SEQUENCE FROM N.A., SEQUENCE OF 21-133; 139-141 AND 148-350, RP ALTERNATIVE SPLICING, AND ALLOZYMES FAST AND SLOW. RC STRAIN=Canton-S, Oregon-R, and Ogasawara; RX MEDLINE=90067829; PubMed=2511555; RA Bewley G.C., Cook J.L., Kusakabe S., Mukai T., Rigby D.L., RA Chambers G.K.; RT "Sequence, structure and evolution of the gene coding for RT sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster."; RL Nucleic Acids Res. 17:8553-8567(1989). RN [3] RP SEQUENCE FROM N.A., AND MUTATION ANALYSIS. RC STRAIN=Tasmania; RX MEDLINE=93165753; PubMed=8094564; RA Reed D.S., Gibson J.B.; RT "Defective P element insertions affect the expression of RT sn-glycerol-3-phosphate dehydrogenase alleles in natural populations RT of Drosophila melanogaster."; RL Proc. R. Soc. Lond., B, Biol. Sci. 251:39-45(1993). RN [4] RP SEQUENCE FROM N.A., AND ALLELE GPDH-ACB62. RC STRAIN=Cardwell; RX MEDLINE=95360026; PubMed=7633467; RA Symonds J.E., Gibson J.B., Wilks A.V., Wilanowski T.M.; RT "Molecular analysis of a Drosophila melanogaster sn-glycerol-3- RT phosphate dehydrogenase allozyme variant that has cold labile RT activity."; RL Insect Biochem. Mol. Biol. 25:789-798(1995). RN [5] RP SEQUENCE FROM N.A. (ISOFORM GPDH-2). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP SEQUENCE OF 2-363 FROM N.A., AND ALLELES GPDH-MB5 AND GPDH-ACYG22. RC STRAIN=Cygnet, and Mission beach; RX MEDLINE=95085592; PubMed=7993372; RA Reed D.S., Gibson J.B.; RT "Molecular heterogeneity of naturally occurring sn-glycerol-3- RT phosphate dehydrogenase low-activity variants in Drosophila RT melanogaster."; RL Biochem. Genet. 32:161-179(1994). RN [7] RP SEQUENCE OF 206-245 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=86304307; PubMed=3755720; RA Cook J.L., Shaffer J.B., Bewley G.C., MacIntyre R.J., Wright D.A.; RT "Isolation of a genomic clone for Drosophila sn-glycerol-3-phosphate RT dehydrogenase using synthetic oligonucleotides."; RL J. Biol. Chem. 261:11751-11755(1986). RN [8] RP SEQUENCE OF 298-350 FROM N.A., ALTERNATIVE SPLICING, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Canton-S; RX MEDLINE=88273210; PubMed=2839508; RA Cook J.L., Bewley G.C., Shaffer J.B.; RT "Drosophila sn-glycerol-3-phosphate dehydrogenase isozymes are RT generated by alternate pathways of RNA processing resulting in RT different carboxyl-terminal amino acid sequences."; RL J. Biol. Chem. 263:10858-10864(1988). CC -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) = GLYCERONE CC PHOSPHATE + NADH. CC -!- PATHWAY: THIS ENZYME IS ONE OF THE TWO ENZYMES CONSTITUTING THE CC ALPHA-GLYCEROPHOSPHATE CYCLE, IN WHICH THIS ENZYME OPERATES IN CC CONJUNCTION WITH A MITOCHONDRIAL ALPHA-GLYCEROPHOSPHATE OXIDASE. CC THE ALPHA-GLYCEROPHOSPHATE CYCLE IS ESSENTIAL FOR THE PRODUCTION CC OF ENERGY FOR FLIGHT IN INSECTS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=GPDH-4; CC IsoId=P13706-1; Sequence=Displayed; CC Name=GPDH-1; Synonyms=GPDH-411; CC IsoId=P13706-2; Sequence=VSP_001589; CC Name=GPDH-2; Synonyms=GPDH-37; CC IsoId=P13706-3; Sequence=VSP_001591; CC Name=GPDH-3; Synonyms=GPDH-1A; CC IsoId=P13706-4; Sequence=VSP_001590; CC -!- TISSUE SPECIFICITY: ISOFORM GPDH-1 IS PREDOMINANT IN THORAX AND CC ISOFORM GPDH-3 IN ABDOMEN. CC -!- DEVELOPMENTAL STAGE: ISOFORMS GPDH-2 AND GPDH-3 ARE EXPRESSED IN CC BOTH LARVAE AND ADULTS. ISOFORM GPDH-1 IS EXPRESSED ONLY IN CC ADULTS. CC -!- POLYMORPHISM: THERE ARE TWO COMMON ALLELES; FAST AND SLOW. THE CC SEQUENCE OF FAST IS SHOWN HERE. CC -!- SIMILARITY: BELONGS TO THE NAD-DEPENDENT GLYCEROL-3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04567; AAA28591.1; -. DR EMBL; J04567; AAA28592.1; -. DR EMBL; J04567; AAA28593.1; -. DR EMBL; X14179; CAA32379.1; -. DR EMBL; X14179; CAA32380.1; -. DR EMBL; X14179; CAA32381.1; -. DR EMBL; X67650; CAA47892.1; -. DR EMBL; X61223; -; NOT_ANNOTATED_CDS. DR EMBL; X61224; CAA43536.1; -. DR EMBL; AE003611; AAF52304.1; -. DR EMBL; X80204; CAA56497.1; -. DR EMBL; M13786; AAA28590.1; -. DR EMBL; J03927; AAA28553.1; -. DR EMBL; J03927; AAA28554.1; -. DR EMBL; J03927; AAA28555.1; -. DR PIR; S06758; S06758. DR PIR; S06759; S06759. DR PIR; S06760; S06760. DR PIR; S21963; S21963. DR FlyBase; FBgn0001128; Gpdh. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006168; NAD_Gly3P_dh. DR InterPro; IPR006109; NAD_Gly3P_dom. DR Pfam; PF01210; NAD_Gly3P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR ProDom; PD001278; NAD_Gly3P_dom; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. KW Oxidoreductase; NAD; Alternative splicing; Polymorphism. FT VARSPLIC 351 360 Missing (in isoform GPDH-1). FT /FTId=VSP_001589. FT VARSPLIC 351 363 Missing (in isoform GPDH-3). FT /FTId=VSP_001590. FT VARSPLIC 361 363 Missing (in isoform GPDH-2). FT /FTId=VSP_001591. FT VARIANT 14 14 N -> Y (IN ALLELE GPDH-ACYG22). FT VARIANT 266 266 C -> G (IN ALLELE GPDH-ACB62). FT VARIANT 273 273 R -> C (IN ALLELE GPDH-ACYG22). FT VARIANT 337 337 N -> K (in allele GPDH-AT198, allele FT GPDH-ACB62 and allele GPDH-S). FT CONFLICT 351 363 DTSIMPSPKLQNL -> GYVHHAVAKTCKICKSPKEAETFL FT TFLCTTENKCIFSAQRQLDESLDSIF (IN REF. 3). SQ SEQUENCE 363 AA; 39684 MW; 49FA09CE7FB6FDF4 CRC64; MADKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEELIDGKK LTEIINETHE NVKYLKGHKL PPNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR DLFQANHFRV VVVDDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPNDLI DCIRNHPEHM DTSIMPSPKL QNL // ID GPK1_DROME STANDARD; PRT; 700 AA. AC P32865; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE G protein-coupled receptor kinase 1 (EC 2.7.1.-). GN GPRK1 OR GPRK-1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92107891; PubMed=1662381; RA Cassill J.A., Whitney M., Joazeiro C.A., Becker A., Zuker C.S.; RT "Isolation of Drosophila genes encoding G protein-coupled receptor RT kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 88:11067-11070(1991). CC -!- FUNCTION: SPECIFICALLY PHOSPHORYLATES THE ACTIVATED FORMS OF G CC PROTEIN-COUPLED RECEPTORS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. GPRK CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RGS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M80493; AAA28588.1; -. DR HSSP; P05132; 1CTP. DR FlyBase; FBgn0004833; Gprk1. DR InterPro; IPR000239; GPCR_kinase. DR InterPro; IPR001849; PH. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000342; Regl_Gprotein. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00169; PH; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR00717; GPCRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00315; RGS; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50132; RGS; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding. FT DOMAIN 1 190 N-TERMINAL. FT DOMAIN 191 454 PROTEIN KINASE. FT DOMAIN 455 700 C-TERMINAL. FT DOMAIN 54 175 RGS. FT DOMAIN 557 657 PH. FT NP_BIND 197 205 ATP (BY SIMILARITY). FT BINDING 220 220 ATP (BY SIMILARITY). FT ACT_SITE 318 318 BY SIMILARITY. SQ SEQUENCE 700 AA; 80567 MW; 45FA3D3577EBA3DF CRC64; MADLEAVLAD VSYLMAMEKS KCTPAARASK KLNLPDPSVR SVMYKYLEKE GELNFHKNFN EVLGYLLFKD FCENDSEEPI QQLKFFEQIK LFEKTECYDE RKKMARDIYD NFIMEEMLSH TYEYSKHAVA SVQKYLLKNE VPVDLFEPYL EEIFTQLKGK PFKKFLESDK FTRFCQWKNL ELNIQLTMND FSVHRIIGRG GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGEMLALNER NMLQAVSTGI DCPFIVCMTY AFHTPDKLCF ILDLMNGGDL HYHLSQHGIF SEDEMKFYAA EVILGLEHMH KRCIVYRDLK PANILLDENG HIRISDLGLA CDFSKKKPHA SVGTHGYMAP EVLSKGTSYD SCADWFSFGC MLYKLLKGHS PFRQHKTKDK LEIDKMTLTM NVELPESFSL ELKNLLEMLL QRDVSKRLGC MGNGADEVKM HNFFCGIDWH QVYIQKYTPP LVPPRGEVNA ADAFDIGSFD EEDTKGIKLN DADQDLYKMF SLTISERWQQ EVSETVFDTV NTETDKLEQK RKLKQKQHFD ADEKESDCIL HGYIKKLGGS FASLWQTKYA KLYPNRLELH SESGNNKPEL IFMDQVEDIS SDFILHKNEN CIQIRINDGT RDGRIILTNS DEIGLKEWSS SLRSAHKISQ DLLGSMAKKA GKIYGSERDV NKSMYIFGGN CSTKTSNGSN // ID GPK2_DROME STANDARD; PRT; 714 AA. AC P32866; Q9V9X6; DT 01-OCT-1993 (Rel. 27, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE G protein-coupled receptor kinase 2 (EC 2.7.1.-). GN GPRK2 OR GPRK-2 OR CG17998. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97359973; PubMed=9217001; RA Schneider L.E., Spradling A.C.; RT "The Drosophila G-protein-coupled receptor kinase homologue Gprk2 is RT required for egg morphogenesis."; RL Development 124:2591-2602(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 201-714 FROM N.A. RX MEDLINE=92107891; PubMed=1662381; RA Cassill J.A., Whitney M., Joazeiro C.A., Becker A., Zuker C.S.; RT "Isolation of Drosophila genes encoding G protein-coupled receptor RT kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 88:11067-11070(1991). CC -!- FUNCTION: SPECIFICALLY PHOSPHORYLATES THE ACTIVATED FORMS OF G CC PROTEIN-COUPLED RECEPTORS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. GPRK CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 RGS DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF004674; AAB61467.1; -. DR EMBL; AE003778; AAF57152.1; -. DR EMBL; M80494; AAA28589.1; ALT_INIT. DR HSSP; Q63450; 1A06. DR FlyBase; FBgn0004834; Gprk2. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0004703; F:G-protein coupled receptor kinase activity; IMP. DR InterPro; IPR000239; GPCR_kinase. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000342; Regl_Gprotein. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR00717; GPCRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00315; RGS; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50132; RGS; 2. KW Transferase; Serine/threonine-protein kinase; ATP-binding; Repeat. FT DOMAIN 1 308 N-TERMINAL. FT DOMAIN 309 574 PROTEIN KINASE. FT DOMAIN 575 714 C-TERMINAL. FT DOMAIN 53 174 RGS 1. FT DOMAIN 177 294 RGS 2. FT NP_BIND 315 323 ATP (BY SIMILARITY). FT BINDING 338 338 ATP (BY SIMILARITY). FT ACT_SITE 435 435 BY SIMILARITY. FT DOMAIN 139 170 ASN-RICH. FT CONFLICT 70 70 F -> C (IN REF. 1). FT CONFLICT 206 206 S -> N (IN REF. 3). FT CONFLICT 232 232 H -> P (IN REF. 2). SQ SEQUENCE 714 AA; 80726 MW; D965166DE5D12BA2 CRC64; MELENIVANT VYLKAREGGS DSNKGKSKKW RKILQFPHIS QCINLKDKLD ISYGYVIDQQ PIGRELFRLF CENKRPVYFR YITFLDEVVK YEIEYISNRI FIGHDIGRRF LDVEAQLELR NGSGGDALDA ETQEELLLNS SNANPTETAE TEHCNNTTAN NCNNINNSNN SQHSSDINHK KLDTRNHNGD DATGNGSSHQ DDGDESVKCQ EGHDDAEKGG GGEGGGGGKC VHVGGYPDEL VLDVLNDDLI AQVRNKLNSG GKDIFAQCVN AVKAFLAGEP FREFESSMYF HRYLQWKWLE AQPITYKTFR MYRVLGKGGF GEVCACQVRA TGKMYACKKL EKKRIKKRKG ESMVLIEKQI LQKINSPFVV NLAYAYETKD ALCLVLTIMN GGDLKFHIYN MGGEPGFELE RARFYAAEVA CGLQHLHKQG IVYRDCKPEN ILLDDHGHVR ISDLGLAVEI PEGEMVRGRV GTVGYMAPEV IDNEKYAFSP DWFSFGCLLY EMIEGQAPFR MRKEKVKREE VDRRVKEDPE KYSSKFNDEA KSMCQQLLAK SIKQRLGCRN GRMGGQDVMA HPFFHSTQLN WRRLEAGMLE PPFVPDPHAV YAKDVLDIEQ FSTVKGVNID ESDTNFYTKF NTGSVSISWQ NEMMETECFR ELNVFGPEEC PTPDLQINAA PEPDKAGCFP FRRKKKQPAR TQPIPIPEHL LTTSHSVSST TVES // ID GPRS_DROME STANDARD; PRT; 1302 AA. AC O61366; Q9V7S2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine-enriched protein. GN GPRS OR CG18471/CG5967. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE OF 526-1302 FROM N.A. RC STRAIN=Canton-S; RA Da Lage J.-L.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003806; AAF57972.2; -. DR EMBL; AF022713; AAD09150.2; -. DR FlyBase; FBgn0024232; gprs. DR InterPro; IPR000210; BTB_POZ. DR SMART; SM00225; BTB; 1. DR PROSITE; PS50097; BTB; 1. FT DOMAIN 40 158 BTB. FT CONFLICT 691 691 E -> D (IN REF. 3). FT CONFLICT 744 744 Q -> H (IN REF. 3). FT CONFLICT 788 788 D -> V (IN REF. 3). FT CONFLICT 808 808 Q -> L (IN REF. 3). FT CONFLICT 894 894 D -> V (IN REF. 3). FT CONFLICT 1167 1167 R -> G (IN REF. 3). FT CONFLICT 1301 1301 S -> N (IN REF. 3). SQ SEQUENCE 1302 AA; 144768 MW; DA3603B725140215 CRC64; MPEALILPGM ADAEPDLSTF ENKTGLAEDM KFLASMPELC DVTFLVGDTR EPVCAVKAVL ASRSRVFAKM LYAAPSPQRK RETSTKENKL RLFLKRSSEP LLNLQNAAQQ RTGYTQQLAP IPEPSGQQHQ TLIIEEFEPD VFRQLIEYIH TGCVTLQPRT LLGVMNAADY YGLEELRRAC AGFVQCCINV DTVCALLASA ERYIQYKCTK TLVQKVLEFV DEHGTEVLNL GSFTLLPQHV VRLILAREEL RADEFTKFQA ALMWSKKYYD NNPNIDIKEI LGTFCEYIQF HKIPANVLMR EIHPLNLVPY AIIMNALAYQ ADPESIDPGK LSPNSSRQHH RHRHHHQSLP KIRKAKSQSF RTRRSPSERR SPNNAPNLTL NTSLTSGNGE KKRSPLTPKS PVMPVPESKS PGSSSQKTPT SLSRQGTLRA SNRRKNSGQL SISLGTQGRR SPVGLNDRSP QGRRSPLFPS SGLRSPNDPM TSPTVRSPTG EPRRSSPTFS VHTQERRSPL GAVAPTDFGC QFGVPGTRRS PTSTVHVQDM ATEPEEAGFV GLKRPSISLF TPIYFASEKR SPMGPIPPIT VSNPAETYKS AEREREAAEA AAREKEKEKE KEAAQPQEKK SVMREILAFV RKPSKHLSSR TNRFANAFTR AESGSSGGPL IRQSTFSASP AASSTAAKSA VQKQMSEVGF EPKISQKFTH YAKMSLRLRR STKRDDEEKE KQKQSSASGS KRPSADLSQT NADQQVGGSS DELPFELANV HFEKVGESYI KHERLRELQE PEVVKEEDTE KDAEAEVEVE QTDAAMAQFV EEVTNSLKVV ALNGEGGTAA VHHFTRRSES REPIEPRISE ERESDSNDLM IPDDMRAELV EILKAYPPEP VYVNLQALRR ETEDADLAIA QAEAAALAAA EPAKKPLQCP TIEFEPPSRR SSFDPPRSPF LEQLRSPGVD TETDLINLQR LDSGGDSFEL VESKWSKSSR GESSFDCPYS SRDTSFDVSI SRYQSTSYED QTSSFEIVDT DEKGQGRRAV DLRKSSIELV DAETFQRSGS SCGGRKSSLE THFDYTPTEG GGRSPSLPFP AMSKKQRTEN FRQLHVSQFS AFSRARSPLS QQTSSNYSSR DSYDSSGSYP HGYGYPPEPQ RSPYGDPSRK HFPLTVRQKG EEEREVRTFL CTDQRCASIF EPRPSSVLTQ QLSTGSMSTP SGYTNGTPRI PGAAPVGPVP LPHPSAPLSS CGFSSGSEFE PPSPRRAASA SPKHTFTFRI VMKKVDSSPE ALCPERHRSR IIDRYRRRDS RRKRIHDAGK SF // ID GRAU_DROME STANDARD; PRT; 570 AA. AC Q9U405; Q9W2N7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor grauzone. GN GRAU OR CG3282. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND MUTANTS QQ36 AND RP QE70. RX MEDLINE=20148536; PubMed=10683177; RA Chen B., Harms E., Chu T., Henrion G., Strickland S.; RT "Completion of meiosis in Drosophila oocytes requires transcriptional RT control by grauzone, a new zinc finger protein."; RL Development 127:1243-1251(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION, AND DNA-BINDING. RX MEDLINE=20384592; PubMed=10924478; RA Harms E., Chu T., Henrion G., Strickland S.; RT "The only function of Grauzone required for Drosophila oocyte meiosis RT is transcriptional activation of the cortex gene."; RL Genetics 155:1831-1839(2000). CC -!- FUNCTION: TRANSCRIPTION FACTOR INVOLVED IN FEMALE MEIOSIS. CC SPECIFICALLY REQUIRED TO BIND TO THE PROMOTER REGION OF THE CORTEX CC GENE AND ACTIVATE ITS EXPRESSION IN OVARIES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: PRESENT THROUGHOUT EMBRYOGENESIS, IN LARVAE, CC IN OVARIES AND OTHER TISSUES OF ADULT FEMALES, AND IN ADULT MALES. CC IN OVARIES, IT IS EXPRESSED IN BOTH FOLLICLE CELLS AND NURSE CC CELLS. EXPRESSED FROM STAGE 9 IN THE GERMARIUM. WEAKLY OR NOT CC EXPRESSED IN THE OOCYTE NUCLEUS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: CONTAINS 7 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF208016; AAF25356.1; -. DR EMBL; AE003452; AAF46653.2; -. DR EMBL; AY047537; AAK77269.1; -. DR GermOnline; 209995; -. DR FlyBase; FBgn0001133; grau. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003704; F:specific RNA polymerase II transcription fa...; IMP. DR GO; GO:0007143; P:female meiosis; IMP. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 8. DR SMART; SM00355; ZnF_C2H2; 8. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7. KW Meiosis; DNA-binding; Transcription regulation; Activator; KW Metal-binding; Zinc; Zinc-finger; Repeat. FT ZN_FING 296 319 C2H2-TYPE 1. FT ZN_FING 327 349 C2H2-TYPE 2. FT ZN_FING 387 409 C2H2-TYPE 3. FT ZN_FING 417 441 C2H2-TYPE 4. FT ZN_FING 448 471 C2H2-TYPE 5. FT ZN_FING 476 498 C2H2-TYPE 6. FT ZN_FING 504 527 C2H2-TYPE 7. FT DOMAIN 293 570 DNA-BINDING. FT DOMAIN 383 399 BIPARTITE NUCLEAR LOCALIZATION SIGNAL 1 FT (POTENTIAL). FT DOMAIN 523 539 BIPARTITE NUCLEAR LOCALIZATION SIGNAL 2 FT (POTENTIAL). FT DOMAIN 146 172 ASP/GLU-RICH (ACIDIC). FT MUTAGEN 298 298 C->Y: IN QQ36; DEFECTS IN FEMALE MEIOSIS. FT ABOLISHES DNA-BINDING ACTIVITY. FT MUTAGEN 493 493 E->K: IN QE70; DEFECTS IN FEMALE MEIOSIS. FT ABOLISHES DNA-BINDING ACTIVITY. SQ SEQUENCE 570 AA; 65967 MW; 33B550B964C1EA7C CRC64; MDICRLCLRG VSGAQMCLQI FDVDSGESKV AEVLRQHFWF EVLPNDEISK VICNVCWTQV SEFHQFYVSI QEAQVIYATT SKFKQDPEMV NTSWPEEVLM PADVLAVDND VGAQINVNPL DELDLSQPMS PEDSKVGIKT ERQSPDMELL FEDANNEQDE DYEDDEDDDT DDLIVTRSGR KRKRDVAKPA KTKRGTVSVG RKGKEKMVVK RGPPKRIFKM ERLPPFCKED EELIKRYIVM GCELCIFLAE DFDGIREHFK DKHPDERPYI KCCGRKLNKR CLIQEHARRH ENPEYIKCKD CGKVFANSSV LRAHWLVHHV PDEECDFQCE DCGKRFSRRN LLELHKGSHV PVNERKFICP QCPKHNAFAT EYHMQVHISM QHRKAANICH VCGKKIKDKA VFEKHVRLHF EESGPRIKCP RPDCESWLKD EDNLKQHLRR HNDEGKLFIC SECGKSCKNS RALIGHKRYS HSNVIYTCEQ CGKTFKKDIS LKEHMAQHTG EPLYKCPFCP RTFNSNANMH SHKKKMHPVE WDIWRKTKTG SSQKVLPSAQ VAQMFRDDAD VAAIANDYSG // ID GRIM_DROME STANDARD; PRT; 138 AA. AC Q24570; Q9VVP6; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cell death protein Grim. GN GRIM OR CG4345. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96312451; PubMed=8698237; RA Chen P., Nordstrom W., Gish B., Abrams J.M.; RT "Grim, a novel cell death gene in Drosophila."; RL Genes Dev. 10:1773-1782(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: FUNCTIONS INDEPENDENTLY OF RPR AND HID AS AN ACTIVATOR CC OF APOPTOSIS. CC -!- DEVELOPMENTAL STAGE: ITS EXPRESSION COINCIDED WITH THE ONSET OF CC PROGRAMMED CELL DEATH AT ALL STAGES OF EMBRYONIC DEVELOPMENT. CC -!- SIMILARITY: LIMITED AT THE N-TERMINAL, TO HID AND RPR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U61976; AAC47727.1; -. DR EMBL; AE003521; AAF49265.1; -. DR PDB; 1JD5; 05-DEC-01. DR FlyBase; FBgn0015946; grim. DR GO; GO:0005739; C:mitochondrion; IDA. DR GO; GO:0006917; P:induction of apoptosis; IGI. KW Apoptosis; 3D-structure. FT DOMAIN 40 52 POLY-GLN. FT CONFLICT 93 93 F -> L (IN REF. 1). SQ SEQUENCE 138 AA; 15486 MW; DE3FAC0487F0DB4E CRC64; MAIAYFIPDQ AQLLARSYQQ NGQQTAASPR TTATAAAPSQ QQQQSQQQQQ QQRHHHQQQR PQFRANISVP LGSQQGSMTM SEFGCWDLLA QIFCYALRIY SYSSSQRQPT VIQISFEISS GGQNNDEDDV TDATSKEN // ID GRK_DROME STANDARD; PRT; 295 AA. AC P42287; Q9VLL2; DT 01-NOV-1995 (Rel. 32, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein gurken precursor. GN GRK OR CG17610. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94006539; PubMed=7691414; RA Neuman-Silberberg F.S., Schuepbach T.; RT "The Drosophila dorsoventral patterning gene gurken produces a RT dorsally localized RNA and encodes a TGF alpha-like protein."; RL Cell 75:165-174(1993). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; RX MEDLINE=20253067; PubMed=10790337; RA Thio G.L., Ray R.P., Barcelo G., Schupbach T.; RT "Localization of gurken RNA in Drosophila oogenesis requires elements RT in the 5' and 3' regions of the transcript."; RL Dev. Biol. 221:435-446(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CRITICAL FOR DEFINING THE ANTERIOR-POSTERIOR AND DORSAL- CC VENTRAL AXES OF THE EGG. MAY SIGNAL DIRECTLY TO DORSAL FOLLICLE CC CELLS THROUGH THE RECEPTOR TORPEDO (TOP). DURING OOGENESIS THIS CC SIGNALING PATHWAY INSTRUCTS FOLLICLE CELLS TO FOLLOW A DORSAL CC PATHWAY OF DEVELOPMENT RATHER THAN THE DEFAULT VENTRAL PATHWAY. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED IN NURSE CELLS AND OOCYTE UP TO CC OOGENESIS STAGE 7. SPECIFICALLY ACCUMULATES IN DORSAL ANTERIOR CC CORNER OF THE OOCYTE DURING STAGES 9/10, AT LATER STAGES CC EXPRESSION IS SEEN AS AN ANTERIOR RING. CC -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L22531; AAA28598.1; ALT_INIT. DR EMBL; AF223394; AAF72000.1; ALT_INIT. DR EMBL; AE003621; AAF52675.3; -. DR EMBL; AY051814; AAK93238.1; -. DR PIR; A48844; A48844. DR FlyBase; FBgn0001137; grk. DR GO; GO:0005154; F:epidermal growth factor receptor binding; NAS. DR GO; GO:0007173; P:EGF receptor signaling pathway; NAS. DR GO; GO:0030381; P:eggshell pattern formation (sensu Insecta); IMP. DR GO; GO:0008070; P:maternal determination of dorsal/ventral ax...; IMP. DR GO; GO:0007314; P:oocyte anterior/posterior axis determination; NAS. DR InterPro; IPR006209; EGF_like. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; FALSE_NEG. DR PROSITE; PS50026; EGF_3; 1. KW Developmental protein; Transmembrane; Signal; EGF-like domain. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 295 PROTEIN GURKEN. FT DOMAIN 27 247 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 248 268 POTENTIAL. FT DOMAIN 269 295 CYTOPLASMIC (POTENTIAL). FT DOMAIN 179 224 EGF-LIKE. FT DISULFID 183 198 BY SIMILARITY. FT DISULFID 192 212 BY SIMILARITY. FT DISULFID 214 223 BY SIMILARITY. FT CARBOHYD 188 188 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 205 205 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 295 AA; 33280 MW; 80E993704DE3123B CRC64; MMQIPFTRIF KVIFVLSTIV AVTDCCSSRI LLLREHTLKI VQHQHSHMHE HAHELQQQIQ ETAVELLNRL ELQRKQLEAS AQEEADQLHP DTDPNPDSGG QLPNADDSIA ADPEQDGIIL GSSTDTWLAS ESSTPITDSE TVTTPETVTH TGEPPPDPSS SSTPDSTTPS PNDKETEIQM LPCSEAYNTS FCLNGGHCFQ HPMVNNTVFH SCLCVNDYDG ERCAYKSWNG DYIYSPPTAQ RKVRMAHIVF SFPVLLMLSS LYVLFAAVFM LRNVPDYRRK QQQLHLHKQR FFVRC // ID GROU_DROME STANDARD; PRT; 719 AA. AC P16371; Q9V3F7; DT 01-AUG-1990 (Rel. 15, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Groucho protein (Enhancer of split M9/10). GN GRO OR E(SPL)M9/M10 OR BCDNA:LD33829 OR CG8384. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89051868; PubMed=3142687; RA Hartley D., Preiss A., Artavanis-Tsakonas S.; RT "A deduced gene product from the Drosophila neurogenic locus, RT enhancer of split, shows homology to mammalian G-protein beta RT subunit."; RL Cell 55:785-795(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [4] RP BINDING TO HAIRY-RELATED PROTEINS. RX MEDLINE=95094252; PubMed=8001118; RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., RA Brent R., Ish-Horowicz D.; RT "Groucho is required for Drosophila neurogenesis, segmentation, and RT sex determination and interacts directly with hairy-related bHLH RT proteins."; RL Cell 79:805-815(1994). CC -!- FUNCTION: INVOLVED IN NEUROGENESIS; IN THE SEGREGATION OF THE CC NEUROECTODERM. DIRECTLY OR INDIRECTLY INTERACTS WITH NOTCH AND CC DELTA. CC -!- SUBUNIT: FORMS A COMPLEX WITH THE HAIRY/ENHANCER OF SPLIT/DEADPAN CC FAMILY OF BASIC HELIX-LOOP-HELIX PROTEINS IN ORDER TO REPRESS CC TRANSCRIPTION. ITS ACTIVITY IN REGULATING TRANSCRIPTION DEPENDS ON CC OTHER PROTEINS AS IT LACKS A DNA-BINDING MOTIF. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 6 WD REPEATS. CC -!- SIMILARITY: BELONGS TO THE WD-REPEAT GROUCHO/TLE FAMILY. CC PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M20571; AAA28512.1; -. DR EMBL; AE003754; AAF56556.1; -. DR EMBL; AF145695; AAD38670.1; -. DR PIR; A30047; A30047. DR TRANSFAC; T02451; -. DR FlyBase; FBgn0001139; gro. DR GO; GO:0003714; F:transcription co-repressor activity; IPI. DR GO; GO:0045810; P:negative regulation of frizzled signaling p...; NAS. DR GO; GO:0007399; P:neurogenesis; IMP. DR InterPro; IPR005617; TLE_N. DR InterPro; IPR001680; WD40. DR Pfam; PF03920; TLE_N; 1. DR Pfam; PF00400; WD40; 6. DR ProDom; PD000018; WD40; 1. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. KW Differentiation; Neurogenesis; Nuclear protein; Repeat; WD repeat; KW Phosphorylation; Wnt signaling pathway; Transcription regulation. FT DOMAIN 1 133 GLN-RICH. FT DOMAIN 134 194 GLY/PRO-RICH. FT DOMAIN 195 256 CCN DOMAIN. FT DOMAIN 216 219 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT BINDING 251 414 BASIC HELIX-LOOP-HELIX DOMAIN (BHLH). FT DOMAIN 257 398 SER/PRO-RICH. FT REPEAT 431 460 WD 1. FT REPEAT 477 507 WD 2. FT REPEAT 521 551 WD 3. FT REPEAT 563 593 WD 4. FT REPEAT 645 675 WD 5. FT REPEAT 686 716 WD 6. FT MOD_RES 231 231 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 247 247 PHOSPHORYLATION (BY CDC2) (POTENTIAL). FT CONFLICT 41 41 Q -> H (IN REF. 1). SQ SEQUENCE 719 AA; 78919 MW; D495291FD77026A5 CRC64; MYPSPVRHPA AGGPPPQGPI KFTIADTLER IKEEFNFLQA QYHSIKLECE KLSNEKTEMQ RHYVMYYEMS YGLNVEMHKQ TEIAKRLNTL INQLLPFLQA DHQQQVLQAV ERAKQVTMQE LNLIIGQQIH AQQVPGGPPQ PMGALNPFGA LGATMGLPHG PQGLLNKPPE HHRPDIKPTG LEGPAAAEER LRNSVSPADR EKYRTRSPLD IENDSKRRKD EKLQEDEGEK SDQDLVVDVA NEMESHSPRP NGEHVSMEVR DRESLNGERL EKPSSSGIKQ ERPPSRSGSS SSRSTPSLKT KDMEKPGTPG AKARTPTPNA AAPAPGVNPK QMMPQGPPPA GYPGAPYQRP ADPYQRPPSD PAYGRPPPMP YDPHAHVRTN GIPHPSALTG GKPAYSFHMN GEGSLQPVPF PPDALVGVGI PRHARQINTL SHGEVVCAVT ISNPTKYVYT GGKGCVKVWD ISQPGNKNPV SQLDCLQRDN YIRSVKLLPD GRTLIVGGEA SNLSIWDLAS PTPRIKAELT SAAPACYALA ISPDSKVCFS CCSDGNIAVW DLHNEILVRQ FQGHTDGASC IDISPDGSRL WTGGLDNTVR SWDLREGRQL QQHDFSSQIF SLGYCPTGDW LAVGMENSHV EVLHASKPDK YQLHLHESCV LSLRFAACGK WFVSTGKDNL LNAWRTPYGA SIFQSKETSS VLSCDISTDD KYIVTGSGDK KATVYEVIY // ID GRPE_DROME STANDARD; PRT; 213 AA. AC P48604; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE GrpE protein homolog, mitochondrial precursor. GN ROE1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Lee J.Y.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: COOPERATES WITH MITOCHONDRIAL HSP70 IN THE IMPORT CC OF PROTEINS FROM THE CYTOPLASM (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE GRPE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U34903; AAA79044.1; -. DR HSSP; P09372; 1DKG. DR FlyBase; FBgn0014877; Roe1. DR InterPro; IPR000740; GrpE. DR InterPro; IPR009012; GrpE_head. DR Pfam; PF01025; GrpE; 1. DR PRINTS; PR00773; GRPEPROTEIN. DR PROSITE; PS01071; GRPE; 1. KW Chaperone; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 213 GRPE PROTEIN HOMOLOG. SQ SEQUENCE 213 AA; 23960 MW; E88DAAF38094A588 CRC64; MSAKAALPLQ MFGRRLVHLR SSVTSQNMSA LRLYSTEKQP EEATEQKATE SSPELEKLTK ELAAAKEQNA ELMDKYKRSL ADSENMRNRL NKQISDAKIF GIQSFCKDLL EVADTLGHAT QAVPKDKLSG NTDLKNLYEG LTMTRASLLQ VFKRHGLESL DPINQKFDPN QHEALFQKED KTVEPNTVVE VTKLGYKLHE RCIRPALVGV SKC // ID GRP_DROME STANDARD; PRT; 512 AA. AC O61661; Q960N7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative serine/threonine kinase grp (EC 2.7.1.37) (Grapes DE protein). GN GRP OR CG17161/CG4711. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RX MEDLINE=97342864; PubMed=9197245; RA Fogarty P., Campbell S.D., Abu-Shumays R., de Saint Phalle B., RA Yu K.R., Uy G.L., Goldberg M.L., Sullivan W.; RT "The Drosophila grapes gene is related to checkpoint gene chk1/rad27 RT and is required for late syncytial division fidelity."; RL Curr. Biol. 7:418-426(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: HAS A ROLE IN A DEVELOPMENTALLY REGULATED DNA CC REPLICATION/DAMAGE CHECKPOINT OPERATING DURING THE LATE SYNCYTIAL CC DIVISIONS TO MONITOR THE STATE OF CHROMATIN. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- COFACTOR: MAGNESIUM (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC MATERNAL EXPRESSION DEGRADES AFTER NUCLEAR STAGE 13. ZYGOTIC CC EXPRESSION IS SEEN AT REDUCED LEVELS LATER IN EMBRYOGENESIS AND CC DURING LARVAL DEVELOPMENT. HIGHER EXPRESSION IS SEEN IN PUPAE, CC COINCIDENT WITH OVARIAN DIFFERENTIATION. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. NIM1 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF057041; AAC13566.1; -. DR EMBL; AE003652; AAF53552.2; -. DR EMBL; AY051961; AAK93385.1; -. DR HSSP; Q63450; 1A06. DR FlyBase; FBgn0011598; grp. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Chromatin regulator; Transferase; Kinase; KW Serine/threonine-protein kinase; ATP-binding; Cell cycle; DNA damage; KW Nuclear protein. FT DOMAIN 22 279 PROTEIN KINASE. FT NP_BIND 28 36 ATP (BY SIMILARITY). FT BINDING 51 51 ATP (BY SIMILARITY). FT ACT_SITE 143 143 BY SIMILARITY. FT CONFLICT 46 49 EAVA -> GGCG (IN REF. 1). FT CONFLICT 197 198 HA -> QP (IN REF. 1). FT CONFLICT 260 260 L -> LL (IN REF. 1). FT CONFLICT 339 339 S -> T (IN REF. 1). FT CONFLICT 352 359 SKEDGGDR -> IQGGWRRP (IN REF. 1). SQ SEQUENCE 512 AA; 57833 MW; 504CAB3C0B642EA0 CRC64; MAATLTEAGT GPAATREFVE GWTLAQTLGE GAYGEVKLLI NRQTGEAVAM KMVDLKKHPD AANSVRKEVC IQKMLQDKHI LRFFGKRSQG SVEYIFLEYA AGGELFDRIE PDVGMPQHEA QRYFTQLLSG LNYLHQRGIA HRDLKPENLL LDEHDNVKIS DFGMATMFRC KGKERLLDKR CGTLPYVAPE VLQKAYHAQP ADLWSCGVIL VTMLAGELPW DQPSTNCTEF TNWRDNDHWQ LQTPWSKLDT LAISLLRKLL ATSPGTRLTL EKTLDHKWCN MQFADNERSY DLVDSAAALE ICSPKAKRQR LQSSAHLSNG LDDSISRNYC SQPMPTMRSD DDFNVRLGSG RSKEDGGDRQ TLAQEARLSY SFSQPALLDD LLLATQMNQT QNASQNYFQR LVRRMTRFFV TTRWDDTIKR LVGTIERLGG YTCKFGDDGV VTVSTVDRNK LRLVFKAHII EMDGKILVDC RLSKGCGLEF KRRFIKIKNA LEDIVLKGPT TWPIAIATNS VP // ID GS1_DROME STANDARD; PRT; 231 AA. AC Q94529; O02536; Q9VR01; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GS1-like protein. GN GS1L OR CG15441. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=97208882; PubMed=9055824; RA Soehnge H., Huang X., Becker M., Conover D., Stern M.; RT "Cloning and sequencing of ribosomal protein L27a and a gene similar RT to human GS1 in Drosophila."; RL Gene 185:257-263(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE CBBY/CBBZ/GPH/YIEH FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-16 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U66356; AAC47470.1; -. DR EMBL; U66355; AAC47473.1; -. DR EMBL; U66356; AAC47471.1; ALT_INIT. DR EMBL; U66355; AAC47474.1; ALT_INIT. DR EMBL; AE003576; AAF51007.1; -. DR PIR; JC6201; JC6201. DR FlyBase; FBgn0019982; Gs1l. DR InterPro; IPR006402; HAD-SF-IA-v3. DR InterPro; IPR005834; Hydrolase. DR Pfam; PF00702; Hydrolase; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. FT VARIANT 176 177 FE -> VQ (IN REF. 1). SQ SEQUENCE 231 AA; 25784 MW; 3D4421C9665B69D4 CRC64; MANKVLRKVT HCVFDMDGLL LDTERLYTVA TEMILEPYGK TYPFEIKEQV MGLQTEPLAR FMVEHYELPM SWEEYARQQR ANTEILMRNA QLMPGAERLL RHLHANKVPF CLATSSGADM VELKTAQHRE LFSLFNHKVC GSSDKEVVNG KPAPDIFLVA AGRFGVPPKP SDCLVFEDSP NGVTAANSAG MQVVMVPDPR LSQEKTSHAT QVLASLADFK PEQFGLPAFT D // ID GS28_DROME STANDARD; PRT; 232 AA. AC Q9VE50; Q8SWZ4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable 28 kDa Golgi SNARE protein (Golgi SNAP receptor complex DE member 1). GN GOS28 OR CG7700. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN TRANSPORT FROM THE ER TO THE GOLGI APPARATUS CC AS WELL AS IN INTRA-GOLGI TRANSPORT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE IV MEMBRANE PROTEIN. GOLGI (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GOSR1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003723; AAF55579.1; -. DR EMBL; AY094935; AAM11288.1; -. DR FlyBase; FBgn0044871; Gos28. DR GO; GO:0000138; C:Golgi trans cisterna; ISS. DR GO; GO:0005484; F:SNAP receptor activity; ISS. DR GO; GO:0006888; P:ER to Golgi transport; ISS. DR GO; GO:0006891; P:intra-Golgi transport; ISS. DR InterPro; IPR007705; V-SNARE. DR Pfam; PF05008; V-SNARE; 1. KW Coiled coil; Transmembrane; Transport; Protein transport; Golgi stack. FT DOMAIN 1 211 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 212 232 ANCHOR FOR TYPE IV MEMBRANE PROTEIN FT (POTENTIAL). FT DOMAIN 6 23 COILED COIL (POTENTIAL). FT DOMAIN 52 80 COILED COIL (POTENTIAL). FT CONFLICT 34 34 S -> C (IN REF. 2). SQ SEQUENCE 232 AA; 25562 MW; 45C657EA56C33125 CRC64; MGGSSYDVLR KQARSLENEI DLKLVAFSKI GAGSGGGGSG GLGGVDTSPL LGEHVFDSLS EEIEQMLEKL SSLNESMSDL PASGAAAMHT LQRHREILQG YRQEFNKICA NHTMRIEREE LLRGSGLATS SGSPSISGLN RREMYLKESG HLNSASHLVN DQINIAIETR DHLHAQRQAF KRLQTRFNDI SNRFPLISSL IQRINIKKRR DSLILGAVIG FCVILLLLYA FN // ID GSBN_DROME STANDARD; PRT; 449 AA. AC P09083; Q9W0W5; DT 01-NOV-1988 (Rel. 09, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gooseberry neuro protein (Gooseberry proximal protein) (BSH4). GN GSB-N OR GSB-P OR GSBA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=88112802; PubMed=3123319; RA Baumgartner S., Bopp D., Burri M., Noll M.; RT "Structure of two genes at the gooseberry locus related to the paired RT gene and their spatial expression during Drosophila embryogenesis."; RL Genes Dev. 1:1247-1267(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 10-146 AND 162-241 FROM N.A. RX MEDLINE=87051758; PubMed=2877747; RA Bopp D., Burri M., Baumgartner S., Frigerio G., Noll M.; RT "Conservation of a large protein domain in the segmentation gene RT paired and in functionally related genes of Drosophila."; RL Cell 47:1033-1040(1986). CC -!- FUNCTION: EXPRESSED IN A SEGMENTALLY REPEATING PATTERN TO DEFINE CC THE POLARITY OF EMBRYONIC SEGMENTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN A SINGLE-SEGMENT REPEAT IN THE CC NEURECTODERM DURING GERM-BAND EXTENSION AND LATER IN SINGLE CC NEURONS DURING NEURONAL DIFFERENTIATION. CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 PAIRED BOX DOMAIN. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003466; AAF47314.1; -. DR EMBL; AY071593; AAL49215.1; -. DR EMBL; M14941; AAA28834.1; -. DR EMBL; M14943; AAA28835.1; -. DR PIR; A26332; A26332. DR HSSP; P06601; 1FJL. DR TRANSFAC; T01821; -. DR FlyBase; FBgn0001147; gsb-n. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0007367; P:segment polarity determination; IEP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR001523; Paired_box. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_BOX; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Segmentation polarity protein; Paired box; Transcription regulation. FT DOMAIN 20 141 PAIRED BOX. FT DNA_BIND 182 241 HOMEOBOX. FT DOMAIN 302 324 ALA/HIS-RICH. FT DOMAIN 402 428 ALA/HIS-RICH. FT CONFLICT 10 11 RP -> AA (IN REF. 4; AAA28835). FT CONFLICT 199 199 R -> G (IN REF. 1 AND 4; AAA28834). FT CONFLICT 314 314 A -> R (IN REF. 1). SQ SEQUENCE 449 AA; 48187 MW; 885C618306E900F8 CRC64; MDMSSANSLR PLFAGYPFQG QGRVNQLGGV FINGRPLPNH IRLKIVEMAA SGVRPCVISR QLRVSHGCVS KILNRYQETG SIRPGVIGGS KPKVTSPEIE TRIDELRKEN PSIFSWEIRE KLIKEGFADP PSTSSISRLL RGSDRGSEDG RKDYTINGIL GGRDSDISDT ESEPGIPLKR KQRRSRTTFT AEQLEALERA FSRTQYPDVY TREELAQTTA LTEARIQVWF SNRRARLRKH SGGSNSGLSP MNSGSSNVGV GVGLSGATAP LGYGPLGVGS MAGYSPAPGT TATGAGMNDG VHHAAHAPSS HHSAATAAAA AHHHTQMGGY DLVQSAAQHG FPGGFAQPGH FGSQNYYHQD YSKLTIDDFS KLTADSVSKI SPSLHLSDNY SKLEAPSNWS QAAYHAAANY NAHVAQHQLN DYAAAAAHGN PASAYSHPLP TQGQAKYWS // ID GSB_DROME STANDARD; PRT; 427 AA. AC P09082; Q9W0W4; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gooseberry protein (Gooseberry distal protein) (BSH9). GN GSB OR GSB-D OR GSBB OR CG3388. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=88112802; PubMed=3123319; RA Baumgartner S., Bopp D., Burri M., Noll M.; RT "Structure of two genes at the gooseberry locus related to the paired RT gene and their spatial expression during Drosophila embryogenesis."; RL Genes Dev. 1:1247-1267(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 9-148 AND 165-244 FROM N.A. RX MEDLINE=87051758; PubMed=2877747; RA Bopp D., Burri M., Baumgartner S., Frigerio G., Noll M.; RT "Conservation of a large protein domain in the segmentation gene RT paired and in functionally related genes of Drosophila."; RL Cell 47:1033-1040(1986). CC -!- FUNCTION: EXPRESSED IN SEGMENTALLY REPEATING PATTERN TO DEFINE THE CC POLARITY OF EMBRYONIC SEGMENTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE POSTERIOR VENTROLATERAL PART CC OF EACH SEGMENT THROUGHOUT THE EMBRYO, INCLUDING HEAD AND TAIL CC SEGMENTS. AT FIRST EXPRESSION IS RESTRICTED TO THE ECTODERM. CC DURING GERM-BAND EXTENSION, EXPRESSION IS INDUCED IN THE MESODERM. CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 PAIRED BOX DOMAIN. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M14944; AAA28836.1; -. DR EMBL; M14942; AAA28837.1; -. DR EMBL; AE003466; AAF47315.2; -. DR PIR; A43698; A43698. DR HSSP; P06601; 1PDN. DR TRANSFAC; T01820; -. DR FlyBase; FBgn0001148; gsb. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR001523; Paired_box. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_BOX; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Segmentation polarity protein; Paired box; Transcription regulation. FT DOMAIN 19 143 PAIRED BOX. FT DNA_BIND 185 244 HOMEOBOX. SQ SEQUENCE 427 AA; 45515 MW; 04E22DF9B29F832B CRC64; MAVSALNMTP YFGGYPFQGQ GRVNQLGGVF INGRPLPNHI RRQIVEMAAA GVRPCVISRQ LRVSHGCVSK ILNRFQETGS IRPGVIGGSK PRVATPDIES RIEELKQSQP GIFSWEIRAK LIEAGVCDKQ NAPSVSSISR LLRGSSGSGT SHSIDGILGG GAGSVGSEDE SEDDAEPSVQ LKRKQRRSRT TFSNDQIDAL ERIFARTQYP DVYTREELAQ STGLTEARVQ VWFSNRRARL RKQLNTQQVP SFAPTSTSFG ATPTTSAAPA PNMGMSLYSS QSWPSSGAYE NHAAYGGSVA SMSPASSTSG TSSAAHSPVQ TQAQQPGTGS EFMTSTYGVG SSNATYPSAA YSMPQTPATS AEQLRSQFAS AAASGSHHPS TWDSYNFAGS FFPPASAAGN HISGYHHQVD QKSSMMTTAP TYPYFGF // ID GSC_DROME STANDARD; PRT; 419 AA. AC P54366; Q9VPR9; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein goosecoid. GN GSC OR CG2851. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=96202483; PubMed=8625850; RA Goriely A., Stella M., Coffinier C., Kessler D., Mailhos C., RA Dessain S., Desplan C.; RT "A functional homologue of goosecoid in Drosophila."; RL Development 122:1641-1650(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96272167; PubMed=8670808; RA Hahn M., Jackle H.; RT "Drosophila goosecoid participates in neural development but not in RT body axis formation."; RL EMBO J. 15:3077-3084(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: APPEARS TO REGULATE REGIONAL DEVELOPMENT OF SPECIFIC CC TISSUES. CAN RESCUE AXIS POLARITY IN UV-RADIATED XENOPUS CC EMBRYOS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: IN EARLY EMBRYO DEVELOPMENT, EXPRESSION CC CONFINED TO TWO REGIONS; A HORSESHOE-LIKE PATTERN ACROSS THE CC DORSAL SIDE WHICH IS DESTINED TO FORM THE BRAIN HEMISPHERES AND A CC SECOND DOMAIN WHICH INVAGINATES INSIDE THE STOMODEUM AND WHICH, IS CC FATED TO FORM THE FOREGUT, RING GLAND AND STOMATOGASTRIC NERVOUS CC SYSTEM (SNS). CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. BICOID CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-5 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95420; CAA64699.1; -. DR EMBL; U52968; AAB17948.1; -. DR EMBL; AE003589; AAF51473.1; -. DR PIR; S70617; S70617. DR HSSP; P06601; 1FJL. DR TRANSFAC; T04041; -. DR FlyBase; FBgn0010323; Gsc. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Developmental protein; Nuclear protein; DNA-binding; Homeobox. FT DOMAIN 104 107 POLY-ALA. FT DOMAIN 164 169 POLY-SER. FT DOMAIN 195 199 POLY-ALA. FT DNA_BIND 286 345 HOMEOBOX. SQ SEQUENCE 419 AA; 44949 MW; 851A4C46AA861FB9 CRC64; MLAQMVETNS PPAGYTLKRS PSDLGEQQQP PRQISRSPGN TAAYHLTTAM LLNSQQCGYL GQRLQSVLQQ QHAQHQQSQS QTPSSDDGSQ SGVTILEEER RGGAAAASLF TIDSILGSRQ QGGGTAPSQG SHISSNGNQN GLTSNGISLG LKRSGAESPA SPNSNSSSSA AASPIRPQRV PAMLQHPGLH LGHLAAAAAS GFAASPSDFL VAYPNFYPNY MHAAAVAHVA AAQMQAHVSG AAAGLSGHGH HPHHPHGHPH HPHLGAHHHG QHHLSHLGHG PPPKRKRRHR TIFTEEQLEQ LEATFDKTHY PDVVLREQLA LKVDLKEERV EVWFKNRRAK WRKQKREEQE RLRKLQEEQC GSTTNGTTNS SSGTTSSTGN GSLTVKCPGS DHYSAQLVHI KSDANGYSDA DESSDLEVA // ID GSH1_DROME STANDARD; PRT; 717 AA. AC Q9W3K5; Q9NGQ3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-glutamylcysteine DE synthetase) (Gamma-ECS) (GCS). GN GCLC OR GCSH OR CG2259. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC TISSUE=Embryo; RX MEDLINE=20141256; PubMed=10675565; RA Saunders R.D.C., McLellan L.I.; RT "Molecular cloning of Drosophila gamma-glutamylcysteine synthetase by RT functional complementation of a yeast mutant."; RL FEBS Lett. 467:337-340(2000). RN [2] RP SEQUENCE FROM N.A. RA Orr W.C., Sohal R.S.; RT "Molecular organization of the gamma-glutamylcysteine synthetase gene RT in Drosophila melanogaster."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + L-CYSTEINE = ADP + CC PHOSPHATE + GAMMA-L-GLUTAMYL-L-CYSTEINE. CC -!- PATHWAY: GLUTATHIONE BIOSYNTHESIS; FIRST STEP. CC -!- SIMILARITY: BELONGS TO THE GLUTAMATE--CYSTEINE LIGASE FAMILY 3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF244351; AAF66980.1; -. DR EMBL; AE003442; AAF46321.1; -. DR EMBL; AY071586; AAL49208.1; -. DR FlyBase; FBgn0040319; Gclc. DR GO; GO:0004357; F:glutamate-cysteine ligase activity; NAS. DR GO; GO:0006750; P:glutathione biosynthesis; NAS. DR InterPro; IPR004308; GCS. DR InterPro; IPR008994; Nucleic_acid_OB. DR Pfam; PF03074; GCS; 1. KW Glutathione biosynthesis; Ligase. FT DOMAIN 491 507 ALA/GLN-RICH. FT DOMAIN 515 526 ASN/GLY-RICH. FT CONFLICT 35 35 H -> Y (IN REF. 2). FT CONFLICT 53 64 YIIVKFDDEQKV -> SLLSSSTMTAA (IN REF. 2). FT CONFLICT 502 502 A -> AQA (IN REF. 2). FT CONFLICT 530 530 S -> G (IN REF. 2). FT CONFLICT 550 550 S -> N (IN REF. 2). SQ SEQUENCE 717 AA; 80745 MW; E0C555163E370488 CRC64; MGLLSEGSPL SWEETKALAD HVREHGVNQF INLYHRLKDR QGDILKWGDE VEYIIVKFDD EQKVARVALR AQDLLAQLNE KELADPNGVK SLWRPEYGAY MIEGTPGKPF GGLMAHFNLV EANMRYRREE VTELLAKDEC VMSITNFPRL GAPNFTYPLA QPRPEDPLSS ARSLYFPDEA IFPGHPRFKT LTRNIRKRRG EKVSIKLKVF KDTKTKLPVE GAPPGEPDVV LLDAMGFGMG CCCLQLTFQA CNITEARRLY DQLAPLCPIM LALTAASPIY RGYLTESDCR WNVISSSVDC RTEEERGLAP LDQQKFRIAK SRYDSIDSYL SPEGAKYNDV PLTYDEKVYQ RLVEGGIDHL LAQHVAHLFI RDTVSLFSEK VHQNDNEDTD HFENIQSTNW QTMRFKPPPP NSSIGWRVEF RPCEAQISDF ENAAIVCFVV LLTRVILSYQ LNFLTPISKV DENMQTAQKR DACRKEKFWF RKSSKTTEQR AAKAQAQAQA QAKAQAQTNG KATLNGNGLA NGNGNGSENS DQEEQQPLTN GSAKMNGHGS GTTNGTNGSS NGSSNGTDSD HTDTDDEENE LFQLLSINEI FNGKPNVFPG LVPLIRSYLQ SMEVDTDTHC TIEQYLRFIQ KRAAGELITT ATWMREQVLS HPDYKQDSVV SERINYDLLK RIQGIQEGKQ VEPALLGQDY HSKTKTKDFI PPALQKQLAK NGCCEEK // ID GTR3_DROME STANDARD; PRT; 507 AA. AC P53403; Q9VER2; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glucose transporter type 3 (Glucose transporter-like protein) (Glut- DE 1). GN GLUT3 OR GLUT-L OR CG3853. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95396803; PubMed=7667301; RA Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D., RA Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.; RT "Complete sequence of the bithorax complex of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: FACILITATIVE GLUCOSE TRANSPORTER (POTENTIAL). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE SUGAR TRANSPORTER FAMILY. GLUCOSE CC TRANSPORTER SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U31961; AAA84407.1; -. DR EMBL; AE003714; AAF55358.1; -. DR FlyBase; FBgn0015230; Glut3. DR InterPro; IPR007114; MFS. DR InterPro; IPR005828; Sub_transporter. DR InterPro; IPR005829; Sug_transporter. DR InterPro; IPR003663; Sugar_transpt. DR Pfam; PF00083; sugar_tr; 1. DR PRINTS; PR00171; SUGRTRNSPORT. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; FALSE_NEG. DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1. KW Transmembrane; Sugar transport; Transport; Glycoprotein. FT DOMAIN 1 53 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 54 74 1 (POTENTIAL). FT DOMAIN 75 95 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 96 116 2 (POTENTIAL). FT DOMAIN 117 124 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 125 145 3 (POTENTIAL). FT DOMAIN 146 152 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 153 173 4 (POTENTIAL). FT DOMAIN 174 183 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 184 204 5 (POTENTIAL). FT DOMAIN 205 207 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 208 228 6 (POTENTIAL). FT DOMAIN 229 293 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 294 314 7 (POTENTIAL). FT DOMAIN 315 324 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 325 345 8 (POTENTIAL). FT DOMAIN 346 351 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 352 372 9 (POTENTIAL). FT DOMAIN 373 374 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 375 395 10 (POTENTIAL). FT DOMAIN 396 420 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 421 441 11 (POTENTIAL). FT DOMAIN 442 450 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 451 471 12 (POTENTIAL). FT DOMAIN 472 507 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 507 AA; 56705 MW; F111CF99CEC15D1E CRC64; MRKGGIQDAE PVEPPQSSRK SGTWFAKRPS EMPERHVERA PVRQKINNVG LYKATLYSNI GSFFFGIAVG WSGTAERSVM EQHSYSFQPT ELQWSGVCIL LTLGAALWCL PMGLMVRLLG CRRTILIQLL PNFLGWFLTV FARSVPMLYA GRFFLGMCGG AHCVVVPIYN AEISTTKKRG AMGVVFEGAC ICGVIYSFAM SLFLELRIIN FVNLGLLALG PLQILMPESP AYYVDHGNIP RAEDSLRFLR GQKYDTRREI DFLTRDPTES EREVRQGPLL GFKYKKVRRS LARSLAIALL QKLCGALIFI FYGLNMLDCL RIRREFGLIL CLGLILGFLA CFFLVDRLGR RPLLIFSSAG IVFVSIYLGL HFKVWMTMGL TVMSWIALFC IAIFVGCYTA GVGSLTWVLN AELLVRPMRP LGCSIVCAFN WLTAFFVICW FGSHGVKCQP YLFLLFAIIA SLILLFSLIY IPETKKLSSA KIQQRLGGLI NRPAVITFTS SSDSSNA // ID GTS1_DROME STANDARD; PRT; 249 AA. AC P41043; Q9V7Y4; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutathione S-transferase S1 (EC 2.5.1.18) (GST class-sigma 1) DE (Glutathione S-transferase 2). GN GSTS1 OR GST2 OR CG8938. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93074960; PubMed=1445191; RA Beall C., Fyrberg C., Song S., Fyrberg E.; RT "Isolation of a Drosophila gene encoding glutathione S-transferase."; RL Biochem. Genet. 30:515-527(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER CC OF EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES. MAY BE CC INVOLVED IN THE DETOXIFICATION OF METABOLITES PRODUCED DURING CC CELLULAR DIVISION AND MORPHOGENESIS. CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT WITH CC HIGHEST LEVELS BEING OBSERVED IN NONFEEDING STAGES, I.E. DURING CC EMBRYONIC AND PUPAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. SIGMA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95198; AAA28596.1; -. DR EMBL; AE003804; AAF57900.1; -. DR EMBL; AY118328; AAM48357.1; -. DR PIR; A48982; A48982. DR PDB; 1M0U; 11-FEB-03. DR FlyBase; FBgn0010226; GstS1. DR GO; GO:0004602; F:glutathione peroxidase activity; IDA. DR GO; GO:0004364; F:glutathione transferase activity; NAS. DR GO; GO:0006803; P:glutathione conjugation reaction; NAS. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; 3D-structure. FT CONFLICT 61 70 AEPLRYLFAY -> PSPCATCSD (IN REF. 1). FT CONFLICT 79 85 RVTRDEW -> AHPRRV (IN REF. 1). FT CONFLICT 224 224 L -> V (IN REF. 1). SQ SEQUENCE 249 AA; 27613 MW; 11AB417F550859BD CRC64; MADEAQAPPA EGAPPAEGEA PPPAEGAEGA VEGGEAAPPA EPAEPIKHSY TLFYFNVKAL AEPLRYLFAY GNQEYEDVRV TRDEWPALKP TMPMGQMPVL EVDGKRVHQS ISMARFLAKT VGLCGATPWE DLQIDIVVDT INDFRLKIAV VSYEPEDEIK EKKLVTLNAE VIPFYLEKLE QTVKDNDGHL ALGKLTWADV YFAGITDYMN YMVKRDLLEP YPALRGVVDA VNALEPIKAW IEKRPVTEV // ID GTT1_DROME STANDARD; PRT; 209 AA. AC P20432; Q9TX88; Q9VG99; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutathione S-transferase 1-1 (EC 2.5.1.18) (GST class-theta). GN GSTD1 OR GST1 OR GST OR CG10045. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-20. RC STRAIN=Oregon-R; RX MEDLINE=90115864; PubMed=2296588; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "Drosophila glutathione S-transferase 1-1 shares a region of sequence RT homology with the maize glutathione S-transferase III."; RL Proc. Natl. Acad. Sci. U.S.A. 87:31-35(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91337061; PubMed=1872839; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "The Drosophila glutathione S-transferase 1-1 is encoded by an RT intronless gene at 87B."; RL Biochem. Biophys. Res. Commun. 178:1205-1211(1991). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=93252851; PubMed=7683659; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "The glutathione S-transferase D genes. A divergently organized, RT intronless gene family in Drosophila melanogaster."; RL J. Biol. Chem. 268:9737-9746(1993). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER OF CC EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES. CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER. CC -!- MISCELLANEOUS: HAS A SPECIFIC ACTIVITY TOWARD CC 1-CHLORO-2,4-DINITROBENZENE COMPARABLE TO THAT FOR THE MAMMALIAN CC GLUTATHIONE S-TRANSFERASES BUT DID NOT HAVE AS BROAD A SUBSTRATE CC SPECIFICITY PATTERN. HAS NO GSH PEROXIDASE ACTIVITY. CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. THETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14233; CAA32449.1; -. DR EMBL; M97702; -; NOT_ANNOTATED_CDS. DR EMBL; AE003695; AAF54786.1; -. DR PIR; A34798; XUFF11. DR FlyBase; FBgn0001149; GstD1. DR GO; GO:0004364; F:glutathione transferase activity; IDA. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. SQ SEQUENCE 209 AA; 23866 MW; 4AD8E237CCF804F2 CRC64; MVDFYYLPGS SPCRSVIMTA KAVGVELNKK LLNLQAGEHL KPEFLKINPQ HTIPTLVDNG FALWESRAIQ VYLVEKYGKT DSLYPKCPKK RAVINQRLYF DMGTLYQSFA NYYYPQVFAK APADPEAFKK IEAAFEFLNT FLEGQDYAAG DSLTVADIAL VATVSTFEVA KFEISKYANV NRWYENAKKV TPGWEENWAG CLEFKKYFE // ID GTT2_DROME STANDARD; PRT; 215 AA. AC Q9VG98; Q9TX91; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutathione S-transferase D2 (EC 2.5.1.18) (DmGST21). GN GSTD2 OR GSTD21 OR CG4181. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93252851; PubMed=7683659; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "The glutathione S-transferase D genes. A divergently organized, RT intronless gene family in Drosophila melanogaster."; RL J. Biol. Chem. 268:9737-9746(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER OF CC EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. THETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97702; -; NOT_ANNOTATED_CDS. DR EMBL; AE003695; AAF54787.1; -. DR PIR; D46681; D46681. DR FlyBase; FBgn0010038; GstD2. DR GO; GO:0004364; F:glutathione transferase activity; IDA. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. SQ SEQUENCE 215 AA; 24535 MW; 221A9961BBF0E5B5 CRC64; MDFYYMPGGG GCRTVIMVAK ALGLELNKKL LNTMEGEQLK PEFVKLNPQH TIPTLVDNGF SIWESRAIAV YLVEKYGKDD YLLPNDPKKR AVINQRLYFD MGTLYESFAK YYYPLFRTGK PGSDEDLKRI ETAFGFLDTF LEGQEYVAGD QLTVADIAIL STVSTFEVSE FDFSKYSNVS RWYDNAKKVT PGWDENWEGL MAMKALFDAR KLAAK // ID GTT3_DROME STANDARD; PRT; 199 AA. AC Q9VG97; Q8MT68; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutathione S-transferase D3 (EC 2.5.1.18) (DmGST22). GN GSTD3 OR GSTD22 OR BCDNA:LP11313 OR CG4381. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93252851; PubMed=7683659; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "The glutathione S-transferase D genes. A divergently organized, RT intronless gene family in Drosophila melanogaster."; RL J. Biol. Chem. 268:9737-9746(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 125-199 FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER OF CC EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. THETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97702; -; NOT_ANNOTATED_CDS. DR EMBL; AE003695; AAO41561.1; -. DR EMBL; AY118350; AAM48379.1; -. DR PIR; A46681; A46681. DR FlyBase; FBgn0010039; GstD3. DR GO; GO:0004364; F:glutathione transferase activity; NAS. DR GO; GO:0006803; P:glutathione conjugation reaction; NAS. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. SQ SEQUENCE 199 AA; 22907 MW; 0B4D0EF24ADBBC60 CRC64; MVGKALGLEF NKKIINTLKG EQMNPDFIKI NPQHSIPTLV DNGFTIWESR AILVYLVEKY GKDDALYPKD IQKQAVINQR LYFDMALMYP TLANYYYKAF TTGQFGSEED YKKVQETFDF LNTFLEGQDY VAGDQYTVAD IAILANVSNF DVVGFDISKY PNVARWYDHV KKITPGWEEN WAGALDVKKR IEEKQNAAK // ID GTT4_DROME STANDARD; PRT; 215 AA. AC Q9VG96; Q9TX90; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutathione S-transferase D4 (EC 2.5.1.18) (DmGST23). GN GSTD4 OR GSTD23 OR CG11512. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93252851; PubMed=7683659; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "The glutathione S-transferase D genes. A divergently organized, RT intronless gene family in Drosophila melanogaster."; RL J. Biol. Chem. 268:9737-9746(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER OF CC EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. THETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97702; -; NOT_ANNOTATED_CDS. DR EMBL; AE003695; AAF54789.1; -. DR PIR; E46681; E46681. DR FlyBase; FBgn0010040; GstD4. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. FT CONFLICT 142 142 E -> V (IN REF. 1). SQ SEQUENCE 215 AA; 24736 MW; 9556E0A1A54BBE1F CRC64; MDFYYSPRSS GSRTIIMVAK ALGLELNKKQ LRITEGEHLK PEFLKLNPQH TIPTLVDNGF AIWESRAIAV YLVEKYGKDD SLFPNDPQKR ALINQRLYFD MGTLHDSFMK YYYPFIRTGQ LGNAENYKKV EAAFEFLDIF LEGQDYVAGS QLTVADIAIL SSVSTFEVVE FDISKYPNVA RWYANAKKIT PGWDENWKGL LQMKTMYEAQ KASLK // ID GTT5_DROME STANDARD; PRT; 216 AA. AC Q9VG95; Q9TX92; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutathione S-transferase D5 (EC 2.5.1.18) (DmGST24). GN GSTD5 OR GSTD24 OR CG12242. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93252851; PubMed=7683659; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "The glutathione S-transferase D genes. A divergently organized, RT intronless gene family in Drosophila melanogaster."; RL J. Biol. Chem. 268:9737-9746(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER OF CC EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. THETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97702; -; NOT_ANNOTATED_CDS. DR EMBL; AE003695; AAF54790.1; -. DR PIR; C46681; C46681. DR FlyBase; FBgn0010041; GstD5. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. FT CONFLICT 44 49 MISSING (IN REF. 2). SQ SEQUENCE 216 AA; 24713 MW; 9136816534D39A18 CRC64; MDFYYSPRGS GCRTVIMVAK ALGVKLNMKL LNTLEKDQLK PEFVKLNPQH TIPTLVDNGF SIWESRAIAV YLVEKYGKDD TLFPKDPKKQ ALVNQRLYFD MGTLYDSFAK YYYPLFHTGK PGSDEDFKKI ESSFEYLNIF LEGQNYVAGD HLTVADIAIL STVSTFEIFD FDLNKYPNVA RWYANAKKVT PGWEENWKGA VELKGVFDAR QAAAKQ // ID GTT6_DROME STANDARD; PRT; 215 AA. AC Q9VG94; Q9TX93; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutathione S-transferase D6 (EC 2.5.1.18) (DmGST25). GN GSTD6 OR GSTD25 OR CG4423. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93252851; PubMed=7683659; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "The glutathione S-transferase D genes. A divergently organized, RT intronless gene family in Drosophila melanogaster."; RL J. Biol. Chem. 268:9737-9746(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER OF CC EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. THETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97702; -; NOT_ANNOTATED_CDS. DR EMBL; AE003695; AAF54791.1; -. DR FlyBase; FBgn0010042; GstD6. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. SQ SEQUENCE 215 AA; 24485 MW; 6195738AD6E20D4D CRC64; MDLYNMSGSP STRAVMMTAK AVGVEFNSIQ VNTFVGEQLE PWFVKINPQH TIPTLVDNLF VIWETRAIVV YLVEQYGKDD SLYPKDPQKQ ALINQRLYFD MGTLYDGIAK YFFPLLRTGK PGTQENLEKL NAAFDLLNNF LDGQDYVAGN QLSVADIVIL ATVSTTEMVD FDLKKFPNVD RWYKNAQKVT PGWDENLARI QSAKKFLAEN LIEKL // ID GTT7_DROME STANDARD; PRT; 224 AA. AC Q9VG93; Q9TX87; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutathione S-transferase D7 (EC 2.5.1.18) (DmGST26). GN GSTD7 OR GSTD26 OR CG4371. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP PRELIMINARY SEQUENCE FROM N.A. RX MEDLINE=93252851; PubMed=7683659; RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.; RT "The glutathione S-transferase D genes. A divergently organized, RT intronless gene family in Drosophila melanogaster."; RL J. Biol. Chem. 268:9737-9746(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER OF CC EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. THETA FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC FRAMESHIFTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97702; -; NOT_ANNOTATED_CDS. DR EMBL; AE003695; AAF54792.1; -. DR HSSP; P24472; 1GUK. DR FlyBase; FBgn0010043; GstD7. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. SQ SEQUENCE 224 AA; 25419 MW; D4478B93C59E565A CRC64; MPNLDLYNFP MAPASRAIQM VAKALGLELN SKLINTMEGD QLKPEFVRIN PQHTIPTLVD NGFVIWESRA IAVYLVEKYG KPDSPLYPND PQKRALINQR LYFDMGTLYD ALTKYFFLIF RTGKFGDQEA LDKVNSAFGF LNTFLEGQDF VAGSQLTVAD IVILATVSTV EWFSFDLSKF PNVERWLKNA PKVTPGWEQN LESLQQGKKF LQDLQAAKEK EVKA // ID H15_DROME STANDARD; PRT; 544 AA. AC Q94890; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE T-box protein H15. GN H15. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye; RA Brook W.J., Cohen S.M.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 T-BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98766; CAA67304.1; -. DR HSSP; P24781; 1XBR. DR TRANSFAC; T04412; -. DR FlyBase; FBgn0016660; H15. DR InterPro; IPR008967; P53-like. DR InterPro; IPR001699; TF_T-box. DR Pfam; PF00907; T-box; 1. DR PRINTS; PR00937; TBOX. DR SMART; SM00425; TBOX; 1. DR PROSITE; PS01283; TBOX_1; 1. DR PROSITE; PS01264; TBOX_2; FALSE_NEG. DR PROSITE; PS50252; TBOX_3; 1. KW DNA-binding; Nuclear protein. FT DOMAIN 56 59 POLY-ALA. FT DOMAIN 83 91 POLY-GLN. FT DOMAIN 118 125 POLY-PRO. FT DNA_BIND 170 356 T-BOX. FT DOMAIN 242 245 POLY-PRO. FT DOMAIN 436 443 POLY-PRO. SQ SEQUENCE 544 AA; 60010 MW; 4D4EDB8E78244132 CRC64; MRTMMLTLMW STAVTRKCRR QLRQRRGGNN SSGCSGSIAG AATSASGIAC CTATTAAAAT TKAADTSPRN NWQATTPTSQ SSQQQHQQQQ QLRQQQHQQQ IKQPARAFAA AVGAAATPSP PPPPPSQSPE ELERLSPEES PAQQPTPKIV GSCNCDDLTP VQCHLETKEL WDKFHELGTE MIITKSGRRM FPTVRVSFSG PLRQIQPADR YAVLLDVVPL DSRRYRYAYH RSSWLVAGKA DPPPPSRIYA HPDCPLSPEA LRKQVVSFEK VKLTNNEMDK SGQVVLNSMH RYQPRIHLVR LSHGQSIPGS PKELQDMDHK TFVFPETVFT AVTAYQNQLI TKLKIDSNPF AKGFRDSSRL SDFDRDPMDA FFFDQHMRTA PLRFFPDPLM SQLTPQEADA ASMALLEKAR QHLQMFGRSP YTEMLLPHLY QRSAAPPPPP PAPHLSAFQL GMWQQQWPQL TAGFLASANQ QAALALAAAG ANRTPPPSMA VAPPAPATPT SSCGSASPDL RARPQLNHYP QRFSPYQVPQ HQASPPASNR AESP // ID H1_DROME STANDARD; PRT; 256 AA. AC P02255; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone H1. GN HIS1 AND HIS1:CG31617. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86286566; PubMed=3090518; RA Murphy T.J., Blumenfeld M.; RT "Nucleotide sequence of a Drosophila melanogaster H1 histone gene."; RL Nucleic Acids Res. 14:5563-5563(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=AK-194; RX MEDLINE=89098383; PubMed=2536150; RA Matsuo Y., Yamazaki T.; RT "tRNA derived insertion element in histone gene repeating unit of RT Drosophila melanogaster."; RL Nucleic Acids Res. 17:225-238(1989). RN [3] RP SEQUENCE FROM N.A. (HIS1:CG31617). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 14-47 AND 63-215 FROM N.A. RA Goldberg M.L.; RL Thesis (1979), University of Stanford, U.S.A. RN [6] RP SEQUENCE OF 22-117; 125-172 AND 185-231. RX MEDLINE=91126478; PubMed=1899487; RA Croston G.E., Kerrigan L.A., Lira L.M., Marshak D.R., Kadonaga J.T.; RT "Sequence-specific antirepression of histone H1-mediated inhibition RT of basal RNA polymerase II transcription."; RL Science 251:643-649(1991). RN [7] RP SEQUENCE OF 1-11 FROM N.A. RX MEDLINE=92164660; PubMed=1311255; RA Kas E., Laemmli U.K.; RT "In vivo topoisomerase II cleavage of the Drosophila histone and RT satellite III repeats: DNA sequence and structural characteristics."; RL EMBO J. 11:705-716(1992). CC -!- FUNCTION: HISTONES H1 ARE NECESSARY FOR THE CONDENSATION OF CC NUCLEOSOME CHAINS INTO HIGHER ORDER STRUCTURES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE HISTONE H1/H5 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04073; CAA27716.1; -. DR EMBL; X14215; CAA32433.1; -. DR EMBL; AE003670; AAN11123.1; -. DR EMBL; X60225; CAA42786.1; -. DR PIR; A02585; HSFF1. DR PIR; S07371; S07371. DR HSSP; P02259; 1HST. DR FlyBase; FBgn0001195; His1. DR FlyBase; FBgn0051617; His1:CG31617. DR InterPro; IPR005818; Histone_H1/H5. DR InterPro; IPR005819; Histone_H5. DR InterPro; IPR003216; Linkerhist_N. DR Pfam; PF00538; linker_histone; 1. DR PRINTS; PR00624; HISTONEH5. DR ProDom; PD000373; Linkerhist_N; 1. DR SMART; SM00526; H15; 1. KW Chromosomal protein; Nuclear protein; DNA-binding; Multigene family. SQ SEQUENCE 256 AA; 26359 MW; 5314DA250A7D0B23 CRC64; MSDSAVATSA SPVAAPPATV EKKVVQKKAS GSAGTKAKKA SATPSHPPTQ QMVDASIKNL KERGGSSLLA IKKYITATYK CDAQKLAPFI KKYLKSAVVN GKLIQTKGKG ASGSFKLSAS AKKEKDPKAK SKVLSAEKKV QSKKVASKKI GVSSKKTAVG AADKKPKAKK AVATKKTAEN KKTEKAKAKD AKKTGIIKSK PAATKAKVTA AKPKAVVAKA SKAKPAVSAK PKKTVKKASV SATAKKPKAK TTAAKK // ID H2AV_DROME STANDARD; PRT; 140 AA. AC P08985; Q26252; Q9VBB1; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone H2A variant. GN HIS2AV OR HIS2AVD OR H2AVD OR CG5499. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=88319938; PubMed=3137528; RA van Daal A., White E.M., Gorovsky M.A., Elgin S.C.R.; RT "Drosophila has a single copy of the gene encoding a highly conserved RT histone H2A variant of the H2A.F/Z type."; RL Nucleic Acids Res. 16:7487-7497(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90264951; PubMed=2111857; RA van Daal A., White E.M., Elgin S.C.R., Gorovsky M.A.; RT "Conservation of intron position indicates separation of major and RT variant H2As is an early event in the evolution of eukaryotes."; RL J. Mol. Evol. 30:449-455(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 1-52 FROM N.A., AND CHARACTERIZATION. RX MEDLINE=92360915; PubMed=1498368; RA Van Daal A., Elgin S.C.R.; RT "A histone variant, H2AvD, is essential in Drosophila melanogaster."; RL Mol. Biol. Cell 3:593-602(1992). CC -!- FUNCTION: VARIANT HISTONES H2A ARE SYNTHESIZED THROUGHOUT THE CELL CC CYCLE AND ARE VERY DIFFERENT FROM CLASSICAL S-PHASE REGULATED H2A. CC VITAL FOR VIABILITY, BUT THE EXACT FUNCTION OF VARIANT HISTONES CC H2A IS NOT KNOWN. CC -!- SUBUNIT: THE NUCLEOSOME IS AN OCTAMER CONTAINING TWO MOLECULES CC EACH OF H2A, H2B, H3 AND H4. THE OCTAMER WRAPS APPROXIMATELY 146 CC BP OF DNA. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC EXPRESSED IN EMBRYOS THROUGH TO ADULTS (FEMALE ONLY). CC -!- SIMILARITY: BELONGS TO THE HISTONE H2A FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07485; CAA30370.1; -. DR EMBL; X15549; CAA33555.1; -. DR EMBL; AE003758; AAF56631.1; -. DR EMBL; S42733; AAB22897.1; -. DR PIR; S08118; S08118. DR FlyBase; FBgn0001197; His2Av. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0005700; C:polytene chromosome; IDA. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR002119; Histone_H2A. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00620; HISTONEH2A. DR ProDom; PD000522; Histone_H2A; 1. DR SMART; SM00414; H2A; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. KW Chromosomal protein; Nucleosome core; Nuclear protein; DNA-binding; KW Multigene family. FT INIT_MET 0 0 SQ SEQUENCE 140 AA; 14850 MW; 0DA462B0E9B9CA8F CRC64; AGGKAGKDSG KAKAKAVSRS ARAGLQFPVG RIHRHLKSRT TSHGRVGATA AVYSAAILEY LTAEVLELAG NASKDLKVKR ITPRHLQLAI RGDEELDSLI KATIAGGGVI PHIHKSLIGK KEETVQDPQR KGNVILSQAY // ID H2A_DROME STANDARD; PRT; 123 AA. AC P02267; DT 21-JUL-1986 (Rel. 01, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone H2A. GN (HIS2A OR H2A) AND (HIS2A:CG31618 OR CG31618). OS Drosophila melanogaster (Fruit fly), OS Drosophila erecta (Fruit fly), OS Drosophila hydei (Fruit fly), OS Drosophila simulans (Fruit fly), OS Drosophila yakuba (Fruit fly), OS Rhynchosciara americana (Fungus gnat), and OS Tigriopus californicus (Marine copepod). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7220, 7224, 7240, 7245, 7186, 6832; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=AK-194; RX MEDLINE=89098383; PubMed=2536150; RA Matsuo Y., Yamazaki T.; RT "tRNA derived insertion element in histone gene repeating unit of RT Drosophila melanogaster."; RL Nucleic Acids Res. 17:225-238(1989). RN [2] RP SEQUENCE FROM N.A. (HIS2A:CG31618). RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=D.erecta, D.simulans, and D.yakuba; STRAIN=s2, and y6; RX MEDLINE=21919061; PubMed=11922104; RA Tsunemoto K., Matsuo Y.; RT "Molecular evolutionary analysis of a histone gene repeating unit from RT Drosophila simulans."; RL Genes Genet. Syst. 76:355-361(2001). RN [5] RP SEQUENCE OF 1-121 FROM N.A. RC SPECIES=D.melanogaster; RA Goldberg M.L.; RL Thesis (1979), University of Stanford, U.S.A. RN [6] RP SEQUENCE FROM N.A. RC SPECIES=D.hydei; RX MEDLINE=90221886; PubMed=2109309; RA Kremer H., Hennig W.; RT "Isolation and characterization of a Drosophila hydei histone DNA RT repeat unit."; RL Nucleic Acids Res. 18:1573-1580(1990). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=D.hydei; RA Strausbaugh L.D., Fitch D.H.A., Barrett V.; RL Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases. RN [8] RP SEQUENCE FROM N.A. RC SPECIES=R.americana; RA Santelli R.V., Siviero F., Navarro-Cattapan L.D.; RT "The complete sequence of the histone gene repeat of Rhynchosciara RT americana."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [9] RP SEQUENCE FROM N.A. RC SPECIES=T.californicus; RX MEDLINE=93076000; PubMed=1446074; RA Brown D., Cook A., Wagner M., Wells D.; RT "Closely linked H2B genes in the marine copepod, Tigriopus RT californicus indicate a recent gene duplication or gene conversion RT event."; RL DNA Seq. 2:387-396(1992). CC -!- SUBUNIT: THE NUCLEOSOME IS AN OCTAMER CONTAINING TWO MOLECULES CC EACH OF H2A, H2B, H3 AND H4. THE OCTAMER WRAPS APPROXIMATELY 146 CC BP OF DNA. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE HISTONE H2A FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S49144; AAA12278.1; -. DR EMBL; AE003670; AAN11125.1; -. DR EMBL; AB055959; BAC54548.1; -. DR EMBL; AB073634; BAC54552.1; -. DR EMBL; AB073635; BAC54556.1; -. DR EMBL; X14215; CAA32431.1; -. DR EMBL; X14215; CAA32436.1; -. DR EMBL; X17072; CAA34921.1; -. DR EMBL; X52576; CAA36807.1; -. DR EMBL; AF378198; AAK58063.1; -. DR EMBL; M84797; AAC41555.1; -. DR PIR; C56612; C56612. DR PIR; S10094; HSFF2. DR PIR; S21938; S21938. DR FlyBase; FBgn0001196; His2A. DR FlyBase; FBgn0051618; His2a:CG31618. DR FlyBase; FBgn0064619; Dere\His2A. DR FlyBase; FBgn0012375; Dhyd\His2A. DR FlyBase; FBgn0028772; Dsim\His2A. DR FlyBase; FBgn0028752; Dyak\His2A. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0005704; C:polytene chromosome band; IDA. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR002119; Histone_H2A. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00620; HISTONEH2A. DR ProDom; PD000522; Histone_H2A; 1. DR SMART; SM00414; H2A; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. KW Chromosomal protein; Nucleosome core; Nuclear protein; DNA-binding; KW Multigene family. FT INIT_MET 0 0 FT BINDING 118 118 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 123 AA; 13231 MW; 723D5617C97C55F6 CRC64; SGRGKGGKVK GKAKSRSNRA GLQFPVGRIH RLLRKGNYAE RVGAGAPVYL AAVMEYLAAE VLELAGNAAR DNKKTRIIPR HLQLAIRNDE ELNKLLSGVT IAQGGVLPNI QAVLLPKKTE KKA // ID H2B_DROME STANDARD; PRT; 122 AA. AC P02283; Q9W5U7; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Histone H2B. GN HIS2B AND HIS2B:CG17949. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE (HIS2B). RX MEDLINE=80088273; PubMed=117830; RA Elgin S.C.R., Schilling J., Hood L.E.; RT "Sequence of histone 2B of Drosophila melanogaster."; RL Biochemistry 18:5679-5685(1979). RN [2] RP SEQUENCE FROM N.A. (HIS2B). RC STRAIN=AK-194; RX MEDLINE=89098383; PubMed=2536150; RA Matsuo Y., Yamazaki T.; RT "tRNA derived insertion element in histone gene repeating unit of RT Drosophila melanogaster."; RL Nucleic Acids Res. 17:225-238(1989). RN [3] RP SEQUENCE FROM N.A. (HIS2B:CG17949). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 1-117 FROM N.A. (HIS2B). RA Goldberg M.L.; RL Thesis (1979), University of Stanford, U.S.A. CC -!- SUBUNIT: THE NUCLEOSOME IS AN OCTAMER CONTAINING TWO MOLECULES CC EACH OF H2A, H2B, H3 AND H4. THE OCTAMER WRAPS APPROXIMATELY 146 CC BP OF DNA. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE HISTONE H2B FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14215; CAA32432.1; -. DR EMBL; AE003670; AAN11124.1; -. DR PIR; S10095; HSFF22. DR FlyBase; FBgn0001198; His2B. DR FlyBase; FBgn0061209; His2B:CG17949. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000558; Histone_H2B. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR ProDom; PD000497; Histone_H2B; 1. DR SMART; SM00427; H2B; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. KW Nuclear protein; Chromosomal protein; Nucleosome core; DNA-binding; KW Multigene family. FT INIT_MET 0 0 FT CONFLICT 76 76 R -> C (IN REF. 3). SQ SEQUENCE 122 AA; 13565 MW; 6184F9AF79003062 CRC64; PPKTSGKAAK KAGKAQKNIT KTDKKKKRKR KESYAIYIYK VLKQVHPDTG ISSKAMSIMN SFVNDIFERI AAEASRLAHY NKRSTITSRE IQTAVRLLLP GELAKHAVSE GTKAVTKYTS SK // ID H33_HUMAN STANDARD; PRT; 135 AA. AC P06351; P33155; Q9V3W4; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone H3.3 (H3.A) (H3.B) (H3.3Q). GN (H3F3A OR HIS3.3A OR CG5825) AND (H3F3B OR HISH3-3Q OR HIS3.3B OR GN CG8989). OS Homo sapiens (Human), OS Mus musculus (Mouse), OS Rattus norvegicus (Rat), OS Oryctolagus cuniculus (Rabbit), OS Gallus gallus (Chicken), OS Spisula solidissima (Atlantic surf-clam), OS Drosophila melanogaster (Fruit fly), and OS Drosophila hydei (Fruit fly). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 10090, 10116, 9986, 9031, 6584, 7227, 7224; RN [1] RP SEQUENCE FROM N.A. (H3F3A). RC SPECIES=Human; TISSUE=Fibroblast; RX MEDLINE=85190590; PubMed=2859593; RA Wells D., Kedes L.; RT "Structure of a human histone cDNA: evidence that basally expressed RT histone genes have intervening sequences and encode polyadenylylated RT mRNAs."; RL Proc. Natl. Acad. Sci. U.S.A. 82:2834-2838(1985). RN [2] RP SEQUENCE FROM N.A. (H3F3A). RC SPECIES=Human; RX MEDLINE=87174815; PubMed=3031613; RA Wells D., Hoffman D., Kedes L.; RT "Unusual structure, evolutionary conservation of non-coding sequences RT and numerous pseudogenes characterize the human H3.3 histone RT multigene family."; RL Nucleic Acids Res. 15:2871-2889(1987). RN [3] RP SEQUENCE FROM N.A. (H3F3B). RC SPECIES=Human; TISSUE=Testis; RX MEDLINE=96163879; PubMed=8586426; RA Albig W., Bramlage B., Gruber K., Klobeck H.-G., Kunz J., Doenecke D.; RT "The human replacement histone H3.3B gene (H3F3B)."; RL Genomics 30:264-272(1995). RN [4] RP PARTIAL SEQUENCE. RC SPECIES=Human; RX MEDLINE=82075746; PubMed=7309716; RA Ohe Y., Iwai K.; RT "Human spleen histone H3. Isolation and amino acid sequence."; RL J. Biochem. 90:1205-1211(1981). RN [5] RP SEQUENCE FROM N.A. (H3F3B). RC SPECIES=Mouse; RX MEDLINE=89240011; PubMed=2470025; RA Hraba-Renevey S., Kress M.; RT "Expression of a mouse replacement histone H3.3 gene with a highly RT conserved 3' noncoding region during SV40- and polyoma-induced Go to RT S-phase transition."; RL Nucleic Acids Res. 17:2449-2461(1989). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=Rat; STRAIN=Sprague-Dawley; TISSUE=Embryonic brain; RA di Liegro I.; RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. (H3F3A). RC SPECIES=Rabbit; RX MEDLINE=90272438; PubMed=2349118; RA Chalmers M., Wells D.; RT "Extreme sequence conservation characterizes the rabbit H3.3A histone RT cDNA."; RL Nucleic Acids Res. 18:3075-3075(1990). RN [8] RP SEQUENCE FROM N.A. (H3F3B). RC SPECIES=Chicken; RX MEDLINE=85295962; PubMed=2863747; RA Brush D., Dodgson J.B., Choi O.R., Wilkins Stevens P., Engel J.D.; RT "Replacement variant histone genes contain intervening sequences."; RL Mol. Cell. Biol. 5:1307-1317(1985). RN [9] RP SEQUENCE FROM N.A. (H3F3B). RC SPECIES=Chicken; STRAIN=White leghorn; TISSUE=Liver; RX MEDLINE=87316886; PubMed=3627987; RA Dodgson J.B., Yamamoto M., Engel J.D.; RT "Chicken histone H3.3B cDNA sequence confirms unusual 3' UTR RT structure."; RL Nucleic Acids Res. 15:6294-6294(1987). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=S.solidissima; RX MEDLINE=87305176; PubMed=3040499; RA Swenson K.I., Borgese N., Pietrini G., Ruderman J.V.; RT "Three translationally regulated mRNAs are stored in the cytoplasm of RT clam oocytes."; RL Dev. Biol. 123:10-16(1987). RN [11] RP SEQUENCE FROM N.A. (H3F3B). RC SPECIES=D.melanogaster; RX MEDLINE=92084129; PubMed=1748304; RA Fretzin S., Allan B.D., van Daal A., Elgin S.C.R.; RT "A Drosophila melanogaster H3.3 cDNA encodes a histone variant RT identical with the vertebrate H3.3."; RL Gene 107:341-342(1991). RN [12] RP SEQUENCE FROM N.A. (H3F3A AND H3F3B). RC SPECIES=D.melanogaster, and D.hydei; STRAIN=Tuebingen; RX MEDLINE=96023949; PubMed=7557364; RA Akhmanova A.S., Bindels P.S.T., Xu J., Miedema K., Kremer H., RA Hennig W.; RT "Structure and expression of histone H3.3 genes in Drosophila RT melanogaster and Drosophila hydei."; RL Genome 38:586-600(1995). RN [13] RP SEQUENCE FROM N.A. (H3F3A AND H3F3B). RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: HISTONE H3, ALONG WITH HISTONE H4, PLAYS A CENTRAL ROLE CC IN NUCLEOSOME FORMATION. CC -!- SUBUNIT: THE NUCLEOSOME IS AN OCTAMER CONTAINING TWO MOLECULES CC EACH OF H2A, H2B, H3 AND H4. THE OCTAMER WRAPS APPROXIMATELY 146 CC BP OF DNA. CC -!- MISCELLANEOUS: THIS HISTONE IS THE PREDOMINANT FORM IN NONDIVIDING CC CELLS. CC -!- SIMILARITY: BELONGS TO THE HISTONE H3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11354; AAA52653.1; -. DR EMBL; M11353; AAA52654.1; -. DR EMBL; Z48950; CAA88778.1; -. DR EMBL; X05855; CAA29288.1; ALT_SEQ. DR EMBL; X05856; CAA29288.1; JOINED. DR EMBL; X05857; CAA29288.1; JOINED. DR EMBL; X73683; CAA52035.1; -. DR EMBL; X13605; CAA31940.1; -. DR EMBL; X51897; CAA36179.1; -. DR EMBL; M11393; AAA48794.1; -. DR EMBL; Y00392; CAA68458.1; -. DR EMBL; M17876; AAA29965.1; -. DR EMBL; X53822; CAA37819.1; -. DR EMBL; X82257; CAA57712.1; -. DR EMBL; X81205; CAA57077.1; -. DR EMBL; X81206; CAA57078.1; -. DR EMBL; X81207; CAA57080.1; -. DR EMBL; X81208; CAA57081.1; -. DR EMBL; AE003446; AAF46452.1; -. DR EMBL; AE003608; AAF52213.1; -. DR PIR; A27501; HSHU33. DR PIR; A45941; A45941. DR PIR; I50245; I50245. DR PIR; S04186; S04186. DR PIR; S10168; S10168. DR PIR; S34185; S34185. DR PIR; S61218; S61218. DR PIR; S61220; S61220. DR FlyBase; FBgn0014721; Dhyd\His3.3A. DR FlyBase; FBgn0014722; Dhyd\His3.3B. DR FlyBase; FBgn0014857; His3.3A. DR FlyBase; FBgn0004828; His3.3B. DR Genew; HGNC:4764; H3F3A. DR Genew; HGNC:4765; H3F3B. DR MIM; 601058; -. DR MIM; 601128; -. DR MGD; MGI:1101768; H3f3b. DR GO; GO:0000786; C:nucleosome; ISS. DR GO; GO:0003677; F:DNA binding; ISS. DR GO; GO:0007001; P:chromosome organization and biogenesis (sen...; ISS. DR GO; GO:0006334; P:nucleosome assembly; ISS. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000164; Histone_H3. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. KW Nuclear protein; Chromosomal protein; DNA-binding; Nucleosome core; KW Multigene family. FT INIT_MET 0 0 SQ SEQUENCE 135 AA; 15197 MW; E937D4279E30A725 CRC64; ARTKQTARKS TGGKAPRKQL ATKAARKSAP STGGVKKPHR YRPGTVALRE IRRYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSAAIG ALQEASEAYL VGLFEDTNLC AIHAKRVTIM PKDIQLARRI RGERA // ID H3_DROME STANDARD; PRT; 135 AA. AC P02299; DT 21-JUL-1986 (Rel. 01, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone H3. GN HIS3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AK-194; RX MEDLINE=89098383; PubMed=2536150; RA Matsuo Y., Yamazaki T.; RT "tRNA derived insertion element in histone gene repeating unit of RT Drosophila melanogaster."; RL Nucleic Acids Res. 17:225-238(1989). RN [2] RP SEQUENCE FROM N.A. RA Goldberg M.L.; RL Thesis (1979), University of Stanford, U.S.A. CC -!- FUNCTION: HISTONE H3, ALONG WITH HISTONE H4, PLAYS A CENTRAL ROLE CC IN NUCLEOSOME FORMATION. CC -!- SUBUNIT: THE NUCLEOSOME IS AN OCTAMER CONTAINING TWO MOLECULES CC EACH OF H2A, H2B, H3 AND H4. THE OCTAMER WRAPS APPROXIMATELY 146 CC BP OF DNA. CC -!- SIMILARITY: BELONGS TO THE HISTONE H3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14215; CAA32434.1; -. DR PIR; A02630; A02630. DR PDB; 1KNA; 20-MAR-02. DR PDB; 1KNE; 20-MAR-02. DR FlyBase; FBgn0001199; His3. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000164; Histone_H3. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. KW Nuclear protein; Chromosomal protein; DNA-binding; Nucleosome core; KW Multigene family; 3D-structure. FT INIT_MET 0 0 FT CONFLICT 31 31 A -> P (IN REF. 2). SQ SEQUENCE 135 AA; 15285 MW; D7B285BDD55537D5 CRC64; ARTKQTARKS TGGKAPRKQL ATKAARKSAP ATGGVKKPHR YRPGTVALRE IRRYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSSAVM ALQEASEAYL VALFEDTNLC AIHAKRITIM PKDIQLARRI RGERA // ID H4_DROME STANDARD; PRT; 102 AA. AC P02307; Q9VFH7; DT 21-JUL-1986 (Rel. 01, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone H4. GN (HIS4 OR H4) AND (HIS4R OR H4R OR CG3379) AND GN (HIS4:CG31611 OR CG31611). OS Drosophila melanogaster (Fruit fly), OS Drosophila erecta (Fruit fly), OS Drosophila hydei (Fruit fly), OS Drosophila simulans (Fruit fly), OS Drosophila yakuba (Fruit fly), OS Tigriopus californicus (Marine copepod), OS Chironomus thummi thummi (Midge), OS Asellus aquaticus (Water hoglouse), OS Acrolepiopsis assectella (Leek moth), OS Myrmica ruginodis, and OS Rhynchosciara americana (Fungus gnat). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7220, 7224, 7240, 7245, 6832, 7155, 92525, 57686, OX 34708, 7186; RN [1] RP SEQUENCE FROM N.A. (HIS4). RC SPECIES=D.melanogaster; STRAIN=AK-194; RX MEDLINE=89098383; PubMed=2536150; RA Matsuo Y., Yamazaki T.; RT "tRNA derived insertion element in histone gene repeating unit of RT Drosophila melanogaster."; RL Nucleic Acids Res. 17:225-238(1989). RN [2] RP SEQUENCE FROM N.A. (HIS4R). RC SPECIES=D.melanogaster, and D.hydei; STRAIN=Canton-S, and Tuebingen; RX MEDLINE=96275536; PubMed=8690091; RA Akhmanova A., Miedema K., Hennig W.; RT "Identification and characterization of the Drosophila histone H4 RT replacement gene."; RL FEBS Lett. 388:219-222(1996). RN [3] RP SEQUENCE FROM N.A. (HIS4R AND HIS4:CG31611). RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 1-71 FROM N.A. (HIS4). RC SPECIES=D.melanogaster; RA Goldberg M.L.; RL Thesis (1979), University of Stanford, U.S.A. RN [7] RP SEQUENCE FROM N.A. (HIS4). RC SPECIES=D.hydei; RX MEDLINE=90221886; PubMed=2109309; RA Kremer H., Hennig W.; RT "Isolation and characterization of a Drosophila hydei histone DNA RT repeat unit."; RL Nucleic Acids Res. 18:1573-1580(1990). RN [8] RP SEQUENCE FROM N.A. (HIS4). RC SPECIES=D.hydei; RX MEDLINE=93254234; PubMed=8487638; RA Fitch D.H., Strausbaugh L.D.; RT "Low codon bias and high rates of synonymous substitution in RT Drosophila hydei and D. melanogaster histone genes."; RL Mol. Biol. Evol. 10:397-413(1993). RN [9] RP SEQUENCE FROM N.A. RC SPECIES=D.erecta, D.simulans, and D.yakuba; RX MEDLINE=21919061; PubMed=11922104; RA Tsunemoto K., Matsuo Y.; RT "Molecular evolutionary analysis of a histone gene repeating unit RT from Drosophila simulans."; RL Genes Genet. Syst. 76:355-361(2001). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=T.californicus; RX MEDLINE=92127060; PubMed=1840514; RA Porter D., Brown D., Wells D.; RT "An H3-H4 histone gene pair in the marine copepod Tigriopus RT californicus, contains an intergenic dyad symmetry element."; RL DNA Seq. 1:197-206(1991). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=T.californicus; RX MEDLINE=93076000; PubMed=1446074; RA Brown D., Cook A., Wagner M., Wells D.; RT "Closely linked H2B genes in the marine copepod, Tigriopus RT californicus indicate a recent gene duplication or gene conversion RT event."; RL DNA Seq. 2:387-396(1992). RN [12] RP SEQUENCE FROM N.A. RC SPECIES=C.t.thummi; RX MEDLINE=91039309; PubMed=2172549; RA Hankeln T., Schmidt E.R.; RT "New foldback transposable element TFB1 found in histone genes of the RT midge Chironomus thummi."; RL J. Mol. Biol. 215:477-482(1990). RN [13] RP SEQUENCE FROM N.A. RC SPECIES=C.t.thummi; RX MEDLINE=94087747; PubMed=8263935; RA Hankeln T., Schmidt E.R.; RT "Divergent evolution of an 'orphon' histone gene cluster in RT Chironomus."; RL J. Mol. Biol. 234:1301-1307(1993). RN [14] RP SEQUENCE FROM N.A. RC SPECIES=A.aquaticus; RX MEDLINE=20250485; PubMed=10791823; RA Barzotti R., Pelliccia F., Bucciarelli E., Rocchi A.; RT "Organization, nucleotide sequence, and chromosomal mapping of a RT tandemly repeated unit containing the four core histone genes and a RT 5S rRNA gene in an isopod crustacean species."; RL Genome 43:341-345(2000). RN [15] RP SEQUENCE FROM N.A. RC SPECIES=A.assectella, and M.ruginodis; RA Hamelin E., Bigot Y.Y.B., Rouleux F., Renault S., Periquet G.; RT "Fast cloning and sequencing of histone H4 and actin messenger RNA RT fragments and their uses as control."; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. RN [16] RP SEQUENCE FROM N.A. RC SPECIES=R.americana; RA Santelli R.V., Siviero F., Navarro-Cattapan L.D.; RT "The complete sequence of the histone gene repeat of Rhynchosciara RT americana."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: HISTONE H4, ALONG WITH HISTONE H3, PLAYS A CENTRAL ROLE CC IN NUCLEOSOME FORMATION. CC -!- SUBUNIT: THE NUCLEOSOME IS AN OCTAMER CONTAINING TWO MOLECULES CC EACH OF H2A, H2B, H3 AND H4. THE OCTAMER WRAPS APPROXIMATELY 146 CC BP OF DNA. CC -!- SIMILARITY: BELONGS TO THE HISTONE H4 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14215; CAA32435.1; -. DR EMBL; X97436; CAA66066.1; -. DR EMBL; X97437; CAA66067.1; -. DR EMBL; X97438; CAA66068.1; -. DR EMBL; AE003705; AAF55080.1; -. DR EMBL; AE003670; AAN11126.1; -. DR EMBL; BT001842; AAN71603.1; -. DR EMBL; X17072; CAA34920.1; -. DR EMBL; X52576; CAA36806.1; -. DR EMBL; X52393; CAA36639.1; -. DR EMBL; AB055959; BAC54547.1; -. DR EMBL; AB073634; BAC54551.1; -. DR EMBL; AB073635; BAC54555.1; -. DR EMBL; M84797; AAC41553.1; -. DR EMBL; X56335; CAA39772.1; -. DR EMBL; X72803; CAA51323.1; -. DR EMBL; AJ238321; CAB64686.1; -. DR EMBL; X91508; CAA62808.1; -. DR EMBL; X91514; CAA62814.1; -. DR EMBL; AF378198; AAK58065.1; -. DR PIR; B56580; B56580. DR PIR; B56654; B56654. DR PIR; S09656; S09656. DR PIR; S10098; HSFF4. DR FlyBase; FBgn0001200; His4. DR FlyBase; FBgn0013981; His4r. DR FlyBase; FBgn0051611; His4:CG31611. DR FlyBase; FBgn0064617; Dere\His4. DR FlyBase; FBgn0012378; Dhyd\His4. DR FlyBase; FBgn0064361; Dsim\His4. DR FlyBase; FBgn0064256; Dyak\His4. DR FlyBase; FBgn0016205; Dhyd\His4r. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR001951; Histone_H4. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00623; HISTONEH4. DR ProDom; PD001827; Histone_H4; 1. DR SMART; SM00417; H4; 1. DR PROSITE; PS00047; HISTONE_H4; 1. KW Chromosomal protein; Nucleosome core; Nuclear protein; DNA-binding; KW Multigene family. FT INIT_MET 0 0 FT DNA_BIND 16 20 SQ SEQUENCE 102 AA; 11250 MW; 1CF18E9006144075 CRC64; TGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKV FLENVIRDAV TYTEHAKRKT VTAMDVVYAL KRQGRTLYGF GG // ID HAIR_DROME STANDARD; PRT; 337 AA. AC P14003; Q9VSN8; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Hairy protein. GN H OR CG6494. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90059896; PubMed=2479541; RA Rushlow C.A., Hogan A., Pierchin S.M., Howe K.M., Lardelli M., RA Ish-Horowicz D.; RT "The Drosophila hairy protein acts in both segmentation and bristle RT patterning and shows homology to N-myc."; RL EMBO J. 8:3095-3103(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP WRPW MOTIF. RX MEDLINE=95094252; PubMed=8001118; RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., RA Brent R., Ish-Horowicz D.; RT "Groucho is required for Drosophila neurogenesis, segmentation, and RT sex determination and interacts directly with hairy-related bHLH RT proteins."; RL Cell 79:805-815(1994). CC -!- FUNCTION: PAIR-RULE PROTEIN THAT REGULATES EMBRYONIC SEGMENTATION CC AND ADULT BRISTLE PATTERNING. TRANSCRIPTIONAL REPRESSOR OF GENES CC THAT REQUIRE A BHLH PROTEIN FOR THEIR TRANSCRIPTION (EG. THE FUSHI CC TARAZU GENE). CC -!- SUBUNIT: TRANSCRIPTION REPRESSION REQUIRES FORMATION OF A COMPLEX CC WITH A CO-REPRESSOR PROTEIN (GROUCHO). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DOMAIN: HAS A PARTICULAR TYPE OF BASIC DOMAIN (PRESENCE OF A CC HELIX-INTERRUPTING PROLINE) THAT BINDS TO THE N-BOX (CACNAG), CC RATHER THAN THE CANONICAL E-BOX (CANNTG). CC -!- DOMAIN: THE CARBOXYL-TERMINAL WRPW MOTIF IS A TRANSCRIPTIONAL CC REPRESSION DOMAIN NECESSARY FOR THE INTERACTION WITH GROUCHO, A CC TRANSCRIPTIONAL CO-REPRESSOR RECRUITED TO SPECIFIC TARGET DNA BY CC HAIRY-RELATED PROTEINS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ORANGE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15904; CAA34018.1; -. DR EMBL; X15905; CAA34019.1; -. DR EMBL; AE003554; AAF50378.1; -. DR TRANSFAC; T00345; -. DR FlyBase; FBgn0001168; h. DR GO; GO:0007461; P:restriction of R8 fate; NAS. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR003650; Orange. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00511; ORANGE; 1. DR PROSITE; PS50888; HLH; 1. KW Nuclear protein; Developmental protein; Pair-rule protein; KW DNA-binding; Transcription regulation; Repressor; Polymorphism. FT DNA_BIND 32 44 BASIC DOMAIN. FT DOMAIN 45 89 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 149 157 GLN-RICH. FT DOMAIN 222 237 GLN-RICH. FT DOMAIN 241 250 POLY-ALA. FT DOMAIN 334 337 WRPW MOTIF (REQUIRED FOR ACTIVITY). FT VARIANT 292 292 S -> P. SQ SEQUENCE 337 AA; 36995 MW; 6D2ECAF7F2D56C0B CRC64; MVTGVTAANM TNVLGTAVVP AQLKETPLKS DRRSNKPIME KRRRARINNC LNELKTLILD ATKKDPARHS KLEKADILEK TVKHLQELQR QQAAMQQAAD PKIVNKFKAG FADCVNEVSR FPGIEPAQRR RLLQHLSNCI NGVKTELHQQ QRQQQQQSIH AQMLPSPPSS PEQDSQQGAA APYLFGIQQT ASGYFLPNGM QVIPTKLPNG SIALVLPQSL PQQQQQQLLQ HQQQQQQLAV AAAAAAAAAA QQQPMLVSMP QRTASTGSAS SHSSAGYESA PGSSSSCSYA PSSPANSSYE PMDIKPSVIQ RVPMEQQPLS LVIKKQIKEE EQPWRPW // ID HASP_DROME STANDARD; PRT; 566 AA. AC P83103; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative serine/threonine-protein kinase Haspin homolog (EC 2.7.1.-). GN HASPIN OR CG40080. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). RN [2] RP CONCEPTUAL TRANSLATION. RA Manning G., Sudarsanam S., Plowman G.; RT "Prediction of novel protein kinases from the Drosophila genome RT project and EST sequences."; RL Unpublished observations (AUG-2001). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. DR FlyBase; FBgn0046706; Haspin. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. KW Hypothetical protein; Transferase; Serine/threonine-protein kinase; KW ATP-binding. FT DOMAIN 248 566 PROTEIN KINASE. FT NP_BIND 254 262 ATP (By similarity). FT BINDING 282 282 ATP (By similarity). FT ACT_SITE 418 418 By similarity. SQ SEQUENCE 566 AA; 65322 MW; 46363EAAFAF66967 CRC64; MLSISKTKMD FLEEGRWKDP FDELLDSRTK LSKMNIVKQN VRVTYNIDSS VENSSYIEIK EPNHKNEPLT LEDCSIKVYC PSDSISTPCD KRLGGTTGLF ETDLSPITRL KLEGVEDSRD KCADTNEADL YVNVEILFQN INSSPKKCSN FGKKRLSNLN KMVTAVHPSI SLNPGKWRKS LNNFIRSKIT ETNFTKKVER RSSICQDRKS LVLKGEHKFE NKYEEDVLKY CHQCTPLPFN TAYEQHKLLN TKKIGEGAYG EVFRCSRNQE VLKDHISDIV LKIIPLEGST VINGEKQKTF SQILPEIIIT KKMCSLRTSK TNSTNGFVSI QKVSLVKGRY PPHFIKLWEK YDNEKGSEND HPELFGDNQL FAVLELKFAG SDMANFKFLN SEQSYYALQQ IILALAVGEE EYQFEHRDLH LGNILIEYTN KKHIVCTFKS SNLTLLSKGV NVTIIDYTLS RVTINDCCYF NDLSRDEELF QATGDYQYDV YRMMRNELKN NWSSFSPKTN IIWLSYVIVK VLDSVKYKSI NTKVHRMYID KIKELKNIIM TFESASHCAN YLFNLN // ID HCD2_DROME STANDARD; PRT; 255 AA. AC O18404; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 3-hydroxyacyl-CoA dehydrogenase type II (EC 1.1.1.35) (Type II HADH) DE (Scully protein). GN SCU OR CG7113. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND MUTAGENESIS OF LEU-33 AND PHE-120. RC STRAIN=Canton-S; RX MEDLINE=98252852; PubMed=9585418; RA Torroja L., Ortuno-Sahagun D., Ferrus A., Haemmerle B., Barbas J.A.; RT "Scully, an essential gene of Drosophila, is homologous to mammalian RT mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/amyloid-beta RT peptide-binding protein."; RL J. Cell Biol. 141:1009-1018(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY PLAY A ROLE IN GERM LINE FORMATION. CC -!- CATALYTIC ACTIVITY: (S)-3-HYDROXYACYL-COA + NAD(+) = 3-OXOACYL-COA CC + NADH. CC -!- SUBUNIT: MULTIMER (POTENTIAL). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: FOUND IN MANY TISSUES INCLUDING CNS. HIGHEST CC EXPRESSION IN BOTH EMBRYONIC GONADAL PRIMORDIA AND MATURE OVARIES CC AND TESTES. CC -!- SIMILARITY: BELONGS TO THE SHORT-CHAIN DEHYDROGENASES/REDUCTASES CC (SDR) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y15102; CAA75377.1; -. DR EMBL; AE003507; AAF48797.1; -. DR HSSP; O70351; 1E6W. DR FlyBase; FBgn0021765; scu. DR InterPro; IPR002198; ADH_short. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. KW Oxidoreductase; NAD; Mitochondrion. FT NP_BIND 6 31 NAD (BY SIMILARITY). FT ACT_SITE 162 162 BY SIMILARITY. FT MUTAGEN 33 33 L->Q: LETHAL ALLELE. FT MUTAGEN 120 120 F->I: LETHAL ALLELE. SQ SEQUENCE 255 AA; 26905 MW; F58690643FA0FD03 CRC64; MIKNAVSLVT GGASGLGRAT AERLAKQGAS VILADLPSSK GNEVAKELGD KVVFVPVDVT SEKDVSAALQ TAKDKFGRLD LTVNCAGTAT AVKTFNFNKN VAHRLEDFQR VININTVGTF NVIRLSAGLM GANEPNQDGQ RGVIVNTASV AAFDGQIGQA AYSASKAAVV GMTLPIARDL STQGIRICTI APGLFNTPML AALPEKVRTF LAKSIPFPQR LGEPSEYAHL VQAIYENPLL NGEVIRIDGA LRMMP // ID HDA1_DROME STANDARD; PRT; 520 AA. AC Q94517; O17429; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone deacetylase RPD3 (HD) (dRPD3). GN RPD3 OR HDAC1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=97113416; PubMed=8955276; RA de Rubertis F., Kadosh D., Henchoz S., Pauli D., Reuter G., Struhl K., RA Spierer P.; RT "The histone deacetylase RPD3 counteracts genomic silencing in RT Drosophila and yeast."; RL Nature 384:589-591(1996). RN [2] RP SEQUENCE FROM N.A. RA Johnson C.A., White D., O'Neill L.P., Turner B.M.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP INTERACTION WITH SU(VAR)39. RX MEDLINE=21486105; PubMed=11571273; RA Czermin B., Schotta G., Huelsmann B.B., Brehm A., Becker P.B., RA Reuter G., Imhof A.; RT "Physical and functional association of SU(VAR)3-9 and HDAC1 in RT Drosophila."; RL EMBO Rep. 2:915-919(2001). CC -!- FUNCTION: RESPONSIBLE FOR THE DEACETYLATION OF LYSINE RESIDUES ON CC THE N-TERMINAL PART OF THE CORE HISTONES (H2A, H2B, H3 AND H4). CC HISTONE DEACETYLATION GIVES A TAG FOR EPIGENETIC REPRESSION AND CC PLAYS AN IMPORTANT ROLE IN TRANSCRIPTIONAL REGULATION, CELL CYCLE CC PROGRESSION AND DEVELOPMENTAL EVENTS. HISTONE DEACETYLASES ACT VIA CC THE FORMATION OF LARGE MULTIPROTEIN COMPLEXES. ACTS DOWNSTREAM OF CC SU(VAR)39. DEACETYLATION OF HISTONE H3 MAY BE PREREQUISITE FOR CC RECRUITING SU(VAR)39 TO HISTONES. IN DROSOPHILA, IT IS INVOLVED IN CC POSITION-EFFECT VARIEGATION (PEV). CC -!- SUBUNIT: INTERACTS WITH THE HISTONE METHYLTRANSFERASE SU(VAR)39. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE HISTONE DEACETYLASE FAMILY. SUBFAMILY CC 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y09258; CAA70455.1; -. DR EMBL; AF026949; AAC23917.1; -. DR FlyBase; FBgn0015805; Rpd3. DR GO; GO:0005717; C:chromatin; IDA. DR GO; GO:0005737; C:cytoplasm; TAS. DR GO; GO:0000118; C:histone deacetylase complex; TAS. DR GO; GO:0005634; C:nucleus; TAS. DR GO; GO:0004407; F:histone deacetylase activity; TAS. DR GO; GO:0008134; F:transcription factor binding; TAS. DR GO; GO:0016568; P:chromatin modification; TAS. DR GO; GO:0006342; P:chromatin silencing; IGI. DR GO; GO:0008340; P:determination of adult life span; IMP. DR GO; GO:0016458; P:gene silencing; IMP. DR GO; GO:0006340; P:negative regulation of transcription of hom...; IPI. DR GO; GO:0016481; P:negative regulation of transcription; IEP. DR InterPro; IPR000286; His_deacetylse. DR Pfam; PF00850; Hist_deacetyl; 1. DR PRINTS; PR01270; HDASUPER. KW Hydrolase; Nuclear protein; Chromatin regulator; KW Transcription regulation; Repressor. FT DOMAIN 7 318 HISTONE DEACETYLASE. FT ACT_SITE 138 138 BY SIMILARITY. FT CONFLICT 50 51 DI -> EIY (IN REF. 2). FT CONFLICT 66 66 C -> S (IN REF. 2). FT CONFLICT 96 96 D -> N (IN REF. 2). FT CONFLICT 105 105 E -> D (IN REF. 2). FT CONFLICT 295 295 V -> VV (IN REF. 2). FT CONFLICT 370 370 L -> V (IN REF. 2). FT CONFLICT 506 506 S -> T (IN REF. 2). SQ SEQUENCE 520 AA; 58183 MW; D02EA3DBD3C64688 CRC64; MQSHSKKRVC YYYDSDIGNY YYGQGHPMKP HRIRMTHNLL LNYGLYRKMD IRPHKATADE MTKFHCDEYV RFLRSIRPDN MSEYNKQMQR FNVGEDCPVF DGLYEFCQLS AGGSVAAAVK LNKQASEICI NWGGGLHHAK KSEASGFCYV NDIVLGILEL LKYHQRVLYI DIDVHHGDGV EEAFYTTDRV MTVSFHKYGE YFPGTGDLRD IGAGKGKYYA VNIPLRDGMD DDAYESIFVP IISKVMETFQ PAAVVLQCGA DSLTGDRLGC FNLTVKGHGK CVEFVKKYNL PFLMVGGGGY TIRKVSRCWT YETSVALAVE IANELPYNDY FEYFGPDFKL HISPSNMTNQ NTSEYLEKIK NRLFENLRML PHAPGVQIQA IPEDAINDES DDEDKVDKDD RLPQSDKDKR IVPENEYSDS EDEGEGGRRD NRSYKGQRKR PRLDKDTNSN KASSETSSEI KDEKEKGDGA DGEESTASNT NSNNNSNNKS DNDAGATANA GSGSGSGSGA GAKGAKENNI // ID HDC_DROME STANDARD; PRT; 1080 AA. AC Q9N2M8; Q24480; Q9VA84; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Headcase protein [Contains: Headcase short protein]. GN HDC OR CG15532. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=96171720; PubMed=8575315; RA Weaver T.A., White R.A.; RT "Headcase, an imaginal specific gene required for adult morphogenesis RT in Drosophila melanogaster."; RL Development 121:4149-4160(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP PARTIAL SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=98198453; PubMed=9531534; RA Steneberg P., Englund C., Kronhamn J., Weaver T.A., Samakovlis C.; RT "Translational readthrough in the hdc mRNA generates a novel branching RT inhibitor in the drosophila trachea."; RL Genes Dev. 12:956-967(1998). CC -!- FUNCTION: REQUIRED FOR IMAGINAL CELL DIFFERENTIATION, MAY BE CC INVOLVED IN HORMONAL RESPONSIVENESS DURING METAMORPHOSIS. INVOLVED CC IN AN INHIBITORY SIGNALING MECHANISM TO DETERMINE THE NUMBER OF CC CELLS THAT WILL FORM UNICELLULAR SPROUTS IN THE TRACHEA. REGULATED CC BY TRANSCRIPTION FACTOR ESG. THE LONGER HDC PROTEIN IS COMPLETELY CC FUNCTIONAL AND THE SHORTER PROTEIN CARRIES SOME FUNCTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: EXPRESSED IN ALL IMAGINAL CELLS OF THE EMBRYO CC AND LARVAE. EXPRESSED IN A SUBSET OF TRACHEAL FUSION CELLS FROM CC STAGE 14 TO THE END OF EMBRYOGENESIS IN METAMERES 2-9, LATERAL CC TRUNK AND VENTRAL ANASTOMOSES. CC -!- MISCELLANEOUS: READTHROUGH OF THE TERMINATOR UAA OCCURS BETWEEN CC CODONS FOR ALA-650 AND HIS-652. READTHROUGH IS NOT ALWAYS CC SUPPRESSED AS THE SHORTER PROTEIN IS MORE ABUNDANT. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z50097; CAA90425.1; -. DR EMBL; Z50097; CAB58233.1; -. DR EMBL; AE003773; AAF57033.1; ALT_SEQ. DR FlyBase; FBgn0010113; hdc. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0007430; P:terminal branching of trachea, cytoplasmic ...; NAS. KW Developmental protein. FT CHAIN 1 1080 HEADCASE PROTEIN. FT CHAIN 1 650 HEADCASE SHORT PROTEIN. FT DOMAIN 57 66 POLY-GLY. FT DOMAIN 211 218 POLY-ASN. FT DOMAIN 219 227 POLY-GLY. FT DOMAIN 343 350 POLY-GLN. FT DOMAIN 381 395 POLY-GLN. FT DOMAIN 723 769 GLN-RICH. FT DOMAIN 801 815 POLY-GLN. FT DOMAIN 845 854 POLY-SER. FT DOMAIN 887 891 POLY-SER. FT DOMAIN 965 970 POLY-SER. FT DOMAIN 1030 1036 POLY-SER. FT CONFLICT 85 85 H -> P (IN REF. 1). FT CONFLICT 190 191 PT -> SN (IN REF. 1). FT CONFLICT 226 226 A -> G (IN REF. 1). FT CONFLICT 243 244 SY -> HD (IN REF. 1). FT CONFLICT 279 310 SGVLQTSALATFSNILNTNNVLGLDLRARAGS -> PACCR FT PVRWPLSATSSIRTMSWPGPARQGWQ (IN REF. 1). FT CONFLICT 342 342 P -> A (IN REF. 1). FT CONFLICT 353 353 L -> V (IN REF. 1). FT CONFLICT 383 383 Q -> P (IN REF. 1). FT CONFLICT 432 432 D -> E (IN REF. 1). FT CONFLICT 641 641 T -> S (IN REF. 1). FT CONFLICT 695 695 P -> Q (IN REF. 1). FT CONFLICT 852 852 S -> SS (IN REF. 1). FT CONFLICT 1067 1067 A -> R (IN REF. 1). SQ SEQUENCE 1080 AA; 117446 MW; 87EB144BA0D1B787 CRC64; MAPRRNSNIS SSGNSTQQQH QQQLQQQHQT QQHQLLQFYA ENVNSSGVLM APMQGTGGVG GVGGGGMVHC CLPSGDCRKL DTLIHLNELS LADCIRVLCN NENCSAGQYM HRECFEWWEA SVLQALKANG RARSWSERQR LQHLWTKKGY ELVQKACSCK CGRGQLRKDL DWVPPSSQGV IYLNGSGNRP TLANGSLSED DDKKKAKKKR NRNNNNNNGG GGGGGAGVNG NTKTPLSNNN GNSYAGLTPN PNVGVIGSGL PHNNGNTASN GSSGNNGSSG VLQTSALATF SNILNTNNVL GLDLRARAGS LSSSGAGSGS TSPSDSQSSG EISVSPVQQL LPQQQQQQQQ SLLIQPLGPA FGSNLLQNGL GLSKNLLIAP QQQQQQQLQQ QQQQQNNLPA LANISNFKPL ASYEQQQLVQ QQKNKEVELY SDRVRSTSGC NGIFSRRLDF SSFNLLPKTR LNSYQVKIED EGNHGNDETR LFILSSLAQS QMSRVACILC EEPLLVFDRY PLVDGSFFLS PKQHSSGCIE VKYEGRTLYL TCVCMSCLDG TSSSRAINCR FCKEPWDGSS LVLGTMYAYD IFAAMPCCAE RFKCNNCFKM LMHPQQRLSF YSDYSHGVTC PYCNTQDTHF VKPLTFCYAK TTATRLPTLA XHEAPLESPV GTGATTTQVP NAQGSPTASG CSSNTIASKQ PPKQPLYNAA IDYSAPLQQQ INPDLIGAHP HAQQHQQQVR QQQQQQQQQQ PQQQQQQQQQ QTQQQQSQQQ QQQQQQQHQP VVSTFQRGNF PQQSHKTMNM MAMADVMSKY QQQQHQQQQQ QRQQQHNLQP QQQHATQKGL EGLLLTNTNT SNNNSSSSSS SSISNLIISH NSASNTGNKM QPTWGQSDAI SALWGCSSSS SGCSSGSGSQ PSLSPTASSN GNDGSKMMLW AAQSSPQNAA TLRDGFKELQ RQQPPQQQVP QQQPHAASPT ASLTSSSSSS NGWSASHYGK PNIWELPGST GQRTPASSHD IFTDLLCNLS ISQDNSSQQA SSKADASDVS SNSSSSAGEL LEAANIWRFP EYASSQLYME EPTGGAAACM QLFNDYLNMN // ID HE47_DROME STANDARD; PRT; 424 AA. AC Q27268; Q9VMQ1; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable ATP-dependent RNA helicase WM6. GN HEL25E OR DBP25F OR WM6 OR CG7269. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95107265; PubMed=7808417; RA Warbrick E., Glover D.; RT "A Drosophila gene encoding a DEAD box RNA helicase can suppress loss RT of wee1/mik1 function in Schizosaccharomyces pombe."; RL Mol. Gen. Genet. 245:654-657(1994). RN [2] RP SEQUENCE FROM N.A. RA Lorenz L.J., Melnick M.B., Eberl D.F., Snood V., Lasko P., RA Perrimon N.; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE RNA HELICASE THAT MAY REGULATE ENTRY INTO CC MITOSIS BY DOWN-REGULATING THE EXPRESSION OF OTHER GENES WHOSE CC ACTIVITY MAY BE RATE-LIMITING FOR ENTRY INTO MITOSIS. BINDS CC CHROMOSOMES AND MODIFIES POSITION EFFECT VARIEGATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. DECD CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X79802; CAA56197.1; -. DR EMBL; L06018; AAB65835.1; -. DR EMBL; AE003610; AAF52261.1; -. DR PIR; S51601; S51601. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0014189; Hel25E. DR InterPro; IPR001410; DEAD. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. KW ATP-binding; RNA-binding; Helicase; Nuclear protein. FT NP_BIND 85 92 ATP (POTENTIAL). FT SITE 193 196 DECD BOX. SQ SEQUENCE 424 AA; 48652 MW; CE132476090E1AFE CRC64; MADNDDLLDY EDEEQTETTA VENQEAPKKD VKGTYVSIHS SGFRDFLLKP EILRAIVDCG FEHPSEVQHE CIPQAVLGMD ILCQAKSGMG KTAVFVLATL QQLEPSDNNT CHVLVMCHTR ELAFQISKEY ERFSKYMPTV KVAVFFGGMA IQKDEETLKS GTPHIVVGTP GRILALIRNK KLNLKLLKHF VLDECDKMLE QLDMRRDVQE IFRSTPHGKQ VMMFSATLSK DIRPVCKKFM QDPMEVYVDD EAKLTLHGLQ QHYVNLKENE KNKKLFELLD VLEFNQVVIF VKSVQRCVAL SQLLTEQNFP AIGIHRGMTQ EERLNRYQQF KDFQKRILVA TNLFGRGMDI ERVNIVFNYD MPEDSDTYLH RVARAGRFGT KGLAITFVSD ENDAKILNEV QDRFDVNISE LPEEIDLSTY IEGR // ID HEM6_DROME STANDARD; PRT; 390 AA. AC Q9V3D2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Coproporphyrinogen III oxidase (EC 1.3.3.3) (Coproporphyrinogenase) DE (Coprogen oxidase) (COX). GN COPROX OR BCDNA:GM14838 OR CG3433. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2) + 2 H(2)O. CC -!- COFACTOR: IRON (BY SIMILARITY). CC -!- PATHWAY: HEME BIOSYNTHESIS; SIXTH STEP. CC -!- SIMILARITY: BELONGS TO THE AEROBIC COPROPORPHYRINOGEN III OXIDASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003615; AAF52469.1; -. DR EMBL; AF160897; AAD46837.1; -. DR FlyBase; FBgn0021944; Coprox. DR InterPro; IPR001260; Coprogen_oxidas. DR Pfam; PF01218; Coprogen_oxidas; 1. DR PRINTS; PR00073; COPRGNOXDASE. DR PROSITE; PS01021; COPROGEN_OXIDASE; 1. KW Porphyrin biosynthesis; Oxidoreductase; Heme biosynthesis; Iron. SQ SEQUENCE 390 AA; 44419 MW; E63FBA5583530863 CRC64; MNALRHTISL VSLGTFQLVR RTRGPHARGF LLGTGLGLAS FSAVTYAHSA EAVDPKVNGV QMNTSRFMAE PITDSKALLG DKENMRHRME ILIMEIQAEF CRALEAEENC GQKFKVDRWE RPEGGGGITC VLQDGDVFEK AGVNISVVTG SLPPAAVQQM RARGKNLKEG ASLPFFASGV SAVIHPRNPH VPTIHFNYRY FEVETAKGEK QWWFGGGTDL TPYYLCEKDA SHFHQTLKSA CDEHDPTYYP RFKKWCDDYF RIKHRNESRG IGGIFFDDID SPNQEAAFNF VSSCARAVIP SYVPLVRKHK NREYGNNERQ WQLLRRGRYV EFNLIYDRGT KFGLYTPGAR YESILMSLPL HARWEYMHEP KSQSEEGKLM KVLKNPKDWV // ID HEMZ_DROME STANDARD; PRT; 384 AA. AC Q9V9S8; O76533; Q8IGA4; Q8IH67; Q95U82; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ferrochelatase, mitochondrial precursor (EC 4.99.1.1) (Protoheme DE ferro-lyase) (Heme synthetase). GN FECH OR CG2098. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), AND CHARACTERIZATION. RX MEDLINE=98380446; PubMed=9712849; RA Sellers V.M., Wang K.-F., Johnson M.K., Dailey H.A.; RT "Evidence that the fourth ligand to the 2Fe-2S cluster in animal RT ferrochelatase is a cysteine. Characterization of the enzyme from RT Drosophila melanogaster."; RL J. Biol. Chem. 273:22311-22316(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS A; B AND C). RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CATALYZES THE FERROUS INSERTION INTO PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRIN + FE(2+) = PROTOHEME + 2 H(+). CC -!- COFACTOR: BINDS 1 2FE-2S CLUSTER. CC -!- PATHWAY: PROTOHEME BIOSYNTHESIS; LAST STEP. CC -!- SUBCELLULAR LOCATION: BOUND TO THE MITOCHONDRIAL INNER MEMBRANE IN CC EUKARYOTIC CELLS WITH ITS ACTIVE SITE ON THE MATRIX SIDE OF THE CC MEMBRANE (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=Q9V9S8-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9V9S8-2; Sequence=VSP_007689, VSP_007690; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q9V9S8-3; Sequence=VSP_007691, VSP_007692; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE FERROCHELATASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF076220; AAC26225.1; -. DR EMBL; AE003779; AAF57206.1; -. DR EMBL; AE003779; AAN14294.1; -. DR EMBL; AY058251; AAL13480.1; -. DR EMBL; BT001392; AAN71147.1; -. DR EMBL; BT001878; AAN71652.1; -. DR FlyBase; FBgn0024891; Fech. DR GO; GO:0004325; F:ferrochelatase activity; IDA. DR InterPro; IPR001015; Ferrochelatase. DR Pfam; PF00762; Ferrochelatase; 1. DR ProDom; PD002792; Ferrochelatase; 1. DR TIGRFAMs; TIGR00109; hemH; 1. DR PROSITE; PS00534; FERROCHELATASE; 1. KW Porphyrin biosynthesis; Heme biosynthesis; Lyase; Mitochondrion; KW Transit peptide; Metal-binding; Iron-sulfur; Iron; 2Fe-2S; KW Alternative splicing. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 384 FERROCHELATASE. FT METAL 156 156 IRON-SULFUR (2FE-2S). FT METAL 363 363 IRON-SULFUR (2FE-2S). FT METAL 366 366 IRON-SULFUR (2FE-2S). FT METAL 371 371 IRON-SULFUR (2FE-2S). FT ACT_SITE 190 190 BY SIMILARITY. FT ACT_SITE 343 343 BY SIMILARITY. FT VARSPLIC 1 158 Missing (in isoform B). FT /FTId=VSP_007689. FT VARSPLIC 159 173 SGSSFNSIFTHYRSN -> MHNCSYLFDPLYLFS (in FT isoform B). FT /FTId=VSP_007690. FT VARSPLIC 281 281 G -> V (in isoform C). FT /FTId=VSP_007691. FT VARSPLIC 282 384 Missing (in isoform C). FT /FTId=VSP_007692. FT CONFLICT 269 269 P -> A (IN REF. 1). SQ SEQUENCE 384 AA; 43597 MW; 923B3BE7606566C5 CRC64; MFLHNTKFCR LASGLAGGVR NLSGQKPKTA ILMLNMGGPT HTDQVHDYLL RIMTDRDMIQ LPVQSRLGPW IAQRRTPEVQ KKYKEIGGGS PILKWTELQG QLMCEQLDRI SPETAPHKHY VGFRYVNPLT ENTLAEIEKD KPERVVLFSQ YPQYSCATSG SSFNSIFTHY RSNNLPSDIK WSIIDRWGTH PLLIKTFAQR IRDELAKFVE TKRNDVVILF TAHSLPLKAV NRGDAYPSEI GASVHMVMQE LGQTNPYSLA WQSKVGPLPW LAPATDDAIK GYVKQGLKNF ILVPIAFVNE HIETLHELDI EYCDELAKEV GVEEIRRAAT PNDHPLFIDA LTNVVADHLK SQQAVNPKFL MRCPMCSNPK CRESKSWYRQ LCSN // ID HEM_DROME STANDARD; PRT; 1126 AA. AC P55162; Q9VNU8; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Membrane-associated protein Hem (dHem-2). GN HEM OR HEM2 OR CG5837. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95371111; PubMed=7643388; RA Baumgartner S., Martin D., Chiquet-Ehrismann R., Sutton J., RA Desai A., Huang I., Kato K., Hromas R.; RT "The HEM proteins: a novel family of tissue-specific transmembrane RT proteins expressed from invertebrates through mammals with an RT essential function in oogenesis."; RL J. Mol. Biol. 251:41-49(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PLAY A ROLE DURING GROWTH OF THE OOCYTE. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MATERNALLY IN THE OOCYTE AND SHOWS CC UNIFORM EXPRESSION DURING THE FIRST HALF OF EMBRYOGENESIS, BUT CC BECOMES RESTRICTED TO THE BRAIN AND THE NERVOUS SYSTEM DURING LATE CC EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE HEM-1/HEM-2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X80028; CAA56332.1; -. DR EMBL; AE003597; AAF51820.1; -. DR PIR; S57832; S49208. DR FlyBase; FBgn0011771; Hem. DR GO; GO:0007409; P:axonogenesis; IMP. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; IMP. KW Transmembrane. FT TRANSMEM 989 1006 POTENTIAL. SQ SEQUENCE 1126 AA; 129379 MW; 125FE7177AECC0E5 CRC64; MARPIFPNQQ KIAEKLIILN DRGLGILTRI YNIKKACGDT KSKPGFLSEK SLESSIKFIV KRFPNIDVKG LNAIVNIKAE IIKSLSLYYH TFVDLLDFKD NVCELLTTMD ACQIHLDITL NFELTKYYLD LVVTYVSLMI VLSRVEDRKA VLGLYNAAYE LQNNQADTGF PRLGQMILDY EVPLKKLAEE FIPHQRLLTS ALRSLTSIYA LRNLPADKWR EMQKLSLVGN PAILLKAVRT DTMSCEYISL EAMDRWIIFG LLLNHQMLGQ YPEVNKIWLS ALESSWVVAL FRDEVLQIHQ YIQATFDGIK GYSKRIGEVK EAYNTAVQKA ALMHRERRKF LRTALKELAL IMTDQPGLLG PKAIFIFIGL CLARDEILWL LRHNDNPPLL KNKGKSNEDL VDRQLPELLF HMEELRALVR KYSQVMQRYY VQYLSGFDAT DLNIRMQSLQ MCPEDESIIF SSLYNTAAAL TVKQVEDNEL FYFRPFRLDW FRLQTYMSVG KAALRIAEHA ELARLLDSMV FHTRVVDNLD EILVETSDLS IFCFYNKMFD DQFHMCLEFP AQNRYIIAFP LICSHFQNCT HEMCPEERHH IRERSLSVVN IFLEEMAKEA KNIITTICDE QCTMADALLP KHCAKILSVQ SARKKKDKSK SKHFDDIRKP GDESYRKTRE DLTTMDKLHM ALTELCFAIN YCPTVNVWEF AFAPREYLCQ NLEHRFSRDL VGMVMFNQET MEIAKPSELL ASVRAYMNVL QTVENYVHID ITRVFNNCLL QQTQALDSHG EKTIAALYNT WYSEVLLRRV SAGNIVFSIN QKAFVPISPE GWVPFNPQEF SDLNELRALA ELVGPYGIKT LNETLMWHIA NQVQELKSLV STNKEVLITL RTSFDKPEVM KEQFKRLQDV DRVLQRMTII GVIICFRNLV HEALVDVLDK RIPFLLSSVK DFQEHLPGGD QIRVASEMAS AAGLLCKVDP TLATTLKSKK PEFDEGEHLT ACLLMVFVAV SIPKLARNEN SFYRATIDGH SNNTHCMAAA INNIFGALFT ICGQSDMEDR MKEFLALASS SLLRLGQESD KEATRNRESI YLLLDEIVKQ SPFLTMDLLE SCFPYVLIRN AYHGVYKQEQ ILGLAL // ID HEP_DROME STANDARD; PRT; 487 AA. AC Q23977; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Dual specificity mitogen-activated protein kinase kinase hemipterous DE (EC 2.7.1.-) (MAPKK). GN HEP OR HEM. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96067643; PubMed=8521475; RA Glise B., Bourbon H., Noselli S.; RT "Hemipterous encodes a novel Drosophila MAP kinase kinase, required RT for epithelial cell sheet movement."; RL Cell 83:451-461(1995). CC -!- FUNCTION: REQUIRED FOR THE EPITHELIAL CELL SHEET MOVEMENT CALLED CC DORSAL CLOSURE (DC), WHICH ALLOWS ESTABLISHMENT OF THE DORSAL CC EPIDERMIS. CONTROLS THE EXPRESSION IN THE DORSAL EPITHELIUM EDGES CC OF ANOTHER DORSAL CLOSURE GENE, PUCKERED (PUC). CC -!- PTM: MAPKK IS ITSELF DEPENDENT ON SER/THR PHOSPHORYLATION FOR CC ACTIVITY CATALYZED BY MAP KINASE KINASE KINASES (BY SIMILARITY). CC -!- PTM: WEAKLY AUTOPHOSPHORYLATED. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. MAP CC KINASE KINASE SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05240; AAC46944.1; -. DR FlyBase; FBgn0010303; hep. DR GO; GO:0004672; F:protein kinase activity; IDA. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR GO; GO:0030381; P:eggshell pattern formation (sensu Insecta); IMP. DR GO; GO:0000165; P:MAPKKK cascade; NAS. DR GO; GO:0046844; P:micropyle formation; IMP. DR GO; GO:0007395; P:spreading of leading edge cells; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; Tyrosine-protein kinase; KW ATP-binding; Phosphorylation; Developmental protein. FT DOMAIN 95 106 POLY-SER. FT DOMAIN 195 454 PROTEIN KINASE. FT NP_BIND 201 209 ATP (BY SIMILARITY). FT BINDING 224 224 ATP (BY SIMILARITY). FT ACT_SITE 318 318 BY SIMILARITY. FT MOD_RES 346 346 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 350 350 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 487 AA; 53079 MW; 09E248DBD14A1E45 CRC64; MSTIEFETIG SRLQSLEAKL QAQNESHDQI VLSGARGPVV SGSVPSARVP PLATSASAAT SATHAPSLGA SSVSGSGISI AQRPAPPVPH ATLRSPSASS SSSSRSAFRS AAPATGLRWT YTPPTTRVSR ATPTLPMLSS GPGGDVECTR PVILPLPTPP HPPVSETDMK LKIIMEQTGK LNINGRQYPT DINDLKHLGD LGNGTSGNVV KMMHLSSNTI IAVKQMRRTG NAEENKRILM DLDVVLKSHD CKYIVKCLGC FVRDPDVWIC MELMSMCFDK LLKLSKKPVP EQILGKVTVA TVNALSYLKD KHGVIHRDVK PSNILIDERG NIKLCDFGIS GRLVDSKANT RSAGCAAYMA PERIDPKKPK YDIRADVWSL GITLVELATA RSPYEGCNTD FEVLTKVLDS EPPCLPYGEG YNFSQQFRDF VIKCLTKNHQ DRPKYPELLA QPFIRIYESA KVDVPNWFQS IKDNDCGQWR SNAPEVT // ID HGD_DROME STANDARD; PRT; 439 AA. AC Q9VKJ0; Q86P40; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homogentisate 1,2-dioxygenase (EC 1.13.11.5) (Homogentisicase) DE (Homogentisate oxygenase) (Homogentisic acid oxidase). GN HGO OR CG4779. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Schmidt S.R.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: HOMOGENTISATE + O(2) = 4-MALEYLACETOACETATE. CC -!- COFACTOR: IRON (BY SIMILARITY). CC -!- PATHWAY: CATABOLISM OF TYROSINE; THIRD STEP. CC -!- PATHWAY: CATABOLISM OF PHENYLALANINE; FOURTH STEP. CC -!- SIMILARITY: BELONGS TO THE HOMOGENTISATE DIOXYGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF131124; AAF36489.1; -. DR EMBL; AE003631; AAF53078.2; -. DR EMBL; BT003496; AAO39500.1; -. DR HSSP; Q93099; 1EYB. DR FlyBase; FBgn0040211; hgo. DR InterPro; IPR005708; HmgA. DR Pfam; PF04209; HgmA; 1. DR TIGRFAMs; TIGR01015; hmgA; 1. KW Oxidoreductase; Dioxygenase; Iron; Phenylalanine catabolism; KW Tyrosine catabolism. FT METAL 335 335 IRON (BY SIMILARITY). FT METAL 341 341 IRON (BY SIMILARITY). FT METAL 371 371 IRON (BY SIMILARITY). FT CONFLICT 96 106 MISSING (IN REF. 1). SQ SEQUENCE 439 AA; 49397 MW; 08418138B9600FE1 CRC64; MSEYKYLSGF GSHFSSEDER YPNSLPVGQN SPQVCPYKLY AEQLSGSAFT APRTENMRTW LYRKLPSAAH LPFQPFKGAE YFSQNWDEQP PNPNQLRWKP FDLPPKDGKN VNFVEGLHTV CGAGDPRSRH GLAIHIYSCN GSMDNSAFYN SDGDFLIVPQ QGVLDITTEF GRMSVAPNEI CVIPQGIRFA VNVDSPSRGY ILEVYDDHFV LPDLGPIGAN GLANPRDFET PVAWFDDRDV KDFQVISKFQ GRLFVAKQNH TVFDVVAWHG NYVPFKYDLS KFMVINSVSF DHCDPSIFTV LTCPSLRAGT AIADFVIFPP RWSVQEHTFR PPYYHRNCMS EFMGLILGKY EAKEDGFAAG GATLHSMMTP HGPDVKCFEG ASNAKLVPER VAEGTQAFMF ESSLSLAVTK WGEETCQKLD AAYYECWQAL KNNFQITKN // ID HH_DROME STANDARD; PRT; 421 AA. AC Q02936; Q9VCQ4; DT 01-FEB-1994 (Rel. 28, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Hedgehog protein precursor. GN HH OR CG4637. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG), FUNCTION, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=93185922; PubMed=8166882; RA Tashiro S., Michiue T., Higashijima S.-I., Zenno S., Ishimaru S., RA Takahashi F., Orihara M., Kojima T., Saigo K.; RT "Structure and expression of hedgehog, a Drosophila segment-polarity RT gene required for cell-cell communication."; RL Gene 124:183-189(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORM LONG), FUNCTION, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RX MEDLINE=93008241; PubMed=1394430; RA Lee J.J., von Kessler D.P., Parks S., Beachy P.A.; RT "Secretion and localized transcription suggest a role in positional RT signaling for products of the segmentation gene hedgehog."; RL Cell 71:33-50(1992). RN [3] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=93083438; PubMed=1280560; RA Mohler J., Vani K.; RT "Molecular organization and embryonic expression of the hedgehog gene RT involved in cell-cell communication in segmental patterning of RT Drosophila."; RL Development 115:957-971(1992). RN [4] RP SEQUENCE FROM N.A. (ISOFORM LONG), FUNCTION, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94040725; PubMed=1340474; RA Tabata T., Eaton S., Kornberg T.B.; RT "The Drosophila hedgehog gene is expressed specifically in posterior RT compartment cells and is a target of engrailed regulation."; RL Genes Dev. 6:2635-2645(1992). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP AUTOPROTEOLYTIC CLEAVAGE. RX MEDLINE=95191685; PubMed=7885476; RA Porter J.A., von Kessler D.P., Ekker S.C., Young K.E., Lee J.J., RA Moses K., Beachy P.A.; RT "The product of hedgehog autoproteolytic cleavage active in local and RT long-range signalling."; RL Nature 374:363-366(1995). RN [7] RP FUNCTION, AND MUTAGENESIS OF CYS-35. RX MEDLINE=21220785; PubMed=11319862; RA Lee J.D., Kraus P., Gaiano N., Nery S., Kohtz J., Fishell G., RA Loomis C.A., Treisman J.E.; RT "An acylatable residue of Hedgehog is differentially required in RT Drosophila and mouse limb development."; RL Dev. Biol. 233:122-136(2001). RN [8] RP PALMITOYLATION, MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-35. RX MEDLINE=21442023; PubMed=11486055; RA Chamoun Z., Mann R.K., Nellen D., von Kessler D.P., Bellotto M., RA Beachy P.A., Basler K.; RT "Skinny hedgehog, an acyltransferase required for palmitoylation and RT activity of the hedgehog signal."; RL Science 293:2080-2084(2001). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 208-358, AND MUTAGENESIS. RX MEDLINE=97474313; PubMed=9335337; RA Hall T.M.T., Porter J.A., Young K.E., Koonin E.V., Beachy P.A., RA Leahy D.J.; RT "Crystal structure of a Hedgehog autoprocessing domain: homology RT between Hedgehog and self-splicing proteins."; RL Cell 91:85-97(1997). CC -!- FUNCTION: INTERCELLULAR SIGNAL ESSENTIAL FOR A VARIETY OF CC PATTERNING EVENTS DURING DEVELOPMENT. ESTABLISHES THE ANTERIOR- CC POSTERIOR AXIS OF THE EMBRYONIC SEGMENTS AND PATTERNS THE LARVAL CC IMAGINAL DISKS. BINDS TO THE PATCHED (PTC) RECEPTOR, WHICH CC FUNCTIONS IN ASSOCIATION WITH SMOOTHENED (SMO), TO ACTIVATE THE CC TRANSCRIPTION OF TARGET GENES WINGLESS (WG), DECAPENTAPLEGIC (DPP) CC AND PTC. IN THE ABSENCE OF HH, PTC REPRESSES THE CONSTITUTIVE CC SIGNALING ACTIVITY OF SMO THROUGH FUSED (FU). CC -!- SUBCELLULAR LOCATION: NUCLEAR UP TO EMBRYONIC STAGE 10 AND THEN AT CC STAGE 11 SHIFTS TO THE CYOPLASM. C-TERMINAL PEPTIDE DIFFUSES FROM CC THE CELL, THE N-TERMINAL PEPTIDE REMAINS ASSOCIATED WITH THE CELL CC SURFACE. ALSO SECRETED IN EITHER CLEAVED OR UNCLEAVED FORM TO CC MEDIATE SIGNALING TO OTHER CELLS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q02936-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q02936-2; Sequence=VSP_002065, VSP_002066; CC -!- TISSUE SPECIFICITY: IN EMBRYOS, EXPRESSION STARTS AT STAGE 5 AS A CC FEW STRIPES AT THE ANTERIOR AND POSTERIOR ENDS, THIS EXPANDS TO 17 CC STRIPES DURING STAGES 8-11. EXPRESSION IS ALSO SEEN IN CNS AND CC SOME PNS CELLS UNTIL STAGE 13-14, AND IN FOREGUT, HINDGUT AND CC SALIVARY GLANDS. IN LARVAE, EXPRESSION IS SEEN IN THE POSTERIOR CC COMPARTMENT OF THE WING IMAGINAL DISK. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN EMBRYOS, LARVAE AND PUPAE AT CC HIGH LEVELS WITH MAXIMUM EXPRESSION IN 6-12 HOUR EMBRYOS AND 0-24 CC HOUR PUPAE. LOW LEVELS OF EXPRESSION ARE SEEN IN ADULTS. CC -!- PTM: THE C-TERMINAL DOMAIN DISPLAYS AN AUTOPROTEOLYSIS ACTIVITY CC AND A CHOLESTEROL TRANSFERASE ACTIVITY. BOTH ACTIVITIES RESULT IN CC THE CLEAVAGE OF THE FULL-LENGTH HEDGEHOG PROTEIN AND COVALENT CC ATTACHMENT OF A CHOLESTEROL MOIETY TO THE C-TERMINAL OF THE NEWLY CC GENERATED AMINO-TERMINAL FRAGMENT (N-PRODUCT). THIS COVALENT CC MODIFICATION APPEARS TO PLAY AN ESSENTIAL ROLE IN RESTRICTING THE CC SPATIAL DISTRIBUTION OF THE HEDGEHOG ACTIVITY TO THE CELL SURFACE. CC AMINO-TERMINAL PALMITOYLATION OF HEDGEHOG N-PRODUCT IS REQUIRED CC FOR THE EMBRYONIC AND LARVAL PATTERNING ACTIVITIES OF THE HEDGEHOG CC SIGNAL. THE N-PRODUCT IS THE ACTIVE SPECIES IN BOTH LOCAL AND CC LONG-RANGE SIGNALING, WHEREAS THE C-TERMINAL PRODUCT HAS NO CC SIGNALING ACTIVITY. CC -!- PTM: RASP ACTS WITHIN THE SECRETORY PATHWAY TO CATALYZE THE N- CC TERMINAL PALMITOYLATION OF HH. CC -!- MASS SPECTROMETRY: MW=20238.44; METHOD=MALDI; RANGE=35-207. CC -!- SIMILARITY: BELONGS TO THE HEDGEHOG FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L05404; AAA28604.1; ALT_INIT. DR EMBL; L05405; -; NOT_ANNOTATED_CDS. DR EMBL; L02793; AAA16458.1; ALT_INIT. DR EMBL; Z11840; -; NOT_ANNOTATED_CDS. DR EMBL; S66384; AAB28646.1; ALT_INIT. DR EMBL; AE003742; AAF56102.1; ALT_INIT. DR PIR; A46400; A46400. DR PDB; 1AT0; 12-NOV-97. DR MEROPS; C46.001; -. DR FlyBase; FBgn0004644; hh. DR GO; GO:0005737; C:cytoplasm; IEP. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0005634; C:nucleus; IEP. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0005113; F:patched binding; NAS. DR GO; GO:0005119; F:smoothened binding; NAS. DR GO; GO:0007267; P:cell-cell signaling; NAS. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; NAS. DR GO; GO:0009880; P:embryonic pattern specification; IEP. DR GO; GO:0008347; P:glia cell migration; IMP. DR GO; GO:0007442; P:hindgut morphogenesis; IMP. DR GO; GO:0007447; P:imaginal disc pattern formation; NAS. DR GO; GO:0007458; P:progression of morphogenetic furrow (sensu ...; IEP. DR GO; GO:0016540; P:protein autoprocessing; IDA. DR GO; GO:0045464; P:R8 cell fate specification; NAS. DR GO; GO:0042127; P:regulation of cell proliferation; NAS. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP. DR GO; GO:0007367; P:segment polarity determination; IEP. DR GO; GO:0007224; P:smoothened signaling pathway; IGI. DR GO; GO:0007427; P:tracheal cell migration (sensu Insecta); IMP. DR InterPro; IPR009045; Hedgehog/DD_pept. DR InterPro; IPR003587; Hedgehog_hint_N. DR InterPro; IPR003586; Hedgehog_hintC. DR InterPro; IPR000320; HH_signal. DR InterPro; IPR006141; Intein_S. DR InterPro; IPR001767; Pept_C46_hint. DR InterPro; IPR001657; Peptidase_C46. DR Pfam; PF01085; HH_signal; 1. DR Pfam; PF01079; Hint; 1. DR PRINTS; PR00632; SONICHHOG. DR ProDom; PD003042; HH_signal; 1. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. KW Hydrolase; Protease; Developmental protein; KW Segmentation polarity protein; Nuclear protein; Signal; KW Autocatalytic cleavage; Lipoprotein; Palmitate; Alternative splicing; KW 3D-structure. FT SIGNAL 1 34 POTENTIAL. FT CHAIN 35 421 HEDGEHOG PROTEIN. FT CHAIN 35 207 HEDGEHOG PROTEIN N-PRODUCT. FT CHAIN 208 421 HEDGEHOG PROTEIN C-PRODUCT. FT SITE 207 208 CLEAVAGE (AUTO-). FT SITE 253 253 INVOLVED IN CHOLESTEROL TRANSFER. FT SITE 276 276 INVOLVED IN AUTO-CLEAVAGE. FT ACT_SITE 279 279 ESSENTIAL FOR AUTO-CLEAVAGE. FT LIPID 35 35 N-palmitoyl cysteine. FT LIPID 207 207 Cholesterol glycine ester. FT VARSPLIC 111 142 RCKEKLNVLAYSVMNEWPGIRLLVTESWDEDY -> VRKTL FT KHRKLVTKFVIHHWESFAYRNHCDKVT (in isoform FT Short). FT /FTId=VSP_002065. FT VARSPLIC 143 421 Missing (in isoform Short). FT /FTId=VSP_002066. FT MUTAGEN 35 35 C->S: N-PRODUCT IS MADE BUT FAILS FT TO UNDERGO PALMITOYLATION. FT MUTAGEN 253 253 D->A: NO CHOLESTEROL TRANSFER. FT MUTAGEN 276 276 T->A: GREATLY REDUCED AUTOPROCESSING FT ACTIVITY. FT MUTAGEN 279 279 H->A: NO AUTOPROCESSING ACTIVITY. FT CONFLICT 106 106 R -> G (IN REF. 1). FT CONFLICT 297 297 D -> H (IN REF. 1). FT CONFLICT 323 323 V -> L (IN REF. 1). FT CONFLICT 357 357 Q -> P (IN REF. 3). SQ SEQUENCE 421 AA; 47110 MW; AFBC1DE079E70654 CRC64; MRHIAHTQRC LSRLTSLVAL LLIVLPMVFS PAHSCGPGRG LGRHRARNLY PLVLKQTIPN LSEYTNSASG PLEGVIRRDS PKFKDLVPNY NRDILFRDEE GTGADRLMSK RCKEKLNVLA YSVMNEWPGI RLLVTESWDE DYHHGQESLH YEGRAVTIAT SDRDQSKYGM LARLAVEAGF DWVSYVSRRH IYCSVKSDSS ISSHVHGCFT PESTALLESG VRKPLGELSI GDRVLSMTAN GQAVYSEVIL FMDRNLEQMQ NFVQLHTDGG AVLTVTPAHL VSVWQPESQK LTFVFADRIE EKNQVLVRDV ETGELRPQRV VKVGSVRSKG VVAPLTREGT IVVNSVAASC YAVINSQSLA HWGLAPMRLL STLEAWLPAK EQLHSSPKVV SSAQQQNGIH WYANALYKVK DYVLPQSWRH D // ID HID_DROME STANDARD; PRT; 410 AA. AC Q24106; Q9VVP1; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Head involution defective protein (Wrinkled protein). GN W OR HID OR CG5123. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Eye imaginal disk; RX MEDLINE=95347579; PubMed=7622034; RA Grether M.E., Abrams J.M., Agapite J., White K., Steller H.; RT "The head involution defective gene of Drosophila melanogaster RT functions in programmed cell death."; RL Genes Dev. 9:1694-1708(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR INDUCTION OF APOPTOSIS. HID MUTANTS CONTAIN CC EXTRA CELLS IN THE HEAD OWING TO DECREASED LEVELS OF CELL DEATH CC AND SHOW A PRONOUNCED DEFECT IN THE MORPHOGENETIC MOVEMENTS OF CC HEAD INVOLUTION. ECTOPIC EXPRESSION IN THE RETINA RESULTS IN CC COMPLETE EYE ABLATION. SEEMS TO ACT GENETICALLY UPSTREAM OF CC BACULOVIRAL ANTI-APOPTOTIC P35. CC -!- DEVELOPMENTAL STAGE: EXPRESSION CORRESPONDS APPROXIMATELY TO THE CC PATTERN OF PROGRAMMED CELL DEATH IN THE EMBRYO, PARTICULARLY IN CC THE HEAD. CC -!- SIMILARITY: LIMITED AT THE N-TERMINAL REGION, TO GRIM AND RPR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U31226; AAA79985.1; -. DR EMBL; AE003521; AAF49270.1; -. DR FlyBase; FBgn0003997; W. DR GO; GO:0008258; P:head involution; IMP. DR GO; GO:0006917; P:induction of apoptosis; IGI. DR GO; GO:0002165; P:larval/pupal development (sensu Insecta); IMP. DR GO; GO:0012501; P:programmed cell death; IMP. KW Apoptosis; Developmental protein; Polymorphism. FT DOMAIN 17 79 SER-RICH. FT DOMAIN 237 240 POLY-SER. FT DOMAIN 332 340 POLY-SER. FT VARIANT 171 171 P -> S (IN ALLELE A22). FT VARIANT 261 261 S -> L (IN ALLELE A206). FT CONFLICT 351 351 P -> S (IN REF. 1). SQ SEQUENCE 410 AA; 43876 MW; 63EBF913149E27E1 CRC64; MAVPFYLPEG GADDVASSSS GASGNSSPHN HPLPSSASSS VSSSGVSSAS ASSASSSSSA SSDGASSAAS QSPNTTTSSA TQTPMQSPLP TDQVLYALYE WVRMYQSQQS APQIFQYPPP SPSCNFTGGD VFFPHGHPNP NSNPHPRTPR TSVSFSSGEE YNFFRQQQPQ PHPSYPAPST PQPMPPQSAP PMHCSHSYPQ QSAHMMPHHS APFGMGGTYY AGYTPPPTPN TASAGTSSSS AAFGWHGHPH SPFTSTSTPL SAPVAPKMRL QRSQSDAARR KRLTSTGEDE REYQSDHEAT WDEFGDRYDN FTAGRERLQE FNGRIPPRKK KSSNSHSSSS NNPVCHTDSQ PGGTSQAESG AIHGHISQQR QVERERQKAK AEKKKPQSFT WPTVVTVFVL AMGCGFFAAR // ID HIG_DROME STANDARD; PRT; 958 AA. AC Q09101; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Locomotion-related protein Hikaru genki precursor. GN HIG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Head; RX MEDLINE=93213498; PubMed=8461133; RA Hoshino M., Matsuzaki F., Nabeshima Y.-I., Hama C.; RT "Hikaru genki, a CNS-specific gene identified by abnormal locomotion RT in Drosophila, encodes a novel type of protein."; RL Neuron 10:395-407(1993). CC -!- FUNCTION: HAS A ROLE IN THE DEVELOPMENT OF CNS FUNCTIONS INVOLVED CC IN LOCOMOTOR ACTIVITY. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=3; CC IsoId=Q09101-1; Sequence=Displayed; CC Name=1; CC IsoId=Q09101-2; Sequence=VSP_002513; CC Name=2; CC IsoId=Q09101-3; Sequence=VSP_002512, VSP_002513; CC Name=4; CC IsoId=Q09101-4; Sequence=VSP_002512; CC -!- TISSUE SPECIFICITY: EXPRESSED IN PCC NEURONS AND NEUROBLASTS IN CC THE PROCEPHALIC NEUROGENIC REGION IN THE CENTRAL NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: MOST ABUNDANT DURING AND/OR AFTER NEURONAL CC DIFFERENTIATION AND DURING CELL SPECIFICATION OR AXOGENESIS. CC -!- SIMILARITY: CONTAINS 1 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAIN. CC -!- SIMILARITY: CONTAINS 4 SUSHI (SCR) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D13884; BAA02984.1; -. DR EMBL; D13885; BAA02985.1; -. DR EMBL; D13886; BAA02986.1; -. DR EMBL; D13887; BAA02987.1; -. DR HSSP; P10998; 1VVD. DR FlyBase; FBgn0010114; hig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003599; Ig. DR InterPro; IPR002396; Selectin. DR InterPro; IPR000436; Sushi_SCR_CCP. DR Pfam; PF00084; sushi; 5. DR PRINTS; PR00343; SELECTIN. DR SMART; SM00032; CCP; 5. DR SMART; SM00409; IG; 1. DR PROSITE; PS50835; IG_LIKE; 1. KW Glycoprotein; Alternative splicing; Immunoglobulin domain; Repeat; KW Sushi; Signal. FT SIGNAL 1 31 POTENTIAL. FT CHAIN 32 958 LOCOMOTION-RELATED PROTEIN HIKARU GENKI. FT DOMAIN 612 708 IG-LIKE C2-TYPE. FT DOMAIN 713 769 SUSHI 1. FT DOMAIN 772 828 SUSHI 2. FT DOMAIN 831 891 SUSHI 3. FT DOMAIN 893 952 SUSHI 4. FT SITE 318 320 CELL ATTACHMENT SITE. FT DISULFID 714 755 BY SIMILARITY. FT DISULFID 741 768 BY SIMILARITY. FT DISULFID 773 814 BY SIMILARITY. FT DISULFID 800 827 BY SIMILARITY. FT DISULFID 832 877 BY SIMILARITY. FT DISULFID 863 890 BY SIMILARITY. FT DISULFID 894 939 BY SIMILARITY. FT DISULFID 922 952 BY SIMILARITY. FT CARBOHYD 376 376 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 525 525 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 605 605 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 620 620 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 752 752 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 789 789 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 529 553 Missing (in isoform 2 and isoform 4). FT /FTId=VSP_002512. FT VARSPLIC 892 958 Missing (in isoform 1 and isoform 2). FT /FTId=VSP_002513. SQ SEQUENCE 958 AA; 107027 MW; 4161258E85ABC764 CRC64; MWSRQRMRHK PLWALISLTV LLLVLDKSNA NTEPVETSTT SEPDASPGCR APDVRFTIVK PEATTEQPLA KFETTQIYLP DDFTTADVEF VDSVPRHPNE NHAAVINPYS LDLGDDHLHV GDAAASLVGD DDLGDEDEDH HGDPEDKRLN ANRKQGKRRR AGSGRRRRIE NENGQTGRGR GSRYKRHAIL HDTEASPETD RWAGSKLAAE GDVYYVHIAD ILKSREPNRE LKSKLHKLKM KARLNKCLAE GGKEKCTRLL KKKPKKKVVE KEQTLKKEKK FPKEEQSKEK VLENGQTPKE DELELDHPET AAAHHRRRGD SHAAELDQRD RSPRWRRRRS TEFKGDLGQL PPESGIGPEP EPLADQNLKD LQQYGNQSSS ARVALLWQRV KRKSGRTAGA LSRPKGGGDS SSKTTSRKDK GIYDEEAGYT PIHPDDPEFD EEEEEDEEVD ILQQFTEVSE IRFPGEIGPM GDRRLCKIRC VKGKWVGPLC ATNEEDDNGN VKFQPLYKSC HVNRIPSHLL LSYRNISVTP IPPNRGWRKT RLSKSTLLSN TEINVGWDLP HGHSLQARCQ ELGIYKLLGE SRVLCSNGLW APRMPSCVPT TVLTNYSEDS APSIRIKIFN GSHSFEPSGV MAVPPHSTVL MDCMYPRVRG TPEWSWTSWY MQYSTGWSPA QEEKAVRYRL SIKNIENNDS GTFTCTSPRG LTNSIAVVVA TSTCPRLTEP LAPLKLRLEG NKLGQRAHYE CPEGFRLDGA WNATCLASGS WSSPTPTCHA IQCPRLELDD PHLSLIELNT SAWGRAVFKC QWGFKLTGPA QLDCEPSGVW SGPVPRCKVI QCVMPVAPLN GRIGGTSLSQ RRLTVGALVT FSCNDGHSLV GESSIICTEN GQWSHSPPFC KSQCPYPGDP PNGLIAPLKF NYDAGDYLSV QCRPGFVQSY EGPPERPKCQ PDGRWSGPMP KCKSYEEV // ID HIRA_DROME STANDARD; PRT; 1047 AA. AC O17468; O46105; O77144; Q9W3Q3; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE HIRA protein homolog (dHIRA). GN HIRA OR DHH OR CG12153. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG), AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=98278847; PubMed=9611274; RA Kirov N., Shtilbans A., Rushlow C.; RT "Isolation and characterization of a new gene encoding a member of the RT HIRA family of proteins from Drosophila melanogaster."; RL Gene 212:323-332(1998). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=98380288; PubMed=9712723; RA Llevadot R., Marques G., Pritchard M., Estivill X., Ferrus A., RA Scambler P.; RT "Cloning, chromosome mapping and expression analysis of the HIRA gene RT from Drosophila melanogaster."; RL Biochem. Biophys. Res. Commun. 249:486-491(1998). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COULD PLAY A PART IN MECHANISMS OF TRANSCRIPTIONAL CC REGULATION SIMILAR TO THAT PLAYED BY YEAST HIR1 AND HIR2 TOGETHER. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=O17468-1; Sequence=Displayed; CC Name=Short; CC IsoId=O17468-2; Sequence=VSP_006775, VSP_006776, VSP_006777; CC -!- DEVELOPMENTAL STAGE: EXPRESSED MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT TO ADULTS (MALE AND FEMALE). CC -!- SIMILARITY: BELONGS TO THE WD-REPEAT HIR1 FAMILY. CC -!- SIMILARITY: CONTAINS 4 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF031081; AAC48360.1; -. DR EMBL; AJ222709; CAA10954.1; -. DR EMBL; AF071881; AAC64041.1; -. DR EMBL; AE003441; AAF46267.1; -. DR FlyBase; FBgn0022786; Hira. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 2. DR SMART; SM00320; WD40; 6. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Transcription regulation; Repeat; WD repeat; Nuclear protein; KW Alternative splicing. FT REPEAT 68 98 WD 1. FT REPEAT 127 157 WD 2. FT REPEAT 170 200 WD 3. FT REPEAT 264 310 WD 4. FT DOMAIN 932 942 POLY-THR. FT DOMAIN 944 972 POLY-SER. FT VARSPLIC 63 63 L -> LPVLSDKAEFDADVPKML (in isoform FT Short). FT /FTId=VSP_006775. FT VARSPLIC 430 437 KDGKRRIT -> LSLICKIF (in isoform Short). FT /FTId=VSP_006776. FT VARSPLIC 438 1047 Missing (in isoform Short). FT /FTId=VSP_006777. FT CONFLICT 53 53 A -> G (IN REF. 1). FT CONFLICT 58 58 D -> E (IN REF. 1). FT CONFLICT 64 64 C -> G (IN REF. 1). FT CONFLICT 72 72 C -> S (IN REF. 1). FT CONFLICT 159 163 QAFPH -> RHFHN (IN REF. 2; AAC64041). FT CONFLICT 169 169 K -> E (IN REF. 2; AAC64041). FT CONFLICT 179 179 S -> W (IN REF. 1). FT CONFLICT 232 232 G -> A (IN REF. 2; AAC64041). FT CONFLICT 242 242 N -> D (IN REF. 2; CAA10954). FT CONFLICT 330 330 D -> Y (IN REF. 1). FT CONFLICT 416 416 A -> V (IN REF. 1). FT CONFLICT 453 455 MNI -> LNF (IN REF. 1). FT CONFLICT 459 459 S -> R (IN REF. 2). FT CONFLICT 536 536 L -> V (IN REF. 1). FT CONFLICT 1043 1047 KTDQT -> PNRSDMRRKTPIPNKPPKL (IN REF. 1). SQ SEQUENCE 1047 AA; 113415 MW; 3614D5F411DC440C CRC64; MRLLKPAWVH HDDKQIFSVD IHKDCTKFAT GGQGSDCGRV VIWNLLPVLS DKAEFDADVP KMLCQMDQHL ACVNCVRWSQ NGQNLASGSD DKLIMIWRKS AGSSGVFGTG GMQKNHESWK CFYTLRGHDG DVLDLAWSPN DVYLASCSID NTVIIWDAQA FPHSVATLKG HTGLVKGVSW DPLGRFLASQ SDDRSIKIWN TMNWSLSHTI TEPFEECGGT THILRLSWSP DGQYLVSAHA MNGGGPTAQI IEREGWKCDK DFVGHRKAVT CVRFHNSILS RQENDGSPSK PLQYCCLAVG SRDRSLSVWM TALQRPMVVI HELFNASILD LTWGPQECLL MACSVDGSIA CLKFTEEELG KAISEEEQNA IIRKMYGKNY VNGLGKSAPV LEHPQRLLLP QGDKPTKFPL SNNNEANQRP ISKQTETRTK DGKRRITPMF IPLHEDGPTS LSMNIVSSSG SSTTALTSCS AAIGTLPAAA PTESAATPLM PLEPLVSKID LGRLDSRLKT QPASQRRQSL PFDPGQSNEL LRTPRLEEHQ SSTCSPSNLN VTATGKSEFV KAALDYRLHV SNGHLKTQHG MLAKVTASDS KEMLWEFYVG SPLVNLNLCE KYAMLCSLDG SMRLISMETG CPVFPAISLT SSAVHCAFSP DNSLVGVLTE CGLLRIWDIA KKVVSLAAGC LELLNKHGTA AQFSVTNQGM PLIGFPSGNS YSYSTSLQSW LVLATKDAIM YHGIRGTLPR DMDQMQQKFP LLSMQASSQN YFSFTGSMEL RHSESWQQCA KIRFIENQIK LCEALQSLDE LQHWHKMLTF QLATHGSEKR MRVFLDDLLS MPEPGISQFV PKLELMQCVL DTLKPHSEWN RLHSEYTELL KECKSERQKD IFATPAPPQQ KTASSAGSSP RSGEATGEEV TEKDGATAVA AAVVAGSRMA VTTGTSTTTT TTASSSLSSS GSSSSTSGSG SSSSSSSTSS LSVPQPAPSL SPEIQTLDSP TVCIDDEILS ASSSLPPLDT SPVEVSPAST SGGAASTSPA ASVAGSAPVS SSKTDQT // ID HLES_DROME STANDARD; PRT; 1077 AA. AC Q02308; Q9VDK0; Q9VDK1; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Hairless protein. GN H OR CG5460. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=92387549; PubMed=1516831; RA Bang A.G., Posakony J.W.; RT "The Drosophila gene Hairless encodes a novel basic protein that RT controls alternative cell fates in adult sensory organ development."; RL Genes Dev. 6:1752-1769(1992). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=93041287; PubMed=1419850; RA Maier D., Stumm G., Kuhn K., Preiss A.; RT "Hairless, a Drosophila gene involved in neural development, encodes RT a novel, serine rich protein."; RL Mech. Dev. 38:143-156(1992). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: IS A POTENT ANTAGONIST OF NEUROGENIC GENE ACTIVITY CC DURING SENSORY ORGAN DEVELOPMENT. THE EXPRESSION OF DISTINCT CELL CC FATES BY THE TRICHOGEN (SHAFT) / TORMOGEN (SOCKET) SISTER CELL CC PAIR DEPENDS ON THE LEVEL OF H ACTIVITY. A CERTAIN THRESHOLD LEVEL CC OF H ACTIVITY IS REQUIRED, BELOW WHICH BOTH SISTER CELLS ADOPT THE CC TORMOGEN FATE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q02308-1; Sequence=Displayed; CC Name=2; CC IsoId=Q02308-2; Sequence=VSP_006952; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: OVARY, EMBRYOS, LARVAL AND PUPAL IMAGINAL CC DISCS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95192; AAA28607.1; ALT_INIT. DR EMBL; X67239; CAA47664.1; -. DR EMBL; AE003731; AAF55790.1; -. DR EMBL; AE003731; AAF55791.1; -. DR PIR; A44067; A44067. DR FlyBase; FBgn0001169; H. DR GO; GO:0003714; F:transcription co-repressor activity; IDA. DR GO; GO:0007219; P:N signaling pathway; NAS. DR GO; GO:0008052; P:sensory organ determination; IMP. KW Developmental protein; Nuclear protein; DNA-binding; KW Alternative splicing. FT DOMAIN 115 123 THR-RICH. FT DOMAIN 642 648 POLY-SER. FT DOMAIN 879 891 POLY-ALA. FT DOMAIN 937 946 POLY-ALA. FT DOMAIN 964 974 ALA-RICH. FT DOMAIN 979 1008 HIS/PRO-RICH (PRD MOTIF). FT VARSPLIC 1 18 Missing (in isoform 2). FT /FTId=VSP_006952. FT CONFLICT 151 151 S -> A (IN REF. 2). FT CONFLICT 680 680 S -> F (IN REF. 3). FT CONFLICT 702 703 QH -> LL (IN REF. 2). FT CONFLICT 891 891 A -> R (IN REF. 2). FT CONFLICT 964 967 AAVA -> RLLP (IN REF. 2). FT CONFLICT 974 974 MISSING (IN REF. 2). SQ SEQUENCE 1077 AA; 111039 MW; A94BF1A27579E2F1 CRC64; MALLNDVTSV AECNRQTTMT DEHKSNINSN SSHSSNNNNN GSSSNNDNNS NDDAASSSNS KNNNTSNESS HSNNNTSSII AEAAAKFLLK NGLNGSSSTS YPPLPPPLPA NLSRTTTPTT TTTPSSSSST ASNGFLPHAK TPKSSSIMAA SAAVAASVVG ATASKPTIDV LGGVLDYSSL GGAATGSLPT TAVVAAAAGT AKIGKGSNSG GSFDMGRTPI STHGNNSWGG YGGRLQFFKD GKFILELARS KDGDKSGWVS VTRKTFRPPS AATSATVTPT SAVTTAYPKN ENSTSLSFSD DNSSIQSSPW QRDQPWKQSR PRRGISKELS LFFHRPRNST LGRAALRTAA RKRRRPHEPL TTSEDQQPIF ATAIKAENGD DTLKAEAAEA VEIENVAVAD TTTNEIKIEK PDTIKGEDDA ERLEKEPKKA VSDDSESKEA SPGQQVEPQP KDETVDVEMK MNTSEDEEPM TELPRITNAV NGDLNGDLKA SIGKPKSKPK PKAKLSSIIQ KLIDSVPARL EQMSKTSAVI ASTTTSSDRI GGGLSHALTH KVSPPSSATA AGRLVEYHTQ HVSPRKRILR EFEKVSLEDN GCVNNGSGGA SSGGAGGKRS RAKGTSTSSP AGKASPMNLA PPQGKPSPSP GSSSSSTSPA TLSTQPTRLN SSYSIHSLLG GSSGSGSSSS SSSGKKCGDH PAAIISNVHH PQHSMYQPSS SSYPRALLTS PKSPDVSGSN GGGGKSPSHT GTKKRSPPYS AGSPVDYGHS FYRDPYAGAG RPSTSGSASQ DLSPPRSSPA SPATTPRTVP KKTASIRREF ASPSASSSSC PSPGDRSASP PERRHMQQQP HLQRSSPLHY YMYPPPPQVN GNGSAGSPTS APPTSNSSAA AVAAAAAAAA AYIPSPSIYN PYISTLAALR HNPLWMHHYQ TGASPLLSPH PQPGGSAAAA AAAAAARLSP QSAYHAFAYN GVGAAVAAAA AAAAFGQPAP SPHTHPHLAH PHQHPHPAAL TTHHSPAHLA TPKLTDSSTD QMSATSSHRT ASTSPSSSSA SASSSAATSG ASSSAMFHTS SLRNEQSSDL PLNLSKH // ID HMAA_DROME STANDARD; PRT; 590 AA. AC P29555; Q9VER1; DT 01-APR-1993 (Rel. 25, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein abdominal-A. GN ABD-A OR CG10325. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95396803; PubMed=7667301; RA Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D., RA Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.; RT "Complete sequence of the bithorax complex of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORM ABD-A1). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 261-590 FROM N.A. RX MEDLINE=91071585; PubMed=1979297; RA Karch F., Bender W., Weiffenbach B.; RT "abdA expression in Drosophila embryos."; RL Genes Dev. 4:1573-1587(1990). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC REQUIRED FOR SEGMENTAL IDENTITY OF THE SECOND THROUGH EIGHTH CC ABDOMINAL SEGMENTS. ONCE A PATTERN OF ABD-A EXPRESSION IS TURNED CC ON IN A GIVEN PARASEGMENT, IT REMAINS ON THE MORE POSTERIOR CC PARASEGMENT, SO THAT THE COMPLEX PATTERN OF EXPRESSION IS BUILT UP CC IN THE SUCCESSIVE PARASEGMENTS. APPEARS TO REPRESS EXPRESSION OF CC UBX WHENEVER THEY APPEAR IN THE SAME CELL, BUT ABD-A IS REPRESSED CC BY ABDB ONLY IN THE EIGHT AND NINTH ABDOMINAL SEGMENTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Abd-A2; CC IsoId=P29555-1; Sequence=Displayed; CC Name=Abd-A1; CC IsoId=P29555-2; Sequence=VSP_002394; CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U31961; AAA84405.1; -. DR EMBL; U31961; AAA84406.1; -. DR EMBL; X54453; CAA38321.1; -. DR EMBL; AE003715; AAF55359.1; -. DR PIR; A35915; A35915. DR HSSP; P02833; 9ANT. DR TRANSFAC; T01992; -. DR FlyBase; FBgn0000014; abd-A. DR GO; GO:0007438; P:oenocyte development; IMP. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; FALSE_NEG. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Alternative splicing. FT DOMAIN 35 50 POLY-ALA. FT DOMAIN 51 119 SER-RICH. FT DOMAIN 136 139 POLY-GLN (OPA-REPEAT). FT DOMAIN 144 147 POLY-GLN (OPA-REPEAT). FT DOMAIN 160 165 POLY-GLN (OPA-REPEAT). FT DOMAIN 172 177 POLY-ALA. FT DOMAIN 240 250 POLY-ALA. FT SITE 368 373 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 398 457 HOMEOBOX. FT DOMAIN 425 428 POLY-ARG. FT DOMAIN 491 518 POLY-GLN (OPA-REPEAT). FT VARSPLIC 1 260 Missing (in isoform Abd-A1). FT /FTId=VSP_002394. SQ SEQUENCE 590 AA; 62409 MW; FF080CC2D71ECA82 CRC64; MSKFVFDSML PKYPQFQPFI SSHHLTTTPP NSSSAAVAAA LAAAAASASA SVSASSSSNN NSSNTIAGSN TSNTNNSSSS PSSSSNNNSN LNLSGGSLSP SHLSQHLGQS PHSPVSSSSP FQQHHPQVQQ QHLNHQQQQH LHHQQQQHHH QYSSLSAALQ LQQQQHHISK LAAAAVASHG HAHQQLLLTP PSAGNSQAGD SSCSPSPSAS GSSSLHRSLN DNSPGSASAS ASASAASSVA AAAAAAAAAA SSSFAIPTSK MYPYVSNHPS SHGGLSGMAG FTGLEDKSCS RYTDTVMNSY QSMSVPASAS AQFAQFYQHA TAAASAVSAA SAGAIGVDSL GNACTQPASG VMPGAGGAGG AGIADLPRYP WMTLTDWMGS PFERVVCGDF NGPNGCPRRR GRQTYTRFQT LELEKEFHFN HYLTRRRRIE IAHALCLTER QIKIWFQNRR MKLKKELRAV KEINEQARRD REEQEKMKAQ ETMKSAQQNK QVQQQQQQQQ QQQQQQQQQH QQQQQQPQDH HSIIAHNPGH LHHSVVGQND LKLGLGMGVG VGVGGIGPGI GGGLGGNLGM MSALDKSNHD LLKAVSKVNS // ID HMAB_DROME STANDARD; PRT; 493 AA. AC P09087; Q9VEQ8; Q9VEQ9; DT 01-NOV-1988 (Rel. 09, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein abdominal-B (P3) (Infraabdominal 7) (IAB-7) (PH189). GN ABD-B OR CG10291. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS M AND R). RC STRAIN=Canton-S; RX MEDLINE=95396803; PubMed=7667301; RA Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D., RA Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.; RT "Complete sequence of the bithorax complex of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORM R), AND CHARACTERIZATION. RC TISSUE=Embryo; RX MEDLINE=89030618; PubMed=2903049; RA Delorenzi M., Ali N., Saari G., Henry C., Wilcox M., Bienz M.; RT "Evidence that the Abdominal-B r element function is conferred by a RT trans-regulatory homeoprotein."; RL EMBO J. 7:3223-3231(1988). RN [3] RP SEQUENCE FROM N.A. (ISOFORM M), AND CHARACTERIZATION. RC TISSUE=Embryo, and Pupae; RX MEDLINE=90108690; PubMed=2575066; RA Celniker S.E., Keelan D.J., Lewis E.B.; RT "The molecular genetics of the bithorax complex of Drosophila: RT characterization of the products of the Abdominal-B domain."; RL Genes Dev. 3:1424-1436(1989). RN [4] RP SEQUENCE FROM N.A. (ISOFORM M). RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=90152341; PubMed=2482824; RA Zavortink M., Sakonju S.; RT "The morphogenetic and regulatory functions of the Drosophila RT Abdominal-B gene are encoded in overlapping RNAs transcribed from RT separate promoters."; RL Genes Dev. 3:1969-1981(1989). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS M AND R). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP SEQUENCE OF 387-447 FROM N.A. RX MEDLINE=86079516; PubMed=2416463; RA Regulski M., Harding K., Kostriken R., Karch F., Levine M., RA McGinnis W.; RT "Homeo box genes of the Antennapedia and bithorax complexes of RT Drosophila."; RL Cell 43:71-80(1985). RN [7] RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=89030619; PubMed=2903050; RA Kuziora M.A., McGinnis W.; RT "Different transcripts of the Drosophila Abd-B gene correlate with RT distinct genetic sub-functions."; RL EMBO J. 7:3233-3244(1988). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=M; Synonyms=Morphogenetic, Abd-BI; CC IsoId=P09087-1; Sequence=Displayed; CC Name=R; Synonyms=Regulatory, Abd-BII; CC IsoId=P09087-2; Sequence=VSP_002396; CC -!- TISSUE SPECIFICITY: BOTH ISOFORMS ARE EXPRESSED IN ECTODERMAL AND CC MESODERMAL TISSUES AND CENTRAL NERVOUS SYSTEM OF FOURTH TO NINTH CC EMBRYONIC ABDOMINAL SEGMENTS. LATER IN EMBRYOGENESIS, EXPRESSION CC IS SEEN IN VISCERAL MESODERM SURROUNDING HINDGUT AND IN TWO CC MALPIGHIAN TUBULES. CC -!- DEVELOPMENTAL STAGE: HIGHLY EXPRESSED DURING EMBRYOGENESIS, LOWER CC EXPRESSION IN LARVAE, PUPAE AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE ABD-B HOMEOBOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U31961; AAA84402.1; -. DR EMBL; U31961; AAA84403.1; -. DR EMBL; M21173; AAA28400.1; -. DR EMBL; X16134; CAA34260.1; -. DR EMBL; X51663; CAB57859.1; -. DR EMBL; AE003715; AAF55362.1; -. DR EMBL; AE003715; AAF55363.1; -. DR EMBL; X15080; CAA33187.1; -. DR PIR; A32584; A32584. DR PIR; A34220; A34220. DR PIR; B24780; B24780. DR HSSP; P02834; 1B8I. DR TRANSFAC; T01476; -. DR FlyBase; FBgn0000015; Abd-B. DR GO; GO:0007483; P:genital disc metamorphosis; NAS. DR GO; GO:0007385; P:specification of segmental identity, abdomen; NAS. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Alternative splicing. FT DOMAIN 1 192 GLN-RICH. FT DOMAIN 306 311 POLY-ALA. FT DNA_BIND 387 446 HOMEOBOX. FT DOMAIN 454 458 POLY-ASN. FT VARSPLIC 1 223 Missing (in isoform R). FT /FTId=VSP_002396. FT CONFLICT 15 15 Q -> H (IN REF. 4). FT CONFLICT 74 74 MISSING (IN REF. 3). FT CONFLICT 177 180 ASGA -> PVR (IN REF. 3). FT CONFLICT 317 318 ER -> DG (IN REF. 3). SQ SEQUENCE 493 AA; 55096 MW; 55A11B5E97983A5F CRC64; MQQHHLQQQQ QQQQQQEQQH LQEQQQHLQQ LHHHAHHHLP QPLHTTSHHH SAHPHLQQQQ QQQQHAVVAS SPSSVLQQQQ QQSTPTTHST PTHAVMYEDP PPVPLVAVQQ QHLPAPQQQQ QLQQQQQQQQ QQLATTPVAG ALSPAQTPTG PSAQQQQHLT SPHHQQLPQQ QTPNSVASGA SSNLQQQQQQ QNAAVAPGQT QIVAPTTASV SPSSVSSQKE DINMSIQLAP LHIPAIRAGP GFETDTSAAV KRHTAHWAYN DEGFNQHYGS GYYDRKHMFA YPYPETQFPV GQYWGPNYRP DQTTSAAAAA AYMNEAERHV SAAARQSVEG TSTSSYEPPT YSSPGGLRGY PSENYSSSGA SGGLSVGAVG PCTPNPGLHE WTGQVSVRKK RKPYSKFQTL ELEKEFLFNA YVSKQKRWEL ARNLQLTERQ VKIWFQNRRM KNKKNSQRQA NQQNNNNNSS SNHNHAQATQ QHHSGHHLNL SLNMGHHAAK MHQ // ID HMAN_DROME STANDARD; PRT; 378 AA. AC P02833; Q95SZ6; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeotic antennapedia protein. GN ANTP OR BG:DS07700.1 OR CG1028. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RA Schneuwly S., Kuroiwa A., Baumgartner P., Gehring W.J.; RT "Structural organization and sequence of the homeotic gene RT Antennapedia of Drosophila melanogaster."; RL EMBO J. 5:733-739(1986). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Oregon-R; TISSUE=Embryo, Larva, and Pupae; RX MEDLINE=87089828; PubMed=2879222; RA Stroeher V.L., Jorgensen E.M., Garber R.L.; RT "Multiple transcripts from the Antennapedia gene of Drosophila RT melanogaster."; RL Mol. Cell. Biol. 6:4667-4675(1986). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=87089829; PubMed=2879223; RA Laughon A., Boulet A.M., Bermingham J.R. Jr., Laymon R.A., Scott M.P.; RT "Structure of transcripts from the homeotic Antennapedia gene of RT Drosophila melanogaster: two promoters control the major RT protein-coding region."; RL Mol. Cell. Biol. 6:4676-4689(1986). RN [4] RP SEQUENCE FROM N.A. (ISOFORM 1). RA Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., RA Palazzolo M.J.; RT "Complete sequence of the Antennapedia complex of Drosophila."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [7] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [8] RP SEQUENCE OF 296-364 FROM N.A. RX MEDLINE=84248068; PubMed=6330741; RA Scott M.P., Weiner A.J.; RT "Structural relationships among genes that control development: RT sequence homology between the Antennapedia, Ultrabithorax, and fushi RT tarazu loci of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4115-4119(1984). RN [9] RP SEQUENCE OF 296-378 FROM N.A. RX MEDLINE=84205674; PubMed=6327065; RA McGinnis W., Garber R.L., Wirz J., Kuroiwa A., Gehring W.J.; RT "A homologous protein-coding sequence in Drosophila homeotic genes RT and its conservation in other metazoans."; RL Cell 37:403-408(1984). RN [10] RP SEQUENCE OF 297-357 FROM N.A. RX MEDLINE=86079516; PubMed=2416463; RA Regulski M., Harding K., Kostriken R., Karch F., Levine M., RA McGinnis W.; RT "Homeo box genes of the Antennapedia and bithorax complexes of RT Drosophila."; RL Cell 43:71-80(1985). RN [11] RP MUTANT ANALYSIS. RX MEDLINE=87144589; PubMed=3821869; RA Schneuwly S., Klemenz R., Gehring W.J.; RT "Redesigning the body plan of Drosophila by ectopic expression of the RT homoeotic gene Antennapedia."; RL Nature 325:816-818(1987). RN [12] RP STRUCTURE BY NMR OF HOMEOBOX. RX MEDLINE=90317820; PubMed=2164583; RA Billeter M., Qian Y.-Q., Otting G., Mueller M., Gehring W.J., RA Wuethrich K.; RT "Determination of the three-dimensional structure of the Antennapedia RT homeodomain from Drosophila in solution by 1H nuclear magnetic RT resonance spectroscopy."; RL J. Mol. Biol. 214:183-197(1990). RN [13] RP STRUCTURE BY NMR OF HOMEOBOX. RX MEDLINE=94087721; PubMed=7903397; RA Qian Y.-Q., Otting G., Billeter M., Mueller M., Gehring W.J., RA Wuethrich K.; RT "Nuclear magnetic resonance spectroscopy of a DNA complex with the RT uniformly 13C-labeled Antennapedia homeodomain and structure RT determination of the DNA-bound homeodomain."; RL J. Mol. Biol. 234:1070-1083(1993). RN [14] RP STRUCTURE BY NMR OF HOMEOBOX. RX MEDLINE=94087722; PubMed=7903398; RA Billeter M., Qian Y.-Q., Otting G., Mueller M., Gehring W.J., RA Wuethrich K.; RT "Determination of the nuclear magnetic resonance solution structure RT of an Antennapedia homeodomain-DNA complex."; RL J. Mol. Biol. 234:1084-1097(1993). RN [15] RP STRUCTURE BY NMR OF 279-363. RX MEDLINE=93066318; PubMed=1359544; RA Qian Y.-Q., Otting G., Furukubo-Tokunaga K., Affolter M., RA Gehring W.J., Wuethrich K.; RT "NMR structure determination reveals that the homeodomain is RT connected through a flexible linker to the main body in the RT Drosophila Antennapedia protein."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10738-10742(1992). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 297-356. RX MEDLINE=98363212; PubMed=9699632; RA Fraenkel E., Pabo C.O.; RT "Comparison of X-ray and NMR structures for the Antennapedia RT homeodomain-DNA complex."; RL Nat. Struct. Biol. 5:692-697(1998). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT REGULATES SEGMENTAL CC IDENTITY IN THE MESOTHORAX. PROVIDES CELLS WITH SPECIFIC CC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=A, B, I, J; CC IsoId=P02833-1; Sequence=Displayed; CC Name=2; Synonyms=H; CC IsoId=P02833-2; Sequence=VSP_008097, VSP_008098; CC Note=No experimental confirmation available; CC -!- MISCELLANEOUS: LOSS OF ANTP RESULTS IN ALTERED DEVELOPMENT OF THE CC EMBRYONIC THORACIC SEGMENTS. OVEREXPRESSION CAN CAUSE ANTENNAE TO CC BE TRANSFORMED INTO LEGS. CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. CC -!- CAUTION: REF.5 (AAN13353) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03790; CAA27417.1; -. DR EMBL; X03791; CAA27417.1; JOINED. DR EMBL; M20704; AAA70214.1; -. DR EMBL; M20705; AAA70216.1; -. DR EMBL; AE001572; AAD19793.1; -. DR EMBL; AE003673; AAG22205.3; -. DR EMBL; AE003673; AAN13353.2; ALT_SEQ. DR EMBL; AY060407; AAL25446.1; -. DR EMBL; M14496; AAA28376.1; -. DR EMBL; K01948; AAA28373.1; ALT_SEQ. DR EMBL; M12009; AAA79241.1; -. DR PIR; A23450; A25399. DR PDB; 1AHD; 31-OCT-93. DR PDB; 1HOM; 31-OCT-93. DR PDB; 1SAN; 30-APR-94. DR PDB; 2HOA; 31-OCT-93. DR PDB; 9ANT; 18-NOV-98. DR TRANSFAC; T00026; -. DR FlyBase; FBgn0000095; Antp. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0009948; P:anterior/posterior axis specification; IMP. DR GO; GO:0007384; P:specification of segmental identity, thorax; IMP. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Repeat; Alternative splicing; 3D-structure. FT DOMAIN 76 81 GLN-RICH (OPA-REPEAT). FT DOMAIN 110 155 GLN-RICH (OPA-REPEAT). FT SITE 283 288 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 297 356 HOMEOBOX. FT VARSPLIC 296 297 ER -> GK (in isoform 2). FT /FTId=VSP_008097. FT VARSPLIC 298 378 Missing (in isoform 2). FT /FTId=VSP_008098. FT CONFLICT 300 300 G -> E (IN REF. 10). FT HELIX 306 316 FT TURN 317 318 FT HELIX 324 334 FT TURN 335 335 FT HELIX 338 354 SQ SEQUENCE 378 AA; 42761 MW; D653232A8622D055 CRC64; MTMSTNNCES MTSYFTNSYM GADMHHGHYP GNGVTDLDAQ QMHHYSQNAN HQGNMPYPRF PPYDRMPYYN GQGMDQQQQH QVYSRPDSPS SQVGGVMPQA QTNGQLGVPQ QQQQQQQQPS QNQQQQQAQQ APQQLQQQLP QVTQQVTHPQ QQQQQPVVYA SCKLQAAVGG LGMVPEGGSP PLVDQMSGHH MNAQMTLPHH MGHPQAQLGY TDVGVPDVTE VHQNHHNMGM YQQQSGVPPV GAPPQGMMHQ GQGPPQMHQG HPGQHTPPSQ NPNSQSSGMP SPLYPWMRSQ FGKCQERKRG RQTYTRYQTL ELEKEFHFNR YLTRRRRIEI AHALCLTERQ IKIWFQNRRM KWKKENKTKG EPGSGGEGDE ITPPNSPQ // ID HMBC_DROME STANDARD; PRT; 494 AA. AC P09081; DT 01-NOV-1988 (Rel. 09, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeotic bicoid protein (PRD-4). GN BCD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=89005064; PubMed=2901954; RA Berleth T., Burri M., Thoma G., Bopp D., Richstein S., Frigerio G., RA Noll M., Nuesslein-Volhard C.; RT "The role of localization of bicoid RNA in organizing the anterior RT pattern of the Drosophila embryo."; RL EMBO J. 7:1749-1756(1988). RN [2] RP SEQUENCE OF 86-156 FROM N.A. RX MEDLINE=87051745; PubMed=2877746; RA Frigerio G., Burri M., Bopp D., Baumgartner S., Noll M.; RT "Structure of the segmentation gene paired and the Drosophila PRD RT gene set as part of a gene network."; RL Cell 47:735-746(1986). RN [3] RP POSSIBLE RNA-BINDING DOMAIN. RX MEDLINE=89324068; PubMed=2752425; RA Rebagliati M.; RT "An RNA recognition motif in the bicoid protein."; RL Cell 58:231-232(1989). CC -!- FUNCTION: BICOID IS A POLARITY PROTEIN THAT PROVIDES POSITIONAL CC CUES FOR THE DEVELOPMENT OF HEAD AND THORACIC SEGMENTS. BCD CC REGULATES THE EXPRESSION OF ZYGOTIC GENES, POSSIBLY THROUGH ITS CC HOMEODOMAIN, AND INHIBITS THE ACTIVITY OF OTHER MATERNAL GENE CC PRODUCTS. IT IS POSSIBLE THAT BCD ALSO BINDS RNA. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P09081-1; Sequence=Displayed; CC Name=2; CC IsoId=P09081-2; Sequence=VSP_002234; CC Name=3; CC IsoId=P09081-3; Sequence=VSP_002235; CC -!- TISSUE SPECIFICITY: MATERNAL EXPRESSION IS AN ANTERIOR CAP CC CONCENTRATED IN THE CORTICAL CYTOPLASM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. BICOID CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14458; CAA32627.1; -. DR EMBL; X14459; CAB37631.1; -. DR EMBL; M14549; AAA28385.1; -. DR EMBL; X14460; CAA32629.1; -. DR EMBL; X07870; CAA30720.1; -. DR EMBL; K03517; AAA28391.1; -. DR PIR; S00835; WJFFBC. DR HSSP; P02836; 2HDD. DR TRANSFAC; T00063; -. DR FlyBase; FBgn0000166; bcd. DR GO; GO:0016015; F:morphogen activity; NAS. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; NAS. DR GO; GO:0006357; P:regulation of transcription from Pol II pro...; NAS. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation; RNA-binding; Alternative splicing. FT DOMAIN 12 40 HIS/PRO-RICH (PRD MOTIF). FT DNA_BIND 97 156 HOMEOBOX. FT DOMAIN 260 294 GLN-RICH (OPA REPEAT). FT DOMAIN 433 440 RNA-BINDING (BY SIMILARITY). FT VARSPLIC 81 85 Missing (in isoform 2). FT /FTId=VSP_002234. FT VARSPLIC 56 400 Missing (in isoform 3). FT /FTId=VSP_002235. FT CONFLICT 298 298 F -> S (IN REF. 1; CAB37631). SQ SEQUENCE 494 AA; 54493 MW; 561D84A2CF711FD3 CRC64; MAQPPPDQNF YHHPLPHTHT HPHPHSHPHP HSHPHPHHQH PQLQLPPQFR NPFDLLFDER TGAINYNYIR PYLPNQMPKP DVFPSEELPD SLVMRRPRRT RTTFTSSQIA ELEQHFLQGR YLTAPRLADL SAKLALGTAQ VKIWFKNRRR RHKIQSDQHK DQSYEGMPLS PGMKQSDGDP PSLQTLSLGG GATPNALTPS PTPSTPTAHM TEHYSESFNA YYNYNGGHNH AQANRHMHMQ YPSGGGPGPG STNVNGGQFF QQQQVHNHQQ QLHHQGNHVP HQMQQQQQQA QQQQYHHFDF QQKQASACRV LVKDEPEADY NFNSSYYMRS GMSGATASAS AVARGAASPG SEVYEPLTPK NDESPSLCGI GIGGPCAIAV GETEAADDMD DGTSKKTTLQ ILEPLKGLDK SCDDGSSDDM STGIRALAGT GNRGAAFAKF GKPSPPQGPQ PPLGMGGVAL GESNQYQCTM DTIMQAYNPH RNAAGNSQFA YCFN // ID HMBP_DROME STANDARD; PRT; 382 AA. AC P22809; Q24254; Q9VDA6; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein bagpipe (NK-3). GN BAP OR BGP OR NK3 OR CG7902. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93321862; PubMed=8101173; RA Azpiazu N., Frasch M.; RT "Tinman and bagpipe: two homeo box genes that determine cell fates in RT the dorsal mesoderm of Drosophila."; RL Genes Dev. 7:1325-1340(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 95-288 FROM N.A. RX MEDLINE=90046666; PubMed=2573058; RA Kim Y., Nirenberg M.; RT "Drosophila NK-homeobox genes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7716-7720(1989). CC -!- FUNCTION: INVOLVED IN THE DETERMINATION OF CELL FATES IN THE CC DORSAL MESODERM. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: IS EXPRESSED IN A SEGMENTED PATTERN IN CC VISCERAL MUSCLE AND IN A SUBSET OF CARDIAC MUSCLES. LOSS OF CC ACTIVITY RESULTS IN SEGMENTAL GAPS IN MIDGUT VISCERAL MUSCLE. CC -!- SIMILARITY: BELONGS TO THE NK-3 HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L17133; AAC37165.1; -. DR EMBL; AE003734; AAF55891.1; -. DR EMBL; M27291; AAA28618.1; -. DR PIR; C33976; C33976. DR HSSP; P22808; 1NK3. DR TRANSFAC; T02665; -. DR FlyBase; FBgn0004862; bap. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DNA_BIND 175 234 HOMEOBOX. FT CONFLICT 251 251 V -> I (IN REF. 1). SQ SEQUENCE 382 AA; 41993 MW; 49A8DFE19A2022B9 CRC64; MLNMESAGVS AAMAGLSKSL TTPFSINDIL TRSNPETRRM SSVDSEPEPE KLKPSSDRER SISKSPPLCC RDLGLYKLTQ PKEIQPSARQ PSNYLQYYAA AMDNNNHHHQ ATGTSNSSAA DYMQRKLAYF GSTLAAPLDM RRCTSNDSDC DSPPPLSSSP SESPLSHDGS GLSRKKRSRA AFSHAQVFEL ERRFAQQRYL SGPERSEMAK SLRLTETQVK IWFQNRRYKT KRKQIQQHEA ALLGASKRVP VQVLVREDGS TTYAHMAAPG AGHGLDPALI NIYRHQLQLA YGGLPLPQMQ MPFPYFYPQH KVPQPIPPPT QSSSFVTASS ASSSPVPIPI PGAVRPQRTP CPSPNGQMMS VESGAESVHS AAEDVDENVE ID // ID HMCA_DROME STANDARD; PRT; 472 AA. AC P09085; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Homeotic caudal protein. GN CAD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87102895; PubMed=2433048; RA Mlodzik M., Gehring W.J.; RT "Expression of the caudal gene in the germ line of Drosophila: RT formation of an RNA and protein gradient during early RT embryogenesis."; RL Cell 48:465-478(1987). RN [2] RP SEQUENCE OF 183-379 FROM N.A. RA Mlodzik M., Fjose A., Gehring W.J.; RT "Isolation of caudal, a Drosophila homeo box-containing gene with RT maternal expression, whose transcripts form a concentration gradient RT at the pre-blastoderm stage."; RL EMBO J. 4:2961-2969(1985). CC -!- FUNCTION: CAUDAL SHOWS MATERNAL AS WELL AS ZYGOTIC EXPRESSION CC DURING DROSOPHILA DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE CAUDAL HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M21070; AAA28409.1; -. DR EMBL; M21069; AAA28409.1; JOINED. DR EMBL; X03062; CAA26868.1; -. DR PIR; A26357; A26357. DR HSSP; P14653; 1B72. DR TRANSFAC; T00079; -. DR FlyBase; FBgn0000251; cad. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; KW Developmental protein; Nuclear protein. FT DOMAIN 80 86 POLY-HIS. FT DOMAIN 87 138 ALA/GLY/SER-RICH. FT DOMAIN 186 213 GLN-RICH. FT SITE 222 227 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 243 302 HOMEOBOX. FT CONFLICT 328 330 TKL -> ANV (IN REF. 1; AAA28409). FT CONFLICT 382 382 H -> N (IN REF. 1). SQ SEQUENCE 472 AA; 51306 MW; 0DF2DE2EC5D8CD7A CRC64; MELDAQLPPH AAEPQFLGDV DSSHAAHHAA AAHQMYYNSH HMFHSAAAAS AGEWHSPASS TADNFVQNVP TSAHQLMQQH HHHHAHASSS SASSGSSSSA GAPGAPQLNE TNSSIGVGGA GVGGGVGGAT DGGPGSAAPN HQQHIAEGLP SPPITVSGSE ISSPGAPTSA SSPHHHLAHH LSAVANNNNN NNNNNSPSTH NNNNNNNSVS NNNRTSPSKP PYFDWMKKPA YPAQPQPGKT RTKDKYRVVY TDFQRLELEK EYCTSRYITI RRKSELAQTL SLSERQVKIW FQNRRAKERT SNKKGSDPNV MGVGVQHADY SQLLDAKTKL EPGLHLSHSL AHSMNPMAAM NIPAMRLHPH LAAHSHSLAA VAAHSHQLQQ QHSAQMSLRA QWARSRCDTT IPVMRRAATV TTTWSPIIRC WVVASGWSRR RRRRRRRRRT TVRCVLQCSR SRLGLGLTLR SRSQTVSTEP KS // ID HMCU_DROME STANDARD; PRT; 2175 AA. AC P10180; Q9W3Q6; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein cut. GN CT OR CG11387. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88232956; PubMed=2897632; RA Blochlinger K., Bodmer R., Jack J., Jan L.Y., Jan Y.N.; RT "Primary structure and expression of a product from cut, a locus RT involved in specifying sensory organ identity in Drosophila."; RL Nature 333:629-635(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REGULATOR OF CELL FATE DECISIONS IN MULTIPLE LINEAGES. CC SPECIFICALLY, FUNCTIONS AS A DETERMINATION FACTOR THAT SPECIFIES CC SENSORY ORGAN IDENTITY IN PRECURSOR CELLS. PROBABLY ALSO INVOLVED CC IN CELL TYPE SPECIFICATION OF MALPIGHIAN TUBULES. IN ABSENCE OF CC CUT GENE EXTERNAL SENSORY ORGANS ARE TRANSFORMED INTO CHORDOTONAL CC ORGANS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: DETECTED IN MANY CELLS IN THE CENTRAL NERVOUS CC SYSTEM, ALL EXTERNAL SENSORY ORGANS, SOME PERIPHERAL NEURONS, AND CC IN THE NON-NEURAL CELLS OF THE SPIRACLES AND THE MALPIGHIAN CC TUBULES. CC -!- DEVELOPMENTAL STAGE: CELL-SPECIFIC PATTERN OF EXPRESSION. BROADLY CC EXPRESSED DURING EMBRYONIC DEVELOPMENT. CC -!- DOMAIN: ASN AT POSITION 47 OF THE HOMEOBOX MAY PARTICIPATE IN CC REGULATING DNA-BINDING ACTIVITY BY PROMOTING HOMO- AND CC HETERODIMERIZATION. CC -!- SIMILARITY: BELONGS TO THE CUT HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- SIMILARITY: CONTAINS 3 CUT DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07985; CAA30794.1; -. DR EMBL; AE003441; AAF46264.2; -. DR PIR; S03170; S03170. DR TRANSFAC; T02004; -. DR FlyBase; FBgn0004198; ct. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0008587; P:wing margin morphogenesis; NAS. DR InterPro; IPR007108; Cut_homeo. DR InterPro; IPR003350; Hmoeo_CUT. DR InterPro; IPR001356; Homeobox. DR Pfam; PF02376; CUT; 3. DR Pfam; PF00046; homeobox; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; KW Developmental protein; Nuclear protein; Repeat; Coiled coil. FT DOMAIN 265 343 COILED COIL (POTENTIAL). FT DOMAIN 433 499 COILED COIL (POTENTIAL). FT DNA_BIND 798 964 CUT 1. FT DOMAIN 1056 1161 COILED COIL (POTENTIAL). FT DNA_BIND 1329 1417 CUT 2. FT DOMAIN 1463 1522 COILED COIL (POTENTIAL). FT DNA_BIND 1608 1695 CUT 3. FT DNA_BIND 1745 1804 HOMEOBOX. FT DOMAIN 194 210 ALA/GLN-RICH. FT DOMAIN 235 243 ALA-RICH. FT DOMAIN 271 293 ASP/GLU-RICH (ACIDIC). FT DOMAIN 384 428 ASN-RICH. FT DOMAIN 547 554 ASP/GLU-RICH (ACIDIC). FT DOMAIN 574 584 ASP/GLU-RICH (ACIDIC). FT DOMAIN 616 630 ALA-RICH. FT DOMAIN 665 699 HIS/GLN-RICH (OPA-REPEAT). FT DOMAIN 2004 2014 ALA-RICH. FT DOMAIN 2071 2077 ASP/GLU-RICH (ACIDIC). FT DOMAIN 2124 2136 ALA/PRO-RICH. SQ SEQUENCE 2175 AA; 233628 MW; 08BF80C4861BD0AB CRC64; MQPTLPQAAG TADMDLTAVQ SINDWFFKKE QIYLLAQFWQ QRATLAEKEV NTLKEQLSTG NPDSNLNSEN SDTAAAAATA AAVAAVVAGA TATNDIEDEQ QQQLQQTASG GILESDSDKL LNSSIVAAAI TLQQQNGSNL LANTNTPSPS PPLLSAEQQQ QLQSSLQQSG GVGGACLNPK LFFNHAQQMM MMEAAAAAAA AALQQQQQQQ SPLHSPANEV AIPTEQPAAT VATGAAAAAA AAATPIATGN VKSGSTTSNA NHTNSNNSHQ DEEELDDEEE DEEEDEDEDD EEENASMQSN ADDMELDAQQ ETRTEPSATT QQQHQQQDTE DLEENKDAGE ASLNVSNNHN TTDSNNSCSR KNNNGGNESE QHVASSAEDD DCANNNTNTS NNNNTSNTAT SNTNNNNNNN SSSGNSEKRK KKNNNNNNGQ PAVLLAAKDK EIKALLDELQ RLRAQEQTHL VQIQRLEEHL EVKRQHIIRL EARLDKQQIN EALAEATALS AAASTNNNNN SQSSDNNKKL NTAAERPMDA SSNADLPEST KAPVPAEDDE EDEDQAMLVD SEEAEDKPED SHHDDDEDED EDREAVNATT TDSNELKIKK EQHSPLDLNV LSPNSAIAAA AAAAAAAACA NDPNKFQALL IERTKALAAE ALKNGASDAL SEDAHHQQQQ HHQQQHQHQQ QHHQQQHLHQ QHHHHLQQQP NSGSNSNPAS NDHHHGHHLH GHGLLHPSSA HHLHHQTTES NSNSSTPTAA GNNNGSNNSS SNTNANSTAQ LAASLASTLN GTKSLMQEDS NGLAAVAMAA HAQHAAALGP GFLPGLPAFQ FAAAQVAAGG DGRGHYRFAD SELQLPPGAS MAGRLGESLI PKGDPMEAKL QEMLRYNMDK YANQALDTLH ISRRVRELLS VHNIGQRLFA KYILGLSQGT VSELLSKPKP WDKLTEKGRD SYRKMHAWAC DDNAVMLLKS LIPKKDSGLP QYAGRGAGGA GGDDSMSEDR IAHILSEASS LMKQSSVAQH REQERRSHGG EDSHSNEDSK SPPQSCTSPF FKVENQLKQH QHLNPEQAAA QQREREREQR EREQQQRLRH DDQDKMARLY QELIARTPRE TAFPSFLFSP SLFGGAAGMP GAASNAFPAM ADENMRHVFE REIAKLQQHQ QQQQAAQAQA QFPNFSSLMA LQQQVLNGAQ DLSLAAAAAK DIKLNGQRSS LEHSAGSSSC SKDGERDDAY PSSLHGRKSE GGGTPAPPAP PSGPGTGAGA PPTAAPPTGG ASSNSAAPSP LSNSILPPAL SSQGEEFAAT ASPLQRMASI TNSLITQPPV TPHHSTPQRP TKAVLPPITQ QQFDMFNNLN TEDIVRRVKE ALSQYSISQR LFGESVLGLS QGSVSDLLAR PKPWHMLTQK GREPFIRMKM FLEDENAVHK LVASQYKIAP EKLMRTGSYS GSPQMPQGLA SKMQAASLPM QKMMSELKLQ EPAQAQHLMQ QMQAAAMSAA MQQQQVAQAQ QQAQQAQQAQ QHLQQQAQQH LQQQQHLAQQ QHPHQQHHQA AAAAAALHHQ SMLLTSPGLP PQHAISLPPS AGGAQPGGPG GNQGSSNPSN SEKKPMLMPV HGTNAMRSLH QHMSPTVYEM AALTQDLDTH DITTKIKEAL LANNIGQKIF GEAVLGLSQG SVSELLSKPK PWHMLSIKGR EPFIRMQLWL SDANNVERLQ LLKNERREAS KRRRSTGPNQ QDNSSDTSSN DTNDFYTSSP GPGSVGSGVG GAPPSKKQRV LFSEEQKEAL RLAFALDPYP NVGTIEFLAN ELGLATRTIT NWFHNHRMRL KQQVPHGPAG QDNPIPSRES TSATPFDPVQ FRILLQQRLL ELHKERMGMS GAPIPYPPYF AAAAILGRSL AGIPGAAAAA GAAAAAAAVG ASGGDELQAL NQAFKEQMSG LDLSMPTLKR ERSDDYQDDL ELEGGGHNLS DNESLEGQEP EDKTTDYEKV LHKSALAAAA AYMSNAVRSS RRKPAAPQWV NPAGAVTNPS AVVAAVAAAA AAAADNERII NGVCVMQASE YGRDDTDSNK PTDGGNDSDH EHAQLEIDQR FMEPEVHIKQ EEDDDEEQSG SVNLDNEDNA TSEQKLKVIN EEKLRMVRVR RLSSTGGGSS EEMPAPLAPP PPPPAASSSI VSGESTTSSS SSSNTSSSTP AVTTAAATAA AGWNY // ID HMDF_DROME STANDARD; PRT; 590 AA. AC P07548; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Homeotic deformed protein. GN DFD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Regulski M., McGinnis N., Chadwick R., McGinnis W.; RT "Developmental and molecular analysis of Deformed: a homeotic gene RT controlling Drosophila head development."; RL EMBO J. 6:767-777(1987). RN [2] RP SEQUENCE OF 163-590 FROM N.A. RX MEDLINE=86162966; PubMed=3938363; RA Laughon A., Carroll S.B., Storfer F.A., Riley P.D., Scott M.P.; RT "Common properties of proteins encoded by the Antennapedia complex RT genes of Drosophila melanogaster."; RL Cold Spring Harb. Symp. Quant. Biol. 50:253-262(1985). RN [3] RP SEQUENCE OF 366-485 FROM N.A. RX MEDLINE=86079516; PubMed=2416463; RA Regulski M., Harding K., Kostriken R., Karch F., Levine M., RA McGinnis W.; RT "Homeo box genes of the Antennapedia and bithorax complexes of RT Drosophila."; RL Cell 43:71-80(1985). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- FUNCTION: HOMEOTIC PROTEIN CONTROLLING DROSOPHILA HEAD CC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. DEFORMED CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05136; CAA28782.1; -. DR EMBL; M13373; AAA28375.1; -. DR PIR; A26638; A26638. DR HSSP; P02833; 9ANT. DR TRANSFAC; T00193; -. DR FlyBase; FBgn0000439; Dfd. DR GO; GO:0009795; P:embryonic morphogenesis; IMP. DR GO; GO:0006917; P:induction of apoptosis; IGI. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; KW Developmental protein; Nuclear protein. FT SITE 343 348 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 366 425 HOMEOBOX. FT CONFLICT 227 227 S -> I (IN REF. 2). FT CONFLICT 442 442 G -> A (IN REF. 3). FT CONFLICT 443 443 N -> K (IN REF. 2). FT CONFLICT 456 456 MISSING (IN REF. 3). FT CONFLICT 545 545 MISSING (IN REF. 2). SQ SEQUENCE 590 AA; 63837 MW; 22407D2562FF24AB CRC64; MSSFLMGYPH APHHVQSPMS MGNGLDPKFP PVADDYHHYN GHYSMTASTG HMSGAVGGGA GVGSVGGGGA GGMTGHPHSM HPADMVSDYM AHHHNPHSHS HSHTHSLPHH HSNSAISGHH QASAGGYSSN YANATPPSHP HSHPHAHPHQ SLGYYVHHAP EFISAGAVHS DPTNGYGPAA NVPNTSNGGG GGGSGAVLGG GAVGGSANGY YGGYGGGYGT ANGSVGSTHS QGHSPHSQMM DLPLQCSSTE PPTNTALGLQ ELGLKLEKRI EEAVPAGQQL QELGMRLRCD DMGSENDDMS EEDRLMLDRS PDELGSNDND DDLGDSDSDE DLMAETTDGE RIIYPWMKKI HVAGVANGSY QPGMEPKRQR TAYTRHQILE LEKEFHYNRY LTRRRRIEIA HTLVLSERQI KIWFQNRRMK WKKDNKLPNT KNVRKKTVDA NGNPTPVAKK PTKRAASKKQ QQAQQQQQSQ QQQTQQTQQT PVMNECIRSD SLESIGDVSS SLGNPPYIPA APETTSSYPG SQQHLSNNNN NGSGNNNNNN NNNNNSNLNN NNNNNQMGHT NLHGHLQQQQ SDLMTNLQLH IKQDYDLTAL // ID HMDH_DROME STANDARD; PRT; 916 AA. AC P14773; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 3-hydroxy-3-methylglutaryl-coenzyme A reductase (EC 1.1.1.34) (HMG-CoA DE reductase). GN HMGCR OR HMG-COAR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88302188; PubMed=3136321; RA Gertler F.B., Chiu C.-Y., Richter-Mann L., Chin D.J.; RT "Developmental and metabolic regulation of the Drosophila RT melanogaster 3-hydroxy-3-methylglutaryl coenzyme A reductase."; RL Mol. Cell. Biol. 8:2713-2721(1988). CC -!- FUNCTION: SYNTHESIS OF MEVALONATE FOR THE PRODUCTION OF NON- CC STEROL ISOPRENOIDS, WHICH ARE ESSENTIAL FOR GROWTH CC DIFFERENTIATION. CC -!- CATALYTIC ACTIVITY: (R)-MEVALONATE + COA + 2 NADP(+) = (S)-3- CC HYDROXY-3-METHYLGLUTARYL-COA + 2 NADPH. CC -!- ENZYME REGULATION: THE ACTIVITY OF HMG-COA-REDUCTASE IS SUPPRESSED CC BY EXOGENOUS MEVALONATE. CC -!- PATHWAY: ISOPRENOID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM. CC -!- SIMILARITY: BELONGS TO THE HMG-COA REDUCTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M21329; AAA28608.1; -. DR PIR; S32572; S32572. DR FlyBase; FBgn0001205; Hmgcr. DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH)...; NAS. DR InterPro; IPR002202; HMG-CoA_red. DR InterPro; IPR009023; HMG_CoA_NAD_bind. DR InterPro; IPR004554; HMG_CoA_R_NADP. DR InterPro; IPR009029; HMG_CoA_sub_bind. DR InterPro; IPR004816; HMG_CoAred. DR InterPro; IPR000731; SSD_5TM. DR Pfam; PF00368; HMG-CoA_red; 1. DR PRINTS; PR00071; HMGCOARDTASE. DR TIGRFAMs; TIGR00920; 2A060605; 1. DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 1. DR PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1. DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1. DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1. DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1. DR PROSITE; PS50156; SSD; 1. KW Oxidoreductase; Glycoprotein; Endoplasmic reticulum; Transmembrane; KW Isoprene biosynthesis; NADP. FT DOMAIN 1 380 MEMBRANE-BOUND. FT DOMAIN 381 494 LINKER. FT DOMAIN 495 825 CATALYTIC. FT TRANSMEM 11 33 POTENTIAL. FT TRANSMEM 100 127 POTENTIAL. FT TRANSMEM 133 159 POTENTIAL. FT TRANSMEM 167 191 POTENTIAL. FT TRANSMEM 202 226 POTENTIAL. FT TRANSMEM 234 262 POTENTIAL. FT TRANSMEM 358 381 POTENTIAL. FT ACT_SITE 582 582 BY SIMILARITY. FT ACT_SITE 789 789 BY SIMILARITY. FT ACT_SITE 888 888 GENERAL BASE (BY SIMILARITY). FT CARBOHYD 338 338 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 342 342 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 439 439 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 471 471 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 793 793 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 798 798 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 892 892 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 906 906 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 916 AA; 98295 MW; B13C4574E794068B CRC64; MIGPLFRATQ FCASHPWEVI VALLTITACM LNGGQEQYPG CEQRIGHSTA SAAAAGSGSG AGSGASGTIP PSSMGGSATS SRHRPCHGWS QSCDGLEAEY NAADVILMTI VRCTAVLYCY YQFCSLHRLG SKYVLGIAGL FTVFSSFIFT TAIIKFLGSD ISELKDALFF LLLVIDLSNS GRLRSGAMGS NQAEVTQNIA RGLELLGPAI SLDTIVVVLL VGVGTLSGVQ RLEVLCMFAV LSVLVNYVVF MTFYPACLSL IFDLSRSGVD MSVVREKAKG SLPLKSLTEE EQKANPVLQR VKLIMTTGLM AVHIYSREVS PAATTMVDKT LTPTLSLNVS NNRTESGEIA DIIIKWLTMS ADHIVISIVL IALVVKFICF DNRDPLPDQL RQSGPVAIEA KASQTTPIDE EHVEQEKDTE NSAAVRTLLF TIEDQSSANA STQTDLLPLR HRLVGPIKPP RPVQECLDIL NSTEEGSGPA ALSDEEIVSI VHAGGTHCPL HKIESVLDDP ERGVRIRRQI IGSRAKMPVG RLDVLPYEHF DYRKVLNACC ENVLGYVPIP VGYAGPLLLD GETYYVPMAT TEGALVASTN RGCKALSVRG VRSVVEDVGM TRAPCVRFPS VARAAEAKSW IENDENYRVV KTEFDSTSRF GRLKDCHIAM DGPQLYIRFV AITGDRMGMN MVSKALRWPF AEFTLHFPDM QIISLSGNFC CDKKPAAINW IKGRGKRVVT ECTISAATLR SVLKTDAKTL VECNKLKNMG GSAMAGSIGG NNAHAANMVT AVFLATGQDP AQNVTSSNCS TAMECWAENS EDLYMTCTMP SLEVGTVGGG TGLPGQSACL EMLGVRGAHA TRPGDNAKKL AQIVCATVMA GELSLMAALV NSDLVKSHMR HNRSSIAVNS ANNPLNVTVS SCSTIS // ID HMDL_DROME STANDARD; PRT; 327 AA. AC P20009; DT 01-FEB-1991 (Rel. 17, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeotic distal-less protein (Protein brista). GN DLL OR BA OR BR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93046644; PubMed=1358457; RA Vachon G., Cohen B., Pfeifle C., McGuffin M.E., Botas J., Cohen S.M.; RT "Homeotic genes of the Bithorax complex repress limb development in RT the abdomen of the Drosophila embryo through the target gene RT Distal-less."; RL Cell 71:437-450(1992). RN [2] RP SEQUENCE OF 124-184 FROM N.A. RX MEDLINE=89181930; PubMed=2564639; RA Cohen S.M., Broenner G., Kuettner F., Juergens G., Jaeckle H.; RT "Distal-less encodes a homoeodomain protein required for limb RT development in Drosophila."; RL Nature 338:432-434(1989). CC -!- FUNCTION: MAY PLAY A CRUCIAL ROLE IN LIMB MORPHOGENESIS, PARTIALLY CC SPECIFYING PATTERN ALONG THE PROXIMO-DISTAL AXIS OF THE LIMB. CC REQUIRED FOR LARVAL AND ADULT LIMBS DEVELOPMENT. PROMOTE THE CC DEVELOPMENT OF LIMB STRUCTURES ABOVE THE EVOLUTIONARY GROUND STATE CC OF BODY WALL. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: OPTIC CENTER OF THE DEVELOPING LARVAL BRAIN. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S47947; AAB24059.1; -. DR PIR; A44168; A44168. DR HSSP; P23441; 1FTT. DR TRANSFAC; T02005; -. DR FlyBase; FBgn0000157; Dll. DR GO; GO:0007484; P:genital morphogenesis (sensu Holometabola); NAS. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DNA_BIND 124 183 HOMEOBOX. SQ SEQUENCE 327 AA; 35247 MW; E55137F35549F8D0 CRC64; MDAPDAPHTP KYMDGGNTAA SVTPGINIPG KSAFVELQQH AAAGYGGIRS TYQHFGPQGG QDSGFPSPRS ALGYPFPPMH QNSYSGYHLG SYAPPCASPP KDDFSISDKC EDSGLRVNGK GKKMRKPRTI YSSLQLQQLN RRFQRTQYLA LPERAELAAS LGLTQTQVKI WFQNRRSKYK KMMKAAQGPG TNSGMPLGGG GPNPGQHSPN QMHSGGNNGG GSNSGSPSHY LPPGHSPTPS STPVSELSPE FPPTGLSPPT QAPWDQKPHW IDHKPPPQMT PQPPHPAATL HPQTHHHNPP PQMGGYVPQY WYLPETNPSL VTVWPAV // ID HMEN_DROME STANDARD; PRT; 552 AA. AC P02836; P02837; Q24356; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Segmentation polarity homeobox protein engrailed. GN EN. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85099327; PubMed=3917855; RA Poole S.J., Kauvar L.M., Drees B., Kornberg T.; RT "The engrailed locus of Drosophila: structural analysis of an RT embryonic transcript."; RL Cell 40:37-43(1985). RN [2] RP SEQUENCE OF 447-520 FROM N.A. RX MEDLINE=90114393; PubMed=2481829; RA Fjose A., McGinnis W., Gehring W.J.; RT "Isolation of a homoeo box-containing gene from the engrailed region RT of Drosophila and the spatial distribution of its transcripts."; RL Nature 313:284-289(1985). RN [3] RP CHARACTERIZATION. RX MEDLINE=93327762; PubMed=8334991; RA Han K., Manley J.L.; RT "Functional domains of the Drosophila Engrailed protein."; RL EMBO J. 12:2723-2733(1993). RN [4] RP PHOSPHORYLATION. RX MEDLINE=88289425; PubMed=2899884; RA Gay N.J., Poole S.J., Kornberg T.B.; RT "The Drosophila engrailed protein is phosphorylated by a RT serine-specific protein kinase."; RL Nucleic Acids Res. 16:6637-6647(1988). RN [5] RP SUBCELLULAR LOCATION. RX MEDLINE=86079515; PubMed=3935318; RA Dinardo S., Kuner J.M., Theis J., O'Farrell P.H.; RT "Development of embryonic pattern in D. melanogaster as revealed by RT accumulation of the nuclear engrailed protein."; RL Cell 43:59-69(1985). RN [6] RP INTERACTION WITH WG AND EN. RC TISSUE=Embryo; RX MEDLINE=93113685; PubMed=1335365; RA Siegfried E., Chou T.B., Perrimon N.; RT "wingless signaling acts through zeste-white 3, the Drosophila homolog RT of glycogen synthase kinase-3, to regulate engrailed and establish RT cell fate."; RL Cell 71:1167-1179(1992). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 453-512. RX MEDLINE=91029489; PubMed=1977522; RA Kissinger C.R., Liu B., Martin-Blanco E., Kornberg T.B., Pabo C.O.; RT "Crystal structure of an engrailed homeodomain-DNA complex at 2.8-A RT resolution: a framework for understanding homeodomain-DNA RT interactions."; RL Cell 63:579-590(1990). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 458-512 OF MUTANT LYS-503. RX MEDLINE=97454790; PubMed=9309220; RA Tucker-Kellogg L., Rould M.A., Chambers K.A., Ades S.E., Sauer R.T., RA Pabo C.O.; RT "Engrailed (Gln50-->Lys) homeodomain-DNA complex at 1.9-A resolution: RT structural basis for enhanced affinity and altered specificity."; RL Structure 5:1047-1054(1997). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 455-512. RX MEDLINE=99033052; PubMed=9813123; RA Fraenkel E., Rould M.A., Chambers K.A., Pabo C.O.; RT "Engrailed homeodomain-DNA complex at 2.2-A resolution: a detailed RT view of the interface and comparison with other engrailed RT structures."; RL J. Mol. Biol. 284:351-361(1998). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 456-512. RX MEDLINE=20349343; PubMed=10889025; RA Grant R.A., Rould M.A., Klemm J.D., Pabo C.O.; RT "Exploring the role of glutamine 50 in the homeodomain-DNA interface: RT crystal structure of engrailed (Gln50 --> Ala) complex at 2.0 A."; RL Biochemistry 39:8187-8192(2000). CC -!- FUNCTION: THIS PROTEIN SPECIFIES THE BODY SEGMENTATION PATTERN. IT CC IS REQUIRED FOR THE DEVELOPMENT OF THE CENTRAL NERVOUS SYSTEM. CC TRANSCRIPTIONAL REGULATOR THAT REPRESSES ACTIVATED PROMOTERS. WG CC SIGNALING OPERATES BY INACTIVATING THE SGG REPRESSION OF EN CC AUTOACTIVATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSION INITIATES PRIOR TO THE NINTH CC EMBRYONIC NUCLEAR DIVISION CYCLE WITHIN 1.5 HR AFTER CC FERTILIZATION. BY THE CELLULAR BLASTODERM STAGE (THE 14TH NUCLEAR CC DIVISION CYCLE) IS LOCALIZED INTO 14 STRIPES, 1-2 CELLS WIDE, CC SPACED ALONG THE ANTERIOR-POSTERIOR AXIS OF THE EMBRYO. CC -!- PTM: PHOSPHORYLATED. PHOSPHORYLATION MAY DIRECTLY OR CC ALLOSTERICALLY MODIFY ITS FUNCTION. CC -!- SIMILARITY: BELONGS TO THE ENGRAILED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M10017; AAA65478.1; -. DR EMBL; K03055; -; NOT_ANNOTATED_CDS. DR EMBL; K03056; -; NOT_ANNOTATED_CDS. DR EMBL; X01765; CAA25906.1; -. DR PIR; A90862; WJFFEN. DR PDB; 1ENH; 31-AUG-94. DR PDB; 1HDD; 15-JAN-92. DR PDB; 2HDD; 27-MAY-98. DR PDB; 3HDD; 11-NOV-98. DR PDB; 1DU0; 07-AUG-00. DR TRANSFAC; T00253; -. DR FlyBase; FBgn0000577; en. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007386; P:compartment specification; NAS. DR GO; GO:0007400; P:neuroblast cell fate determination; IGI. DR GO; GO:0007367; P:segment polarity determination; NAS. DR InterPro; IPR000747; Engrailed. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00026; ENGRAILED. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00033; ENGRAILED; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Segmentation polarity protein; 3D-structure; Transcription regulation; KW Repressor; Phosphorylation. FT DOMAIN 26 53 GLN-RICH. FT DOMAIN 68 87 ALA-RICH. FT DOMAIN 232 240 ALA-RICH. FT DOMAIN 320 368 SER-RICH. FT DNA_BIND 454 513 HOMEOBOX. FT CONFLICT 486 486 Q -> E (IN REF. 2). FT CONFLICT 519 520 LA -> WH (IN REF. 2). FT HELIX 463 475 FT HELIX 481 491 FT TURN 492 492 FT HELIX 495 509 SQ SEQUENCE 552 AA; 59419 MW; 576590658974348D CRC64; MALEDRCSPQ SAPSPITLQM QHLHHQQQQQ QQQQQQMQHL HQLQQLQQLH QQQLAAGVFH HPAMAFDAAA AAAAAAAAAA AHAHAAALQQ RLSGSGSPAS CSTPASSTPL TIKEEESDSV IGDMSFHNQT HTTNEEEEAE EDDDIDVDVD DTSAGGRLPP PAHQQQSTAK PSLAFSISNI LSDRFGDVQK PGKSIENQAS IFRPFEANRS QTATPSAFTR VDLLEFSRQQ QAAAAAATAA MMLERANFLN CFNPAAYPRI HEEIVQSRLR RSAANAVIPP PMSSKMSDAN PEKSALGSLC KAVSQIGQPA APTMTQPPLS SSASSLASPP PASNASTISS TSSVATSSSS SSSGCSSAAS SLNSSPSSRL GASGSGVNAS SPQPQPIPPP SAVSRDSGME SSDDTRSETG STTTEGGKNE MWPAWVYCTR YSDRPSSGPR YRRPKQPKDK TNDEKRPRTA FSSEQLARLK REFNENRYLT ERRRQQLSSE LGLNEAQIKI WFQNKRAKIK KSTGSKNPLA LQLMAQGLYN HTTVPLTKEE EELEMRMNGQ IP // ID HMES_DROME STANDARD; PRT; 497 AA. AC P18488; Q9VFQ1; DT 01-NOV-1990 (Rel. 16, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Empty spiracles homeotic protein. GN EMS OR E4 OR CG2988. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92289690; PubMed=1376248; RA Walldorf U., Gehring W.J.; RT "Empty spiracles, a gap gene containing a homeobox involved in RT Drosophila head development."; RL EMBO J. 11:2247-2259(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90152339; PubMed=2576012; RA Dalton D., Chadwick R., McGinnis W.; RT "Expression and embryonic function of empty spiracles: a Drosophila RT homeo box gene with two patterning functions on the RT anterior-posterior axis of the embryo."; RL Genes Dev. 3:1940-1956(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTS AS A HOMEOTIC SELECTOR GENE CONTROLLING ANTENNAL CC AND MANDIBULAR SEGMENT IDENTITY. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EMS HAS TWO DIFFERENT SPATIAL PATTERNS OF CC EXPRESSION DURING EMBRYOGENESIS. THE EMS HEAD-SPECIFIC EXPRESSION CC PATTERN INITIATES PRIOR TO CELLULAR BLASTODERM AND CONTINUES ONLY CC UNTIL EARLY GERM-BAND EXTENSION. THE EMS METAMERIC EXPRESSION CC PATTERN INITIATES AFTER GASTRULATION AND IS EXPRESSED IN THE CC LATERAL NEUROBLASTS, IN ECTODERMAL CELLS AT THE ANTERIOR LATERAL CC BORDERS OF EACH SEGMENT, AND IN THE FILZKOERPER PRIMORDIA. CC -!- MISCELLANEOUS: THE SEQUENCE SHOWN IS THAT OF STRAIN CANTON S. CC -!- SIMILARITY: BELONGS TO THE EMX HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66270; CAA46985.1; -. DR EMBL; X51653; CAA35965.1; -. DR EMBL; AE003702; AAF54999.1; -. DR PIR; S22708; S22708. DR HSSP; P06601; 1FJL. DR TRANSFAC; T02008; -. DR FlyBase; FBgn0000576; ems. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DOMAIN 1 387 PRO-RICH. FT DOMAIN 99 362 GLN-RICH. FT DOMAIN 334 341 POLY-ALA. FT DNA_BIND 391 450 HOMEOBOX. FT DOMAIN 471 497 ASP/GLU-RICH (ACIDIC). FT VARIANT 4 4 M -> T (IN STRAIN OREGON-R). FT VARIANT 102 104 MISSING (IN STRAINS BERKELEY AND OREGON- FT R). FT VARIANT 131 131 H -> Q (IN STRAINS BERKELEY AND OREGON- FT R). FT VARIANT 158 159 SG -> TR (IN STRAIN OREGON-R). FT VARIANT 304 305 EL -> DV (IN STRAIN OREGON-R). SQ SEQUENCE 497 AA; 53784 MW; BB7E4548155C0A5C CRC64; MTKMIPPVPT AAAAVMMPTP KQKIGFSIES IVGNDVSTAG GNSTPDLSGP QSPPPGERNV PGSPPQTPPA TLTLIPGSPP HHLMAPPAHG LPYPHPHAQQ QQQQHLQAPH PHPHLSPAQQ HVLHQHLLMQ HQHPGTPKSH QDIQELLQRL HHNAAMASGL SPLQTRLSPE TEQPQMAVSL KRERSPAPPA MEQAENPAQR IQPPHTPPKS VSPQSSQPSS SPTLLISSPH ATPPQQQQQQ PPPNYPKPAM MHPGGAGPMM MPGMPPAGLV RPFPMGPGGP PMPQGQPGLP DIKALPPYIN APPELPPQHN PHLIAAAQFQ MAAALQAGHV LGPAAAAAAA AGLPPHAAQF MPNPGMARDS YQLYPWLLSR HGRIFPHRFP GSFLVPPFRK PKRIRTAFSP SQLLKLEHAF ESNQYVVGAE RKALAQNLNL SETQVKVWFQ NRRTKHKRMQ QEDEKGGEGG SQRNMHNGSG DEDDDELIDM EMDECPSDEE HELDASH // ID HMEV_DROME STANDARD; PRT; 376 AA. AC P06602; P07667; Q9V5E6; DT 01-JAN-1988 (Rel. 06, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Segmentation protein even-skipped. GN EVE OR CG2328. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87051744; PubMed=2877745; RA McDonald P.M., Ingham P., Struhl G.; RT "Isolation, structure, and expression of even-skipped: a second pair- RT rule gene of Drosophila containing a homeo box."; RL Cell 47:721-734(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87218536; PubMed=2884106; RA Frasch M., Hoey T., Rushlow C., Doyle H., Levine M.; RT "Characterization and localization of the even-skipped protein of RT Drosophila."; RL EMBO J. 6:749-759(1987). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 1-58 FROM N.A. RC STRAIN=OR-RC, WA-F, ZM56, AF-S, and FL-S; RX MEDLINE=96038621; PubMed=8524036; RA Ludwig M.Z., Kreitman M.; RT "Evolutionary dynamics of the enhancer region of even-skipped in RT Drosophila."; RL Mol. Biol. Evol. 12:1002-1011(1995). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 70-189. RX MEDLINE=96134926; PubMed=8557047; RA Hirsch J.A., Aggarwal A.K.; RT "Structure of the even-skipped homeodomain complexed to AT-rich DNA: RT new perspectives on homeodomain specificity."; RL EMBO J. 14:6280-6291(1995). CC -!- FUNCTION: MAY PLAY A ROLE IN DETERMINING NEURONAL IDENTITY. MAY BE CC DIRECTLY INVOLVED IN SPECIFYING IDENTITY OF INDIVIDUAL NEURONS. CC PAIR-RULE PROTEIN REQUIRED FOR SEGMENTATION; INVOLVED IN CC TRANSFORMING THE BROAD, SPATIAL, APERIODIC EXPRESSION PATTERNS OF CC THE GAP GENES INTO A SYSTEM OF PRECISE PERIODIC EXPRESSION CC PATTERNS OF THE PAIR-RULE AND SEGMENTARY POLARITY GENES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE EVEN-SKIPPED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M14767; AAA28522.1; -. DR EMBL; X05138; CAA28784.1; -. DR EMBL; AE003831; AAF58865.1; -. DR EMBL; U32087; AAB05358.1; -. DR EMBL; U32088; AAB05359.1; -. DR EMBL; U32089; AAB05360.1; -. DR EMBL; U32090; AAB05361.1; -. DR EMBL; U32091; AAB05362.1; -. DR PIR; A26066; A26066. DR PDB; 1JGG; 06-JUL-01. DR TRANSFAC; T00272; -. DR FlyBase; FBgn0000606; eve. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; NAS. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW DNA-binding; Developmental protein; Embryo; Pair-rule protein; KW Transcription regulation; Homeobox; Nuclear protein; 3D-structure. FT DNA_BIND 70 129 HOMEOBOX. FT DOMAIN 165 179 ALA-RICH. FT CONFLICT 300 300 L -> V (IN REF. 1). SQ SEQUENCE 376 AA; 39970 MW; 59058E0634B1BED0 CRC64; MHGYRTYNME SHHAHHDASP VDQKPLVVDL LATQYGKPQT PPPSPNECLS SPDNSLNGSR GSEIPADPSV RRYRTAFTRD QLGRLEKEFY KENYVSRPRR CELAAQLNLP ESTIKVWFQN RRMKDKRQRI AVAWPYAAVY SDPAFAASIL QAAANSVGMP YPPYAPAAAA AAAAAAAVAT NPMMATGMPP MGMPQMPTMQ MPGHSGHAGH PSPYGQYRYT PYHIPARPAP PHPAGPHMHH PHMMGSSATG SSYSAGAAGL LGALPSATCY TGLGVGVPKT QTPPLDLQSS SSPHSSTLSL SPVGSDHAKV FDRSPVAQSA PSVPAPAPLT TTSPLPAPGL LMPSAKRPAS DMSPPPTTTV IAEPKPKLFK PYKTEA // ID HMFT_DROME STANDARD; PRT; 410 AA. AC P02835; O96929; Q9V3W3; DT 21-JUL-1986 (Rel. 01, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Segmentation protein fushi tarazu. GN FTZ OR BG:DS07876.1 OR CG2047. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84245843; PubMed=6330566; RA Laughon A., Scott M.P.; RT "Sequence of a Drosophila segmentation gene: protein structure RT homology with DNA-binding proteins."; RL Nature 310:25-31(1984). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., RA Palazzolo M.J.; RT "Complete sequence of the Antennapedia complex of Drosophila."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 247-320 FROM N.A. RX MEDLINE=84205674; PubMed=6327065; RA McGinnis W., Garber R.L., Wirz J., Kuroiwa A., Gehring W.J.; RT "A homologous protein-coding sequence in Drosophila homeotic genes RT and its conservation in other metazoans."; RL Cell 37:403-408(1984). RN [5] RP SEQUENCE OF 250-320 FROM N.A. RX MEDLINE=84248068; PubMed=6330741; RA Scott M.P., Weiner A.J.; RT "Structural relationships among genes that control development: RT sequence homology between the Antennapedia, Ultrabithorax, and fushi RT tarazu loci of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4115-4119(1984). RN [6] RP SEQUENCE OF 207-218 FROM N.A., AND MUTAGENESIS. RX MEDLINE=91115083; PubMed=2276626; RA Kellerman K.A., Mattson D.M., Duncan I.; RT "Mutations affecting the stability of the fushi tarazu protein of RT Drosophila."; RL Genes Dev. 4:1936-1950(1990). RN [7] RP FUNCTION. RX MEDLINE=88099492; PubMed=2892267; RA Doe C.Q., Hiromi Y., Gehring W.J., Goodman C.S.; RT "Expression and function of the segmentation gene fushi tarazu during RT Drosophila neurogenesis."; RL Science 239:170-175(1988). RN [8] RP CHARACTERIZATION. RX MEDLINE=89006213; PubMed=3049237; RA Krause H.M., Klemenz R., Gehring W.J.; RT "Expression, modification, and localization of the fushi tarazu RT protein in Drosophila embryos."; RL Genes Dev. 2:1021-1036(1988). RN [9] RP PHOSPHORYLATION. RX MEDLINE=89305523; PubMed=2743978; RA Krause H.M., Gehring W.J.; RT "Stage-specific phosphorylation of the fushi tarazu protein during RT Drosophila development."; RL EMBO J. 8:1197-1204(1989). RN [10] RP STRUCTURE BY NMR OF HOMEOBOX. RX MEDLINE=94231558; PubMed=7909851; RA Qian Y.Q., Furukubo-Tokunaga K., Resendez-Perez D., Mueller M., RA Gehring W.J., Wuethrich K.; RT "Nuclear magnetic resonance solution structure of the fushi tarazu RT homeodomain from Drosophila and comparison with the Antennapedia RT homeodomain."; RL J. Mol. Biol. 238:333-345(1994). CC -!- FUNCTION: MAY PLAY A ROLE IN DETERMINING NEURONAL IDENTITY, MAY BE CC DIRECTLY INVOLVED IN SPECIFYING IDENTITY OF INDIVIDUAL NEURONS. CC REQUIRED DURING EMBRYOGENESIS FOR THE PROCESS OF BODY CC SEGMENTATION. HOMEOTIC PROTEIN, REQUIRED IN ALTERNATING SEGMENT CC PRIMORDIA, IT SPECIFIES THE CORRECT NUMBER OF SEGMENTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED EARLY IN DEVELOPMENT IN A STRIPED CC PATTERN AT THE BLASTODERM STAGE. LATER EXPRESSED IN A SPECIFIC CC SUBSET OF NEURONAL PRECURSOR CELLS, NEURONS AND GLIA IN THE CC DEVELOPING CNS. BETWEEN 5 AND 6 HRS OF DEVELOPMENT, FOUND IN THE CC MIDLINE PRECURSOR-2 CELLS IN A SEGMENTALLY REPEATING PATTERN. CC EXPRESSION IN MANY OTHER NEURONAL PRECURSORS FOLLOWS AND REACHES A CC SECOND PEAK OF ABUNDANCE AT 9 HR OF DEVELOPMENT. EXPRESSED IN THE CC HINDGUT BETWEEN 11-15 HRS OF DEVELOPMENT. CC -!- PTM: PHOSPHORYLATED AT AS MANY AS 16 SITES. CC -!- MISCELLANEOUS: 'FUSHI TARAZU' MEANS 'SEGMENT DEFICIENT' IN CC JAPANESE. CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X00854; CAA25408.1; -. DR EMBL; AE003673; AAF54081.1; -. DR EMBL; AE001572; AAD19794.1; -. DR EMBL; K01947; AAA28372.1; -. DR EMBL; X78905; CAA55518.1; -. DR PIR; A93334; WJFFFT. DR PDB; 1FTZ; 31-MAY-94. DR TRANSFAC; T00295; -. DR FlyBase; FBgn0001077; ftz. DR GO; GO:0006357; P:regulation of transcription from Pol II pro...; NAS. DR InterPro; IPR005567; FTZ. DR InterPro; IPR001356; Homeobox. DR Pfam; PF03867; FTZ; 1. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation; Pair-rule protein; Phosphorylation; KW 3D-structure. FT DNA_BIND 254 313 HOMEOBOX. FT MUTAGEN 208 208 P->L: IN ALLELE FTZ-UAL2; HALF-LIFE IS FT INCREASED. FT MUTAGEN 212 212 P->S: IN ALLELE FTZ-UAL3; HALF-LIFE IS FT INCREASED. FT MUTAGEN 212 212 P->L: IN ALLELE FTZ-UAL1; HALF-LIFE IS FT INCREASED. FT CONFLICT 47 47 Y -> YHSY (IN REF. 1). FT CONFLICT 141 141 S -> T (IN REF. 1). FT CONFLICT 247 249 LAS -> MLT (IN REF. 4). FT CONFLICT 395 395 H -> Q (IN REF. 1). FT HELIX 263 273 FT TURN 274 275 FT HELIX 281 290 FT TURN 291 292 FT HELIX 295 305 FT TURN 306 307 FT TURN 309 310 FT HELIX 315 317 SQ SEQUENCE 410 AA; 46479 MW; 517154F3DAF8262F CRC64; MATTNSQSHY SYADNMNMYN MYHPHSLPPT YYDNSGSNAY YQNTSNYQGY YPQESYSESC YYYNNQEQVT TQTVPPVQPT TPPPKATKRK AEDDAASIIA AVEERPSTLR ALLTNPVKKL KYTPDYFYTT VEQVKKAPAV STKVTASPAP SYDQEYVTVP TPSASEDVDY LDVYSPQSQT QKLKNGDFAT PPPTTPTSLP PLEGISTPPQ SPGEKSSSAV SQEINHRIVT APNGAGDFNW SHIEETLASD CKDSKRTRQT YTRYQTLELE KEFHFNRYIT RRRRIDIANA LSLSERQIKI WFQNRRMKSK KDRTLDSSPE HCGAGYTAML PPLEATSTAT TGAPSVPVPM YHHHQTTAAY PAYSHSHSHG YGLLNDYPQQ QTHQQYDAYP QQYQHQCSYQ QHPQDLYHLS // ID HMG2_DROME STANDARD; PRT; 393 AA. AC Q24537; Q23998; Q24285; Q95SD7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE High mobility group protein DSP1 (Dorsal switch protein 1). GN DSP1 OR SSRP2 OR CG12223. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RC TISSUE=Embryo; RX MEDLINE=94352416; PubMed=8072548; RA Lehming N., Thanos D., Brickman J.M., Ma J., Maniatis T., Ptashne M.; RT "An HMG-like protein that can switch a transcriptional activator to a RT repressor."; RL Nature 371:175-179(1994). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=97183675; PubMed=9031641; RA Canaple L., Decoville M., Leng M., Locker D.L.D.; RT "The Drosophila DSP1 gene encoding an HMG 1-like protein: genomic RT organization, evolutionary conservation and expression."; RL Gene 184:285-290(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM C). RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: BINDS PREFERENTIALLY SINGLE-STRANDED DNA AND UNWINDS CC DOUBLE STRANDED DNA. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=A; CC IsoId=Q24537-1; Sequence=Displayed; CC Name=B; CC IsoId=Q24537-2; Sequence=VSP_002183; CC Name=C; CC IsoId=Q24537-3; Sequence=VSP_002184; CC -!- SIMILARITY: BELONGS TO THE HMG1/HMG2 PROTEIN FAMILY. CC -!- SIMILARITY: CONTAINS 2 HMG BOX DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13881; AAA50238.1; -. DR EMBL; X89811; CAA61938.1; -. DR EMBL; X81456; CAA57212.1; -. DR EMBL; AE003502; AAN09395.1; -. DR EMBL; AY060841; AAL28389.1; -. DR PIR; JC6179; JC6179. DR PIR; S50068; S50068. DR HSSP; P07155; 1AAB. DR FlyBase; FBgn0011764; Dsp1. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003697; F:single-stranded DNA binding; NAS. DR GO; GO:0006268; P:DNA unwinding; NAS. DR InterPro; IPR000135; Highmoblty_12. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 2. DR PRINTS; PR00886; HIGHMOBLTY12. DR SMART; SM00398; HMG; 2. DR PROSITE; PS00353; HMG_BOX_1; 1. DR PROSITE; PS50118; HMG_BOX_2; 2. KW Nuclear protein; Chromosomal protein; DNA-binding; Repeat; KW Alternative splicing. FT DNA_BIND 179 249 HMG BOX 1. FT DNA_BIND 271 339 HMG BOX 2. FT DOMAIN 7 162 GLN-RICH. FT DOMAIN 99 106 POLY-ALA. FT DOMAIN 376 391 ASP/GLU-RICH (ACIDIC). FT VARSPLIC 1 65 Missing (in isoform B). FT /FTId=VSP_002183. FT VARSPLIC 8 15 Missing (in isoform C). FT /FTId=VSP_002184. FT CONFLICT 129 129 Q -> T (IN REF. 1). FT CONFLICT 255 257 VVG -> LWD (IN REF. 1). FT CONFLICT 368 368 A -> R (IN REF. 1). SQ SEQUENCE 393 AA; 44935 MW; FD270250B723FD31 CRC64; MEHFHQIQQT IQHYQQQLAA QQQQQVQQQQ LQQHQVVVQQ NQQQAHQNSS NTTAGVGTQQ LFTYKMASSF PNPATTMAQV VATSNAAGTT GYDYRLNMAQ AAAAAAVPGS QWWYSAANQG QVDANTAAQL QHQQQQQQQQ QQQQQQQHQQ QQQMQQQQQQ QNVINSASPM SRVKADAKPR GRMTAYAYFV QTCREEHKKK HPDETVIFAE FSRKCAERWK TMVDKEKKRF HEMAEKDKQR YEAEMQNYVP PKGAVVGRGK KRKQIKDPNA PKRSLSAFFW FCNDERNKVK ALNPEFGVGD IAKELGRKWS DVDPEVKQKY ESMAERDKAR YEREMTEYKT SGKIAMSAPS MQASMQAQAQ KAALLAAAAQ QQHQQLEEQH DDDDGDGDDD ENQ // ID HMGD_DROME STANDARD; PRT; 112 AA. AC Q05783; Q9W2D3; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE High mobility group protein D (HMG-D). GN HMGD OR CG17950. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 45-77. RC TISSUE=Embryo; RX MEDLINE=92236564; PubMed=1373803; RA Wagner C.R., Hamana K., Elgin S.C.R.; RT "A high-mobility-group protein and its cDNAs from Drosophila RT melanogaster."; RL Mol. Cell. Biol. 12:1915-1923(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94021387; PubMed=8414994; RA Ner S.S., Churchill M.E.A., Searles M.A., Travers A.A.; RT "dHMG-Z, a second HMG-1-related protein in Drosophila melanogaster."; RL Nucleic Acids Res. 21:4369-4371(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP CHARACTERIZATION. RX MEDLINE=94222028; PubMed=8168480; RA Ner S.S., Travers A.A.; RT "HMG-D, the Drosophila melanogaster homologue of HMG 1 protein, is RT associated with early embryonic chromatin in the absence of histone RT H1."; RL EMBO J. 13:1817-1822(1994). RN [5] RP CHARACTERIZATION. RX MEDLINE=95237208; PubMed=7720717; RA Churchill M.E.A., Jones D.N.M., Glaser T., Hefner H., Searles M.A., RA Travers A.A.; RT "HMG-D is an architecture-specific protein that preferentially binds RT to DNA containing the dinucleotide TG."; RL EMBO J. 14:1264-1275(1995). RN [6] RP STRUCTURE BY NMR OF 2-74. RX MEDLINE=95006330; PubMed=7922039; RA Jones D.N.M., Searles M.A., Shaw G.L., Churchill M.E.A., Ner S.S., RA Keeler J., Travers A.A., Neuhaus D.; RT "The solution structure and dynamics of the DNA-binding domain of RT HMG-D from Drosophila melanogaster."; RL Structure 2:609-627(1994). CC -!- FUNCTION: BINDS PREFERENTIALLY SINGLE-STRANDED DNA AND UNWINDS CC DOUBLE STRANDED DNA. PREFERS SITES CONTAINING THE SEQUENCE 5'-TTG- CC 3'. FACILITATES DNA BENDING. ASSOCIATED WITH EARLY EMBRYONIC CC CHROMATIN IN THE ABSENCE OF HISTONE H1. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: PRESENT IN ALL STAGES OF DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE HMG1/HMG2 PROTEIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X71138; CAA50468.1; -. DR EMBL; M77023; AAA28609.1; -. DR EMBL; AE003455; AAM71011.1; -. DR PIR; A44382; A44382. DR PDB; 1HMA; 31-JUL-94. DR PDB; 1E7J; 29-MAR-01. DR PDB; 1QRV; 26-SEP-01. DR FlyBase; FBgn0004362; HmgD. DR GO; GO:0003680; F:AT DNA binding; IDA. DR GO; GO:0006325; P:establishment and/or maintenance of chromat...; IDA. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW Nuclear protein; Chromosomal protein; DNA-binding; 3D-structure. FT DNA_BIND 5 71 HMG BOX. FT DOMAIN 101 112 ASP/GLU-RICH (ACIDIC). FT HELIX 11 26 FT TURN 27 28 FT HELIX 32 45 FT HELIX 50 71 FT TURN 72 73 SQ SEQUENCE 112 AA; 12416 MW; 3F537CCFD62FEC9F CRC64; MSDKPKRPLS AYMLWLNSAR ESIKRENPGI KVTEVAKRGG ELWRAMKDKS EWEAKAAKAK DDYDRAVKEF EANGGSSAAN GGGAKKRAKP AKKVAKKSKK EESDEDDDDE SE // ID HMGZ_DROME STANDARD; PRT; 111 AA. AC Q06943; Q9W2D4; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE High mobility group protein Z (HMG-Z). GN HMGZ OR CG17921. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94021387; PubMed=8414994; RA Ner S.S., Churchill M.E.A., Searles M.A., Travers A.A.; RT "dHMG-Z, a second HMG-1-related protein in Drosophila melanogaster."; RL Nucleic Acids Res. 21:4369-4371(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE HMG1/HMG2 PROTEIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X71139; CAA50469.1; -. DR EMBL; AE003454; AAF46758.1; -. DR PIR; S41765; S41765. DR HSSP; Q05783; 1HMA. DR FlyBase; FBgn0010228; HmgZ. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW Nuclear protein; Chromosomal protein; DNA-binding. FT DNA_BIND 6 72 HMG BOX. FT DOMAIN 100 111 ASP/GLU-RICH (ACIDIC). SQ SEQUENCE 111 AA; 12656 MW; 3B95E3572BB4530A CRC64; MSGDRPKRPL SAYMLWLNET REQIKKDNPG SKVTDIAKRG GELWRGLKDK TEWEQKAIKM KEEYNKAVKE YEANGGTDSG APKKRKKAAA KPAKKAKKKE SSEEEEEDES E // ID HMH2_DROME STANDARD; PRT; 410 AA. AC P10035; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein H2.0. GN H2.0. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88329003; PubMed=2901348; RA Barad M., Jack T., Chadwick R., McGinnis W.; RT "A novel, tissue-specific, Drosophila homeobox gene."; RL EMBO J. 7:2151-2161(1988). CC -!- FUNCTION: MAY HAVE AN IMPORTANT ROLE IN THE MORPHOGENESIS OF A CC SINGLE TISSUE TYPE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXHIBITS A TISSUE SPECIFIC PATTERN OF CC EXPRESSION. IT ACCUMULATES IN CELLS OF THE VISCERAL MUSCULATURE CC AND ITS ANLAGEN. CC -!- SIMILARITY: BELONGS TO THE H2.0 HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00843; CAA68766.1; -. DR PIR; S00994; WJFFH2. DR HSSP; P06601; 1FJL. DR FlyBase; FBgn0001170; H2.0. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DOMAIN 180 204 HIS/GLN-RICH (OPA-REPEAT). FT DNA_BIND 287 346 HOMEOBOX. SQ SEQUENCE 410 AA; 44950 MW; D81E71395A12D5BD CRC64; MEQSMPENLS THMYGECEVN PTLAKCPDPV NVDHELPTKE SCASTTIVST SPTSATSTTK VKLSFSVDRL LGSEPEESHR QSSSSPSTKS CCDGSILACC SFPHCFSQAN AESRRFGHAT LPPTFTPTSS HTYPFVGLDK LFPGPYMDYK SVLRPTPIRA AEHAAPTYPT LATNALLRFH QHQKQQHQQH HHHQHHPKHL HQQHKPPPHN STTATALLAP LHSLTSLQLT QQQQRFLGKT PQQLLDIAPT SPAAAAAAAT SQNGAHGHGG GNGQGNASAG SNGKRKRSWS RAVFSNLQRK GLEIQFQQQK YITKPDRRKL AARLNLTDAQ VKVWFQNRRM KWRHTRENLK SGQEKQPSAV PESGGVFKTS TPSGDGAPQE ALDYSSDSCS SVDLSEQADE DDNIEINVVE // ID HMIN_DROME STANDARD; PRT; 576 AA. AC P05527; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Homeobox protein invected. GN INV. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88112775; PubMed=2892756; RA Coleman K.G., Poole S.J., Weir M.P., Soeller W.C., Kornberg T.; RT "The invected gene of Drosophila: sequence analysis and expression RT studies reveal a close kinship to the engrailed gene."; RL Genes Dev. 1:19-28(1987). CC -!- FUNCTION: THE DEVELOPMENTAL ROLE OF THE INVECTED PROTEIN IS CC NOT KNOWN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ENGRAILED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05273; CAA28885.1; -. DR PIR; A26628; A26628. DR HSSP; P02836; 1HDD. DR FlyBase; FBgn0001269; inv. DR GO; GO:0007400; P:neuroblast cell fate determination; IGI. DR InterPro; IPR000747; Engrailed. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00026; ENGRAILED. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00033; ENGRAILED; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DNA_BIND 471 530 HOMEOBOX. SQ SEQUENCE 576 AA; 60953 MW; 9E536D583A4EB05E CRC64; MSTLASTRPP PLKLTIPSLE EAEDHAQERR AGGGGQEVGK MHPDCLPLPL VQPGNSPQVR EEEEDEQTEC EEQLNIEDEE VEEEHDLDLE DPASCCSENS VLSVGQEQSE AAQAALSAQA QARQRLLISQ IYRPSAFSST ATTVLPPSEG PPFSPEDLMQ LPPSTGTFQE EFLRKSQLYA EELMKQQMHL MAAARVNALT AAAAGKQLQM AMAAAAVATV PSGQDALAQL TATALGLGPG GAVHPHQQLL LQRDQVHHHH HMQNHLNNNE NLHERALKFS IDNILKADFG SRLPKIGALS GNIGGGSVSG SSTGSSKNSG TTNGNRSPLK APKKSGKPLN LAQSNAAANS SLSFSSSLAN ICSNSNDSNS TATSSSTTNT SGAPVDLVKS PPPAAGAGAT GASGKSGEDS GTPIVWPAWV YCTRYSDRPS SGRSPRARKP KKPATSSSAA GGGGGGVEKG EAADGGGVPE DKRPRTAFSG TQLARLKHEF NENRYLTEKR RQQLSGELGL NEAQIKIWFQ NKRAKLKKSS GTKNPLALQL MAQGLYNHST IPLTREEEEL QELQEAASAR AAKEPC // ID HMLA_DROME STANDARD; PRT; 635 AA. AC P10105; O97065; DT 01-MAR-1989 (Rel. 10, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeotic labial protein (F24) (F90-2). GN LAB OR BG:DS00004.9 OR CG1264. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=89052673; PubMed=2461299; RA Mlodzik M., Fjose A., Gehring W.J.; RT "Molecular structure and spatial expression of a homeobox gene from RT the labial region of the Antennapedia-complex."; RL EMBO J. 7:2569-2578(1988). RN [2] RP SEQUENCE FROM N.A. (ISOFORM SHORT), AND CHARACTERIZATION. RC STRAIN=Oregon-R, and Canton-S; TISSUE=Embryo; RX MEDLINE=89252817; PubMed=2566560; RA Diederich R.J., Merrill V.K.L., Pultz M.A., Kaufman T.C.; RT "Isolation, structure, and expression of labial, a homeotic gene of RT the Antennapedia Complex involved in Drosophila head development."; RL Genes Dev. 3:399-414(1989). RN [3] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; RA Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., RA Palazzolo M.J.; RT "Complete sequence of the Antennapedia complex of Drosophila."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [6] RP SEQUENCE OF 500-567 FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; RX MEDLINE=86259687; PubMed=3014511; RA Hoey T., Doyle H.J., Harding K., Wedeen C., Levine M.; RT "Homeo box gene expression in anterior and posterior regions of the RT Drosophila embryo."; RL Proc. Natl. Acad. Sci. U.S.A. 83:4809-4813(1986). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC REQUIRED FOR PROPER HEAD DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P10105-1; Sequence=Displayed; CC Name=Short; CC IsoId=P10105-2; Sequence=VSP_002397; CC -!- TISSUE SPECIFICITY: DURING EMBRYOGENESIS, EXPRESSED IN MANDIBULAR CC LOBE, HYPOPHARYNGEAL ORGAN, NEURAL AND EPIDERMAL CELLS OF CC PROCEPHALIC LOBE, SENSORY CELLS OF CLYPEOLABRUM, POSTERIOR MIDGUT, CC THORACIC AND ABDOMINAL SEGMENTS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC HIGH EXPRESSION IN EMBRYOS AND THIRD INSTAR LARVAE, LOWER CC EXPRESSION IN PUPAE. CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. "LABIAL" CC SUBFAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1, MET-2 OR MET-7 IS THE CC INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13103; CAA31495.1; -. DR EMBL; X13104; CAB57786.1; -. DR EMBL; X13105; CAB57786.1; JOINED. DR EMBL; X13106; CAB57786.1; JOINED. DR EMBL; X13104; CAB57787.1; -. DR EMBL; X13105; CAB57787.1; JOINED. DR EMBL; X13106; CAB57787.1; JOINED. DR EMBL; AE001572; AAD19811.1; -. DR EMBL; AE003674; AAF54098.1; -. DR EMBL; AY095089; AAM11417.1; -. DR EMBL; M13570; AAA28610.1; -. DR PIR; A30168; A30168. DR PIR; S01164; S01164. DR HSSP; P14653; 1B72. DR FlyBase; FBgn0002522; lab. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; FALSE_NEG. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; KW Developmental protein; Nuclear protein; Alternative splicing. FT DOMAIN 11 18 HIS-RICH. FT DOMAIN 42 64 GLN-RICH. FT DOMAIN 96 111 GLN-RICH. FT DOMAIN 129 134 SER/THR-RICH. FT DOMAIN 191 196 GLN-RICH. FT DOMAIN 306 339 GLN/HIS-RICH. FT DOMAIN 361 370 SER/THR-RICH. FT DNA_BIND 507 566 HOMEOBOX. FT VARSPLIC 406 411 Missing (in isoform Short). FT /FTId=VSP_002397. FT CONFLICT 31 31 S -> A (IN REF. 2). FT CONFLICT 46 46 P -> H (IN REF. 2). FT CONFLICT 139 139 T -> K (IN REF. 1). FT CONFLICT 444 444 G -> D (IN REF. 1). FT CONFLICT 447 447 N -> S (IN REF. 1 AND 2). SQ SEQUENCE 635 AA; 68154 MW; B39A58813F4D5778 CRC64; MMDVSSMYGN HPHHHHPHAN AYDGYSTTTA SAANASSYFA PQQHQPHLQL QQQQQHQHLQ QPQQHLTYNG YESSSPGNYY PQQQAQLTPP PTSSHQVVQQ HQQQQQAQQQ QLYPHSHLFS PSAAEYGITT STTTGNPGTP LHPSSHSPAD SYYESDSVHS YYATAAVATV APPSNSSPIT AANASATSNT QQQQQQAAII SSENGMMYTN LDCMYPTAQA QAPVHGYAGQ IEEKYAAVLH ASYAPGMVLE DQDPMMQQAT QSQMWHHQQH LAGSYALDAM DSLGMHAHMH HGLPHGHLGN LANNPHQQQP QVQQQQQQPH QQPQHPQNQS PAAHQQHHQN SVSPNGGMNR QQRGGVISPG SSTSSSTSAS NGAHPASTQS KSPNHSSSIP TYKWMQLKRN VPKPQAPSYL PAPKLPASGI ASMHDYQMNG QLDMCRGGGG GGSGVGNGPV GVGGNGSPGI GGVLSVQNSL IMANSAAAAG SAHPNGMGVG LGSGSGLSSC SLSSNTNNSG RTNFTNKQLT ELEKEFHFNR YLTRARRIEI ANTLQLNETQ VKIWFQNRRM KQKKRVKEGL IPADILTQHS TSVISEKPPQ QQQPQPPELQ LKSQGSDLGG NELATGAPST PTTAMTLTAP TSKQS // ID HMN1_DROME STANDARD; PRT; 659 AA. AC P22807; Q9VD96; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein slou (S59/2) (Slouch protein) (Homeobox protein NK- DE 1). GN SLOU OR NK1 OR S59 OR CG6534. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91099659; PubMed=1980118; RA Dohrmann C., Azpiazu N., Frasch M.; RT "A new Drosophila homeo box gene is expressed in mesodermal precursor RT cells of distinct muscles during embryogenesis."; RL Genes Dev. 4:2098-2111(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 497-625 FROM N.A. RX MEDLINE=90046666; PubMed=2573058; RA Kim Y., Nirenberg M.; RT "Drosophila NK-homeobox genes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7716-7720(1989). CC -!- FUNCTION: MAY PLAY A ROLE IN SPECIFYING THE IDENTITY OF PARTICULAR CC SOMATIC MUSCLES AND NEURONS OF THE CNS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: MESODERMAL PRECURSOR CELLS OF DISTINCT MUSCLES CC DURING EMBRYOGENESIS, A SUBSET OF NEURONAL CELLS OF THE CNS AND CC THEIR PRECURSORS AND ALSO IN CELLS OF A SMALL REGION OF THE CC MIDGUT. CC -!- DEVELOPMENTAL STAGE: POSTGASTRULATION-STAGE. CC -!- SIMILARITY: BELONGS TO THE NK-1 HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55393; CAA39067.1; -. DR EMBL; AE003735; AAF55901.3; -. DR EMBL; M27289; AAA28616.1; -. DR PIR; A36664; A36664. DR HSSP; P14653; 1B72. DR TRANSFAC; T04257; -. DR FlyBase; FBgn0002941; slou. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; NAS. DR GO; GO:0007501; P:mesoderm cell fate specification; NAS. DR GO; GO:0007521; P:muscle cell fate determination; IEP. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Repeat. FT DOMAIN 201 239 HIS-RICH. FT DOMAIN 221 234 7 X 2 AA TANDEM REPEATS OF H-P. FT DOMAIN 364 372 POLY-ALA. FT DOMAIN 477 522 ASP/GLU-RICH (ACIDIC). FT DOMAIN 536 542 POLY-GLY. FT DNA_BIND 545 604 HOMEOBOX. SQ SEQUENCE 659 AA; 69955 MW; 5D401F55C4670280 CRC64; MVMLQSPAQK ASDSASAQNT AVGGLMSPNS NPDSPKSNTS PDVASADSVV SGTGGGSTPP AAKIPKFIIS ANGAAVAGKQ EQELRYSLER LKQMSSESGS LLSRLSPLQE DSQDKEKPNH NNNNSLTNHN ANSNTRRSQS PPASVGSVSF SSPAQQRKLL ELNAVRHLAR PEPLQHPHAA LLQQHPHLLQ NPQFLAAAQQ HMHHHQHQHH QHPAHPHSHQ HPHPHPHPHP HPHPSAVFHL RAPSSSSTAP PSPATSPLSP PTSPAMHSDQ QMSPPIAPPQ NPPHSSQPPQ QQQVAAPSDM DLERIKLVAA VAARTTQASS TSALASASNS VSNASISISN SSSGSPSGRD LSDYGFRIQL GGLAAAAAAA AATSRQIAAA TYARSDTSEE LNVDGNDEDS NDGSHSTPSV CPVDLTRSVN SSAAANPSSA STSASSDRDA ATKRLAFSVE NILDPNKFTG NKLPSGPFGH PRQWSYERDE EMQERLDDDQ SEDMSAQDLN DMDQDDMCDD GSDIDDPSSE TDSKKGGSRN GDGKSGGGGG GGSKPRRART AFTYEQLVSL ENKFKTTRYL SVCERLNLAL SLSLTETQVK IWFQNRRTKW KKQNPGMDVN SPTIPPPGGG SFGPGAYASG LLYSHAVPYP PYGPYFHPLG AHHLSHSHS // ID HMN2_DROME STANDARD; PRT; 722 AA. AC P22808; Q24589; DT 01-AUG-1991 (Rel. 19, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein vnd (Ventral nervous system defective protein) DE (Homeobox protein NK-2). GN VND OR NK2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95354667; PubMed=7628450; RA Jimenez F., Martin-Morris L.E., Velasco L., Chu H., Sierra J., RA Rosen D.R., White K.; RT "vnd, a gene required for early neurogenesis of Drosophila, encodes a RT homeodomain protein."; RL EMBO J. 14:3487-3495(1995). RN [2] RP SEQUENCE OF 476-633 FROM N.A. RX MEDLINE=90046666; PubMed=2573058; RA Kim Y., Nirenberg M.; RT "Drosophila NK-homeobox genes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7716-7720(1989). RN [3] RP STRUCTURE BY NMR OF 537-612. RX MEDLINE=95371127; PubMed=7643404; RA Tsao D.H.H., Gruschus J.M., Wang L.-H., Nirenberg M., Ferretti J.A.; RT "The three-dimensional solution structure of the NK-2 homeodomain RT from Drosophila."; RL J. Mol. Biol. 251:297-307(1995). RN [4] RP STRUCTURE BY NMR OF 543-605. RX MEDLINE=97299770; PubMed=9154919; RA Gruschus J.M., Tsao D.H.H., Wang L.-H., Nirenberg M., Ferretti J.A.; RT "Interactions of the vnd/NK-2 homeodomain with DNA by nuclear magnetic RT resonance spectroscopy: basis of binding specificity."; RL Biochemistry 36:5372-5380(1997). CC -!- FUNCTION: PROBABLE TRANSCRIPTIONAL REGULATOR INVOLVED IN THE CC REGULATION OF THE PRONEURAL AS-C GENES AND THE NEUROGENIC GENES OF CC THE ENHANCER OF SPLIT COMPLEX. COULD SPECIFICALLY ACTIVATE CC PRONEURAL GENES IN THE VENTRAL-MOST NEUROECTODERM. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE CNS AND MIDGUT. CC -!- SIMILARITY: BELONGS TO THE NK-2 HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X87141; CAA60619.1; -. DR EMBL; M27290; AAA28617.1; -. DR PIR; S57246; S57246. DR PDB; 1VND; 08-NOV-96. DR PDB; 1NK2; 23-FEB-99. DR PDB; 1NK3; 23-FEB-99. DR PDB; 1QRY; 06-JUL-99. DR TRANSFAC; T04258; -. DR FlyBase; FBgn0003986; vnd. DR GO; GO:0007400; P:neuroblast cell fate determination; IMP. DR GO; GO:0007419; P:ventral cord development; NAS. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; 3D-structure; KW Developmental protein; Nuclear protein; Neurogenesis. FT DOMAIN 108 111 POLY-SER. FT DOMAIN 215 223 POLY-ALA. FT DOMAIN 336 343 POLY-ALA. FT DOMAIN 351 359 POLY-ALA. FT DOMAIN 482 486 POLY-ASN. FT DOMAIN 489 492 POLY-ASN. FT DNA_BIND 544 603 HOMEOBOX. FT DOMAIN 688 693 POLY-ALA. FT VARIANT 578 578 A -> T (IN VND29). FT CONFLICT 632 633 RR -> VG (IN REF. 2). FT TURN 553 554 FT HELIX 555 565 FT HELIX 571 581 FT TURN 582 582 FT HELIX 585 594 SQ SEQUENCE 722 AA; 76468 MW; D036AE4D890014DA CRC64; MTTSASLERT PSKRDRDRER DNSSGLGSAG SLPASPQSAI TVSPSSPATP KRPLRTSTPS LERKREREDR EDREDRKERQ ERHERDREHE RFAAVFSTAS TTVPTNTSSS SGLAPEQLRI PTGAAAFSGF PGLHSMSSLM LPSSAAVARA AAPFLPWSPI LLPPWNHALL PAAFYPAALR NALPGLFDAK VPSSQRSGFH ISDILNLEGS ELKNAAAAAA AAAHHGSDLS HHSASESTSG HRGQGSHTSP SALSPTPAGV SADEHHNGSG TGGGAGEADH HSTTEHHAPP SHPQQQHPHH QQHHHPHLLL PQQHHQQAVA PLPLAHHQSG EAQSHAHANA AAAHLLASHN AAAAAAVAAG KYLPNLPKNF PGSFGDEMSS YHHMAQTMLQ HSGRSAWMKE NELYGTQQPA SPDSTSPVTS EVSYTYIGSN CQTSPALSGD YKSYSRSADS DALSVGDALH TLHGSSGNGS AGGAPTAHAL HNNNNNTTNN NNHSLKAEGI NGAGSGHDDS LNEDGIEEDI DDVDDADGSG GGDANGSDGL PNKKRKRRVL FTKAQTYELE RRFRQQRYLS APEREHLASL IRLTPTQVKI WFQNHRYKTK RAQNEKGYEG HPGLLHGHAT HPHHPSALPS PRRVAVPVLV RNGKPCLGDS SKLGADCVSV SSATATAMQN AAAHHLVALN GAAAYQHAAA AAAGLHAHAH AHAHAHGHGH PHAHAQRAAW WP // ID HMOC_DROME STANDARD; PRT; 671 AA. AC P22810; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeotic protein orthodenticle (Ocelliless protein). GN OTD OR OC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91071580; PubMed=1979296; RA Finkelstein R., Smouse D., Capaci T.M., Spradling A.C., Perrimon N.; RT "The orthodenticle gene encodes a novel homeo domain protein involved RT in the development of the Drosophila nervous system and ocellar RT visual structures."; RL Genes Dev. 4:1516-1527(1990). CC -!- FUNCTION: INVOLVED IN THE DEVELOPMENT OF THE DROSOPHILA NERVOUS CC SYSTEM AND OCELLAR VISUAL STRUCTURES. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE ANTERIOR REGION OF THE CC EMBRYO BEFORE CELLULARIZATION AND BECOMES LOCALIZED TO THE CC PROCEPHALIC HEAD REGION FOLLOWING GASTRULATION. CC -!- DOMAIN: CONTAINS MULTIPLE REPEATS CONSISTING OF SINGLE AMINO ACIDS CC (E.G., GLY, SER, HIS, AND ASN) AND PAIRS OF AMINO ACIDS (E.G., CC GLY-VAL). CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58983; CAA41732.1; -. DR PIR; A35912; A35912. DR HSSP; P06601; 1FJL. DR TRANSFAC; T02078; -. DR FlyBase; FBgn0004102; oc. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation; Repeat. FT DNA_BIND 73 132 HOMEOBOX. FT DOMAIN 229 266 2 X 19 AA TANDEM REPEATS. FT REPEAT 229 247 1. FT REPEAT 248 266 2. SQ SEQUENCE 671 AA; 69666 MW; 515B69536E0E9B44 CRC64; MAAGFLKSGD LGPHPHSYGG PHPHHSVPHG PLPPGMPMPS LGPFGLPHGL EAVGFSQGMW GDLCYPGVNT RKQRRERTTF TRAQLDVLEA LFGKTRYPDI FMREEVALKI NLPESRVQVW FKNRRAKCRQ QLQQQQQSNS LSSSKNASGG GSGNSCSSSS ANSRSNSNNN GSSSNNNTQS SGGNNSNKSS QKQGNSQSSQ QGGGSSGGNN SNNNSAAAAA SAAAAVAAAQ SIKTHHSSFL SAAAAASAQS IKTHHSSFLS AAAAASGGTN QSANNNSNNN NQGNSTPNSS SSGGGSQAGG HLSAAAAAAA LNVTAAHQNS SPLLPTPATS VSPVSIVCKK EHLSGGYGSS VGGGGGGGGG GASSGGLNLG VGVGVGVGVG VGVSQDLLRS PYDQLKDAGG DIGAGVHHHH SIYGSAAGSN PRLLQPGGNI TPMDSSSSIT TPSPPITPMS PQSAPQRPMP PNRPSPPTIL PPIRPPICPI MIRITSGTIS TSNIRITMPR RPATTHRWST LAIRIRSTTT WAIRATRPPI LVCRHRHPSR APCPRRPSPR TAWITCRRRI STRIWCRIYS SNTAAVAATT TVQRGQVVRV RVRVRVRVLV LVVDLVLVLV LVLDRGAIVL PSWSSTIISS TSTSYSSISI TRIITRINTR ITTAIIIISS NTIMMMNSDR I // ID HMPB_DROME STANDARD; PRT; 782 AA. AC P31264; O97058; Q9VI44; DT 01-JUL-1993 (Rel. 26, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeotic proboscipedia protein. GN PB OR BG:DS01719.1 OR CG31481/CG17880. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS A; B; C AND D). RC STRAIN=Canton-S; RX MEDLINE=92224882; PubMed=1348688; RA Cribbs D.L., Pultz M.A., Johnson D., Mazzulla M., Kaufman T.C.; RT "Structural complexity and evolutionary conservation of the RT Drosophila homeotic gene proboscipedia."; RL EMBO J. 11:1437-1449(1992). RN [2] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; RA Celniker S.E., Pfeiffer B.D., Knafels J., Martin C.H., Mayeda C.A., RA Palazzolo M.J.; RT "Complete sequence of the Antennapedia complex of Drosophila."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M.J., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC CONTROLS DEVELOPMENT OF MOUTHPARTS, AND LABIAL AND MAXILLARY CC PALPS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist; CC Name=A; CC IsoId=P31264-1; Sequence=Displayed; CC Name=C; CC IsoId=P31264-2; Sequence=VSP_002398; CC Name=B; CC IsoId=P31264-3; Sequence=VSP_002399; CC Name=D; CC IsoId=P31264-4; Sequence=VSP_002400; CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. PROBOSCIPEDIA CC SUBFAMILY. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63729; CAA45272.1; -. DR EMBL; X63728; CAA45271.1; -. DR EMBL; AE001572; AAD19802.1; -. DR EMBL; AE003674; AAF54089.2; ALT_SEQ. DR PIR; S20881; S20881. DR HSSP; P02833; 9ANT. DR TRANSFAC; T02084; -. DR FlyBase; FBgn0051481; pb. DR GO; GO:0007381; P:specification of segmental identity, labial...; IMP. DR GO; GO:0007382; P:specification of segmental identity, maxill...; NAS. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Alternative splicing. FT SITE 164 169 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 198 257 HOMEOBOX. FT DOMAIN 472 494 GLN-RICH. FT DOMAIN 472 706 GLN/HIS-RICH. FT VARSPLIC 184 189 GDNSIT -> A (in isoform C). FT /FTId=VSP_002398. FT VARSPLIC 189 194 TEFVPE -> K (in isoform B). FT /FTId=VSP_002399. FT VARSPLIC 184 193 Missing (in isoform D). FT /FTId=VSP_002400. FT CONFLICT 520 520 H -> D (IN REF. 1). FT CONFLICT 651 651 Q -> E (IN REF. 1). FT CONFLICT 685 685 H -> D (IN REF. 1). FT CONFLICT 701 701 P -> H (IN REF. 1). FT CONFLICT 768 782 SNLANDFAPEYYQLS -> ATWPTTLRRNTTNSVSSCRKYA FT RGQCKYLLA (IN REF. 1). SQ SEQUENCE 782 AA; 83747 MW; BAB876E2B1429F00 CRC64; MQEVCSSLDT TSMGTQIKSE SPLNPLQVQT GQTSLPVGGC GGAGVVGGVG GVGVSVGQPG IGQQGVPPVP SVLMVNKMTP NCDKRSADTA YWMTASEGGF INSQPSMAEF LNHLSPESPK IGTPVGSGAI GGVGVNVNVN VGVGVGYPVG VVPQTPDGMD SVPEYPWMKE KKTSRKSSNN NNQGDNSITE FVPENGLPRR LRTAYTNTQL LELEKEFHFN KYLCRPRRIE IAASLDLTER QVKVWFQNRR MKHKRQTLSK TDDEDNKDSL KGDDDQSDSN SNSKKSCQGC ELPSDDIPDS TSNSRGHNNN TPSATNNNPS AGNLTPNSSL ETGISSNLMG STTVSASNVI SADSSVASSV SLDEDIEESS PIKVKKKDDG QVIKKEAVST SSKASPFGYE NSTPSLVSFR RDSDASAVGN APTSKAVGKK RFQSAANAIA TPTPLSDSNS GNGSGGGPAG GYFPGYYPSP KQQQQVQQQQ LHPQQQQLPQ QQPQDYYGKY DIEFAASPHH NPHNKQQALH GEYLSPKPSS ANFHQNSQQQ QQNDHFYYNY NDTNGTPYLN HQQQHHHHAQ HHQQQQHHQN HVADFEGPVN GPSNFNNGAY YDNMSFQQQA QAHQHQTVVF QQQQPHQPAA INHQHMHHLG NGETYSALGL QMENCEGYNN FGAAGTGGGY YEAGQQPPIP ATHGHGHHPH HVQVPAQAHA PIHAHHNSAA IPGGVGVGPP PSHIHGFAIN GGPAVQGQAF GNNGSTAAGT AAISGLENSN SSDFNFLSNL ANDFAPEYYQ LS // ID HMPR_DROME STANDARD; PRT; 613 AA. AC P06601; Q9VKB6; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Segmentation protein paired. GN PRD OR CG6716. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B). RX MEDLINE=87051745; PubMed=2877746; RA Frigerio G., Burri M., Bopp D., Baumgartner S., Noll M.; RT "Structure of the segmentation gene paired and the Drosophila PRD RT gene set as part of a gene network."; RL Cell 47:735-746(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-154. RX MEDLINE=95171459; PubMed=7867071; RA Xu W., Rould M.A., Jun S., Desplan C., Pabo C.O.; RT "Crystal structure of a paired domain-DNA complex at 2.5-A resolution RT reveals structural basis for Pax developmental mutations."; RL Cell 80:639-650(1995). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 196-276. RX MEDLINE=95401261; PubMed=7671301; RA Wilson D.S., Guenther B., Desplan C., Kuriyan J.; RT "High resolution crystal structure of a paired (Pax) class RT cooperative homeodomain dimer on DNA."; RL Cell 82:709-719(1995). CC -!- FUNCTION: PAIR-RULE PROTEIN EXPRESSED IN A SEGMENTALLY REPEATING CC PATTERN TO DEFINE THE POLARITY OF EMBRYONIC SEGMENTS. CAPABLE OF CC SEQUENCE-SPECIFIC DNA-BINDING. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=P06601-1; Sequence=Displayed; CC Name=A; CC IsoId=P06601-2; Sequence=VSP_007021; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 PAIRED BOX DOMAIN. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M14548; AAB59221.1; -. DR EMBL; AE003634; AAN10801.1; -. DR EMBL; AE003634; AAF53160.1; -. DR EMBL; AY059447; AAL13353.1; -. DR PIR; A26062; A26062. DR PDB; 1FJL; 20-JUN-96. DR PDB; 1PDN; 31-JUL-95. DR TRANSFAC; T00699; -. DR FlyBase; FBgn0003145; prd. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0003704; F:specific RNA polymerase II transcription fa...; NAS. DR GO; GO:0007366; P:periodic partitioning by pair rule gene; NAS. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR001523; Paired_box. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_BOX; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Paired box; Repeat; Pair-rule protein; Transcription regulation; KW 3D-structure; Alternative splicing. FT DOMAIN 27 151 PAIRED BOX. FT DNA_BIND 213 272 HOMEOBOX. FT DOMAIN 541 576 HIS/PRO-RICH REGION. FT VARSPLIC 1 23 Missing (in isoform A). FT /FTId=VSP_007021. FT VARIANT 164 164 A -> T. FT VARIANT 220 220 F -> I. FT STRAND 29 31 FT TURN 33 34 FT STRAND 37 39 FT TURN 40 41 FT HELIX 46 57 FT TURN 58 59 FT HELIX 62 69 FT TURN 70 70 FT HELIX 73 86 FT TURN 105 105 FT HELIX 106 112 FT TURN 113 116 FT TURN 118 119 FT HELIX 122 131 FT TURN 132 132 FT TURN 138 139 FT HELIX 143 149 FT HELIX 222 234 FT HELIX 240 250 FT TURN 251 251 FT HELIX 254 275 SQ SEQUENCE 613 AA; 65497 MW; 777772C6E704C1A2 CRC64; MTVTAFAAAM HRPFFNGYST MQDMNSGQGR VNQLGGVFIN GRPLPNNIRL KIVEMAADGI RPCVISRQLR VSHGCVSKIL NRYQETGSIR PGVIGGSKPR IATPEIENRI EEYKRSSPGM FSWEIREKLI REGVCDRSTA PSVSAISRLV RGRDAPLDND MSSASGSPAG DGTKASSSCG SDVSGGHHNN GKPSDEDISD CESEPGIALK RKQRRCRTTF SASQLDELER AFERTQYPDI YTREELAQRT NLTEARIQVW FSNRRARLRK QHTSVSGGAP GGAAASVSHV AASSSLPSVV SSVPSMAPLA MMPGSLDPAT VYQQQYDFYG SHANISVSAA APMASSNLSP GITTTPPHHH QFYNPSANTA SYIMPGENGN TTPTGNIIVS SYETQLGSVY GTETETHQTM PRNESPNESV SSAFGQLPPT PNSLSAVVSG AGVTSSSGAN SGADPSQSLA NASAGSEELS AALKVESVDL IAASQSQLYG GWSSMQALRP NAPLSPEDSL NSTSSTSQAL DVTAHQMFHP YQHTPQYASY PAPGHAHSHH GHPHAPHPHA HPHPQYAGAH PHYPPPSSSA HFMPQNFNAA AFPSPSKVNY TTMPPQPFYP SWY // ID HMRO_DROME STANDARD; PRT; 350 AA. AC P10181; Q24487; Q9VBA7; DT 01-MAR-1989 (Rel. 10, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein rough. GN RO OR CG6348. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89051867; PubMed=2903798; RA Tomlinson A., Kimmel B.E., Rubin G.M.; RT "Rough, a Drosophila homeobox gene required in photoreceptors R2 and RT R5 for inductive interactions in the developing eye."; RL Cell 55:771-784(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 182-258 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88261567; PubMed=2898735; RA Saint R., Kalionis B., Lockett T.J., Elizur A.; RT "Pattern formation in the developing eye of Drosophila melanogaster RT is regulated by the homoeo-box gene, rough."; RL Nature 334:151-154(1988). CC -!- FUNCTION: ROUGH SEEMS TO BE IMPLICATED IN THE PATTERN FORMATION CC IN THE DEVELOPING EYE OF FRUIT FLY. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23629; AAA56800.1; -. DR EMBL; AE003758; AAF56635.1; -. DR EMBL; X12528; CAC32035.1; -. DR PIR; S03168; S03168. DR HSSP; P14653; 1B72. DR TRANSFAC; T00732; -. DR FlyBase; FBgn0003267; ro. DR GO; GO:0045680; P:negative regulation of R8 differentiation; NAS. DR GO; GO:0007461; P:restriction of R8 fate; NAS. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; KW Developmental protein; Nuclear protein; Vision. FT DNA_BIND 191 250 HOMEOBOX. FT DOMAIN 120 131 GLN/HIS-RICH. FT DOMAIN 322 328 GLN-RICH. FT CONFLICT 304 304 A -> T (IN REF. 1). SQ SEQUENCE 350 AA; 39430 MW; D5A39EF19D39DEAF CRC64; MQRHKVEIGS PDGSPGIKRS DSLDPIANTT ILSVPQRPSS PRQFFERLYG HLETRSSENG EIDVGTHAHK PPPCDTPYHS DGGSVSSPDI SISDERTSLA AYPAYDFYGH AKDYPQHPSQ QHQQHHHHHH HPPQLVHQKL SYVSPPPAIA AGGAANPVLP HAFPAGFPSD PHFSAGFSAF LARRRRKEGR QRRQRTTFST EQTLRLEVEF HRNEYISRSR RFELAETLRL TETQIKIWFQ NRRAKDKRIE KAQIDQHYRN FVVANGFMSS IMGQAATTMP PGGVTGGVAV GVGLNYYAAA ATPAALPKDN TQDANFIDID DQFQRQQQQK QQQQQQQQRR RETTTPINIC // ID HMSH_DROME STANDARD; PRT; 515 AA. AC Q03372; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Muscle segmentation homeobox (Protein Drop). GN DR OR MSH. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97042058; PubMed=8887329; RA D'Alessio M., Frasch M.; RT "msh may play a conserved role in dorsoventral patterning of the RT neuroectoderm and mesoderm."; RL Mech. Dev. 58:217-231(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98146200; PubMed=9486795; RA Nose A., Isshiki T., Takeichi M.; RT "Regional specification of muscle progenitors in Drosophila: the role RT of the msh homeobox gene."; RL Development 125:215-223(1998). RN [3] RP SEQUENCE OF 420-480 FROM N.A. RX MEDLINE=91200674; PubMed=1673109; RA Holland P.W.H.; RT "Cloning and evolutionary analysis of msh-like homeobox genes from RT mouse, zebrafish and ascidian."; RL Gene 98:253-257(1991). CC -!- FUNCTION: PROBABLE MORPHOGENETIC ROLE IN PRONEURAL AND PROMUSCULAR CC CLUSTER FORMATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE MSH HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U33319; AAC47329.1; -. DR EMBL; AF009038; AAB62975.1; -. DR EMBL; M38582; AAA28611.1; -. DR PIR; PS0404; PS0404. DR HSSP; P14653; 1B72. DR TRANSFAC; T03551; -. DR FlyBase; FBgn0000492; Dr. DR GO; GO:0007450; P:dorsal/ventral pattern formation, imaginal ...; IMP. DR GO; GO:0007419; P:ventral cord development; NAS. DR GO; GO:0007476; P:wing morphogenesis; IMP. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DOMAIN 38 45 POLY-SER. FT DOMAIN 94 108 POLY-GLN. FT DOMAIN 175 179 POLY-PRO. FT DOMAIN 205 214 POLY-ALA. FT DOMAIN 225 229 POLY-GLN. FT DOMAIN 364 371 POLY-ALA. FT DNA_BIND 421 480 HOMEOBOX. SQ SEQUENCE 515 AA; 54264 MW; AE475EBA29320A0D CRC64; MLKLSPASMT VTGLRQTMTS PTVPPSTNTP AGNLIITSSS SNSGSNSGSN MSSGNMTSSN LTNLSPSHPA GLNALASPTS PSALLLAHQQ HLLQQHQQHQ QQQQQQQQAA ALQLAAVHPP AHHLHKTTSR LSNFSVASLL ADTRPRTPPN QAADGPQNLT SSAATSPISQ ASSTPPPPPA SAAAQVPANT FHPAAVAHHA HLLQAAHAAA AAHAQHQAMA AQLRQQQQQA DARANSPPAS TSSTPSSTPL GSALGSQGNV ASTPAKNERH SPLGSHTDSE LEYDEEMLQD HEADHDEEED SIVDIEDMNA DDSPRSTPDG LDGSGKSLES PHGPPPGSHM QSTILSPAAL ASGHVPIRPT PFSALAAAAV AWTGMGGGVP WPGTRQMPPF GPPGMFPGAG FGGDANEPPR IKCNLRKHKP NRKPRTPFTT QQLLSLEKKF REKQYLSIAE RAEFSSSLRL TETQVKIWFQ NRRAKAKRLQ EAEIEKIKMA ALGRGAPGAQ WAMAGYFHPS LMHLG // ID HMTI_DROME STANDARD; PRT; 416 AA. AC P22711; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Muscle-specific homeobox protein tinman (Msh-2) (NK-4). GN TIN OR MSH2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91209226; PubMed=1982429; RA Bodmer R., Jan L.Y., Jan Y.N.; RT "A new homeobox-containing gene, msh-2, is transiently expressed RT early during mesoderm formation of Drosophila."; RL Development 110:661-669(1990). RN [2] RP SEQUENCE OF 267-416 FROM N.A. RX MEDLINE=90046666; PubMed=2573058; RA Kim Y., Nirenberg M.; RT "Drosophila NK-homeobox genes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7716-7720(1989). RN [3] RP CHARACTERIZATION. RX MEDLINE=94357069; PubMed=7915669; RA Bodmer R.; RT "The gene tinman is required for specification of the heart and RT visceral muscles in Drosophila."; RL Development 118:719-729(1993). CC -!- FUNCTION: REQUIRED FOR THE DEVELOPMENT OF VISCERAL MUSCLE; FOR THE CC FORMATION OF SOMATIC MUSCLES. HAS A CRUCIAL FUNCTION IN THE EARLY CC MESODERMAL SUBDIVISIONS. LOSS OF ACTIVITY RESULTS IN ABSENCE OF CC CARDIAC AND MIDGUT VISCERAL MUSCLE, AND DEFECTS IN A SUBSET OF CC DORSAL BODY WALL MUSCLES. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: IS INITIALLY EXPRESSED THROUGHOUT THE CC PRESUMPTIVE MESODERM AND BECOMES RESTRICTED TO CARDIAC AND CC VISCERAL MUSCLE. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55192; CAA38978.1; -. DR EMBL; M27292; AAA28619.1; -. DR PIR; A43561; A43561. DR HSSP; P23441; 1FTT. DR TRANSFAC; T03612; -. DR FlyBase; FBgn0004110; tin. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DOMAIN 119 122 POLY-PRO. FT DNA_BIND 301 360 HOMEOBOX. FT DOMAIN 398 405 POLY-GLN. FT DOMAIN 409 414 POLY-GLN. SQ SEQUENCE 416 AA; 46124 MW; 77A6AE6F1EAA4FD7 CRC64; MLQHHQQQAQ SGGYYDHYTQ SPSPGSLTNA DALNTTPFSV KDILNMVNQT EAYEGSYGHI DGAATASALF AAGEYQNPHQ YLNHQQHQQS ELPIPQQQLH HQHLDDGATT SSSLSPLLPP PPHQLYGGYQ DYGMPAHMFQ HHHGHPHQSF QHSASAYNMS ASQFYAGASA TAYQTPATYN YNYAGSGEVY GGATPSAVDI KSEYIPTPYV TPSPTLDLNS SAEVDSLQAP TQKLCVNPLS QRLMETASNS SSLRSIYGSD EGAKKKDNSQ VTSSRSELRK NSISGNSNPG SNSGSTKPRM KRKPRVLFSQ AQVLELECRF RLKKYLTGAE REIIAQKLNL SATQVKIWFQ NRRYKSKRGD IDCEGIAKHL KLKSEPLDSP TSLPPPIPNH VMWPPTMQQS QQQQQHHAQQ QQMQHM // ID HMUX_DROME STANDARD; PRT; 389 AA. AC P02834; Q9TX83; Q9VER4; Q9VER5; DT 21-JUL-1986 (Rel. 01, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Homeotic Ultrabithorax protein. GN UBX OR CG10388. OS Drosophila melanogaster (Fruit fly), and OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7240; RN [1] RP SEQUENCE FROM N.A. (ISOFORM IB). RC SPECIES=D.melanogaster; STRAIN=Canton-S; RA Weinzierl R., Axton J.M., Ghysen A., Akam M.; RT "Ultrabithorax mutations in constant and variable regions of the RT protein coding sequence."; RL Genes Dev. 1:386-397(1987). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS IA; IB; IIA; IIB; IVA AND IVB). RC SPECIES=D.melanogaster; RX MEDLINE=89232720; PubMed=2565858; RA Kornfeld K., Saint R.B., Beachy P.A., Harte P.J., Peattie D.A., RA Hogness D.S.; RT "Structure and expression of a family of Ultrabithorax mRNAs RT generated by alternative splicing and polyadenylation in RT Drosophila."; RL Genes Dev. 3:243-258(1989). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS IA; IB; IIA; IIB AND IVA). RC SPECIES=D.melanogaster; STRAIN=Canton-S; RX MEDLINE=95396803; PubMed=7667301; RA Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D., RA Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.; RT "Complete sequence of the bithorax complex of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS, AND ALTERNATIVE SPLICING. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE FROM N.A. (ISOFORM IA). RC SPECIES=D.melanogaster; STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE OF 290-389 FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=84205674; PubMed=6327065; RA McGinnis W., Garber R.L., Wirz J., Kuroiwa A., Gehring W.J.; RT "A homologous protein-coding sequence in Drosophila homeotic genes RT and its conservation in other metazoans."; RL Cell 37:403-408(1984). RN [8] RP SEQUENCE OF 290-384 FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=84248068; PubMed=6330741; RA Scott M.P., Weiner A.J.; RT "Structural relationships among genes that control development: RT sequence homology between the Antennapedia, Ultrabithorax, and fushi RT tarazu loci of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4115-4119(1984). RN [9] RP SEQUENCE OF 294-355 FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=93259465; PubMed=8098307; RA Chan S.K., Mann R.S.; RT "The segment identity functions of Ultrabithorax are contained within RT its homeo domain and carboxy-terminal sequences."; RL Genes Dev. 7:796-811(1993). RN [10] RP SEQUENCE OF 1-8 FROM N.A. RC SPECIES=D.melanogaster; RA Saari G., Bienz M.; RT "The structure of the ultrabithorax promoter of Drosophila RT melanogaster."; RL EMBO J. 6:1775-1779(1987). RN [11] RP SEQUENCE FROM N.A. (ISOFORM IB). RC SPECIES=D.simulans; STRAIN=Tsimbazaza; RX MEDLINE=99068642; PubMed=9853753; RA Stern D.L.; RT "A role of Ultrabithorax in morphological differences between RT Drosophila species."; RL Nature 396:463-466(1998). RN [12] RP DNA-BINDING. RC SPECIES=D.melanogaster; RX MEDLINE=91216112; PubMed=1673656; RA Ekker S.C., Young K.E., von Kessler D.P., Beachy P.A.; RT "Optimal DNA sequence recognition by the Ultrabithorax homeodomain of RT Drosophila."; RL EMBO J. 10:1179-1186(1991). RN [13] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RC SPECIES=D.melanogaster; STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94274046; PubMed=7911773; RA Bomze H.M., Lopez A.J.; RT "Evolutionary conservation of the structure and expression of RT alternatively spliced Ultrabithorax isoforms from Drosophila."; RL Genetics 136:965-977(1994). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 233-356 IN COMPLEX WITH EXD. RC SPECIES=D.melanogaster; RX MEDLINE=99165220; PubMed=10067897; RA Passner J.M., Ryoo H.-D., Shen L., Mann R.S., Aggarwal A.K.; RT "Structure of a DNA-bound Ultrabithorax-Extradenticle homeodomain RT complex."; RL Nature 397:714-719(1999). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC BINDS THE CONSENSUS REGION 5'-TTAAT[GT][GA]-3'. THIS HOMEOTIC CC PROTEIN CONTROLS DEVELOPMENT OF THE CELLS IN THE POSTERIOR CC THORACIC AND FIRST ABDOMINAL SEGMENTS. IT ACTIVATES THE SYNTHESIS CC OF THE DECAPENTAPLEGIC (DPP) GROWTH FACTOR. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=IB; CC IsoId=P02834-1; Sequence=Displayed; CC Note=Has been shown to exist only in D.simulans so far; CC Name=IA; CC IsoId=P02834-2; Sequence=VSP_002405; CC Name=IIA; CC IsoId=P02834-3; Sequence=VSP_002406; CC Name=IIB; CC IsoId=P02834-4; Sequence=VSP_002408; CC Name=IVA; CC IsoId=P02834-5; Sequence=VSP_002407; CC Name=IVB; CC IsoId=P02834-6; Sequence=VSP_002409; CC -!- TISSUE SPECIFICITY: IN THE EMBRYO, EXPRESSION IS SEEN IN THE CC EPIDERMIS, SOMATIC AND VISCERAL MESODERM, AND THE PERIPHERAL AND CC CENTRAL NERVOUS SYSTEM. CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05723; CAA29194.1; -. DR EMBL; X05724; CAA29194.1; JOINED. DR EMBL; X05725; CAA29194.1; JOINED. DR EMBL; X05727; CAA29194.1; JOINED. DR EMBL; X76210; CAA53803.1; -. DR EMBL; U31961; AAA84412.1; -. DR EMBL; U31961; AAA84411.1; -. DR EMBL; U31961; AAA84410.1; -. DR EMBL; U31961; AAA84409.1; -. DR EMBL; U31961; AAA84408.1; -. DR EMBL; AE003714; AAF55355.2; -. DR EMBL; AE003714; AAF55356.1; -. DR EMBL; AE003714; AAN13717.1; -. DR EMBL; AE003714; AAN13718.1; -. DR EMBL; AE003714; AAN13719.1; -. DR EMBL; BT010241; AAQ23559.1; -. DR EMBL; K01963; AAA29008.1; ALT_SEQ. DR EMBL; K01959; AAA28615.1; ALT_SEQ. DR EMBL; X05427; CAA29009.1; -. DR EMBL; AF099983; AAD16402.1; -. DR EMBL; AF099980; AAD16402.1; JOINED. DR EMBL; AF099981; AAD16402.1; JOINED. DR EMBL; AF099982; AAD16402.1; JOINED. DR PIR; B27867; B27867. DR PIR; D26995; D26995. DR PDB; 1B8I; 12-APR-99. DR TRANSFAC; T00863; -. DR FlyBase; FBgn0003944; Ubx. DR FlyBase; FBgn0014820; Dsim\Ubx. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0045449; P:regulation of transcription; IDA. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Activator; Homeobox; DNA-binding; KW Developmental protein; Nuclear protein; Alternative splicing; KW 3D-structure. FT DOMAIN 33 39 POLY-ALA. FT DOMAIN 111 129 POLY-GLY. FT SITE 239 244 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 295 354 HOMEOBOX. FT DOMAIN 322 325 POLY-ARG. FT DOMAIN 372 381 POLY-ALA. FT VARSPLIC 248 256 Missing (in isoform IA). FT /FTId=VSP_002405. FT VARSPLIC 248 273 Missing (in isoform IIA). FT /FTId=VSP_002406. FT VARSPLIC 248 290 Missing (in isoform IVA). FT /FTId=VSP_002407. FT VARSPLIC 258 274 Missing (in isoform IIB). FT /FTId=VSP_002408. FT VARSPLIC 257 290 Missing (in isoform IVB). FT /FTId=VSP_002409. FT CONFLICT 75 75 N -> Y (IN REF. 3). FT CONFLICT 330 330 H -> Y (IN REF. 7). FT CONFLICT 340 340 K -> E (IN REF. 7). FT HELIX 304 316 FT HELIX 322 332 FT TURN 333 333 FT HELIX 336 351 FT TURN 352 353 SQ SEQUENCE 389 AA; 40040 MW; D452E8FFE55D8F53 CRC64; MNSYFEQASG FYGHPHQATG MAMGSGGHHD QTASAAAAAY RGFPLSLGMS PYANHHLQRT TQDSPYDASI TAACNKIYGD GAGAYKQDCL NIKADAVNGY KDIWNTGGSN GGGGGGGGGG GGGAGGTGGA GNANGGNAAN ANGQNNPAGG MPVRPSACTP DSRVGGYLDT SGGSPVSHRG GSAGGNVSVS GGNGNAGGVQ SGVGVAGAGT AWNANCTISG AAAQTAAASS LHQASNHTFY PWMAIAGECP EDPTKSKIRS DLTQYGGIST DMGKRYSESL AGSLLPDWLG TNGLRRRGRQ TYTRYQTLEL EKEFHTNHYL TRRRRIEMAH ALCLTERQIK IWFQNRRMKL KKEIQAIKEL NEQEKQAQAQ KAAAAAAAAA AVQGGHLDQ // ID HMZ1_DROME STANDARD; PRT; 353 AA. AC P09089; Q9VI45; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Zerknuellt protein 1 (ZEN-1). GN ZEN OR ZEN1 OR Z1 OR CG1046. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88112803; PubMed=2892759; RA Rushlow C., Doyle H., Hoey T., Levine M.; RT "Molecular characterization of the zerknullt region of the RT Antennapedia gene complex in Drosophila."; RL Genes Dev. 1:1268-1279(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., RA Palazzolo M.J.; RT "Complete sequence of the Antennapedia complex of Drosophila."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE DIFFERENTIATION OF THE DORSAL-VENTRAL CC PATTERN, AND DOES NOT APPEAR TO BE INVOLVED IN THE PROCESS OF CC SEGMENTATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X68347; CAA48416.1; -. DR EMBL; AE001572; AAD19800.1; -. DR EMBL; AE003674; AAF54087.1; -. DR PIR; A43697; A43697. DR PDB; 1KZ2; 19-JUN-02. DR TRANSFAC; T00917; -. DR FlyBase; FBgn0004053; zen. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; Nuclear protein; KW Developmental protein; 3D-structure. FT DNA_BIND 90 149 HOMEOBOX. SQ SEQUENCE 353 AA; 39302 MW; 1FA64031C160CE2B CRC64; MSSVMHYYPV HQAKVGSYSA DPSEVKYSDL IYGHHHDVNP IGLPPNYNQM NSNPTTLNDH CSPQHVHQQH VSSDENLPSQ PNHDSQRVKL KRSRTAFTSV QLVELENEFK SNMYLYRTRR IEIAQRLSLC ERQVKIWFQN RRMKFKKDIQ GHREPKSNAK LAQPQAEQSA HRGIVKRLMS YSQDPREGTA AAEKRPMMAV APVNPKPDYQ ASQKMKTEAS TNNGMCSSAD LSEILEHLAQ TTAAPQVSTA TSSTGTSTNS ASSSSSGHYS YNVDLVLQSI KQDLEAAAQA WSKSKSAPIL ATQSWHPSSQ SQVPTSVHAA PSMNLSWGEP AAKSRKLSVN HMNPCVTSYN YPN // ID HMZ2_DROME STANDARD; PRT; 252 AA. AC P09090; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Zerknuellt protein 2 (ZEN-2). GN ZEN2 OR Z2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88112803; PubMed=2892759; RA Rushlow C., Doyle H., Hoey T., Levine M.; RT "Molecular characterization of the zerknullt region of the RT Antennapedia gene complex in Drosophila."; RL Genes Dev. 1:1268-1279(1987). CC -!- FUNCTION: REQUIRED FOR THE DIFFERENTIATION OF THE DORSAL-VENTRAL CC PATTERN, AND DOES NOT APPEAR TO BE INVOLVED IN THE PROCESS OF CC SEGMENTATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X68348; CAA48417.1; -. DR PIR; B43697; B43697. DR HSSP; P14653; 1B72. DR TRANSFAC; T00917; -. DR TRANSFAC; T02099; -. DR FlyBase; FBgn0004054; zen2. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; Nuclear protein; KW Developmental protein. FT DNA_BIND 43 102 HOMEOBOX. SQ SEQUENCE 252 AA; 29119 MW; 4FE5EF488E2FD7E6 CRC64; MFAIQSENYF VDNYSVSDLM MYPCVEFNVE AARTATTRSS EKSKRSRTAF SSLQLIELER EFHLNKYLAR TRRIEISQRL ALTERQVKIW FQNRRMKLKK STNRKGAIGA LTTSIPLSSQ SSEDLQKDDQ IVERLLRYAN TNVETAPLRQ VDHGVLEEGQ ITPPYQSYDY LHEFSPEPMA LPQLPFNEFD ANWASSWLGL EPTIPIAENV IEHNTQDQPM IQNFCWDSNS SSASSSDILD VDYDFIQNLL NF // ID HNF4_DROME STANDARD; PRT; 666 AA. AC P49866; Q9VLI8; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor HNF-4 homolog (dHNF4). GN HNF4 OR NR2A4 OR CG9310. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=93178427; PubMed=8440243; RA Zhong W., Sladek F.M., Darnell J.E. Jr.; RT "The expression pattern of a Drosophila homolog to the mouse RT transcription factor HNF-4 suggests a determinative role in gut RT formation."; RL EMBO J. 12:537-544(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTIONALLY CONTROLLED TRANSCRIPTION FACTOR. CC IMPORTANT FOR THE DIFFERENTIATION OF VARIOUS SPECIALIZED CELL CC TYPES THAT ARISE FROM BOTH ENDODERM AND MESODERM. MAY HAVE A ROLE CC IN EARLY GUT FORMATION. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: IN DEVELOPING EMBRYOS IT IS EXPRESSED IN MID- CC GUT, FAT BODIES AND THE DISTAL REGION OF MALPIGHIAN TUBULES. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR2 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U70874; AAB09592.1; -. DR EMBL; AE003622; AAF52703.1; -. DR PIR; S36218; S36218. DR HSSP; P19793; 2NLL. DR TRANSFAC; T02739; -. DR FlyBase; FBgn0004914; Hnf4. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 104 169 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 104 124 C4-TYPE. FT ZN_FING 140 164 C4-TYPE. FT DOMAIN 66 69 POLY-ASN. FT DOMAIN 89 99 POLY-GLN. FT DOMAIN 511 517 POLY-ALA. FT DOMAIN 519 523 POLY-SER. FT DOMAIN 553 556 POLY-GLN. FT DOMAIN 601 606 POLY-GLY. FT CONFLICT 75 75 N -> Y (IN REF. 1). FT CONFLICT 79 79 S -> N (IN REF. 1). SQ SEQUENCE 666 AA; 71899 MW; 97D9A44B7634BACD CRC64; MHADALASAY PAASQPHSPI GLALSPNGGG LGLSNSSNQS SENFALCNGN GNAGSAGGGS ASSGSNNNNS MFSPNNNLSG SGSGTNSSQQ QLQQQQQQQS PTVCAICGDR ATGKHYGASS CDGCKGFFRR SVRKNHQYTC RFARNCVVDK DKRNQCRYCR LRKCFKAGMK KEAVQNERDR ISCRRTSNDD PDPGNGLSVI SLVKAENESR QSKAGAAMEP NINEDLSNKQ FASINDVCES MKQQLLTLVE WAKQIPAFNE LQLDDQVALL RAHAGEHLLL GLSRRSMHLK DVLLLSNNCV ITRHCPDPLV SPNLDISRIG ARIIDELVTV MKDVGIDDTE FACIKALVFF DPNAKGLNEP HRIKSLRHQI LNNLEDYISD RQYESRGRFG EILLILPVLQ SITWQMIEQI QFAKIFGVAH IDSLLQEMLL GGELADNPLP LSPPNQSNDY QSPTHTGNME GGNQVNSSLD SLATSGGPGS HSLDLEVQHI QALIEANSAD DSFRAYAAST AAAAAAAVSS SSSAPASVAP ASISPPLNSP KSQHQHQQHA THQQQQESSY LDMPVKHYNG SRSGPLPTQH SPQRMHPYQR AVASPVEVSS GGGGLGLRNP ADITLNEYNR SEGSSAEELL RRTPLKIRAP EMLTAPAGYG TEPCRMTLKQ EPETGY // ID HOBO_DROME STANDARD; PRT; 644 AA. AC P12258; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transposable element Hobo transposase. GN T. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Streck R.D., Macgaffey J.E., Beckendorf S.K.; RT "The structure of hobo transposable elements and their insertion RT sites."; RL EMBO J. 5:3615-3623(1986). RN [2] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND VARIANT. RX MEDLINE=91330295; PubMed=1651170; RA Calvi B.R., Hong T.J., Findley S.D., Gelbart W.M.; RT "Evidence for a common evolutionary origin of inverted repeat RT transposons in Drosophila and plants: hobo, Activator, and Tam3."; RL Cell 66:465-471(1991). CC -!- FUNCTION: ESSENTIAL FOR HOBO TRANSPOSASE ACTIVITY. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- POLYMORPHISM: THE NUMBER OF REPEATS IS HIGHLY POLYMORPHIC AND CC VARIES AMONG DIFFERENT STRAINS. CC -!- SIMILARITY: CONTAINS 1 BED-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04705; CAA28410.1; -. DR EMBL; M69216; AAA51465.1; ALT_INIT. DR PIR; A25684; A25684. DR FlyBase; FBgn0014191; hobo\T. DR InterPro; IPR003656; BED_finger. DR InterPro; IPR008906; HATC. DR Pfam; PF05699; hATC; 1. DR SMART; SM00614; ZnF_BED; 1. DR PROSITE; PS50808; ZF_BED; 1. KW DNA integration; DNA recombination; Nuclear protein; DNA-binding; KW Repeat; Zinc-finger; Transposable element. FT ZN_FING 73 131 BED-TYPE. FT DOMAIN 521 550 10 X 3 AA TANDEM REPEATS OF T-P-E. FT REPEAT 521 523 1. FT REPEAT 524 526 2. FT REPEAT 527 529 3. FT REPEAT 530 532 4. FT REPEAT 533 535 5. FT REPEAT 536 538 6. FT REPEAT 539 541 7. FT REPEAT 542 544 8. FT REPEAT 545 547 9. FT REPEAT 548 550 10. FT VARIANT 521 541 MISSING. FT CONFLICT 576 576 P -> L (IN REF. 2). FT CONFLICT 638 644 ELKECFP -> AAERVFSLAGNIITEKRNRLCPKSVDSLLF FT LHSYYKNLNNSQ (IN REF. 2). SQ SEQUENCE 644 AA; 73387 MW; 83168CE40F64D3A6 CRC64; MAPYIMIVEF LCLWSSVSAV NCPFFVFYDA ITSLLGFSII WKPKEKVTIM AEAADFVKNK INNGTYSVAN KHKGKSVIWS ILCDILKEDE TVLDGWLFCR QCQKVLKFLH KNTSNLSRHK CCLTLRRPTE LKIVSENDKK VAIEKCTQWV VQDCRPFSAV TGAGFKNLVK FFLQIGAIYG EQVDVDDLLP DPTTLSRKAK SDAEEKRSLI SSEIKKAVDS GRASATVDMW TDQYVQRNFL GITFHYEKEF KLCDMILGLK SMNFQKSTAE NILMKIKGLF SEFNVENIDN VKFVTDRGAN IKKALEGNTR LNCSSHLLSN VLEKSFNEAN ELKKIVKSCK KIVKYCKKSN LQHTLETTLK SACPTRWNSN YKMMKSILDN WRSVDKILGE ADIHVDFNKS SLKVVVDILG DFERIFKKLQ TSSSPSICFV LPSISKILEL CEPNILDLSA AALLKERILE NIRKIWMANL SIWHKAAFFL YPPAAHLQEE DILEIKVFCI SQIQVPISYT LSLESTETPR TPETPETPET PETPETPETP ETPETPETPE SLESPNLFPK KNKTISSENE FFFPKPVTES NSNFNESPLD EIERYIRQRV PLSQNFEVIE WWKNNANLYP QLSKLALKLL SIPASSAELK ECFP // ID HOW_DROME STANDARD; PRT; 405 AA. AC O01367; O02392; P91680; Q8IN11; Q8T999; Q94539; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Held out wings protein (KH-domain protein KH93F) (Putative RNA-binding DE protein) (Muscle-specific protein) (Wings held out protein) (Struthio DE protein) (Quaking-related 93F). GN HOW OR WHO OR STRU OR KH93F OR QKR93F OR CG10293. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM ZYGOTIC), FUNCTION, INDUCTION, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF ARG-185. RX MEDLINE=97236479; PubMed=9118803; RA Baehrecke E.H.; RT "who encodes a KH RNA binding protein that functions in muscle RT development."; RL Development 124:1323-1332(1997). RN [2] RP SEQUENCE FROM N.A. (ISOFORM ZYGOTIC), FUNCTION, AND SUBCELLULAR RP LOCATION. RC STRAIN=Oregon-R; RX MEDLINE=97313250; PubMed=9169854; RA Zaffran S., Astier M., Gratecos D., Semeriva M.; RT "The held out wings (how) Drosophila gene encodes a putative RNA- RT binding protein involved in the control of muscular and cardiac RT activity."; RL Development 124:2087-2098(1997). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS MATERNAL AND ZYGOTIC), FUNCTION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=98008900; PubMed=9344542; RA Lo P.C.H., Frasch M.; RT "A novel KH-domain protein mediates cell adhesion processes in RT Drosophila."; RL Dev. Biol. 190:241-256(1997). RN [4] RP SEQUENCE FROM N.A. (ISOFORM ZYGOTIC), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=97473527; PubMed=9332381; RA Fyrberg C., Becker J., Barthmaier P., Mahaffey J., Fyrberg E.; RT "A Drosophila muscle-specific gene related to the mouse quaking RT locus."; RL Gene 197:315-323(1997). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [7] RP SEQUENCE FROM N.A. (ISOFORM ZYGOTIC). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR INTEGRIN-MEDIATED CELL-ADHESION IN WING CC BLADE. VITAL ROLE IN STEROID REGULATION OF MUSCLE DEVELOPMENT AND CC TO CONTROL HEART RATE. REQUIRED DURING EMBRYOGENESIS, IN LATE CC STAGES OF SOMATIC MUSCLE DEVELOPMENT, FOR MYOTUBE MIGRATION AND CC DURING METAMORPHOSIS FOR MUSCLE REORGANIZATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Zygotic; Synonyms=A; CC IsoId=O01367-1; Sequence=Displayed; CC Name=Maternal; Synonyms=B; CC IsoId=O01367-2; Sequence=VSP_050197; CC -!- TISSUE SPECIFICITY: DURING EMBRYOGENESIS, EXPRESSION IS SEEN IN CC MESODERMAL PRECURSORS OF SOMATIC, VISCERAL AND PHARYNGEAL MUSCLE. CC LATER IN EMBRYOGENESIS, EXPRESSION IS RESTRICTED TO HEART AND CC MUSCLE ATTACHMENT SITES OF THE EPIDERMIS. DURING ONSET OF CC METAMORPHOSIS, EXPRESSION IS SEEN IN MUSCLE AND MUSCLE ATTACHMENT CC CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC DURING EMBRYONIC, LARVAL AND PUPAL DEVELOPMENT. CC -!- INDUCTION: BY 20-HYDROXYECDYSONE AT THE ONSET OF METAMORPHOSIS. CC -!- MISCELLANEOUS: MUTANTS EXHIBIT WING BLISTERS AND FLIGHT CC IMPAIRMENT. CC -!- SIMILARITY: CONTAINS 1 KH DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85651; AAB51251.1; -. DR EMBL; U72331; AAB17350.1; -. DR EMBL; AF003106; AAB60946.1; -. DR EMBL; AF003107; AAB60947.1; -. DR EMBL; U87150; AAB47553.1; -. DR EMBL; AE003737; AAF55952.1; -. DR EMBL; AE003737; AAN13901.1; -. DR EMBL; AY069862; AAL40007.1; -. DR FlyBase; FBgn0017397; how. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003723; F:RNA binding; IDA. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_type_1. DR Pfam; PF00013; KH; 1. DR SMART; SM00322; KH; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. KW Developmental protein; Nuclear protein; RNA-binding; KW Alternative splicing. FT DOMAIN 11 73 GLN-RICH. FT DOMAIN 142 210 KH. FT VARSPLIC 370 405 VGAIKQQRRLATNREHPYQRATVGVPAKPAGFIEIQ -> G FT GLFAR (in isoform Maternal). FT /FTId=VSP_050197. FT MUTAGEN 185 185 R->C: IN ALLELE HOW-E44; EMBRYONIC FT LETHAL. FT CONFLICT 33 33 Q -> QQA (IN REF. 3). FT CONFLICT 46 46 Q -> QAQ (IN REF. 7). FT CONFLICT 52 52 P -> S (IN REF. 7). FT CONFLICT 338 339 QT -> RA (IN REF. 4). FT CONFLICT 370 370 MISSING (IN REF. 2, 4 AND 7). FT CONFLICT 384 384 E -> A (IN REF. 4). SQ SEQUENCE 405 AA; 44325 MW; DCA3A29A12D1A55E CRC64; MSVCESKAVV QQQLQQHLQQ QAAAAVVAVA QQQQAQAQAQ AQAQAQQQQQ APQVVVPMTP QHLTPQQQQQ STQSIADYLA QLLKDRKQLA AFPNVFTHVE RLLDEEIARV RASLFQINGV KKEPLTLPEP EGSVVTMNEK VYVPVREHPD FNFVGRILGP RGMTAKQLEQ ETGCKIMVRG KGSMRDKKKE DANRGKPNWE HLSDDLHVLI TVEDTENRAT VKLAQAVAEV QKLLVPQAEG EDELKKRQLM ELAIINGTYR DTTAKSVAVC DEEWRRLVAA SDSRLLTSTG LPGLAAQIRA PAAAPLGAPL ILNPRMTVPT TAASILSAQA APTAAFDQTG HGMIFAPYDY ANYAALAGNP LLTEYADHSV GAIKQQRRLA TNREHPYQRA TVGVPAKPAG FIEIQ // ID HP1_DROME STANDARD; PRT; 206 AA. AC P05205; Q9VLR6; DT 13-AUG-1987 (Rel. 05, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heterochromatin protein 1 (HP1) (Nonhistone chromosomal protein C1A9 DE antigen). GN SU(VAR)205 OR HP1 OR CG8409. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87089729; PubMed=3099166; RA James T.C., Elgin S.C.R.; RT "Identification of a nonhistone chromosomal protein associated with RT heterochromatin in Drosophila melanogaster and its gene."; RL Mol. Cell. Biol. 6:3862-3872(1986). RN [2] RP REVISIONS, SEQUENCE FROM N.A. RX MEDLINE=91088623; PubMed=2124708; RA Eissenberg J.C., James T.C., Forster-Hartnett D.W., Hartnett T., RA Ngan V., Elgin S.C.R.; RT "Mutation in a heterochromatin-specific chromosomal protein is RT associated with suppression of position-effect variegation in RT Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9923-9927(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP CHROMO DOMAIN. RX MEDLINE=91204431; PubMed=1708124; RA Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., RA Paro R., James T.C., Gaunt S.J.; RT "A sequence motif found in a Drosophila heterochromatin protein is RT conserved in animals and plants."; RL Nucleic Acids Res. 19:789-794(1991). RN [6] RP INTERACTION WITH SU(VAR)39. RX MEDLINE=21856321; PubMed=11867540; RA Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S., RA Jenuwein T., Dorn R., Reuter G.; RT "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation RT and heterochromatic gene silencing."; RL EMBO J. 21:1121-1131(2002). CC -!- FUNCTION: STRUCTURAL COMPONENT OF HETEROCHROMATIN, INVOLVED IN CC GENE REPRESSION AND THE MODIFICATION OF POSITION-EFFECT- CC VARIEGATION. RECOGNIZES AND BINDS HISTONE H3 TAILS METHYLATED AT CC LYS-9, LEADING TO EPIGENETIC REPRESSION. CC -!- SUBUNIT: PROBABLY ASSOCIATES WITH SU(VAR)39. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 2 CHROMO DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M57574; AAA28620.1; -. DR EMBL; M14131; AAA28402.1; ALT_SEQ. DR EMBL; AE003620; AAF52618.1; -. DR EMBL; AY061119; AAL28667.1; -. DR PIR; A39268; A39268. DR PDB; 1KNA; 20-MAR-02. DR PDB; 1KNE; 20-MAR-02. DR FlyBase; FBgn0003607; Su(var)205. DR GO; GO:0006343; P:establishment of chromatin silencing; IMP. DR InterPro; IPR000953; Chromo. DR InterPro; IPR008251; Chromo_shadow. DR Pfam; PF00385; chromo; 1. DR Pfam; PF01393; Chromo_shadow; 1. DR PRINTS; PR00504; CHROMODOMAIN. DR SMART; SM00298; CHROMO; 2. DR SMART; SM00300; ChSh; 1. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 2. KW Chromatin regulator; Nuclear protein; Transcription regulation; KW Repressor; Repeat; 3D-structure. FT DOMAIN 18 23 POLY-GLU. FT DOMAIN 24 82 CHROMO 1. FT DOMAIN 147 205 CHROMO 2. FT DOMAIN 95 206 BINDS TO SU(VAR)39. SQ SEQUENCE 206 AA; 23185 MW; 6A5B204C487526B7 CRC64; MGKKIDNPES SAKVSDAEEE EEEYAVEKII DRRVRKGKVE YYLKWKGYPE TENTWEPENN LDCQDLIQQY EASRKDEEKS AASKKDRPSS SAKAKETQGR ASSSTSTASK RKSEEPTAPS GNKSKRTTDA EQDTIPVSGS TGFDRGLEAE KILGASDNNG RLTFLIQFKG VDQAEMVPSS VANEKIPRMV IHFYEERLSW YSDNED // ID HR38_DROME STANDARD; PRT; 1073 AA. AC P49869; O18383; Q9VIK4; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable nuclear hormone receptor HR38 (dHR38). GN HR38 OR NR4A4 OR CG1864. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC TISSUE=Larva; RX MEDLINE=95372400; PubMed=7644522; RA Sutherland J.D., Kozlova T., Tzertzinis G., Kafatos F.C.; RT "Drosophila hormone receptor 38: a second partner for Drosophila USP RT suggests an unexpected role for nuclear receptors of the nerve growth RT factor-induced protein B type."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7966-7970(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORM SHORT), AND TISSUE SPECIFICITY. RX MEDLINE=98370123; PubMed=9704500; RA Komonyi O., Mink M., Csiha J., Maroy P.; RT "Genomic organization of DHR38 gene in Drosophila: presence of RT Alu-like repeat in a translated exon and expression during embryonic RT development."; RL Arch. Insect Biochem. Physiol. 38:185-192(1998). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG), AND CHARACTERIZATION. RC TISSUE=Larva; RX MEDLINE=98315108; PubMed=9649534; RA Kozlova T., Pokholkova G.V., Tzertzinis G., Sutherland J.D., RA Zhimulev I.F., Kafatos F.C.; RT "Drosophila hormone receptor 38 functions in metamorphosis: a role in RT adult cuticle formation."; RL Genetics 149:1465-1475(1998). RN [4] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 528-1073 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96068664; PubMed=7479849; RA Fisk G.J., Thummel C.S.; RT "Isolation, regulation, and DNA-binding properties of three RT Drosophila nuclear hormone receptor superfamily members."; RL Proc. Natl. Acad. Sci. U.S.A. 92:10604-10608(1995). CC -!- FUNCTION: BINDS TO NGFI-B RESPONSE ELEMENTS. PLAYS AN IMPORTANT CC ROLE IN LATE STAGES OF EPIDERMAL METAMORPHOSIS. CC -!- SUBUNIT: FORMS A HETERODIMER WITH USP. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P49869-1; Sequence=Displayed; CC Name=Short; CC IsoId=P49869-2; Sequence=VSP_003714; CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED IN PREBLASTODERM CC EMBRYOS, SPECIFICALLY IN CENTRAL NERVOUS SYSTEM AND INTESTINAL CC TRACT. HIGHLY EXPRESSED IN THIRD INSTAR LARVAL IMAGINAL DISKS AND CC BRAIN COMPLEXES, BUT NOT IN OVARIES. CC -!- DEVELOPMENTAL STAGE: LOW LEVELS IN 0-8 HOUR EMBRYOS AND ADULTS. CC HIGHER IN LATE EMBRYOGENESIS AND DURING LARVAL AND PUPAL STAGES. CC SHORT ISOFORM IS ENRICHED IN PUPAE AND ADULTS, LONG ISOFORM IN CC LARVAE. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR4 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X89246; CAA61534.1; -. DR EMBL; Y15606; CAA75690.1; -. DR EMBL; AJ002073; CAA05172.1; -. DR EMBL; AE003667; AAF53914.1; -. DR EMBL; U36762; AAC46926.1; -. DR HSSP; P19793; 2NLL. DR TRANSFAC; T02760; -. DR FlyBase; FBgn0014859; Hr38. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Alternative splicing; Developmental protein. FT DNA_BIND 744 809 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 744 764 C4-TYPE. FT ZN_FING 780 804 C4-TYPE. FT DOMAIN 188 192 POLY-ALA. FT DOMAIN 206 218 POLY-ALA. FT DOMAIN 221 228 POLY-ALA. FT DOMAIN 268 272 POLY-THR. FT DOMAIN 294 312 POLY-GLN. FT DOMAIN 441 462 POLY-GLN. FT DOMAIN 505 508 POLY-SER. FT DOMAIN 619 626 POLY-GLN. FT DOMAIN 661 665 POLY-ALA. FT VARSPLIC 1 522 Missing (in isoform Short). FT /FTId=VSP_003714. FT CONFLICT 667 667 V -> VSSPSV (IN REF. 4). FT CONFLICT 685 685 S -> L (IN REF. 1 AND 3). FT CONFLICT 689 692 STAQ -> LHGER (IN REF. 2). FT CONFLICT 697 697 A -> D (IN REF. 2). FT CONFLICT 702 702 N -> S (IN REF. 2). FT CONFLICT 1041 1041 S -> R (IN REF. 2). FT CONFLICT 1064 1064 E -> D (IN REF. 2). SQ SEQUENCE 1073 AA; 116991 MW; 126A30DAFA1C096A CRC64; MMRDRLASLI VVKQEGGSNT SISHHQATAI KCEASLYTES SLFQEINNNS CYRQNLNAPT HQQSHTSHLQ HAQQHQTHQQ HPLLPPPLPT LPLIYPCRNL FPDGCDINHL ACCSSSNSNS NCNSDSNSTS SSPGNSHFFA NGNTCAAALT PAPPATEPRK IKPLGAGKLK VGKTDSNSDS NSNCDSRAAA AASTSATSAT SATTLAATAA ATAAAAEAGG AASAAAAAKI SQVRLTNQAT TSMLLLQPNS SFSSLSPFDN FSTQTASTTT TTSASAAGHH QHHNHLLHQQ HHNQQQQQQQ QQQQQQQQQQ QQEHLQQQHQ QQLVSPQQHL LKSETLLSHE EDQLISNLTD SSVVSHSELF SDLFFPSDSN NSLLSPTTSG YPDNPAEDLT SSIENLTKLT CLRDKRLSSI PEQQLSSEQE QQLCLLSLRS SSDPAIALHA QQQQQQQQQQ QQQQQQHQQQ QQHLQLQLIS PIGGPLSCGS SLPSFQETYS LKYNSSSGSS PQQASSSSTA APTPTDQVLT LKMDEDCFPP LSGGWSASPP APSQLQQLHT LQSQAQMSHP NSSNNSSNNA GNSHNNSGGY NYHGHFNAIN ASANLSPSSS ASSLYEYNGV SAADNFYGQQ QQQQQQSYQQ HNYNSHNGER YSLPTFPTIS ELAAATAAVE AAAAATVGGP PPVRRASLPV QRTVSPAGST AQSPKLAKIT LNQRHSHAHA HALQLNSAPN SAASSPASAD LQAGRLLQAP SQLCAVCGDT AACQHYGVRT CEGCKGFFKR TVQKGSKYVC LADKNCPVDK RRRNRCQFCR FQKCLVVGMV KEVVRTDSLK GRRGRLPSKP KSPQESPPSP PISLITALVR SHVDTTPDPS CLDYSHYEEQ SMSEADKVQQ FYQLLTSSVD VIKQFAEKIP GYFDLLPEDQ ELLFQSASLE LFVLRLAYRA RIDDTKLIFC NGTVLHRTQC LRSFGEWLND IMEFSRSLHN LEIDISAFAC LCALTLITER HGLREPKKVE QLQMKIIGSL RDHVTYNAEA QKKQHYFSRL LGKLPELRSL SVQGLQRIFY LKLEDLVPAP ALIENMFVTT LPF // ID HR3_DROME STANDARD; PRT; 487 AA. AC P31396; Q9V5I0; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable nuclear hormone receptor HR3 (dHR3). GN HR46 OR HR3 OR NR1F4 OR CG11823. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92335259; PubMed=1631105; RA Koelle M.R., Segraves W.A., Hogness D.S.; RT "DHR3: a Drosophila steroid receptor homolog."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6167-6171(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PUTATIVE RECEPTOR WHOSE LIGAND IS NOT YET KNOWN. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- INDUCTION: THE EXPRESSION OF THIS PROTEIN IS DEVELOPMENTALLY CC REGULATED SHOWING PEAKS AT MIDEMBRYOGENESIS. HR3 TRANSCRIPTION CC IS ECDYSONE-INDUCED. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR1 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M90806; AAA28461.1; -. DR EMBL; AE003830; AAF58826.1; -. DR PIR; A46146; A46146. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T02750; -. DR FlyBase; FBgn0000448; Hr46. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; IDA. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 51 116 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 51 71 C4-TYPE. FT ZN_FING 87 111 C4-TYPE. FT DOMAIN 255 487 LIGAND-BINDING (POTENTIAL). SQ SEQUENCE 487 AA; 55284 MW; 774587D2E79204EC CRC64; MYTQRMFDMW SSVTSKLEAH ANNLGQSNVQ SPAGQNNSSG SIKAQIEIIP CKVCGDKSSG VHYGVITCEG CKGFFRRSQS SVVNYQCPRN KQCVVDRVNR NRCQYCRLQK CLKLGMSRDA VKFGRMSKKQ REKVEDEVRF HRAQMRAQSD AAPDSSVYDT QTPSSSDQLH HNNYNSYSGG YSNNEVGYGS PYGYSASVTP QQTMQYDISA DYVDSTTYEP RSTIIDPEFI SHADGDINDV LIKTLAEAHA NTNTKLEAVH DMFRKQPDVS RILYYKNLGQ EELWLDCAEK LTQMIQNIIE FAKLIPGFMR LSQDDQILLL KTGSFELAIV RMSRLLDLSQ NAVLYGDVML PQEAFYTSDS EEMRLVSRIF QTAKSIAELK LTETELALYQ SLVLLWPERN GVRGNTEIQR LFNLSMNAIR QELETNHAPL KGDVTVLDTL LNNIPNFRDI SILHMESLSK FKLQHPNVVF PALYKELFSI DSQQDLT // ID HR78_DROME STANDARD; PRT; 601 AA. AC Q24142; Q24108; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Nuclear hormone receptor HR78 (dHR78) (Nuclear receptor XR78E/F). GN HR78 OR HR78D OR NR2D1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=96068664; PubMed=7479849; RA Fisk G.J., Thummel C.S.; RT "Isolation, regulation, and DNA-binding properties of three RT Drosophila nuclear hormone receptor superfamily members."; RL Proc. Natl. Acad. Sci. U.S.A. 92:10604-10608(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96068638; PubMed=7479823; RA Zelhof A.C., Yao T.P., Evans R.M., McKeown M.; RT "Identification and characterization of a Drosophila nuclear receptor RT with the ability to inhibit the ecdysone response."; RL Proc. Natl. Acad. Sci. U.S.A. 92:10477-10481(1995). CC -!- FUNCTION: BINDS TO DIRECT REPEATS OF THE SEQUENCE 5'-AGGTCA-3'. CC INHIBITS THE ECDYSONE RESPONSE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: HIGHEST EXPRESSION IN THIRD-INSTAR LARVAE AND CC PREPUPAE. CC -!- INDUCTION: BY 20-HYDROXYECDYSONE (20HE) 106 HOURS AFTER EGG CC LAYING. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR2 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36791; AAC46927.1; -. DR EMBL; U31517; AAC46924.1; -. DR HSSP; P19793; 2NLL. DR TRANSFAC; T02759; -. DR FlyBase; FBgn0015239; Hr78. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; IDA. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 52 117 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 52 72 C4-TYPE. FT ZN_FING 88 112 C4-TYPE. FT DOMAIN 215 226 POLY-GLN. FT CONFLICT 142 142 G -> S (IN REF. 2). FT CONFLICT 178 188 ATPPVHSAPAT -> PRLQCTARQQR (IN REF. 2). FT CONFLICT 194 197 ENIF -> AEYI (IN REF. 2). FT CONFLICT 277 277 A -> V (IN REF. 2). FT CONFLICT 517 517 L -> F (IN REF. 2). FT CONFLICT 519 519 Q -> H (IN REF. 2). SQ SEQUENCE 601 AA; 65335 MW; AFE0D82CEEEA0654 CRC64; MDGVKVETFI KSEENRAMPL IGGGSASGGT PLPGGGVGMG AGASATLSVE LCLVCGDRAS GRHYGAISCE GCKGFFKRSI RKQLGYQCRG AMNCEVTKHH RNRCQFCRLQ KCLASGMRSD SVQHERKPIV DRKEGIIAAA GGSSTSGGGN GSSTYLSGKS GYQQGRGKGH SVKAESAATP PVHSAPATAF NLNENIFPMG LNFAELTQTL MFATQQQQQQ QQQHQQSGSY SPDIPKADPE DDEDDSMDNS STLCLQLLAN SASNNNSQHL NFNAGEAPTA LPTTSTMGLI QSSLDMRVIH KGLQILQPIQ NQLERNGNLS VKPECDSEAE DSGTEDAVDA ELEHMELDFE CGGNRSGGSD FAINEAVFEQ DLLTDVQCAF HVQPPTLVHS YLNIHYVCET GSRIIFLTIH TLRKVPVFEQ LEAHTQVKLL RGVWPALMAI ALAQCQGQLS VPTIIGQFIQ STRQLADIDK IEPLKISKMA NLTRTLHDFV QELQSLDVTD MEFGLLRLIL LFNPTLLQQR KERSLRGYVR RVQLYALSSL RRQGGIGGGE ERFNVLVARL LPLSSLDAEA MEELFFANLV GQMQMDALIP FILMTSNTSG L // ID HR96_DROME STANDARD; PRT; 723 AA. AC Q24143; Q9VBZ7; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nuclear hormone receptor HR96 (dHR96). GN HR96 OR NR1J1 OR CG11783. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=96068664; PubMed=7479849; RA Fisk G.J., Thummel C.S.; RT "Isolation, regulation, and DNA-binding properties of three RT Drosophila nuclear hormone receptor superfamily members."; RL Proc. Natl. Acad. Sci. U.S.A. 92:10604-10608(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: BINDS SELECTIVELY TO THE HSP27 20E RESPONSE ELEMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: HIGHEST EXPRESSION IN THIRD-INSTAR LARVAE AND CC PREPUPAE. CC -!- INDUCTION: BY 20-HYDROXYECDYSONE (20HE) 106 HOURS AFTER EGG CC LAYING. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR1 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36792; AAC46928.1; -. DR EMBL; AE003750; AAF56379.1; -. DR EMBL; AY051486; AAK92910.1; -. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T02756; -. DR FlyBase; FBgn0015240; Hr96. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 7 72 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 7 27 C4-TYPE. FT ZN_FING 43 67 C4-TYPE. SQ SEQUENCE 723 AA; 81028 MW; 439CC96A723AE9B6 CRC64; MSPPKNCAVC GDKALGYNFN AVTCESCKAF FRRNALAKKQ FTCPFNQNCD ITVVTRRFCQ KCRLRKCLDI GMKSENIMSE EDKLIKRRKI ETNRAKRRLM ENGTDACDAD GGEERDHKAP ADSSSSNLDH YSGSQDSQSC GSADSGANGC SGRQASSPGT QVNPLQMTAE KIVDQIVSDP DRASQAINRL MRTQKEAISV MEKVISSQKD ALRLVSHLID YPGDALKIIS KFMNSPFNAL TVFTKFMSSP TDGVEIISKI VDSPADVVEF MQNLMHSPED AIDIMNKFMN TPAEALRILN RILSGGGANA AQQTADRKPL LDKEPAVKPA APAERADTVI QSMLGNSPPI SPHDAAVDLQ YHSPGVGEQP STSSSHPLPY IANSPDFDLK TFMQTNYNDE PSLDSDFSIN SIESVLSEVI RIEYQAFNSI QQAASRVKEE MSYGTQSTYG GCNSAANNSQ PHLQQPICAP STQQLDRELN EAEQMKLREL RLASEALYDP VDEDLSALMM GDDRIKPDDT RHNPKLLQLI NLTAVAIKRL IKMAKKITAF RDMCQEDQVA LLKGGCTEMM IMRSVMIYDD DRAAWKVPHT KENMGNIRTD LLKFAEGNIY EEHQKFITTF DEKWRMDENI ILIMCAIVLF TSARSRVIHK DVIRLEQNSY YYLLRRYLES VYSGCEARNA FIKLIQKISD VERLNKFIIN VYLNVNPSQV EPLLREIFDL KNH // ID HS22_DROME STANDARD; PRT; 174 AA. AC P02515; Q95SZ4; Q9VSX1; DT 21-JUL-1986 (Rel. 01, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 22. GN HSP22 OR CG4460. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83189140; PubMed=6302284; RA Southgate R., Ayme A., Voellmy R.; RT "Nucleotide sequence analysis of the Drosophila small heat shock gene RT cluster at locus 67B."; RL J. Mol. Biol. 165:35-57(1983). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=82248004; PubMed=6285380; RA Ingolia T.D., Craig E.A.; RT "Four small Drosophila heat shock proteins are related to each other RT and to mammalian alpha-crystallin."; RL Proc. Natl. Acad. Sci. U.S.A. 79:2360-2364(1982). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01098; AAA28635.1; -. DR EMBL; AE003552; AAF50290.1; -. DR EMBL; AY060412; AAL25451.1; -. DR EMBL; AY119034; AAM50894.1; -. DR PIR; A02918; HHFF22. DR PIR; A20647; A20647. DR FlyBase; FBgn0001223; Hsp22. DR InterPro; IPR001436; Crystallin_alpha. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Multigene family. FT CONFLICT 44 44 H -> Q (IN REF. 3 AND 4). FT CONFLICT 53 53 L -> F (IN REF. 3 AND 4). FT CONFLICT 54 54 A -> P (IN REF. 2). FT CONFLICT 90 90 A -> G (IN REF. 3 AND 4). FT CONFLICT 109 111 RRF -> GRY (IN REF. 1). FT CONFLICT 115 115 E -> D (IN REF. 1). FT CONFLICT 123 128 TSTLSS -> SSSLSD (IN REF. 1). FT CONFLICT 168 168 K -> N (IN REF. 3 AND 4). FT CONFLICT 171 171 T -> A (IN REF. 3 AND 4). SQ SEQUENCE 174 AA; 19796 MW; EEE10ACC37BE9720 CRC64; MRSLPMFWRM AEEMARMPRL SSPFHAFFHE PPVWSVALPR NWQHIARWQE QELAPPATVN KDGYKLTLDV KDYSELKVKV LDESVVLVEA KSEQQEAEQG GYSSRHFLRR FVLPEGYEAD KVTSTLSSDG VLTISVPNPP GVQETLKERE VTIEQTGEPA KKSAEEPKDK TASQ // ID HS23_DROME STANDARD; PRT; 186 AA. AC P02516; Q9VSX5; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 23. GN HSP23 OR CG4463. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83189140; PubMed=6302284; RA Southgate R., Ayme A., Voellmy R.; RT "Nucleotide sequence analysis of the Drosophila small heat shock gene RT cluster at locus 67B."; RL J. Mol. Biol. 165:35-57(1983). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=82248004; PubMed=6285380; RA Ingolia T.D., Craig E.A.; RT "Four small Drosophila heat shock proteins are related to each other RT and to mammalian alpha-crystallin."; RL Proc. Natl. Acad. Sci. U.S.A. 79:2360-2364(1982). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01100; AAA28637.1; -. DR EMBL; V00210; CAA23494.1; -. DR EMBL; X03889; CAA27525.1; -. DR EMBL; AE003552; AAF50286.1; -. DR EMBL; AY061081; AAL28629.1; -. DR PIR; B20647; B20647. DR FlyBase; FBgn0001224; Hsp23. DR InterPro; IPR001436; Crystallin_alpha. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Multigene family. FT CONFLICT 31 33 QRN -> RRI (IN REF. 2). FT CONFLICT 81 81 K -> E (IN REF. 2). FT CONFLICT 88 88 K -> G (IN REF. 2). FT CONFLICT 95 95 L -> V (IN REF. 2). FT CONFLICT 173 173 N -> S (IN REF. 2). FT CONFLICT 182 182 N -> G (IN REF. 2). SQ SEQUENCE 186 AA; 20629 MW; 3C6EDCDA1719B5A0 CRC64; MANIPLLLSL ADDLGRMSMV PFYEPYYCQR QRNPYLALVG PMEQQLRQLE KQVGASSGSS GAVSKIGKDG FQVCMDVSHF KPSELVVKVQ DNSVLVEGNH EEREDDHGFI TRHFVRRYAL PPGYEADKVA STLSSDGVLT IKVPKPPAIE DKGNERIVQI QQVGPAHLNV KENPKEAVEQ DNGNDK // ID HS26_DROME STANDARD; PRT; 208 AA. AC P02517; Q9VSX3; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 26. GN HSP26 OR CG4183. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83189140; PubMed=6302284; RA Southgate R., Ayme A., Voellmy R.; RT "Nucleotide sequence analysis of the Drosophila small heat shock gene RT cluster at locus 67B."; RL J. Mol. Biol. 165:35-57(1983). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=82248004; PubMed=6285380; RA Ingolia T.D., Craig E.A.; RT "Four small Drosophila heat shock proteins are related to each other RT and to mammalian alpha-crystallin."; RL Proc. Natl. Acad. Sci. U.S.A. 79:2360-2364(1982). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01099; AAA28636.1; -. DR EMBL; X03890; CAA27526.1; -. DR EMBL; AE003552; AAF50288.1; -. DR PIR; C20647; C20647. DR FlyBase; FBgn0001225; Hsp26. DR InterPro; IPR001436; Crystallin_alpha. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Multigene family. FT CONFLICT 35 35 L -> LL (IN REF. 2). FT CONFLICT 192 192 E -> D (IN REF. 2). SQ SEQUENCE 208 AA; 22994 MW; 75781CB2C309E33C CRC64; MSLSTLLSLV DELQEPRSPI YELGLGLHPH SRYVLPLGTQ QRRSINGCPC ASPICPSSPA GQVLALRREM ANRNDIHWPA TAHVGKDGFQ VCMDVAQFKP SELNVKVVDD SILVEGKHEE RQDDHGHIMR HFVRRYKVPD GYKAEQVVSQ LSSDGVLTVS IPKPQAVEDK SKERIIQIQQ VGPAHLNVKA NESEVKGKEN GAPNGKDK // ID HS27_DROME STANDARD; PRT; 213 AA. AC P02518; Q9VSX6; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 27. GN HSP27 OR CG4466. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83189140; PubMed=6302284; RA Southgate R., Ayme A., Voellmy R.; RT "Nucleotide sequence analysis of the Drosophila small heat shock gene RT cluster at locus 67B."; RL J. Mol. Biol. 165:35-57(1983). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=82248004; PubMed=6285380; RA Ingolia T.D., Craig E.A.; RT "Four small Drosophila heat shock proteins are related to each other RT and to mammalian alpha-crystallin."; RL Proc. Natl. Acad. Sci. U.S.A. 79:2360-2364(1982). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01101; AAA28638.1; -. DR EMBL; X03891; CAA27527.1; -. DR EMBL; AE003552; AAF50285.1; -. DR PIR; A02921; HHFF27. DR PIR; D20647; D20647. DR FlyBase; FBgn0001226; Hsp27. DR InterPro; IPR001436; Crystallin_alpha. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Multigene family. FT CONFLICT 40 40 H -> N (IN REF. 2). FT CONFLICT 66 66 H -> P (IN REF. 2). FT CONFLICT 94 94 M -> I (IN REF. 2). FT CONFLICT 143 147 FDPNE -> LTPTK (IN REF. 2). FT CONFLICT 161 161 K -> R (IN REF. 2). FT CONFLICT 167 170 SKEQ -> GRER (IN REF. 2). FT CONFLICT 178 178 Q -> R (IN REF. 2). SQ SEQUENCE 213 AA; 23617 MW; E08B39801A181F39 CRC64; MSIIPLLHLA RELDHDYRTD WGHLLEDDFG FGVHAHDLFH PRRLLLPNTL GLGRRRYSPY ERSHGHHNQM SRRASGGPNA LLPAVGKDGF QVCMDVSQFK PNELTVKVVD NTVVVEGKHE EREDGHGMIQ RHFVRKYTLP KGFDPNEVVS TVSSDGVLTL KAPPPPSKEQ AKSERIVQIQ QTGPAHLSVK APAPEAGDGK AENGSGEKME TSK // ID HS2S_DROME STANDARD; PRT; 349 AA. AC P25722; Q9VIW4; DT 01-MAY-1992 (Rel. 22, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heparin sulfate O-sulfotransferase (EC 2.8.2.-). GN HS2ST OR CG10234. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; RX MEDLINE=92038937; PubMed=1936954; RA Powers P.A., Ganetzky B.; RT "On the components of segregation distortion in Drosophila RT melanogaster. V. Molecular analysis of the Sd locus."; RL Genetics 129:133-144(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM S1). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI MEMBRANE (BY CC SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=S1; CC IsoId=P25722-1; Sequence=Displayed; CC Name=S2; CC IsoId=P25722-2; Sequence=VSP_004382; CC Name=S4; CC IsoId=P25722-3; Sequence=VSP_004383; CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT TO BE SD. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 296. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60218; CAA42779.1; ALT_FRAME. DR EMBL; AE003663; AAF53800.1; -. DR EMBL; AY058422; AAL13651.1; -. DR PIR; S18765; S18765. DR FlyBase; FBgn0024230; Hs2st. DR InterPro; IPR007734; HS2ST. DR Pfam; PF05040; HS2ST; 1. KW Transferase; Transmembrane; Glycoprotein; Golgi stack; Signal-anchor; KW Alternative splicing. FT DOMAIN 1 17 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 18 38 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 39 349 LUMENAL (POTENTIAL). FT CARBOHYD 107 107 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 126 126 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 282 282 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 24 MFRKLLKMWILLRPTHWLILIALC -> MKRSAECSEWQAF FT FESDDGFRQPGIIITIDEAFEAII (in isoform S2). FT /FTId=VSP_004382. FT VARSPLIC 1 255 Missing (in isoform S4). FT /FTId=VSP_004383. FT CONFLICT 28 28 C -> S (IN REF. 1). FT CONFLICT 180 181 DN -> EH (IN REF. 1). SQ SEQUENCE 349 AA; 41273 MW; E4655D92D7615C41 CRC64; MFRKLLKMWI LLRPTHWLIL IALCAVTCAG YWLLWSEIRL EHAFKPLSKL GDSLSPDQHA SSTTDDFDFE EHLVVLYNRV PKTGSTSFVN IAYDLCKPNK FHVLHINVTA NMHVLSLPNQ IQFVRNVSRW HEMKPALYHG HMAFLDFSKF QIAHKPIYIN LVRKPLDRLV SYYYFLRFGD NYRPNLVRKK AGNKITFDEC VVQKQPDCDP KNMWLQIPFF CGHAAECWEP GSSWALDQAK RNLVNEYFLV GVTEQMYEFV DLLERSLPRI FHGFREHYHN SNKSHLRVTS SKLPPSESTI KSIQKTKIWQ MENDLYDFAL AQFEFNKKKL MQPDNKHVQK FMYEKIRPK // ID HS68_DROME STANDARD; PRT; 635 AA. AC O97125; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 68. GN HSP68 OR CG5436. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA McColl G., McKechnie S.W.; RT "The heat shock gene hsp68 of D. melanogaster."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF096275; AAD16140.1; -. DR EMBL; AE003746; AAF56230.1; -. DR HSSP; P19120; 3HSC. DR FlyBase; FBgn0001230; Hsp68. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; FALSE_NEG. KW ATP-binding; Heat shock. SQ SEQUENCE 635 AA; 69743 MW; B3A429D415BA8035 CRC64; MPAIGIDLGT TYSCVGVFQY GKVEIIANDQ GNRTTPSYVA FTDSERLIGD AAKNQVAMNP KNSVFDAKRL IGRRFDDSKI QEDIKHWPFK VINDNGKPKI SVEFKGANKC FSPEEISSMV LTKMKETAEA YLGTTVKDAV ITVPAYFNDS QRQATKDAGA IAGINVLRII NEPTAAALAY GLDKNLKGER NVLIFDLGGG TFDVSILTID EGSLFEVRST AGDTHLGGED FDNRLVNHFA EEFKRKYKKD LRSNPRALRR LRTAAERAKR TLSSSTEASL EIDALYEGHD FYSKVSRARF EELCGDLFRN TLEPVEKALK DAKMDKSQIH DIVLVGGSTR IPKVQNLLQN FFGGKTLNLS INPDEAVAYG AAIQAAILSG DKSSEIKDVL LVDVAPLSLG IETAGGVMTK LIERNSRIPC KQSKTFTTYA DNQPAVTIQV FEGERALTKD NNVLGTFDLT GVPPAPRGVP KIDVTFDLDA NGILNVTAKE QGTGNAKNIT IKNDKGRLSQ ADIDRMLSEA EKYAEEDERH RQRIAARNQL ETYLFGVKEA AENGGDRISA ADKSSIVERC SEAMKWLDSN TTAEKEEYEY KLKELEQFCS PIMTKMHKGG GDGQQAPNFG QQAGGYKGPT VEEVD // ID HS6A_DROME STANDARD; PRT; 238 AA. AC P05812; Q9VSX4; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 67B1. GN HSP67BA OR CG4167. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86055735; PubMed=3933974; RA Ayme A., Tissieres A.; RT "Locus 67B of Drosophila melanogaster contains seven, not four, RT closely related heat shock genes."; RL EMBO J. 4:2949-2954(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M26267; AAA28634.1; -. DR EMBL; AE003552; AAF50287.1; ALT_SEQ. DR PIR; A24675; HHFF67. DR FlyBase; FBgn0001227; Hsp67Ba. DR InterPro; IPR001436; Crystallin_alpha. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Multigene family. SQ SEQUENCE 238 AA; 26591 MW; 4D6CEA7610352F51 CRC64; MSLIPFILDL AEELHDFNRS LAMDIDDSAG FGLYPLEATS QLPQLSRGVG AWECNDVGAH QGSVGGHRSI AIIRTIVWPE PRLLAAISRW WSWKRNWAIR ARPGQAARPV ANGASKSAYS VVNRNGFQVS MNVKQFAANE LTVKTIDNCI VVEGQHDEKE DGHGVISRHF IRKYILPKGY DPNEVHSTLS SDGILTVKAP QPLPVVKGSL ERQERIVDIQ QISQQQKDKD AHRQSRQR // ID HS6B_DROME STANDARD; PRT; 111 AA. AC P22978; Q9VSX0; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 67B2. GN HSP67BB OR CG4456. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88245191; PubMed=2454316; RA Pauli D., Tonka C.H., Ayme-Southgate A.; RT "An unusual split Drosophila heat shock gene expressed during RT embryogenesis, pupation and in testis."; RL J. Mol. Biol. 200:47-53(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING EMBRYOGENESIS AND PUPATION. CC -!- SIMILARITY: CONTAINS 1 RHODANESE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07311; CAA30276.1; -. DR EMBL; AE003552; AAF50291.1; -. DR PIR; S00688; S00688. DR FlyBase; FBgn0001228; Hsp67Bb. DR InterPro; IPR001763; Rhodanese-like. DR Pfam; PF00581; Rhodanese; 1. DR SMART; SM00450; RHOD; 1. DR PROSITE; PS50206; RHODANESE_3; 1. KW Heat shock. FT DOMAIN 12 110 RHODANESE. SQ SEQUENCE 111 AA; 12614 MW; 9D04C1BCE0986658 CRC64; MATYEQVKDV PNHPDVYLID VRRKEELQQT GFIPASINIP LDELDKALNL DGSAFKNKYG RSKPEKQSPI IFTCRSGNRV LEAEKIAKSQ GYSNVVIYKG SWNEWAQKEG L // ID HS6C_DROME STANDARD; PRT; 169 AA. AC P22979; Q9VSW9; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 67B3 (Heat shock 18 kDa protein). GN HSP67BC OR CG4190. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88118925; PubMed=3123699; RA Pauli D., Tonka C.H.; RT "A Drosophila heat shock gene from locus 67B is expressed during RT embryogenesis and pupation."; RL J. Mol. Biol. 198:235-240(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING EMBRYOGENESIS AND PUPATION. CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06542; CAA29788.1; -. DR EMBL; AE003552; AAF50292.1; ALT_SEQ. DR PIR; S00900; S00900. DR FlyBase; FBgn0001229; Hsp67Bc. DR InterPro; IPR001436; Crystallin_alpha. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR PROSITE; PS01031; HSP20; FALSE_NEG. KW Heat shock; Multigene family. SQ SEQUENCE 169 AA; 18799 MW; 65495B5777FFD141 CRC64; MPDIPFVLNL DSPDSMYYGH DMFPNRMYRR LHSRQHHDLD LHTLGLIARM GAHAHHLVAN KRNGELAALS RGGASNKQGN FEVHLDVGLF QPGELTVKLV NECIVVEGKH EEREDDHGHV SRHFVPAVSA AQGVRFGCHC FHFVGGWSSQ YHGSTISFQG GAQGAHHTH // ID HS70_DROME STANDARD; PRT; 642 AA. AC P82910; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Major heat shock 70 kDa protein Aa (Heat shock protein 70Aa) (HSP70- DE 87A7). GN HSP70AA OR HSP70A OR CG18743. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=122, AUS, B28, FRV3-1, QD18, and Z(H)1; RA Bettencourt B.R.; RT "Rapid concerted evolution via gene conversion at the Drosophila heat RT shock protein Hsp70 genes."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., RA Gabor Miklos G.L., Abril J.F., Agbayani A., An H.J., RA Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., RA Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., RA Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., RA Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., RA Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., RA Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., RA Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., RA Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., RA Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., RA Gu Z., Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., RA Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., RA Wei M.H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., RA Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., RA Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., RA Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., RA Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., RA Pollard J., Puri V., Reese M.G., Reinert K., Remington K., RA Saunders R.D., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., RA Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., RA Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., RA Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., RA Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., RA Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- INDUCTION: HEAT SHOCK INDUCES THE SYNTHESIS OF SEVEN PROTEINS AT CC FIVE OTHERWISE INACTIVE SITES IN THE POLYTENE CHROMOSOMES OF FRUIT CC FLY LARVAE. TWO SEPARATE SITES, PRODUCING TWO AND THREE COPIES, CC RESPECTIVELY, CODE FOR THE 70 KDA PROTEIN. CC -!- MISCELLANEOUS: THERE ARE TWO COPIES OF THE GENE CODING FOR THIS CC PROTEIN AT CHROMOSOME LOCUS 87A7. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF295933; AAG26887.1; -. DR EMBL; AF295934; AAG26888.1; -. DR EMBL; AF295935; AAG26889.1; -. DR EMBL; AF295936; AAG26890.1; -. DR EMBL; AF295937; AAG26891.1; -. DR EMBL; AF295938; AAG26892.1; -. DR EMBL; AE003693; AAG22148.1; ALT_SEQ. DR HSSP; P08107; 1HJO. DR FlyBase; FBgn0013275; Hsp70Aa. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock; Multigene family; KW Polymorphism. FT VARIANT 441 441 Y -> S (IN STRAIN FRV3-1). FT VARIANT 495 495 K -> T (IN STRAIN QD18). FT VARIANT 593 593 L -> M (IN STRAIN 122). FT VARIANT 615 615 MISSING (IN STRAIN 122). FT VARIANT 636 636 P -> R (IN STRAIN QD18). FT CONFLICT 241 241 E -> D (IN REF. 1). FT CONFLICT 350 350 E -> D (IN REF. 1). SQ SEQUENCE 642 AA; 70188 MW; A2C0E3030CEECE32 CRC64; MPAIGIDLGT TYSCVGVYQH GKVEIIANDQ GNRTTPSYVA FTDSERLIGD PAKNQVAMNP RNTVFDAKRL IGRKYDDPKI AEDMKHWPFK VVSDGGKPKI GVEYKGESKR FAPEEISSMV LTKMKETAEA YLGESITDAV ITVPAYFNDS QRQATKDAGH IAGLNVLRII NEPTAAALAY GLDKNLKGER NVLIFDLGGG TFDVSILTID EGSLFEVRST AGDTHLGGED FDNRLVTHLA EEFKRKYKKD LRSNPRALRR LRTAAERAKR TLSSSTEATI EIDALFEGQD FYTKVSRARF EELCADLFRN TLQPVEKALN DAKMDKGQIH DIVLVGGSTR IPKVQSLLQE FFHGKNLNLS INPDEAVAYG AAVQAAILSG DQSGKIQDVL LVDVAPLSLG IETAGGVMTK LIERNCRIPC KQTKTFSTYA DNQPGVSIQV YEGERAMTKD NNALGTFDLS GIPPAPRGVP QIEVTFDLDA NGILNVSAKE MSTGKAKNIT IKNDKGRLSQ AEIDRMVNEA EKYADEDEKH RQRITSRNAL ESYVFNVKQA VEQAPAGKLD EADKNSVLDK CNDTIRWLDS NTTAEKEEFD HKLEELTRHC SPIMTKMHQQ GAGAGAGGPG ANCGQQAGGF GGYSGPTVEE VD // ID HS71_DROME STANDARD; PRT; 643 AA. AC P02825; DT 21-JUL-1986 (Rel. 01, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Major heat shock 70 kDa protein Ab (Heat shock protein 70Ab) (HSP70- DE 87A7). GN HSP70AB OR HSP70A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82055575; PubMed=6795353; RA Karch F., Toeroek I., Tissieres A.; RT "Extensive regions of homology in front of the two hsp70 heat shock RT variant genes in Drosophila melanogaster."; RL J. Mol. Biol. 148:219-230(1981). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=122, 58H8, AUS, B28, FrV3-1, QD18, and Z(H)1; RA Bettencourt B.R.; RT "Rapid concerted evolution via gene conversion at the Drosophila heat RT shock protein Hsp70 genes."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., RA Gabor Miklos G.L., Abril J.F., Agbayani A., An H.J., RA Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., RA Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., RA Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., RA Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., RA Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., RA Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., RA Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., RA Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., RA Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., RA Gu Z., Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., RA Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., RA Wei M.H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., RA Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., RA Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., RA Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., RA Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., RA Pollard J., Puri V., Reese M.G., Reinert K., Remington K., RA Saunders R.D., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., RA Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., RA Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., RA Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., RA Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., RA Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP PRELIMINARY PARTIAL SEQUENCE FROM N.A. RX MEDLINE=81076551; PubMed=6255408; RA Toeroek I., Karch F.; RT "Nucleotide sequences of heat shock activated genes in Drosophila RT melanogaster. I. Sequences in the regions of the 5' and 3' ends of RT the hsp 70 gene in the hybrid plasmid 56H8."; RL Nucleic Acids Res. 8:3105-3123(1980). RN [5] RP SEQUENCE OF 1-100 FROM N.A. RX MEDLINE=82197526; PubMed=6804941; RA Ingolia T.D., Craig E.A.; RT "Drosophila gene related to the major heat shock-induced gene is RT transcribed at normal temperatures and not induced by heat shock."; RL Proc. Natl. Acad. Sci. U.S.A. 79:525-529(1982). CC -!- INDUCTION: HEAT SHOCK INDUCES THE SYNTHESIS OF SEVEN PROTEINS AT CC FIVE OTHERWISE INACTIVE SITES IN THE POLYTENE CHROMOSOMES OF FRUIT CC FLY LARVAE. TWO SEPARATE SITES, PRODUCING TWO AND THREE COPIES, CC RESPECTIVELY, CODE FOR THE 70 KDA PROTEIN. CC -!- MISCELLANEOUS: THERE ARE TWO COPIES OF THE GENE CODING FOR THIS CC PROTEIN AT CHROMOSOME LOCUS 87A7. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01103; AAA28640.1; -. DR EMBL; AF295939; AAG26893.1; -. DR EMBL; AF295940; AAG26894.1; -. DR EMBL; AF295941; AAG26895.1; -. DR EMBL; AF295942; AAG26896.1; -. DR EMBL; AF295943; AAG26897.1; -. DR EMBL; AF295944; AAG26898.1; -. DR EMBL; AF295945; AAG26899.1; -. DR EMBL; AE003693; -; NOT_ANNOTATED_CDS. DR EMBL; V00213; CAA23495.1; ALT_SEQ. DR EMBL; V00214; CAA23496.1; ALT_SEQ. DR PIR; A03308; A03308. DR HSSP; P08107; 1HJO. DR FlyBase; FBgn0013276; Hsp70Ab. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock; Multigene family; Polymorphism. FT VARIANT 190 190 E -> G (IN STRAIN B28). FT VARIANT 195 195 I -> N (IN STRAIN Z(H)1). FT VARIANT 263 263 R -> G (IN STRAIN 122). FT VARIANT 490 490 K -> R (IN STRAIN FRV3-1). FT VARIANT 568 568 D -> V (IN STRAINS 122, AUS, B28, FRV3-1, FT QD18 AND Z(H)1). FT VARIANT 574 574 D -> G (IN STRAIN 122). FT VARIANT 637 637 R -> P (IN STRAINS 122, 56H8, AUS, FRV3- FT 1, QD18 AND Z(H)1). FT CONFLICT 50 50 E -> D (IN REF. 2). FT CONFLICT 129 129 MISSING (IN REF. 2). FT CONFLICT 531 531 R -> H (IN REF. 2). FT CONFLICT 535 535 V -> I (IN REF. 2). FT CONFLICT 544 546 HVL -> YVF (IN REF. 2). SQ SEQUENCE 643 AA; 70265 MW; E9A2BF7F89905536 CRC64; MPAIGIDLGT TYSCVGVYQH GKVEIIANDQ GNRTTPSYVA FTDSERLIGE PAKNQVAMNP RNTVFDAKRL IGRKYDDPKI AEDMKHWPFK VVSDGGKPKI GVEYKGESKR FAPEEISSMV LTKMKETAAE AYLGESITDA VITVPAYFND SQRQATKDAG HIAGLNVLRI INEPTAAALA YGLDKNLKGE RNVLIFDLGG GTFDVSILTI DEGSLFEVRS TAGDTHLGGE DFDNRLVTHL ADEFKRKYKK DLRSNPRALR RLRTAAERAK RTLSSSTEAT IEIDALFEGQ DFYTKVSRAR FEELCADLFR NTLQPVEKAL NDAKMDKGQI HDIVLVGGST RIPKVQSLLQ DFFHGKNLNL SINPDEAVAY GAAVQAAILS GDQSGKIQDV LLVDVAPLSL GIETAGGVMT KLIERNCRIP CKQTKTFSTY ADNQPGVSIQ VYEGERAMTK DNNALGTFDL SGIPPAPRGV PQIEVTFDLD ANGILNVSAK EMSTGKAKNI TIKNDKGRLS QAEIDRMVNE AEKYADEDEK RRQRVTSRNA LESHVLNVKQ AVEQAPAGKL DEADKNSDLD KCNDTIRWLD SNTTAEKEEF DHKLEELTRH CSPIMTKMHQ QGAGAGAGGP GANCGQQAGG FGGYSGRTVE EVD // ID HS72_DROME STANDARD; PRT; 641 AA. AC P02824; DT 21-JUL-1986 (Rel. 01, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Major heat shock 70 kDa protein B (Heat shock protein 70B) (HSP70- DE 87C1). GN HSP70BA AND HSP70BB AND HSP70BC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (HSP70BB AND HSP70BC). RX MEDLINE=81064669; PubMed=6777045; RA Ingolia T.D., Craig E.A., McCarthy B.J.; RT "Sequence of three copies of the gene for the major Drosophila heat RT shock induced protein and their flanking regions."; RL Cell 21:669-679(1980). RN [2] RP SEQUENCE FROM N.A. (HSP70BA; HSP70BB AND HSP70BC). RC STRAIN=A28, AUS, B25, B28, FRV3-1, QD18, ZZ30, and Z(H)1; RA Bettencourt B.R.; RT "Rapid concerted evolution via gene conversion at the Drosophila heat RT shock protein Hsp70 genes."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (HSP70BA; HSP70BB AND HSP70BC). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- INDUCTION: HEAT SHOCK INDUCES THE SYNTHESIS OF SEVEN PROTEINS AT CC FIVE OTHERWISE INACTIVE SITES IN THE POLYTENE CHROMOSOMES OF FRUIT CC FLY LARVAE. TWO SEPARATE SITES, PRODUCING TWO AND THREE COPIES, CC RESPECTIVELY, CODE FOR THE 70 KDA PROTEIN. CC -!- MISCELLANEOUS: THERE ARE THREE COPIES OF THE GENE CODING FOR THIS CC PROTEIN AT CHROMOSOME LOCUS 87C1. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01104; AAD15226.1; -. DR EMBL; J01104; AAD15227.1; -. DR EMBL; AF295946; AAG26900.1; -. DR EMBL; AF295947; AAG26901.1; -. DR EMBL; AF295948; AAG26902.1; -. DR EMBL; AF295949; AAG26903.1; -. DR EMBL; AF295950; AAG26904.1; -. DR EMBL; AF295951; AAG26905.1; -. DR EMBL; AF295952; AAG26906.1; -. DR EMBL; AF295953; AAG26907.1; -. DR EMBL; AF295954; AAG26908.1; -. DR EMBL; AF295955; AAG26909.1; -. DR EMBL; AF295956; AAG26910.1; -. DR EMBL; AF295957; AAG26911.1; -. DR EMBL; AF295958; AAG26912.1; -. DR EMBL; AF295959; AAG26913.1; -. DR EMBL; AF295960; AAG26914.1; -. DR EMBL; AF295961; AAG26915.1; -. DR EMBL; AF295962; AAG26916.1; -. DR EMBL; AE003696; -; NOT_ANNOTATED_CDS. DR PIR; A03307; HHFF72. DR HSSP; P08107; 1HJO. DR FlyBase; FBgn0013277; Hsp70Ba. DR FlyBase; FBgn0013278; Hsp70Bb. DR FlyBase; FBgn0013279; Hsp70Bc. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock; Multigene family; Polymorphism. FT VARIANT 60 60 P -> S (IN HSP70BB; STRAIN FRV3-1). FT VARIANT 93 93 S -> I (IN HSP70BC; STRAIN FRV3-1). FT VARIANT 187 187 K -> N (IN HSP70BB; STRAIN QD18). FT VARIANT 195 195 F -> L (IN HSP70BA; STRAIN QD18 AND FT HSP70BB; STRAIN ZZ30). FT VARIANT 210 210 D -> Y (IN HSP70BC; STRAIN AUS). FT VARIANT 241 241 E -> D (IN HSP70BA; STRAIN Z(H)1 AND FT HSP70BB; STRAIN Z(H)1). FT VARIANT 350 350 E -> D (IN HSP70BA; STRAIN Z(H)1 AND FT HSP70BB; STRAIN Z(H)1). FT VARIANT 430 430 S -> A (IN HSP70BA; STRAIN Z(H)1 AND FT HSP70BB; STRAIN Z(H)1). FT VARIANT 475 475 T -> I (IN HSP70BC; STRAIN B28). FT VARIANT 516 516 M -> I (IN HSP70BA; STRAIN A28 AND FT HSP70BB; STRAIN B28). FT VARIANT 524 524 A -> V (IN HSP70BA; STRAIN A28 AND FT HSP70BB; STRAIN B28). FT VARIANT 545 545 F -> Y (IN HSP70BA; STRAIN AUS). FT VARIANT 555 555 P -> T (IN HSP70BA; STRAIN AUS). FT VARIANT 573 573 E -> D (IN HSP70BA; STRAIN A28). FT VARIANT 606 606 K -> T (IN HSP70BA; STRAIN QD18). FT VARIANT 634 634 G -> R (IN HSP70BC; STRAIN AUS). FT CONFLICT 26 28 IAN -> NAY (IN REF. 1). FT CONFLICT 48 50 IGD -> NGE (IN REF. 1). FT CONFLICT 306 306 D -> N (IN REF. 1). SQ SEQUENCE 641 AA; 70195 MW; F2C9C204F67EBB59 CRC64; MPAIGIDLGT TYSCVGVYQH GKVEIIANDQ GNRTTPSYVA FTDSERLIGD PAKNQVAMNP RNTVFDAKRL IGRKYDDPKI AEDMKHWPFK VVSDGGKPKI GVEYKGESKR FAPEEISSMV LTKMKETAEA YLGESITDAV ITVPAYFNDS QRQATKDAGH IAGLNVLRII NEPTAAALAY GLDKNLKGER NVLIFDLGGG TFDVSILTID EGSLFEVRST AGDTHLGGED FDNRLVTHLA EEFKRKYKKD LRSNPRALRR LRTAAERAKR TLSSSTEATI EIDALFEGQD FYTKVSRARF EELCADLFRN TLQPVEKALN DAKMDKGQIH DIVLVGGSTR IPKVQSLLQE FFHGKNLNLS INPDEAVAYG AAVQAAILSG DQSGKIQDVL LVDVAPLSLG IETAGGVMTK LIERNCRIPC KQTKTFSTYS DNQPGVSIQV YEGERAMTKD NNALGTFDLS GIPPAPRGVP QIEVTFDLDA NGILNVSAKE MSTGKAKNIT IKNDKGRLSQ AEIDRMVNEA EKYADEDEKH RQRITSRNAL ESYVFNVKQS VEQAPAGKLD EADKNSVLDK CNETIRWLDS NTTAEKEEFD HKMEELTRHC SPIMTKMHQQ GAGAAGGPGA NCGQQAGGFG GYSGPTVEEV D // ID HS7A_DROME STANDARD; PRT; 641 AA. AC P29843; Q9VUA7; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock 70 kDa protein cognate 1 (Heat shock 70 kDa protein 70C). GN HSC70-1 OR HSC1 OR CG8937. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93292982; PubMed=8514184; RA Rubin D.M., Mehta A., Zhu J., Shoham S., Chen X.J., Wells Q., RA Palter K.B.; RT "Genomic structure and sequence analysis of Drosophila melanogaster RT HSC70 genes."; RL Gene 128:155-163(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-68 FROM N.A. RX MEDLINE=82197526; PubMed=6804941; RA Ingolia T.D., Craig E.A.; RT "Drosophila gene related to the major heat shock-induced gene is RT transcribed at normal temperatures and not induced by heat shock."; RL Proc. Natl. Acad. Sci. U.S.A. 79:525-529(1982). CC -!- DEVELOPMENTAL STAGE: HEAT SHOCK COGNATE PROTEINS ARE EXPRESSED CC CONSTITUTIVELY DURING NORMAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L01501; AAA28625.1; -. DR EMBL; AE003536; AAF49782.1; -. DR EMBL; J01085; AAA28629.1; -. DR PIR; B03309; B03309. DR PIR; JN0668; JN0668. DR HSSP; P19120; 3HSC. DR FlyBase; FBgn0001216; Hsc70-1. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock; Multigene family. SQ SEQUENCE 641 AA; 70686 MW; DB86DB45E0C4BCA6 CRC64; MPKLPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTESERL IGDAAKNQVA MNPNNTIFDA KRLIGRRFDD ATVQSDMKHW PFEVFAENGK PRIRVEYKGE RKSFYPEEVS SMVLTKMRET AEAYLGGTVT DAVVTVPAYF NDSQRQATKD AGAIAGLNVL RIINEPTAAA IAYGLDKQGT SERNVLIFDL GGGTFDVSVL TIEDGIFEVK ATAGDTHLGG EDFDNRLVNH FVQEFQRKHK KDLGQNKRAL RRLRTACERA KRTLSSSTQA SIEIDSLFEG VDFYTSVTRA RFEELNGDLF RGTMEPVAKA LRDAKMDKGQ IHDIVLVGGS TRIPKVQRLL QDFFNGKELN KSINPDEAVA YGAAVQAAIL HGDKSEAVQD LLLLDVTPLS LGIETAGGVM TTLIKRNTTI PTKQTQIFTT YADNQPGVLI QVFEGERAMT RDNNSLGKFE LSAIPPAPRG VPQVEVTFDI DANGILNVTA LEKSTGKENR ITITNDKGRL SKEDIERMVN DAEAYRQADE QQRDRINAKN QLESYCFQLR STLDDEHLSS RFSPADRETI QQRSSETIAW LDANQLAERQ EFEHKQQELE RICSPIITRL YQGAGMAPPP TAGGSNPGAT GGSGPTIEEV D // ID HS7B_DROME STANDARD; PRT; 633 AA. AC P11146; Q9VFZ5; DT 01-JUL-1989 (Rel. 11, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock 70 kDa protein cognate 2 (Heat shock 70 kDa protein 87D). GN HSC2 OR HSC70-2 OR CG7756. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-68 FROM N.A. RX MEDLINE=84005511; PubMed=6311649; RA Craig E.A., Ingolia T.D., Manseau L.J.; RT "Expression of Drosophila heat-shock cognate genes during heat shock RT and development."; RL Dev. Biol. 99:418-426(1983). CC -!- DEVELOPMENTAL STAGE: HEAT SHOCK COGNATE PROTEINS ARE EXPRESSED CC CONSTITUTIVELY DURING NORMAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003698; AAF54899.1; -. DR EMBL; K01297; AAA28630.1; -. DR EMBL; K01296; AAA28630.1; JOINED. DR HSSP; P08107; 1HJO. DR FlyBase; FBgn0001217; Hsc70-2. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock; Multigene family. SQ SEQUENCE 633 AA; 69722 MW; 851D3FBEDB227F08 CRC64; MGKIPAIGID LGTTYSCVGV WQNSKVEIIA NDQGNRTTPS YVAFNETERL IGDPAKNQVA MNAKNTVFDA KRLIGRKFDD KKIQEDLKLW PFKVINEKGK PKIEVEFKGE RKRFAPEEIS SMVLTKMREI AEVYLGGKVK DAVVTVPAYF NDSQRQATKD AGSIAGLNVL RIINEPTAAA LAYGLDKNLK GERNVLIFDL GGGTFDVSVL SIDEGSLFEV KATAGDTHLG GEDFDNRLVN HFAEEFKRKH KSDIKGNARA LRRLRTACER AKRTLSSSTE ASLEIDALHE GIDFYSKISR ARFEELNMDL FRSTMQPVER ALSDAKMDKK AIHDVVLVGG STRIPKIQKL LQDLFGGKQL NLSINPDEAV AYGAAVQAAI LTGVGSSQIQ DLLLVDVAPL SLGIETAGGV MTNLVERNAR IPCKQQQIFT TYSDNQNAVT IQVYEGERAM TKDNNLLGTF NLTGIPPAPR GVPQIEVAFD LNADGILNVN AKDNSTGKSE KITISNDKGR LSKAEIDRML SEAEKYKVED DRQRERVQSK NNLEAYIYAC RQAVDDAPSG VLSETERSKV RDKCSSEASW LDKNSLAEKE EFESHLKECQ RICTPIMSKI HGGKKGKSSM GKGSHPTVEE VDG // ID HS7C_DROME STANDARD; PRT; 656 AA. AC P29844; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Heat shock 70 kDa protein cognate 3 precursor (78 kDa glucose DE regulated protein homolog) (GRP 78) (Heat shock protein cognate 72). GN HSC3 OR HSC70-3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93292982; PubMed=8514184; RA Rubin D.M., Mehta A., Zhu J., Shoham S., Chen X.J., Wells Q., RA Palter K.B.; RT "Genomic structure and sequence analysis of Drosophila melanogaster RT HSC70 genes."; RL Gene 128:155-163(1993). CC -!- FUNCTION: PROBABLY PLAYS A ROLE IN FACILITATING THE ASSEMBLY OF CC MULTIMERIC PROTEIN COMPLEXES INSIDE THE ER. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L01498; AAA28626.1; -. DR HSSP; P19120; 1HPM. DR FlyBase; FBgn0001218; Hsc70-3. DR InterPro; IPR000886; ER_target_S. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Endoplasmic reticulum; Signal. FT SIGNAL 1 18 FT CHAIN 19 656 HEAT SHOCK 70 kDa PROTEIN COGNATE 3. FT SITE 653 656 PREVENT SECRETION FROM ER. SQ SEQUENCE 656 AA; 72235 MW; B6653976EC34383F CRC64; MKLCILLAVV AFVGLSLGEE KKEKDKELGT VIGIDLGTTY SCVGVYKNGR VEIIANDQGN RITPSYVAFT ADGERLIGDA AKNQLTTNPE NTVFDAKRLI GREWSDTNVQ HDIKFFPFKV VEKNSKPHIS VDTSQGAKVF APEEISAMVL GKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGVI AGLQVMRIIN EPTAAAIAYG LDKKEGEKNV LVFDLGGGTF DVSLLTIDNG VFEVVATNGD THLGGEDFDQ RVMDHFIKLY KKKKGKDIRK DNRAVQKLRR EVEKAKRALS GSHQVRIEIE SFFEGDDFSE TLTRAKFEEL NLDLFRSTLK PVQKVLEDAD MNKKDVHEIV LVGGSTRIPK VQQLVKDFFG GKEPSRGINP DEAVAYGAAV QAGVLSGEQD TDAIVLLDVN PLTMGIETVG GVMTKLIPRN TVIPTKKSQV FSTASDNQHT VTIQVYEGER PMTKDNHLLG KFDLTGIPPA PRGIPQIEVS FEIDANAILT VSAEDKGTGN KEKIVITNDQ NRLTPEDIDR MIRDAEKFAD EDKKLKERVE SRNELESYAY SLKNQIGDKD KLGAKLSDDE KTKLESAIDE SIKWLEQNPD ADPEEYKKQK KDLEAIVQPV IAKLYQGAGG APPPEGGDDA DLKDEL // ID HS7D_DROME STANDARD; PRT; 651 AA. AC P11147; Q9VFB0; DT 01-JUL-1989 (Rel. 11, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock 70 kDa protein cognate 4 (Heat shock 70 kDa protein 88E). GN HSC70-4 OR HSC4 OR CG4264. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93292982; PubMed=8514184; RA Rubin D.M., Mehta A., Zhu J., Shoham S., Chen X., Wells Q., RA Palter K.B.; RT "Genomic structure and sequence analysis of Drosophila melanogaster RT HSC70 genes."; RL Gene 128:155-163(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90258915; PubMed=2111451; RA Perkins L.A., Doctor J.S., Zhang K., Stinson L., Perrimon N., RA Craig E.A.; RT "Molecular and developmental characterization of the heat shock RT cognate 4 gene of Drosophila melanogaster."; RL Mol. Cell. Biol. 10:3232-3238(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 1-104 FROM N.A. RX MEDLINE=84005511; PubMed=6311649; RA Craig E.A., Ingolia T.D., Manseau L.J.; RT "Expression of Drosophila heat-shock cognate genes during heat shock RT and development."; RL Dev. Biol. 99:418-426(1983). RN [5] RP SEQUENCE OF 580-592. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- SUBCELLULAR LOCATION: LOCALIZED TO A MESHWORK OF CYTOPLASMIC CC FIBERS AROUND THE NUCLEUS. TRANSLOCATES TO THE NUCLEUS AFTER CC THERMAL STRESS. CC -!- DEVELOPMENTAL STAGE: HEAT SHOCK COGNATE PROTEINS ARE EXPRESSED CC CONSTITUTIVELY DURING NORMAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L01500; AAB59186.1; -. DR EMBL; M36114; AAA28627.1; -. DR EMBL; J02569; AAA28631.1; ALT_SEQ. DR EMBL; AE003708; AAF55150.1; -. DR PIR; A36333; A36333. DR HSSP; P19120; 1ATR. DR FlyBase; FBgn0001219; Hsc70-4. DR GO; GO:0003773; F:heat shock protein activity; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; IGI. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock; Nuclear protein; Multigene family. FT CONFLICT 167 167 L -> P (IN REF. 2). FT CONFLICT 170 170 L -> P (IN REF. 2). FT CONFLICT 625 625 P -> G (IN REF. 2). SQ SEQUENCE 651 AA; 71131 MW; 30F6BD7E07407B63 CRC64; MSKAPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA MNPTQTIFDA KRLIGRKFDD AAVQSDMKHW PFEVVSADGK PKIEVTYKDE KKTFFPEEIS SMVLTKMKET AEAYLGKTVT NAVITVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKAV GERNVLIFDL GGGTFDVSIL SIDDGIFEVK STAGDTHLGG EDFDNRLVTH FVQEFKRKHK KDLTTNKRAL RRLRTACERA KRTLSSSTQA SIEIDSLFEG TDFYTSITRA RFEELNADLF RSTMDPVEKA LRDAKLDKSV IHDIVLVGGS TRIPKVQRLL QDLFNGKELN KSINPDEAVA YGAAVQAAIL HGDKSQEVQD LLLLDVTPLS LGIETAGGVM SVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA LERSTNKENK ITITNDKGRL SKEDIERMVN EAEKYRNEDE KQKETIAAKN GLESYCFNMK ATLDEDNLKT KISDSDRTTI LDKCNETIKW LDANQLADKE EYEHRQKELE GVCNPIITKL YQGAGFPPGG MPGGPGGMPG AAGAAGAAGA GGAGPTIEEV D // ID HS7E_DROME STANDARD; PRT; 687 AA. AC P29845; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Heat shock 70 kDa protein cognate 5. GN HSC5 OR HSC70-5. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93292982; PubMed=8514184; RA Rubin D.M., Mehta A., Zhu J., Shoham S., Chen X.J., Wells Q., RA Palter K.B.; RT "Genomic structure and sequence analysis of Drosophila melanogaster RT HSC70 genes."; RL Gene 128:155-163(1993). CC -!- DEVELOPMENTAL STAGE: HEAT SHOCK COGNATE PROTEINS ARE EXPRESSED CC CONSTITUTIVELY DURING NORMAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L01502; AAA28628.1; -. DR PIR; JN0667; JN0667. DR HSSP; P04475; 1DG4. DR FlyBase; FBgn0001220; Hsc70-5. DR GO; GO:0003773; F:heat shock protein activity; NAS. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock; Multigene family. SQ SEQUENCE 687 AA; 74208 MW; 43F6BCA1D2052EFB CRC64; MLRVPKFLPR LARQAGVVPS HMSGASSMFR NLPGASNGIS SQLRYKSGEV KGAVIGIDLG TTNSCLAVME GKQAKVIENA EGARTTPSHV AFTKDGERLV GMPAKRQAVT NSANTFYATK RLIGRRFDDP EVKKDITNLS YKVVKASNGD AWVSSTDGKV YSPSQIGAFI LMKMKETAEA YLNTPVKNAV VTVPAYFNDS QRQATKDAGQ IAGLNVLRVI NEPTAAALAY GMDKTEDKII AVYDLGGGTF DISILEIQKG VFEVKSTNGD TLLGGEDFDN HIVNFLVVEF KKDSGIDIRK DNIAMQRLKE AAEKAKCELS SSQQTDINLP YLTMDAAGPQ HMNLKLTRSK LESLVGDLIK RTIQPCQKAL SDAEVSKSEI GEVLLVGGMT RMPKVQSTVQ ELFGRQPSRS VNPDEAVAVG AAVQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTRLISR NTTIPTKKSQ VFSTASDGQT QVEIKVHQGE REMANDNKLL GSFTLVGIPP APRGVPQIEV VFDIDANGIV HVSAKDKGTG KEQQIVIQSS GGLSKDEIEN MIKKAEEYAT ADKQKRELIE IVNQGESIVH DTETKMEEFK SQLPAEECEK LKKEIADLRT LLANKETADL EEVRKATSSL QQSSLKLFEL AYKKMSAERE TNAGAGSSDS SSSSDTSASQ EGREELN // ID HS83_DROME STANDARD; PRT; 717 AA. AC P02828; P92174; P92202; Q9VZT3; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock protein 83 (HSP 82). GN HSP83 OR CG1242. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86281707; PubMed=2426456; RA Blackman R.K., Meselson M.; RT "Interspecific nucleotide sequence comparisons used to identify RT regulatory and structural features of the Drosophila hsp82 gene."; RL J. Mol. Biol. 188:499-515(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 1-375 FROM N.A. RX MEDLINE=84041500; PubMed=6314271; RA Hackett R.W., Lis J.T.; RT "Localization of the hsp83 transcript within a 3292 nucleotide RT sequence from the 63B heat shock locus of D. melanogaster."; RL Nucleic Acids Res. 11:7011-7030(1983). RN [5] RP SEQUENCE OF 1-371 FROM N.A. RC STRAIN=DPF-2, DPF-30, DPF-62, MA-10.2, DPF-82.1, 178.7, DPF-13, RC MA-4.4, EM-10, VC-805, MA-4.2, DPF-46, DPF-77, VC-815, and 709.6; RX MEDLINE=97132593; PubMed=8978045; RA Hasson E., Eanes W.F.; RT "Contrasting histories of three gene regions associated with RT In(3L)Payne of Drosophila melanogaster."; RL Genetics 144:1565-1575(1996). CC -!- FUNCTION: MOLECULAR CHAPERONE. HAS ATPASE ACTIVITY (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- INDUCTION: IN CONTRAST TO OTHER MAJOR HEAT SHOCK PROTEINS, THIS CC ONE IS ALSO EXPRESSED AT NORMAL GROWTH TEMPERATURES. IT IS ALSO CC DEVELOPMENTALLY EXPRESSED DURING OOGENESIS. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 90 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03810; CAA27435.1; -. DR EMBL; X00065; CAA24938.1; -. DR EMBL; AE003477; AAF47734.1; -. DR EMBL; AY122080; AAM52592.1; -. DR EMBL; U57459; AAB46677.1; -. DR EMBL; U57460; AAB46678.1; -. DR EMBL; U57461; AAB46679.1; -. DR EMBL; U57462; AAB46680.1; -. DR EMBL; U57463; AAB46681.1; -. DR EMBL; U57464; AAB46682.1; -. DR EMBL; U57465; AAB46683.1; -. DR EMBL; U57466; AAB46684.1; -. DR EMBL; U57467; AAB46685.1; -. DR EMBL; U57468; AAB46686.1; -. DR EMBL; U57469; AAB46687.1; -. DR EMBL; U57470; AAB46688.1; -. DR EMBL; U57471; AAB46689.1; -. DR EMBL; U57472; AAB46690.1; -. DR EMBL; U57473; AAB46691.1; -. DR PIR; A24827; HHFF83. DR HSSP; P07900; 1YER. DR FlyBase; FBgn0001233; Hsp83. DR GO; GO:0005813; C:centrosome; ISS. DR GO; GO:0003763; F:chaperonin ATPase activity; ISS. DR GO; GO:0003773; F:heat shock protein activity; ISS. DR GO; GO:0007098; P:centrosome cycle; IMP. DR GO; GO:0045187; P:regulation of sleep; IMP. DR GO; GO:0009408; P:response to heat; ISS. DR InterPro; IPR003594; ATPbind_ATPase. DR InterPro; IPR001404; Hsp90. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00183; HSP90; 1. DR PRINTS; PR00775; HEATSHOCK90. DR SMART; SM00387; HATPase_c; 1. DR PROSITE; PS00298; HSP90; 1. KW Chaperone; ATP-binding; Heat shock. FT VARIANT 234 234 MISSING (IN STRAINS MA-10.2, DPF-13, DPF- FT 82.1, EM-10, 178.7, 709.6 AND MA-4.4). FT VARIANT 368 368 N -> K (IN STRAINS DPF-2, DPF-30, DPF-62, FT MA-10.2, DPF-82.1, 178.7, DPF-13, MA-4.4, FT EM-10, VC-805, MA-4.2, DPF-46, DPF-77, FT VC-815 AND 709.6). SQ SEQUENCE 717 AA; 81865 MW; A71B96B2FE1684E6 CRC64; MPEEAETFAF QAEIAQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYE SLTDPSKLDS GKELYIKLIP NKTAGTLTII DTGIGMTKSD LVNNLGTIAK SGTKAFMEAL QAGADISMIG QFGVGFYSAY LVADKVTVTS KNNDDEQYVW ESSAGGSFTV RADNSEPLGR GTKIVLYIKE DQTDYLEESK IKEIVNKHSQ FIGYPIKLLV EKEREKEVSD DEADDEKKEG DEKKEMETDE PKIEDVGEDE DADKKDKDAK KKKTIKEKYT EDEELNKTKP IWTRNPDDIS QEEYGEFYKS LTNDWEDHLA VKHFSVEGQL EFRALLFIPR RTPFDLFENQ KKRNNIKLYV RRVFIMDNCE DLIPEYLNFM KGVVDSEDLP LNISREMLQQ NKVLKVIRKN LVKKTMELIE ELTEDKENYK KFYDQFSKNL KLGVHEDSNN RAKLADFLRF HTSASGDDFC SLADYVSRMK DNQKHVYFIT GESKDQVSNS AFVERVKARG FEVVYMTEPI DEYVIQHLKE YKGKQLVSVT KEGLELPEDE SEKKKREEDK AKFESLCKLM KSILDNKVEK VVVSNRLVDS PCCIVTSQFG WSANMERIMK AQALRDTATM GYMAGKKQLE INPDHPIVET LRQKADADKN DKAVKDLVIL LFETSLLSSG FSLDSPQVHA SRIYRMIKLG LGIDEDEPMT TDDAQSAGDA PSLVEDTEDA SHMEEVD // ID HSF_DROME STANDARD; PRT; 691 AA. AC P22813; Q9V8C1; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heat shock factor protein (HSF) (Heat shock transcription factor) DE (HSTF). GN HSF OR CG5748. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=91077922; PubMed=2257625; RA Clos J., Westwood J.T., Becker P.B., Wilson S., Lambert K., Wu C.; RT "Molecular cloning and expression of a hexameric Drosophila heat RT shock factor subject to negative regulation."; RL Cell 63:1085-1097(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP STRUCTURE BY NMR OF 43-150. RX MEDLINE=95360744; PubMed=7634100; RA Vuister G.W., Kim S.-J., Orosz A., Marquardt J., Wu C., Bax A.; RT "Solution structure of the DNA-binding domain of Drosophila heat RT shock transcription factor."; RL Nat. Struct. Biol. 1:605-613(1994). CC -!- FUNCTION: DNA-BINDING PROTEIN THAT SPECIFICALLY BINDS HEAT SHOCK CC PROMOTER ELEMENTS (HSE) AND ACTIVATES TRANSCRIPTION. IN HIGHER CC EUKARYOTES, HSF IS UNABLE TO BIND TO THE HSE UNLESS THE CELLS ARE CC HEAT SHOCKED. CC -!- SUBUNIT: HOMOTRIMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: EXHIBITS TEMPERATURE-DEPENDENT PHOSPHORYLATION (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE HSF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60070; AAA28642.1; -. DR EMBL; AE003800; AAF57749.1; -. DR PIR; A36295; A36295. DR PDB; 1HKS; 30-SEP-94. DR PDB; 1HKT; 30-SEP-94. DR TRANSFAC; T00386; -. DR FlyBase; FBgn0001222; Hsf. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0005700; C:polytene chromosome; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0003704; F:specific RNA polymerase II transcription fa...; IDA. DR GO; GO:0009408; P:response to heat; IDA. DR InterPro; IPR000232; HSF_DNA_bind. DR InterPro; IPR002341; HSF_ETS. DR Pfam; PF00447; HSF_DNA-bind; 1. DR PRINTS; PR00056; HSFDOMAIN. DR ProDom; PD001788; HSF_DNA_bind; 1. DR SMART; SM00415; HSF; 1. DR PROSITE; PS00434; HSF_DOMAIN; 1. KW Transcription regulation; Nuclear protein; DNA-binding; Activator; KW Phosphorylation; Heat shock; 3D-structure. FT DNA_BIND 46 150 FT DOMAIN 16 26 POLY-GLU. FT HELIX 48 56 FT TURN 59 60 FT STRAND 63 63 FT TURN 64 65 FT STRAND 66 69 FT TURN 70 73 FT STRAND 74 76 FT TURN 82 87 FT TURN 89 92 FT HELIX 98 107 FT TURN 108 108 FT STRAND 110 110 FT STRAND 128 130 FT TURN 132 133 FT TURN 139 140 FT TURN 143 144 SQ SEQUENCE 691 AA; 76933 MW; E013428B22C98D35 CRC64; MSRSRSSAKA VQFKHESEEE EEDEEEQLPS RRMHSYGDAA AIGSGVPAFL AKLWRLVDDA DTNRLICWTK DGQSFVIQNQ AQFAKELLPL NYKHNNMASF IRQLNMYGFH KITSIDNGGL RFDRDEIEFS HPFFKRNSPF LLDQIKRKIS NNKNGDDKGV LKPEAMSKIL TDVKVMRGRQ DNLDSRFSAM KQENEVLWRE IASLRQKHAK QQQIVNKLIQ FLITIVQPSR NMSGVKRHVQ LMINNTPEID RARTTSETES ESGGGPVIHE LREELLDEVM NPSPAGYTAA SHYDQESVSP PAVERPRSNM SISSHNVDYS NQSVEDLLLQ GNGTAGGNIL VGGAASPMAQ SVSQSPAQHD VYTVTEAPDS HVQEVPNSPP YYEEQNVLTT PMVREQEQQK RQQLKENNKL RRQAGDVILD AGDILVDSSS PKAQRTSIQH STQPDVMVQP MIIKSEPENS SGLMDLMTPA NDLYSVNFIS EDMPTDIFED ALLPDGVEEA AKLDQQQKFG QSTVSSGKFA SNFDVPTNST LLDANQASTS KAAAKAQASE EEGMAVAKYS GAENGNNRDT NNSQLLRMAS VDELHGHLES MQDELETLKD LLRGDGVAID QNMLMGLFND SDLMDNYGLS FPNDSISSEK KAPSGSELIS YQPMYDLSDI LDTDDGNNDQ EASRRQMQTQ SSVLNTPRHE L // ID HTS_DROME STANDARD; PRT; 1156 AA. AC Q02645; Q9V8U4; Q9V8U5; DT 01-JUL-1993 (Rel. 26, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Hu-li tai shao protein. GN HTS OR CG9325. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC TISSUE=Egg; RX MEDLINE=94040709; PubMed=1340461; RA Yue L., Spradling A.C.; RT "hu-li tai shao, a gene required for ring canal formation during RT Drosophila oogenesis, encodes a homolog of adducin."; RL Genes Dev. 6:2443-2454(1992). RN [2] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC TISSUE=Embryo; RX MEDLINE=93211992; PubMed=7681599; RA Ding D., Parkhurst S.M., Lipshitz H.D.; RT "Different genetic requirements for anterior RNA localization RT revealed by the distribution of Adducin-like transcripts during RT Drosophila oogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 90:2512-2516(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: REQUIRED FOR ASSEMBLING ACTIN AT RING CANALS IN CC DEVELOPING EGG CHAMBERS. PROBABLY INTERACTS WITH OTHER CC DEVELOPMENTAL PROTEINS INVOLVED IN NURSE CELL/OOCYTE TRANSPORT CC THROUGH THE RING CANALS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q02645-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q02645-2; Sequence=VSP_000191, VSP_000192; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: OOGENESIS AND EARLY EMBRYOGENESIS. CC -!- MISCELLANEOUS: 'HU-LI TAI SHAO' MEANS 'TOO LITTLE NURSING' IN CC CHINESE. CC -!- SIMILARITY: BELONGS TO THE ALDOLASE CLASS II FAMILY. ADDUCIN CC SUBFAMILY. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L05016; AAA28643.1; -. DR EMBL; AF151708; AAB59182.1; -. DR EMBL; AE003796; AAF57565.3; ALT_SEQ. DR EMBL; AE003796; AAF57566.2; ALT_SEQ. DR PIR; A47397; A47397. DR FlyBase; FBgn0004873; hts. DR GO; GO:0045169; C:fusome; IDA. DR GO; GO:0045170; C:spectrosome; IDA. DR GO; GO:0008302; P:ring canal formation, actin assembly; IMP. DR InterPro; IPR001303; Aldolase_II_N. DR Pfam; PF00596; Aldolase_II; 1. KW Cytoskeleton; Membrane; Developmental protein; Alternative splicing. FT VARSPLIC 659 718 ALVSQLAQKYAFLYSPGQYMYACMKMAPLMHKVYVIHKVEP FT VSKHNYPPVNDGNMSIHHN -> GENVQNGDHSEAHLSTFS FT QSSKEFQDVSTDGSPKKDKKKKKGLRTPSFLKKKKEKKKAE FT A (in isoform Short). FT /FTId=VSP_000191. FT VARSPLIC 719 1156 Missing (in isoform Short). FT /FTId=VSP_000192. FT CONFLICT 351 351 A -> V (IN REF. 1). FT CONFLICT 680 682 ACM -> GCL (IN REF. 1). FT CONFLICT 689 689 H -> Q (IN REF. 1 AND 2). FT CONFLICT 725 727 MAQ -> LAH (IN REF. 1). FT CONFLICT 746 746 L -> F (IN REF. 1). FT CONFLICT 912 912 N -> D (IN REF. 1). FT CONFLICT 1089 1089 G -> C (IN REF. 2). SQ SEQUENCE 1156 AA; 127938 MW; 5AA90E8938A84A0A CRC64; MTEVEQPPQN GIDPTAGEDD DNSKARPADI EQDMREMERR KRVEAIMGSK LFREELERIV DSARDGGAGA SGILQQLSDI VGVPVSRVGS VFKSSNCMVP INDIRGVESM GYAKGEKILR CKLAATFRLL DLYGWTQGLG AQITARLKVD QEYFLVNPYG LLYHEITASA LNKVDMQGQI VEQGTTNFGG NKSHFVLHSV VHAARPDIRC AIYIGCSPVV AISSLKTGLL PLTKDACVLG EITTHAYTGL FDEEERNRLV RSLGPNSKVI LLTNHGALCC GETIEEAFFA ACHIVQACET QLKLLPVGLD NLVLIPEESR KAIYEQSRRP PEDLEKKFAA VAAAEDGAAT AEKDAAEAVP KVGSPPKWRV GGAEFEALMR MLDNAGYRTG YIYRHPLIKS DPPKPKNDVE LPPAVSSLGY LLEEEELFRQ GIWKKGDIRK GGDRSRWLNS PNVYQKVEVL ETGTPDPKKI TKWVAEGSPT HSTPVRIEDP LQFVPAGTNP REFKRVQQLI KDNRRADKIS AGPQSHILEG VTWDEASRLK DATVSQAGDH VVMMGAASKG IIQRGFQHNA TVYKAPYAKN PFDNVTDDEL NEYKRTVERK KKSVHGEYTD TDFSESEAVL QAGTKKYPQS EPETEHQVIE IQTQQAPVPR QAEVVLSDAL VSQLAQKYAF LYSPGQYMYA CMKMAPLMHK VYVIHKVEPV SKHNYPPVND GNMSIHHNES GAGFMAQESS VISSTPVRNA LASVSLPEER NHSILGLSST PYRTISHFGF NCPLITSPTI LLHPEHRSIW QRVAEQREKV VSFIDLTTLS LDNRKLLNVV TSTHPTQCQS QSQSFISEKH IQLEVTPPKR KQRVYSATIS SGLDDSLDEL DSLMSGLAIN MPRSREQDSG LYRSYTFLPS NHALPKDTDA NNRDQTDRER PEAEQEESFH CAGDSGIGDS TGRRPRLATT SNDSSIQEAE AYTQGKHVKL TLSSSPTPTA TQSPATIEIL INVSLRNAEC VQTVQTHEQE FRAKLERVID EEIHYISQQL AFKQRQAELH EQQTTSRAPI ATPSFTTMHP PAPASSSSMV HRSNSAPELC HTYSYVAVGD LSTKQDQASP QLPAEGEPLN DILSSLEKEL ERLLNSVVTA HMLHNKAIIH ECRARFSQLA DGIVSS // ID HUGN_DROME STANDARD; PRT; 191 AA. AC Q9VG55; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Hugin protein precursor [Contains: Hug-gamma; Hug-peptide; PK-2 (Drm- DE PK-2) (Pyrokinin-2) (Myotrophin-2) (MT-2)]. GN HUG OR CG6371. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF N-TERMINUS; 140-147 AND 174-180. RX MEDLINE=22194680; PubMed=12204246; RA Meng X., Wahlstreom G., Immonen T., Kolmer M., Tirronen M., Predel R., RA Kalkkinen N., Heino T., Sariola H., Roos C.; RT "The Drosophila hugin gene codes for myostimulatory and ecdysis- RT modifying neuropeptides."; RL Mech. Dev. 117:5-5(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 174-181, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- FUNCTION: PROBABLY HAS A ROLE IN LARVAL MOLTING. CC -!- TISSUE SPECIFICITY: SUBGROUP OF NEUROSECRETORY CELLS IN THE CC SUBOESOPHAGEAL GANGLION FROM EMBRYONIC STAGE 9 TO LARVAL STAGES. CC -!- DEVELOPMENTAL STAGE: DURING EMBRYOGENESIS THROUGH TO ADULT STAGES CC WITH HIGHEST EXPRESSION AT LATER HALF OF EMBRYOGENESIS AND DURING CC LARVAL STAGES. CC -!- SIMILARITY: BELONGS TO THE PYROKININ FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ133105; CAB88005.1; -. DR EMBL; AE003696; AAF54833.1; -. DR EMBL; AY047528; AAK77260.1; -. DR FlyBase; FBgn0028374; hug. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0005184; F:neuropeptide hormone activity; NAS. DR GO; GO:0018990; P:ecdysis (sensu Insecta); IMP. DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS. DR InterPro; IPR001484; Pyrokinin. DR PROSITE; PS00539; PYROKININ; FALSE_NEG. KW Signal; Neuropeptide; Amidation; Pyrokinin; KW Cleavage on pair of basic residues. FT SIGNAL 1 24 FT PROPEP 25 119 FT PEPTIDE 121 137 HUG-GAMMA (POTENTIAL). FT PEPTIDE 140 ? HUG-PEPTIDE (POTENTIAL). FT PROPEP ? 171 FT PEPTIDE 174 181 PK-2. FT PROPEP 185 191 FT MOD_RES 137 137 AMIDATION (G-138 PROVIDE AMIDE GROUP) FT (POTENTIAL). FT MOD_RES 181 181 AMIDATION (G-182 PROVIDE AMIDE GROUP). SQ SEQUENCE 191 AA; 20622 MW; 78F4A9811C57D932 CRC64; MCGPSYCTLL LIAASCYILV CSHAKSLQGT SKLDLGNHIS AGSARGSLSP ASPALSEARQ KRAMGDYKEL TDIIDELEEN SLAQKASATM QVAAMPPQGQ EFDLDTMPPL TYYLLLQKLR QLQSNGEPAY RVRTPRLGRS IDSWRLLDAE GATGMAGGEE AIGGQFMQRM VKKSVPFKPR LGKRAQVCGG D // ID HUNB_DROME STANDARD; PRT; 758 AA. AC P05084; Q24018; DT 01-APR-1988 (Rel. 07, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Hunchback protein. GN HB OR CG9786. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RA Tautz D., Lehmann R., Schnuerch H., Schuh R., Seifert E., RA Kienlin A., Jones K., Jaeckle H.; RT "Finger protein of novel structure encoded by hunchback, a second RT member of the gap class of Drosophila segmentation genes."; RL Nature 327:383-389(1987). RN [2] RP REVISION TO 525. RA Tautz D.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=94259232; PubMed=8200478; RA Margolis J.S., Borowsky M., Shim C.W., Posakony J.W.; RT "A small region surrounding the distal promoter of the hunchback gene RT directs maternal expression."; RL Dev. Biol. 163:381-388(1994). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 281-349 FROM N.A. RX MEDLINE=93066327; PubMed=1438276; RA Sommer R.J., Retzlaff M., Goerlich K., Sander K., Tautz D.; RT "Evolutionary conservation pattern of zinc-finger domains of RT Drosophila segmentation genes."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10782-10786(1992). RN [6] RP POLYMORPHISM. RA Tautz D., Nigro L.; RT "Microevolutionary divergence pattern of the segmentation gene RT hunchback in Drosophila."; RL Mol. Biol. Evol. 15:1403-1411(1998). CC -!- FUNCTION: GAP CLASS SEGMENTATION PROTEIN THAT CONTROLS DEVELOPMENT CC OF HEAD STRUCTURES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: IN EMBRYO, EXPRESSION OF MATERNAL TRANSCRIPT CC IS HIGHEST IN ANTERIOR REGION. ZYGOTIC TRANSCRIPT IS EXPRESSED IN CC ANTERIOR REGION UNTIL THE BEGINNING OF GASTRULATION AND IN CC POSTERIOR REGION UNTIL EARLY GASTRULATION. AFTER THIS, IT IS CC EXPRESSED IN DEVELOPING NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MATERNALLY AND ZYGOTICALLY. CC EXPRESSION OF THE MATERNAL TRANSCRIPT DECREASES UNTIL EMBRYONIC CC STAGE 14, ZYGOTIC TRANSCRIPT IS FIRST DETECTED AT STAGE 11. CC -!- SIMILARITY: BELONGS TO THE HUNCHBACK FAMILY OF C2H2-TYPE ZINC- CC FINGER PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00274; CAA68377.1; -. DR EMBL; U17742; AAB60232.1; -. DR EMBL; AE003680; AAF54270.1; -. DR PIR; A93395; A29253. DR TRANSFAC; T00395; -. DR FlyBase; FBgn0001180; hb. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0016563; F:transcriptional activator activity; IDA. DR GO; GO:0007355; P:anterior region determination; NAS. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; NAS. DR GO; GO:0007400; P:neuroblast cell fate determination; IMP. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 6. DR SMART; SM00355; ZnF_C2H2; 6. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. KW Developmental protein; Gap protein; Zinc-finger; KW Metal-binding; DNA-binding; Repeat; Nuclear protein; Polymorphism. FT DOMAIN 61 69 POLY-GLN. FT DOMAIN 102 108 POLY-GLN. FT DOMAIN 117 122 POLY-HIS. FT ZN_FING 240 262 C2H2-TYPE. FT ZN_FING 269 291 C2H2-TYPE. FT ZN_FING 297 319 C2H2-TYPE. FT ZN_FING 325 349 C2H2-TYPE. FT DOMAIN 404 409 POLY-GLN. FT DOMAIN 555 561 POLY-GLN. FT ZN_FING 705 727 C2H2-TYPE. FT ZN_FING 733 757 C2H2-TYPE. FT VARIANT 437 437 A -> P. FT VARIANT 649 649 V -> M. SQ SEQUENCE 758 AA; 83113 MW; AD74802EB856ACD7 CRC64; MQNWETTATT NYEQHNAWYN SMFAANIKQE PGHHLDGNSV ASSPRQSPIP STNHLEQFLK QQQQQLQQQP MDTLCAMTPS PSQNDQNSLQ HYDANLQQQL LQQQQYQQHF QAAQQQHHHH HHLMGGFNPL TPPGLPNPMQ HFYGGNLRPS PQPTPTSAST IAPVAVATGS SEKLQALTPP MDVTPPKSPA KSSQSNIEPE KEHDQMSNSS EDMKYMAESE DDDTNIRMPI YNSHGKMKNY KCKTCGVVAI TKVDFWAHTR THMKPDKILQ CPKCPFVTEF KHHLEYHIRK HKNQKPFQCD KCSYTCVNKS MLNSHRKSHS SVYQYRCADC DYATKYCHSF KLHLRKYGHK PGMVLDEDGT PNPSLVIDVY GTRRGPKSKN GGPIASGGSG SGSRKSNVAA VAPQQQQSQP AQPVATSQLS AALQGFPLVQ GNSAPPAASP VLPLPASPAK SVASVEQTPS LPSPANLLPP LASLLQQNRN MAFFPYWNLN LQMLAAQQQA AVLAQLSPRM REQLQQQNQQ QSDNEEEEQD DEYERKSVDS AMDLSQGTPV KEDEQQQQPQ QPLAMNLKVE EEATPLMSSS NASRRKGRVL KLDTLLQLRS EAMTSPEQLK VPSTPMPTAS SPIAGRKPMP EEHCSGTSSA DESMETAHVP QANTSASSTA SSSGNSSNAS SNSNGNSSSN SSSNGTTSAV AAPPSGTPAA AGAIYECKYC DIFFKDAVLY TIHMGYHSCD DVFKCNMCGE KCDGPVGLFV HMARNAHS // ID HXK1_DROME STANDARD; PRT; 465 AA. AC Q9NFT9; Q9VBF1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Hexokinase type 1 (EC 2.7.1.1). GN HEX-T1 OR HEX OR CG33102/CG5443. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND VARIANTS HIS-33 AND PHE-243. RC STRAIN=DPF96e3_3.0, DPF96e3_4.2, DPF96e3_23.1, DPF96e3_74.2, RC DPF96e3_84.3, VT97e3_1, VT97e3_39, VT97e3_41, SC96e3_12.3, RC SC96e3_19.4, HFL97e3_8, HFL97e3_12, HFL97e3_13, HFL97e3_15, RC HFL97e3_16, ZIM(S)e3_24, ZIM(S)e3_35, ZIM(H)e3_38.4, and RC ZIM(H)e3_39; RA Duvernell D.D., Eanes W.F.; RT "Contrasting molecular population genetics of four hexokinases in RT Drosophila melanogaster and Drosophila simulans."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-K; RA Deobagkar D.D., Kulkarni G.V., Deobagkar D.N.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- CATALYTIC ACTIVITY: ATP + D-HEXOSE = ADP + D-HEXOSE 6-PHOSPHATE. CC -!- PATHWAY: FIRST STEP OF SEVERAL METABOLIC PATHWAYS. CC -!- SIMILARITY: BELONGS TO THE HEXOKINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF257590; AAG22891.1; -. DR EMBL; AF257591; AAG22893.1; -. DR EMBL; AF257592; AAG22895.1; -. DR EMBL; AF257593; AAG22897.1; -. DR EMBL; AF257594; AAG22899.1; -. DR EMBL; AF257595; AAG22901.1; -. DR EMBL; AF257596; AAG22903.1; -. DR EMBL; AF257597; AAG22905.1; -. DR EMBL; AF257598; AAG22907.1; -. DR EMBL; AF257599; AAG22909.1; -. DR EMBL; AF257600; AAG22911.1; -. DR EMBL; AF257601; AAG22913.1; -. DR EMBL; AF257602; AAG22915.1; -. DR EMBL; AF257603; AAG22917.1; -. DR EMBL; AF257604; AAG22919.1; -. DR EMBL; AF257605; AAG22921.1; -. DR EMBL; AF257606; AAG22923.1; -. DR EMBL; AF257607; AAG22925.1; -. DR EMBL; AF257608; AAG22927.1; -. DR EMBL; AJ271350; CAB72131.1; -. DR EMBL; AE003756; AAF56591.2; -. DR HSSP; Q26609; 1BDG. DR FlyBase; FBgn0042711; Hex-t1. DR InterPro; IPR001312; Hexokinase. DR Pfam; PF03727; hexokinase2; 1. DR Pfam; PF00349; hexokinase; 1. DR PRINTS; PR00475; HEXOKINASE. DR ProDom; PD001109; Hexokinase; 1. KW Transferase; Kinase; Glycolysis; ATP-binding; KW Multigene family; Polymorphism. FT BINDING 88 88 ATP (BY SIMILARITY). FT DOMAIN 139 165 GLUCOSE-BINDING (POTENTIAL). FT VARIANT 33 33 N -> H (IN STRAINS HFL97E3_12 AND FT ZIM(S)E3_24). FT VARIANT 243 243 Y -> F (IN STRAINS DPF96E3_3.0, FT DPF96E3_4.2, DPF96E3_23.1, DPF96E3_74.2, FT VT97E3_41, SC96E3_12.3, HFL97E3_8, FT HFL97E3_12, HFL97E3_15, ZIM(S)E3_24, FT ZIM(S)E3_35). SQ SEQUENCE 465 AA; 52260 MW; 67B611920D56B6DD CRC64; MANTFNPEED FPEVYKVCKL FNPSIDDLEK IKNAMDREIT MGLSRDHHDR STVPCHLSYV QDLPTGRERG QFLALEMMPT NCRIMLVKFS SERDIYTSSK CVIMPHTVAA GRGTEVFTFL ATSIANFVKE KKVDKDNLPL GIAFAFTLKK LALDVGILVS WTKEFGAQGA IGKDVVQLLR DALAKFPEIS VDVMGIINVG AGSLLALCWA QPDTRIGLIM GSIANSCYVE RVERCETYEG DEYRKLMIIN SDWAHFGDTG QLDFIRNEYD RQLDTESINP GTRIYEKFSG ALCMGELVRI IVLRLMKSGA IFAEDRRDYI GIQWKLDMVS LIEIVSDPPG VYTKAQEVMD KFRIRHCKER DLAALKYICD TVTNRAAMLV ASGVSCLIDR MRLPQISIAV DGGIYRLHPT FSTVLNKYTR LLADPNYNFE FVITQDSCGV GAAIMAGMAH ANKYKTDAKL FTMDY // ID HXK2_DROME STANDARD; PRT; 453 AA. AC Q9NFT7; Q95U08; Q9NFT8; Q9VBF1; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Hexokinase type 2 (EC 2.7.1.1). GN HEX-T2 OR HEX OR CG32849/CG5443. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND VARIANTS ASN-161; THR-219; ASN-347; ASN-451 RP AND ILE-453. RC STRAIN=DPF96e3_3.0, DPF96e3_4.2, DPF96e3_23.1, DPF96e3_74.2, RC DPF96e3_84.3, VT97e3_1, VT97e3_39, VT97e3_41, SC96e3_12.3, RC SC96e3_19.4, HFL97e3_8, HFL97e3_12, HFL97e3_13, HFL97e3_15, RC HFL97e3_16, ZIM(S)e3_24, ZIM(S)e3_35, ZIM(H)e3_38.4, and RC ZIM(H)e3_39; RA Duvernell D.D., Eanes W.F.; RT "Contrasting molecular population genetics of four hexokinases in RT Drosophila melanogaster and Drosophila simulans."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-K; RA Deobagkar D.D., Kulkarni G.V., Deobagkar D.N.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: ATP + D-HEXOSE = ADP + D-HEXOSE 6-PHOSPHATE. CC -!- PATHWAY: FIRST STEP OF SEVERAL METABOLIC PATHWAYS. CC -!- SIMILARITY: BELONGS TO THE HEXOKINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF257590; AAG22892.1; -. DR EMBL; AF257591; AAG22894.1; -. DR EMBL; AF257592; AAG22896.1; -. DR EMBL; AF257593; AAG22898.1; -. DR EMBL; AF257594; AAG22900.1; -. DR EMBL; AF257595; AAG22902.1; -. DR EMBL; AF257596; AAG22904.1; -. DR EMBL; AF257597; AAG22906.1; -. DR EMBL; AF257598; AAG22908.1; -. DR EMBL; AF257599; AAG22910.1; -. DR EMBL; AF257600; AAG22912.1; -. DR EMBL; AF257601; AAG22914.1; -. DR EMBL; AF257602; AAG22916.1; -. DR EMBL; AF257603; AAG22918.1; -. DR EMBL; AF257604; AAG22920.1; -. DR EMBL; AF257605; AAG22922.1; -. DR EMBL; AF257606; AAG22924.1; -. DR EMBL; AF257607; AAG22926.1; -. DR EMBL; AF257608; AAG22928.1; -. DR EMBL; AJ271350; CAB67701.1; ALT_INIT. DR EMBL; AJ271350; CAB72132.1; -. DR EMBL; AE003756; AAN14073.1; -. DR EMBL; AY058394; AAL13623.1; -. DR HSSP; P05708; 1BG3. DR FlyBase; FBgn0042710; Hex-t2. DR GO; GO:0004396; F:hexokinase activity; NAS. DR GO; GO:0006096; P:glycolysis; NAS. DR InterPro; IPR001312; Hexokinase. DR Pfam; PF03727; hexokinase2; 1. DR Pfam; PF00349; hexokinase; 1. DR PRINTS; PR00475; HEXOKINASE. DR ProDom; PD001109; Hexokinase; 1. DR PROSITE; PS00378; HEXOKINASES; 1. KW Transferase; Kinase; Glycolysis; ATP-binding; KW Multigene family; Polymorphism. FT BINDING 95 95 ATP. FT DOMAIN 134 160 GLUCOSE-BINDING (POTENTIAL). FT VARIANT 161 161 S -> N (IN STRAIN HFL97E3_15). FT VARIANT 219 219 S -> T (IN STRAIN ZIM(S)E3_24). FT VARIANT 347 347 S -> N (IN STRAINS SC96E3_12.3 AND FT ZIM(S)E3_35). FT VARIANT 451 451 S -> N (IN STRAINS DPF96E3_23.1, FT SC96E3_12.3, HFL97E3_8, HFL97E3_12, FT HFL97E3_16, ZIM(S)E3_24 AND ZIM(S)E3_35). FT VARIANT 453 453 L -> I (IN STRAINS DPF96E3_23.1, FT SC96E3_12.3, HFL97E3_8, HFL97E3_12, FT HFL97E3_16 AND ZIM(S)E3_24). FT CONFLICT 134 134 P -> A (IN REF. 1). SQ SEQUENCE 453 AA; 49739 MW; DF20800D5C862DD9 CRC64; MPSLVNTEIE AAVKGFLIDQ EKMTEVVERM TKEIKMGLAK DTHARAVIKC FVSHVQDLPT GKERGKYLAL DLGGSNFRVL LVNLISNSDV ETMSKGYNFP QTLMSGSGKA LFDFLAECLS EFCHSHGLEN ESLPLGFTFS FPLQQQGLSK GILVAWTKGF SCEGVVGKNV VSLLQEAIDR RGDLKINTVA ILNDTVGTLM SCAFYHPNCR IGLIVGTGSN ACYVEKTVNA ECFEGYQTSP KPSMIINCEW GAFGDNGVLE FVRTSYDKAV DKVTPNPGKQ TFEKCISGMY MGELVRLVIT DMIAKGFMFH GIISEKIQER WSFKTAYISD VESDAPGEYR NCNKVLSELG ILGCQEPDKE ALRYICEAVS SRSAKLCACG LVTIINKMNI NEVAIGIDGS VYRFHPKYHD MLQYHMKKLL KPGVKFELVV SEDGSGRGAA LVAATAVQAK SKL // ID HYD_DROME STANDARD; PRT; 2895 AA. AC P51592; DT 01-OCT-1996 (Rel. 34, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin--protein ligase hyd (EC 6.3.2.-) (Hyperplastic discs DE protein). GN HYD OR L(3)C43. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95046871; PubMed=7958417; RA Mansfield E., Hersperger E., Biggs J., Shearn A.; RT "Genetic and molecular analysis of hyperplastic discs, a gene whose RT product is required for regulation of cell proliferation in RT Drosophila melanogaster imaginal discs and germ cells."; RL Dev. Biol. 165:507-526(1994). RN [2] RP REVISIONS. RA Shearn A.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: E3 UBIQUITIN-PROTEIN LIGASE WHICH ACCEPTS UBIQUITIN FROM CC AN E2 UBIQUITIN-CONJUGATING ENZYME IN THE FORM OF A THIOESTER AND CC THEN DIRECTLY TRANSFERS THE UBIQUITIN TO TARGETED SUBSTRATES (BY CC SIMILARITY). REQUIRED FOR REGULATION OF CELL PROLIFERATION IN CC IMAGINAL DISCS AND GERM CELLS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: PUPAE AND LARVAE. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN- CC THIOLESTER FORMATION. CC -!- SIMILARITY: CONTAINS 1 HECT-TYPE E3 UBIQUITIN-PROTEIN LIGASE CC DOMAIN. CC -!- SIMILARITY: CONTAINS 1 UBA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L14644; AAB88625.1; -. DR PIR; T08437; T08437. DR HSSP; O95071; 1I2T. DR FlyBase; FBgn0002431; hyd. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0008585; P:female gonad development; IMP. DR GO; GO:0007446; P:imaginal disc growth; IMP. DR GO; GO:0007283; P:spermatogenesis; IMP. DR InterPro; IPR000569; HECT_domain. DR InterPro; IPR002004; PABP/HECT. DR InterPro; IPR000449; UBA_domain. DR InterPro; IPR003126; Znf_Nrecognin. DR Pfam; PF00632; HECT; 1. DR Pfam; PF00658; PABP; 1. DR Pfam; PF00627; UBA; 1. DR Pfam; PF02207; zf-UBR1; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00517; PolyA; 1. DR SMART; SM00396; ZnF_UBR1; 1. DR PROSITE; PS50237; HECT; 1. DR PROSITE; PS50030; UBA; 1. KW Ubl conjugation pathway; Ligase; Nuclear protein; Repeat. FT DOMAIN 151 193 UBA. FT DOMAIN 2512 2566 PABP-LIKE. FT DOMAIN 2792 2895 HECT. FT DOMAIN 621 626 POLY-PRO. FT DOMAIN 700 709 POLY-ALA. FT DOMAIN 2587 2590 POLY-VAL. FT BINDING 2864 2864 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 2895 AA; 319672 MW; 4E172B8D5A12B156 CRC64; MQFVLQPLPG SDDQFIERIR EVSDKVNRFG YGSHRIFEQL KIPVKEVVIG PAHIGVLLED GKAFRVSFSI NSEKLDLTKS DAKCSTSGGS GTASASKAPS SSRPMARSRA RLLRATGRSN SAGQGSGSRS TGVIIGGSTS SRPLVTVPAT YVPEELISQA EVVLQGKSRN LIIRELQRTN LDVNLAVNNL LSRDDEEAED TEEGADNYVP EDLISLLDNG FSGDNNSVII DPSDGLFSEE IFSNYSSIRN LLFDRIRSER SNANANAADS NQSATRSTSS GTALTGNSGL PAQISVNADR EAFSRWRDRQ YYGPRRWISK DDYTWEKDAD SKKKEPSPML SPIWISEELQ PWPEKSSVRF KTIGALYSEF IALAESGDLC QWGWSDAEPY KSEAENVYHP KTVCLNIVER VELISANFIR CSVVTETNRV ATWMDEQLGY IGAKLEHSCC AFNEFISDSI TKIYVCSLYT VVKTESNNIY WWGVLPFDQR RFLWDKFRTK TKKPFKVVAT DINVGAQVIM KKCPMYQSGS IGFTCSNGVP KVGQLLNSVW TFTDVCRMKI ININTNSGVD KSQAAGNNLN AHGITPDKDL PKSTAMPSTG SSKNGQSFSN SKESTDRIDM PPPPSPASST CSDTGSVTSH KRTKRATTKE DSNGPQEGRK DEELWEVKDV VFVEDKVGPV GKVLKVDGDF VAVRFPAINA AAVAAAAAAT SSTSNTASTS KEEGKEDDWQ QCRLLRRKMS DISHCYVTRL LAKQPKKINV GGDAAGAQIL TLAVDSRGIH VIKKVLGKIH YSLYNLYNCK QEQNCLFPTD CNSFIGSTPG NILMACNDDC SGNSSTIVLR DGNGALYPLA KDCLGSIKDP QWFDLPPVKS ITMSTISLPA MLSGVNLKSK VCMTALLFDT QKLMPHILRC DVKNSFAALG RLEREDQADT ALVVEERCDG ARNIFHACVI MCAPSSNKDS PPDSPSGGVE KKSLVGLSVA RSIPTVSTSA YVSSIAFGAS ASSSNENSSF ATMSSSAAGS ASSTSRDNRT NLRDMMNRLI NSDQAEQSGS QPMATNNEDH AYIPWPAETP AASNLSASSS QNVSDSIEDD ISKIIPSSSQ SSMLSNIKLG SPTYTFDLAQ RREHALTILQ QMCVSPALRP YLCHMLSTKD AQGQTPFMLS VSCRAYEAGI ILLNTILMLS EQDPQLKEAM IFPNGSPADQ SPLHVICYND TCSFTWTGAD HINQNIFECK TCGLTGSLCC CTECARVCHK GHDCKLKRTA PTAYCDCWEK CKCKALIAGN LTKRFALLCK LVSCTDLVTK FNSKGESILL FLIQTVGRQI VEQRQYRFSV RVRNVSTAAT GATGNNSVIS NRKTSAAEID NDMPDHDLEP PKFARKALER LLIDWNAVRS MIMSGAERGD VPNPAGSASE NSNSEGFNMF IQTQHGSTLL DKFTHSLIVK CTSDHLDTLL LTLVRELQNA SVSNRSKEAE EVVRRFVRSV ARAFVIFNLQ KQPNPQKQKS HSSCNKYVQS CVKVFQTLHK ISIEELCEVS EALIAPVRLG VVRPTAPFTC HRSNLDNSDD LFSVDPLAPS NVESPSEQIL VHDAGNDQSA NFNIQQNYDV VAMETIRDAS ESEEVINGEA NSHNQDDELI ENQGNEDGMQ DDESDNDFTF NDAETESDSD DNQSNQEVQR SVQAGATVGS ENDIGVLFLE DESGDSSAQE EDGSEDGESD DQSDEFNFNE QQLERRSTNS NARSDLAPQT MQWAIRSRDT ARSSVRVPTG SNMVFIDPMA LRRSTVRAST TVTTPSIEPH TMATTASNLA RAFGITIRQI SELISILSYN VLNDIETSLK IQNDEAIAVQ AFVEKRLKAT WDWMFTVMDG TEAQLKFGAY LTNYTDPNHP LHPLNLSAQA SSSQTPAPAT SSSVNGVNIM GSNSRRDFFT YCLSLMRSHT SEHRDALPVL DITALRHIAY VLDAFVYYMR NDSGFYDKQD SISGRINNLS PMTESYDTDD ELANLEEFNA DVQMSASSMP SGSQGTRRHA FFARSESTLT LGCSAPEGFE LPLDMAMPLA DKPHLLQPNS KRQELFANLP LLVTTNANNS GATNDGDGAS IFDYTPTRLG FSNSLKRNER VYETVPIDSS KTGDGNVTNK AEGSTDSNIY VQLKKKQGSD DFKSHKEADG ELRVYAVNNL QTLNFQSTRN QSKYEKVVLM ETDDSLPSTS KSTEALMATR PEVIIAPNKA SVSPATAARS VIVLAGGSCL KTIDSDINNY RLQIYRPQNK PNVIHNIKSQ HQTTCYYFLL VVLSFYQSNF SGIAPCNFLL SAKLTLDLFG RPFMDDVGME HGSVLPELRG FPVKEMRFRR HMEKLRNGQQ RDLVLCKLER NRESLIVQTF KELNTQFGNQ SRRIQPPITF NRVKVTFKDE PGEGSGVARS FYTSIAEALL ASAKIPNLES VQVGTNHSKY VVPFSSILRT TVSGSSRDQS TLQRRGSNSK ILWRSARERK ALNLDARPYT PPNSSDNATP ESLNDHLSVH LQQIGERLYP KIHSINQTHA PKITGMLLEI PTPQLLSVIS SDETLRQKVN EAIEIITFKQ KSETSAQSSQ PKKSPSVVVV DPVDDDNEPL FYSPGKRGFY IPRQGFASFE RINAFRNIGR LIGLCLLQNE LLPLFLQRHV LKYILRRKIK FHDLAFFDPA LYESFRQIIQ NAQTKEGEET INRMELCFVI DLMKEEGCGN RELIPGGRDV VSHRVIYSST SDAIQNIDXI KSQEKALEAL KDGVFDVLPD NSMINLTAED LRLLLNGVGD INVSTLISYT TFNDESSEGP DKLXKFKKWF WSIVEKMNIM ERQHLVYFWT GSPALPASEE GFQPLPSVTI RPADDSHLPT ANTCISRLYI PLYSSKSILR SKMLMAIKSK NFGFV // ID I17A_DROME STANDARD; PRT; 179 AA. AC Q9VNA0; Q8MZB4; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial import inner membrane translocase subunit TIM17 DE 1. GN TIM17B1 OR BCDNA:AT16284 OR CG1158. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPONENT OF THE PREPROTEIN IMPORT MACHINERY OF THE CC MITOCHONDRIAL INNER MEMBRANE. INTEGRAL PART OF A PROTEIN- CC CONDUCTING CHANNEL OF THE MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SUBUNIT: FORMS PART OF THE TIM23 RECEPTOR COMPLEX THAT CONSISTS OF CC AT LEAST 3 DIFFERENT PROTEINS; TIM17, TIM23 AND TIM44 (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TIM17/TIM22/TIM23 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003603; AAF52046.2; -. DR EMBL; AY113269; AAM29274.1; -. DR FlyBase; FBgn0037310; Tim17b1. DR InterPro; IPR003397; Tim17_Tim22. DR Pfam; PF02466; Tim17; 1. KW Hypothetical protein; Transport; Protein transport; Translocation; KW Mitochondrion; Inner membrane; Transmembrane. FT TRANSMEM 17 37 POTENTIAL. FT TRANSMEM 61 81 POTENTIAL. FT TRANSMEM 113 133 POTENTIAL. SQ SEQUENCE 179 AA; 18669 MW; F6E5B914146B5F3D CRC64; MAEYGREPCP FRIVEDCGGA FAMGALGGGA FQAIKGFRNA PSGLGYRLSG GLAAVRARSG LVGGNFAVWG ATFSAIDCSL VYFRKKEDPW NAIISGATTG GILAARTGLT SMLSSALVGG ALLALIEGVG IVVSHYSADS YRQVSPVERQ QRYKQELLRQ QKGVSPLAAT YGEIDSSAL // ID I17C_DROME STANDARD; PRT; 222 AA. AC Q9VGA2; Q8MZE4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial import inner membrane translocase subunit TIM17 DE 3. GN TIM17A1 OR CG10090. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPONENT OF THE PREPROTEIN IMPORT MACHINERY OF THE CC MITOCHONDRIAL INNER MEMBRANE. INTEGRAL PART OF A PROTEIN- CC CONDUCTING CHANNEL OF THE MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SUBUNIT: FORMS PART OF THE TIM23 RECEPTOR COMPLEX THAT CONSISTS OF CC AT LEAST 3 DIFFERENT PROTEINS; TIM17, TIM23 AND TIM44 (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TIM17/TIM22/TIM23 FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC STOP CODON IN POSITION 127. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003695; AAF54783.1; -. DR EMBL; AY113219; AAM29224.1; ALT_TERM. DR FlyBase; FBgn0038018; Tim17a1. DR GO; GO:0005744; C:mitochondrial inner membrane pre-sequence t...; ISS. DR GO; GO:0008565; F:protein transporter activity; ISS. DR GO; GO:0045039; P:mitochondrial inner membrane protein import; ISS. DR InterPro; IPR003397; Tim17_Tim22. DR Pfam; PF02466; Tim17; 1. KW Hypothetical protein; Transport; Protein transport; Translocation; KW Mitochondrion; Inner membrane; Transmembrane. FT TRANSMEM 16 36 POTENTIAL. FT TRANSMEM 60 80 POTENTIAL. FT TRANSMEM 115 135 POTENTIAL. SQ SEQUENCE 222 AA; 24159 MW; B43C23FE61ED2050 CRC64; MEYNRQPCPI RIVEDCGCAF MMGTIGGSLF EFLKGFRNAP TGLQRRLYGG IDLVKMRTPS IAGSFAVWGA TFSTVDCALV HYRQREDAWN SILSGAATGG ILAARNGIRA MANSALVGCL VLAMIEGAGA AVATINAADK GAGIVIKPQR AQWEAILETI DPKRASSTQD FALAEFERVL DKCRASREPN LLQDIPVKSH ERDSKQKPFY SLLDLVKLSQ MF // ID I17D_DROME STANDARD; PRT; 224 AA. AC Q9VN97; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial import inner membrane translocase subunit TIM17 DE 4. GN TIM17A2 OR CG14666. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE PREPROTEIN IMPORT MACHINERY OF THE CC MITOCHONDRIAL INNER MEMBRANE. INTEGRAL PART OF A PROTEIN- CC CONDUCTING CHANNEL OF THE MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SUBUNIT: FORMS PART OF THE TIM23 RECEPTOR COMPLEX THAT CONSISTS OF CC AT LEAST 3 DIFFERENT PROTEINS; TIM17, TIM23 AND TIM44 (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TIM17/TIM22/TIM23 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003603; AAF52051.1; -. DR FlyBase; FBgn0037307; Tim17a2. DR InterPro; IPR003397; Tim17_Tim22. DR Pfam; PF02466; Tim17; 1. KW Hypothetical protein; Transport; Protein transport; Translocation; KW Mitochondrion; Inner membrane; Transmembrane. FT TRANSMEM 16 36 POTENTIAL. FT TRANSMEM 60 80 POTENTIAL. FT TRANSMEM 115 135 POTENTIAL. SQ SEQUENCE 224 AA; 24166 MW; D2417F0878F2E486 CRC64; MEYNRQPCPI RIVEDCGCAF MMGTMGGSLF QYLKGFRNAP SGLRRGLHGG IESVRLRTPA IAGSFAIWGA TFSTVDCVMV SYRQREDSWN AIVSGAATGG ILAARNGIRA MANSAFVGCL VLAMLEGAGA AVATIYASDG GVKAEESLIT VDQQMQRPQW ETSVADSNLT GAELERVLDE CRAYRAHNKM QQPMRSDAVE GKELGQLMKP MHSLVDLVKL AEIV // ID IAP1_DROME STANDARD; PRT; 438 AA. AC Q24306; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Apoptosis 1 inhibitor (Inhibitor of apoptosis 1) (dIAP1) (Thread DE protein). GN IAP1 OR TH. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye imaginal disk; RX MEDLINE=96128128; PubMed=8548811; RA Hay B.A., Wassarman D.A., Rubin G.M.; RT "Drosophila homologs of baculovirus inhibitor of apoptosis proteins RT function to block cell death."; RL Cell 83:1253-1262(1995). CC -!- FUNCTION: APOPTOTIC SUPPRESSOR. OVEREXPRESSION SUPPRESSES RPR AND CC HID-DEPENDENT CELL DEATH IN THE EYE. CC -!- SIMILARITY: BELONGS TO THE IAP FAMILY. CC -!- SIMILARITY: CONTAINS 2 BIR REPEATS. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L49440; AAC41609.1; -. DR PDB; 1JD4; 05-DEC-01. DR PDB; 1JD5; 05-DEC-01. DR PDB; 1JD6; 05-DEC-01. DR FlyBase; FBgn0003691; th. DR GO; GO:0008189; F:apoptosis inhibitor activity; IDA. DR GO; GO:0006916; P:anti-apoptosis; IDA. DR InterPro; IPR001370; BIR. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00653; BIR; 2. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00238; BIR; 2. DR SMART; SM00184; RING; 1. DR PROSITE; PS01282; BIR_REPEAT_1; 2. DR PROSITE; PS50143; BIR_REPEAT_2; 2. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW Apoptosis; Zinc-finger; Repeat; 3D-structure. FT REPEAT 44 110 BIR 1. FT REPEAT 226 293 BIR 2. FT ZN_FING 391 426 RING-TYPE. SQ SEQUENCE 438 AA; 48098 MW; A6C22C8EDF5AEF29 CRC64; MASVVADLPS YGPIAFDQVD NNTNATQLFK NNINKTRMND LNREETRLKT FTDWPLDWLD KRQLAQTGMY FTHAGDKVKC FFCGVEIGCW EQEDQPVPEH QRWSPNCPLL RRRTTNNVPI NAEALDRILP PISYDICGAN DSTLEMREHA YAEGVIPMSQ LIQSIGMNAV NAAGSVTGTA APQPRVTVAT HASTATQATG DVQPETCRPS AASGNYFPQY PEYAIETARL RTFEAWPRNL KQKPHQLAEA GFFYTGVGDR VRCFSCGGGL MDWNDNDEPW EQHALWLSQC RFVKLMKGQL YIDTVAAKPV LAEEKEESTS IGGDTVASTQ ASEEEQQTSL SSEEAVSGDV APSVAPTAAT RIFNKIVEAT AVATPSTNSS GSTSIPEEKL CKICYGAEYN TAFLPCGHVV ACAKCASSVT KCPLCRKPFT DVMRVYFS // ID IAP2_DROME STANDARD; PRT; 498 AA. AC Q24307; Q24115; Q24149; Q24177; Q960U3; Q9V7G1; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Apoptosis 2 inhibitor (Inhibitor of apoptosis 2) (dIAP2) (DIAP) (IAP DE homolog A) (IAP-like protein) (DILP). GN IAP2 OR ILP OR DIHA OR CG8293. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye imaginal disk; RX MEDLINE=96128128; PubMed=8548811; RA Hay B.A., Wassarman D.A., Rubin G.M.; RT "Drosophila homologs of baculovirus inhibitor of apoptosis proteins RT function to block cell death."; RL Cell 83:1253-1262(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=96149249; PubMed=8552191; RA Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G., RA Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.; RT "Suppression of apoptosis in mammalian cells by NAIP and a related RT family of IAP genes."; RL Nature 379:349-353(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96256286; PubMed=8654366; RA Duckett C.S., Nava V.E., Gedrich R.W., Clem R.J., van Dongen J.L., RA Gilfillan M.C., Shiels H., Hardwick J.M., Thompson C.B.; RT "A conserved family of cellular genes related to the baculovirus iap RT gene and encoding apoptosis inhibitors."; RL EMBO J. 15:2685-2694(1996). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Ross J.L.; RL Thesis (1991), Vanderbilt University / Nashville, U.S.A. RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [7] RP SEQUENCE OF 17-498 FROM N.A. RC TISSUE=Larva; RX MEDLINE=96209843; PubMed=8643514; RA Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.; RT "Cloning and expression of apoptosis inhibitory protein homologs that RT function to inhibit apoptosis and/or bind tumor necrosis factor RT receptor-associated factors."; RL Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996). CC -!- FUNCTION: APOPTOTIC SUPPRESSOR. OVEREXPRESSION SUPPRESSES RPR AND CC HID-DEPENDENT CELL DEATH IN THE EYE. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT HIGH LEVELS THROUGHOUT CC DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE IAP FAMILY. CC -!- SIMILARITY: CONTAINS 3 BIR REPEATS. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L49441; AAC41610.1; -. DR EMBL; U45881; AAC46988.1; -. DR EMBL; U32373; AAC47155.1; -. DR EMBL; M96581; -; NOT_ANNOTATED_CDS. DR EMBL; AE003809; AAF58095.1; -. DR EMBL; AY051844; AAK93268.1; -. DR EMBL; U38809; AAB08398.1; -. DR PIR; S68452; S68452. DR PIR; S69545; S69545. DR HSSP; Q13490; 1QBH. DR FlyBase; FBgn0015247; Iap2. DR GO; GO:0008189; F:apoptosis inhibitor activity; IDA. DR GO; GO:0006916; P:anti-apoptosis; IDA. DR InterPro; IPR001370; BIR. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00653; BIR; 3. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00238; BIR; 3. DR SMART; SM00184; RING; 1. DR PROSITE; PS01282; BIR_REPEAT_1; 3. DR PROSITE; PS50143; BIR_REPEAT_2; 3. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW Apoptosis; Zinc-finger; Repeat. FT REPEAT 9 76 BIR 1. FT REPEAT 113 179 BIR 2. FT REPEAT 212 279 BIR 3. FT ZN_FING 451 486 RING-TYPE. FT CONFLICT 5 5 G -> V (IN REF. 2). FT CONFLICT 40 40 N -> K (IN REF. 2). FT CONFLICT 64 65 ER -> AG (IN REF. 3). FT CONFLICT 94 94 E -> K (IN REF. 1). FT CONFLICT 282 282 A -> D (IN REF. 7). FT CONFLICT 286 286 A -> S (IN REF. 3). FT CONFLICT 302 302 P -> Q (IN REF. 2, 5 AND 6). FT CONFLICT 303 303 P -> T (IN REF. 7). FT CONFLICT 327 327 A -> T (IN REF. 2). FT CONFLICT 369 376 ALEVREPP -> DWRCASR (IN REF. 3). SQ SEQUENCE 498 AA; 54506 MW; 66EC36DA6ED24AD6 CRC64; MTELGMELES VRLATFGEWP LNAPVSAEDL VANGFFATGN WLEAECHFCH VRIDRWEYGD QVAERHRRSS PICSMVLAPN HCGNVPRSQE SDNEGNSVVD SPESCSCPDL LLEANRLVTF KDWPNPNITP QALAKAGFYY LNRLDHVKCV WCNGVIAKWE KNDNAFEEHK RFFPQCPRVQ MGPLIEFATG KNLDELGIQP TTLPLRPKYA CVDARLRTFT DWPISNIQPA SALAQAGLYY QKIGDQVRCF HCNIGLRSWQ KEDEPWFEHA KWSPKCQFVL LAKGPAYVSE VLATTAANAS SPPATAPAPT LQADVLMDEA PAKEALALGI DGGVVRNAIQ RKLLSSGCAF STLDELLHDI FDDAGAGAAL EVREPPEPSA PFIEPCQATT SKAASVPIPV ADSIPAKPQA AEAVANISKI TDEIQKMSVA TPNGNLSLEE ENRQLKDARL CKVCLDEEVG VVFLPCGHLA TCNQCAPSVA NCPMCRADIK GFVRTFLS // ID ICCR_DROME STANDARD; PRT; 764 AA. AC Q08180; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Irregular chiasm C-roughest protein precursor (IRREC protein). GN RST. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94102535; PubMed=7503814; RA Ramos R.G., Igloi G.L., Lichte B., Baumann U., Maier D., RA Schneider T., Brandstaetter J.H., Froehlich A., Fischbach K.-F.; RT "The irregular chiasm C-roughest locus of Drosophila, which affects RT axonal projections and programmed cell death, encodes a novel RT immunoglobulin-like protein."; RL Genes Dev. 7:2533-2547(1993). CC -!- FUNCTION: REQUIRED FOR CORRECT AXONAL PATHWAY FORMATION IN CC THE OPTIC LOBE AND FOR PROGRAMMED CELL DEATH IN THE DEVELOPING CC RETINA. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: POSTEMBRYONIC EXPRESSION IS STRONG IN THE CC DEVELOPING OPTIC LOBE AND IN THE EYE IMAGINAL DISC. CC -!- DEVELOPMENTAL STAGE: STRONGLY EXPRESSED IN EMBRYOS. ALSO FOUND CC IN LATE LARVAL AND PUPAL STAGES. CC -!- SIMILARITY: CONTAINS 5 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z21641; CAA79756.1; -. DR EMBL; L11040; AAA16632.1; -. DR PIR; A49448; A49448. DR FlyBase; FBgn0003285; rst. DR GO; GO:0016202; P:regulation of myogenesis; IMP. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR Pfam; PF00047; ig; 4. DR SMART; SM00408; IGc2; 1. DR PROSITE; PS50835; IG_LIKE; 5. KW Transmembrane; Immunoglobulin domain; Glycoprotein; Signal; Repeat; KW Cell adhesion. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 764 IRREGULAR CHIASM C-ROUGHEST PROTEIN. FT DOMAIN 20 533 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 534 556 POTENTIAL. FT DOMAIN 557 764 CYTOPLASMIC (POTENTIAL). FT DOMAIN 21 123 IG-LIKE C2-TYPE 1. FT DOMAIN 117 230 IG-LIKE C2-TYPE 2. FT DOMAIN 245 261 GLY-RICH. FT DOMAIN 237 343 IG-LIKE C2-TYPE 3. FT DOMAIN 346 419 IG-LIKE C2-TYPE 4. FT DOMAIN 430 530 IG-LIKE C2-TYPE 5. FT DOMAIN 637 660 GLN-RICH (OPA-REPEAT). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 313 313 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 393 393 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 400 400 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 507 507 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 764 AA; 82947 MW; 262225D2B2A1C181 CRC64; MLHTMQLLLL ATIVGMVRSS PYTSYQNQRF AMEPQDQTAV VGARVTLPCR VINKQGTLQW TKDDFGLGTS RDLSGFERYA MVGSDEEGDY SLDIYPVMLD DDARYQCQVS PGPEGQPAIR STFAGLTVLV PPEAPKITQG DVIYATADRK VEIECVSVGG KPAAEITWID GLGNVLTDNI EYTVIPLPDQ RRFTAKSVLR LTPKKEHHNT NFSCQAQNTA DRTYRSAKIR VEVKYAPKVK VNVMGSLPGG AGGSVGGAGG GSVHMSTGSR IVEHSQVRLE CRADANPSDV RYRWFINDEP IIGGQKTEMV IRNVTRKFHD AIVKCEVQNS VGKSEDSETL DISYAPSFRQ RPQSMEADVG SVVSLTCEVD SNPQPEIVWI QHPSDRVVGT STNLTFSVSN ETAGRYYCKA NVPGYAEISA DAYVYLKGSP AIGSQRTQYG LVGDTARIEC FASSVPRARH VSWTFNGQEI SSESGHDYSI LVDAVPGGVK STLIIRDSQA YHYGKYNCTV VNDYGNDVAE IQLQAKKSVS LLMTIVGGIS VVAFLLVLTI LVVVYIKCKK RTKLPPADVI SEHQITKNGG VSCKLEPGDR TSNYSDLKVD ISGGYVPYGD YSTHYSPPPQ YLTTCSTKSN GSSTIMQNNH QNQLQLQQQQ QQSHHQHHTQ TTTLPMTFLT NSSGGSLTGS IIGSREIRQD NGLPSLQSTT ASVVSSSPNG SCSNQSTTAA TTTTTHVVVP SSMALSVDPR YSAIYGNPYL RSSNSSLLPP PTAV // ID ICE1_DROME STANDARD; PRT; 323 AA. AC O02002; Q9W1N0; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Caspase-1 precursor (EC 3.4.22.-). GN DCP-1 OR CG5370. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 216-248. RC TISSUE=Embryo; RX MEDLINE=97153052; PubMed=8999799; RA Song Z., McCall K., Steller H.; RT "DCP-1, a Drosophila cell death protease essential for development."; RL Science 275:536-540(1997). RN [2] RP ERRATUM. RA Song Z., McCall K., Steller H.; RL Science 277:167-167(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE ACTIVATION CASCADE OF CASPASES CC RESPONSIBLE FOR APOPTOSIS EXECUTION (BY SIMILARITY). CC PROTEOLYTICALLY CLEAVES POLY(ADP-RIBOSE) POLYMERASE (PARP). LOSS CC OF ZYGOTIC DCP-1 FUNCTION CAUSES LARVAL LETHALITY AND MELANOTIC CC TUMORS. CC -!- SUBUNIT: HETERODIMER OF A 22 KDA (P22) AND A 13 KDA (P13) SUBUNIT. CC -!- DEVELOPMENTAL STAGE: PRESENT UNIFORMLY THROUGHOUT EMBRYOS OF CC STAGES 4 AND 10. IN STAGE 16 EMBRYOS, THE EXPRESSION BECOMES CC RESTRICTED TO THE CENTRAL NERVOUS SYSTEM, THE DEVELOPING GONADS, CC AND A PORTION OF THE GUT. IN STAGE 17 EMBRYOS, EXPRESSION IS CC MAINLY LOCALIZED IN CELLS ALONG THE MIDLINE OF THE CENTRAL NERVOUS CC SYSTEM. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C14. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF001464; AAB58237.1; -. DR EMBL; AE003461; AAF47027.1; -. DR EMBL; BT010065; AAQ22534.1; -. DR HSSP; P42574; 1PAU. DR MEROPS; C14.016; -. DR FlyBase; FBgn0010501; Dcp-1. DR GO; GO:0004199; F:caspase activity; IDA. DR GO; GO:0004207; F:effector caspase activity; NAS. DR GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; IMP. DR GO; GO:0008632; P:apoptotic program; IDA. DR GO; GO:0006922; P:cleavage of lamin; IMP. DR GO; GO:0009795; P:embryonic morphogenesis; IMP. DR GO; GO:0007300; P:nurse cell/oocyte transport (sensu Insecta); IMP. DR InterPro; IPR002138; ICE_p10. DR InterPro; IPR001309; ICE_p20. DR InterPro; IPR002398; Peptidase_C14. DR Pfam; PF00656; Peptidase_C14; 1. DR PRINTS; PR00376; IL1BCENZYME. DR SMART; SM00115; CASc; 1. DR PROSITE; PS01122; CASPASE_CYS; 1. DR PROSITE; PS01121; CASPASE_HIS; 1. DR PROSITE; PS50207; CASPASE_P10; 1. DR PROSITE; PS50208; CASPASE_P20; 1. KW Hydrolase; Thiol protease; Zymogen; Apoptosis. FT PROPEP 1 33 PROBABLE. FT CHAIN 34 202 CASPASE-1 SUBUNIT P22. FT PROPEP 203 215 FT CHAIN 216 323 CASPASE-1 SUBUNIT P13. FT ACT_SITE 154 154 BY SIMILARITY. FT ACT_SITE 196 196 BY SIMILARITY. SQ SEQUENCE 323 AA; 35926 MW; B5FF0FF75EB8E2BD CRC64; MTDECVTRNY GVGIRSPNGS ENRGSFIMAD NTDAKGCTPE SLVVGGATAA SPLPANKFVA RMPVERYASE YNMSHKHRGV ALIFNHEFFD IPSLKSRTGT NVDAQELKKA FENLGFAVSV HKDCKLRDIL KHVGKAAELD HTDNDCLAVA ILSHGEHGYL YAKDTQYKLD NIWHYFTATF CPSLAGKPKL FFIQACQGDR LDGGITLEKG VTETDGESST SYKIPIHADF LFSYSTIPGY FSWRNINNGS WYMQSLIREL NANGKKYDLL TLLTFVNQRV ALDFESNVPA TPMMDRQKQI PCLTSMLTRI LRFGDKPNGN KAG // ID ICE_DROME STANDARD; PRT; 339 AA. AC O01382; Q9VAH1; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Caspase precursor (EC 3.4.22.-) (drICE). GN ICE OR CG7788. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=97327558; PubMed=9184225; RA Fraser A.G., Evan G.I.; RT "Identification of a Drosophila melanogaster ICE/CED-3-related RT protease, drICE."; RL EMBO J. 16:2805-2813(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN THE ACTIVATION CASCADE OF CASPASES CC RESPONSIBLE FOR APOPTOSIS EXECUTION. ACTS DOWNSTREAM OF RPR. CC CLEAVES BACULOVIRUS P35 AND LAMIN DMO IN VITRO. CC -!- SUBUNIT: HETERODIMER OF A 21 KDA (P21) AND A 12 KDA (P12) SUBUNIT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT ALL STAGES WHERE APOPTOSIS CC OCCURS. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C14. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y12261; CAA72937.1; -. DR EMBL; AE003771; AAF56939.1; -. DR EMBL; AY058451; AAL13680.1; -. DR HSSP; P42574; 1PAU. DR MEROPS; C14.015; -. DR FlyBase; FBgn0019972; Ice. DR GO; GO:0004207; F:effector caspase activity; NAS. DR GO; GO:0006915; P:apoptosis; NAS. DR InterPro; IPR002138; ICE_p10. DR InterPro; IPR001309; ICE_p20. DR InterPro; IPR002398; Peptidase_C14. DR Pfam; PF00656; Peptidase_C14; 1. DR PRINTS; PR00376; IL1BCENZYME. DR SMART; SM00115; CASc; 1. DR PROSITE; PS01122; CASPASE_CYS; 1. DR PROSITE; PS01121; CASPASE_HIS; 1. DR PROSITE; PS50207; CASPASE_P10; 1. DR PROSITE; PS50208; CASPASE_P20; 1. KW Hydrolase; Thiol protease; Zymogen; Apoptosis. FT PROPEP 1 28 BY SIMILARITY. FT CHAIN 29 217 CASPASE SUBUNIT P21 (BY SIMILARITY). FT PROPEP 218 230 BY SIMILARITY. FT CHAIN 231 339 CASPASE SUBUNIT P12 (BY SIMILARITY). FT ACT_SITE 169 169 BY SIMILARITY. FT ACT_SITE 211 211 BY SIMILARITY. FT CONFLICT 151 151 A -> S (IN REF. 1). FT CONFLICT 265 265 S -> T (IN REF. 1). SQ SEQUENCE 339 AA; 37363 MW; E105ED29518507EC CRC64; MDATNNGESA DQVGIRVGNP EQPNDHTDAL GSVGSGGAGS SGLVAGSSHP YGSGAIGQLA NGYSSPSSSY RKNVAKMVTD RHAAEYNMRH KNRGMALIFN HEHFEVPTLK SRAGTNVDCE NLTRVLKQLD FEVTVYKDCR YKDILRTIEY AASQNHSDSD CILVAILSHG EMGYIYAKDT QYKLDNIWSF FTANHCPSLA GKPKLFFIQA CQGDRLDGGV TMQRSQTETD GDSSMSYKIP VHADFLIAYS TVPGFYSWRN TTRGSWFMQS LCAELAANGK RLDILTLLTF VCQRVAVDFE SCTPDTPEMH QQKQIPCITT MLTRILRFSD KQLAPAGRV // ID IDE_DROME STANDARD; PRT; 989 AA. AC P22817; DT 01-AUG-1991 (Rel. 19, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Insulin-degrading enzyme (EC 3.4.24.56) (Insulysin) (Insulinase) DE (Insulin protease). GN IDE. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=91133431; PubMed=2126597; RA Kuo W.L., Gehm B.D., Rosner M.R.; RT "Cloning and expression of the cDNA for a Drosophila RT insulin-degrading enzyme."; RL Mol. Endocrinol. 4:1580-1591(1990). RN [2] RP SEQUENCE OF 1-15. RX MEDLINE=89000606; PubMed=3139025; RA Garcia J.V., Fenton B.W., Rosner M.R.; RT "Isolation and characterization of an insulin-degrading enzyme from RT Drosophila melanogaster."; RL Biochemistry 27:4237-4244(1988). CC -!- FUNCTION: CAN CLEAVE INSULIN AND TGF-ALPHA. CC -!- CATALYTIC ACTIVITY: DEGRADATION OF INSULIN, GLUCAGON AND OTHER CC POLYPEPTIDES. NO ACTION ON PROTEINS. CC -!- COFACTOR: BINDS 1 ZINC ION PER SUBUNIT (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M16. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M58465; AAA28439.1; ALT_SEQ. DR PIR; A37254; SNFFIN. DR MEROPS; M16.002; -. DR FlyBase; FBgn0001247; Ide. DR InterPro; IPR001431; Peptidase_M16. DR InterPro; IPR007863; Peptidase_M16_C. DR Pfam; PF00675; Peptidase_M16; 1. DR Pfam; PF05193; Peptidase_M16_C; 2. DR PROSITE; PS00143; INSULINASE; 1. KW Hydrolase; Metalloprotease; Zinc. FT INIT_MET 0 0 FT METAL 80 80 ZINC (BY SIMILARITY). FT ACT_SITE 83 83 BY SIMILARITY. FT METAL 84 84 ZINC (BY SIMILARITY). FT METAL 161 161 ZINC (BY SIMILARITY). FT CONFLICT 10 10 V -> A (IN REF. 2). SQ SEQUENCE 989 AA; 113502 MW; 3F552D4BC1CB2E90 CRC64; TIAESSQKSV TRKPDSMEPI LRLNNIEKSL QDTRDYRGLQ LENGLKVLLI SDPNTDVSAA ALSVQVGHMS DPTNLPGLAH FCEHMLFLGT EKYPHENGYT TYLSQSGGSS NAATYPLMTK YHFHVAPDKL DGALDRFAQF FIAPLFTPSA TEREINAVNS EHEKNLPSDL WRIKQVNRHL AKPDHAYSKF GSGNKTTLSE IPKSKNIDVR DELLKFHKQW YSANIMCLAV IGKESLDELE GMVLEKFSEI ENKNVKVPGW PRHPYAEERY GQKVKIVPIK DIRSLTISFT TDDLTQFYKS GPDNYLTHLI GHEGKGSILS ELRRLGWCND LMAGHQNTQN GFGFFDIVVD LTQEGLEHVD DIVKIVFQYL EMLRKEGPKK WIFDECVKLN EMRFRFKEKE ESENLVTHAV SSMKIFPLEE VLIAPYLSNE WSPDLIKGLL DELVPSKSRI VIVSQSFEPD CDLAEPYYKT KYGITRVAKD TVQSWENCEL NENLKLALPN SFIPTNFDIS DVPADAPKHP TIILDTPILR VWHKQDNQFN KPKACMTFDM SNPIAYLDPL NCNLNHMMVM LLKDQLNEYL YDAELASLKL SVMGKSCGID FTIRGFSDKQ VVLLEKLLDH LFDFSIDEKR FDILKEEYVR SLKNFKAEQP YQHSIYYLAL LLTENAWANM ELLDAMELVT YDRVLNFAKE FFQRLHTECF IFGNVTKQQA TDIAGRVNTR LEATNASKLP ILARQMLKKR EYKLLAGDSY LFEKENEFHK SSCAQLYLQC GAQTDHTNIM VNLVSQVLSE PCYDCLRTKE QLGYIVFSGV RKVNGANGIR IIVQSAKHPS YVEDRIENFL QTYLQVIEDM PLDEFERHKE ALAVKKLEKP KTIFQQFSQF YGEIAMQTYH FEREEAEVAI LRKISKADFV DYFKKFIAKD GEERRVLSVH IVSQQTDENA TSEAEPVEIT NMERHKPISD IVTFKSCKEL YPIALPFLDI KAKGARSKL // ID IF2A_DROME STANDARD; PRT; 341 AA. AC P41374; Q9V3G2; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Eukaryotic translation initiation factor 2 alpha subunit (eIF-2- DE alpha). GN EIF-2-ALPHA OR EIF2A OR EIF2-ALPHA OR CG9946. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94193004; PubMed=8144032; RA Qu S., Cavener D.R.; RT "Isolation and characterization of the Drosophila melanogaster eIF-2 RT alpha gene encoding the alpha subunit of translation initiation RT factor eIF-2."; RL Gene 140:239-242(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: EIF-2 FUNCTIONS IN THE EARLY STEPS OF PROTEIN SYNTHESIS CC BY FORMING A TERNARY COMPLEX WITH GTP AND INITIATOR TRNA. THIS CC PREINITIATION COMPLEX MEDIATES RIBOSOMAL RECOGNITION OF A START CC CODON DURING THE SCANNING PROCESS OF THE LEADER REGION. CC -!- SUBUNIT: HETEROTRIMER COMPOSED OF AN ALPHA, A BETA AND A GAMMA CC CHAIN. CC -!- PTM: PHOSPHORYLATION OF EIF-2-ALPHA IMPAIRS THE RECYCLING OF EIF-2 CC BETWEEN SUCCESSIVE ROUNDS OF INITIATION AND THUS LEADS TO CC INHIBITION OF TRANSLATION. CC -!- SIMILARITY: BELONGS TO THE EIF-2-ALPHA FAMILY. CC -!- SIMILARITY: CONTAINS 1 S1 MOTIF DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19196; AAA53627.1; -. DR EMBL; AE003502; AAF48615.1; -. DR EMBL; AF145633; AAD38608.1; -. DR FlyBase; FBgn0004925; eIF-2-alpha. DR InterPro; IPR008994; Nucleic_acid_OB. DR InterPro; IPR003029; S1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR PROSITE; PS50126; S1; 1. KW Initiation factor; Protein biosynthesis; RNA-binding; KW Phosphorylation. FT DOMAIN 16 87 S1 MOTIF. FT MOD_RES 51 51 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 341 AA; 38645 MW; D06D1B6FBC628DF6 CRC64; MALTSRFYNE RYPEIEDVVM VNVLSIAEMG AYVHLLEYNN IEGMILLSEL SRRRIRSINK LIRVGKTEPV VVIRVDKEKG YIDLSKRRVS PEDVEKCTER FAKAKAINSL LRHVADILGF EGNEKLEDLY QKTAWHFEKK YNNKTVAYDI FKQSVTDPTV FDECNLEPET KEVLLSNIKR KLVSPTVKIR ADIECSCYGY EGIDAVKASL TKGLELSTEE LPIRINLIAP PLYVMTTSTT KKTDGLKALE VAIEHIRAKT SEYDGEFKVI MAPKLVTAID EADLARRLER AEAENAQVAG DDDEEDGADQ EGMQFDPEKE FNHKGSGAGR ANEEDEEEEE D // ID IF2B_DROME STANDARD; PRT; 312 AA. AC P41375; Q9VTZ3; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Eukaryotic translation initiation factor 2 beta subunit (eIF-2-beta). GN EIF-2-BETA OR EIF2B OR EIF2-BETA OR CG4153. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94252579; PubMed=8194763; RA Ye X., Cavener D.R.; RT "Isolation and characterization of the Drosophila melanogaster gene RT encoding translation-initiation factor eIF-2 beta."; RL Gene 142:271-274(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: EIF-2 FUNCTIONS IN THE EARLY STEPS OF PROTEIN SYNTHESIS CC BY FORMING A TERNARY COMPLEX WITH GTP AND INITIATOR TRNA. THIS CC PREINITIATION COMPLEX MEDIATES RIBOSOMAL RECOGNITION OF A START CC CODON DURING THE SCANNING PROCESS OF THE LEADER REGION. CC -!- SUBUNIT: HETEROTRIMER COMPOSED OF AN ALPHA, A BETA AND A GAMMA CC CHAIN. CC -!- SIMILARITY: BELONGS TO THE EIF-2-BETA / EIF-5 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19197; AAA28504.1; -. DR EMBL; AE003541; AAF49902.1; -. DR FlyBase; FBgn0004926; eIF-2-beta. DR InterPro; IPR002735; eIF5_eIF2B. DR Pfam; PF01873; eIF5_eIF2B; 1. DR ProDom; PD004078; eIF5_eIF2B; 1. DR SMART; SM00653; eIF2B_5; 1. KW Initiation factor; Protein biosynthesis; Zinc-finger. FT DOMAIN 13 19 POLY-LYS. FT DOMAIN 63 70 POLY-LYS. FT DOMAIN 93 99 POLY-GLU. FT DOMAIN 110 118 POLY-LYS. FT ZN_FING 260 284 C4-TYPE (POTENTIAL). SQ SEQUENCE 312 AA; 35217 MW; 163B98C43A35A764 CRC64; MDAEDGFDPT LLKKKKKKKT TFDLDAALGL EDDTKKEDPQ DEASAEGGAA AEEDNLDLES FGKKKKKKKK PFNMDEIEAA IPSFGGDDVA ASEEPEEEEI NLDMDFSMAK KKKKSKKKEL DELFADQADD DKSEDKENDE DNSSTWFGSD RDYTYDELLK RVFEIILDKN PDMAAGRKPK FVMRPPQVLR VGTKKTSFAN FMDIAKTLHR LPKHLLDFLL AELGTSGSMD GNQQLIIKGR FQPKQIENVL RRYIKEYVTC HTCRSPETIL QKDTRLFFLQ CESCGSRCSV ASIKSGFQAV TGKRAAIRAK TT // ID IF2G_DROME STANDARD; PRT; 475 AA. AC Q24208; Q9VFA7; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Eukaryotic translation initiation factor 2 gamma subunit (eIF-2-gamma) DE (Suppressor of variegation protein 3-9). GN SU(VAR)3-9 OR EIF2G OR EIF2-GAMMA OR CG6476. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Oregon-R; RX MEDLINE=94349930; PubMed=7915232; RA Tschiersch B., Hofmann A., Krauss V., Dorn R., Korge G., Reuter G.; RT "The protein encoded by the Drosophila position-effect variegation RT suppressor gene Su(var)3-9 combines domains of antagonistic RT regulators of homeotic gene complexes."; RL EMBO J. 13:3822-3831(1994). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Karsnas; RX MEDLINE=20519450; PubMed=11063691; RA Krauss V., Reuter G.; RT "Two genes become one: the genes encoding heterochromatin protein RT Su(var)3-9 and translation initiation factor subunit eIF-2gamma are RT joined to a dicistronic unit in holometabolic insects."; RL Genetics 156:1157-1167(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: EIF-2 FUNCTIONS IN THE EARLY STEPS OF PROTEIN SYNTHESIS CC BY FORMING A TERNARY COMPLEX WITH GTP AND INITIATOR TRNA. THIS CC COMPLEX BINDS TO A 40S RIBOSOMAL SUBUNIT, FOLLOWED BY MRNA BINDING CC TO FORM A 43S PREINITIATION COMPLEX. JUNCTION OF THE 60S RIBOSOMAL CC SUBUNIT TO FORM THE 80S INITIATION COMPLEX IS PRECEDED BY CC HYDROLYSIS OF THE GTP BOUND TO EIF-2 AND RELEASE OF AN EIF-2-GDP CC BINARY COMPLEX. IN ORDER FOR EIF-2 TO RECYCLE AND CATALYZE ANOTHER CC ROUND OF INITIATION, THE GDP BOUND TO EIF-2 MUST EXCHANGE WITH GTP CC BY WAY OF A REACTION CATALYZED BY EIF-2B (BY SIMILARITY). CC -!- SUBUNIT: HETEROTRIMER COMPOSED OF AN ALPHA, A BETA AND A GAMMA CC CHAIN (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Isoforms A and B share the first 80 amino acid residues. CC Experimental confirmation may be lacking for some isoforms; CC Name=B; Synonyms=eIF-2-gamma; CC IsoId=Q24208-1; Sequence=Displayed; CC Name=A; Synonyms=Su(var)3-9; CC IsoId=P45975-1; Sequence=External; CC Name=C; CC IsoId=Q24208-2; Sequence=VSP_001432; CC -!- SIMILARITY: BELONGS TO THE GTP-BINDING ELONGATION FACTOR FAMILY. CC EIF2G SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X80069; CAA56375.1; -. DR EMBL; AJ290956; CAB93767.1; -. DR EMBL; AE003708; AAF55153.1; -. DR EMBL; AE003708; AAN13641.1; -. DR EMBL; AY061102; AAL28650.1; -. DR PIR; S47005; S46941. DR FlyBase; FBgn0003600; Su(var)3-9. DR InterPro; IPR000795; EF_GTPbind. DR InterPro; IPR004161; EFTU_D2. DR InterPro; IPR009001; Elong_init_C. DR InterPro; IPR009000; Translat_factor. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. KW Initiation factor; Protein biosynthesis; GTP-binding; KW Alternative splicing. FT NP_BIND 47 54 GTP (BY SIMILARITY). FT NP_BIND 133 137 GTP (BY SIMILARITY). FT NP_BIND 189 192 GTP (BY SIMILARITY). FT VARSPLIC 1 22 MATAEAQIGVNRNLQKQDLSNL -> MHLRGDVLLGGVAA FT (in isoform C). FT /FTId=VSP_001432. SQ SEQUENCE 475 AA; 51484 MW; 8370B07089DD5422 CRC64; MATAEAQIGV NRNLQKQDLS NLDVSKLTPL SPEVISRQAT INIGTIGHVA HGKSTVVKAI SGVQTVRFKN ELERNITIKL GYANAKIYKC DNPKCPRPAS FVSDASSKDD SLPCTRLNCS GNFRLVRHVS FVDCPGHDIL MATMLNGAAV MDAALLLIAG NESCPQPQTS EHLAAIEIMK LKQILILQNK IDLIKESQAK EQYEEITKFV QGTVAEGAPI IPISAQLKYN IDVLCEYIVN KIPVPPRDFN APPRLIVIRS FDVNKPGCEV ADLKGGVAGG SILSGVLKVG QEIEVRPGVV TKDSDGNITC RPIFSRIVSL FAEQNELQYA VPGGLIGVGT KIDPTLCRAD RLVGQVLGAV GQLPDIYQEL EISYYLLRRL LGVRTDGDKK GARVEKLQKN EILLVNIGSL STGGRISATK GDLAKIVLTT PVCTEKGEKI ALSRRVENHW RLIGWGQIFG GKTITPVLDS QVAKK // ID IF32_DROME STANDARD; PRT; 326 AA. AC O02195; Q9VMX5; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic translation initiation factor 3 subunit 2 (eIF-3 beta) DE (eIF3i) (TRIP-1 homolog). GN TRIP1 OR DMTRIP OR CG8882. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Cho S.H., Evangelista C., Padgett R.W.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: EIF-3 DISSOCIATES RIBOSOMES, PROMOTES INITIATOR MET-TRNA CC AND MRNA BINDING. CC -!- SUBUNIT: EIF-3 IS COMPOSED OF UP TO 12 DIFFERENT SUBUNITS (BY CC SIMILARITY). CC -!- SIMILARITY: CONTAINS 5 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U90930; AAB53431.1; -. DR EMBL; AE003608; AAF52183.1; -. DR FlyBase; FBgn0015834; Trip1. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 1. DR SMART; SM00320; WD40; 5. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. KW Initiation factor; Protein biosynthesis; Repeat; WD repeat. FT REPEAT 8 38 WD 1. FT REPEAT 50 80 WD 2. FT REPEAT 145 175 WD 3. FT REPEAT 188 218 WD 4. FT REPEAT 285 315 WD 5. SQ SEQUENCE 326 AA; 36159 MW; B07D35F9E47F3F31 CRC64; MRPLMLQGHE RSITQIKYNR EGDLLFSCSK DQKPNVWYSL NGERLGTYDG HQGAVWCLDV DWESRKLITG AGDMTAKIWD VEYGTVIASI PTKSSVRTSN FSFSGNQAAY STDKAMGQSC ELFLIDVRNA DSSLSEQEPT LRIPMTESKI TSMLWGPLDE TIITGHDNGN IAIWDIRKGQ KVVDSGTDHS AGINDMQLSK DGTMFVTASK DTTAKLFDSE SLMCLKTYKT ERPVNSAAIS PIMDHVVLGG GQDAMEVTTT STKAGKFDSR FFHLIYEEEF ARLKGHFGPI NSLAFHPDGK SYASGGEDGF VRVQTFDSTY FENIFE // ID IF36_DROME STANDARD; PRT; 435 AA. AC O77410; Q9VVA2; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable eukaryotic translation initiation factor 3 subunit 6 (eIF-3 DE p48) (eIF3e). GN INT6 OR CG9677. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RA Miyazaki S., Diella F., Gallahan D., Sullivan D., Callahan R.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS TO THE 40S RIBOSOME AND PROMOTES THE BINDING OF CC METHIONYL-TRNAI AND MRNA (BY SIMILARITY). CC -!- SUBUNIT: EIF-3 IS COMPOSED OF AT LEAST 12 DIFFERENT SUBUNITS (BY CC SIMILARITY). CC -!- SIMILARITY: CONTAINS 1 PCI DOMAIN. CC -!- SIMILARITY: BELONGS TO THE EIF3S6 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U89162; AAC62307.1; -. DR EMBL; AF132551; AAD27850.1; -. DR EMBL; AE003526; AAF49412.1; -. DR FlyBase; FBgn0025582; Int6. DR InterPro; IPR000717; PCI. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. KW Initiation factor; Protein biosynthesis. SQ SEQUENCE 435 AA; 51162 MW; 6F79D32FBA3EA711 CRC64; MANFDLTRIN CQFLDRHLTF PLLEFLCGKE IYNQQELLEY ILETVNKTNM IDYTMDTRKR LNLSQEMPEE LVQRKAEVLA TLKQLQNEVA PIMKATDILK NGESMKDSKT FVNALQKDYN FKVEHLESAY KLAKYLYECG NYQESTSYLY FCLIVMSPND KNYLNVLWGK LAAEILTLNW NTALEDLTRL RDYIDNANFS TIQALQQRTW LIHWSVLVFF NHPKGRDLII EMFLYKPLYL NAIQTMCPHI MRYLATAVVI NRTRRNALKD LIKVIQQESY TYRDPITEFL ECLYVNFDFE GARLKLHECQ TVILNDFFIV ACLNEFVEDA RLMIFETFCR IHQCITISML ADKLNMKPNE AECWIVNLIR NARLNAKIDS KLGHVVMGTQ PLSPYQQLVE KIDSLSMRSE HLAGLIERKS KQKQNQESAD SWKYY // ID IF4A_DROME STANDARD; PRT; 403 AA. AC Q02748; Q9U9Y6; Q9VMJ8; DT 01-JUL-1993 (Rel. 26, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic initiation factor 4A (eIF4A) (eIF-4A). GN EIF-4A OR EIF4A OR L(2L)162 OR CG9075. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93204899; PubMed=8455559; RA Dorn R., Morawietz H., Reuter G., Saumweber H.; RT "Identification of an essential Drosophila gene that is homologous to RT the translation initiation factor eIF-4A of yeast and mouse."; RL Mol. Gen. Genet. 237:233-240(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head, and Ovary; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: EIF4A IS BOTH A SUBUNIT OF A HIGH MOLECULAR WEIGHT CC PROTEIN COMPLEX INVOLVED IN CAP RECOGNITION AND IS REQUIRED AS A CC SINGLE POLYPEPTIDE CHAIN FOR MRNA BINDING TO RIBOSOME. IT IS AN CC ATP-DEPENDENT SINGLE STRANDED DNA-BINDING PROTEIN WITH A SEQUENCE- CC INDEPENDENT UNWINDING ACTIVITY (HELICASE). CC -!- SUBUNIT: EIF4F IS A MULTI-SUBUNIT COMPLEX, THE COMPOSITION OF CC WHICH VARIES WITH EXTERNAL AND INTERNAL ENVIRONMENTAL CONDITIONS. CC IT IS COMPOSED OF AT LEAST EIF4A, EIF4E AND EIF4G (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69045; CAA48790.1; -. DR EMBL; AE003612; AAF52317.2; -. DR EMBL; AE003612; AAN10567.1; -. DR EMBL; AF145621; AAD38596.1; -. DR EMBL; AY069283; AAL39428.1; -. DR EMBL; AY121623; AAM51950.1; -. DR PIR; S30278; S30278. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0001942; eIF-4a. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. KW Protein biosynthesis; Helicase; Initiation factor; ATP-binding; KW DNA-binding; RNA-binding. FT NP_BIND 74 81 ATP (BY SIMILARITY). FT SITE 179 182 DEAD BOX. FT CONFLICT 167 167 MISSING (IN REF. 1). SQ SEQUENCE 403 AA; 45878 MW; B870FF8C420CC4F2 CRC64; MDDRNEIPQD GPASMEPEGV IESTWHEVYD NFDDMNLREE LLRGIYGYGF EKPSAIQQRA IIPCVRGRDV IAQAQSGTGK TATFSIAILQ QIDTSIRECQ ALILAPTREL ATQIQRVVMA LGEYMKVHSH ACIGGTNVRE DARILESGCH VVVGTPGRVY DMINRKVLRT QYIKLFVLDE ADEMLSRGFK DQIQDVFKML PPDVQVILLS ATMPPDVLEV SRCFMRDPVS ILVKKEELTL EGIKQFYVNV KQENWKLGTL CDLYDTLSIT QSVIFCNTRR KVDQLTQEMS IHNFTVSAMH GDMEQRDREV IMKQFRSGSS RVLITTDLLA RGIDVQQVSL VINYDLPSNR ENYIHRIGRG GRFGRKGVAI NFITDDDRRI LKDIEQFYHT TIEEMPANIA DLI // ID IF4E_DROME STANDARD; PRT; 259 AA. AC P48598; Q95SV3; Q9VSX8; Q9VSX9; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic translation initiation factor 4E (eIF4E) (eIF-4E) (mRNA DE cap-binding protein) (eIF-4F 25 kDa subunit). GN EIF-4E OR EIF4E OR EIF4F OR CG4035. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM I), AND DEVELOPMENTAL STAGE. RX MEDLINE=95260867; PubMed=7742371; RA Hernandez G., Sierra J.M.; RT "Translation initiation factor eIF-4E from Drosophila: cDNA sequence RT and expression of the gene."; RL Biochim. Biophys. Acta 1261:427-431(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS I AND II), AND FUNCTION. RX MEDLINE=96279193; PubMed=8663200; RA Lavoie C.A., Lachance P.E.D., Sonenberg N., Lasko P.; RT "Alternatively spliced transcripts from the Drosophila eIF4E gene RT produce two different Cap-binding proteins."; RL J. Biol. Chem. 271:16393-16398(1996). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS I AND II), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; RX MEDLINE=97218035; PubMed=9065696; RA Hernandez G., del Corral R., Santoyo J., Campuzano S., Sierra J.M.; RT "Localization, structure and expression of the gene for translation RT initiation factor eIF-4E from Drosophila melanogaster."; RL Mol. Gen. Genet. 253:624-633(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. (ISOFORM I). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: RECOGNIZES AND BINDS THE 7-METHYLGUANOSINE-CONTAINING CC MRNA CAP DURING AN EARLY STEP IN THE INITIATION OF PROTEIN CC SYNTHESIS AND FACILITATES RIBOSOME BINDING BY INDUCING THE CC UNWINDING OF THE MRNAS SECONDARY STRUCTURES. CC -!- SUBUNIT: EIF4F IS A MULTI-SUBUNIT COMPLEX, THE COMPOSITION OF CC WHICH VARIES WITH EXTERNAL AND INTERNAL ENVIRONMENTAL CONDITIONS. CC IT IS COMPOSED OF AT LEAST EIF4A, EIF4E AND EIF4G. EIF4E IS ALSO CC KNOWN TO INTERACT WITH OTHER PARTNERS (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=I; Synonyms=A, B; CC IsoId=P48598-1; Sequence=Displayed; CC Name=II; Synonyms=C; CC IsoId=P48598-2; Sequence=VSP_001437; CC -!- TISSUE SPECIFICITY: PREFERENTIAL EXPRESSION IN THE POLE CELLS, AT CC DIFFERENT DEVELOPMENTAL STAGES. CC -!- DEVELOPMENTAL STAGE: THROUGHOUT DEVELOPMENT. CC -!- PTM: PHOSPHORYLATION INCREASES THE ABILITY OF THE PROTEIN TO BIND CC TO MRNA CAPS AND TO FORM THE EIF4F COMPLEX (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC INITIATION FACTOR 4E FAMILY. CC -!- CAUTION: REF.5 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 105. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U16139; AAC46603.1; -. DR EMBL; U54469; AAC03525.1; -. DR EMBL; U54469; AAC03524.1; -. DR EMBL; U63033; AAC47480.1; -. DR EMBL; U63033; AAC47479.1; -. DR EMBL; AE003552; AAF50283.1; -. DR EMBL; AE003552; AAF50281.1; -. DR EMBL; AY060470; AAL25509.1; ALT_FRAME. DR PIR; S55936; S55936. DR HSSP; P07260; 1AP8. DR FlyBase; FBgn0015218; eIF-4E. DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F...; NAS. DR GO; GO:0000339; F:RNA cap binding; IDA. DR GO; GO:0003743; F:translation initiation factor activity; IDA. DR GO; GO:0006325; P:establishment and/or maintenance of chromat...; IMP. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR GO; GO:0007067; P:mitosis; IMP. DR GO; GO:0007076; P:mitotic chromosome condensation; IMP. DR GO; GO:0016070; P:RNA metabolism; IDA. DR GO; GO:0006413; P:translational initiation; IDA. DR InterPro; IPR001040; TIF_eIF_4E. DR Pfam; PF01652; IF4E; 1. DR ProDom; PD003697; TIF_eIF_4E; 1. DR PROSITE; PS00813; IF4E; 1. KW Protein biosynthesis; Translation regulation; Initiation factor; KW RNA-binding; Phosphorylation; Alternative splicing. FT VARSPLIC 1 18 MQSDFHRMKNFANPKSMF -> MVVLETE (in isoform FT II). FT /FTId=VSP_001437. SQ SEQUENCE 259 AA; 29224 MW; B844B2DD5738758E CRC64; MQSDFHRMKN FANPKSMFKT SAPSTEQGRP EPPTSAAAPA EAKDVKPKED PQETGEPAGN TATTTAPAGD DAVRTEHLYK HPLMNVWTLW YLENDRSKSW EDMQNEITSF DTVEDFWSLY NHIKPPSEIK LGSDYSLFKK NIRPMWEDAA NKQGGRWVIT LNKSSKTDLD NLWLDVLLCL IGEAFDHSDQ ICGAVINIRG KSNKISIWTA DGNNEEAALE IGHKLRDALR LGRNNSLQYQ LHKDTMVKQG SNVKSIYTL // ID IF5A_DROME STANDARD; PRT; 159 AA. AC Q9GU68; Q9NDH0; Q9W1C0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic translation initiation factor 5A (eIF-5A). GN EIF-5A OR CG3186. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Posey K.L., Roman G., He J., Cerda R., Davis R.L., Hardin S.H.; RT "Drosophila melanogaster eukaryotic initiation factor 5A."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RA Irion U., Leptin M.; RT "Drosophila homolog of eIF-5a."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE PRECISE ROLE OF EIF-5A IN PROTEIN BIOSYNTHESIS IS CC NOT KNOWN BUT IT FUNCTIONS BY PROMOTING THE FORMATION OF THE FIRST CC PEPTIDE BOND. CC -!- PTM: EIF-5A SEEMS TO BE THE ONLY EUKARYOTIC PROTEIN TO HAVE AN CC HYPUSINE RESIDUE WHICH IS A POST-TRANSLATIONAL MODIFICATION OF A CC LYSINE BY THE ADDITION OF A BUTYLAMINO GROUP (FROM SPERMIDINE). CC -!- SIMILARITY: BELONGS TO THE EIF-5A FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF159443; AAF80375.1; -. DR EMBL; AF187730; AAG17032.1; -. DR EMBL; AE003462; AAM68297.1; -. DR EMBL; AY071396; AAL49018.1; -. DR HSSP; Q58625; 2EIF. DR FlyBase; FBgn0034967; eIF-5A. DR GO; GO:0005829; C:cytosol; NAS. DR GO; GO:0003743; F:translation initiation factor activity; NAS. DR GO; GO:0006413; P:translational initiation; NAS. DR InterPro; IPR001884; EIF5A_hypusine. DR InterPro; IPR005824; KOW. DR InterPro; IPR008991; Transl_SH3_like. DR Pfam; PF01287; eIF-5a; 1. DR Pfam; PF00467; KOW; 1. DR TIGRFAMs; TIGR00037; eIF_5A; 1. DR PROSITE; PS00302; IF5A_HYPUSINE; 1. KW Protein biosynthesis; Initiation factor; Hypusine. FT MOD_RES 51 51 HYPUSINE (BY SIMILARITY). FT CONFLICT 7 7 Q -> H (IN REF. 1 AND 2). FT CONFLICT 106 106 E -> D (IN REF. 2). SQ SEQUENCE 159 AA; 17591 MW; 3F348B25D5AEA040 CRC64; MAELDDQFET TDSGASTTYP MQCSALRKNG FVMLKSRPCK IVEMSTSKTG KHGHAKVHMV GIDIFSNKKY EDICPSTHNM DVPNVKREDL QLIAISDDSF LTLMTESGDL REDLKVPEGE LGEQLRLDFD SGKDLLCTVL KACGEECVIA IKTNTALDK // ID IF5_DROME STANDARD; PRT; 464 AA. AC Q9VXK6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic translation initiation factor 5 (eIF-5). GN EIF5 OR CG9177. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CATALYZES THE HYDROLYSIS OF GTP BOUND TO THE 40S CC RIBOSOMAL INITIATION COMPLEX (40S.MRNA.MET-TRNA[F].EIF-2.GTP) WITH CC THE SUBSEQUENT JOINING OF A 60S RIBOSOMAL SUBUNIT RESULTING IN THE CC RELEASE OF EIF-2 AND THE GUANINE NUCLEOTIDE. THE SUBSEQUENT CC JOINING OF A 60S RIBOSOMAL SUBUNIT RESULTS IN THE FORMATION OF A CC FUNCTIONAL 80S INITIATION COMPLEX (80S.MRNA.MET-TRNA[F]) (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE EIF-2-BETA / EIF-5 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003500; AAF48554.1; -. DR EMBL; AY060843; AAL28391.1; -. DR FlyBase; FBgn0030719; eIF5. DR GO; GO:0005829; C:cytosol; ISS. DR GO; GO:0003743; F:translation initiation factor activity; ISS. DR GO; GO:0006413; P:translational initiation; ISS. DR InterPro; IPR003307; eIF5C. DR InterPro; IPR002735; eIF5_eIF2B. DR Pfam; PF01873; eIF5_eIF2B; 1. DR Pfam; PF02020; W2; 1. DR ProDom; PD004078; eIF5_eIF2B; 1. DR SMART; SM00653; eIF2B_5; 1. DR SMART; SM00515; eIF5C; 1. KW Initiation factor; Protein biosynthesis; GTP-binding. FT NP_BIND 28 35 GTP (POTENTIAL). SQ SEQUENCE 464 AA; 51700 MW; B236088EA54FD880 CRC64; MATVNVNRSV TDIFYRYKMP RLQAKVEGKG NGIKTVLVNM AEVARAIGRP ATYPTKYFGC ELGAQTLFDH KNERFVVNGS HDVNKLQDLL DGFIRKFVLC PECDNPETNL TVSAKNQTIS QSCKACGFHG LLKVNHKVNT FIVKNPPSLN PAAQGSSLTE GKRSRKQKQK NDNADGSMTN NSLANNSGGE SDGGNGTNQA SQTEAEISAA IPEKTAKDDD DEGWSVDVSK EAIRARLQDL TDGAKGMTIS DDYDKTEKER IDIFYELVKD KRDKKQLDDV QTHKELVIEA ERLDIINKAP LVLAELLFTE NIIKDVQKNR PLLLRFTLNN PKAQRYLIGG VEQTVELHKG ILMSKVAGIF KLFYDLDILD EAVILEWAQK VSKRHVSKNI AAEIHEKAMP FVLWLKNAEE ESSESEEEED DESEEDNYVS SAGQRGGQRV VQRGIPRAVA GDEDDEDDVN IDDI // ID IF6_DROME STANDARD; PRT; 245 AA. AC P56538; Q8MLQ6; Q9W1I5; DT 15-JUL-1998 (Rel. 36, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable eukaryotic translation initiation factor 6 (eIF-6). GN EIF6 OR CG17611. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Kaiser S.; RL Thesis (1996), Johannes-Gutenberg University / Mainz, Germany. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: BINDS TO THE 60S RIBOSOMAL SUBUNIT AND PREVENTS ITS CC ASSOCIATION WITH THE 40S RIBOSOMAL SUBUNIT TO FORM THE 80S CC INITIATION COMPLEX (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE EIF-6 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X97641; -; NOT_ANNOTATED_CDS. DR EMBL; AE003462; AAF47074.1; -. DR EMBL; AY094688; AAM11041.1; -. DR HSSP; Q12522; 1G62. DR FlyBase; FBgn0034915; eIF6. DR InterPro; IPR002769; eIF6. DR Pfam; PF01912; eIF6; 1. DR ProDom; PD006880; eIF6; 1. DR SMART; SM00654; eIF6; 1. KW Initiation factor; Protein biosynthesis; Nuclear protein; KW Phosphorylation. FT MOD_RES 174 174 PHOSPHORYLATION (BY CK1) FT (BY SIMILARITY). FT MOD_RES 175 175 PHOSPHORYLATION (BY CK1) FT (BY SIMILARITY). SQ SEQUENCE 245 AA; 26494 MW; 6FAA472072A4156A CRC64; MALRVQFENN DDIGVFTKLT NTYCLVAIGG SETFYSAFEA ELGDTIPVVH ANVGGCRIIG RLTVGNRNGL LVPNSTTDEE LQHLRNSLPD AVKIYRVEER LSALGNVIAC NDYVALVHPD LDKETEEIIA DVLKVEVFRQ TIADNSLVGS YAVLSNQGGM VHPKTSIQDQ DELSSLLQVP LVAGTVNRGS EVLAAGMVVN DWLSFVGMNT TATEISVIES VFKLNQAQPA TVTTKLRAAL IEDMS // ID IHB_DROME STANDARD; PRT; 946 AA. AC O61643; Q8MRB1; Q8WR60; Q9V497; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Inhibin beta chain precursor (Activin beta chain). GN ACTIVIN-BETA OR CG11062. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 209-946 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=22090541; PubMed=12095682; RA Haerry T.E., O'Connor M.B.; RT "Isolation of Drosophila activin and follistatin cDNAs using novel RT MACH amplification protocols."; RL Gene 291:85-93(2002). RN [5] RP SEQUENCE OF 574-946 FROM N.A., AND DEVELOPMENTAL STAGE. RX MEDLINE=98289585; PubMed=9618266; RA Kutty G., Kutty R.K., Samuel W., Duncan T., Jaworski C., Wiggert B.; RT "Identification of a new member of transforming growth factor-beta RT superfamily in Drosophila: the first invertebrate activin gene."; RL Biochem. Biophys. Res. Commun. 246:644-649(1998). CC -!- SUBUNIT: HOMODIMER OR HETERODIMER; DISULFIDE-LINKED (POTENTIAL). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN EMBRYONIC, LARVAL AND ADULT CC STAGES. CC -!- SIMILARITY: BELONGS TO THE TGF-BETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003846; AAF59386.3; -. DR EMBL; AY121686; AAM52013.1; -. DR EMBL; AF454392; AAL51005.1; -. DR EMBL; AF054822; AAC39083.1; -. DR HSSP; P18075; 1BMP. DR FlyBase; FBgn0024913; activin-beta. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0005160; F:transforming growth factor-beta receptor bi...; NAS. DR GO; GO:0016049; P:cell growth; NAS. DR InterPro; IPR002405; Inhibin_alpha. DR InterPro; IPR001839; TGFb. DR Pfam; PF00019; TGF-beta; 1. DR PRINTS; PR00669; INHIBINA. DR ProDom; PD000357; TGFb; 1. DR SMART; SM00204; TGFB; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. KW Growth factor; Glycoprotein; Signal. FT SIGNAL 1 ? POTENTIAL. FT PROPEP ? 833 POTENTIAL. FT CHAIN 834 946 INHIBIN BETA CHAIN. FT DOMAIN 21 50 CYS-RICH. FT DOMAIN 176 200 ARG-RICH. FT DISULFID 837 846 BY SIMILARITY. FT DISULFID 845 912 BY SIMILARITY. FT DISULFID 874 943 BY SIMILARITY. FT DISULFID 878 945 BY SIMILARITY. FT DISULFID 911 911 INTERCHAIN (BY SIMILARITY). FT CARBOHYD 208 208 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 217 217 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 271 271 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 389 389 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 471 471 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 484 484 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 542 542 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 561 561 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 566 566 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 732 732 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 804 804 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 275 275 I -> V (IN REF. 4). FT CONFLICT 517 517 I -> T (IN REF. 4). SQ SEQUENCE 946 AA; 108791 MW; 7CECD6E73EAA306B CRC64; MRFAFDSNHS QSGAPFKGSR CFFNCQCICC RQGCCVVVVK CCCCFNLNCC NSLGSRKSFP QPAAMRKKVA DLEVLRVSRF VAVILVLARW VTAVATLLTS CILLDIFSVP GQSGVADRSQ ASSRTVHVSV PTTPNETPSS TSETKLKLLY GYTSYDINND QQVKSNNLCR VLCKSRNRKR QRRRRRRRNH RRRRHRYTKR LHHLMQDNMS GFEQRLNFSD AKCQSLETNY GTNYDLVQGG KLFSQSERSL LVSPLREIEA PWPAIHGSMR NCSKIKRNRA NLIWLLIGLV WFEVKLINCN GISSSNYYAS NLESHKGCTL CHESGKPNIY TDKDNPHTDY NIYNKYHSNN NFNKKTNQPH NNIAPSDEVR LESIKRQILT KLGLSHKPNV SHPLPKQFIW ETIYRVDGGR MIPNNAFGSS GKNLDQKTIK LRAFASPGSH LFNGRGGRTD QRSERDPSHH KYRSPFDFTF NISKNNVYGK VLRNRSLERI DKKNSFLNGW TENRQLKINS QIASMPIELK SHHNSSPKEL KSGAVRKVNG INGTQMNENA LKKSTYPIDI NHSIDNKTHT GKNGEMSHND YEYFNDYSVQ THDKNRYHEG RSSIGYQPAI HNIEYENQKG HHESFADDHE NIDHEDFFGN TQEIITFAEE GTQYRQYRIL EFSAQNRRVP SQKLSIRSAQ IHIRIDKPHS LWIEKAKSLP EKHLLNTKRK WGANKPHHRI KIWVFQLSTS INITEKGIDK AIIFRASFQV DPKNLGWQKF DLTDTIREWY GHTSHEKLRL LIDCTGCGGR YSLHLFQTSK LRGNSSDYLS TNPNRPFLVL HTESSRTRRV RRRAVDCGGA LNGQCCKESF YVSFKALGWD DWIIAPRGYF ANYCRGDCTG SFRTPDTFQT FHAHFIEEYR KMGLMNGMRP CCAPIKFSSM SLIYYGDDGI IKRDLPKMVV DECGCP // ID IM01_DROME STANDARD; PRT; 45 AA. AC P82706; Q9V8F6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Immune-induced protein 1 precursor (DIM-1). GN IM1 OR CG18108. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 28-43, AMIDATION, DISULFIDE BOND, AND MASS SPECTROMETRY. RC STRAIN=Oregon-R; TISSUE=Hemolymph; RX MEDLINE=98409659; PubMed=9736738; RA Uttenweiler-Joseph S., Moniatte M., Lagueux M., Van Dorsselaer A., RA Hoffmann J.A., Bulet P.; RT "Differential display of peptides induced during the immune response RT of Drosophila: a matrix-assisted laser desorption ionization time-of- RT flight mass spectrometry study."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: HEMOLYMPH. CC -!- INDUCTION: BY BACTERIAL INFECTION. CC -!- MASS SPECTROMETRY: MW=1687.7; METHOD=MALDI. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003799; AAF57711.1; -. DR FlyBase; FBgn0034329; IM1. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0003793; F:defense/immunity protein activity; IDA. DR GO; GO:0006952; P:defense response; IDA. KW Insect immunity; Amidation; Signal. FT SIGNAL 1 20 POTENTIAL. FT PROPEP 21 27 REMOVED BY A DIPEPTIDYLPEPTIDASE. FT CHAIN 28 43 IMMUNE-INDUCED PROTEIN 1. FT MOD_RES 43 43 AMIDATION (G-44 PROVIDE AMIDE GROUP). FT DISULFID 36 39 SQ SEQUENCE 45 AA; 4670 MW; 5DAB6236C020971D CRC64; MKFFSVVTVF VLGLLAVANA VPLSPDPGNV IINGDCRVCN VHGGK // ID IM02_DROME STANDARD; PRT; 45 AA. AC O77150; Q8MLI5; Q9V8F9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Immune-induced protein 2 precursor (DIM-2). GN IM2 OR BCDNA:RH08291 OR CG18106. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SEQUENCE OF 29-44, AMIDATION, DISULFIDE BOND, AND RP MASS SPECTROMETRY. RC STRAIN=Oregon-R; TISSUE=Hemolymph; RX MEDLINE=98409659; PubMed=9736738; RA Uttenweiler-Joseph S., Moniatte M., Lagueux M., Van Dorsselaer A., RA Hoffmann J.A., Bulet P.; RT "Differential display of peptides induced during the immune response RT of Drosophila: a matrix-assisted laser desorption ionization time-of- RT flight mass spectrometry study."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 28-43, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: HEMOLYMPH. CC -!- INDUCTION: BY BACTERIAL INFECTION. CC -!- MASS SPECTROMETRY: MW=1687.7; METHOD=MALDI. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF074003; AAC62494.1; -. DR EMBL; AE003799; AAM68448.1; -. DR EMBL; AY071680; AAL49302.1; -. DR FlyBase; FBgn0025583; IM2. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0003793; F:defense/immunity protein activity; IDA. DR GO; GO:0006952; P:defense response; IDA. KW Insect immunity; Amidation; Signal. FT SIGNAL 1 20 POTENTIAL. FT PROPEP 21 27 REMOVED BY A DIPEPTIDYLPEPTIDASE. FT CHAIN 28 43 IMMUNE-INDUCED PROTEIN 2. FT MOD_RES 43 43 AMIDATION (G-44 PROVIDE AMIDE GROUP). FT DISULFID 36 39 FT CONFLICT 12 19 FGLLALAN -> LRSAGSGQT (IN REF. 1). SQ SEQUENCE 45 AA; 4740 MW; 81986CD63B8135B7 CRC64; MKFFSVVTVF VFGLLALANA VPLSPDPGNV VINGDCKYCN VHGGK // ID IM04_DROME STANDARD; PRT; 42 AA. AC P82705; Q9W2Q9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Immune-induced protein 4 precursor (DIM-4). GN IM4 OR CG15231. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 27-41, AMIDATION, AND MASS SPECTROMETRY. RC STRAIN=Oregon-R; TISSUE=Hemolymph; RX MEDLINE=98409659; PubMed=9736738; RA Uttenweiler-Joseph S., Moniatte M., Lagueux M., Van Dorsselaer A., RA Hoffmann J.A., Bulet P.; RT "Differential display of peptides induced during the immune response RT of Drosophila: a matrix-assisted laser desorption ionization time-of- RT flight mass spectrometry study."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998). RN [4] RP SEQUENCE OF 27-41, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: HEMOLYMPH. CC -!- INDUCTION: BY BACTERIAL INFECTION. CC -!- MASS SPECTROMETRY: MW=1720.9; METHOD=MALDI. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003452; AAF46631.1; -. DR EMBL; AY070691; AAL48162.1; -. DR FlyBase; FBgn0040653; IM4. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0003793; F:defense/immunity protein activity; IDA. DR GO; GO:0006952; P:defense response; IDA. KW Insect immunity; Amidation; Signal. FT SIGNAL 1 20 POTENTIAL. FT PROPEP 21 26 REMOVED BY A DIPEPTIDYLPEPTIDASE. FT CHAIN 27 41 IMMUNE-INDUCED PROTEIN 4. FT MOD_RES 41 41 AMIDATION (G-42 PROVIDE AMIDE GROUP). SQ SEQUENCE 42 AA; 4523 MW; BDB1A618BD251003 CRC64; MKFFQAAALL LAMFAALANA EPVPQPGTVL IQTDNTQYIR TG // ID IM08_DROME STANDARD; PRT; 88 AA. AC Q9Y1A3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitochondrial import inner membrane translocase subunit Tim8. GN TIM8 OR CG1728. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SD; RA Bauer M.F., Adam A., Brunner M., Hofmann S.; RT "Cloning and mapping of the Tim10/DDP related gene family encoding RT small zinc finger proteins involved in mitochondrial carrier import."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TIM8/TIM10 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF142424; AAD39162.1; -. DR EMBL; AE003485; AAF48036.1; -. DR FlyBase; FBgn0027359; Tim8. DR InterPro; IPR004217; Znf_Tim10/DDP. DR Pfam; PF02953; zf-Tim10_DDP; 1. KW Transport; Protein transport; Translocation; Mitochondrion; KW Inner membrane. SQ SEQUENCE 88 AA; 10062 MW; 7FA4CEABDA7CDF0A CRC64; MSDFENLSGN DKELQEFLLI EKQKAQVNAQ IHEFNEICWE KCIGKPSTKL DHATETCLSN CVDRFIDTSL LITQRFAQML QKRGGGDL // ID IM13_DROME STANDARD; PRT; 92 AA. AC Q9VTN3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitochondrial import inner membrane translocase subunit Tim13. GN TIM13 OR CG11611. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: LIKELY TO BE INVOLVED IN THE IMPORT AND INSERTION OF CC HYDROPHOBIC MEMBRANE PROTEINS INTO THE MITOCHONDRIAL INNER CC MEMBRANE (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TIM8/TIM10 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003543; AAF50014.1; -. DR FlyBase; FBgn0036204; Tim13. DR InterPro; IPR004217; Znf_Tim10/DDP. DR Pfam; PF02953; zf-Tim10_DDP; 1. KW Transport; Protein transport; Translocation; Mitochondrion; KW Inner membrane. SQ SEQUENCE 92 AA; 10693 MW; CAC7D4C2059CEF0C CRC64; MAAANMEKGE LMNQVKQQIA LANAQEMLSK MTEKCFKKCI QKPGKSLDST EQRCISQCMD RFMDAWNLVS RTYGNRLQRE QYRTMESLEM TS // ID IM9A_DROME STANDARD; PRT; 95 AA. AC Q9VYD7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitochondrial import inner membrane translocase subunit Tim9A. GN TIM9A OR CG1660. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TIM8/TIM10 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003492; AAF48265.1; -. DR FlyBase; FBgn0030480; Tim9a. DR InterPro; IPR004217; Znf_Tim10/DDP. DR Pfam; PF02953; zf-Tim10_DDP; 1. KW Transport; Protein transport; Translocation; Mitochondrion; KW Inner membrane. SQ SEQUENCE 95 AA; 11098 MW; 5E0DB04A9085ED77 CRC64; MAKTPENIAI DQLDKDQIKT FSDFLMSYNK LSETCFTDCI RDFTTRDVKD SEEKCSLNCM EKYLKMNQRV SQRFQEFQVI AHENALAMAQ KTGKL // ID IM9B_DROME STANDARD; PRT; 117 AA. AC Q9Y0V3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitochondrial import inner membrane translocase subunit Tim9B. GN TIM9B OR TIM9 OR CG17767. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Bauer M.F., Brunner M., Hofmann S.; RT "Cloning and mapping of the Tim10/DDP gene family encoding small zinc RT finger proteins involved in mitochondrial carrier import."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TIM8/TIM10 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF150104; AAD40010.1; -. DR EMBL; AE003512; AAF48985.1; -. DR FlyBase; FBgn0027358; Tim9b. DR InterPro; IPR004217; Znf_Tim10/DDP. DR Pfam; PF02953; zf-Tim10_DDP; 1. KW Transport; Protein transport; Translocation; Mitochondrion; KW Inner membrane. SQ SEQUENCE 117 AA; 13520 MW; 3327A332075A57E5 CRC64; MDSNLRNLKD FFTLYNKVTE LCFSRCVDNL SQRDLGGHED LCVDRCVTKF ARFNQNMMKV YVDVQTTINA KRMEEMEENA RKAEQQQREQ EKERLKEAAA TAVLTPVQPP VAGNLSM // ID IMA_DROME STANDARD; PRT; 522 AA. AC P52295; Q24431; Q9VL45; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Importin alpha subunit (Karyopherin alpha subunit) (Pendulin). GN PEN OR CG4799. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95310331; PubMed=7790350; RA Kuessel P., Frasch M.; RT "Pendulin, a Drosophila protein with cell cycle-dependent nuclear RT localization, is required for normal cell proliferation."; RL J. Cell Biol. 129:1491-1507(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95310330; PubMed=7790349; RA Torok I., Strand D., Schmitt R., Tick G., Torok T., Kiss I., RA Mechler B.M.; RT "The overgrown hematopoietic organs-31 tumor suppressor gene of RT Drosophila encodes an importin-like protein accumulating in the RT nucleus at the onset of mitosis."; RL J. Cell Biol. 129:1473-1489(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS SPECIFICALLY AND DIRECTLY TO SUBSTRATES CONTAINING CC EITHER A SIMPLE OR BIPARTITE NLS MOTIF. PROMOTES DOCKING OF IMPORT CC SUBSTRATES TO THE NUCLEAR ENVELOPE. SEEMS TO ACT AS A CYTOSOLIC CC RECEPTOR FOR BOTH SIMPLE AND BIPARTITE NLS MOTIFS (BY SIMILARITY). CC -!- FUNCTION: IT IS REQUIRED FOR NORMAL CELL PROLIFERATION AND MAY CC SERVE AS AN ADAPTER MOLECULE TO FORM COMPLEXES WITH OTHER CC PROTEINS. MAY ACT AS A TUMOR SUPPRESSOR IN HEMATOPOIETIC CELLS. CC MAY PLAY A ROLE IN THE NUCLEAR IMPORT OF KARYOPHILIC PROTEINS AND CC SOME OF THESE MAY BE REQUIRED FOR THE NORMAL TRANSMISSION AND CC FUNCTION OF PROLIFERATIVE SIGNALS IN THE CELLS. CC -!- SUBUNIT: FORMS A COMPLEX WITH IMPORTIN BETA SUBUNIT. CC -!- SUBCELLULAR LOCATION: SHUTTLES BETWEEN THE CYTOPLASMIC AND NUCLEUS CC IN A CELL CYCLE-DEPENDENT MANNER. CC -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN THE NEUROBLAST STEM CC CELLS. CC -!- DEVELOPMENTAL STAGE: HIGH LEVELS ARE DETECTED DURING THE FIRST CC HALF OF EMBRYOGENESIS REACHING A MAXIMUM BETWEEN 4 AND 8 HRS OF CC DEVELOPMENT. PROTEIN EXPRESSION INCREASES AGAIN FROM THE THIRD CC LARVAL INSTAR ONWARDS. IT IS EXPRESSED IN A MATERNAL/EARLY CC EMBRYONIC PHASE, AND AGAIN DURING MORPHOGENESIS IN LATE LARVAL AND CC PUPAL STAGES. CC -!- SIMILARITY: BELONGS TO THE IMPORTIN ALPHA FAMILY. CC -!- SIMILARITY: CONTAINS 10 ARM REPEATS. CC -!- CAUTION: WAS ORIGINALLY (REF.2) THOUGHT TO BE THE OVERGROWN CC HEMATOPOIETIC ORGANS-31 PROTEIN (OHO-31). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U12269; AAA85260.1; -. DR EMBL; X85752; CAA59753.1; -. DR EMBL; AE003627; AAF52853.1; -. DR PIR; A57319; A57319. DR HSSP; Q02821; 1BK5. DR FlyBase; FBgn0011823; Pen. DR GO; GO:0007301; P:ovarian ring canal formation; IMP. DR GO; GO:0007291; P:sperm individualization; IMP. DR InterPro; IPR008938; ARM. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR002652; ImportinA_B. DR Pfam; PF00514; Armadillo_seg; 8. DR Pfam; PF01749; IBB; 1. DR SMART; SM00185; ARM; 8. DR PROSITE; PS50176; ARM_REPEAT; 3. KW Transport; Protein transport; Repeat. FT DOMAIN 9 49 IBB. FT REPEAT 64 105 ARM 1. FT REPEAT 106 148 ARM 2. FT REPEAT 149 190 ARM 3. FT REPEAT 191 233 ARM 4. FT REPEAT 234 275 ARM 5. FT REPEAT 276 317 ARM 6. FT REPEAT 318 359 ARM 7. FT REPEAT 360 400 ARM 8. FT REPEAT 401 447 ARM 9. FT REPEAT 448 489 ARM 10. FT DOMAIN 490 522 ASP/GLU-RICH (ACIDIC). FT CONFLICT 69 69 L -> P (IN REF. 1). SQ SEQUENCE 522 AA; 57821 MW; B02773EB76812AD1 CRC64; MSKADSNSRQ GSYKANSINT QDSRMRRHEV TIELRKSKKE DQMFKRRNIN DEDLTSPLKE LNGQSPVQLS VDEIVAAMNS EDQERQFLGM QSARKMLSRE RNPPIDLMIG HGIVPICIRF LQNTNNSMLQ FEAAWALTNI ASGTSDQTRC VIEHNAVPHF VALLQSKSMN LAEQAVWALG NIAGDGAAAR DIVIHHNVID GILPLINNET PLSFLRNIVW LMSNLCRNKN PSPPFDQVKR LLPVLSQLLL SQDIQVLADA CWALSYVTDD DNTKIQAVVD SDAVPRLVKL LQMDEPSIIV PALRSVGNIV TGTDQQTDVV IASGGLPRLG LLLQHNKSNI VKEAAWTVSN ITAGNQKQIQ AVIQAGIFQQ LRTVLEKGDF KAQKEAAWAV TNTTTSGTPE QIVDLIEKYK ILKPFIDLLD TKDPRTIKVV QTGLSNLFAL AEKLGGTENL CLMVEEMGGL DKLETLQQHE NEEVYKKAYA IIDTYFSNGD DEAEQELAPQ EVNGALEFNA TQPKAPEGGY TF // ID IMB_DROME STANDARD; PRT; 884 AA. AC O18388; Q9V3E6; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Importin beta subunit (Karyopherin beta-4 subunit) (Protein ketel). GN FS(2)KET OR CG2637. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20556154; PubMed=11102382; RA Lippai M., Tirian L., Boros I., Mihaly J., Erdelyi M., Belecz I., RA Mathe E., Posfai J., Nagy A., Udvardy A., Paraskeva E., Gorlich D., RA Szabad J.; RT "The Ketel gene encodes a Drosophila homologue of importin-beta."; RL Genetics 156:1889-1900(2000). RN [2] RP SEQUENCE FROM N.A. RA Gorlich D., Hartmann E.; RT "Drosophila melanogaster importin beta."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR NUCLEAR PROTEIN IMPORT AND MEDIATES DOCKING CC OF IMPORT SUBSTRATE TO DISTINCT NUCLEOPORINS. CC -!- SUBUNIT: FORMS A COMPLEX WITH AN IMPORTIN ALPHA SUBUNIT. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE IMPORTIN BETA FAMILY. CC -!- SIMILARITY: CONTAINS 1 IMPORTIN N-TERMINAL DOMAIN. CC -!- SIMILARITY: CONTAINS 8 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ002729; CAA05691.2; -. DR EMBL; AF222745; AAF34680.1; -. DR EMBL; AE003667; AAF53918.1; -. DR FlyBase; FBgn0000986; Fs(2)Ket. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005635; C:nuclear membrane; IDA. DR GO; GO:0007304; P:eggshell formation (sensu Insecta); IMP. DR GO; GO:0006607; P:NLS-bearing substrate-nucleus import; IDA. DR GO; GO:0000059; P:protein-nucleus import, docking; IDA. DR InterPro; IPR008938; ARM. DR InterPro; IPR000357; HEAT. DR InterPro; IPR001494; Importinb_N. DR Pfam; PF03810; IBN_NT; 1. DR PROSITE; PS50077; HEAT_REPEAT; 1. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. KW Transport; Protein transport; Repeat. FT DOMAIN 27 107 IMPORTIN N-TERMINAL. FT REPEAT 174 213 HEAT 1. FT REPEAT 261 298 HEAT 2. FT REPEAT 323 367 HEAT 3. FT REPEAT 368 405 HEAT 4. FT REPEAT 410 447 HEAT 5. FT REPEAT 506 546 HEAT 6. FT REPEAT 607 647 HEAT 7. FT REPEAT 693 732 HEAT 8. FT DOMAIN 335 348 IAB BINDING (BY SIMILARITY). FT DOMAIN 340 425 RAN-GTP BINDING (BY SIMILARITY). SQ SEQUENCE 884 AA; 98695 MW; DE6DACB927B314EC CRC64; MTSDIAMQLI AILEKTVSPD KNELLSAKNF LEQAAASNLP EFLKALSEIL VNTANSAVAR MAAGLQLKNH LTSKDEKVSQ QYQDRWHQFP SEIRELIKNN ILAALGTENT RPSCAAQCVA YVAVIELPIN RWPMLIQTLV NKVVSEGSSE MHRESALEAI GYICQDIRFG VMENQSNDVL TAIIHGMRKV EPSNHVRLAA TTALHNSLEF TKSNFEKDME RNFIMEVVCE ATQCQDSQIC VAALQCLVKI MTLYYQYMEP YMAQALFPIT LAAMKSDNDA VALQGIEFWS NVCDEEIDLA IESQEATDQG RAPQRVSKHY ARGALQFLTP VLVEKLTKQD ECDDEDTWSP AKAASVCLMV LATCCEDEIV PHVLPFIKEN IESPNWRFRD AAVMTFGSVL NGLETNTLKP LVEQAMPTLI RLMYDSSVIV RDTIAWTFGR ICDIIPEAAI NETYLQTLLE CFVKSLKSEP RVAANVCWAF IGLSDAAWEA AVTNDGETPE TYALSPYFEY IITQLLETTD RSDGAQANLR CAAYQALMDM IKNSPLDCYL VVQRTTLVIL ERLNQVMQME TQINNHSDRH QFNDLQSLLC ATLQSVLRKV HEQDAPQISD AIMTALLTMF NSSAGKSGVV QEEAFLAVST LVELLGAQFA KYMPAFKDFL VMGLKNFQEY QVCCAAVGLT GDIFRALKDL MVPYSNEIMT VLINNLTEPT IHRTVKPQVL SAFGDIALSI GNHFLPYLSM VLDMLRVASN LQTDANNFDM NEYINELRES ILEAYTGIIQ GLKGVDQTAH TDVMHMEPHL MHIISFIKRI AQEGDVSDSM LASAAGFIGD LCTSFGPRLY PLLDDAIITQ FLAEGKRSKA QRTKMLCTWA VKEIKKINTQ VITQ // ID IMDH_DROME STANDARD; PRT; 537 AA. AC Q07152; Q26455; Q9W2R8; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) (IMP DE dehydrogenase) (IMPDH) (IMPD) (Raspberry protein). GN RAS OR CG1799. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Nash D., Hu S.; RT "Drosophila inosine monophosphate dehydrogenase is encoded at the RT raspberry locus."; RL (In) Abstracts of the 35th meeting of the Canadian Federation of RL Biological Societies, pp.72-72, Victoria (1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94259281; PubMed=7911114; RA Nash D., Hu S., Leonard N.J., Tiong S.Y., Fillips D.; RT "The raspberry locus of Drosophila melanogaster includes an inosine RT monophosphate dehydrogenase like coding sequence."; RL Genome 37:333-344(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94114565; PubMed=7904480; RA Sifri C.D., Wilson K., Smolik S., Forte M., Ullman B.; RT "Cloning and sequence analysis of a Drosophila melanogaster cDNA RT encoding IMP dehydrogenase."; RL Biochim. Biophys. Acta 1217:103-106(1994). RN [4] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=96069715; PubMed=7476879; RA Slee R., Bownes M.; RT "The raspberry locus encodes Drosophila inosine monophosphate RT dehydrogenase."; RL Mol. Gen. Genet. 248:755-766(1995). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: IMP IS THE RATE LIMITING ENZYME IN THE DE NOVO SYNTHESIS CC OF GUANINE NUCLEOTIDES AND THEREFORE IS INVOLVED IN THE REGULATION CC OF CELL GROWTH. CC -!- CATALYTIC ACTIVITY: INOSINE 5'-PHOSPHATE + NAD(+) + H(2)O = CC XANTHOSINE 5'-PHOSPHATE + NADH. CC -!- PATHWAY: FIRST REACTION UNIQUE TO GMP BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO THE IMPDH/GMPR FAMILY. CC -!- SIMILARITY: CONTAINS 2 CBS DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L14847; AAA21831.1; -. DR EMBL; L22608; AAA16839.1; -. DR EMBL; S80430; AAB35628.1; -. DR EMBL; AE003451; AAF46622.1; -. DR PIR; S41064; S41064. DR HSSP; P12268; 1B3O. DR FlyBase; FBgn0003204; ras. DR InterPro; IPR000644; CBS_domain. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR005990; IMP_dehyd. DR InterPro; IPR001093; IMPDh/GMPRtase. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. KW Oxidoreductase; NAD; GMP biosynthesis; Purine biosynthesis; Repeat; KW CBS domain. FT DOMAIN 134 189 CBS 1. FT DOMAIN 198 251 CBS 2. FT BINDING 350 350 IMP (BY SIMILARITY). FT CONFLICT 38 38 D -> V (IN REF. 4). FT CONFLICT 53 53 T -> P (IN REF. 4). FT CONFLICT 99 102 EMAI -> RCH (IN REF. 4). FT CONFLICT 184 184 D -> A (IN REF. 4). FT CONFLICT 194 194 V -> S (IN REF. 4). FT CONFLICT 216 217 AN -> EH (IN REF. 4). FT CONFLICT 226 229 GKLP -> ATA (IN REF. 4). FT CONFLICT 244 244 T -> A (IN REF. 4). FT CONFLICT 261 262 KQ -> TR (IN REF. 4). FT CONFLICT 265 266 VG -> CP (IN REF. 4). FT CONFLICT 277 278 AR -> GCRA (IN REF. 4). FT CONFLICT 284 284 A -> R (IN REF. 4). FT CONFLICT 301 301 Y -> I (IN REF. 4). FT CONFLICT 387 388 QS -> HA (IN REF. 4). SQ SEQUENCE 537 AA; 57829 MW; A5EAB41AEAA64EBD CRC64; MESTTKVKVN GFVESTSSSA APAIQTKSTT GFDAELQDGL SCKELFQNGE GLTYNDFLIL PGYIDFTAEE VDLSSPLTKS LTLRAPLVSS PMDTVTESEM AIAMALCGGI GIIHHNCTPE YQALEVHKVK KYKHGFMRDP SVMSPTNTVG DVLEARRKNG FTGYPVTENG KLGGKLLGMV TSRDIDFREN QPEVLLADIM TTELVTAPNG INLPTANAIL EKSKKGKLPI VNQAGELVAM IARTDLKKAR SYPNASKDSN KQLLVGAAIG TRSEDKARLA LLVANGVDVI ILDSSQGNSV YQVEMIKYIK ETYPELQVIG GNVVTRAQAK NLIDAGVDGL RVGMGSGSIC ITQEVMACGC PQATAVYQVS TYARQFGVPV IADGGIQSIG HIVKAIALGA SAVMMGSLLA GTSEAPGEYF FSDGVRLKKY RGMGSLEAME RGDAKGAAMS RYYHNEMDKM KVAQGVSGSI VDKGSVLRYL PYLECGLQHS CQDIGANSIN KLRDMIYNGQ LRFMKRTHSA QLEGNVHGLF SYEKRLF // ID IML2_DROME STANDARD; PRT; 263 AA. AC Q09024; Q95SU7; Q9VZF7; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Neural/ectodermal development factor IMP-L2 precursor. GN IMPL2 OR CG15009. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=94139565; PubMed=8306886; RA Garbe J.C., Yang E., Fristrom J.W.; RT "IMP-L2: an essential secreted immunoglobulin family member RT implicated in neural and ectodermal development in Drosophila."; RL Development 119:1237-1250(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ESSENTIAL DEVELOPMENTAL ROLE DURING EMBRYOGENESIS, IN CC PARTICULAR THE NORMAL DEVELOPMENT OF THE NERVOUS SYSTEM. MAY BE CC INVOLVED IN SOME ASPECT OF CELL ADHESION. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: DETECTED IN SEVERAL SITES INCLUDING THE CC VENTRAL NEUROECTODERM, THE TRACHEAL PITS, THE PHARYNX AND CC ESOPHAGUS, AND SPECIFIC NEURONAL CELL BODIES, WHERE IT IS CC PRIMARILY EXPRESSED. CC -!- DEVELOPMENTAL STAGE: FIRST EXPRESSED AT THE CELLULAR BLASTODERM CC STAGE AND CONTINUES TO BE EXPRESSED THROUGH SUBSEQUENT CC DEVELOPMENT. CC -!- INDUCTION: BY 20-HYDROXYECDYSONE. CC -!- SIMILARITY: CONTAINS 2 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L23066; AAB59251.1; -. DR EMBL; AE003480; AAF47866.3; -. DR EMBL; AY060476; AAL25515.1; -. DR FlyBase; FBgn0001257; ImpL2. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003599; Ig. DR InterPro; IPR003598; Ig_c2. DR Pfam; PF00047; ig; 2. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 2. DR PROSITE; PS50835; IG_LIKE; 2. KW Immunoglobulin domain; Cell adhesion; Signal; Repeat; KW Developmental protein. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 263 NEURAL/ECTODERMAL DEVELOPMENT FACTOR FT IMP-L2. FT DOMAIN 44 145 IG-LIKE C2-TYPE 1. FT DOMAIN 170 256 IG-LIKE C2-TYPE 2. FT DISULFID 76 135 BY SIMILARITY. FT DISULFID 191 240 BY SIMILARITY. FT CONFLICT 173 173 I -> V (IN REF. 1). SQ SEQUENCE 263 AA; 29435 MW; CF3AC5F43C2CF71A CRC64; MNLHVCALAL LLFGSIATVR GRAVDLVDDS NDVDNSIEAE EEKPRNRAFE ADWLKFTKTP PTKLQQADGA TIEIVCEMMG SQVPSIQWVV GHLPRSELDD LDSNQVAEEA PSAIVRVRSS HIIDHVLSEA RTYTCVGRTG SKTIYASTVV HPPRSSRLTP EKTYPGAQKP RIIYTEKTHL DLMGSNIQLP CRVHARPRAE ITWLNNENKE IVQGHRHRVL ANGDLLISEI KWEDMGNYKC IARNVVGKDT ADTFVYPVLN EED // ID IMP2_DROME STANDARD; PRT; 466 AA. AC P29681; Q9VZN9; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 20-hydroxyecdysone protein precursor (20-HE). GN IMPE2 OR IMP-E2 OR CG1934. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 444-454. RX MEDLINE=90323384; PubMed=2115480; RA Paine-Saunders S., Fristrom D., Fristrom J.W.; RT "The Drosophila IMP-E2 gene encodes an apically secreted protein RT expressed during imaginal disc morphogenesis."; RL Dev. Biol. 140:337-351(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLY HAS AN ESSENTIAL ROLE IN EMBRYOGENESIS, CC INDUCES MORPHOGENESIS OF IMAGINAL DISKS, AND MAY PARTICIPATE CC IN MULTIMOLECULAR AGGREGATES. CC -!- SUBCELLULAR LOCATION: SECRETED FROM THE APICAL CELL SURFACE. CC -!- DEVELOPMENTAL STAGE: PRODUCED DURING MID EMBRYOGENESIS, AND CC IMAGINAL DISK MORPHOGENESIS. CC -!- DOMAIN: THE REGIONS 203-253, 256-333 AND 335-377 ARE THOUGHT TO CC CONTAIN EITHER ALPHA HELICAL OR BETA PLEATED SHEET MOTIFS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M55099; AAA63632.1; -. DR EMBL; AE003478; AAF47780.1; -. DR EMBL; AY061270; AAL28818.1; -. DR PIR; A37351; A37351. DR FlyBase; FBgn0001254; ImpE2. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005576; C:extracellular; IDA. KW Signal; Glycoprotein; Repeat. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 466 20-HYDROXYECDYSONE PROTEIN. FT DOMAIN 48 157 16 X REPEATS. FT REPEAT 48 50 1 (APPROXIMATE). FT REPEAT 53 55 2 (APPROXIMATE). FT REPEAT 58 60 3 (APPROXIMATE). FT REPEAT 70 72 4 (APPROXIMATE). FT REPEAT 74 76 5 (APPROXIMATE). FT REPEAT 78 80 6 (APPROXIMATE). FT REPEAT 82 84 7 (APPROXIMATE). FT REPEAT 90 92 8 (APPROXIMATE). FT REPEAT 94 96 9 (APPROXIMATE). FT REPEAT 98 100 10 (APPROXIMATE). FT REPEAT 102 104 11 (APPROXIMATE). FT REPEAT 106 108 12 (APPROXIMATE). FT REPEAT 125 127 13 (APPROXIMATE). FT REPEAT 139 141 14 (APPROXIMATE). FT REPEAT 148 150 15 (APPROXIMATE). FT REPEAT 155 157 16 (APPROXIMATE). FT CARBOHYD 294 294 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 352 352 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 466 AA; 49809 MW; A9FE40171C568BA9 CRC64; MKPVALILVF LAISQARVLN LPKEAIDIPV AIVEDKEPPV ALSLVKEEVK AEEVKPEEVK PIAQEEKAKD LKEEVKPEIK PEIKEQPKPD IKDEIKEDLK ADIKEELKEK IEEQINELPN AKPLELKEKS LEAEEKPQEI KEEVQQPEIK KEATEIKEEP AQNILKSLPA EETVVVPAEE LSPNPVEQEQ SENQDAAHPQ VRQATQATPT QQSTTQGNFV QQLIQNSPIG QFLNQFQPQP AAAAAPAAAQ VQADDAAAAA PATPAPTVPG FLNPQAAITS AQQAVQNAAQ SAVNATTQAF QGIQQFASNL GNQFQNTLSS LTGQQQQAVS TTPRPPGPIQ QFVNNVFGGN NNATAAAPPA QQSGNPLQGI INFLGGNRPQ NAPAAAPATQ ATEKPAVDDK IDPANDEVGE FVPESDNELR ASGENIDDSF EDAGVPSNEV IVVNDDAGEE GNAVQNHPVA TDAVAL // ID INL1_DROME STANDARD; PRT; 154 AA. AC Q9VT50; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable insulin-like peptide 1 precursor. GN ILP1 OR CG14173. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE INSULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003550; AAF50205.1; -. DR HSSP; P01343; 1GF1. DR FlyBase; FBgn0044051; Ilp1. DR InterPro; IPR004825; Ins/IGF/relax. DR Pfam; PF00049; Insulin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Cleavage on pair of basic residues; Signal. FT SIGNAL 1 29 POTENTIAL. FT CHAIN 30 154 PROBABLE INSULIN-LIKE PEPTIDE 1. FT CHAIN 30 69 PROBABLE INSULIN-LIKE PEPTIDE 1 B CHAIN FT (POTENTIAL). FT PROPEP 73 122 CONNECTING PEPTIDE (POTENTIAL). FT CHAIN 125 154 PROBABLE INSULIN-LIKE PEPTIDE 1 A CHAIN FT (POTENTIAL). FT DISULFID 49 138 INTERCHAIN (BY SIMILARITY). FT DISULFID 61 151 INTERCHAIN (BY SIMILARITY). FT DISULFID 137 142 BY SIMILARITY. SQ SEQUENCE 154 AA; 16851 MW; 65E78F17EDC12041 CRC64; MFSQHNGAAV HGLRLQSLLI AAMLTAAMAM VTPTGSGHQL LPPGNHKLCG PALSDAMDVV CPHGFNTLPR KRESLLGNSD DDEDTEQEVQ DDSSMWQTLD GAGYSFSPLL TNLYGSEVLI KMRRHRRHLT GGVYDECCVK TCSYLELAIY CLPK // ID INL2_DROME STANDARD; PRT; 137 AA. AC Q9VT51; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable insulin-like peptide 2 precursor (Insulin-related peptide). GN ILP2 OR IRP OR CG8167. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21107400; PubMed=11179818; RA Vanden Broeck J.; RT "Neuropeptides and their precursors in the fruitfly, Drosophila RT melanogaster."; RL Peptides 22:241-254(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE INSULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ291726; CAC17605.1; -. DR EMBL; AE003550; AAF50204.1; -. DR EMBL; AY069095; AAL39240.1; -. DR HSSP; P01344; 1GF2. DR FlyBase; FBgn0036046; Ilp2. DR InterPro; IPR004825; Ins/IGF/relax. DR Pfam; PF00049; Insulin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Cleavage on pair of basic residues; Signal. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 137 PROBABLE INSULIN-LIKE PEPTIDE 2. FT CHAIN 27 50 PROBABLE INSULIN-LIKE PEPTIDE 2 B CHAIN FT (POTENTIAL). FT PROPEP 53 104 CONNECTING PEPTIDE (POTENTIAL). FT CHAIN 108 137 PROBABLE INSULIN-LIKE PEPTIDE 2 A CHAIN FT (POTENTIAL). FT DISULFID 29 119 INTERCHAIN (BY SIMILARITY). FT DISULFID 41 132 INTERCHAIN (BY SIMILARITY). FT DISULFID 118 123 BY SIMILARITY. SQ SEQUENCE 137 AA; 15254 MW; F5B2A357D7B653D6 CRC64; MSKPLSFISM VAVILLASST VKLAQGTLCS EKLNEVLSMV CEEYNPVIPH KRAMPGADSD LDALNPLQFV QEFEEEDNSI SEPLRSALFP GSYLGGVLNS LAEVRRRTRQ RQGIVERCCK KSCDMKALRE YCSVVRN // ID INL3_DROME STANDARD; PRT; 126 AA. AC Q9VT52; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable insulin-like peptide 3 precursor. GN ILP3 OR CG14167. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE INSULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003550; AAF50203.1; -. DR FlyBase; FBgn0044050; Ilp3. DR InterPro; IPR004825; Ins/IGF/relax. DR Pfam; PF00049; Insulin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Cleavage on pair of basic residues; Signal. FT SIGNAL 1 29 POTENTIAL. FT CHAIN 30 126 PROBABLE INSULIN-LIKE PEPTIDE 3. FT CHAIN 30 48 PROBABLE INSULIN-LIKE PEPTIDE 3 B CHAIN FT (POTENTIAL). FT PROPEP 51 89 CONNECTING PEPTIDE (POTENTIAL). FT CHAIN 92 126 PROBABLE INSULIN-LIKE PEPTIDE 3 A CHAIN FT (POTENTIAL). FT DISULFID 34 101 INTERCHAIN (BY SIMILARITY). FT DISULFID 46 114 INTERCHAIN (BY SIMILARITY). FT DISULFID 100 105 BY SIMILARITY. SQ SEQUENCE 126 AA; 14367 MW; 00B4827E61760A83 CRC64; MGIEMRCQDR RILLPSLLLL ILMIGGVQAT MKLCGRKLPE TLSKLCVYGF NAMTKRTLDP VNFNQIDGFE DRSLLERLLS DSSVQMLKTR RLRDGVFDEC CLKSCTMDEV LRYCAAKPRT VTCNKL // ID INL4_DROME STANDARD; PRT; 134 AA. AC Q9VT53; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable insulin-like peptide 4 precursor. GN ILP4 OR CG6736. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE INSULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003550; AAF50202.1; -. DR FlyBase; FBgn0044049; Ilp4. DR InterPro; IPR004825; Ins/IGF/relax. DR Pfam; PF00049; Insulin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Cleavage on pair of basic residues; Signal. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 134 PROBABLE INSULIN-LIKE PEPTIDE 4. FT CHAIN 27 48 PROBABLE INSULIN-LIKE PEPTIDE 4 B CHAIN FT (POTENTIAL). FT PROPEP 51 105 CONNECTING PEPTIDE (POTENTIAL). FT CHAIN 108 134 PROBABLE INSULIN-LIKE PEPTIDE 4 A CHAIN FT (POTENTIAL). FT DISULFID 31 120 INTERCHAIN (BY SIMILARITY). FT DISULFID 43 133 INTERCHAIN (BY SIMILARITY). FT DISULFID 119 124 BY SIMILARITY. SQ SEQUENCE 134 AA; 15139 MW; AE8D916950C16075 CRC64; MSLIRLGLAL LLLLATVSQL LQPVQGRRKM CGEALIQALD VICVNGFTRR VRRSSASKDA RVRDLIRKLQ QPDEDIEQET ETGRLKQKHT DADTEKGVPP AVGSGRKLRR HRRRIAHECC KEGCTYDDIL DYCA // ID INSR_DROME STANDARD; PRT; 2146 AA. AC P09208; Q24023; Q24089; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Insulin-like receptor precursor (EC 2.7.1.112). GN INR OR INR-A OR DIR-A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95354655; PubMed=7628438; RA Fernandez R., Tabarini D., Azpiazu N., Frasch M., Schlessinger J.; RT "The Drosophila insulin receptor homolog: a gene essential for RT embryonic development encodes two receptor isoforms with different RT signaling potential."; RL EMBO J. 14:3373-3384(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95181404; PubMed=7876183; RA Ruan Y., Chen C., Cao Y., Garofalo R.S.; RT "The Drosophila insulin receptor contains a novel carboxyl-terminal RT extension likely to play an important role in signal transduction."; RL J. Biol. Chem. 270:4236-4243(1995). RN [3] RP SEQUENCE OF 652-1749 FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=87100165; PubMed=3099787; RA Nishida Y., Hata M., Nishizuka Y., Rutter W.J., Ebina Y.; RT "Cloning of a Drosophila cDNA encoding a polypeptide similar to the RT human insulin receptor precursor."; RL Biochem. Biophys. Res. Commun. 141:474-481(1986). RN [4] RP SEQUENCE OF 1297-1595 FROM N.A. RX MEDLINE=86259667; PubMed=3014506; RA Petruzzelli L., Herrera R., Arenas-Garcia R., Fernandez R., RA Birnbaum M.J., Rosen O.M.; RT "Isolation of a Drosophila genomic sequence homologous to the kinase RT domain of the human insulin receptor and detection of the RT phosphorylated Drosophila receptor with an anti-peptide antibody."; RL Proc. Natl. Acad. Sci. U.S.A. 83:4710-4714(1986). CC -!- FUNCTION: THIS RECEPTOR PROBABLY BINDS AN INSULIN RELATED PROTEIN CC AND HAS A TYROSINE-PROTEIN KINASE ACTIVITY (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBUNIT: TETRAMER OF 2 ALPHA AND 2 BETA CHAINS LINKED BY DISULFIDE CC BONDS. THE ALPHA CHAINS CONTRIBUTE TO THE FORMATION OF THE LIGAND- CC BINDING DOMAIN, WHILE THE BETA CHAINS CARRY THE KINASE DOMAIN. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. INSULIN CC RECEPTOR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U28136; AAA68953.1; -. DR EMBL; U18351; AAC47458.1; -. DR EMBL; M14778; AAA28644.1; -. DR EMBL; M13568; AAA28645.1; -. DR HSSP; P06213; 1IRK. DR FlyBase; FBgn0013984; InR. DR GO; GO:0005899; C:insulin receptor complex; IDA. DR GO; GO:0005911; C:intercellular junction; IDA. DR GO; GO:0005009; F:insulin receptor activity; IDA. DR GO; GO:0007568; P:aging; IMP. DR GO; GO:0016049; P:cell growth; IMP. DR GO; GO:0001700; P:embryonic development (sensu Insecta); IEP. DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA. DR GO; GO:0030307; P:positive regulation of cell growth; NAS. DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP. DR GO; GO:0045793; P:positive regulation of cell size; NAS. DR GO; GO:0046622; P:positive regulation of organ size; NAS. DR InterPro; IPR000494; EGFR_L_domain. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003961; FN_III. DR InterPro; IPR006211; Furin-like. DR InterPro; IPR006212; Furin_repeat. DR InterPro; IPR009030; Grow_fac_recep. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002011; RecepttyrkinsII. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00757; Furin-like; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF01030; Recep_L_domain; 2. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00060; FN3; 2. DR SMART; SM00261; FU; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Tyrosine-protein kinase; Receptor; Transmembrane; KW Glycoprotein; ATP-binding; Phosphorylation; Signal. FT SIGNAL 1 ? POTENTIAL. FT CHAIN ? 2146 INSULIN-LIKE RECEPTOR. FT CHAIN 651 1077 ALPHA-SUBUNIT. FT CHAIN 1082 2146 BETA-SUBUNIT. FT DOMAIN 1082 1307 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1308 1332 POTENTIAL. FT DOMAIN 1333 2146 CYTOPLASMIC (POTENTIAL). FT DOMAIN 1368 1655 PROTEIN KINASE. FT NP_BIND 1374 1382 ATP (BY SIMILARITY). FT BINDING 1402 1402 ATP (BY SIMILARITY). FT ACT_SITE 1516 1516 BY SIMILARITY. FT MOD_RES 1546 1546 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT CARBOHYD 74 74 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 203 203 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 265 265 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 356 356 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 376 376 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 406 406 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 468 468 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 509 509 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 561 561 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 569 569 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 751 751 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 810 810 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 824 824 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 839 839 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 898 898 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 943 943 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1049 1049 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1143 1143 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1214 1214 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1262 1262 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 29 29 T -> ATTAK (IN REF. 2). FT CONFLICT 89 89 D -> V (IN REF. 2). FT CONFLICT 164 164 C -> F (IN REF. 2). FT CONFLICT 470 470 S -> T (IN REF. 2). FT CONFLICT 485 485 S -> R (IN REF. 2). FT CONFLICT 653 660 DSLERARE -> PPPPPPPL (IN REF. 3). FT CONFLICT 679 681 RES -> GER (IN REF. 3). FT CONFLICT 723 727 ISGDP -> LAAI (IN REF. 3). FT CONFLICT 793 793 E -> V (IN REF. 2 AND 3). FT CONFLICT 822 822 S -> M (IN REF. 2 AND 3). FT CONFLICT 864 877 TQLKAVTIHAMIAG -> NSTKSSDDPCDDRW (IN FT REF. 2). FT CONFLICT 932 932 V -> VTEV (IN REF. 2). FT CONFLICT 951 954 NLMA -> KPYGV (IN REF. 2). FT CONFLICT 1157 1157 MISSING (IN REF. 3). FT CONFLICT 1183 1188 LCSDYD -> SAAIIH (IN REF. 3). FT CONFLICT 1220 1229 ATFSLGRHQL -> VRVRWTPPV (IN REF. 2). FT CONFLICT 1260 1279 DFNQTAGYLIKLNEGLYSFR -> RLQPDCRLFNKAQRGPL FT QLQ (IN REF. 3). FT CONFLICT 1297 1300 IKVE -> LIQQ (IN REF. 4). FT CONFLICT 1454 1455 GD -> VE (IN REF. 3). FT CONFLICT 1466 1481 EERDEAMMTYLNRIGV -> PRSGMRPDDVSLIAWM (IN FT REF. 3). FT CONFLICT 1496 1496 M -> V (IN REF. 3). FT CONFLICT 1516 1517 DL -> PF (IN REF. 4). FT CONFLICT 1566 1575 RDGVYSSASD -> QAWCLLLVPVT (IN REF. 4). FT CONFLICT 1588 1595 TLAAQPYQ -> ILSLWRSP (IN REF. 4). FT CONFLICT 1679 1679 N -> H (IN REF. 2 AND 3). FT CONFLICT 1703 1703 T -> S (IN REF. 3). FT CONFLICT 1712 1712 Q -> E (IN REF. 2). FT CONFLICT 1849 1851 FTT -> SAA (IN REF. 2). FT CONFLICT 1884 1884 Y -> F (IN REF. 2). FT CONFLICT 2092 2146 TKRENLLRIPTPESERQEPETDPTCLKRTGCDRRVRQGLHH FT PMDSSEGRRNRYEL -> SQTRKSPTNPNSGIGATGAGNRS FT NLLKENW LRPASTPRPP PPNGFIGREA (IN FT REF. 2). SQ SEQUENCE 2146 AA; 240488 MW; CC83B42654768E9D CRC64; MFNMPRGVTK SKSKRGKIKM ENDMAAAATT TACTLGHICV LCRQEMLLDT CCCRQAVEAV DSPASSEEAY SSSNSSSCQA SSEISAEEDW FLSHDDIVLC RRPKFDEVET TGKKRDVKCS GHQCSNECDD GSTKNNRQQR ENFNIFSNCH NILRTLHSLL LLMCNCGIFN KRRRRQHQQQ HHHHYQHHHQ QHHQQHLQRQ QANVSYTKFL LLLQTLAAAT TRLSLSPKNY KQQQQLQHNQ QLPRATPQQK QQEKDRHKCF HYKHNYSYSP GISLLLFILL ANTLAIQAVV LPAHQQHLLH NDIADGLDKT ALSVSGTQTR WPRSESNPTM RLSQNVKPCK SMDIRNMVSH FNQLENCTVI EGFLLIDLIN DASPLNRSFP KLTEVTDYII IYRVTGLHSL SKIFPNLSVI RGNKLFDGYA LVVYSNFDLM DLGLHKLRSI TRGGVRIEKN HKLCYDRTID WLEILAENES QLVVLTENGK EKECSLSKCP GEIRIEEGHD NTAIEGELNA SCQLHNNRRL CWNSKLCQTK CPEKCRNNCI DEHTCCSQDC LGGCVIDKNG NESCISCRNV SFNNICMDSC PKGYYQFDSR CVTANECITL TKFETNSVYS GIPYNGQCIT HCPTGYQKSE NKRMCEPCPG GKCDKECSSG LIDSLERARE FHGCTIITGT EPLTISIKRE SGAHVMDELK YGLAAVHKIQ SSLMVHLTYG LKSLKFFQSL TEISGDPPMD ADKYALYVLD NRDLDELWGP NQTVFIRKGG VFFHFNPKLC VSTINQLLPM LASKPKFFEK SDEGADSNGN RGSCGTAVLN VTLQSVGANS ASLNVTTKVE IGEPQKPSNA TIVFKDPRAF IGFVFYHMID PYGTQLKAVT IHAMIAGKVS SPEKSGVMVL SNLIPYTNYS YYVRTMAISS ELTNAESDVK NFRTNPGRPS KVVATAISDS KINVTWSYLD NLMALTRYFI KAKLINRPTR NNNRDYCTEP LVKAMENDLP ATTPTKKISD PLAGDCKCVE GSKKTSSQEY DDRKVQAGME FENALQNFIF VPNIRKSKNG SSDKSDGAEG AALDSNAIPN GGATNPSRRR RDVALEPELD DVEGSVLLRH VRSITDDTDA FFEKDDENTY KDEEDLSSNK QFYEVFAKEL PPNQTHFVFE KLRHFTRYAI FVVACREEIP SEKLRDTSFK KSLCSDYDTV FQTTKRKKFA DIVMDLKVDL EHANNTESPA TFSLGRHQLD PNGEIVTYEV AYKLQKPDQV EEKKCIPAAD FNQTAGYLIK LNEGLYSFRV RANSIAGYGD FTEVEHIKVE PPPSYAKVFF WLLGIGLAFL IVSLFGYVCY LHKRKVPSND LHMNTEVNPF YASMQYIPDD WEVLRENIIQ LAPLGQGSFG MVYEGILKSF PPNGVDRECA IKTVNENATD RERTNFLSEA SVMKEFDTYH VVRLLGVCSR GQPALVVMEL MKKGDLKSYL RAHRPEERDE AMMTYLNRIG VTGNVQPPTY GRIYQMAIEI ADGMAYLAAK KFVHRDLAAR NCMVADDLTV KIGDFGMTRD IYETDYYRKG TKGLLPVRWM PPESLRDGVY SSASDVFSFG VVLWEMATLA AQPYQGLSNE QVLRYVIDGG VMERPENCPD FLHKLMQRCW HHRSSARPSF LDIIAYLEPQ CPNSQFKEVS FYHSEAGLQH REKERKERNQ LDAFAAVPLD QDLQDREQQE DATTPLRMGD YQQNSSLDQP PESPIAMVDD QGSHLPFSLP SGFIASSTPD GQTVMATAFQ NIPAAQGDIS ATYVVPDADA LDGDRGYEIY DPSPKCAELP TSRSGSTGGG KLSGEQHLLP RKGRQPTIMS SSMPDDVIGG SSLQPSTAFT TSSNASSHTG RPSLKKTVAD SVRNKANFIN RHLYNHKRTG SNASHKSNAS NAPSTSSNTN LTSHPVAMGN LGTIESGGSG SAGSYTGTPR FYTPSATPGG GSGMAISDNP NYRLLDESIA SEQATILTTS SPNPNYEMMH PPTSLVSTNP NYMPMNETPV QMAGVTISHN PNYQPMQAPL NARQSQSSSD EDNEQEEDDE DEDDDVDDEH VEHIKMERMP LSRPRQRALP SKTQPPRSRS VTKRENLLRI PTPESERQEP ETDPTCLKRT GCDRRVRQGL HHPMDSSEGR RNRYEL // ID INX1_DROME STANDARD; PRT; 362 AA. AC P27716; Q9W3T8; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Innexin Inx1 (Innexin-1) (Protein ogre) (Optic ganglion reduced DE protein). GN OGRE OR INX1 OR L(1)OGRE OR CG3039. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R, and Canton-S; TISSUE=Embryo; RX MEDLINE=91169249; PubMed=1963867; RA Watanabe T., Kankel D.R.; RT "Molecular cloning and analysis of l(1)ogre, a locus of Drosophila RT melanogaster with prominent effects on the postembryonic development RT of the central nervous system."; RL Genetics 126:1033-1044(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: STRUCTURAL COMPONENT OF THE GAP JUNCTIONS. ESSENTIAL FOR CC GENERATION AND/OR MAINTENANCE OF POSTEMBRYONIC NEUROBLASTS AND CC NORMAL DEVELOPMENT OF OPTIC LOBE. CC -!- SUBUNIT: HETEROOLIGOMER OF INX2 AND OGRE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN LARVAL CNS AND IN TISSUES OUTSIDE CC OF THE CNS. CC -!- SIMILARITY: BELONGS TO THE INNEXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61180; CAA43486.1; -. DR EMBL; AE003439; AAF46226.1; -. DR EMBL; BT004911; AAO49164.1; -. DR PIR; S17285; S17285. DR FlyBase; FBgn0004646; ogre. DR InterPro; IPR000990; Innexin. DR Pfam; PF00876; Innexin; 1. DR PRINTS; PR01262; INNEXIN. KW Gap junction; Transmembrane. FT DOMAIN 1 28 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 29 49 POTENTIAL. FT DOMAIN 50 110 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 111 131 POTENTIAL. FT DOMAIN 132 177 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 178 198 POTENTIAL. FT DOMAIN 199 267 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 268 288 POTENTIAL. FT DOMAIN 289 362 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 362 AA; 42582 MW; 267F5E360B67E894 CRC64; MYKLLGSLKS YLKWQDIQTD NAVFRLHNSF TTVLLLTCSL IITATQYVGQ PISCIVNGVP PHVVNTFCWI HSTFTMPDAF RRQVGREVAH PGVANDFGDE DAKKYYTYYQ WVCFVLFFQA MACYTPKFLW NKFEGGLMRM IVMGLNITIC TREEKEAKRD ALLDYLIKHV KRHKLYAIRY WACEFLCCIN IIVQMYLMNR FFDGEFLSYG TNIMKLSDVP QEQRVDPMVY VFPRVTKCTF HKYGPSGSLQ KHDSLCILPL NIVNEKTYVF IWFWFWILLV LLIGLIVFRG CIIFMPKFRP RLLNASNRMI PMEICRSLSR KLDIGDWWLI YMLGRNLDPV IYKDVMSEFA KQVEPSKHDR AK // ID INX2_DROME STANDARD; PRT; 367 AA. AC Q9V427; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Innexin Inx2 (Innexin-2) (Gap junction protein prp33) (Pas-related DE protein 33). GN INX2 OR PRP33 OR CG4590. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SUBUNIT, AND TISSUE SPECIFICITY. RC TISSUE=Head; RX MEDLINE=99282524; PubMed=10352230; RA Curtin K.D., Zhang Z., Wyman R.J.; RT "Drosophila has several genes for gap junction proteins."; RL Gene 232:191-201(1999). RN [2] RP SEQUENCE FROM N.A., SUBUNIT, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=20346970; PubMed=10888681; RA Stebbings L.A., Todman M.G., Phelan P., Bacon J.P., Davies J.A.; RT "Two Drosophila innexins are expressed in overlapping domains and RT cooperate to form gap-junction channels."; RL Mol. Biol. Cell 11:2459-2470(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: STRUCTURAL COMPONENTS OF THE GAP JUNCTIONS. CC -!- SUBUNIT: MONOMER AND HETEROOLIGOMER WITH OGRE OR INX3. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN CEPHALIC FURROW AND EVENLY CC DISTRIBUTED IN STAGE 8 EMBRYOS. REPEATING EPIDERMAL PATTERN CC EMERGES AT STAGE 11, REFINES TO ONE OR TWO CELLS AT EACH SIDE OF CC THE SEGMENT BORDERS BY STAGE 13. EXPRESSED IN FOREGUT AND HINDGUT CC FROM STAGE 11-17, SEGMENTALLY REPEATED TRACHEAL PLACODES AT STAGE CC 14 AND PROVENTRICULUS IN STAGE 16-17. EXPRESSED IN OPTIC LAMINA OF CC THE ADULT CNS. CC -!- SIMILARITY: BELONGS TO THE INNEXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF137269; AAD50378.1; -. DR EMBL; AF172257; AAF87943.1; -. DR EMBL; AE003439; AAF46229.1; -. DR EMBL; AY060368; AAL25407.1; -. DR FlyBase; FBgn0027108; inx2. DR InterPro; IPR000990; Innexin. DR Pfam; PF00876; Innexin; 1. DR PRINTS; PR01262; INNEXIN. KW Gap junction; Transmembrane. FT DOMAIN 1 22 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 23 43 POTENTIAL. FT DOMAIN 44 109 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 110 130 POTENTIAL. FT DOMAIN 131 179 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 180 200 POTENTIAL. FT DOMAIN 201 266 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 267 287 POTENTIAL. FT DOMAIN 288 367 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 367 AA; 42488 MW; 25DA43DF18920B99 CRC64; MFDVFGSVKG LLKIDQVCID NNVFRMHYKA TVIILIAFSL LVTSRQYIGD PIDCIVDEIP LGVMDTYCWI YSTFTVPERL TGITGRDVVQ PGVGSHVEGE DEVKYHKYYQ WVCFVLFFQA ILFYVPRYLW KSWEGGRLKM LVMDLNSPIV NDECKNDRKK ILVDYFIGNL NRHNFYAFRF FVCEALNFVN VIGQIYFVDF FLDGEFSTYG SDVLKFTELE PDERIDPMAR VFPKVTKCTF HKYGPSGSVQ THDGLCVLPL NIVNEKIYVF LWFWFIILSI MSGISLIYRI AVVAGPKLRH LLLRARSRLA ESEEVELVAN KCNIGDWFLL YQLGKNIDPL IYKEVISDLS REMSGDEHSA HKRPFDA // ID INX3_DROME STANDARD; PRT; 395 AA. AC Q9VAS7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Innexin Inx3 (Innexin-3). GN INX3 OR CG1448. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SUBUNIT, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=20346970; PubMed=10888681; RA Stebbings L.A., Todman M.G., Phelan P., Bacon J.P., Davies J.A.; RT "Two Drosophila innexins are expressed in overlapping domains and RT cooperate to form gap-junction channels."; RL Mol. Biol. Cell 11:2459-2470(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: STRUCTURAL COMPONENTS OF THE GAP JUNCTIONS. CC -!- SUBUNIT: HETEROOLIGOMER OF INX2 AND INX3. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN ANTERIOR AND VENTRAL REGIONS IN CC STAGE 8 EMBRYOS. REPEATING EPIDERMAL PATTERN EMERGES AT STAGE 11, CC REFINES TO ONE OR TWO CELLS AT EACH SIDE OF THE SEGMENT BORDERS BY CC STAGE 13. EXPRESSED IN FOREGUT AND HINDGUT FROM STAGE 11-17. CC -!- SIMILARITY: BELONGS TO THE INNEXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF172258; AAF87944.1; -. DR EMBL; AE003767; AAF56822.1; -. DR EMBL; AY058643; AAL13872.1; -. DR FlyBase; FBgn0028373; inx3. DR InterPro; IPR000990; Innexin. DR Pfam; PF00876; Innexin; 1. DR PRINTS; PR01262; INNEXIN. KW Gap junction; Transmembrane. FT DOMAIN 1 37 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 38 58 POTENTIAL. FT DOMAIN 59 114 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 115 135 POTENTIAL. FT DOMAIN 136 183 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 184 204 POTENTIAL. FT DOMAIN 205 272 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 273 293 POTENTIAL. FT DOMAIN 294 395 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 395 AA; 45357 MW; 86593F952D9DDC07 CRC64; MAVFGMVSAV SGFIKIRYLL DKAVIDNMVF RCHYRITTAI LFTCCIIVTA NNLIGDPISC INDGAIPMHV INTFCWITYT YTIPGQQHRQ IGTDVAGPGL GNEYGQEKRY HSYYQWVPFV LFFQGLMFYV PHWVWKNMED GKIRMITDGL RGMVSVPDDY RRDRQDRILK YFVNSLNTHN GYSFAYFFCE LLNFINVIVN IFMVDKFLGG AFMSYGTDVL KFSNMDQDKR FDPMIEIFPR LTKCTFHKFG PSGSVQKHDT LCVLALNILN EKIYIFLWFW FIILATISGV AVLYSLVVIM MPTTRETIIK RSYRSAQRKE IAGLVRRLEI GDFLILHFLS QNLSTRSYSD MLQQLCGLLG ASRTPSAPST LEMNRISHPI YPPVETFGGG KETET // ID INX4_DROME STANDARD; PRT; 367 AA. AC Q9VRX6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Innexin Inx4 (Innexin-4) (Zero population growth protein). GN ZPG OR INX4 OR CG10125. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Ovary; RX MEDLINE=21959302; PubMed=11960713; RA Stebbings L.A., Todman M.G., Phillips R., Greer C.E., Tam J., RA Phelan P., Jacobs K., Bacon J.P., Davies J.A.; RT "Gap junctions in Drosophila: developmental expression of the entire RT innexin gene family."; RL Mech. Dev. 113:197-205(2002). RN [2] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Ovary; RX MEDLINE=21969349; PubMed=11973283; RA Tazuke S.I., Schulz C., Gilboa L., Fogarty M., Mahowald A.P., RA Guichet A., Ephrussi A., Wood C.G., Lehmann R., Fuller M.T.; RT "A germline-specific gap junction protein required for survival of RT differentiating early germ cells."; RL Development 129:2529-2539(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: STRUCTURAL COMPONENT OF THE GAP JUNCTIONS IN GERM LINE CC CELLS. REQUIRED FOR DIFFERENTIATION AND SURVIVAL OF GERMLINE CYSTS CC IN FEMALES AND OF SPERMATOGONIA IN MALES; GAP JUNCTIONAL CC COMMUNICATION BETWEEN SPERMATOGONIA AND SOMATIC CYST CELLS MAY BE CC REQUIRED FOR NORMAL DIFFERENTIATION AND SURVIVAL OF SPERMATOGONIA. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN; CONCENTRATED AT CC THE INTERFACE BETWEEN GERMLINE AND SOMATIC SUPPORT CELLS IN CC SPERMATOGONIA, EARLY SPERMATOCYTES AND GERM CELLS IN THE OVARY. CC -!- TISSUE SPECIFICITY: EXPRESSED IN NURSE CELLS AND OOCYTE DURING CC OOGENESIS. UNIFORM EXPRESSION IN IMAGINAL WING DISK AND LOW CC EXPRESSION IN DEVELOPING IMAGINAL CNS. EXPRESSED IN EMBRYONIC POLE CC CELLS AND PRIMORDIAL GERM CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC FIRST SEEN AT THE EMBRYONIC SYNCITIAL BLASTODERM STAGE. CC -!- SIMILARITY: BELONGS TO THE INNEXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF271718; AAL36976.1; -. DR EMBL; AE003562; AAF50655.1; -. DR EMBL; AY094856; AAM11209.1; -. DR FlyBase; FBgn0024177; zpg. DR GO; GO:0007281; P:germ-cell development; IMP. DR InterPro; IPR000990; Innexin. DR Pfam; PF00876; Innexin; 1. DR PRINTS; PR01262; INNEXIN. KW Gap junction; Transmembrane. FT DOMAIN 1 21 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 22 42 POTENTIAL. FT DOMAIN 43 110 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 111 131 POTENTIAL. FT DOMAIN 132 186 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 187 207 POTENTIAL. FT DOMAIN 208 268 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 269 289 POTENTIAL. FT DOMAIN 290 367 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 367 AA; 42784 MW; B984A4035DA7CF3E CRC64; MYAAVKPLSK YLQFKSVHIY DAIFTLHSKV TVALLLACTF LLSSKQYFGD PIQCFGDKDM DYVHAFCWIY GAYVSDNVTV TPLRNGAAQC RPDAVSKVVP PENRNYITYY QWVVLVLLLE SFVFYMPAFL WKIWEGGRLK HLCDDFHKMA VCKDKSRTHL RVLVNYFSSD YKETHFRYFV SYVFCEILNL SISILNFLLL DVFFGGFWGR YRNALLSLYN GDYNQWNIIT MAVFPKCAKC EMYKGGPSGS SNIYDYLCLL PLNILNEKIF AFLWIWFILV AMLISLKFLY RLATVLYPGM RLQLLRARAR FMPKKHLQVA LRNCSFGDWF VLMRVGNNIS PELFRKLLEE LYEAQSLIKI PPGADKI // ID INX5_DROME STANDARD; PRT; 428 AA. AC Q9VWL5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable innexin inx5. GN INX5 OR CG7537. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: STRUCTURAL COMPONENT OF THE GAP JUNCTIONS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE INNEXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003511; AAF48923.1; -. DR FlyBase; FBgn0030989; inx5. DR InterPro; IPR000990; Innexin. DR Pfam; PF00876; Innexin; 1. DR PRINTS; PR01262; INNEXIN. KW Hypothetical protein; Gap junction; Transmembrane. FT DOMAIN 1 21 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 22 42 POTENTIAL. FT DOMAIN 43 162 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 163 183 POTENTIAL. FT DOMAIN 184 248 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 249 269 POTENTIAL. FT DOMAIN 270 329 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 330 350 POTENTIAL. FT DOMAIN 351 428 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 428 AA; 50064 MW; 99BA3DDB31528FB4 CRC64; MFSAVKPLSK YLQFKSIRIY DSVFTIHSRC TVVILLTCSL LLSARQYFGD PIQCISEEKN IEYIQSYCWT MGTYILKLDD FGDQEQALVS PNQEVSYNSA FFSSATTNAP QSSSRVRTRP HFRSSLRRIG EYNEAYARSL SIAEGVGPEI RGQTERQYLR YYQWVIILLL FQSFVFYFPS CLWKVWEGRR LKQLCSEVGD ALLSEETYNT RLRMLVKYFT TDYEDMHFCY MAKYVFCEVL NFLISVSRFV NVKRVVNIIV LEVFLNGFWS KYLRALATIP FYDWDRWNRV SSSVFPKIAK CEVLKFGGSG TANVMDNLCI LPLNILNEKI FVFLWAWFLL MALMSGLNLL CRLAMICSRY LREQMIRSQL RFMTKRHVKR ALRDLTIGDW FLMMKVSVNV NPMLFRDLMQ ELCELRTSAS GSTLESPV // ID INX6_DROME STANDARD; PRT; 481 AA. AC Q9VR82; Q9UA15; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Innexin Inx6 (Innexin-6) (Gap junction protein prp6) (Pas-related DE protein 6). GN INX6 OR PRP6 OR CG17063. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 228-431 FROM N.A. RC TISSUE=Head; RX MEDLINE=99282524; PubMed=10352230; RA Curtin K.D., Zhang Z., Wyman R.J.; RT "Drosophila has several genes for gap junction proteins."; RL Gene 232:191-201(1999). CC -!- FUNCTION: STRUCTURAL COMPONENTS OF THE GAP JUNCTIONS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE INNEXIN FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 240. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003572; AAF50922.1; -. DR EMBL; AF137271; AAD50380.1; ALT_FRAME. DR FlyBase; FBgn0027107; inx6. DR InterPro; IPR000990; Innexin. DR Pfam; PF00876; Innexin; 1. DR PRINTS; PR01262; INNEXIN. KW Gap junction; Transmembrane. FT DOMAIN 1 21 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 22 42 POTENTIAL. FT DOMAIN 43 144 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 145 165 POTENTIAL. FT DOMAIN 166 220 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 221 241 POTENTIAL. FT DOMAIN 242 302 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 303 323 POTENTIAL. FT DOMAIN 324 481 CYTOPLASMIC (POTENTIAL). FT CONFLICT 418 418 S -> T (IN REF. 2). FT CONFLICT 431 431 S -> R (IN REF. 2). SQ SEQUENCE 481 AA; 55661 MW; A435A51566B83013 CRC64; MYAAVKPLSN YLRLKTVRIY DPIFTLHSKC TIVILLTCTF LLSAKQYFGE PILCLSSERQ ADYVQSYCWT MGTYILPAEV DRDGGSSWEY ALYAPTSTAA ETFNVSSLRA LVAQNEQYAR FISIAEGVGP ETRGVTKRMY LRYYQWVFMI LLFQSLLFYF PSFLWKVWEG QRMEQLCCEV GDALIVEATY RTRLQMLTRY FRAQFAPIHW CYSIKYAFCE LLNVFISILN FWLMDVVFNG FWYKYIHALA AIPVYDWNLW NLMTSRVFPK VAKCEMFVYG PSGTPNIMDI LCVLPLNILN EKIFAVLYVW FLFIALLAIM NILYRLLVIC CPELRLQLLR THLNGMPKSH VREVLASAGY GDWFVLMCVS INVNPTLFRE LLEQLYAKLN QARCTEPVFA EQPCQQVPQL AQVPQLFSHA KLDRCPSRNC SLLIDPTADR HSICTESSHR VTAMPTAPTL NLMAPNDEII SMDRFFHESH A // ID INX7_DROME STANDARD; PRT; 438 AA. AC Q9V3W6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Innexin Inx7 (Innexin-7) (Gap junction protein prp7) (Pas-related DE protein 7). GN INX7 OR PRP7 OR CG2977. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC TISSUE=Head; RX MEDLINE=99282524; PubMed=10352230; RA Curtin K.D., Zhang Z., Wyman R.J.; RT "Drosophila has several genes for gap junction proteins."; RL Gene 232:191-201(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: STRUCTURAL COMPONENTS OF THE GAP JUNCTIONS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED AROUND GUT LOBES IN EMBRYONIC STAGES CC 15-17. CC -!- SIMILARITY: BELONGS TO THE INNEXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF137270; AAD50379.1; -. DR EMBL; AE003439; AAF46228.1; -. DR FlyBase; FBgn0027106; inx7. DR InterPro; IPR000990; Innexin. DR Pfam; PF00876; Innexin; 1. DR PRINTS; PR01262; INNEXIN. KW Gap junction; Transmembrane. FT DOMAIN 1 23 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 24 44 POTENTIAL. FT DOMAIN 45 58 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 59 79 POTENTIAL. FT DOMAIN 80 112 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 113 133 POTENTIAL. FT DOMAIN 134 283 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 284 304 POTENTIAL. FT DOMAIN 305 438 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 438 AA; 50669 MW; 4FC84B0FE8ED7705 CRC64; MLNTFSSVRQ YLKFDLTRVV IDNIVFKLHY RWTFVILLVA TLLITSRQYI GEHIQCLSDG VVSPVINTFC FFTPTFTVVR DQNQTAYRPG SEPPGIGAFD PEKDTIKRHA YYQWVPFVLF FQALCFYIPH ALWKSWEGGR IKALVFGLRM VGLTRYLKND SLRIGKLNIP SMAEAEERVK DIRRTMIDRM RLNQSWGAHL VFAEVLNLIN LLLQITWTNR FLGGQFLTLG PHALKNRWSD ELSVLDLVFP KITKCKFHKF GDSGSIQMHD ALCVMALNIM NEKIYIILWF WYAFLLIVTV LGLLWRILTL CFYRNVTFTR WSLYWAKPGQ LDENELLAVI DKCNFSNWMF LFFLRSNLSE FLFKKVIYHL ASEFPNPDHD NDVNAYREAP PTPAKNRYPE LSGLDTIDSP LLHLRRNGSP SAGGAQGPST SDMAKLPV // ID IP3R_DROME STANDARD; PRT; 2834 AA. AC P29993; Q24309; Q9U981; Q9VNC8; DT 01-APR-1993 (Rel. 25, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Inositol 1,4,5-trisphosphate receptor (InsP3 receptor) (InsP3R). GN ITP-R83A OR INSP3R OR ITPR OR DIP OR CG1063. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM HEAD). RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=92355637; PubMed=1322910; RA Yoshikawa S., Tanimura T., Miyawaki A., Nakamura M., Yuzaki M., RA Furuichi T., Mikoshiba K.; RT "Molecular cloning and characterization of the inositol 1,4,5- RT trisphosphate receptor in Drosophila melanogaster."; RL J. Biol. Chem. 267:16613-16619(1992). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=99307166; PubMed=10375644; RA Sinha M., Hasan G.; RT "Sequencing and exon mapping of the inositol 1,4,5-trisphosphate RT receptor cDNA from Drosophila embryos suggests the presence of RT differentially regulated forms of RNA and protein."; RL Gene 233:271-276(1999). RN [3] RP SEQUENCE FROM N.A. (ISOFORM HEAD). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 2369-2834 FROM N.A., TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC TISSUE=Brain; RX MEDLINE=93202018; PubMed=1338312; RA Hasan G., Rosbash M.; RT "Drosophila homologs of two mammalian intracellular Ca(2+)-release RT channels: identification and expression patterns of the inositol RT 1,4,5-triphosphate and the ryanodine receptor genes."; RL Development 116:967-975(1992). CC -!- FUNCTION: RECEPTOR FOR INOSITOL 1,4,5-TRISPHOSPHATE, A SECOND CC MESSENGER THAT MEDIATES THE RELEASE OF INTRACELLULAR CALCIUM. CC INSP3R MAY BE INVOLVED IN VISUAL AND OLFACTORY TRANSDUCTION, AND CC MYOBLAST PROLIFERATION. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Head; CC IsoId=P29993-1; Sequence=Displayed; CC Name=2; Synonyms=Embryo; CC IsoId=P29993-2; Sequence=VSP_002703, VSP_002704; CC -!- TISSUE SPECIFICITY: SEGMENTAL EXPRESSION OF HEAD ISOFORM IS FIRST CC DETECTED IN STAGE 13 EMBRYOS IN LATERAL AND POSTERIOR EPIDERMIS. CC EXPRESSION EXTENDS TO HEAD REGION DURING STAGES 13-17: GNATHAL CC BUDS, CLYPEOLABRUM, PROCEPHALIC LOBE, LABIAL ORGAN AND ANTERIOR CC SENSE ORGANS. ADULTS EXHIBIT HIGH EXPRESSION IN ANTENNA AND LOWER CC EXPRESSION IN RETINA, HEAD, LEGS AND THORAX. CC -!- DEVELOPMENTAL STAGE: EMBRYO ISOFORM IS EXPRESSED ONLY IN EARLY CC EMBRYOS. HEAD ISOFORM IS EXPRESSED FROM MID-LATE EMBRYOS TO CC ADULTS. PREDOMINANT EXPRESSION IS IN THE ADULT. CC -!- DOMAIN: THE RECEPTOR CONTAINS A CALCIUM CHANNEL IN ITS C-TERMINAL CC EXTREMITY. ITS LARGE N-TERMINAL CYTOPLASMIC REGION HAS THE LIGAND- CC BINDING SITE IN THE N-TERMINUS AND MODULATORY SITES IN THE MIDDLE CC PORTION IMMEDIATELY UPSTREAM OF THE CHANNEL REGION. CC -!- SIMILARITY: BELONGS TO THE INSP3 RECEPTOR FAMILY. CC -!- SIMILARITY: CONTAINS 5 MIR DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D90403; BAA14399.1; -. DR EMBL; AJ238949; CAB51853.1; -. DR EMBL; AE003602; AAF52015.1; -. DR EMBL; Z18535; CAA79220.1; -. DR PIR; A43360; A43360. DR FlyBase; FBgn0010051; Itp-r83A. DR GO; GO:0008095; F:inositol-1,4,5-triphosphate receptor activity; IDA. DR GO; GO:0007591; P:molting cycle (sensu Insecta); IGI. DR GO; GO:0006979; P:response to oxidative stress; IMP. DR InterPro; IPR000699; Ca-rel_channel. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR000493; InsP3_receptor. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR003608; MIR. DR Pfam; PF00520; ion_trans; 1. DR Pfam; PF02815; MIR; 4. DR Pfam; PF01365; RYDR_ITPR; 2. DR PRINTS; PR00779; INSP3RECEPTR. DR SMART; SM00472; MIR; 2. DR PROSITE; PS50919; MIR; 5. KW Receptor; Transmembrane; Phosphorylation; Endoplasmic reticulum; KW Ionic channel; Ion transport; Calcium channel; Vision; Olfaction; KW Developmental protein; Alternative splicing; Repeat. FT DOMAIN 1 2365 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 2366 2386 POTENTIAL. FT DOMAIN 2387 2397 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2398 2418 POTENTIAL. FT DOMAIN 2419 2433 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 2434 2454 POTENTIAL. FT DOMAIN 2455 2488 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2489 2509 POTENTIAL. FT DOMAIN 2510 2528 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 2529 2549 POTENTIAL. FT DOMAIN 2550 2656 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2657 2677 POTENTIAL. FT DOMAIN 2678 2834 CYTOPLASMIC (POTENTIAL). FT DOMAIN 115 170 MIR 1. FT DOMAIN 178 230 MIR 2. FT DOMAIN 238 294 MIR 3. FT DOMAIN 301 360 MIR 4. FT DOMAIN 399 455 MIR 5. FT VARSPLIC 981 989 Missing (in isoform 2). FT /FTId=VSP_002703. FT VARSPLIC 1393 1395 VHF -> GVGHSV (in isoform 2). FT /FTId=VSP_002704. FT CONFLICT 183 183 MISSING (IN REF. 3). FT CONFLICT 551 551 E -> Q (IN REF. 3). FT CONFLICT 726 726 P -> A (IN REF. 3). FT CONFLICT 1079 1119 PLRPLAMRQVSSSRNNRNRRRLAAPMRLIPSTVPSLWPPRC FT -> AASAASNEASQQQSQQQEPQTPGSSNETDPLDSAESVA FT AGAA (IN REF. 3). FT CONFLICT 1149 1151 SDA -> TP (IN REF. 1). FT CONFLICT 1393 1393 V -> VQ (IN REF. 3). FT CONFLICT 1417 1417 A -> R (IN REF. 3). FT CONFLICT 1464 1464 G -> R (IN REF. 3). FT CONFLICT 2106 2106 L -> V (IN REF. 3). FT CONFLICT 2331 2331 L -> V (IN REF. 3). FT CONFLICT 2481 2493 STYTALYSVLLLR -> QLLYHCIYIAFCFCG (IN REF. FT 3 AND 4). FT CONFLICT 2798 2798 N -> F (IN REF. 1). SQ SEQUENCE 2834 AA; 319316 MW; 8D54D14C55B90993 CRC64; MGDNIIGSAS FLHLGDIVSL YAEGSVCGFL STLGLVDDRT VVCPEAGDLS CPPKKFRDCL IKICPMNRYS AQKQFWKAAK QSASSNTDPN LLKRLHHAAE IEKKQNETEN KKLLGTSIQY GRAVVQLLHL KSNKYLTVNK RLPSLLEKNA MRVYLDANGN EGSWFYIKPF YKLRSIGDYV VVVGDKVILS PVNADQQNLH VAANYELPDN PGCKEVNVLN SSTSWKISLF MEHKENQEHI LKGGDVVRLF HAEQEKFLTM DEYKKQYHVF LRTTGRTSAT AATSSKALWE IEVVQHDSCR GGAGDWNSLY RFKHLATGHY LAAEAEIDVS AGAMSATSAS GHDLHLGDCS KDSGLSCSTM NSTINDKPKG KQYRLVSVPY SADIASVFVL DATTMARPDS LVPQSSYVRL QHICSNTWVH ATSIPIDADD DKPVMSMVCC SPIKEDKEAF ALIPVSPVEV RDLDFANDAC KVLATVTSKL DNGSISINER RALISLLQDI VYFIAGMENE QNKTKALEFT IKNPIRDRQK LLREQYILKQ LFKILQGPFQ EHTAGDGPFL RLDELSDPKN SPYKNIFRLC YRILRLSQQD YRKNQEYIAK HFGLMQKQIG YDILAEDTIT ALLHNNRKLL EKHITAAEIE TFVGLVRKNM HNWDSRFLDY LSDLCVSNRK AIAVTQELIC KSVLSDKNKD ILIETQVKAL RTGSGPVRCY KGNSEDVCLA TLAEDPGDDE DRSDVQSTST TTTWDSASLN EDDGTPSTGD KYEIHLKWTG QPTSRSMADL ASCDGGELEA AILNYYRHQL NLFSNMCLNR QYLALNELSP RLDIDLILKC MSDETMPYEL RASFCRLMLH LHVDRDPQEP VTPVKYARLW SEIPSKMSIQ DYDGKNQQPD QNKQACRAKF NTTIAFVENY LCNVATKVWL FTDQEQNKLT FEVVKLARDL IYFGFYSFSD LLRLTKTLLS ILDCVSDTSS GEFASTDIDS VEEETNAEAE GGVLRSIGDI NTVMTSLALG SVGQAIAAPT ISLQQRKSVS QLMKEYPLVM DTKLKIIEIL QFILDVRLDY RISCLLSIFK REFDESEVPL RPLAMRQVSS SRNNRNRRRL AAPMRLIPST VPSLWPPRCA AAATTARQKN IDLESIGVQA EGIFDCERSD AANLDLDGQG GRTFLRVLLH LIMHDYAPLV SGALHLLFRH FSQRQEVLQA FRQVQLLVSD SDVESYKQIK SDLDILRQSV EKSELWVYKA KATDELGATD AGGDAVSLEY NAALSQEQRN EYRKVKEILI RMNKFCVTAS GPGSVVKPRK HEQRLLRNVG VHTVVLDLLQ NPYDEKDDEL MKELMCLAHE FLQNFCLGNQ QNQVLLHNHL DLFLNPGILE AKTVCAIFKD NLALCNEVTD KVVHFVHCIE IHGRHVAYLQ FLQTVVAAEN QFIRRCQDMV MQELINSGED VLVFYNDKGS FNHFVQMMQQ QMLGMEKLSD DSPLKYHVEL VKLLACCTMG KNVYTEIKCN NLLSLDDIVT IICHPLCMPE VKEAYVDFLN HCYIDTEVEM KEIYASGHMW SLFEKSFLVD INQLITNPAA ASNKTLQAYV LNGVTNLLGS FFASPFSDQS AIVQSRQLIF VQLLQAAHRI TQCRWLSLGD RFNVENCIRT LTESAKMRSI ALPPELEQQV ATMSSKTAML TRQTTKWLLA SKQPKYEAQQ AASLMRWDRS IIEGLQDIVS LLEDQLKPVV EAELSLLVDI LYRSELLFPA GTEARKRCES GGFIRKLIKH TEKLLEEKEE RMCVKVLRTL REMMAIDVNY GEKGDALRQT LLLRYFQTKS TPRLPEDEVP LLAAPLMDPA KQNHLVTHGP GAKYLQRAGK TLHEMQNHLD REGASDLVVE LVIKSVHSPN IFVEAVELGI ALLEGGNPII QKGMFQKFLS DDLNQAFFKV FFEKMKDAQQ EIKSTVTVNT TDIAAKAHEH KQDTNLELDK IARKHGLKSN GVVITEELKR ELHNAGLATA RAYGNARNIH SGEESSAISV NSPLEDILAE KLEKHKDSRD QRNQLSNKVL VMQPILRFLQ LLCENHNPDM QNLLRNQNNK TNNNLVSETL MFLDCICGST TGGLGLLGLY INEHNLALIN QTLEALTEYC QGPCHENQNC IATHESNGLD IITALILNNI NPLGENRMDL VLELKNNASK LLLAIMESRG DSENAERILY NMNPKQLVEV ACKAYHQEEL IDEQDDGDEP DAGSDDDDAT VSPREVGHNI YILCHQLAQH NKELAGLLKA SEDPQSASFD AKTSQALMYY ATHTAQIEIV RNDRTLEQIV FPIPEICEYL TTDTKIKILN TAERDDQGSK LADFFDKAEE MFNEMKWQKK LRSQPLLFWI SSYMSLWSNI LFNCVVVINM IVAFFYPFDN TVPELSSHIS LLFWIITIFS LVIVLALPRE SGIRTFIGSV ILRFIFLLGP ESTLCLLGVV TVTLKSVHIV SIMGNKGTLE KQLIKIITDF STYTALYSVL LLRLIFHPFF YSLLLFDVVY REETLVNVIR SVTRNGRSIV LTAVLALILV YLFSIIGYMF FKDDFLVSVD FEEQDNAPPP SVPLTLSVPV SGDSCSAPDD LGNCQAAKEV APPSAGGGEV KERSCDSLVM CIVTTLNQGL RNGGGIGDIL RAPSSKEGLF VARVIYDLLF FFIVIIIVLN LIFGVIIDTF ADLRSEKQQK EAILKTTCFI CSLNRSAFDN KTVSFEEHIK SEHNMWHYLY FIVLVKVKDP TEFTGPESYV YAMVKAGILE WFPRLRAMSL AAVDADGEQI ELRSMQAQLL DTQLLIKNLS TQLHELKDHM TEQRKQKQRL GLLNTTANSL LPFQ // ID IPOU_DROME STANDARD; PRT; 394 AA. AC P24350; O77214; Q26465; DT 01-MAR-1992 (Rel. 21, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Inhibitory POU protein (I-POU) (Abnormal chemosensory jump 6 protein). GN IPOU OR ACJ6. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM I-POU). RX MEDLINE=91204052; PubMed=1673230; RA Treacy M.N., He X., Rosenfeld M.G.; RT "I-POU: a POU-domain protein that inhibits neuron-specific gene RT activation."; RL Nature 350:577-584(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORM TI-POU). RC STRAIN=Canton-S; RA Clyne P.J., Certel S., de Bruyne M., Zaslavsky L., Johnson W., RA Carlson J.R.; RT "The odor-specificities of a subset of olfactory receptor neurons are RT governed by Acj6, a POU domain transcription factor."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 318-375 FROM N.A. (ISOFORM TI-POU). RX MEDLINE=92154665; PubMed=1346754; RA Treacy M.N., Neilson L.I., Turner E.E., He X., Rosenfeld M.G.; RT "Twin of I-POU: a two amino acid difference in the I-POU homeodomain RT distinguishes an activator from an inhibitor of transcription."; RL Cell 68:491-505(1992). RN [4] RP DNA-BINDING. RX MEDLINE=97140288; PubMed=8986770; RA Turner E.E.; RT "Similar DNA recognition properties of alternatively spliced RT Drosophila POU factors."; RL Proc. Natl. Acad. Sci. U.S.A. 93:15097-15101(1996). CC -!- FUNCTION: MODULATES GENE TRANSCRIPTION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=I-POU; CC IsoId=P24350-1; Sequence=Displayed; CC Name=TI-POU; Synonyms=Twin-of-I-POU; CC IsoId=P24350-2; Sequence=VSP_002342; CC -!- TISSUE SPECIFICITY: EXPRESSED EXCLUSIVELY IN THE CENTRAL NERVOUS CC SYSTEM. CC -!- SIMILARITY: BELONGS TO THE POU TRANSCRIPTION FACTOR FAMILY. CC CLASS-4 SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT THAT I-POU HOMEOBOX IS CC UNABLE TO BIND DNA BECAUSE IT LACKS TWO N-TERMINAL BASIC RESIDUES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58436; CAA41342.1; -. DR EMBL; AF086816; AAC35369.1; -. DR EMBL; S82271; AAB21441.1; -. DR EMBL; S82267; AAB21441.1; JOINED. DR PIR; S14795; S14795. DR HSSP; P10037; 1AU7. DR TRANSFAC; T01898; -. DR FlyBase; FBgn0000028; acj6. DR GO; GO:0003714; F:transcription co-repressor activity; IGI. DR GO; GO:0008039; P:synaptic target recognition; IMP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000327; POU_domain. DR InterPro; IPR007103; POU_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00157; pou; 1. DR PRINTS; PR00028; POUDOMAIN. DR ProDom; PD000010; Homeobox; 1. DR ProDom; PD000583; POU_domain; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00352; POU; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00035; POU_1; 1. DR PROSITE; PS00465; POU_2; 1. KW Homeobox; Transcription regulation; Nuclear protein; DNA-binding; KW Alternative splicing. FT DOMAIN 86 95 POU-IV BOX. FT DOMAIN 226 299 POU. FT DNA_BIND 320 377 HOMEOBOX (TRUNCATED). FT VARSPLIC 322 322 R -> RKR (in isoform TI-POU). FT /FTId=VSP_002342. FT CONFLICT 54 72 MISSING (IN REF. 1). FT CONFLICT 127 216 QRPLQENPFSRQMHHSMDQLDMLDPTGSMTTLAPISESPLT FT PTHQHLHGSYHSMNHMMSHHHPGTLSGHTGGHHGHSAVHHP FT VITAAVAA -> HASVADAPLDGPTGHAGSDGLDDHTGAHL FT GVARNAHTPTPARFLSQHESHDEPPPSGHVKWPHGGTSWTL FT GGTSSCYHRSGS (IN REF. 1). FT CONFLICT 266 266 L -> V (IN REF. 1). SQ SEQUENCE 394 AA; 43419 MW; 069CC77EB0721CD5 CRC64; MTMSMYSTTD KMKMSAPSCF PGRYSPSYRS SEQMRRCMPN PSIHISSSCD SLESRLLEDA SLLCNSWSAR QNGDIFAGIN DGILSRAEAL AAVDIQKHQA QHVHSQMPSQ IKHDVMYHHH SMSGPPQRPL QENPFSRQMH HSMDQLDMLD PTGSMTTLAP ISESPLTPTH QHLHGSYHSM NHMMSHHHPG TLSGHTGGHH GHSAVHHPVI TAAVAAAGLH PDTDTDPREL EAFAERFKQR RIKLGVTQAD VGKALANLKL PGVGALSQST ICRFESLTLS HNNMIALKPI LQAWLEEAEA QAKNKRRDPD APSVLPAGEK KRTSIAAPEK RSLEAYFAVQ PRPSGEKIAA IAEKLDLKKN VVRVWFCNQR QKQKRIVSSV TPSMTGHGSA GFGY // ID IPYR_DROME STANDARD; PRT; 290 AA. AC O77460; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho- DE hydrolase) (PPase) (Nucleosome remodeling factor 38 kDa subunit). GN NURF-38. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., PARTIAL SEQUENCE, AND MUTAGENESIS OF ARG-81. RX MEDLINE=99003073; PubMed=9784495; RA Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C.; RT "Inorganic pyrophosphatase is a component of the Drosophila nucleosome RT remodeling factor complex."; RL Genes Dev. 12:3206-3216(1998). CC -!- FUNCTION: COMPONENT OF THE NUCLEOSOME REMODELING FACTOR COMPLEX CC (NURF), A PROTEIN COMPLEX THAT FACILITATES THE PERTURBATION OF CC CHROMATIN STRUCTURE IN VITRO IN AN ATP-DEPENDENT MANNER. NURF-38 CC MAY HAVE ADAPTED TO DELIVER PYROPHOSPHATASE TO CHROMATIN TO ASSIST CC IN REPLICATION OR TRANSCRIPTION BY EFFICIENT REMOVAL OF THE CC INHIBITORY METABOLITE. CC -!- CATALYTIC ACTIVITY: DIPHOSPHATE + H(2)O = 2 PHOSPHATE. CC -!- COFACTOR: BINDS 4 MAGNESIUM IONS PER SUBUNIT. OTHER METAL IONS CAN CC SUPPORT ACTIVITY, BUT AT A LOWER RATE. TWO MAGNESIUM IONS ARE CC REQUIRED FOR THE ACTIVATION OF THE ENZYME AND ARE PRESENT BEFORE CC SUBSTRATE BINDS, TWO ADDITIONAL MAGNESIUM IONS FORM COMPLEXES WITH CC SUBSTRATE AND PRODUCT (BY SIMILARITY). CC -!- SUBUNIT: NURF IS COMPOSED OF FOUR SUBUNITS; A 215 KDA PROTEIN, CC IMITATION SWITCH (ISWI), NURF-55, AND NURF-38. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- MISCELLANEOUS: THE ATPASE ACTIVITY OF NURF IS STIMULATED BY THE CC PRESENCE OF NUCLEOSOMES RATHER THAN BY FREE DNA. CC -!- SIMILARITY: BELONGS TO THE PPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF085600; AAC97111.1; -. DR EMBL; AF085601; AAC97112.1; -. DR HSSP; P00817; 1WGI. DR FlyBase; FBgn0016687; Nurf-38. DR GO; GO:0004427; F:inorganic diphosphatase activity; NAS. DR InterPro; IPR008162; Pyrophosphatase. DR Pfam; PF00719; Pyrophosphatase; 1. DR PROSITE; PS00387; PPASE; 1. KW Hydrolase; Metal-binding; Magnesium; Nuclear protein. FT METAL 118 118 MAGNESIUM 1 (BY SIMILARITY). FT METAL 123 123 MAGNESIUM 1 AND 2 (BY SIMILARITY). FT METAL 155 155 MAGNESIUM 1 (BY SIMILARITY). FT BINDING 81 81 INORGANIC PYROPHOSPHATE (BY SIMILARITY). FT MUTAGEN 81 81 R->A: DRASTIC REDUCTION OF ACTIVITY. SQ SEQUENCE 290 AA; 32707 MW; 76216B86875F21C9 CRC64; MALYETVEKG AKNSPSYSLY FKNKCGNVIS PMHDIPLYAN EEKTIYNMVV EVPRWTNAKM EISLKTPMNP IKQDIKKGKL RFVANCFPHK GYIWNYGALP QTWENPDHIE PSTGCKGDND PIDVIEIGYR VAKRGDVLKV KVLGQFALID EGETDWKIIA IDVNDPLASK VNDIADVDQY FPGLLRATVE WFKIYKIPDG KPENQFAFNG DAKNADFANT IIAETHKFWQ NLVHQSPASG SISTTNITNR NSEHVIPKEE AEKILAEAPD GGQVEEVSDT VDTWHFIHLK // ID IRS1_DROME STANDARD; PRT; 968 AA. AC Q9XTN2; Q9U4G2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Insulin receptor substrate-1 (Chico protein) (dIRS). GN CHICO OR IRS OR BCDNA:GH11263 OR CG5686. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=99325502; PubMed=10399915; RA Boehni R., Riesgo-Escovar J., Oldham S.M., Brogiolo W., Stocker H., RA Andruss B.F., Beckingham K., Hafen E.; RT "Autonomous control of cell and organ size by CHICO, a Drosophila RT homolog of vertebrate IRS1-4."; RL Cell 97:865-875(1999). RN [2] RP SEQUENCE FROM N.A., AND FUNCTION. RC TISSUE=Embryo; RX MEDLINE=20390102; PubMed=10801879; RA Poltilove R.M.K., Jacobs A.R., Haft C.R., Xu P., Taylor S.I.; RT "Characterization of Drosophila insulin receptor substrate."; RL J. Biol. Chem. 275:23346-23354(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 551-968 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: MAY MEDIATE THE CONTROL OF VARIOUS CELLULAR PROCESSES BY CC INSULIN-LIKE PEPTIDES. WHEN PHOSPHORYLATED BY THE INSULIN RECEPTOR CC BINDS SPECIFICALLY TO VARIOUS CELLULAR PROTEINS CONTAINING SH2 CC DOMAINS. INVOLVED IN CONTROL OF CELL PROLIFERATION, CELL SIZE, AND CC BODY AND ORGAN GROWTH THROUGHOUT DEVELOPMENT. ALSO HAS A ROLE IN A CC SIGNALING PATHWAY CONTROLLING THE PHYSIOLOGICAL RESPONSE REQUIRED CC TO ENDURE PERIODS OF LOW NUTRIENT CONDITIONS. CC -!- SUBUNIT: BINDINGS TO PHOSPHATIDYLINOSITOL 3-KINASE AND SHP2. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING G1, S AND G2 PHASE OF THE CC CELL CYCLE. CC -!- MISCELLANEOUS: 'CHICO' MEANS 'SMALL BOY' IN SPANISH. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PTB DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF154826; AAD40880.1; -. DR EMBL; AF092046; AAD43005.1; -. DR EMBL; AE003628; AAF52882.1; -. DR EMBL; AF181643; AAD55429.1; ALT_INIT. DR HSSP; P35568; 1IRS. DR FlyBase; FBgn0024248; chico. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IGI. DR GO; GO:0007568; P:aging; IMP. DR GO; GO:0000902; P:cellular morphogenesis; IMP. DR GO; GO:0007295; P:egg chamber growth (sensu Insecta); IMP. DR GO; GO:0008286; P:insulin receptor signaling pathway; IGI. DR GO; GO:0030307; P:positive regulation of cell growth; NAS. DR GO; GO:0045793; P:positive regulation of cell size; NAS. DR GO; GO:0046622; P:positive regulation of organ size; NAS. DR GO; GO:0007296; P:vitellogenesis; IMP. DR InterPro; IPR002404; Insln_receptorS1. DR InterPro; IPR001849; PH. DR Pfam; PF02174; IRS; 1. DR Pfam; PF00169; PH; 1. DR PRINTS; PR00628; INSULINRSI. DR SMART; SM00233; PH; 1. DR SMART; SM00310; PTBI; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. KW Phosphorylation; Growth regulation. FT DOMAIN 8 109 PH. FT DOMAIN 122 234 PTB. FT DOMAIN 855 858 POLY-SER. FT DOMAIN 870 873 POLY-ALA. FT DOMAIN 956 963 POLY-SER. FT MOD_RES 411 411 PHOSPHORYLATION (BY INSR) (By FT similarity). FT MOD_RES 911 911 PHOSPHORYLATION (BY INSR) (By FT similarity). FT MOD_RES 948 948 PHOSPHORYLATION (BY INSR) (By FT similarity). SQ SEQUENCE 968 AA; 107831 MW; 04E9856F37F7A4CF CRC64; MASISDDGMA LSGYLKKLKT MKKKFFVLYE ETSTSAARLE YYDTEKKFLQ RAEPKRVIYL KNCFNINRRL DTKHRFVIVL SSRDGGFGIV LENENDLRKW LDKLLVLQRN IANSNGTAHS PYDHVWQVVI QKKGISEKVG ITGTYHCCLT SKSLTFVCIG PEKTPNGEDR VASIEILLTT IRRCGHASPQ CIFYVELGRQ SVLGSGDLWM ETDNAAIATN MHNTILSAMS AKTESNTNLI NVYQNRPDLS HEPMRKRSSS ANEASKPINV NVIQNSQNSL ELRSCSSPHN YGFGRERCDS LPTRNGTLSE SSNQTYFGSN HGLRSNTISG IRPHSTNKHS NSPTFTMPLR CSESEESSIS VDESDDNGSF SHYRLNTRSS ETAIPEENID DFASAELFSK VTEQNVSDEN YIPMNPVNPT DAIHEKEKAD MQRLEDASLH FNFPEHASEK LAKDFDLDSD NQCCRPIRAY SIGNKVEHLK FNKRLGHLND TGQNPNRVRA YSVGSKSKIP RCDLQRVVLV EDNKHEFTAN RSQSSITKEG TSYGSSANRQ KKSTSAPLLS LKNQINSDRM SDLMEIDFSQ ATNLEKQKFI KNNEIPKYIE NVFPKAPRTD SSSLTLHATS QKDIFNGTKL NNTAITSEDG YLEMKPVGNG YTPSSNCLPM KVEKLKLSDY QTAPPLTATA APVHDLNKIS TYNISAEKWR EQPSRSEEKK SNSPLNDNTF SSKPTNVEST SKSHDVHSAN QIDCEKVCAQ SSDKLNNHLA DKIVENNNLD IGGHEEKKLV HSISSEDYTQ IKDKSNDFTK FNEAGYKILQ IKSDSSLISS KLYQKGIHKD NLERSQRLTE SVNTIPDNAT ATAVSSSSLT KFNINSAKPA AAADSRSTGT DPSTPQNILQ IKDLNFPSRS SSRISQPELH YASLDLPHCS GQNPAKYLKR GSRESPPVSA CPEDGNTYAK IDFDQSDSSS SSSNIFNT // ID ISWI_DROME STANDARD; PRT; 1027 AA. AC Q24368; Q9V6E8; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Iswi protein (Imitation swi protein) (Nucleosome remodeling factor 140 DE kDa subunit) (NURF-140) (CHRAC 140 kDa subunit). GN ISWI OR CG8625. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1; RX MEDLINE=94187693; PubMed=7908117; RA Elfring L.K., Deuring R., McCallum C.M., Peterson C.L., Tamkun J.W.; RT "Identification and characterization of Drosophila relatives of the RT yeast transcriptional activator SNF2/SWI2."; RL Mol. Cell. Biol. 14:2225-2234(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE NUCLEOSOME REMODELING FACTOR COMPLEX CC (NURF), A PROTEIN COMPLEX THAT FACILITATES THE PERTURBATION OF CC CHROMATIN STRUCTURE IN VITRO IN AN ATP-DEPENDENT MANNER. THE CC HYDROLYSIS OF ATP DURING THE REMODELING OF CHROMATIN IS LIKELY TO CC BE MEDIATED BY ISWI, RELEASING INORGANIC PHOSPHATE. IT IS ALSO A CC COMPONENT OF THE ATP-UTILIZING CHROMATIN ASSEMBLY AND REMODELING CC FACTOR (ACF) AND OF THE CHROMATIN ACCESSIBILITY COMPLEX (CHRAC). CC THIS SUBUNIT MAY SERVE AS THE ENERGY-TRANSDUCING COMPONENT OF CC CHROMATIN-REMODELING MACHINES. CC -!- SUBUNIT: NURF IS COMPOSED OF FOUR SUBUNITS; A 215 KDA PROTEIN, CC IMITATION SWITCH (ISWI), NURF-55, AND NURF-38. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE SNF2/RAD54 HELICASE FAMILY. SNF2L CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L27127; AAA19868.1; -. DR EMBL; AE003821; AAM68637.1; -. DR PIR; A56533; A56533. DR FlyBase; FBgn0011604; Iswi. DR GO; GO:0008623; C:chromatin accessibility complex; IDA. DR GO; GO:0005679; C:nucleosome remodeling complex; IDA. DR GO; GO:0008094; F:DNA dependent ATPase activity; IDA. DR GO; GO:0006333; P:chromatin assembly/disassembly; IDA. DR GO; GO:0016584; P:nucleosome spacing; IDA. DR InterPro; IPR001410; DEAD. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR001005; Myb_DNA_binding. DR InterPro; IPR000330; SNF2_N. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00176; SNF2_N; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00717; SANT; 2. KW Nuclear protein; Helicase; ATP-binding. FT NP_BIND 153 160 ATP (POTENTIAL). FT SITE 256 259 DEAH BOX. FT DOMAIN 978 981 POLY-LYS. FT DOMAIN 1023 1027 POLY-LYS. SQ SEQUENCE 1027 AA; 118873 MW; 008FC81AE15E071F CRC64; MSKTDTAAVE ATEENSNETT SDAATSSSGE KEAEFDNKIE ADRSRRFDFL LKQTEIFTHF MTNSAKSPTK PKGRPKKIKD KDKEKDVADH RHRKTEQEED EELLAEDSAT KEIFRFDASP AYIKSGEMRD YQIRGLNWMI SLYENGINGI LADEMGLGKT LQTISLLGYL KHFKNQAGPH IVIVPKSTLQ NWVNEFKKWC PSLRAVCLIG DQDTRNTFIR DVLMPGEWDV CVTSYEMCIR EKSVFKKFNW RYLVIDEAHR IKNEKSKLSE ILREFKTANR LLITGTPLQN NLHELWALLN FLLPDVFNSS EDFDEWFNTN TCLGDDALIT RLHAVLKPFL LRRLKAEVEK RLKPKKEMKI FVGLSKMQRD WYTKVLLKDI DVVNGAGKVE KMRLQNILMQ LRKCTNHPYL FDGAEPGPPY TTDTHLVYNS GKMAILDKLL PKLQEQGSRV LIFSQMTRML DILEDYCHWR NYNYCRLDGQ TPHEDRNRQI QEFNMDNSAK FLFMLSTRAG GLGINLATAD VVIIYDSDWN PQMDLQAMDR AHRIGQKKQV RVFRLITEST VEEKIVERAE VKLRLDKMVI QGGRLVDNRS NQLNKDEMLN IIRFGANQVF SSKETDITDE DIDVILERGE AKTAEQKAAL DSLGESSLRT FTMDTNGEAG TSSVYQFEGE DWREKQKLNA LGNWIEPPKR ERKANYAVDA YFREALRVSE PKAPKAPRPP KQPIVQDFQF FPPRLFELLD QEIYYFRKTV GYKVPKNTEL GSDATKVQRE EQRKIDEAEP LTEEEIQEKE NLLSQGFTAW TKRDFNQFIK ANEKYGRDDI DNIAKDVEGK TPEEVIEYNA VFWERCTELQ DIERIMGQIE RGEGKIQRRL SIKKALDQKM SRYRAPFHQL RLQYGNNKGK NYTEIEDRFL VCMLHKLGFD KENVYEELRA AIRASPQFRF DWFIKSRTAL ELQRRCNTLI TLIERENIEL EEKERAEKKK KAPKGSVSAG SGSASSNTPA PAPQPKASQK RKSEVVATSS NSKKKKK // ID ITA1_DROME STANDARD; PRT; 1146 AA. AC Q24247; Q9VYF6; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Integrin alpha-PS1 precursor (Position-specific antigen 1, alpha DE chain) (Protein multiple edematous wings). GN MEW OR CG1771. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=Oregon-R; RX MEDLINE=94059764; PubMed=8240969; RA Wehrli M., Diantonio A., Fearnley I.M., Smith R.J., Wilcox M.; RT "Cloning and characterization of alpha PS1, a novel Drosophila RT melanogaster integrin."; RL Mech. Dev. 43:21-36(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INTEGRIN ALPHA-PS1/BETA-PS IS A RECEPTOR FOR LAMININ. CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. THE ALPHA CC SUBUNIT IS COMPOSED OF AN HEAVY AND A LIGHT CHAIN LINKED BY A CC DISULFIDE BOND. ALPHA-PS1 ASSOCIATES WITH BETA-PS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE INTEGRIN ALPHA CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 7 FG-GAP REPEATS. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73975; CAA52155.1; -. DR EMBL; AE003491; AAF48242.1; ALT_SEQ. DR PIR; S40311; S40311. DR HSSP; P11215; 1A8X. DR FlyBase; FBgn0004456; mew. DR GO; GO:0004895; F:cell adhesion receptor activity; IMP. DR GO; GO:0007476; P:wing morphogenesis; IEP. DR InterPro; IPR000413; Integrin_alpha. DR Pfam; PF01839; FG-GAP; 3. DR Pfam; PF00357; integrin_A; 1. DR SMART; SM00191; Int_alpha; 5. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. KW Integrin; Cell adhesion; Receptor; Glycoprotein; Transmembrane; KW Signal; Repeat. FT SIGNAL 1 30 POTENTIAL. FT CHAIN 31 1146 INTEGRIN ALPHA-PS1. FT CHAIN 31 ?960 INTEGRIN ALPHA-PS1 HEAVY CHAIN FT (POTENTIAL). FT CHAIN ?961 1146 INTEGRIN ALPHA-PS1 LIGHT CHAIN FT (POTENTIAL). FT DOMAIN 31 1085 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1086 1106 POTENTIAL. FT DOMAIN 1107 1146 CYTOPLASMIC (POTENTIAL). FT REPEAT 49 116 FG-GAP 1. FT REPEAT ? ? FG-GAP 2. FT REPEAT 199 263 FG-GAP 3. FT REPEAT 264 317 FG-GAP 4. FT REPEAT 318 374 FG-GAP 5. FT REPEAT 377 434 FG-GAP 6. FT REPEAT 443 497 FG-GAP 7. FT CARBOHYD 68 68 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 147 147 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 470 470 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 511 511 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 657 657 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 680 680 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 711 711 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 718 718 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 761 761 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 928 928 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1027 1027 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 730 731 ML -> IV (IN REF. 1). FT CONFLICT 815 815 D -> E (IN REF. 1). SQ SEQUENCE 1146 AA; 127973 MW; E8AB75BC8DE6854E CRC64; MLELPFTTIR PNCRLRQNLG ILIILQCVLT CYNFNLEQRL PIVKYGHPHS HFGYSVATHT IGEANGPNKT NCVLVGAPLD QNRQPNTTHS GALWRCPMTQ RFDDCEQVIT DGRRNFDSEI LSPPGNDEIK EDQWMGVTVR SNPLQANGSG GKVIVCAHRY MYIVRENRYG QGLCYLLTND LQFEEVHEPC KGRPVQRQHE DYGLCQAGTS AALLDDDTMV LGSPGPYTWR GSIWVTQVGG EYLQRDKTTY YSDHSDLNSP VDKYSYLGMS VTGGRFFGHM SYAAGAPRSE GHGQVVIFDK STDNPIPVHS ILDGEQFGSS FGYELATADI NGDHRPDLIV AAPLYFTKTE GGAVYVYQNI QDTLPMKYTL KLTGPLESRF GLALANIGDL NKDNCEDLAV GAPYEGNGVV YIYLGSSQGL NSKPAQKIQA SELGGTIPNG QPIRTFGISI SGNTDLDDNS YPDVVIGAFN SSAAVILLAR PIISIQTSVQ RKELHNMDPN TPGCLDDPAS NLTCFTFRAC CSIEPYDEKN KELRLAYSVE AETFDHLKKF SRVFFFDREN KRTNVLSRVV RVHTNGRTEC QAVTGYIKAN TRDIQTPVRF RLKYSLVEPP LADSALVRLN PILDQTQAHV DFEGTFQKDC GDDDLCESNL IIRVEPNITE SSGNEYTLIL DETELEVRIN VSNLADSAYE AQLFIAHQAG VSYVATKKPT NATCNSYNTT LVACSLGNPM LRDTTTFVTI RFQPKGLEPS EKIMLFHIFA NTTSKLVGPE RPERDLRVNV VRRAKLNFRG WAIPEQSFYS GSSVANSVAN TAATDIEGHG PMGMDDVGSQ VHHMFTIFNE GPSTAPKVQM VIHWPYSLYS DPQSGRPVQY LLYLEQVPTV EVSQGECHVA KEYVNPLNLA SGSRENPAYL SAPAQMRMFP SQSRHSFNKS LIHSQRSYYS SSHRDDHSDD TQSNRNRVRR SFLERVTRLE RLMYDPESSN AANGKKQDIV ELDCNKGATN CVRIECDILN MPALSEAQVV VKARLWNSTL VSEYPRVERV RIFSTATAQI PESYGVEVMD HNNIEVETRA YPELRNQQRD TSIPWLIIIL GIVGGLLLLA LVTYVLWKVG FFKRIRPTDP TLSGNLEKMN EEKPFLAPSK NTHHVF // ID ITA2_DROME STANDARD; PRT; 1396 AA. AC P12080; Q9VXB6; DT 01-OCT-1989 (Rel. 12, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Integrin alpha-PS2 precursor (Position-specific antigen 2, alpha DE chain) (Protein inflated). GN IF OR CG9623. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM PS2C). RX MEDLINE=88080480; PubMed=2961459; RA Bogaert T., Brown N.H., Wilcox M.; RT "The Drosophila PS2 antigen is an invertebrate integrin that, like RT the fibronectin receptor, becomes localized to muscle attachments."; RL Cell 51:929-940(1987). RN [2] RP SEQUENCE FROM N.A. (ISOFORM PS2C). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP ALTERNATIVE SPLICING. RX MEDLINE=90003228; PubMed=2507168; RA Brown N.H., King D.L., Wilcox M., Kafatos F.C.; RT "Developmentally regulated alternative splicing of Drosophila integrin RT PS2 alpha transcripts."; RL Cell 59:185-195(1989). RN [4] RP CHARACTERIZATION. RX MEDLINE=98325030; PubMed=9660786; RA Graner M.W., Bunch T.A., Baumgartner S., Kerschen A., Brower D.L.; RT "Splice variants of the Drosophila PS2 integrins differentially RT interact with RGD-containing fragments of the extracellular proteins RT tiggrin, ten-m, and D-laminin 2."; RL J. Biol. Chem. 273:18235-18241(1998). CC -!- FUNCTION: ALPHA-PS2/BETA-PS IS A RECEPTOR FOR TIGGRIN. ALSO BINDS CC TO WING BLISTER AND TEN-M. CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. THE ALPHA CC SUBUNIT IS COMPOSED OF AN HEAVY AND A LIGHT CHAIN LINKED BY A CC DISULFIDE BOND. ALPHA-PS2 ASSOCIATES WITH BETA-PS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=PS2C; CC IsoId=P12080-1; Sequence=Displayed; CC Name=PS2M8; CC IsoId=P12080-2; Sequence=VSP_002739; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: THE RELATIVE RATIO OF ISOFORM 1/PS2C AND CC ISOFORM 2/PS2M8 VARIES WIDELY DURING DEVELOPMENT. CC -!- PTM: THE HEAVY-LIGHT CHAIN CLEAVAGE SITE IS EITHER IN 1230-1231, CC OR 1233-1234, OR 1243-1244. CC -!- SIMILARITY: BELONGS TO THE INTEGRIN ALPHA CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 7 FG-GAP REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19059; AAC12788.1; -. DR EMBL; AE003503; AAF48661.1; -. DR PIR; A29637; A29637. DR HSSP; P11215; 1A8X. DR FlyBase; FBgn0001250; if. DR GO; GO:0030484; C:muscle fiber; IDA. DR GO; GO:0004895; F:cell adhesion receptor activity; IDA. DR GO; GO:0045185; P:maintenance of protein localization; IMP. DR GO; GO:0016203; P:muscle attachment; IMP. DR GO; GO:0030239; P:myofibril assembly; IMP. DR GO; GO:0007476; P:wing morphogenesis; IEP. DR InterPro; IPR000413; Integrin_alpha. DR Pfam; PF01839; FG-GAP; 4. DR Pfam; PF00357; integrin_A; 1. DR SMART; SM00191; Int_alpha; 5. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. KW Integrin; Cell adhesion; Receptor; Glycoprotein; Transmembrane; KW Signal; Repeat; Alternative splicing. FT SIGNAL 1 31 POTENTIAL. FT CHAIN 32 1396 INTEGRIN ALPHA-PS2. FT CHAIN 32 ?1243 INTEGRIN ALPHA-PS2 HEAVY CHAIN. FT CHAIN ?1244 1396 INTEGRIN ALPHA-PS2 LIGHT CHAIN. FT DOMAIN 32 1341 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1342 1366 POTENTIAL. FT DOMAIN 1367 1396 CYTOPLASMIC (POTENTIAL). FT REPEAT 47 115 FG-GAP 1. FT REPEAT 128 180 FG-GAP 2. FT REPEAT 197 255 FG-GAP 3. FT REPEAT 276 327 FG-GAP 4. FT REPEAT 329 397 FG-GAP 5. FT REPEAT 398 457 FG-GAP 6. FT REPEAT 463 517 FG-GAP 7. FT DOMAIN 932 938 SER-RICH. FT DOMAIN 1015 1023 SER-RICH. FT DOMAIN 1049 1054 SER-RICH. FT DOMAIN 1217 1226 SER-RICH. FT CARBOHYD 69 69 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 209 209 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 322 322 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 584 584 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 598 598 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 741 741 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 783 783 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 833 833 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 959 959 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1005 1005 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1299 1299 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1307 1307 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 225 249 Missing (in isoform PS2M8). FT /FTId=VSP_002739. FT CONFLICT 29 29 A -> G (IN REF. 1). FT CONFLICT 968 976 SPKQVEQRR -> RSQASGATA (IN REF. 1). FT CONFLICT 1063 1064 MISSING (IN REF. 1). FT CONFLICT 1235 1235 N -> D (IN REF. 1). FT CONFLICT 1242 1242 E -> K (IN REF. 1). FT CONFLICT 1245 1245 L -> Q (IN REF. 1). SQ SEQUENCE 1396 AA; 154321 MW; 2384B07DDBA28372 CRC64; MSGDSIHRRR MALHCPITSL ILLLIAMSAH GYNIDLPSYV RFRQSSNSMF GFSIAMHKGR SGFYGNQNNV SLIVGAPKFD TSRYQQGVTE AGGVFKCSLN DDDCKLVPFD SKGNNRNVDK EVVDRKSYQW LGATVATGRD SDLVVACAPR YVFHTMTPSR AFRIDPVGTC FTSHNFEEFY EVSPCRTNNW GYHRQGSCQA GFSAAINGNG SRLFIGAPGS WYWQGQTYSI PPDAKFPFKP PLYQPFGTGG MASSHDVTRP ENQVFSTSES ASVNDDSYLG YSMVTGDFDG DRSEDVAIGM PRGGNLVGRI VVNRWNMANI FNITGRQIGE YFGYSLATSD VDGDGLDDLL IGAPMYTDPD NVEGKYDVGR VYILLQGGPT EEKRWTTEHI RDGYHSKGRF GLALTTLGDV NGDGYGDFAV GAPYDGPEGR GVVYIFHGSP MGPLAKPSQI IKSEQLVEGA PYPRTFGFAL SGGLDMDGNT YPDLAVGAYS SDQVFIFKSR PVAAVNAETS FASNSKLISL DDRSCQLVRD HKKVPCMLLT TCWSYTGRYL PEQLDFDVSW LLDAKKLLNP RMFFLRDEGK NIRNQTIRLN YGQKYCLNET VYLLDKVQDK LTPLEVEARY NLRSSRPLDP MVRHRRSILE PVIDQNREIV LRDAINIQKN CGPDNICEPD LKLKVSTVDK YLFGSPEPLV IEVFISNTNE DAFEAAFYMV TPPDLQFRKL QQLGEKKDTP ITCSPPTPEN NHTLKCDIGN PLESGKIAHF KISLVPEEKY GSSSSYDFYW EANSTNLEKP GSEYDNKIRQ SVGIWVDTDL DIKGTSLPDY QLYKADDYKE LENATKEDDI GPQVVHIYEI RNNRPSIIEE AEVFIHLPYE TIVGDPLMYL LNQPETGGKI QCDDVAFNEY NLLLDEKLVK KSYLQAQGAI WNSAQVSGQS SSSSSSGGAS VHIEKARGEG FVRGVLVSNS TDAGDKLSPK QVEQRRQEDT LEALGDASFV HRDRASQAVQ EPQVNQTSFT TYSTSSSSSG SGAPSAQLRG HSTQGHIQMA GPVQHTSSSS SSNYRSWPAQ QQQQHQQLLL AGSGGSGLGS PVTFNDKSQF GGRNNNFHTG TLDLGTLNRG NVDNELYRSQ GQYQNPSQSL GQSQGQFQAN ANQGHYQGQN QAQFQARNPG FQGQTSYQGQ TQYSGQPGGY QTHHVTYSSG SKPYYGRENE DFYDEDNLQQ ATPGHWSSSS SSSSSSGTRR LRRSNDKDGA TEKPLQIDLN SPCQSARCKS IRCVVTNLGT EDGDAAFVAI RARMVAKTME KLASNVPLNV STLAVANVTL LPFIGAPKDA IVKTHEIFYK AEPEPLQVPD VVPLWVVVLA ACAGALIFLL LVWLLYKCGF FNRNRPTDHS QERQPLRNGY HGDEHL // ID ITA3_DROME STANDARD; PRT; 1115 AA. AC O44386; O44387; O46186; Q9V7A3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Integrin alpha-PS3 precursor (Position-specific antigen 3, alpha DE chain) (Scab protein) (Volado protein). GN SCB OR VOL OR CG8095. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=98072333; PubMed=9409675; RA Stark K.A., Yee G.H., Roote C.E., Williams E.L., Zusman S., RA Hynes R.O.; RT "A novel alpha integrin subunit associates with betaPS and functions RT in tissue morphogenesis and movement during Drosophila development."; RL Development 124:4583-4594(1997). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RX MEDLINE=98121110; PubMed=9461212; RA Grotewiel M.S., Beck C.D.O., Wu K.H., Zhu X.R., Davis R.L.; RT "Integrin-mediated short-term memory in Drosophila."; RL Nature 391:455-460(1998). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INTEGRIN ALPHA-PS3/BETA-PS MAY BE A RECEPTOR FOR CC LAMININ. ALSO BINDS TO WING BLISTER. IMPORTANT DURING CC EMBRYOGENESIS FOR THE DEVELOPMENT OF THE TRACHEA, DORSAL VESSEL CC AND SALIVARY GLAND, AS WELL AS FOR DORSAL CLOSURE. CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. THE ALPHA CC SUBUNIT IS COMPOSED OF AN HEAVY AND A LIGHT CHAIN LINKED BY A CC DISULFIDE BOND. ALPHA-PS3 ASSOCIATES WITH BETA-PS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Vol-L; CC IsoId=O44386-1; Sequence=Displayed; CC Name=2; Synonyms=Vol-S; CC IsoId=O44386-2; Sequence=VSP_002740; CC -!- SIMILARITY: BELONGS TO THE INTEGRIN ALPHA CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 7 FG-GAP REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF034199; AAC38853.1; -. DR EMBL; AF034200; AAC38854.1; -. DR EMBL; AE003811; AAF58155.1; -. DR EMBL; U76605; AAC04505.1; -. DR EMBL; AE003811; AAF58156.1; -. DR PIR; T09403; T09403. DR FlyBase; FBgn0003328; scb. DR GO; GO:0008305; C:integrin complex; NAS. DR GO; GO:0004895; F:cell adhesion receptor activity; IPI. DR GO; GO:0005198; F:structural molecule activity; NAS. DR GO; GO:0040011; P:locomotion; NAS. DR GO; GO:0007613; P:memory; NAS. DR GO; GO:0008355; P:olfactory learning; NAS. DR InterPro; IPR000413; Integrin_alpha. DR Pfam; PF01839; FG-GAP; 3. DR SMART; SM00191; Int_alpha; 6. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. KW Integrin; Cell adhesion; Receptor; Glycoprotein; Transmembrane; KW Signal; Repeat; Alternative splicing. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 1115 INTEGRIN ALPHA-PS3. FT CHAIN 25 ?929 INTEGRIN ALPHA-PS3 HEAVY CHAIN FT (POTENTIAL). FT CHAIN ?930 1115 INTEGRIN ALPHA-PS3 LIGHT CHAIN FT (POTENTIAL). FT DOMAIN 25 1054 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1055 1075 POTENTIAL. FT DOMAIN 1076 1115 CYTOPLASMIC (POTENTIAL). FT REPEAT 50 108 FG-GAP 1. FT REPEAT 128 180 FG-GAP 2. FT REPEAT ? ? FG-GAP 3. FT REPEAT ? ? FG-GAP 4. FT REPEAT 347 407 FG-GAP 5. FT REPEAT 408 465 FG-GAP 6. FT REPEAT 471 525 FG-GAP 7. FT CARBOHYD 46 46 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 82 82 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 166 166 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 438 438 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 696 696 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 845 845 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 868 868 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 964 964 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 63 MNAESTMFPHIFLALLALISHIEAFNFMPRPSRVINSPKHL FT KFHINQTRSSYFGYTLVIRQTS -> MVGQDRDFWALLVLG FT LWCLSSHCNAFNLSPLPNRQILDPQFATNVPKVRASYFGFT FT MSLRPNG (in isoform 2). FT /FTId=VSP_002740. FT CONFLICT 630 630 I -> V (IN REF. 2). FT CONFLICT 664 664 D -> N (IN REF. 2). FT CONFLICT 753 753 I -> S (IN REF. 2). FT CONFLICT 792 792 S -> R (IN REF. 2). SQ SEQUENCE 1115 AA; 124544 MW; B3DFB52212E84185 CRC64; MNAESTMFPH IFLALLALIS HIEAFNFMPR PSRVINSPKH LKFHINQTRS SYFGYTLVIR QTSIIVGAPR AQSTLESQRT INETGAIYRC SLTNGVCSPY VLDSRGNVDA PYSEYTFDSE RKDFQWLGGS MDGGTKDTDK LLVCAPRFYA PSSRDNHLHG VCYWVNNTVA STPQHVTRIS PLRLKSEQVK EEDNGNKASF FYIMGELGLS AHVADDNTKF LIGAPGINTW RGSVILYRQV DPVDNPTASR RDTSKALRRT YRDVDSNDYT PEHYAPEIPT PGLWGQEEDS YFGYAVSSGF FDSSNPTKLL YVATAPQANK QSGEAYIFDV RGKSIHKYHV FRGEQFGEYF GYSVLAEDLN GDGKTDVIVS APQHALEDSH DNGAIYVFIN KGFFNFERQI LRSPVETMAR FGTALSRLGD INHDGYNDVA VGAPFAGNGT VFIYLGSENG LRDQPSQRLD APSQQPSKYG SHMFGHGLSR GSDIDGNGFN DFAIGAPNAE AVYLYRAYPV VKVHATVKSE SREIKPEQEK VKITACYRLS TTSTDKLVQE QELAIRIAMD KQLKRVKFTQ TQTNEISFKV NANFGEQCRD FETQVRYSEK DIFTPIDLEM HYELTKKVPD SEEFCETCAI VDPTEPKVST QNIIFSTGCA TDVCTADLQL RSKDVSPTYI LGSADTLRLN YEITNIGETA YLPQFNVTST SRLAFAQVPG NCKVVDAVMV CDLNRGRPLA KGDTDSVTIS FDVSQLSGQS LIIHAEVFST GYEQNPTDNR QTNVIGLKEF TEIDASGGQT NSQIDLEHYS NSAEIVNNYE IKSNGPSVIE QLTVSFYIPI AYKVAGSTAI IPIINVTSLK MQASYDSQLL SIDLYDQNNT MLVVDPVEVT TTLSGGLERT VITQNRQSYD IHTSGHVHQT MEVLDTSMVA TASMSRKRRD LKALTANREQ YARISNVKAH DLLSDDFKGK LPVNRTIVFN CRDPEMTICV RAEMRVHFRP EKSINLNMRY SVDLNEVNAI LVDPWEYFVI LTDLKLQKKG DPTSTSFSIN RRIEPNIISK HQETGLPIWI IIVSVIGGLL LLSAISYLLY KFGFFNRTKK DELDRLVQQN PVEPEAENLN SGGNN // ID ITA4_DROME STANDARD; PRT; 1015 AA. AC Q9V7A4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Integrin alpha-PS4 precursor (Position-specific antigen 4, alpha DE chain). GN ALPHA-PS4 OR CG16827. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: POSSIBLE ROLE IN CELL-CELL INTERACTIONS (BY SIMILARITY). CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. ALPHA-PS4 CC ASSOCIATES WITH BETA-PS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE INTEGRIN ALPHA CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 7 FG-GAP REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003811; AAF58154.1; -. DR HSSP; P11215; 1A8X. DR FlyBase; FBgn0034005; alpha-PS4. DR InterPro; IPR000413; Integrin_alpha. DR Pfam; PF01839; FG-GAP; 3. DR SMART; SM00191; Int_alpha; 4. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. KW Integrin; Cell adhesion; Receptor; Glycoprotein; Transmembrane; KW Signal; Repeat. FT SIGNAL 1 ? POTENTIAL. FT CHAIN ? 1015 INTEGRIN ALPHA-PS4. FT DOMAIN ? 931 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 932 952 POTENTIAL. FT DOMAIN 953 1015 CYTOPLASMIC (POTENTIAL). FT REPEAT ? ? FG-GAP 1. FT REPEAT ? ? FG-GAP 2. FT REPEAT 212 267 FG-GAP 3. FT REPEAT 270 331 FG-GAP 4. FT REPEAT 332 388 FG-GAP 5. FT REPEAT 394 446 FG-GAP 6. FT REPEAT ? ? FG-GAP 7. FT CARBOHYD 228 228 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 361 361 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 455 455 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 589 589 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 607 607 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 746 746 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 821 821 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 842 842 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 853 853 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 877 877 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1015 AA; 112761 MW; 964DBE424FB1FEC6 CRC64; MVAAPRANSS LEAQRNISEP GVIFRCYFES GNNCSPYNID TKGNYKGMPN DGLLTAKNKD FRWLGGAMDG GTRDSDKFLV CAPRFYSINN ENDYNNGMCY WLSDTPKNID STEVMEKWPL RIEKKQVLKL ADTNLIPYYS MGELGLSAHV SDDNSKLLMG APGIDQWKGS VHLKQEVPSI KTSSGRQRRG MNTNRKCNEC NPEPKNFGQE EFSYFGYAVS SGYFDSSNLS TVLYVATAPR GNNQFGEAYI FDIYEDSIYK YHEFRGNHFG EYFGYSVLAE DLNGDGKTDV IISAPLYALR NSYDDGAIYV FINKGSFTFE ERIIRSPAGS GGRFGTTLSR IGDINKDGYN DVAVGAPFAG NGSVFIYLGS ENGLRDPPSQ CLDAPSQQPS KYGSYMFGHG LSRGSDIDGN GFNDFAIGAP NAEAVYLYRA YPVVKIHAII KPKLQNVNPE EERVNITVCY RLSSKSDSKA KALMEQELVI RIDIDTKSKI KLAVFDEEHG SQMSFKAKAF HEEICSEFQI EMDKRAKFTP IALEMQYELS KKIPNSGDFC EDCAVVDPAE PKFVTEYITF NTGCATDVCV ADLKISCINA SSTLVLGTTA VLRLTYNITN NGEFAYHPKF SVTNSAGLSL AQVPGNCKVN EAVMVCDLNH GQRMAKGDTD SLTISFDVRQ LRGRSLEIQA EVLSARDESN PENNKLTNVL SLREKADIYV SGVQTNDHVV LKESPYTAEV VNYYEIKSHG PSTLENLTVS LYIPVAYKTP DSTNVKHIVT SSPKIQSKYA HKIMPINFID QNNALANNFA IDHDQSTLLF SATPQHENVG NLSGIVEQNP SISLLNEDLP VNNTLVLNCQ DTNVTLCVPV EIRLENGLQL KPEELMNMTV SFTVNLKDAD DIWEYFVIQT DLKVHKIGDP TLSSFTIEKK IESNVICKHA EIAIWKIIVS VIVGILVFSA ATYALYKRGF FKRAIKDDLK QLIRDSFEDG IIRTEMEENA QSQGDADLDE KLDAYADTTG KCTHV // ID ITA5_DROME STANDARD; PRT; 1000 AA. AC Q9W1M8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Integrin alpha-PS5 precursor (Position-specific antigen 5, alpha DE chain). GN ALPHA-PS5 OR CG5372. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: POSSIBLE ROLE IN CELL-CELL INTERACTIONS (BY SIMILARITY). CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. ALPHA-PS5 CC ASSOCIATES WITH BETA-PS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE INTEGRIN ALPHA CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 7 FG-GAP REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003461; AAF47029.1; -. DR FlyBase; FBgn0034880; alpha-PS5. DR InterPro; IPR000413; Integrin_alpha. DR Pfam; PF01839; FG-GAP; 3. DR SMART; SM00191; Int_alpha; 3. KW Integrin; Cell adhesion; Receptor; Glycoprotein; Transmembrane; KW Signal; Repeat. FT SIGNAL 1 ? POTENTIAL. FT CHAIN ? 1000 INTEGRIN ALPHA-PS5. FT DOMAIN ? 929 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 930 950 POTENTIAL. FT DOMAIN 951 1000 CYTOPLASMIC (POTENTIAL). FT REPEAT 26 84 FG-GAP 1. FT REPEAT ? ? FG-GAP 2. FT REPEAT ? ? FG-GAP 3. FT REPEAT 215 272 FG-GAP 4. FT REPEAT 273 332 FG-GAP 5. FT REPEAT 334 391 FG-GAP 6. FT REPEAT 397 451 FG-GAP 7. FT CARBOHYD 58 58 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 231 231 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 516 516 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 592 592 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 622 622 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 732 732 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 771 771 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 829 829 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 842 842 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 853 853 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 922 922 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1000 AA; 110543 MW; BD1D95C924D0B71E CRC64; MNFSPLPNRV IDAPKHLKTR MIQVRSSYFG YSLVIRPTSI FVGAPRAQST LESQGSINET GAVYRCPLAS GSCSHYVLND KLNKQFQWLG GSMDGGTKDT DKLLVCAPRF FVPKNKNYGQ MRGICYWVRD TVADTPPLSD VRTISLIPSQ AEEHFMLELG LSAHVTDDNS GFLIGAPGVR SWKGSVLVHR GEDLAAQGSY AVKMLDSWDW VKNHFTYVGY ALSSGYFSSN NRTSLLYVTT APSSVLNTGK AYIFDVVGEI VRKLHVFHGE QLGEYFGYSV VAEDLNGDGL TDVVVSAPLN ALGDSYDVGA IYVFINKGLF KFEKKIIRLP LSSGARFGSS LSKVGDINHD GYNDLAVGAP FAGNGAVFIF LGSEHGLRDE PSQRLDAPSR EPGPYGAHMF GQGLSRGSDI DGNGFNDLAI GAPGAEAVYL YRAYPVVKIH ATVRSESRAI RPEQETITVT ACYRLETTSK ARQMQQQELT FRMTIDELLQ RVSFAPMRTN EVSFQAQAGL SGSCRNFSVG VHYTGGIFTP IDLELHYELA KKIPHSHEAF CESCAVVDPL EPKYATGTLS FMTGCAAHVC VSDLQLSSKD VNSSFIFGSL EVLSFSYEIT NSGEPAYVAQ FNVTSSARLP FAKVPGNCRV RHEVMLCDLN GGRALARGDS ESLTIIFDVT QLSGQSLTIE AAVSSAGMDQ NPKDNTMSTT ISLREYAEID ASGGPIDGHI ALKEYPYSAE VNNSYEFKSH GPSIIDELTV YVDVPIAYTV TGSAGIKSIF NISSLQMQAT HGSELVPIKL YDQTNTLAKE YPLEDSSRRA NRKRRELQQD QYAIMPDVNI SDILTKENLP ANRTLVLDCL RGNWTICVRS QMRVQLKPEQ PIDLRISFKV DLNDFVNTFD YLVIFTNVEM FKEGDSTSIA LKRNLKPNVI FNYSETPLPI WYIILSLIAG HLLLGAMTYI LYKLRFFKRG KKEELKRLLE EHRSETKEPA TDCEGNQEEI NVEMHSDLEN // ID ITBN_DROME STANDARD; PRT; 799 AA. AC Q27591; Q9VIG7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Integrin beta-nu precursor. GN BETA-INT-NU OR CG1762. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Midgut endoderm; RX MEDLINE=94357079; PubMed=8076521; RA Yee G.H., Hynes R.O.; RT "A novel, tissue-specific integrin subunit, beta nu, expressed in the RT midgut of Drosophila melanogaster."; RL Development 118:845-858(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLY PLAYS A ROLE IN CELL ADHESION. CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE INTEGRIN BETA CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 VWFA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13305; AAC37169.1; -. DR EMBL; AE003669; AAF53952.1; -. DR HSSP; P05106; 1JV2. DR FlyBase; FBgn0010395; beta-Int-nu. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR002369; Integrin_B. DR InterPro; IPR001169; Integrin_beta_C. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR003659; Plexin-like. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00362; integrin_B; 1. DR PRINTS; PR00011; EGFLAMININ. DR PRINTS; PR01186; INTEGRINB. DR ProDom; PD001811; Integrin_B; 1. DR SMART; SM00187; INB; 1. DR SMART; SM00423; PSI; 1. DR SMART; SM00327; VWA; 1. DR PROSITE; PS00022; EGF_1; UNKNOWN_4. DR PROSITE; PS01186; EGF_2; UNKNOWN_4. DR PROSITE; PS00243; INTEGRIN_BETA; 1. DR PROSITE; PS50234; VWFA; 1. KW Integrin; Cell adhesion; Receptor; Transmembrane; Glycoprotein; KW Signal. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 799 INTEGRIN BETA-NU. FT DOMAIN 27 725 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 726 746 POTENTIAL. FT DOMAIN 747 799 CYTOPLASMIC (POTENTIAL). FT DOMAIN 136 372 VWFA. FT CARBOHYD 73 73 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 167 167 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 409 409 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 505 505 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 655 655 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 680 680 E -> G (IN REF. 1). FT CONFLICT 701 701 V -> A (IN REF. 1). SQ SEQUENCE 799 AA; 90841 MW; 351869D523F07DEB CRC64; MTSLGGRAFL WIYLVFLIAE ISHSDADSID DQCRHADSCE RCLSAHLECA WCTDKEYQVG YRCLSRRQLL NYNCSETDIY ENQPVLDVLQ DKPLKDYETS DQAVQVTPQR AYLKLVKGNT QRMKLSYRTA RNNPLDLYVL MDLTWTMRDD KKTLEELGAQ LSQTLKNLTG NYRLGFGSFA DKPTLPMILP QHRENPCAAE RATCEPTYGY RHQLSLTDDI PAFTSAVANS KITGNLDNLE GGLDALMQVI VCTKEIGWKE QARKVVILVT DGFMHLAGDG LLAGIIQRND KQCHLNKAGE YTGSLNYDYP SLEEIYRELL RRKINVIFAV TEEVVSSYWE LSALMKEISY VDILSADSSN ILELIKKSYE SLIKRTQFAD NSPDFIDMAY YTDCGGQFPS LQKRNYCNNV TLGKQIDFYV DVTLKKYPDN QVYTHKIRVE ETSLSEFMDL DVELQRPCPC QETPDPENEE GRFLCDYKGY LYCGMCECDE GWTGTYCNCP TDATNVTSNE ALLQKCRQPF SDKSTSELVC SNHGDCDCGT CLCDPGYTGP FCECRECLDC DEKLADCFCG QCVCKYGWSG SKCNCDGDTD ACVGPTGEIC SERGTCQCEE CQCEEPYLGK FCEIDPEKDN KLCLFYEPCV TCLIEQKQGM GVCENLTEIC SSLDRQETYP YNFVHELDPE QDQCLVRLVN KHGIQCDSFF VYQVIDHSNF LTIQAVDCEP PDYVALVGYI SAFTLLIGLL IIFIILWYIR AKDAREYAKF EEDQKNSVRQ ENPIYRDPVG RYEVPKALSV KYDENPFAS // ID ITBX_DROME STANDARD; PRT; 846 AA. AC P11584; Q8MYX9; Q9W3L2; DT 01-OCT-1989 (Rel. 12, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Integrin beta-PS precursor (Position-specific antigen, beta chain) DE (Myospheroid protein) (Olfactory C protein). GN MYS OR L(1)MYS OR OLFC OR CG1560. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88190122; PubMed=3128792; RA Mackrell A.J., Blumberg B., Haynes S.R., Fessler J.H.; RT "The lethal myospheroid gene of Drosophila encodes a membrane protein RT homologous to vertebrate integrin beta subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 85:2633-2637(1988). RN [2] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF RP ASP-807; PHE-811; PHE-814; GLU-817; TYR-831 AND TYR-843. RC TISSUE=Embryo, and Imaginal disks; RX MEDLINE=94163982; PubMed=8119134; RA Grinblat Y., Zusman S., Yee G., Hynes R.O., Kafatos F.C.; RT "Functions of the cytoplasmic domain of the beta PS integrin subunit RT during Drosophila development."; RL Development 120:91-102(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP FUNCTION. RX MEDLINE=20279204; PubMed=10821184; RA Ayyub C., Rodrigues V., Hasan G., Siddiqi O.; RT "Genetic analysis of olfC demonstrates a role for the RT position-specific integrins in the olfactory system of Drosophila RT melanogaster."; RL Mol. Gen. Genet. 263:498-504(2000). CC -!- FUNCTION: INTEGRIN ALPHA-PS1/BETA-PS IS A RECEPTOR FOR LAMININ. CC INTEGRIN ALPHA-PS2/BETA-PS IS A RECEPTOR FOR TIG (TIGGRIN). ALSO CC BINDS TO WB (WING BLISTER) AND TEN-M (TENASCIN MAJOR). REQUIRED CC FOR MANY EMBRYONIC (DORSAL CLOSURE AND SOMATIC MUSCLE ATTACHMENTS) CC AND POST-EMBRYONIC DEVELOPMENTAL PROCESSES (ATTACHMENT BETWEEN CC CELL LAYERS OF IMAGINAL DISKS, ORGANIZATION OF OMMATIDIAL ARRAYS CC AND FLIGHT MUSCLE DEVELOPMENT). INVOLVED IN THE FUNCTION AND/OR CC DEVELOPMENT OF THE OLFACTORY SYSTEM. CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. BETA-PS CC ASSOCIATES WITH EITHER ALPHA-PS1, ALPHA-PS2 OR ALPHA-PS3. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EMBRYONIC DORSAL CUTICLE, LARVAL EYE AND WING CC IMAGINAL DISK. CC -!- MISCELLANEOUS: THE ABSENCE OF THE BETA-PS SUBUNIT RESULTS IN CC DETACHMENT AND ROUNDING UP OF THE MUSCLES, THUS THE GENE ENCODING CC BETA-PS IS CALLED MYOSPHEROID. CC -!- SIMILARITY: BELONGS TO THE INTEGRIN BETA CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 2 VWFA-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03251; AAA28714.1; -. DR EMBL; AE003442; AAF46313.2; -. DR EMBL; AY113499; AAM29504.1; -. DR PIR; A30889; A30889. DR HSSP; P05106; 1JV2. DR FlyBase; FBgn0004657; mys. DR GO; GO:0008305; C:integrin complex; NAS. DR GO; GO:0007417; P:central nervous system development; IMP. DR GO; GO:0007517; P:muscle development; IMP. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR002369; Integrin_B. DR InterPro; IPR001169; Integrin_beta_C. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00362; integrin_B; 1. DR PRINTS; PR01186; INTEGRINB. DR ProDom; PD001811; Integrin_B; 1. DR SMART; SM00187; INB; 1. DR SMART; SM00327; VWA; 1. DR PROSITE; PS00243; INTEGRIN_BETA; 3. DR PROSITE; PS00022; EGF_1; UNKNOWN_2. DR PROSITE; PS01186; EGF_2; UNKNOWN_1. KW Behavior; Flight; Olfaction; Vision; Integrin; Cell adhesion; KW Receptor; Transmembrane; Glycoprotein; Repeat; Signal; KW Phosphorylation. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 846 INTEGRIN BETA-PS. FT DOMAIN 24 776 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 777 799 POTENTIAL. FT DOMAIN 800 846 CYTOPLASMIC (POTENTIAL). FT DOMAIN 115 143 SER-RICH. FT DOMAIN 186 419 VWFA-LIKE. FT DOMAIN 507 687 4 CYSTEINE-RICH TANDEM REPEATS. FT REPEAT 507 560 I. FT REPEAT 561 605 II. FT REPEAT 606 646 III. FT REPEAT 647 687 IV. FT DISULFID 46 55 BY SIMILARITY. FT DISULFID 249 252 BY SIMILARITY. FT DISULFID 300 341 BY SIMILARITY. FT DISULFID 441 453 BY SIMILARITY. FT DISULFID 473 741 BY SIMILARITY. FT DISULFID 503 507 BY SIMILARITY. FT DISULFID 522 533 BY SIMILARITY. FT DISULFID 530 571 BY SIMILARITY. FT DISULFID 535 544 BY SIMILARITY. FT DISULFID 546 561 BY SIMILARITY. FT DISULFID 584 599 BY SIMILARITY. FT DISULFID 601 606 BY SIMILARITY. FT DISULFID 622 627 BY SIMILARITY. FT DISULFID 624 656 BY SIMILARITY. FT DISULFID 629 638 BY SIMILARITY. FT DISULFID 640 647 BY SIMILARITY. FT DISULFID 662 667 BY SIMILARITY. FT DISULFID 664 715 BY SIMILARITY. FT DISULFID 669 682 BY SIMILARITY. FT DISULFID 685 688 BY SIMILARITY. FT DISULFID 692 701 BY SIMILARITY. FT DISULFID 698 771 BY SIMILARITY. FT DISULFID 719 749 BY SIMILARITY. FT CARBOHYD 72 72 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 266 266 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 277 277 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 403 403 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 428 428 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 557 557 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 603 603 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 644 644 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 718 718 N-LINKED (GLCNAC...) (POTENTIAL). FT MOD_RES 831 831 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 843 843 PHOSPHORYLATION (BY SIMILARITY). FT MUTAGEN 807 807 D->A: RESCUES DORSAL CLOSURE DEFECT, FT MUSCLE ATTACHMENT DEFECT, DISORGANISED FT OMMATIDIAL ARRAY AND LOSS OF CELL LAYER FT ATTACHMENT IN MUTANTS; WHEN ASSOCIATED FT WITH A-817. FT MUTAGEN 811 811 F->A: RESCUES MUSCLE ATTACHMENT DEFECT FT AND LOSS OF CELL LAYER ATTACHMENT IN FT MUTANTS; WHEN ASSOCIATED WITH A-814. FT MUTAGEN 814 814 F->A: RESCUES MUSCLE ATTACHMENT DEFECT FT AND LOSS OF CELL LAYER ATTACHMENT IN FT MUTANTS; WHEN ASSOCIATED WITH A-811. FT MUTAGEN 817 817 E->A: RESCUES DORSAL CLOSURE DEFECT, FT MUSCLE ATTACHMENT DEFECTS, DISORGANISED FT OMMATIDIAL ARRAY AND LOSS OF CELL LAYER FT ATTACHMENT IN MUTANTS; WHEN ASSOCIATED FT WITH A-807. FT MUTAGEN 831 831 Y->A: NO EFFECT ON LETHALITY; WHEN FT ASSOCIATED WITH A-843. FT MUTAGEN 843 843 Y->A: NO EFFECT ON LETHALITY; WHEN FT ASSOCIATED WITH A-831. FT CONFLICT 18 18 I -> M (IN REF. 1). FT CONFLICT 24 24 G -> A (IN REF. 1). FT CONFLICT 27 27 D -> N (IN REF. 1). SQ SEQUENCE 846 AA; 92656 MW; 3618C74FA1B99AFB CRC64; MILERNRRCQ LALLMIAILA AIAGQTDAQK AAKLTAVSTC ASKEKCHTCI QTEGCAWCMQ PDFKGQSRCY QNTSSLCPEE FAYSPITVEQ ILVNNKLTNQ YKAELAAGGG GSAMSGSSSS SYSSSSSSSS FYSQSSSGSS SASGYEEYSA GEIVQIQPQS MRLALRVNEK HNIKISYSQA EGYPVDLYYL MDLSKSMEDD KAKLSTLGDK LSETMKRITN NFHLGFGSFV DKVLMPYVST IPKKLEHPCE NCKAPYGYQN HMPLNNNTES FSNEVKNATV SGNLDAPEGG FDAIMQAIAC RSQIGWREQA RRLLVFSTDA GFHYAGDGKL GGVIAPNDGE CHLSPKGEYT HSTLQDYPSI SQINQKVKDN AINIIFAVTA SQLSVYEKLV EHIQGSSAAK LDNDSSNVVE LVKEEYRKIS SSVEMKDNAT GDVKITYFSS CLSNGPEVQT SKCDNLKEGQ QVSFTAQIQL LKCPEDPRDW TQTIHISPVG INEVMQIQLT MLCSCPCENP GSIGYQVQAN SCSGHGTSMC GICNCDDSYF GNKCECSATD LTSKFANDTS CRADSTSTTD CSGRGHCVCG ACECHKRPNP IEIISGKHCE CDNFSCERNR NQLCSGPDHG TCECGRCKCK PGWTGSNCGC QESNDTCMPP GGGEICSGHG TCECGVCKCT VNDQGRFSGR HCEKCPTCSG RCQELKDCVQ CQMYKTGELK NGDDCARNCT QFVPVGVEKV EIDETKDEQM CKFFDEDDCK FMFKYSEQGE LHVYAQENKE CPAKVFMLGI VMGVIAAIVL VGLAILLLWK LLTTIHDRRE FARFEKERMN AKWDTGENPI YKQATSTFKN PMYAGK // ID JAK_DROME STANDARD; PRT; 1177 AA. AC Q24592; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tyrosine-protein kinase hopscotch (EC 2.7.1.112). GN HOP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94148222; PubMed=8314084; RA Binari R., Perrimon N.; RT "Stripe-specific regulation of pair-rule genes by hopscotch, a RT putative Jak family tyrosine kinase in Drosophila."; RL Genes Dev. 8:300-312(1994). CC -!- FUNCTION: TYROSINE KINASE OF THE NON-RECEPTOR TYPE, PHOSPHORYLATES CC THE MARELLE PROTEIN. INVOLVED IN THE CONTROL OF PAIR-RULE GENE CC TRANSCRIPTION IN A STRIPE-SPECIFIC MANNER. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: WHOLLY INTRACELLULAR, POSSIBLY MEMBRANE CC ASSOCIATED (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. CC -!- DOMAIN: POSSESSES TWO PHOSPHOTRANSFERASE DOMAINS. THE SECOND ONE CC PROBABLY CONTAINS THE CATALYTIC DOMAIN (BY SIMILARITY), WHILE THE CC PRESENCE OF SLIGHT DIFFERENCES SUGGEST A DIFFERENT ROLE FOR DOMAIN CC 1 (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. JAK CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 FERM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L26975; AAA62441.1; -. DR PIR; A36984; A36984. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0004864; hop. DR GO; GO:0004718; F:Janus kinase activity; NAS. DR GO; GO:0008283; P:cell proliferation; IMP. DR GO; GO:0045317; P:equator specification; IMP. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR GO; GO:0007259; P:JAK-STAT cascade; IGI. DR GO; GO:0007480; P:leg morphogenesis (sensu Holometabola); NAS. DR GO; GO:0016318; P:ommatidial rotation; IMP. DR GO; GO:0007365; P:periodic partitioning; IMP. DR GO; GO:0007538; P:primary sex determination; IMP. DR GO; GO:0019827; P:stem cell maintenance; IMP. DR GO; GO:0007476; P:wing morphogenesis; NAS. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000980; SH2. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00069; pkinase; 2. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00295; B41; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; FALSE_NEG. DR PROSITE; PS50057; FERM_3; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; FALSE_NEG. KW Transferase; Tyrosine-protein kinase; ATP-binding; Phosphorylation; KW SH2 domain; Repeat; Developmental protein. FT DOMAIN 46 414 FERM. FT DOMAIN 433 539 SH2 (ATYPICAL). FT DOMAIN 542 547 POLY-LEU. FT DOMAIN 582 843 PROTEIN KINASE 1. FT DOMAIN 892 1164 PROTEIN KINASE 2. FT NP_BIND 898 906 ATP (BY SIMILARITY). FT BINDING 926 926 ATP (BY SIMILARITY). FT ACT_SITE 1014 1014 BY SIMILARITY. FT MOD_RES 1047 1047 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). SQ SEQUENCE 1177 AA; 135027 MW; 903A92B450EE823F CRC64; MALANGGEDR MDDSSSGRTS LADSASLTNS SLRSGTSSQS IHTNDGTIRV FNFTTGEFER FHPNMLCEEI CNTMCRQLGI APIAQLLYGI REHSTSRRPS PLVRLDLTWC LPGERLNCQL VYCFRMRFRV PELDSQLELI DGRSHKFLYR QMRYDMRTEQ IPEIRYPEHK DKSTGLAVMD MLIDDQEQSE DQQAMRSIEK LYKLYLPPSL WRAHSFFVGS KIREVFRSLK ANSLSVERLK WHYVHQVSHL APTYMTEQFT CTVQYLPNEE VARGSGPIGT SLAHSTSTLA SSGSTNTLST LTTNTNSVAL GGSGKKAKRR STSGGIDVYV RVFPHDSLEP GLKVARVTSE ATLKWILVGA VEGIVMISKI NDTSVRLEIV GLPKGYEMQF QTEKEMKSFI SYLGIYIRLS SKWMQDLCHS YRTPSLEELS SLHCHGPIGG AYSLMKLHEN GDKCGSYIVR ECDREYNIYY IDINTKIMAK KTDQERCKTE TFRIVRKDSQ WKLSYNNGEH VLNSLHEVAH IIQADSPDRY RIPASKYDKP PLLLLLLPKN LKAKKTDLQL SEAELQRRNP QIFNPRTDLQ WYPDSISLSD DAMMFTMRGD WIQQSPVKDV SVTMKMLKSD GNFMEFFRLA QTWSLIQSPQ FLKLYGLTLA DPYTMVMEYS RYGPLNKFLH SMPNVTLHCL LDLMHGLVRG MHYLEDNKII HNYIRCSNLY VTKYDPNSYV LDAKISDPGY PRPYRESDSP WIPVKYYRNL QAAKTDQFAQ LWAFATTIYE IFSRCKEDLS TLRQEQLLRQ KNLDGNILKM LDQDICPAPI FETIMDGWSD DETKRFSHHD IFSRLNTIKA EILPNYMPPP EIATNGTGDE TVIDRSDIPF LPFPRSNMLM VIPLTSECRV IYNMENMIGR GHYGTVYKGH LEFNDKDQPR EQVAIKMLNT MQVSTDFHRE IGIMRTLSHP NIVKFKYWAE KSHCIIMEYL QSGSFDIYLR FTAPNLNNPR LVSFALDIAN GMKYLSDMGL IHRDLAARNI LVDHNGDGDC VKISDFGLAQ FANSDGYYYA KSKRDIPIRW YSPEAISTCR FSSYSDVWSY GVTLFEMFSR GEEPNLVPIQ TSQEDFLNRL QSGERLNRPA SCPDFIYDLM QLCWHATPRS RPSFATIVDI ITREVATKVT HPTDGHQSPP NQPTDAE // ID JANA_DROME STANDARD; PRT; 135 AA. AC P20348; Q9VAB6; DT 01-FEB-1991 (Rel. 17, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sex-regulated protein janus-A. GN JANA OR CG7933. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89343970; PubMed=2503707; RA Yanicostas C., Vincent A., Lepesant J.-A.; RT "Transcriptional and posttranscriptional regulation contributes to RT the sex-regulated expression of two sequence-related genes at the RT janus locus of Drosophila melanogaster."; RL Mol. Cell. Biol. 9:2526-2535(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: SOMATIC AND GERM LINE CELLS. CC -!- DEVELOPMENTAL STAGE: THE NON-SEX-SPECIFIC TRANSCRIPT IS PRESENT AT CC ALL STAGES. CC -!- MISCELLANEOUS: TRANSCRIPTION OF JANA GIVES RISE TO TWO CC SEX-SPECIFIC AND TO ONE NON-SEX-SPECIFIC TRANSCRIPTS. CC -!- SIMILARITY: BELONGS TO THE JANUS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27033; AAC34203.1; -. DR EMBL; M27033; AAC34202.1; ALT_INIT. DR EMBL; AE003772; AAF56997.1; -. DR PIR; A32317; A32317. DR FlyBase; FBgn0001280; janA. DR InterPro; IPR007702; Ocnus. DR Pfam; PF05005; Ocnus; 1. SQ SEQUENCE 135 AA; 15220 MW; 2720237CE77F3132 CRC64; MNRLQLLSKG LRLIHKMSEE ALAGVPLVHI SPEGIFKYVM INVFDGGDAS KAVIRGFADC TWHADIFERE EEVFKKLGLR AECPGGGRIE HNPEKKYLKV YGYSQGFGKA DHAQTKRILA TKYPDYTIEI SDEGY // ID JANB_DROME STANDARD; PRT; 140 AA. AC P20349; Q9VAB7; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sex-regulated protein janus-B. GN JANB OR CG7931. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89343970; PubMed=2503707; RA Yanicostas C., Vincent A., Lepesant J.-A.; RT "Transcriptional and posttranscriptional regulation contributes to RT the sex-regulated expression of two sequence-related genes at the RT janus locus of Drosophila melanogaster."; RL Mol. Cell. Biol. 9:2526-2535(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: GERM LINE CELLS OF ADULT MALES. CC -!- DEVELOPMENTAL STAGE: FROM THE THIRD-INSTAR LARVAL STAGE TO THE CC ADULT STAGE. CC -!- SIMILARITY: BELONGS TO THE JANUS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27033; AAC34204.1; -. DR EMBL; AE003772; AAF56996.1; -. DR PIR; B32317; B32317. DR FlyBase; FBgn0001281; janB. DR InterPro; IPR007702; Ocnus. DR Pfam; PF05005; Ocnus; 1. SQ SEQUENCE 140 AA; 15859 MW; 5750CC28BB61D7FE CRC64; MKMFKSLRLL PHIVSPFQKC YSTDLISLVG VPRVKITKGQ NRYLLVNIHT HGFTKYGRVI VRGADVDNHL AVFDSILEEL EPEGICAKIL GGGRILNEAE NKKIKIYGTS RTFGGADHTR TRNILQAWTT YKDFKITVKQ // ID JDP_DROME STANDARD; PRT; 182 AA. AC Q9TVP3; Q9V3I7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE J domain containing protein. GN JDP OR CG2239. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RX MEDLINE=20011296; PubMed=10542335; RA Hahn Y., Lee J., Seong C., Yoon J., Chung J.H.; RT "Structural analysis of phylogenetically conserved J domain protein RT gene."; RL Biochim. Biophys. Acta 1447:325-333(1999). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RX MEDLINE=20225482; PubMed=10760603; RA Lee J., Hahn Y., Yun J.H., Mita K., Chung J.H.; RT "Characterization of JDP genes, an evolutionarily conserved J domain- RT only protein family, from human and moths."; RL Biochim. Biophys. Acta 1491:355-363(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; Synonyms=JDPa; CC IsoId=Q9TVP3-1; Sequence=Displayed; CC Name=b; Synonyms=JDPb; CC IsoId=Q9TVP3-2; Sequence=VSP_001297; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE HEAD. CC -!- SIMILARITY: CONTAINS 1 J DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF192462; AAF12790.1; -. DR EMBL; AF192463; AAF12791.1; -. DR EMBL; AF132905; AAD51421.1; -. DR EMBL; AF132902; AAD51421.1; JOINED. DR EMBL; AF132903; AAD51421.1; JOINED. DR EMBL; AF132904; AAD51421.1; JOINED. DR EMBL; AF132905; AAD48755.1; -. DR EMBL; AF132902; AAD48755.1; JOINED. DR EMBL; AF132903; AAD48755.1; JOINED. DR EMBL; AF132904; AAD48755.1; JOINED. DR EMBL; AE003774; AAF57063.1; -. DR EMBL; AY060331; AAL25370.1; -. DR HSSP; P08622; 1BQZ. DR FlyBase; FBgn0027654; jdp. DR InterPro; IPR001623; DnaJ_N. DR InterPro; IPR003095; Hsp_DnaJ. DR Pfam; PF00226; DnaJ; 1. DR PRINTS; PR00625; DNAJPROTEIN. DR SMART; SM00271; DnaJ; 1. DR PROSITE; PS00636; DNAJ_1; FALSE_NEG. DR PROSITE; PS50076; DNAJ_2; 1. KW Chaperone; Alternative splicing. FT DOMAIN 17 82 J-DOMAIN. FT VARSPLIC 102 102 Q -> QVRRYTIAEKVDKE (in isoform b). FT /FTId=VSP_001297. SQ SEQUENCE 182 AA; 20062 MW; ACA939D82D27677A CRC64; MSAVDAIINY KRSPNEDFYG LLHCDENSSP EQIQAEYKVL ALQYHPDKNS GDKEAEAKFQ QLKEAKETLC DPEKRAIYDK WRNSGISMSY KQWLGMKEHV GQSMHWVTPK TKDRMLPETG GAAAQGPGTG AGCSSGGLTA ASPNPAHRRA SEGGAALYYG SRKGEWGGEN TDVANKFRNY EI // ID JIP1_DROME STANDARD; PRT; 490 AA. AC Q9W0K0; Q9NH69; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE JNK-interacting protein 1 (JIP-1) (Eye developmental protein SP512) DE (APP-like interacting protein 1) (APLIP1). GN APLIP1 OR SP512 OR CG1200. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP INTERACTION WITH APPL; HEP AND KLC. RC TISSUE=Embryo; RX MEDLINE=22028091; PubMed=11912189; RA Taru H., Iijima K.-I., Hase M., Kirino Y., Yagi Y., Suzuki T.; RT "Interaction of Alzheimer's beta-amyloid precursor family proteins RT with scaffold proteins of the JNK signaling cascade."; RL J. Biol. Chem. 277:20070-20078(2002). RN [2] RP SEQUENCE FROM N.A. RA Serano T.L., Pendleton J.D., Rubin G.M.; RT "A reverse genetic screen for genes involved in Drosophila eye RT development."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE JNK-INTERACTING PROTEIN (JIP) GROUP OF SCAFFOLD CC PROTEINS SELECTIVELY MEDIATES JNK SIGNALING BY AGGREGATING CC SPECIFIC COMPONENTS OF THE MAPK CASCADE TO FORM A FUNCTIONAL JNK CC SIGNALING MODULE. MAY FUNCTION AS A REGULATOR OF CC VESICLE TRANSPORT, THROUGH INTERATIONS WITH THE JNK-SIGNALING CC COMPONENTS AND MOTOR PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: FORMS HOMO- AND HETEROOLIGOMERIC COMPLEXES. BINDS HEP, A CC DUAL SPECIFICITY PROTEIN KINASE IN THE JNK PATHWAY, BUT NOT ITS CC DOWNSTREAM TARGET BSK. THE C-TERMINAL OF APLIP2 INTERACTS WITH THE CC KINESIN LIGHT CHAIN PROTEIN, KLC, AND THE C-TERMINAL PTY MOTIF OF CC BETA AMYLOID PROTEIN PRECURSOR-LIKE PROTEIN, APPL. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE BRAIN, CNS, PNS AND CELLS CC POSTERIOR TO THE MORPHOGENETIC FURROW IN THE EYE IMAGINAL DISK OF CC LATE EMBRYOS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM EMBRYONIC STAGE 12 THROUGH TO CC ADULTHOOD. CC -!- SIMILARITY: BELONGS TO THE JIP SCAFFOLD FAMILY. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PID DOMAIN. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF220194; AAL50332.1; -. DR EMBL; AF231037; AAF34806.1; -. DR EMBL; AE003470; AAF47446.1; ALT_SEQ. DR EMBL; AY051495; AAK92919.1; -. DR FlyBase; FBgn0040281; Aplip1. DR GO; GO:0005737; C:cytoplasm; ISS. DR GO; GO:0019894; F:kinesin binding; IPI. DR GO; GO:0005078; F:MAP-kinase scaffold activity; IPI. DR GO; GO:0019901; F:protein kinase binding; IPI. DR GO; GO:0046328; P:regulation of JNK cascade; ISS. DR GO; GO:0016192; P:vesicle-mediated transport; ISS. DR InterPro; IPR006020; PTB_PID. DR InterPro; IPR001452; SH3. DR Pfam; PF00640; PID; 1. DR Pfam; PF00018; SH3; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00462; PTB; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS01179; PID; 1. DR PROSITE; PS50002; SH3; 1. KW SH3 domain; Developmental protein. FT DOMAIN 150 153 POLY-ARG. FT DOMAIN 185 189 POLY-GLY. FT DOMAIN 251 260 PRO-RICH. FT DOMAIN 271 333 SH3. FT DOMAIN 344 479 PID. SQ SEQUENCE 490 AA; 53815 MW; 2744E85790EE043F CRC64; MADSEFEEFH RPIFEPHTIA GFGSGAGSKK NNPHAFYSLI PNDDLEDSHS SKSDGDGSDQ EDGIGLVDHE PKMRQVEDDE LGDGLKVTLS SDGSLDTNDS FNSHRHHPLN HQDAIGGFLG MDTSGLGGNS APVTIGASTD LLAPNTAATR RRRKLPEIPK NKKSSILHLL GGSNFGSLAD EFRNGGGGGI PPAVRSGQQR SFLSLKCGYL MDEDSSPDSE RMQSLGDVDS GHSTAHSPND FKSMSPQITS PVSQSPFPPP FGGVPFGQLE MLEATHRGLH KFVPRHHDEI ELEIGDAIYV QKEAEDLWCE GVNLRTGRQG IFPSAYAVDL DYNEFDPTVQ LVKKERYLLG YLGSVETLAH KGTGVVCQAV RKIVGEYGNS PTGQTCILEV SDQGLRMVDR SGPNQNKKDK KPCIDYFYSL KNVSFCAFHP RDHRFIGFIT KHPTVQRFAC HVFKGSESTR PVAEAVGRAF QRFYQKFIET AYPIEDIYIE // ID JIP3_DROME STANDARD; PRT; 1227 AA. AC Q9GQF1; Q95SK0; Q9VSC0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE JNK-interacting protein 3 (Sunday driver protein). GN SYD OR CG8110. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG), AND INTERACTION WITH KLC. RX MEDLINE=20560743; PubMed=11106729; RA Bowman A.B., Kamal A., Ritchings B.W., Philp A.V., McGrail M., RA Gindhart J.G., Goldstein L.S.B.; RT "Kinesin-dependent axonal transport is mediated by the sunday driver RT (SYD) protein."; RL Cell 103:583-594(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 937-1227 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE JNK-INTERACTING PROTEIN (JIP) GROUP OF SCAFFOLD CC PROTEINS SELECTIVELY MEDIATES JNK-SIGNALING BY AGGREGATING CC SPECIFIC COMPONENTS OF THE MAPK CASCADE TO FORM A FUNCTIONAL JNK CC SIGNALING MODULE. MAY FUNCTION AS A REGULATOR OF VESICLE CC TRANSPORT, THROUGH INTERATIONS WITH THE JNK-SIGNALING COMPONENTS CC AND MOTOR PROTEINS. SYD IS REQUIRED FOR EFFICIENT KINESIN-I CC MEDIATED AXONAL TRANSPORT. CC -!- SUBUNIT: FORMS HOMO- AND HETEROLIGOMERIC COMPLEXES. BINDS THE TPR CC MOTIF-CONTAINING C-TERMINAL OF KINESIN LIGHT CHAIN, KLC. PRE- CC ASSEMBLED SYD SCAFFOLDING COMPLEXES ARE THEN TRANSPORTED AS A CC CARGO OF KINESIN, TO THE REQUIRED SUBCELLULAR LOCATION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9GQF1-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q9GQF1-2; Sequence=VSP_002780; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE JIP SCAFFOLD FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF262045; AAG36930.1; -. DR EMBL; AE003557; AAF50505.2; -. DR EMBL; AE003557; AAN12032.1; -. DR EMBL; AY060748; AAL28296.1; -. DR FlyBase; FBgn0024187; syd. DR GO; GO:0005737; C:cytoplasm; ISS. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA. DR GO; GO:0019894; F:kinesin binding; IPI. DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISS. DR GO; GO:0019901; F:protein kinase binding; ISS. DR GO; GO:0008088; P:axon cargo transport; IMP. DR GO; GO:0046328; P:regulation of JNK cascade; ISS. DR GO; GO:0016192; P:vesicle-mediated transport; IEP. KW Coiled coil; Alternative splicing. FT DOMAIN 84 191 COILED COIL (POTENTIAL). FT DOMAIN 363 489 COILED COIL (POTENTIAL). FT DOMAIN 814 849 COILED COIL (POTENTIAL). FT VARSPLIC 1 55 Missing (in isoform Short). FT /FTId=VSP_002780. FT CONFLICT 983 983 S -> G (IN REF. 3). SQ SEQUENCE 1227 AA; 136711 MW; 2162C18066A057B8 CRC64; MMDNDDALLN NGGPQSGAET VYGTEDNNMV MSEKNEQVVS IVQQLAGSIY QEFERMINRY DEDVVKNLMP LLVNVLECLD ASYRINQEQD VEVELLREDN EQLVTQYERE KSARKQSEQK LLEAEDLAEQ ENKELATRLE SVESIVRMLE LKHKNSLEHA SRLEEREADL KKEYNKLHER YTELFKNHVD YMERTKMLMG STHSQMSTAS ERMDVSRARL NPVARSSGPV SYGFASLENS VMLDTETICS VGSQSDDSGP PSLQNELDNL SGTLERGAAT DALQQQHHAT SPQSPDSSPV VPNVPTNVGR STTKKEQRSD NNLYQELSFQ DNEESEENEI VTGSWVHPGE YASSANDNYF GMGKEVENLI MENNELLATK NALNIVKDDL IVKVDELTGE VEIVREELNA MQQSRTKLRQ RISELEDELK KAKEQVKQQN TEQEENDVPL AQRKRFTRVE MAMVLMERNQ YKERLMELQE AVRLTEILRA SRTVDNLDRK SKQSIWKYFS NLFTPSNRPT ERVADGLGGG PMFRHTGGGS PAHSHGSPSR GSGGGDNRLA LTSGQPPVHP ASAGLANALI MPKDYAEEGS SERISARRRE QYRQLRAHVQ KEDGRLHAYG WSLPINKASQ EANPNRHSGG VPVPVYCNPL AEASPHMKVF CAAGVNLHGG FTKNGQSLIP ANSPYAPKST LKIAEITSPT ADQSMEALDR QMARVSLETL EPETQLSSFV WICTSTHAAS TVSVVDANQS ATVLDAFPIC ASHLLCIASV QGAMESDYAL LEQSEVVKAG EMLQRPGEGT ELLGKVEFVR VKPKSDDEQN SNEKQQQEEE EAKEATEKSN EQLPAVSAEE PLGNVEAIKI RQPLPGAPQR LSTDGNQTNN NNNSSSSSNL LFATKSLNPI LETKDRDEPA MSSVGPTMWL GAQDGWLYVH SSVGRWHECL HRVLLPDAVL AIVHVEARVV VALANAQLAV FRRQTDGQWD LNSYHLVTLG DRNHSIRCLC VAGERIWAAH RNKIFIVDPV SLNIVHSLDA HPRKESQVRQ MAATGAGVWV SIRLDSTLRL YNTHTFEHKQ DVDIEPYVSK MLGTGKLGFS FVRITALMVS CNRLWIGTSN GVIISVPLAE VQPKSSSDPH GQMPLCCMAN AQLSFHGHRD AVKFFVSVPM LQQPNLNGGL TFTNKRPDML VMCGGEGYID FRINDNDMEN SIQLEPNQTI ENRGDKSYLI VWHVSQR // ID JNK_DROME STANDARD; PRT; 372 AA. AC P92208; O01366; Q94542; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Stress-activated protein kinase JNK (EC 2.7.1.37) (dJNK) (Basket DE protein). GN BSK OR JNK OR CG5680. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=97102675; PubMed=8946915; RA Sluss H.K., Han Z., Barrett T., Davis R.J., Ip Y.T.; RT "A JNK signal transduction pathway that mediates morphogenesis and an RT immune response in Drosophila."; RL Genes Dev. 10:2745-2758(1996). RN [2] RP SEQUENCE FROM N.A., MUTAGENESIS, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=97102676; PubMed=8946916; RA Riesgo-Escovar J.R., Jenni M., Fritz A., Hafen E.; RT "The Drosophila Jun-N-terminal kinase is required for cell RT morphogenesis but not for DJun-dependent cell fate specification in RT the eye."; RL Genes Dev. 10:2759-2768(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION. RX MEDLINE=97367953; PubMed=9224720; RA Riesgo-Escovar J.R., Hafen E.; RT "Drosophila Jun kinase regulates expression of decapentaplegic via the RT ETS-domain protein Aop and the AP-1 transcription factor DJun during RT dorsal closure."; RL Genes Dev. 11:1717-1727(1997). RN [6] RP FUNCTION, AND ENZYME REGULATION. RX MEDLINE=99365283; PubMed=10433922; RA Zeitlinger J., Bohmann D.; RT "Thorax closure in Drosophila: involvement of Fos and the JNK RT pathway."; RL Development 126:3947-3956(1999). RN [7] RP FUNCTION. RX MEDLINE=21643948; PubMed=11784101; RA Raemet M., Lanot R., Zachary D., Manfruelli P.; RT "JNK signaling pathway is required for efficient wound healing in RT Drosophila."; RL Dev. Biol. 241:145-156(2002). CC -!- FUNCTION: RESPONDS TO ACTIVATION BY ENVIRONMENTAL STRESS BY CC PHOSPHORYLATING A NUMBER OF TRANSCRIPTION FACTORS, PRIMARILY CC COMPONENTS OF AP-1 SUCH AS JRA AND ALSO THE TRANSCRIPTIONAL CC REPRESSOR AOP, AND THUS REGULATES TRANSCRIPTIONAL ACTIVITY. CC COMPONENT OF THE IMMUNE RESPONSE ACTIVATED BY BACTERIAL INFECTION, CC AND IS INVOLVED IN WOUND HEALING AND IN DORSAL CLOSURE, A CC MORPHOGENETIC MOVEMENT DURING EMBRYOGENESIS. CONTROLS THE CC EXPRESSION OF A PHOSPHATASE, PUCKERED, AT THE EDGES OF WOUNDED CC EPIDERMAL TISSUE AND IN THE DORSAL EPITHELIUM DURING DORSAL CC CLOSURE. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- COFACTOR: MAGNESIUM (BY SIMILARITY). CC -!- ENZYME REGULATION: ACTIVATED BY THREONINE AND TYROSINE CC PHOSPHORYLATION BY THE DUAL SPECIFICITY KINASE, HEP. INHIBITED BY CC DUAL SPECIFICITY PHOSPHATASE, PUCKERED. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: DURING GASTRULATION, EXPRESSION IS SEEN IN CC CELLS UNDERGOING MORPHOGENETIC MOVEMENTS. BY STAGE 9 OF EMBRYONIC CC DEVELOPMENT, EXPRESSION IS UBIQUITOUS. AT STAGES 12-14, EXPRESSION CC OCCURS IN EPIDERMIS AND CENTRAL NERVOUS SYSTEM. AT STAGE 15, CC EXPRESSION IS RESTRICTED TO VENTRAL NERVE CORD, BRAIN AND SOME CC PERIPHERAL NEURONS. IN LARVAE, EXPRESSION IS SEEN IN ALL IMAGINAL CC DISKS, WITH HIGHEST LEVELS IN WING AND EYE DISKS, AND IN THE CNS. CC ADULTS EXPRESS THE PROTEIN IN FAT BODY AND HEMOCYTES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MATERNALLY AND ZYGOTICALLY THROUGH CC TO ADULT (MALE AND FEMALE). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. MAP CC KINASE SUBFAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 331. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U49180; AAB97094.1; -. DR EMBL; U50965; AAB51187.1; -. DR EMBL; U50966; AAB51188.1; -. DR EMBL; U49249; AAB48381.1; -. DR EMBL; U73196; AAC47325.1; -. DR EMBL; AE003628; AAF52883.1; -. DR EMBL; AY122221; AAM52733.1; -. DR EMBL; AY070865; AAL48487.1; -. DR HSSP; Q16539; 1WFC. DR FlyBase; FBgn0000229; bsk. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0004705; F:JUN kinase activity; IDA. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IDA. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR GO; GO:0009795; P:embryonic morphogenesis; IDA. DR GO; GO:0007392; P:initiation of dorsal closure; IMP. DR GO; GO:0007254; P:JNK cascade; IDA. DR GO; GO:0000165; P:MAPKKK cascade; NAS. DR GO; GO:0046844; P:micropyle formation; IMP. DR GO; GO:0006950; P:response to stress; IDA. DR GO; GO:0042060; P:wound healing; IDA. DR InterPro; IPR008351; JNK_MAPK. DR InterPro; IPR003527; MAP_kin. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR01772; JNKMAPKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Transferase; Serine/threonine-protein kinase; Developmental protein; KW ATP-binding; Phosphorylation. FT DOMAIN 24 320 PROTEIN KINASE. FT NP_BIND 31 36 ATP (BY SIMILARITY). FT BINDING 53 53 ATP (BY SIMILARITY). FT ACT_SITE 149 149 BY SIMILARITY. FT MOD_RES 181 181 PHOSPHORYLATION (ACTIVATES THE KINASE) FT (BY SIMILARITY). FT MOD_RES 183 183 PHOSPHORYLATION (ACTIVATES THE KINASE) FT (BY SIMILARITY). FT MUTAGEN 225 225 G->E: IN BSK-1; DEFECT IN DORSAL CLOSURE. FT MUTAGEN 316 372 MISSING: IN BSK-2; DEFECT IN DORSAL FT CLOSURE. FT CONFLICT 331 372 APAPEPYDHSVDEREHTVEQWKELIYEEVMDYEAHNTNNRT FT R -> RPLRSHMITAWTKGNTLWSSGRS (IN REF. 2). SQ SEQUENCE 372 AA; 43027 MW; 96662B278ABCCA19 CRC64; MTTAQHQHYT VEVGDTNFTI HSRYINLRPI GSGAQGIVCA AYDTITQQNV AIKKLSRPFQ NVTHAKRAYR EFKLMKLVNH KNIIGLLNAF TPQRNLEEFQ DVYLVMELMD ANLCQVIQMD LDHDRMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKAD CTLKILDFGL ARTAGTTFMM TPYVVTRYYR APEVILGMGY TENVDIWSVG CIMGEMIRGG VLFPGTDHID QWNKIIEQLG TPSPSFMQRL QPTVRNYVEN RPRYTGYSFD RLFPDGLFPN DNNQNSRRKA SDARNLLSKM LVIDPEQRIS VDEALKHEYI NVWYDAEEVD APAPEPYDHS VDEREHTVEQ WKELIYEEVM DYEAHNTNNR TR // ID K10_DROME STANDARD; PRT; 463 AA. AC P13468; O46075; Q9W505; DT 01-JAN-1990 (Rel. 13, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-binding protein K10 (Female sterile protein K10). GN FS(1)K10 OR EG:30B8.5 OR CG3218. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Prost E., Deryckere F., Roos C., Haenlin M., Pantesco V., RA Mohier V.; RT "Role of the oocyte nucleus in determination of the dorsoventral RT polarity of Drosophila as revealed by molecular analysis of the K10 RT gene."; RL Genes Dev. 2:891-900(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY HAVE A REGULATORY FUNCTION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12836; CAA31321.1; -. DR EMBL; AL009195; CAA15702.1; -. DR EMBL; AE003423; AAF45758.1; -. DR EMBL; AY060415; AAL25454.1; -. DR PIR; T13425; T13425. DR FlyBase; FBgn0000810; fs(1)K10. DR GO; GO:0005634; C:nucleus; IDA. KW DNA-binding; Nuclear protein; Repeat. FT DOMAIN 87 142 7 X APPROXIMATE TANDEM REPEATS. FT REPEAT 87 94 1. FT REPEAT 95 102 2. FT REPEAT 103 110 3. FT REPEAT 111 118 4. FT REPEAT 119 126 5. FT REPEAT 127 134 6. FT REPEAT 135 142 7. FT DOMAIN 284 290 POLY-PRO. FT DNA_BIND 397 416 H-T-H MOTIF (POTENTIAL). FT CONFLICT 277 278 PM -> HH (IN REF. 1). FT CONFLICT 282 286 GGPPP -> VDHHR (IN REF. 1). SQ SEQUENCE 463 AA; 51267 MW; D03C097192D1FDD0 CRC64; MVSKNQFYQN WTMQSQQQHP HQMQQQFQQQ QQPNLQHRNN QSNNNNCNNN PRAAAAPYRK PFRSGKINSG PGGNGNGNRV NGNNQMMFSS SQMPSDPLYI DFSSPPPGFK HNQVGSPKKK SMKGIKQQQH PSPNQQQPPS PNQQQHPSPN QQQHPSPNQQ QHPNSNQQQH LSPNQQQGKM NNQNNNHMNQ SQQPFNNQMN GSDWQRHPGN NPNQIRGGFN GFQRGPPPNR PPPRLMMGPP MGPMGPGPRG PGPMGPGGPY PQMPFPPPVP GMRGPGPMGP MGGPPPPPPP LFMRRNGPGP GPMMGVPPPM HMMGPRMPPR GIPPVGPYGP MNMNGGRIMK PNPKLIKQVV KGKSSIKTLK NLINQYPIEK PWVTDEIRSE HDKKVDIENR LKGHKDDELF AQYKGQRDKF VSLYEAAREE YLKQEAATVK AKDAKSDKDK NAISSQSAAP KAGSAKDATI PNP // ID K6PF_DROME STANDARD; PRT; 787 AA. AC P52034; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 6-phosphofructokinase (EC 2.7.1.11) (Phosphofructokinase) DE (Phosphohexokinase). GN PFK. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95014229; PubMed=7929140; RA Currie P.D., Sullivan D.T.; RT "Structure and expression of the gene encoding phosphofructokinase RT (PFK) in Drosophila melanogaster."; RL J. Biol. Chem. 269:24679-24687(1994). CC -!- CATALYTIC ACTIVITY: ATP + D-FRUCTOSE 6-PHOSPHATE = ADP + D- CC FRUCTOSE 1,6-BISPHOSPHATE. CC -!- PATHWAY: KEY CONTROL STEP OF GLYCOLYSIS. CC -!- SIMILARITY: BELONGS TO THE PHOSPHOFRUCTOKINASE FAMILY. TWO DOMAINS CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L27653; AAA62385.1; -. DR PIR; A55034; A55034. DR HSSP; P00512; 3PFK. DR FlyBase; FBgn0003071; Pfk. DR InterPro; IPR000023; Ppfruckinase. DR Pfam; PF00365; PFK; 2. DR PIRSF; PIRSF000533; PFK_euk; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR ProDom; PD000707; Ppfruckinase; 2. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2. KW Kinase; Transferase; Glycolysis; Repeat. SQ SEQUENCE 787 AA; 86911 MW; 17247938FE75E436 CRC64; MNSEINQRFL ARGSQKDKGL AVFTSGGDSQ GMNAAVRACV RMAIYLGCKV YFIREGYQGM VDGGDCIRKS NWASVSSIIP FVGWHHPLLR PLPDFRERQG RLKAANNLIQ RGITNLVVIG GDGSLTGANL LPQEWSSLLD ELVKNKTITT EQQEKFNVLH MLGLVGSIDN DFCGTDMTIG TDTALHRIIE QSKAKVQSPV QPNSHQRTFI MEGQVSHCGY LALVGGLACE AIHIHPNAPG RLGQTGSALS WTQRSAGQRL NIVIVAEGAM DREGHPITAE DVKKVIDERL KHDARITVLG HVQRGGNPSA FDRFLACRMG AEPLWPLMEA TKDSVPVVIS LDGNQAVRVP LMECVERTQA GKAMAEKRWA DAVNVRGRSF ERNLETYKML TRLKPPKENF DADGKGIEGY RLAVMHIGAP ACGMNAAVRS FVRNAIYRGD VVYGINDGVE GLIARNVREL GWSDVSGWVG QGGAYLGSKR TLPEGKFKEI AARLKEFKIQ GLLIIGGFES YHAAGQIADQ RTTTHSFCIP IVVIPSTISN NVPGTEFSLG CDTGLNEITE ICDRIRQSAQ GTKRRVFVIE TMGGYCGYLP PLAGLAGGAD AAYIYEEKFS IKELQQDVYH MPPRWPRRLP RSNPANEKAS ENYSTDFIYR LYSEEGKGLF TCRMNILGHM QQGGSPTPFD RNMGTKMAAK CVDCWPPRSR RTSTANGVVN CKSPDTATLL GIVSRQYRFS PLVDLIAETN FDQRIPKKQW WLRLRPLLRI LAKHDSAYEE EGMYITVEEE CDTDAVA // ID KAPC_DROME STANDARD; PRT; 352 AA. AC P12370; Q9VL99; DT 01-OCT-1989 (Rel. 12, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE cAMP-dependent protein kinase catalytic subunit (EC 2.7.1.37) (PKA C). GN PKA-C1 OR CDKA OR DC0 OR CG4379. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88115281; PubMed=2828348; RA Foster J.L., Higgins G.C., Jackson R.F.; RT "Cloning, sequence, and expression of the Drosophila cAMP-dependent RT protein kinase catalytic subunit gene."; RL J. Biol. Chem. 263:1676-1681(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89107990; PubMed=3215511; RA Kalderon D., Rubin G.M.; RT "Isolation and characterization of Drosophila cAMP-dependent protein RT kinase genes."; RL Genes Dev. 2:1539-1556(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ENZYME REGULATION: ACTIVATED BY CAMP. CC -!- SUBUNIT: COMPOSED OF TWO REGULATORY CHAINS AND TWO CATALYTIC CC CHAINS. CC -!- TISSUE SPECIFICITY: MORE ABUNDANT IN ADULT HEAD THAN ADULT BODY. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CAMP CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18655; AAA28412.1; -. DR EMBL; X16969; CAA34840.1; -. DR EMBL; AE003625; AAF52797.1; -. DR PIR; C31751; C31751. DR HSSP; P05132; 1ATP. DR FlyBase; FBgn0000273; Pka-C1. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0007448; P:anterior/posterior pattern formation, imagi...; IMP. DR GO; GO:0019933; P:cAMP-mediated signaling; NAS. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); NAS. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0007611; P:learning and/or memory; NAS. DR GO; GO:0007480; P:leg morphogenesis (sensu Holometabola); NAS. DR GO; GO:0045475; P:locomotor rhythm; NAS. DR GO; GO:0008355; P:olfactory learning; NAS. DR GO; GO:0007314; P:oocyte anterior/posterior axis determination; IMP. DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP. DR GO; GO:0008359; P:regulation of bicoid mRNA localization; IMP. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localiz...; IMP. DR GO; GO:0045473; P:response to ethanol (sensu Insecta); NAS. DR GO; GO:0007622; P:rhythmic behavior; IMP. DR GO; GO:0007476; P:wing morphogenesis; IMP. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00433; pkinase_C; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; cAMP; KW Phosphorylation; Myristate; Lipoprotein. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 N-myristoyl glycine (By similarity). FT DOMAIN 45 299 PROTEIN KINASE. FT NP_BIND 51 59 ATP (BY SIMILARITY). FT BINDING 74 74 ATP (BY SIMILARITY). FT ACT_SITE 168 168 BY SIMILARITY. SQ SEQUENCE 352 AA; 40707 MW; 88E42BCFA95E9640 CRC64; GNNATTSNKK VDAAETVKEF LEQAKEEFED KWRRNPTNTA ALDDFERIKT LGTGSFGRVM IVQHKPTKDY YAMKILDKQK VVKLKQVEHT LNEKRILQAI QFPFLVSLRY HFKDNSNLYM VLEYVPGGEM FSHLRKVGRF SEPHSRFYAA QIVLAFEYLH YLDLIYRDLK PENLLIDSQG YLKVTDFGFA KRVKGRTWTL CGTPEYLAPE IILSKGYNKA VDWWALGVLV YEMAAGYPPF FADQPIQIYE KIVSGKVRFP SHFGSDLKDL LRNLLQVDLT KRYGNLKAGV NDIKNQKWFA STDWIAIFQK KIEAPFIPRC KGPGDTSNFD DYEEEALRIS STEKCAKEFA EF // ID KAPR_DROME STANDARD; PRT; 376 AA. AC P16905; Q8IGP3; Q8IPU2; Q8MR47; Q95TK7; Q9VPA6; DT 01-AUG-1990 (Rel. 15, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE cAMP-dependent protein kinase regulatory chain type I (DRI class I to DE class IV). GN PKA-R1 OR CDKR OR CG3263. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3). RC STRAIN=Canton-S; RX MEDLINE=89107990; PubMed=3215511; RA Kalderon D., Rubin G.M.; RT "Isolation and characterization of Drosophila cAMP-dependent protein RT kinase genes."; RL Genes Dev. 2:1539-1556(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3). RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBUNIT: TETRAMER, COMPOSED OF 2 REGULATORY (R) AND 2 CATALYTIC CC (C) SUBUNITS. IN THE PRESENCE OF CAMP IT DISSOCIATES INTO 2 ACTIVE CC MONOMERIC C SUBUNITS AND AN R DIMER. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=DRI-1, A, C; CC IsoId=P16905-1; Sequence=Displayed; CC Name=2; Synonyms=DRI-2, D; CC IsoId=P16905-2; Sequence=VSP_002795; CC Note=Ref.1 isoform 2 (CAA34837) is in conflict in position(s): CC 1:MPK->M; CC Name=3; Synonyms=DRI-3-4, B; CC IsoId=P16905-3; Sequence=VSP_002796; CC -!- PTM: THE PSEUDOPHOSPHORYLATION SITE BINDS TO THE SUBSTRATE-BINDING CC REGION OF THE CATALYTIC CHAIN BUT IS NOT PHOSPHORYLATED. THE CC PHYSIOLOGICAL SIGNIFICANCE OF PHOSPHORYLATIONS BY OTHER KINASES IS CC UNCLEAR. CC -!- MISCELLANEOUS: BY ANALOGY WITH MAMMALIAN RII PROTEIN, BOTH CC TRUNCATED DROSOPHILA RI PROTEINS (RI CLASS II AND RI CLASS III/IV) CC WOULD BE EXPECTED TO RETAIN DOMAINS FOR BINDING OF CATALYTIC CC SUBUNIT (C) AND CAMP BUT ONLY THE FULL-LENGTH ANALOG (CLASS I) CC WOULD RETAIN A DIMERIZATION DOMAIN. CC -!- SIMILARITY: CONTAINS 2 CYCLIC NUCLEOTIDE-BINDING DOMAINS. CC -!- SIMILARITY: BELONGS TO THE CAMP-DEPENDENT KINASE REGULATORY CHAIN CC FAMILY. CC -!- CAUTION: REF.4 (AAN71433) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC A FRAMESHIFT IN POSITION 189. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16963; CAA34837.1; -. DR EMBL; X16964; CAA34837.1; JOINED. DR EMBL; X16970; CAA34841.1; -. DR EMBL; X16971; CAA34841.1; JOINED. DR EMBL; X16966; CAA34838.1; -. DR EMBL; X16968; CAA34839.1; -. DR EMBL; AE003592; AAF51649.3; -. DR EMBL; AE003592; AAG22179.2; -. DR EMBL; AE003592; AAN12147.1; -. DR EMBL; AY058709; AAL13938.1; -. DR EMBL; AY122131; AAM52643.1; -. DR EMBL; BT001678; AAN71433.1; ALT_FRAME. DR PIR; A31751; OKFF1R. DR HSSP; P00514; 1APK. DR FlyBase; FBgn0000275; Pka-R1. DR GO; GO:0008603; F:cAMP-dependent protein kinase, intrinsic re...; IMP. DR GO; GO:0007015; P:actin filament organization; IMP. DR GO; GO:0019933; P:cAMP-mediated signaling; NAS. DR GO; GO:0007591; P:molting cycle (sensu Insecta); IMP. DR GO; GO:0008355; P:olfactory learning; IMP. DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP. DR InterPro; IPR002373; cAMP_kin. DR InterPro; IPR000595; cNMP_binding. DR InterPro; IPR003117; RIIa. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF02197; RIIa; 1. DR PRINTS; PR00103; CAMPKINASE. DR SMART; SM00100; cNMP; 1. DR SMART; SM00394; RIIa; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. KW cAMP-binding; Phosphorylation; Repeat; Alternative splicing. FT DOMAIN 1 131 DIMERIZATION AND PHOSPHORYLATION. FT SITE 91 95 PSEUDOPHOSPHORYLATION MOTIF. FT NP_BIND 132 249 CAMP. FT NP_BIND 250 376 CAMP. FT REPEAT 132 249 1. FT REPEAT 250 376 2. FT DISULFID 17 17 INTERCHAIN (WITH C-38) (BY SIMILARITY). FT DISULFID 38 38 INTERCHAIN (WITH C-17) (BY SIMILARITY). FT MOD_RES 96 96 PHOSPHORYLATION (BY SIMILARITY). FT BINDING 197 197 CAMP. FT BINDING 206 206 CAMP. FT BINDING 321 321 CAMP. FT BINDING 330 330 CAMP. FT VARSPLIC 1 58 MSYMMAKTLEEQSLRECEHYIQTHGIQRVLKDCIVQLCVCR FT PENPVQFLRQYFQKLER -> MPK (in isoform 2). FT /FTId=VSP_002795. FT VARSPLIC 1 80 Missing (in isoform 3). FT /FTId=VSP_002796. FT CONFLICT 303 303 E -> EQ (IN REF. 1). SQ SEQUENCE 376 AA; 42239 MW; F7B89D9C3EC313A5 CRC64; MSYMMAKTLE EQSLRECEHY IQTHGIQRVL KDCIVQLCVC RPENPVQFLR QYFQKLEREQ VKLDASRQVI SPDDCEDLSP MPQTAAPPVR RRGGISAEPV TEEDATNYVK KVVPKDYKTM NALSKAIAKN VLFAHLDESE RSDIFDAMFP VNHIAGENII QQGDEGDNFY VIDVGEVDVF VNSELVTTIS EGGSFGELAL IYGTPRAATV RAKTDVKLWG IDRDSYRRIL MGSTIRKRKM YEEFLSRVSI LESLDKWERL TVADSLETCS FDDGETIVKQ GAAGDDFYII LEGCAVVLQQ RSEGEDPAEV GRLGSSDYFG EIALLLDRPR AATVVARGPL KCVKLDRARF ERVLGPCADI LKRNITQYNS FVSLSV // ID KARG_DROME STANDARD; PRT; 354 AA. AC P48610; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Arginine kinase (EC 2.7.3.3) (AK). GN ARGK. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Hecht L.B., Scott L.M., Collier G.E.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-ARGININE = ADP + N-PHOSPHO-L-ARGININE. CC -!- SIMILARITY: BELONGS TO THE ATP:GUANIDO PHOSPHOTRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U26939; AAA68172.1; -. DR EMBL; U26940; AAA68173.1; -. DR HSSP; P51541; 1BG0. DR FlyBase; FBgn0000116; Argk. DR InterPro; IPR000749; ATP-gua_Ptrans. DR Pfam; PF00217; ATP-gua_Ptrans; 1. DR Pfam; PF02807; ATP-gua_PtransN; 1. DR PROSITE; PS00112; GUANIDO_KINASE; 1. KW Transferase; Kinase. FT ACT_SITE 271 271 BY SIMILARITY. SQ SEQUENCE 354 AA; 39623 MW; A11516D7E5BA4786 CRC64; MVDAAVLAKL EEGYAKLAAS DSKSLLKKYL TKEVFDNLKN KGHAHLQVDP ADVIQSGLEN HDSASAIYAP DAEAYTVFAD LFDPFIEDYH GGFKKTDKHP ASNFGDVSTF GNVDPTNEYV ISTRVRCGRS MQGYPFNPCL TEAQYKEMES KVSSTLSGLE GELKGKFYPL TGMEKAVQQQ LIDDHFLFKE GDRFLQAANA CRFWPSGRGI YHNDAKTFLV WCNEEDHLRI ISMQQGGDLG QIYKRLVTAV NEIEKRVPFS HDDRLGFLTF CPTNLGTTIL ASVHIKVPKL PSNKAKLEEV AAKYNLQVAN PREHTEAEGG SYDISNKRRM GLTEFEAVKE MYDGITELIK LEKS // ID KC1A_DROME STANDARD; PRT; 337 AA. AC P54367; Q9VYK2; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Casein kinase I, alpha isoform (EC 2.7.1.-) (CKI-alpha) (DmCK1). GN CKI-ALPHA OR CKI OR CG2028. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Glover C.V.C., Kandala G.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96429306; PubMed=8832407; RA Santos J.A., Logarinho E., Tapia C., Allende C.C., Allende J.E., RA Sunkel C.E.; RT "The casein kinase 1 alpha gene of Drosophila melanogaster is RT developmentally regulated and the kinase activity of the protein RT induced by DNA damage."; RL J. Cell Sci. 109:1847-1856(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CASEIN KINASES ARE OPERATIONALLY DEFINED BY THEIR CC PREFERENTIAL UTILIZATION OF ACIDIC PROTEINS SUCH AS CASEINS AS CC SUBSTRATES. IT CAN PHOSPHORYLATE A LARGE NUMBER OF PROTEINS. CC PARTICIPATES IN WNT SIGNALING (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CASEIN KINASE I SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U55848; AAB16904.1; -. DR EMBL; X94695; CAA64358.1; -. DR EMBL; AE003490; AAF48193.1; -. DR EMBL; AY069346; AAL39491.1; -. DR HSSP; Q06486; 1CKJ. DR FlyBase; FBgn0015024; CkI-alpha. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004672; F:protein kinase activity; IDA. DR GO; GO:0006281; P:DNA repair; IDA. DR GO; GO:0030163; P:protein catabolism; NAS. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Wnt signaling pathway; Transferase; Serine/threonine-protein kinase; KW ATP-binding. FT DOMAIN 20 288 PROTEIN KINASE. FT NP_BIND 26 34 ATP (BY SIMILARITY). FT BINDING 49 49 ATP (BY SIMILARITY). FT ACT_SITE 139 139 BY SIMILARITY. FT CONFLICT 1 3 MISSING (IN REF. 2). FT CONFLICT 331 337 GKPLIAD -> ASP (IN REF. 2). SQ SEQUENCE 337 AA; 39535 MW; 495144945093E69D CRC64; MDKMRILKES RPEIIVGGKY RVIRKIGSGS FGDIYLGMSI QSGEEVAIKM ESAHARHPQL LYEAKLYRIL SGGVGFPRIR HHGKEKNFNT LVMDLLGPSL EDLFNFCTRH FTIKTVLMLV DQMIGRLEYI HLKCFIHRDI KPDNFLMGIG RHCNKLFLID FGLAKKFRDP HTRHHIVYRE DKNLTGTARY ASINAHLGIE QSRRDDMESL GYVMMYFNRG VLPWQGMKAN TKQQKYEKIS EKKMSTPIEV LCKGSPAEFS MYLNYCRSLR FEEQPDYMYL RQLFRILFRT LNHQYDYIYD WTMLKQKTHQ GQPNPAILLE QLDKDKEKQN GKPLIAD // ID KC2A_DROME STANDARD; PRT; 335 AA. AC P08181; Q9W5T2; DT 01-AUG-1988 (Rel. 08, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Casein kinase II, alpha chain (EC 2.7.1.37) (CK II alpha subunit). GN CKII-ALPHA OR CASK-II-A OR CG17520. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88065475; PubMed=3119988; RA Saxena A., Padmanabha R., Glover C.V.C.; RT "Isolation and sequencing of cDNA clones encoding alpha and beta RT subunits of Drosophila melanogaster casein kinase II."; RL Mol. Cell. Biol. 7:3409-3417(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-41. RX MEDLINE=87109340; PubMed=3468112; RA Padmanabha R., Glover C.V.C.; RT "Casein kinase II of yeast contains two distinct alpha polypeptides RT and an unusually large beta subunit."; RL J. Biol. Chem. 262:1829-1835(1987). CC -!- FUNCTION: CASEIN KINASES ARE OPERATIONALLY DEFINED BY THEIR CC PREFERENTIAL UTILIZATION OF ACIDIC PROTEINS SUCH AS CASEINS CC AS SUBSTRATES. THE ALPHA CHAIN CONTAINS THE CATALYTIC SITE. CC MAY PARTICIPATE IN WNT SIGNALING. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA CHAINS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CK2 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16534; AAA28429.1; -. DR EMBL; AE002786; AAF45439.1; -. DR PIR; A26688; A26688. DR HSSP; P28523; 1A6O. DR FlyBase; FBgn0000258; CkII-alpha. DR GO; GO:0005829; C:cytosol; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0005956; C:protein kinase CK2 complex; IDA. DR GO; GO:0004682; F:protein kinase CK2 activity; IDA. DR GO; GO:0007222; P:frizzled signaling pathway; IDA. DR GO; GO:0045475; P:locomotor rhythm; IMP. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Wnt signaling pathway. FT INIT_MET 0 0 FT DOMAIN 36 321 PROTEIN KINASE. FT NP_BIND 42 50 ATP (BY SIMILARITY). FT BINDING 65 65 ATP (BY SIMILARITY). FT ACT_SITE 153 153 BY SIMILARITY. SQ SEQUENCE 335 AA; 39828 MW; 46A478E30726D85A CRC64; TLPSAARVYT DVNAHKPDEY WDYENYVVDW GNQDDYQLVR KLGRGKYSEV FEAINITTTE KCVVKILKPV KKKKIKREIK ILENLRGGTN IITLLAVVKD PVSRTPALIF EHVNNTDFKQ LYQTLTDYEI RYYLFELLKA LDYCHSMGIM HRDVKPHNVM IDHENRKLRL IDWGLAEFYH PGQEYNVRVA SRYFKGPELL VDYQMYDYSL DMWSLGCMLA SMIFRKEPFF HGHDNYDQLV RIAKVLGTEE LYAYLDKYNI DLDPRFHDIL QRHSRKRWER FVHSDNQHLV SPEALDFLDK LLRYDHVDRL TAREAMAHPY FLPIVNGQMN PNNQQ // ID KC2B_DROME STANDARD; PRT; 215 AA. AC P08182; Q9VYU4; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Casein kinase II beta chain (CK II). GN CKII-BETA OR CASK-II-B OR CG15224. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88065475; PubMed=3119988; RA Saxena A., Padmanabha R., Glover C.V.C.; RT "Isolation and sequencing of cDNA clones encoding alpha and beta RT subunits of Drosophila melanogaster casein kinase II."; RL Mol. Cell. Biol. 7:3409-3417(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Glover C.V.C., Beckman J.S., Bidwai A.P., Carlson L.K., RA Cerjan C.M., Crawford M.J., McCann R.O., Saxena A., Zhao W.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PARTICIPATES IN WNT SIGNALING (BY SIMILARITY). PLAYS A CC COMPLEX ROLE IN REGULATING THE BASAL CATALYTIC ACTIVITY OF THE CC ALPHA SUBUNIT. CC -!- SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA CHAINS. CC -!- PTM: PHOSPHORYLATED BY ALPHA CHAIN (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CASEIN KINASE 2 BETA CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16535; AAA28430.1; -. DR EMBL; U52952; AAC13880.1; -. DR EMBL; AE003487; AAF48092.1; -. DR FlyBase; FBgn0000259; CkII-beta. DR GO; GO:0005829; C:cytosol; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0005956; C:protein kinase CK2 complex; IDA. DR GO; GO:0008605; F:protein kinase CK2, intrinsic regulator act...; IDA. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR InterPro; IPR000704; CAS_kinase_II. DR Pfam; PF01214; CK_II_beta; 1. DR PRINTS; PR00472; CASNKINASEII. DR ProDom; PD003829; CAS_kinase_II; 1. DR PROSITE; PS01101; CK2_BETA; 1. KW Transferase; Serine/threonine-protein kinase; Phosphorylation; KW Wnt signaling pathway. FT MOD_RES 2 2 PHOSPHORYLATION (AUTO-) (PROBABLE). FT DOMAIN 55 64 ASP/GLU-RICH (ACIDIC). SQ SEQUENCE 215 AA; 24829 MW; 51D375BCEC4AC06F CRC64; MSSSEEVSWV TWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPNYRQAL DMILDLEPED ELEDNPLQSD MTEQAAEMLY GLIHARYILT NRGIAQMIEK YQTGDFGHCP RVYCESQPML PLGLSDIPGE AMVKTYCPKC IDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPT NQFVPRLYGF KIHSLAYQIQ LQAAANFKMP LRAKN // ID KC2C_DROME STANDARD; PRT; 219 AA. AC O96863; Q9V919; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Casein kinase II beta' chain (CK II). GN CKII-BETA-2 OR CG8914. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20393234; PubMed=10329473; RA Bidwai A.P., Zhao W., Glover C.V.C.; RT "A gene located at 56F1-2 in Drosophila melanogaster encodes a novel RT metazoan beta-like subunit of casein kinase II."; RL Mol. Cell Biol. Res. Commun. 1:21-28(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PARTICIPATES IN WNT SIGNALING (BY SIMILARITY). PLAYS A CC COMPLEX ROLE IN REGULATING THE BASAL CATALYTIC ACTIVITY OF THE CC ALPHA SUBUNIT. CC -!- SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA' CHAINS. CC -!- PTM: PHOSPHORYLATED BY ALPHA CHAIN (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CASEIN KINASE 2 BETA CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U51209; AAD00080.1; -. DR EMBL; AE003792; AAF57483.1; -. DR FlyBase; FBgn0026136; CkII-beta-2. DR InterPro; IPR000704; CAS_kinase_II. DR Pfam; PF01214; CK_II_beta; 1. DR PRINTS; PR00472; CASNKINASEII. DR ProDom; PD003829; CAS_kinase_II; 1. DR PROSITE; PS01101; CK2_BETA; 1. KW Transferase; Serine/threonine-protein kinase; Phosphorylation; KW Wnt signaling pathway. FT MOD_RES 2 2 PHOSPHORYLATION (AUTO-) (PROBABLE). FT DOMAIN 63 71 ASP/GLU-RICH (ACIDIC). SQ SEQUENCE 219 AA; 24966 MW; E43E80AA465DB666 CRC64; MTDSDESSWI HWFCKQRGNE FFCEVDEEYI QDKFNLNFLD SNVKNYKCAL EVILDLNPGS ASEDPAEPEL EASAEKLYGL IHARFILTNR GIELMLDKYN KGEFGTCPRA FCHSQPVLPI GLSDNPGEDM VRIYCPKCND VYIPKASRHS NLDGAFFGTG FPHMFFMEKP DARPKRAKQK FVPRLYGFKI HPTAYRTAAE IQKDVTMTPV GEIDSPSHI // ID KDC1_DROME STANDARD; PRT; 376 AA. AC P16911; P16910; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Protein kinase DC1 (EC 2.7.1.37). GN PKA-C2 OR DC1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; RX MEDLINE=89107990; PubMed=3215511; RA Kalderon D., Rubin G.M.; RT "Isolation and characterization of Drosophila cAMP-dependent protein RT kinase genes."; RL Genes Dev. 2:1539-1556(1988). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=P16911-1; Sequence=Displayed; CC Name=A; CC IsoId=P16911-2; Sequence=VSP_004911, VSP_004912; CC -!- TISSUE SPECIFICITY: MORE ABUNDANT IN ADULT BODY THAN ADULT HEAD. CC -!- DEVELOPMENTAL STAGE: IN EMBRYOS, PUPAE AND ADULTS. CC -!- SIMILARITY: STRONG TO CAMP-DEPENDENT PROTEIN KINASE CATALYTIC CC SUBUNIT (DC0). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16960; CAA34833.1; -. DR EMBL; X16960; CAA34834.1; -. DR HSSP; P05132; 1CTP. DR FlyBase; FBgn0000274; Pka-C2. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Alternative splicing. FT DOMAIN 45 298 PROTEIN KINASE. FT NP_BIND 51 59 ATP (BY SIMILARITY). FT BINDING 74 74 ATP (BY SIMILARITY). FT ACT_SITE 168 168 BY SIMILARITY. FT VARSPLIC 285 354 KLERRLQRREESSVVPGRRLVWHSQPGSHRPLPAHHFRRRR FT SVELRELRVQGSVQVPNKPPSRIVCEFLN -> LGNSNDGS FT SDVKSHPWFQGVDWFGILNQEVTAPYQPTISGAEDLSNFEN FT FEFKDRYKSRINRHPELFANF (in isoform A). FT /FTId=VSP_004911. FT VARSPLIC 355 376 Missing (in isoform A). FT /FTId=VSP_004912. SQ SEQUENCE 376 AA; 44109 MW; 41AFDA0846FADCCD CRC64; MSQHTSQYVF NSKEDYNVIL DNMSREFEER WNHQTQSPYT NLENYITRAV LGNGSFGTVM LVREKSGKNY YAAKMMSKED LVRLKQVAHV HNEKHVLNAA RFPFLIYLVD STKCFDYLYL ILPLVNGGEL FSYHRRVRKF NEKHARFYAA QVALALEYMH KMHLMYRDLK PENILLDQRG YIKITDFGFT KRVDGRTSTL CGTPEYLAPE IVQLRPYNKS VDWWAFGILV YEFVAGRSPF AIHNRDVILM YSKICICDYK MPSYFTSQLR SLVESLMQVD TSKRKLERRL QRREESSVVP GRRLVWHSQP GSHRPLPAHH FRRRRSVELR ELRVQGSVQV PNKPPSRIVC EFLNVNVSFE IVVFFSVCLI SRGALS // ID KDC2_DROME STANDARD; PRT; 502 AA. AC P16912; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Protein kinase DC2 (EC 2.7.1.-). GN PKA-C3 OR DC2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89107990; PubMed=3215511; RA Kalderon D., Rubin G.M.; RT "Isolation and characterization of Drosophila cAMP-dependent protein RT kinase genes."; RL Genes Dev. 2:1539-1556(1988). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- TISSUE SPECIFICITY: MORE ABUNDANT IN ADULT HEAD THAN ADULT BODY. CC -!- DEVELOPMENTAL STAGE: IN EMBRYONS, PUPAE AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CAMP CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16961; CAA34835.1; -. DR HSSP; P05132; 1ATP. DR FlyBase; FBgn0000489; Pka-C3. DR GO; GO:0008602; F:cAMP-dependent protein kinase, intrinsic ca...; IDA. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00433; pkinase_C; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding. FT DOMAIN 193 447 PROTEIN KINASE. FT NP_BIND 199 207 ATP (BY SIMILARITY). FT BINDING 222 222 ATP (BY SIMILARITY). FT ACT_SITE 316 316 BY SIMILARITY. SQ SEQUENCE 502 AA; 56960 MW; CAAC474A5A40193D CRC64; MSTATCARFC TPLSSGTAGS TSKLTTGNGS GNTMTSAYKK KIPSNNSTTA NDSSNTETTF TFKLGRSNGR SSSNVASSES SDPLESDYSE EDPEQEQQRP DPATKSRSSS TATTTTTSSA DHDNDVDEED EEDDEDEGEG NGRDADDATH DSSESIEEDD GNETDDEEDD DESEESSSVQ TAKGVRKYHL DDYQIIKTVG TGTFGRVCLC RDRISEKYCA MKILAMTEVI RLKQIEHVKN ERNILREIRH PFVISLEWST KDDSNLYMIF DYVCGGELFT YLRNAGKFTS QTSNFYAAEI VSALEYLHSL QIVYRDLKPE NLLINRDGHL KITDFGFAKK LRDRTWTLCG TPEYIAPEII QSKGHNKAVD WWALGVLIYE MLVGYPPFYD EQPFGIYEKI LSGKIEWERH MDPIAKDLIK KLLVNDRTKR LGNMKNGADD VKRHRWFKHL NWNDVYSKKL KPPILPDVHH DGDTKNFDDY PEKDWKPAKA VDQRDLQYFN DF // ID KDGE_DROME STANDARD; PRT; 1454 AA. AC Q09103; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Eye-specific diacylglycerol kinase (EC 2.7.1.107) (Retinal DE degeneration A protein) (Diglyceride kinase 2) (DGK 2) (DAG kinase 2). GN RDGA OR DGK2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=94068563; PubMed=8248222; RA Masai I., Okazaki A., Hosoya T., Hotta Y.; RT "Drosophila retinal degeneration A gene encodes an eye-specific RT diacylglycerol kinase with cysteine-rich zinc-finger motifs and RT ankyrin repeats."; RL Proc. Natl. Acad. Sci. U.S.A. 90:11157-11161(1993). CC -!- FUNCTION: REQUIRED FOR THE MAINTENANCE OF THE PHOTORECEPTOR. ITS CC ABSENCE LEADS TO RHABDOMERE DEGENERATION DUE TO DEFECTIVE CC PHOSPHOLIPID TURNOVER. CC -!- CATALYTIC ACTIVITY: ATP + 1,2-DIACYLGLYCEROL = ADP + 1,2- CC DIACYLGLYCEROL 3-PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED. CC -!- TISSUE SPECIFICITY: EXPRESSED SPECIFICALLY IN ADULT EYE. CC -!- DISEASE: MUTANTS OF THIS GENE ARE CHARACTERIZED BY HAVING CC PHOTORECEPTOR CELLS THAT DEVELOP NORMALLY BUT DEGENERATE RAPIDLY CC AFTER ECLOSION. CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC DIACYLGLYCEROL KINASE CC FAMILY. CC -!- SIMILARITY: CONTAINS 2 ZINC-DEPENDENT PHORBOL-ESTER AND DAG CC BINDING DOMAINS. CC -!- SIMILARITY: CONTAINS 4 ANK REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D17315; BAA04135.1; -. DR PIR; T13709; T13709. DR FlyBase; FBgn0003217; rdgA. DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IGI. DR GO; GO:0016056; P:rhodopsin mediated signaling; IMP. DR InterPro; IPR002110; ANK. DR InterPro; IPR002219; DAG_PE-bind. DR InterPro; IPR000756; DAGKa. DR InterPro; IPR001206; DAGKc. DR Pfam; PF00023; ank; 4. DR Pfam; PF00130; DAG_PE-bind; 1. DR Pfam; PF00609; DAGKa; 1. DR Pfam; PF00781; DAGKc; 1. DR ProDom; PD002939; DAGKa; 1. DR ProDom; PD005043; DAGKc; 1. DR SMART; SM00248; ANK; 2. DR SMART; SM00109; C1; 2. DR SMART; SM00045; DAGKa; 1. DR SMART; SM00046; DAGKc; 1. DR PROSITE; PS50088; ANK_REPEAT; 2. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; FALSE_NEG. DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; FALSE_NEG. KW Transferase; Kinase; ANK repeat; Repeat; Vision; KW Phorbol-ester binding. FT DOMAIN 592 642 PHORBOL-ESTER AND DAG BINDING 1. FT DOMAIN 662 719 PHORBOL-ESTER AND DAG BINDING 2. FT DOMAIN 807 935 CATALYTIC-A (POTENTIAL). FT DOMAIN 961 1115 CATALYTIC-B (POTENTIAL). FT REPEAT 1317 1346 ANK 1. FT REPEAT 1350 1379 ANK 2. FT REPEAT 1386 1415 ANK 3. FT REPEAT 1419 1448 ANK 4. FT DOMAIN 2 6 POLY-GLN. FT DOMAIN 24 39 THR-RICH. FT DOMAIN 110 115 POLY-SER. FT DOMAIN 227 231 POLY-GLU. FT DOMAIN 758 775 GLY-RICH. FT MUTAGEN 869 869 G->D: IN MUTANT RDGA2. SQ SEQUENCE 1454 AA; 159675 MW; CE4C81099FEA16AA CRC64; MQQQQQPSID QLPEPTASTS NSATTKPTIA TVTTSTTTTS GNNFHQQLQA TTAATMQRLR TTFTRSRTPT GAEMKMQNSL EVPKQVRSAS FDEMQLESQR ASSSLLKQQS SSSASADERS SEAGFLQVPL AAHQQRSHSF DSATASAGSD DSGTFLEVPR RLKARRSSST KTPPPCIHCH YLEEYERRMT AEQRYFIDHR ELTALSYTNT SSEASEDEDE VEGHNAEEEE EGSAAIEDAE EETTEAATEE ADEDPRTEVE SEHDHDPDDD AALEMDIRIG NMSQGSSIEE SRARLPRQMR RHTIGSSSVT SASEDEGLEG SDNGSPHFGN TLLPPQPTTP CGITFTLSPT NGDYPSPPHL PLDPGSPPIS PCSSNSGRLP ALAPIISTPC SSADADDAGA AMGLPVRARR RSISRQEAIF VEPTGNSLEN VSHEEVDKSN TKSSVDTADS LDEASTMATC GSPGAAGGSG ASSSHHNAFV VRDIYLMVPD LKRDRAASVD SCFSKLSSNA KTEELQPSAD GCFLTVPNIN ATRSRSVDIV LPTDEQARYK ALSMTGSTVT YADGRRTASA SNSRRPIRIV PDWTENAVQG EHYWKPTSAS GDLCCLNEEC IKSGQRMKCS ACQLVAHHNC IPFVNEKSTL ACKPTYRDVG IRQYREQTTT HHHWVHRNLE KGKCKQCGKA VQSKLFGSKE IVALACAWCH EIYHNKEACF NQAKIGEECR LGNYAPIIVP PSWIVKLPTK GNFKSSIRVS NKNNAASGSG GGGAGGGAGG GGGGGKSKKQ TQRRQKGKEE KKEPRAFIVK PIPSPEVIPV IVFINPKSGG NQGHKLLGKF QHLLNPRQVF DLTQGGPKMG LDMFRKAPNL RVLACGGDGT VGWVLSVLDQ IQPPLQPAPA VGVLPLGTGN DLARALGWGG GYTDEPIGKI LREIGMSQCV LMDRWRVKVT PNDDVTDDHV DRSKPNVPLN VINNYFSFGV DAHIALEFHE AREAHPERFN SRLRNKMYYG QMGGKDLILR QYRNLSQWVT LECDGQDFTG KLRDAGCHAV LFLNIPSYGG GTHPWNDSFG ASKPSIDDGL MEVVGLTTYQ LPMLQAGMHG TCICQCRKAR IITKRTIPMQ VDGEACRVKP SVIEIELLNK ALMLSKRKHG RGDVQVNPLE KMQLHILRVT MQQYEQYHYD KEMLRKLANK LGQIEIESQC DLEHVRNMLN TKFEESISYP KVSQDWCFID SCTAEHYFRI DRAQEHLHYI CDIAIDELYI LDHEAATMPQ TPDQERSFAA FSQRQAQNER RQMDQAQGRG PGSTDEDLQI GSKPIKVMKW KSPILEQTSD AILLAAQSGD LNMLRALHEQ GYSLQSVNKN GQTALHFACK YNHRDIVKYI IASATRRLIN MADKELGQTA LHIAAEQNRR DICVMLVAAG AHLDTLDSGG NTPMMVAFNK NANEIATYLE SKQGTQPVDG WLDD // ID KDGL_DROME STANDARD; PRT; 791 AA. AC Q01583; Q9V327; DT 01-JUL-1993 (Rel. 26, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Diacylglycerol kinase (EC 2.7.1.107) (Diglyceride kinase 1) (DGK 1) DE (DAG kinase 1). GN DGK OR DGK1 OR CG18654/CG1535. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92335231; PubMed=1321433; RA Masai I., Hosoya T., Kojima S., Hotta Y.; RT "Molecular cloning of a Drosophila diacylglycerol kinase gene that is RT expressed in the nervous system and muscle."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6030-6034(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 279-791 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93143713; PubMed=8380995; RA Harden N., Yap S.F., Chiam M.-A., Lim L.; RT "A Drosophila gene encoding a protein with similarity to RT diacylglycerol kinase is expressed in specific neurons."; RL Biochem. J. 289:439-444(1993). CC -!- FUNCTION: UPON CELL STIMULATION CONVERTS THE SECOND MESSENGER CC DIACYLGLYCEROL INTO PHOSPHATIDATE, INITIATING THE RESYNTHESIS CC OF PHOSPHATIDYLINOSITOLS AND ATTENUATING PROTEIN KINASE C CC ACTIVITY (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + 1,2-DIACYLGLYCEROL = ADP + 1,2- CC DIACYLGLYCEROL 3-PHOSPHATE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE NERVOUS SYSTEM AND MUSCLE. CC -!- DEVELOPMENTAL STAGE: DGK IS TRANSCRIBED IN THE EMBRYONIC, PUPAL CC AND ADULT STAGES, WITH LITTLE EXPRESSION DURING THE LARVAL CC STAGES. EXPRESSION IN LATE EMBRYOS IS SPECIFIC TO THE CENTRAL CC NERVOUS SYSTEM AND HEAD. CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC DIACYLGLYCEROL KINASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D11120; BAA01894.1; -. DR EMBL; AE003839; AAF59180.1; -. DR EMBL; X67335; CAA47750.1; -. DR PIR; A46140; A46140. DR FlyBase; FBgn0004568; Dgk. DR InterPro; IPR000756; DAGKa. DR InterPro; IPR001206; DAGKc. DR Pfam; PF00609; DAGKa; 1. DR Pfam; PF00781; DAGKc; 1. DR ProDom; PD002939; DAGKa; 1. DR ProDom; PD005043; DAGKc; 1. DR SMART; SM00045; DAGKa; 1. DR SMART; SM00046; DAGKc; 1. KW Transferase; Kinase. FT DOMAIN 311 372 THR-RICH. FT DOMAIN 401 405 POLY-ALA. FT DOMAIN 430 453 GLN-RICH. FT DOMAIN 534 539 POLY-GLN. FT DOMAIN 130 256 CATALYTIC-A (POTENTIAL). FT DOMAIN 564 755 CATALYTIC-B (POTENTIAL). FT CONFLICT 374 374 M -> T (IN REF. 1). FT CONFLICT 444 444 Q -> QQQQQ (IN REF. 3). SQ SEQUENCE 791 AA; 87297 MW; 9DFD00E280FD64A6 CRC64; MRWELRYGWQ IVTFRTNCAT AAAVACHQLL CPVSLTSAVE IMPNSFPPEG RRRERRSGNL VLRAGCCCIG KYFLHNRCAS SVKKECTLGE YSELIVPPTA ICPAVLDRQR SVNQAHKATH FQITPPDELS CPLLVFVNPK SGGRQGDRIL RKFQYMLNPR QVYDLSKGGP KEGLTLFKDL PRFRVICCGG DGTVGWVLEA MDSIELASQP AIGVIPLGTG NDLARCLRWG GGYEGENIPK LMDKFRRAST VMLDRWSIEV TNTPHSDDMR PKVTLHSNMQ KVIELSQSVV VDKSLMERFE EIQRQSKQVA TSMGTAASST SIMMASKTET EMETMATMEF GSSTTTTNRT TTTKSISMST FETQCLQQTL RTAMSSSSSN TSSGSPCNGN QDAETEVDSH AAAAADVREK SVPRRSGETE KQSLETLLLQ HKQQMQQQQQ QQQQGVTSLA VEEAATATPV GSNQSDNSSQ RNKQNNILKQ QITLSLDLSD HEDEPKDDGG GAGDGTKSNG NSIPATPATP ITPTTPNAAS SVLQQQQQQH LQFEQQQKPI KVQSDKDCTV PYNIINNYFS VGVDAAICVK FHLEREKNPH KFNSRMKNKL WYFEYATSET FAASCKNLHE SIEIVCDGVA LDLANGPHLQ GVALLNIPYT HGGSNLWGEH LSQKRIRKSA GPFGKSKKLR AGDKEFSATS FNSVDLSVAI QDFGDRLIEV IGLENCLHMG QVRTGLRASG RRLAQCSEVI IKTKKTFPMQ IDGEPWMQMP CTIKVTHKNQ VPMLMAPRSE KGRGFFNLLC S // ID KELC_DROME STANDARD; PRT; 1477 AA. AC Q04652; Q04653; Q86PA7; Q9VJA2; DT 01-FEB-1994 (Rel. 28, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ring canal kelch protein [Contains: Kelch short protein]. GN KEL OR CG7210. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=93201592; PubMed=8453663; RA Xue F., Cooley L.; RT "Kelch encodes a component of intercellular bridges in Drosophila egg RT chambers."; RL Cell 72:681-693(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP CHARACTERIZATION. RC TISSUE=Embryo; RX MEDLINE=97236487; PubMed=9118811; RA Robinson D.N., Cooley L.; RT "Examination of the function of two kelch proteins generated by stop RT codon suppression."; RL Development 124:1405-1417(1997). CC -!- FUNCTION: COMPONENT OF RING CANALS THAT REGULATES THE FLOW OF CC CYTOPLASM BETWEEN CELLS. MAY BE INVOLVED IN THE REGULATION OF CC CYTOPLASM FLOW FROM NURSE CELLS TO THE OOCYTE DURING OOGENESIS. CC BINDS ACTIN. CC -!- SUBCELLULAR LOCATION: INNER SURFACE OF CYTOPLASMIC BRIDGES OR RING CC CANALS PRESENT IN EGG CHAMBERS. SUBCORTICALLY IN IMAGINAL DISK CC EPITHELIA. CC -!- TISSUE SPECIFICITY: BOTH PROTEINS ARE EXPRESSED IN OVARIES, MALE CC TESTIS, OVARECTOMIZED FEMALES, CUTICLE, SALIVARY GLAND AND CC IMAGINAL DISKS. KELCH SHORT PROTEIN IS THE PREDOMINANT FORM AND CC IS ALSO EXPRESSED IN FAT BODIES. ON ENTRY INTO METAMORPHOSIS CC LEVELS OF FULL LENGTH PROTEIN INCREASE IN TESTIS AND IMAGINAL CC DISKS. CC -!- DEVELOPMENTAL STAGE: LARVAE, PUPAE AND ADULTS. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 6 KELCH REPEATS. CC -!- CAUTION: REF.5 BELIEVES RESIDUE 690 IS A SELENOCYSTEINE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08483; AAA53471.1; -. DR EMBL; L08483; AAA53472.2; -. DR EMBL; AE003657; AAF53651.1; -. DR EMBL; AE003657; AAN11182.2; -. DR EMBL; BT003250; AAO25007.1; ALT_SEQ. DR HSSP; Q05516; 1CS3. DR FlyBase; FBgn0001301; kel. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0007301; P:ovarian ring canal formation; IDA. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR006651; Kelch. DR InterPro; IPR006652; Kelch_rep. DR Pfam; PF00651; BTB; 1. DR Pfam; PF01344; Kelch; 6. DR PRINTS; PR00501; KELCHREPEAT. DR SMART; SM00225; BTB; 1. DR SMART; SM00612; Kelch; 6. DR PROSITE; PS50097; BTB; 1. KW Cytoskeleton; Actin-binding; Selenium; Selenocysteine; Kelch repeat; KW Repeat. FT CHAIN 1 1477 KELCH PROTEIN. FT CHAIN 1 689 KELCH SHORT PROTEIN. FT DOMAIN 157 223 BTB. FT REPEAT 404 449 KELCH 1. FT REPEAT 450 496 KELCH 2. FT REPEAT 498 543 KELCH 3. FT REPEAT 545 592 KELCH 4. FT REPEAT 594 639 KELCH 5. FT REPEAT 641 687 KELCH 6. FT DOMAIN 18 28 ASN-RICH. FT DOMAIN 29 87 GLN-RICH. FT DOMAIN 29 36 POLY-GLN. FT DOMAIN 78 83 POLY-GLN. FT SE_CYS 690 690 PROBABLE. FT CONFLICT 493 493 V -> A (IN REF. 1). FT CONFLICT 596 596 A -> R (IN REF. 1). FT CONFLICT 824 824 P -> L (IN REF. 1). FT CONFLICT 858 858 G -> D (IN REF. 1). FT CONFLICT 1083 1083 A -> R (IN REF. 1). FT CONFLICT 1086 1086 A -> G (IN REF. 1). SQ SEQUENCE 1477 AA; 160086 MW; 4851EEAE9D9DBA47 CRC64; MIALSALLTK YTIGIMSNLS NGNSNNNNQQ QQQQQQGQNP QQPAQNEGGA GAEFVAPPPG LGAAVGVAAM QQRNRLLQQQ QQQHHHHQNP AAEGSGLERG SCLLRYASQN SLDESSQKHV QRPNGKERGT VGQYSNEQHT ARSFDAMNEM RKQKQLCDVI LVADDVEIHA HRMVLASCSP YFYAMFTSFE ESRQARITLQ SVDARALELL IDYVYTATVE VNEDNVQVLL TAANLLQLTD VRDACCDFLQ TQLDASNCLG IREFADIHAC VELLNYAETY IEQHFNEVIQ FDEFLNLSHE QVISLIGNDR ISVPNEERVY ECVIAWLRYD VPMREQFTSL LMEHVRLPFL SKEYITQRVD KEILLEGNIV CKNLIIEALT YHLLPTETKS ARTVPRKPVG MPKILLVIGG QAPKAIRSVE WYDLREEKWY QAAEMPNRRC RSGLSVLGDK VYAVGGFNGS LRVRTVDVYD PATDQWANCS NMEARRSTLG VAVLNGCIYA VGGFDGTTGL SSAEMYDPKT DIWRFIASMS TRRSSVGVGV VHGLLYAVGG YDGFTRQCLS SVERYNPDTD TWVNVAEMSS RRSGAGVGVL NNILYAVGGH DGPMVRRSVE AYDCETNSWR SVADMSYCRR NAGVVAHDGL LYVVGGDDGT SNLASVEVYC PDSDSWRILP ALMTIGRSYA GVCMIDKPMC MEEQGALARQ AASLAIALLD DENSQAEGTM EGAIGGAIYG NLAPAGGAAA AAAPAAPAQA PQPNHPHYEN IYAPIGQPSN NNNNSGSNSN QAAAIANANA PANAEEIQQQ QQPAPTEPNA NNNPQPPTAA APAPSQQQQQ QQAQPQQPQR ILPMNNYRND LYDRSAAGGV CSAYDVPRAV RSGLGYRRNF RIDMQNGNRC GSGLRCTPLY TNSRSNCQRQ RSFDDTESTD GYNLPYAGAG TMRYENIYEQ IRDEPLYRTS AANRVPLYTR LDVLGHGIGR IERHLSSSCG NIDHYNLGGH YAVLGHSHFG TVGHIRLNAN GSGVAAPGVA GTGTCNVPNC QGYMTAAGST VPVEYANVKV PVKNSASSFF SCLHGENSQS MTNIYKTSGT AAAMAAHNSP LTPNVSMERA SRSASAGAAG SAAAAVEEHS AADSIPSSSN INANRTTGAI PKVKTANKPA KESGGSSTAA SPILDKTTST GSGKSVTLAK KTSTAAARSS SSGDTNGNGT LNRISKSSLQ WLLVNKWLPL WIGQGPDCKV IDFNFMFSRD CVSCDTASVA SQMSNPYGTP RLSGLPQDMV RFQSSCAGAC AAAGAASTIR RDANASARPL HSTLSRLRNG EKRNPNRVAG NYQYEDPSYE NVHVQWQNGF EFGRSRDYDP NSTYHQQRPL LQRARSESPT FSNQQRRLQR QGAQAQQQSQ QPKPPGSPDP YKNYKLNADN NTFKPKPIAA DELEGAVGGA VAEIALPEVD IEVVDPVSLS DNETETTSSQ NNLPSTTNSN NLNEHND // ID KG3H_DROME STANDARD; PRT; 501 AA. AC P83101; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative glycogen synthase kinase-3 homolog (EC 2.7.1.37) (GSK-3) DE (Gasket protein). GN GSKT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Manning G., Sudarsanam S., Plowman G.; RT "Prediction of novel protein kinases from the Drosophila genome RT project and EST sequences."; RL Unpublished observations (AUG-2001). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- PTM: PHOSPHORYLATION AT TYROSINE 193 IS NECESSARY FOR THE CC ACTIVITY (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CDC2/CDKX SUBFAMILY; GSK-3 SUBSUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003778; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0046332; gskt. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Hypothetical protein; Transferase; Serine/threonine-protein kinase; KW ATP-binding; Phosphorylation. FT DOMAIN 33 317 PROTEIN KINASE. FT NP_BIND 39 47 ATP (BY SIMILARITY). FT BINDING 62 62 ATP (BY SIMILARITY). FT ACT_SITE 158 158 BY SIMILARITY. FT DOMAIN 452 499 ASP-RICH. FT MOD_RES 193 193 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 501 AA; 56237 MW; 949DBCADBD72A2C9 CRC64; MASQSKNSGL TNKVTTVVAT NAFGADVMSE ISYTDAKVVG NGSFGVVFQA KMVPSNEMVA IKKVLQDRRF KNRELQIMRK LRHDNIITLK WFFFSSGEKR DEVYLNLVME FLPETLYKVE RQYARAKQTL PVNFVRLYMY QLLRSMGYLH SLGFCHRDIK PQNMLLDSET GVLKLCDFGS AKQLISGEPN VSYICSRYYR APELIFGSTD YTTKIDMWSA GCVMSELLLG QLIFPGDSGV DQIVEIVKVM GTPTSEQLHD MNPHYKQFKL PELKPHPWSK VFRIRTPAEA IDLVSKMLIY SPNARVSPLM GCAHPFFDEL RQDPHQQLPN GRSLPPLFNF TDYEKTIEPD TMPLLLPRAQ GSSTTKEPSA AHRNRNTAGE ESPRKTEDSQ KPATAALSKS PGPSGKALES PPGFLQHDLG NGDHVAVGTM PMEPLTLEQN HFAAESYAVG EDAEDNLEED VGDENDYDYD DGGQCNSTYI SDDMDEASES DDDDFEEEDE N // ID KGP1_DROME STANDARD; PRT; 768 AA. AC Q03042; Q24566; Q9V403; DT 01-JUL-1993 (Rel. 26, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE cGMP-dependent protein kinase, isozyme 1 (EC 2.7.1.37) (CGK). GN PKG21D OR DG1 OR CG3324. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89278147; PubMed=2732245; RA Kalderon D., Rubin G.M.; RT "cGMP-dependent protein kinase genes in Drosophila."; RL J. Biol. Chem. 264:10738-10748(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96394427; PubMed=8798533; RA Foster J.L., Higgins G.C., Jackson F.R.; RT "Biochemical properties and cellular localization of the RT Drosophila DG1 cGMP-dependent protein kinase."; RL J. Biol. Chem. 271:23322-23328(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- MISCELLANEOUS: CGMP-DEPENDENT PROTEIN KINASE 1 CONSISTS OF 3 TYPES CC OF DOMAINS: THE REGULATORY DOMAIN, TWO CGMP-BINDING REGIONS AND CC THE CATALYTIC DOMAIN (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CGMP CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 CYCLIC NUCLEOTIDE-BINDING DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27114; AAA28453.1; -. DR EMBL; M27113; AAA28453.1; JOINED. DR EMBL; U59901; AAB03405.1; -. DR EMBL; AE003588; AAF51459.1; -. DR EMBL; AY058288; AAL13517.1; -. DR PIR; A34106; A34106. DR HSSP; P05132; 1CTP. DR FlyBase; FBgn0000442; Pkg21D. DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR InterPro; IPR002373; cAMP_kin. DR InterPro; IPR002374; cGMP_kin. DR InterPro; IPR000595; cNMP_binding. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00103; CAMPKINASE. DR PRINTS; PR00104; CGMPKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00100; cNMP; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 1. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW cGMP-binding. FT DOMAIN 1 192 REGULATORY (BY SIMILARITY). FT NP_BIND 185 301 CGMP 1. FT NP_BIND 304 427 CGMP 2. FT DOMAIN 457 717 PROTEIN KINASE. FT NP_BIND 463 471 ATP (BY SIMILARITY). FT BINDING 488 488 ATP (BY SIMILARITY). FT ACT_SITE 582 582 BY SIMILARITY. FT CONFLICT 235 235 Q -> H (IN REF. 2). FT CONFLICT 434 434 Q -> R (IN REF. 2). FT CONFLICT 438 438 R -> Q (IN REF. 2). SQ SEQUENCE 768 AA; 86758 MW; 36A97452319BE63C CRC64; MAAGMLTDRE REAIVSNLTK DVQALREMVR SRESELVKLH REIHKLKSVL QQTTNNLNVT RNEKAKKKLY SLPEQCGEQE SRNQNPHLCS SCGMVLPTSP EFALEALSLG PLSPLASTSS ASPSGRTSAD EVRPKAMPAA IKKQGVSAES CVQSMQQSYS IPIPKYEKDF SDKQQIKDAI MDNDFLKNID ASQVRELVDS MYSKSIAAGE FVIREGEVGA HLYVSAAGEF AVMQQGKVLD KMGAGKAFGE LAILYNCTRT ASIRVLSEAA RVWVLDRRVF QQIMMCTGLQ RIENSVNFLR SVPLLMNLSE ELLAKIADVL ELEFYAAGTY IIRQGTAGDS FFLISQGNVR VTQKLTPTSP EETELRTLSR GDYFGEQALI NEDKRTANII ALSPGVECLT LDRDSFKRLI GDLCELKEKD YGDESRKLAM KQAQESCRDE PKEQLQQEFP DLKLTDLEVV STLGIGGFGR VELVKAHHQD RVDIFALKCL KKRHIVDTKQ EEHIFSERHI MLSSRSPFIC RLYRTFRDEK YVYMLLEACM GGEIWTMLRD RGSFEDNAAQ FIIGCVLQAF EYLHARGIIY RDLKPENLML DERGYVKIVD FGFAKQIGTS SKTWTFCGTP EYVAPEIILN KGHDRAVDYW ALGILIHELL NGTPPFSAPD PMQTYNLILK GIDMIAFPKH ISRWAVQLIK RLCRDVPSER LGYQTGGIQD IKKHKWFLGF DWDGLASQLL IPPFVRPIAH PTDVRYFDRF PCDLNEPPDE LSGWDADF // ID KGP2_DROME STANDARD; PRT; 1088 AA. AC Q03043; Q24304; DT 01-JUL-1993 (Rel. 26, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE cGMP-dependent protein kinase, isozyme 2 forms cD4/T1/T3A/T3B DE (EC 2.7.1.37) (CGK) (Foraging protein). GN FOR OR PKG24A OR PGK2 OR DG2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; TISSUE=Imaginal disks; RX MEDLINE=89278147; PubMed=2732245; RA Kalderon D., Rubin G.M.; RT "cGMP-dependent protein kinase genes in Drosophila."; RL J. Biol. Chem. 264:10738-10748(1989). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=T1; CC IsoId=Q03043-1; Sequence=Displayed; CC Name=cD5; CC IsoId=P32023-1; Sequence=External; CC Name=T2; Synonyms=T2a, T2b; CC IsoId=P32023-2; Sequence=External; CC Name=T3A; CC IsoId=Q03043-2; Sequence=VSP_004761; CC Name=T3B; CC IsoId=Q03043-3; Sequence=VSP_004762; CC Name=cD4; CC IsoId=Q03043-4; Sequence=VSP_004763; CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, HIGH DURING CC EMBRYONIC AND ADULT STAGES. ISOFORM T1 IS PREDOMINANTLY EXPRESSED CC DURING EMBRYO AND ADULT STAGES. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CGMP CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 CYCLIC NUCLEOTIDE-BINDING DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27120; AAA28455.1; -. DR EMBL; M27117; AAA28455.1; JOINED. DR EMBL; M27118; AAA28455.1; JOINED. DR EMBL; M27119; AAA28455.1; JOINED. DR EMBL; M30413; AAA28459.1; -. DR PIR; B34106; B34106. DR HSSP; P05132; 1ATP. DR FlyBase; FBgn0000721; for. DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA. DR GO; GO:0008342; P:larval feeding behavior (sensu Insecta); IMP. DR GO; GO:0030536; P:larval feeding behavior; IMP. DR GO; GO:0008345; P:larval locomotory behavior; IMP. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR InterPro; IPR002374; cGMP_kin. DR InterPro; IPR000595; cNMP_binding. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00433; pkinase_C; 1. DR PRINTS; PR00104; CGMPKINASE. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00100; cNMP; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW cGMP-binding; Alternative splicing. FT DOMAIN 1 69 DIMERIZATION (BY SIMILARITY). FT DOMAIN 70 528 REGULATORY (BY SIMILARITY). FT NP_BIND 529 645 CGMP 1 (BY SIMILARITY). FT NP_BIND 646 761 CGMP 2 (BY SIMILARITY). FT DOMAIN 777 1036 PROTEIN KINASE. FT NP_BIND 783 791 ATP (BY SIMILARITY). FT BINDING 807 807 ATP (BY SIMILARITY). FT ACT_SITE 901 901 BY SIMILARITY. FT VARSPLIC 1 169 Missing (in isoform T3A). FT /FTId=VSP_004761. FT VARSPLIC 1 346 Missing (in isoform T3B). FT /FTId=VSP_004762. FT VARSPLIC 1 520 Missing (in isoform cD4). FT /FTId=VSP_004763. SQ SEQUENCE 1088 AA; 121345 MW; E7BDF0AF67DCEB9C CRC64; MRFCFDRLCF ATKRPAQNSN SNAPHSSTTV DAPPRPADVD VATVPVATTA PPPQQPVSNL FYADYQKLQP AIIDRDWERD RDTDTDTRSE AKPPDIVEHI EPVEEQRQIH TQIQSPAEIQ IQIPPTPPAP SIQIQIQQRY RRHSSAEDRN LNTRRNDSNI TEALRKAASM QQEPNANYQF PTDLGLVSIV NNNNNTNTHP SGSNSGTNNN SNINNNLVGG IVTLPAAGGL IGLEHTASGL RLIPAPPTHS DVLTHTLIYG TPPSGAQQLN QDPRSLLHQQ ELQLQQRYQQ LQQLQAQTQG LYTSQGSPVL YHQPSPGSSQ PVAIPGATCH SPTQLQPPNT LNLQQQMQSL RISGCTPSGT GGSATPSPVG LVDPNFIVSN YVAASPQEER FIQIIQAKEL KIQEMQRALQ FKDNEIAELK SHLDKFQSVF PFSRGSAAGC AGTGGASGSG AGGSGGSGPG TATGATRKSG QNFQRQRALG ISAEPQSESS LLLEHVSFPK YDKDERSREL IKAAILDNDF MKNLDLTQIR EIVDCMYPVK YPAKNLIIKE GDVGSIVYVM EDGRVEVSRE GKYLSTLSGA KVLGELAILY NCQRTATITA ITECNLWAIE RQCFQTIMMR TGLIRQAEYS DFLKSVPIFK DLAEDTLIKI SDVLEETHYQ RGDHIVRQGA RGDTFFIISK GKVRVTIKQQ DRQEEKFIRM LGKGDFFGEK ALQGDDLRTA NIICESADGV SCLVIDRETF NQLISNLDEI KHRYDDEGAM ERRKINEEFR DINLTDLRVI ATLGVGGFGR VELVQTNGDS SRSFALKQMK KSQIVETRQQ QHIMSEKEIM GEANCQFIVK LFKTFKDKKY LYMLMESCLG GELWTILRDK GNFDDSTTRF YTACVVEAFD YLHSRNIIYR DLKPENLLLN ERGYGKLVDF GFAKKLQTGR KTWTFCGTPE YVAPEVILNR GHDISADYWS LGVLMFELLT GTPPFTGSDP MRTYNIILKG IDAIEFPRNI TRNASNLIKK LCRDNPAERL GYQRGGISEI QKHKWFDGFY WWGLQNCTLE PPIKPAVKSV VDTTNFDDYP PDPEGPPPDD VTGWDKDF // ID KGP3_DROME STANDARD; PRT; 934 AA. AC P32023; Q24302; Q24303; DT 01-JUL-1993 (Rel. 26, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE cGMP-dependent protein kinase, isozyme 2 forms cD5/T2 (EC 2.7.1.37) DE (CGK) (Foraging protein). GN FOR OR PKG24A OR PGK2 OR DG2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; TISSUE=Imaginal disks; RX MEDLINE=89278147; PubMed=2732245; RA Kalderon D., Rubin G.M.; RT "cGMP-dependent protein kinase genes in Drosophila."; RL J. Biol. Chem. 264:10738-10748(1989). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=cD5; CC IsoId=P32023-1; Sequence=Displayed; CC Name=T1; CC IsoId=Q03043-1; Sequence=External; CC Name=T2; Synonyms=T2a, T2b; CC IsoId=P32023-2; Sequence=VSP_004764; CC Name=T3A; CC IsoId=Q03043-2; Sequence=External; CC Name=T3B; CC IsoId=Q03043-3; Sequence=External; CC Name=cD4; CC IsoId=Q03043-4; Sequence=External; CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, HIGH DURING CC EMBRYONIC AND ADULT STAGES. ISOFORM T2 IS PREDOMINANTLY EXPRESSED CC DURING LARVAL AND ADULT STAGES. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CGMP CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 CYCLIC NUCLEOTIDE-BINDING DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27124; AAA28457.1; -. DR EMBL; M27122; AAA28457.1; JOINED. DR EMBL; M27123; AAA28457.1; JOINED. DR EMBL; M30147; AAA28456.1; -. DR EMBL; M30148; AAA28458.1; -. DR EMBL; M30149; AAA28454.1; -. DR PIR; C34106; C34106. DR PIR; T08418; T08418. DR HSSP; P05132; 1ATP. DR FlyBase; FBgn0000721; for. DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA. DR GO; GO:0008342; P:larval feeding behavior (sensu Insecta); IMP. DR GO; GO:0030536; P:larval feeding behavior; IMP. DR GO; GO:0008345; P:larval locomotory behavior; IMP. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR InterPro; IPR002373; cAMP_kin. DR InterPro; IPR002374; cGMP_kin. DR InterPro; IPR000595; cNMP_binding. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00433; pkinase_C; 1. DR PRINTS; PR00103; CAMPKINASE. DR PRINTS; PR00104; CGMPKINASE. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00100; cNMP; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 1. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW cGMP-binding; Alternative splicing. FT NP_BIND 409 491 CGMP 1 (TRUNCATED) (BY SIMILARITY). FT NP_BIND 492 607 CGMP 2 (BY SIMILARITY). FT DOMAIN 623 882 PROTEIN KINASE. FT NP_BIND 629 637 ATP (BY SIMILARITY). FT BINDING 653 653 ATP (BY SIMILARITY). FT ACT_SITE 747 747 BY SIMILARITY. FT VARSPLIC 368 407 Missing (in isoform T2). FT /FTId=VSP_004764. FT CONFLICT 66 66 A -> V (IN REF. 1; AAA28454). FT CONFLICT 219 219 H -> Q (IN REF. 1; AAA28454). FT CONFLICT 464 464 M -> L (IN REF. 1; AAA28454). FT CONFLICT 510 510 H -> Y (IN REF. 1; AAA28454/AAA28457). SQ SEQUENCE 934 AA; 105932 MW; 2A681C1062B5A1DE CRC64; MKIKHYPGKA VDASLSLEGS SAMGALYEAN WLRAANQPAA PATTGTKLSR QSSSAGSSFL IEGISALSKY QMTLENIRQL ELQSRDKRIA STIKELSGYR PSALQHHQQQ QMHNVWVAED QDQEHEELED ASEGKEKLAS IQEPPAVNHY VLDPTERPRV PRPRQQFSVK PPSLRRSQTM SQPPSYATLR SPPKIKENLS KSSSAYSTFS SAAEDSQDHV VICQQPQRLM APPPREPPPE PPKRVSKPLS RSQTSVQRYA TVRMPNQTTS FSRSVVRSRD STASQRRLSL EQAIEGLKLE GEKAVRQKSP QISPAASSNG SSKDLNGEGF CIPRPRLIVP VHTYARRRRT GNLKEQSSGG QEEEAEKGKG WKDFYVLSQD RHSSFYINRI GQHYDYDYPI DFNNFFPDGR VEVSREGKYL STLSGAKVLG ELAILYNCQR TATITAITEC NLWAIERQCF QTIMMRTGLI RQAEYSDFLK SVPIFKDLAE DTLIKISDVL EETHYQRGDH IVRQGARGDT FFIISKGKVR VTIKQQDTQE EKFIRMLGKG DFFGEKALQG DDLRTANIIC ESADGVSCLV IDRETFNQLI SNLDEIKHRY DDEGAMERRK INEEFRDINL TDLRVIATLG VGGFGRVELV QTNGDSSRSF ALKQMKKSQI VETRQQQHIM SEKEIMGEAN CQFIVKLFKT FKDKKYLYML MESCLGGELW TILRDKGNFD DSTTRFYTAC VVEAFDYLHS RNIIYRDLKP ENLLLNERGY GKLVDFGFAK KLQTGRKTWT FCGTPEYVAP EVILNRGHDI SADYWSLGVL MFELLTGTPP FTGSDPMRTY NIILKGIDAI EFPRNITRNA SNLIKKLCRD NPAERLGYQR GGISEIQKHK WFDGFYWWGL QNCTLEPPIK PAVKSVVDTT NFDDYPPDPE GPPPDDVTGW DKDF // ID KINH_DROME STANDARD; PRT; 975 AA. AC P17210; Q9V7L9; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Kinesin heavy chain. GN KHC OR KIN OR CG7765. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89168428; PubMed=2522352; RA Yang J.T., Laymon R.A., Goldstein L.S.B.; RT "A three-domain structure of kinesin heavy chain revealed by DNA RT sequence and microtubule binding analyses."; RL Cell 56:879-889(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP MUTAGENESIS. RX MEDLINE=93030741; PubMed=1384131; RA Gho M., McDonald K., Ganetzky B., Saxton W.M.; RT "Effects of kinesin mutations on neuronal functions."; RL Science 258:313-316(1992). CC -!- FUNCTION: KINESIN IS A MICROTUBULE-ASSOCIATED FORCE-PRODUCING CC PROTEIN THAT MAY PLAY A ROLE IN ORGANELLE TRANSPORT. CC -!- SUBUNIT: OLIGOMER COMPOSED OF TWO HEAVY CHAINS AND TWO LIGHT CC CHAINS. CC -!- DOMAIN: COMPOSED OF THREE STRUCTURAL DOMAINS: A LARGE GLOBULAR N- CC TERMINAL DOMAIN WHICH IS RESPONSIBLE FOR THE MOTOR ACTIVITY OF CC KINESIN (IT HYDROLYZES ATP AND BINDS MICROTUBULE), A CENTRAL CC ALPHA-HELICAL COILED COIL DOMAIN THAT MEDIATES THE HEAVY CHAIN CC DIMERIZATION; AND A SMALL GLOBULAR C-TERMINAL DOMAIN WHICH CC INTERACTS WITH OTHER PROTEINS (SUCH AS THE KINESIN LIGHT CHAINS), CC VESICLES AND MEMBRANOUS ORGANELLES. CC -!- MISCELLANEOUS: MUTANT FLIES DISPLAY IMPAIRED ACTION POTENTIAL CC PROPAGATION AND NEUROTRANSMITTER RELEASE AT NEUROMUSCULAR CC JUNCTIONS, BUT ARE STILL CAPABLE OF TRANSPORTING CERTAIN CC MEMBRANES, INCLUDING SYNAPTIC VESICLES, TO THE NERVE TERMINAL. CC -!- SIMILARITY: BELONGS TO THE KINESIN-LIKE PROTEIN FAMILY. KINESIN CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24441; AAA28652.1; -. DR EMBL; AE003807; AAF58029.1; -. DR PIR; A31497; A31497. DR HSSP; P33176; 1BG2. DR FlyBase; FBgn0001308; Khc. DR GO; GO:0005871; C:kinesin complex; IDA. DR GO; GO:0008017; F:microtubule binding; IDA. DR GO; GO:0003774; F:motor activity; NAS. DR GO; GO:0007310; P:oocyte dorsal/ventral axis determination; IMP. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localiz...; IMP. DR InterPro; IPR001752; kinesin_motor. DR Pfam; PF00225; kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1. KW Motor protein; Microtubule; ATP-binding; Coiled coil. FT DOMAIN 1 334 KINESIN-MOTOR (BY SIMILARITY). FT DOMAIN 335 931 COILED COIL. FT DOMAIN 932 975 GLOBULAR. FT DOMAIN 180 321 MICROTUBULE-BINDING. FT NP_BIND 92 99 ATP (BY SIMILARITY). FT CONFLICT 515 515 A -> T (IN REF. 1). SQ SEQUENCE 975 AA; 110399 MW; 24840EF414790888 CRC64; MSAEREIPAE DSIKVVCRFR PLNDSEEKAG SKFVVKFPNN VEENCISIAG KVYLFDKVFK PNASQEKVYN EAAKSIVTDV LAGYNGTIFA YGQTSSGKTH TMEGVIGDSV KQGIIPRIVN DIFNHIYAME VNLEFHIKVS YYEIYMDKIR DLLDVSKVNL SVHEDKNRVP YVKGATERFV SSPEDVFEVI EEGKSNRHIA VTNMNEHSSR SHSVFLINVK QENLENQKKL SGKLYLVDLA GSEKVSKTGA EGTVLDEAKN INKSLSALGN VISALADGNK THIPYRDSKL TRILQESLGG NARTTIVICC SPASFNESET KSTLDFGRRA KTVKNVVCVN EELTAEEWKR RYEKEKEKNA RLKGKVEKLE IELARWRAGE TVKAEEQINM EDLMEASTPN LEVEAAQTAA AEAALAAQRT ALANMSASVA VNEQARLATE CERLYQQLDD KDEEINQQSQ YAEQLKEQVM EQEELIANAR REYETLQSEM ARIQQENESA KEEVKEVLQA LEELAVNYDQ KSQEIDNKNK DIDALNEELQ QKQSVFNAAS TELQQLKDMS SHQKKRITEM LTNLLRDLGE VGQAIAPGES SIDLKMSALA GTDASKVEED FTMARLFISK MKTEAKNIAQ RCSNMETQQA DSNKKISEYE KDLGEYRLLI SQHEARMKSL QESMREAENK KRTLEEQIDS LREECAKLKA AEHVSAVNAE EKQRAEELRS MFDSQMDELR EAHTRQVSEL RDEIAAKQHE MDEMKDVHQK LLLAHQQMTA DYEKVRQEDA EKSSELQNII LTNERREQAR KDLKGLEDTV AKELQTLHNL RKLFVQDLQQ RIRKNVVNEE SEEDGGSLAQ KQKISFLENN LDQLTKVHKQ LVRDNADLRC ELPKLEKRLR CTMERVKALE TALKEAKEGA MRDRKRYQYE VDRIKEAVRQ KHLGRRGPQA QIAKPIRSGQ GAIAIRGGGA VGGPSPLAQV NPVNS // ID KL61_DROME STANDARD; PRT; 1066 AA. AC P46863; Q8T0A6; Q9W0I8; DT 01-NOV-1995 (Rel. 32, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bipolar kinesin KRP-130 (Kinesin-like protein Klp61F). GN KLP61F OR KLP2 OR CG9191. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=94043448; PubMed=8227131; RA Heck M.M.S., Pereira A., Pesavento P.A., Yannoni Y., Spradling A.C., RA Goldstein L.S.B.; RT "The kinesin-like protein KLP61F is essential for mitosis in RT Drosophila."; RL J. Cell Biol. 123:665-679(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 228-357 FROM N.A. RC STRAIN=DP CN BW; RX MEDLINE=92020874; PubMed=1924306; RA Stewart R.J., Pesavento P.A., Woerpel D.N., Goldstein L.S.B.; RT "Identification and partial characterization of six members of the RT kinesin superfamily in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 88:8470-8474(1991). RN [6] RP PARTIAL SEQUENCE, AND IDENTIFICATION AS KRP-130. RX MEDLINE=97078747; PubMed=8918872; RA Kashina A.S., Scholey J.M., Leszyk J.D., Saxton W.M.; RT "An essential bipolar mitotic motor."; RL Nature 384:225-225(1996). CC -!- FUNCTION: IMPORTANT ROLE IN MITOTIC DIVIDING CELLS. MICROTUBULE CC MOTOR REQUIRED FOR SPINDLE BODY SEPARATION. SLOW PLUS-END DIRECTED CC MICROTUBULE MOTOR CAPABLE OF CROSS-LINKING AND SLIDING APART CC ANTIPARALLEL MICROTUBULES, THEREBY PUSHING APART THE ASSOCIATED CC SPINDLE POLES DURING SPINDLE ASSEMBLY AND FUNCTION. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- DEVELOPMENTAL STAGE: SPECIFICALLY EXPRESSED IN PROLIFERATING CC TISSUES DURING EMBRYONIC AND LARVAL DEVELOPMENT. CC -!- PTM: PHOSPHORYLATION DURING MITOSIS AT THR-933 CONTROLS THE CC ASSOCIATION OF KLP61F WITH THE SPINDLE APPARATUS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE KINESIN-LIKE PROTEIN FAMILY. BIMC CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U01842; AAA03718.1; -. DR EMBL; AE003471; AAF47458.2; -. DR EMBL; AY069442; AAL39587.1; -. DR EMBL; M74428; AAA28655.1; -. DR PIR; A48669; A48669. DR HSSP; P17119; 3KAR. DR FlyBase; FBgn0004378; Klp61F. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005871; C:kinesin complex; IDA. DR GO; GO:0003774; F:motor activity; IDA. DR GO; GO:0007100; P:centrosome separation; IGI. DR InterPro; IPR001752; kinesin_motor. DR Pfam; PF00225; kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1. KW Motor protein; Cell division; Microtubule; ATP-binding; Coiled coil; KW Mitosis; Cell cycle; Phosphorylation. FT DOMAIN 17 361 KINESIN-MOTOR (BY SIMILARITY). FT DOMAIN 362 462 COILED COIL (POTENTIAL). FT DOMAIN 540 569 COILED COIL (POTENTIAL). FT DOMAIN 639 738 COILED COIL (POTENTIAL). FT DOMAIN 808 875 COILED COIL (POTENTIAL). FT DOMAIN 889 918 COILED COIL (POTENTIAL). FT NP_BIND 103 110 ATP (POTENTIAL). FT MOD_RES 933 933 PHOSPHORYLATION (BY CDC2) (BY FT SIMILARITY). FT VARIANT 595 595 M -> V. FT VARIANT 869 869 R -> K. FT VARIANT 904 904 H -> Q. FT CONFLICT 962 962 L -> Q (IN REF. 1). FT CONFLICT 983 983 V -> D (IN REF. 1). SQ SEQUENCE 1066 AA; 121163 MW; 363647366EE0721F CRC64; MDISGGNTSR QPQKKSNQNI QVYVRVRPLN SRERCIRSAE VVDVVGPREV VTRHTLDSKL TKKFTFDRSF GPESKQCDVY SVVVSPLIEE VLNGYNCTVF AYGQTGTGKT HTMVGNETAE LKSSWEDDSD IGIIPRALSH LFDELRMMEV EYTMRISYLE LYNEELCDLL STDDTTKIRI FDDSTKKGSV IIQGLEEIPV HSKDDVYKLL EKGKERRKTA TTLMNAQSSR SHTVFSIVVH IRENGIEGED MLKIGKLNLV DLAGSENVSK AGNEKGIRVR ETVNINQSLL TLGRVITALV DRAPHVPYRE SKLTRLLQES LGGRTKTSII ATISPGHKDI EETLSTLEYA HRAKNIQNKP EVNQKLTKKT VLKEYTEEID KLKRDLMAAR DKNGIYLAEE TYGEITLKLE SQNRELNEKM LLLKALKDEL QNKEKIFSEV SMSLVEKTQE LKKTEENLLN TKGTLLLTKK VLTKTKRRYK EKKELVASHM KTEQVLTTQA QEILAAADLA TDDTHQLHGT IERRRELDEK IRRSCDQFKD RMQDNLEMIG GSLNLYQDQQ AALKEQLSQE MVNSSYVSQR LALNSSKSIE MLKEMCAQSL QDQTNLHNKL IGEVMKISDQ HSQAFVAKLM EQMQQQQLLM SKEIQTNLQV IEENNQRHKA MLDSMQEKFA TIIDSSLQSV EEHAKQMHKK LEQLGAMSLP DAEELQNLQE ELANERALAQ QEDALLESMM MQMEQIKNLR SKNSISMSVH LNKMEESRLT RNHRIDDIKS GIQDYQKLGI EASQSAQAEL TSQMEAGMLC LDQGVANCSM LQVHMKNLNQ KYEKETNENV GSVRVHHNQV EIICQESKQQ LEAVQEKTEV NLEQMVDARQ QLITEDRQRF IGHATVATDL VQESNRQFSE HAEHQRQQLQ ICEQELVRFQ QSELKTYAPT GTTPSKRDFV YPRTLVATSP HQEIVRRYRQ ELDWSDLDTT ATIDECSEGE HDVSMHSVQE LSETETIMNS TPIEPVDGVT VKRGCGTTRN SNSNALKPPV ATGGKRSSSL SRSLTPSKTS PRGSPAFVRH NKENVA // ID KL68_DROME STANDARD; PRT; 784 AA. AC P46867; Q9VTN8; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Kinesin-like protein KLP68D. GN KLP68D OR KLP5 OR CG7293. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95050960; PubMed=7525600; RA Pesavento P.A., Stewart R.J., Goldstein L.S.B.; RT "Characterization of the KLP68D kinesin-like protein in Drosophila: RT possible roles in axonal transport."; RL J. Cell Biol. 127:1041-1048(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 220-342 FROM N.A. RX MEDLINE=92020874; PubMed=1924306; RA Stewart R.J., Pesavento P.A., Woerpel D.N., Goldstein L.S.B.; RT "Identification and partial characterization of six members of the RT kinesin superfamily in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 88:8470-8474(1991). CC -!- FUNCTION: PLUS-END DIRECTED MICROTUBULE MOTOR THAT MAY BE USED FOR CC ANTEROGRADE AXONAL TRANSPORT AND COULD CONCEIVABLY MOVE CARGOES IN CC FLY NEURONS DIFFERENT THAN THOSE MOVED BY KINESIN HEAVY CHAIN OR CC OTHER PLUS-END DIRECTED MOTORS. CC -!- TISSUE SPECIFICITY: EXPRESSED PRIMARILY IN THE CENTRAL NERVOUS CC SYSTEM AND IN A SUBSET OF THE PERIPHERAL NERVOUS SYSTEM DURING CC EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE KINESIN-LIKE PROTEIN FAMILY. KINESIN CC II SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U15974; AAA69929.1; -. DR EMBL; M74431; AAA28658.1; -. DR EMBL; AE003543; AAF50008.1; -. DR PIR; A55236; A55236. DR HSSP; P17119; 3KAR. DR FlyBase; FBgn0004381; Klp68D. DR GO; GO:0003774; F:motor activity; IDA. DR GO; GO:0008089; P:anterograde axon cargo transport; IEP. DR InterPro; IPR001752; kinesin_motor. DR Pfam; PF00225; kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1. KW Motor protein; Microtubule; ATP-binding; Coiled coil. FT DOMAIN 16 275 KINESIN-MOTOR. FT DOMAIN 351 385 COILED COIL (POTENTIAL). FT DOMAIN 426 582 COILED COIL (POTENTIAL). FT NP_BIND 106 113 ATP (POTENTIAL). FT CONFLICT 220 221 SS -> TC (IN REF. 3). FT CONFLICT 338 342 GSRAK -> VRGQV (IN REF. 3). FT CONFLICT 338 338 G -> A (IN REF. 2). SQ SEQUENCE 784 AA; 88193 MW; 94BB9BADF072DFC0 CRC64; MSAKSRRPGT GSSQTPNECV QVVVRCRPMS NRERSERSPE VVNVYPNRGV VELQNVVDGN KEQRKVFTYD AAYDASATQT TLYHEVVFPL VSSVLEGFNG CIFAYGQTGT GKTFTMEGVR GNDELMGIIP RTFEQIWLHI NRTENFQFLV DVSYLEIYME ELRDLLKPNS KHLEVRERGS GVYVPNLHAI NCKSVEDMIK VMQVGNKNRT VGFTNMNEHS SRSHAIFMIK IEMCDTETNT IKVGKLNLID LAGSERQSKT GASAERLKEA SKINLALSSL GNVISALAES SPHVPYRDSK LTRLLQDSLG GNSKTIMIAN IGPSNYNYNE TLTTLRYGSR AKSIQNQPIK NEDPQDAKLK EYQEEIERLK RLIGPQQQQR SEKQVTAKKQ RVKKPKKETV TKEMSDSLQV STIEQPVEDD SDPEGAESES DKENEAEVAK SNEELERERV ENSKLAAKLA ELEGQLVRGG KNLLDTYSER QIELEKKLVE IAERKKREIE IQQQLELQEE TTLEIRERNV SLEQEVELKK RKLSKCYAKY LALQQELNDC KSDHNQDLRE LEMAQNELVK ELKRQLLIID NFVPIEVKQR LYTQAKYDEE QEEWKFSSMS LPTPPGGDGK FSSKRPVSHP QRRRPTSEYA LQEAKSNSPS SLRFKSENIV NYELEMPCRT TQEYRTPKVS ASLQAVLAQA MQTGGDDIDI VDSHTNSLRS RLENIINANA NGGAGPGAGV AVGSSIPNVR NIKSSRGLPS AASNLDSNRR PPTGRLPAKK PASAYPKARG LVNK // ID KLC_DROME STANDARD; PRT; 508 AA. AC P46824; Q9VU05; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Kinesin light chain (KLC). GN KLC OR CG5433. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=93293894; PubMed=8514798; RA Gauger A.K., Goldstein L.S.B.; RT "The Drosophila kinesin light chain. Primary structure and RT interaction with kinesin heavy chain."; RL J. Biol. Chem. 268:13657-13666(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: KINESIN IS A MICROTUBULE-ASSOCIATED FORCE-PRODUCING CC PROTEIN THAT MAY PLAY A ROLE IN ORGANELLE TRANSPORT. THE LIGHT CC CHAIN MAY FUNCTION IN COUPLING OF CARGO TO THE HEAVY CHAIN OR IN CC THE MODULATION OF ITS ATPASE ACTIVITY. CC -!- SUBUNIT: OLIGOMERIC COMPLEX COMPOSED OF TWO HEAVY CHAINS AND TWO CC LIGHT CHAINS. CC -!- TISSUE SPECIFICITY: UBIQUITOUS. CC -!- DOMAIN: THE LIGHT CHAIN IS COMPOSED OF THREE STRUCTURAL DOMAINS: A CC LARGE GLOBULAR N-TERMINAL DOMAIN WHICH MAY BE INVOLVED IN BINDING CC TO KINESIN HEAVY CHAINS, A CENTRAL ALPHA-HELICAL COILED-COIL CC DOMAIN THAT MEDIATES THE LIGHT CHAIN DIMERIZATION; AND A SMALL CC GLOBULAR C-TERMINAL WHICH MAY PLAY A ROLE IN REGULATING CC MECHANOCHEMICAL ACTIVITY OR ATTACHMENT OF KINESIN TO MEMBRANE- CC BOUND ORGANELLES. CC -!- SIMILARITY: BELONGS TO THE KINESIN LIGHT CHAIN FAMILY. CC -!- SIMILARITY: CONTAINS 6 TPR REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L11013; AAA02481.1; -. DR EMBL; L11328; AAA28669.1; -. DR EMBL; AE003540; AAF49890.2; -. DR EMBL; AY061164; AAL28712.1; -. DR FlyBase; FBgn0010235; Klc. DR InterPro; IPR002151; Kinesin_light. DR InterPro; IPR008940; Prenyl_trans. DR InterPro; IPR001440; TPR. DR Pfam; PF00515; TPR; 5. DR PRINTS; PR00381; KINESINLIGHT. DR SMART; SM00028; TPR; 4. DR PROSITE; PS01160; KINESIN_LIGHT; 4. KW Motor protein; Microtubule; Coiled coil; Repeat; TPR repeat. FT DOMAIN 34 129 COILED COIL. FT REPEAT 186 219 TPR 1. FT REPEAT 228 261 TPR 2. FT REPEAT 270 303 TPR 3. FT REPEAT 312 345 TPR 4. FT REPEAT 354 387 TPR 5. FT REPEAT 437 470 TPR 6. SQ SEQUENCE 508 AA; 58044 MW; B7893FF47EE638A9 CRC64; MTQMSQDEII TNTKTVLQGL EALRVEHVSI MNGIAEVQKD NEKSDMLRKN IENIELGLSE AQVMMALTSH LQNIEAEKHK LKTQVRRLHQ ENAWLRDELA NTQQKFQASE QLVAQLEEEK KHLEFMASVK KYDENQEQDD ACDKSRTDPV VELFPDEENE DRHNMSPTPP SQFANQTSGY EIPARLRTLH NLVIQYASQG RYEVAVPLCK QALEDLERTS GHDHPDVATM LNILALVYRD QNKYKEAANL LNDALSIRGK TLGENHPAVA ATLNNLAVLY GKRGKYKDAE PLCKRALEIR EKVLGKDHPD VAKQLNNLAL LCQNQGKYDE VEKYYQRALD IYESKLGPDD PNVAKTKNNL AGCYLKQGRY TEAEILYKQV LTRAHEREFG AIDSKNKPIW QVAEEREEHK FDNRENTPYG EYGGWHKAAK VDSPTVTTTL KNLGALYRRQ GMFEAAETLE DCAMRSKKEA YDLAKQTKLS QLLTSNEKRR SKAIKEDLDF SEEKNAKP // ID KNIR_DROME STANDARD; PRT; 429 AA. AC P10734; Q9VPC6; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Zygotic gap protein knirps. GN KNI OR NR0A1 OR CG4717. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Salivary gland; RX MEDLINE=89057148; PubMed=2904128; RA Nauber U., Pankratz M.J., Kilnlin A., Seyffert E., Klemm U., RA Jackle H.; RT "Abdominal segmentation of the Drosophila embryo requires a hormone RT receptor-like protein encoded by the gap gene knirps."; RL Nature 336:489-492(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP CHARACTERIZATION. RX MEDLINE=96312963; PubMed=8670869; RA Arnosti D.N., Gray S., Barolo S., Zhou J., Levine M.; RT "The gap protein knirps mediates both quenching and direct repression RT in the Drosophila embryo."; RL EMBO J. 15:3659-3666(1996). CC -!- FUNCTION: TRANSCRIPTIONAL REPRESSOR. BINDS TO MULTIPLE SITES IN CC THE EVE STRIPE 3 ENHANCER ELEMENT. PLAYS AN ESSENTIAL ROLE IN THE CC SEGMENTATION PROCESS BOTH BY REFINING THE EXPRESSION PATTERNS OF CC GAP GENES AND BY ESTABLISHING PAIR-RULES STRIPES OF GENE CC EXPRESSION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR0 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13331; CAA31709.1; -. DR EMBL; AE003592; AAF51629.2; -. DR PIR; S01919; S01919. DR HSSP; P03372; 1HCP. DR TRANSFAC; T00445; -. DR FlyBase; FBgn0001320; kni. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR GO; GO:0007088; P:regulation of mitosis; IMP. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Developmental protein; Repressor. FT DNA_BIND 5 71 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 5 25 C4-TYPE. FT ZN_FING 42 66 C4-TYPE. FT DOMAIN 97 101 POLY-ALA. FT DOMAIN 137 142 POLY-HIS. FT DOMAIN 143 149 POLY-GLN. FT DOMAIN 200 213 POLY-ALA. FT DOMAIN 375 382 POLY-SER. SQ SEQUENCE 429 AA; 45611 MW; 79CEE86A66AB00C7 CRC64; MNQTCKVCGE PAAGFHFGAF TCEGCKSFFG RSYNNISTIS ECKNEGKCII DKKNRTTCKA CRLRKCYNVG MSKGGSRYGR RSNWFKIHCL LQEHEQAAAA AGKAPPLAGG VSVGGAPSAS SPVGSPHTPG FGDMAAHLHH HHQQQQQQQV PRHPHMPLLG YPSYLSDPSA ALPFFSMMGG VPHQSPFQLP PHLLFPGYHA SAAAAAASAA DAAYRQEMYK HRQSVDSVES QNRFSPASQP PVVQPTSSAR QSPIDVCLEE DVHSVHSHQS SASLLHPIAI RATPTTPTSS SPLSFAAKMQ SLSPVSVCSI GGETTSVVPV HPPTVSAQEG PMDLSMKTSR SSVHSFNDSG SEDQEVEVAP RRKFYQLEAE CLTTSSSSSS HSAAHSPNTT TAHAEVKRQK LGGAEATHFG GFAVAHNAAS AMRGIFVCV // ID KNRL_DROME STANDARD; PRT; 647 AA. AC P13054; Q9VPC8; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Knirps-related protein. GN KNRL OR NR0A2 OR CG4761. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89057149; PubMed=2848202; RA Oro A.E., Ong E.S., Margolis J.S., Posakony J.W., McKeown M., RA Evans R.M.; RT "The Drosophila gene knirps-related is a member of the RT steroid-receptor gene superfamily."; RL Nature 336:493-496(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR0 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14153; CAA32365.1; -. DR EMBL; AE003591; AAF51627.2; -. DR EMBL; AY075383; AAL68221.1; -. DR PIR; S06450; S06450. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T02773; -. DR FlyBase; FBgn0001323; knrl. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR GO; GO:0007088; P:regulation of mitosis; IMP. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Developmental protein. FT DNA_BIND 14 80 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 14 34 C4-TYPE. FT ZN_FING 51 75 C4-TYPE. FT DOMAIN 121 262 GLY-RICH. FT DOMAIN 577 597 ASN-RICH. SQ SEQUENCE 647 AA; 68322 MW; E466FA081DAACDC8 CRC64; MMNQDNPYAM NQTCKVCGEP AAGFHFGAFT CEGCKSFFGR SYNNLSSISD CKNNGECIIN KKNRTACKAC RLKKCLMVGM SKSGSRYGRR SNWFKIHCLL QEQQQQAVAA MAAHHNSQQA GGGSSGGSGG GQGMPNGVKG MSGVPPPAAA AAALGMLGHP GGYPGLYAVA NAGGSSRSKE ELMMLGLDGS VEYGSHKHPV VASPSVSSPD SHNSDSSVEV SSVRGNPLLH LGGKSNSGGS SSGADGSHSG GGGGGGGGVT PGRPPQMRKD LSPFLPLPFP GLASMPVMPP PAFLPPSHLL FPGYHPALYS HHQGLLKPTP EQQQAAVAAA AVQHLFNSSG AGQRFAPGTS PFANHQQHHK EEDQPAPARS PSTHANNNHL LTNGGAADEL TKRFYLDAVL KSQQQSPPPT TKLPPHSKQD YSISALVTPN SESGRERVKS RQNEEDDEAR ADGIIDGAEH DDEEEDLVVS MTPPHSPAQQ EERTPAGEDP RPSPGQDNPI DLSMKTTGSS LSSKSSSPEI EPETEISSDV EKNDTDDDDE DLKVTPEEEI SVRETADPEI EEDHSSTTET AKTSIENTHN NNNSISNNNN NNNNNNNSIL SDSEASETIK RKLDELIEAS SENGKRLRLE APVKVATSNA LDLTTKV // ID KP58_DROME STANDARD; PRT; 952 AA. AC Q9VPC0; Q94889; Q9TXB3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein kinase PITSLRE (EC 2.7.1.37) (Cell division DE cycle 2-like). GN PITSLRE OR CG4268. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=97084555; PubMed=8930898; RA Sauer K., Weigmann K., Sigrist S., Lehner C.F.; RT "Novel members of the cdc2-related kinase family in Drosophila: RT cdk4/6, cdk5, PFTAIRE, and PITSLRE kinase."; RL Mol. Biol. Cell 7:1759-1769(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 571-722 FROM N.A. RC TISSUE=Imaginal disks; RX MEDLINE=92335284; PubMed=1378625; RA Biggs W.H. III, Zipursky S.L.; RT "Primary structure, expression, and signal-dependent tyrosine RT phosphorylation of a Drosophila homolog of extracellular signal- RT regulated kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992). CC -!- FUNCTION: ACTS AS A NEGATIVE REGULATOR OF THE NORMAL CELL CYCLE CC PROGRESSION. MAY FUNCTION IN REGULATING PROLIFERATION BY THE CC PHOSPHORYLATION AND SUBSEQUENT PLASMA MEMBRANE TARGETING OF CC GALACTOSYLTRANSFERASE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: PRESENT THROUGHOUT THE EARLY EMBRYO. IN CC LATE EMBRYOS LEVELS ARE HIGHEST IN THE CNS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC HIGHEST LEVELS IN EARLY EMBRYOGENESIS (0-6 HOURS), LOW LEVELS CC DURING LATER EMBRYOGENESIS, MODERATE LEVELS IN PUPAE AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CDC2/CDKX SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99513; CAA67863.1; -. DR EMBL; AE003592; AAF51635.1; -. DR HSSP; P24941; 1B38. DR FlyBase; FBgn0016696; Pitslre. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; Cell cycle; KW Nuclear protein. FT DOMAIN 51 56 NUCLEAR LOCALIZATION SIGNAL FT (POTENTIAL). FT DOMAIN 92 146 HIS-RICH. FT DOMAIN 386 504 SER-RICH. FT DOMAIN 558 851 PROTEIN KINASE. FT NP_BIND 564 572 ATP (BY SIMILARITY). FT BINDING 587 587 ATP (BY SIMILARITY). FT ACT_SITE 685 685 BY SIMILARITY. FT CONFLICT 69 69 D -> E (IN REF. 1). FT CONFLICT 223 223 V -> A (IN REF. 1). FT CONFLICT 283 283 I -> S (IN REF. 1). FT CONFLICT 492 492 V -> A (IN REF. 1). FT CONFLICT 584 584 V -> E (IN REF. 3). FT CONFLICT 603 603 L -> R (IN REF. 3). FT CONFLICT 612 612 G -> GG (IN REF. 3). FT CONFLICT 670 670 MISSING (IN REF. 3). FT CONFLICT 680 680 MISSING (IN REF. 3). FT CONFLICT 717 717 MISSING (IN REF. 3). SQ SEQUENCE 952 AA; 108837 MW; 9CBDE8D459D0713D CRC64; MVNSSGSEDG QLRSPNDVHY HSRGEEDEHE GDADALYIQP PQASRESGSG PRREKKKHSR ERRRHKERDD VGGAALALER DHRYDYRSRE EHYHHHQRER SSNAAAAYAK HHLGHAYHYP QPPQQQQQPL PPAPSYAAHH YHHHQHLSGA RAAPREYHSY PSGYHSGSRH GDYPMEEPTR RSSKYAESKD AESLEQDLRS RLLKKRHNYV KDYETEENYE HRVERSDRRE GGRKERERTV RSTHKQNRHD RVIELLDSPE QEHHHQHQHK SHRSKWREEV EVIRRKVPED LELLARREKL LAAERESRQR KQTAREELEA RRELLRERNE HSDALSPTTV AASVTAGLNI HVKRKSKPDN YEKEIKLKKR REDDIEVIRD DDDEESEESD SNEEVPEQDS EGSATESGSE DSYASKKKSK IKSKSQLEDD DEDLPLPDSP LSVGELYKSP KQRQRSRSVS SKSSSQSSRS SRSRSRSRSQ SSLEDEVDRQ DVGADASPSS STRSEERGMT QEQPEEKPEE KLKEKQKSLE EQIPCDDKGI PLPNYYPGVQ GCRSVEEFQC LNRIEEGTYG VVYRAKDKRT NEIVALKRLK MEKEKEGFPI TSLREINTLL KGQHPNIVTV REIVVGSNMD KIFIVMDYVE HDLKSLMETM KNRKQSFFPG EVKCLTQQLL RAVAHLHDNW ILHRDLKTSN LLLSHKGILK VGDFGLAREY GSPIKKYTSL VVTLWYRAPE LLLCSPVYST PIDVWSVGCI FAEFLQMLPL FPGKSEIDEL NRIFKELGTP NEKIWPGYTE LPAVKNMLSQ NSQFTEYPVS QLRKHFQEKT SEMGLSLLQG LLTYDPKQRL SADAALKHGF FKELPLPIDP SMFPTWPAKS ELGARKAQAS SPKPPSGGSQ FKQLGRDEPI IVGPGNKLSS GIITGNKKSH GAGGSSASTG FVLNAGITQR QLAMGPGFSL KF // ID KPC1_DROME STANDARD; PRT; 679 AA. AC P05130; Q9V7V6; Q9V7V7; DT 13-AUG-1987 (Rel. 05, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein kinase C, brain isozyme (EC 2.7.1.-) (PKC) (dPKC53E(BR)). GN PKC53E OR PKC1 OR CG6622. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=87218499; PubMed=3107983; RA Rosenthal A., Rhee L., Yadegari R., Paro R., Ullrich A., Goeddel D.V.; RT "Structure and nucleotide sequence of a Drosophila melanogaster RT protein kinase C gene."; RL EMBO J. 6:433-441(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; TISSUE=Ovary; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PKC IS ACTIVATED BY DIACYLGLYCEROL WHICH IN TURN CC PHOSPHORYLATES A RANGE OF CELLULAR PROTEINS. PKC ALSO SERVES AS CC THE RECEPTOR FOR PHORBOL ESTERS, A CLASS OF TUMOR PROMOTERS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P05130-1; Sequence=Displayed; CC Name=Short; CC IsoId=P05130-2; Sequence=VSP_004743; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: HEAD NEURAL TISSUE. CC -!- MISCELLANEOUS: THIS IS A CALCIUM-ACTIVATED, PHOSPHOLIPID- CC DEPENDENT, SERINE- AND THREONINE-SPECIFIC ENZYME. CC -!- MISCELLANEOUS: THE SEQUENCE SHOWN IS THAT OF OREGON-R. CC -!- SIMILARITY: CONTAINS 2 ZINC-DEPENDENT PHORBOL-ESTER AND DAG CC BINDING DOMAINS. CC -!- SIMILARITY: CONTAINS 1 C2 DOMAIN. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. PKC CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05076; CAA28736.1; -. DR EMBL; X05279; CAA28890.2; -. DR EMBL; X05280; CAA28890.2; JOINED. DR EMBL; X05281; CAA28890.2; JOINED. DR EMBL; X05282; CAA28890.2; JOINED. DR EMBL; X05283; CAA28890.2; JOINED. DR EMBL; AE003805; AAF57932.1; -. DR EMBL; AE003805; AAF57933.1; -. DR EMBL; AY095003; AAM11331.1; -. DR PIR; A32545; A32545. DR HSSP; P05697; 1TBN. DR FlyBase; FBgn0003091; Pkc53E. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR InterPro; IPR000008; C2. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR002219; DAG_PE-bind. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00168; C2; 1. DR Pfam; PF00130; DAG_PE-bind; 2. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00433; pkinase_C; 1. DR PRINTS; PR00360; C2DOMAIN. DR PRINTS; PR00008; DAGPEDOMAIN. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00499; C2_DOMAIN_1; 1. DR PROSITE; PS50004; C2_DOMAIN_2; 1. DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 1. DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Calcium-binding; Repeat; ATP-binding; Transferase; KW Serine/threonine-protein kinase; Multigene family; Zinc; KW Phorbol-ester binding; Alternative splicing. FT DOMAIN 46 104 PHORBOL-ESTER AND DAG BINDING 1. FT DOMAIN 120 169 PHORBOL-ESTER AND DAG BINDING 2. FT DOMAIN 191 278 C2 DOMAIN. FT DOMAIN 350 608 PROTEIN KINASE. FT NP_BIND 356 364 ATP (BY SIMILARITY). FT BINDING 379 379 ATP (BY SIMILARITY). FT ACT_SITE 474 474 BY SIMILARITY. FT VARSPLIC 67 77 CGYQSGYAWMG -> WG (in isoform Short). FT /FTId=VSP_004743. FT VARIANT 437 437 M -> I. FT CONFLICT 608 608 F -> S (IN REF. 1). FT CONFLICT 634 648 DVSNFDKQFTSEKTD -> MCPTLTSSSHQRKQT (IN FT REF. 1). FT CONFLICT 649 679 MISSING (IN REF. 1). SQ SEQUENCE 679 AA; 77695 MW; 3C69AD351E36B7DC CRC64; MSEGSDNNGD PQQQGAEGEA VGENKMKSRL RKGALKKKNV FNVKDHCFIA RFFKQPTFCS HCKDFICGYQ SGYAWMGFGK QGFQCQVCSY VVHKRCHEYV TFICPGKDKG IDSDSPKTQH NFEPFTYAGP TFCDHCGSLL YGIYHQGLKC SACDMNVHAR CKENVPSLCG CDHTERRGRI YLEINVKENL LTVQIKEGRN LIPMDPNGLS DPYVKVKLIP DDKDQSKKKT RTIKACLNPV WNETLTYDLK PEDKDRRILI EVWDWDRTSR NDFMGALSFG ISEIIKNPTN GWFKLLTQDE GEYYNVPCAD DEQDLLKLKQ KPSQKKPMVM RSDTNTHTSS KKDMIRATDF NFIKVLGKGS FGKVLLAERK GSEELYAIKI LKKDVIIQDD DVECTMIEKR VLALGEKPPF LVQLHSCFQT MDRLFFVMEY VNGGDLMFQI QQFGKFKEPV AVFYAAEIAA GLFFLHTKGI LYRDLKLDNV LLDADGHVKI ADFGMCKENI VGDKTTKTFC GTPDYIAPEI ILYQPYGKSV DWWAYGVLLY EMLVGQPPFD GEDEEELFAA ITDHNVSYPK SLSKEAKEAC KGFLTKQPNK RLGCGSSGEE DVRLHPFFRR IDWEKIENRE VQPPFKPKIK HRKDVSNFDK QFTSEKTDLT PTDKVFMMNL DQSEFVGFSY MNPEYVFSP // ID KPC2_DROME STANDARD; PRT; 700 AA. AC P13677; Q9V7V5; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein kinase C, eye isozyme (EC 2.7.1.-) (PKC) (dPKC53E(EY)) DE (Protein INAC) (Inactivation no after-potential C protein) DE (Photoreceptor-specific PKC) (Eye-PKC). GN INAC OR PKC2 OR CG6518. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89249302; PubMed=2720775; RA Schaeffer E., Smith D., Mardon G., Quinn W., Zuker C.; RT "Isolation and characterization of two new Drosophila protein kinase RT C genes, including one specifically expressed in photoreceptor RT cells."; RL Cell 57:403-412(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP MUTAGENESIS, AND INTERACTION WITH INAD. RX MEDLINE=21326180; PubMed=11342563; RA Kumar R., Shieh B.-H.; RT "The second PDZ domain of INAD is a type I domain involved in binding RT to eye protein kinase C. Mutational analysis and naturally occurring RT variants."; RL J. Biol. Chem. 276:24971-24977(2001). CC -!- FUNCTION: THIS IS A CALCIUM-ACTIVATED, PHOSPHOLIPID-DEPENDENT, CC SERINE-AND THREONINE-SPECIFIC ENZYME. THIS ISOZYME IS A NEGATIVE CC REGULATOR OF THE VISUAL TRANSDUCTION CASCADE AND HAS BEEN SHOWN TO CC BE REQUIRED FOR PHOTORECEPTOR CELL INACTIVATION AND LIGHT CC ADAPTATION. NEGATIVE REGULATION IS DEPENDENT ON INTERACTION WITH CC SCAFFOLDING PROTEIN INAD. CC -!- TISSUE SPECIFICITY: EXCLUSIVELY EXPRESSED IN PHOTORECEPTOR CELLS. CC -!- DOMAIN: TETRAPEPTIDE LIGAND AT C-TERMINUS IS TETHERED TO INAD BY CC INTERACTION WITH THE SECOND PDZ DOMAIN. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. PKC CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 ZINC-DEPENDENT PHORBOL-ESTER AND DAG CC BINDING DOMAINS. CC -!- SIMILARITY: CONTAINS 1 C2 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04845; AAA28817.1; -. DR EMBL; AE003805; AAF57934.1; -. DR PIR; A32392; A32392. DR HSSP; P04410; 1A25. DR FlyBase; FBgn0004784; inaC. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IMP. DR GO; GO:0006928; P:cell motility; IMP. DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP. DR GO; GO:0008585; P:female gonad development; IMP. DR GO; GO:0007602; P:phototransduction; IGI. DR InterPro; IPR000008; C2. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR002219; DAG_PE-bind. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00168; C2; 1. DR Pfam; PF00130; DAG_PE-bind; 2. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00433; pkinase_C; 1. DR PRINTS; PR00360; C2DOMAIN. DR PRINTS; PR00008; DAGPEDOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00109; C1; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00499; C2_DOMAIN_1; 1. DR PROSITE; PS50004; C2_DOMAIN_2; 1. DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 2. DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Calcium-binding; Repeat; ATP-binding; Transferase; KW Serine/threonine-protein kinase; Multigene family; Vision; Zinc; KW Phorbol-ester binding. FT DOMAIN 72 121 PHORBOL-ESTER AND DAG BINDING 1. FT DOMAIN 137 186 PHORBOL-ESTER AND DAG BINDING 2. FT DOMAIN 206 295 C2 DOMAIN. FT DOMAIN 371 629 PROTEIN KINASE. FT NP_BIND 377 385 ATP (BY SIMILARITY). FT BINDING 400 400 ATP (BY SIMILARITY). FT ACT_SITE 495 495 BY SIMILARITY. FT MUTAGEN 697 697 I->E: NO INTERACTION WITH INAD. FT MUTAGEN 697 697 I->K: 90% REDUCED INTERACTION WITH INAD. SQ SEQUENCE 700 AA; 79843 MW; 41B6BFF7FF3F6F8F CRC64; MAAAAVATPG ATVLPPSVPS AAPGAKAPAA GAGKGPGNLL EITGEANIVN YMKNRLRKGA MKRKGLEMVN GHRFGVRFFK NPTYCGHCKD FIWGFGKQGF QCEECRFNIH QKCCKFVVFK CPGKDTDFDA DCAKVKHGWI STTYTTPTFC DECGLLLHGV AHQGVKCENC NLNVHHACQE TVPPMCGADI SEVRGKLLLY VELKGNNLKV DIKEAANLIP MDTNGFSDPY IAVQMHPDRS GRTKKKTKTI QKNLNPVFNE TFTFELQPQD RDKRLLIEVW DWDRTSRNDF MGSFSFSLEE LQKEPVDGWY KFLSQVEGEH YNIPCVDAFN DIARLRDEVR HDRRPNEKRR MDNKDMPHNM SKRDMIRAAD FNFVKVIGKG SFGKVLLAER RGTDELYAVK VLRKDVIIQT DDMELPMNEK KILALSGRPP FLVSMHSCFQ TMDRLFFVME YCKGGDLMYH MQQYGRFKES VAIFYAVEVA IALFFLHERD IIYRDLKLDN ILLDGEGHVK LVDFGLSKEG VTERQTTRTF CGTPNYMAPE IVSYDPYSIA ADWWSFGVLL FEFMAGQAPF EGDDETTVFR NIKDKKAVFP KHFSVEAMDI ITSFLTKKPN NRLGAGRYAR QEITTHPFFR NVDWDKAEAC EMEPPIKPMI KHRKDISNFD DAFTKEKTDL TPTDKLFMMN LDQNDFIGFS FMNPEFITII // ID KPC3_DROME STANDARD; PRT; 634 AA. AC P13678; Q9VAQ6; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein kinase C (EC 2.7.1.-) (PKC) (dPKC98F). GN PKC98E OR PKC3 OR CG1954. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89249302; PubMed=2720775; RA Schaeffer E., Smith D., Mardon G., Quinn W., Zuker C.; RT "Isolation and characterization of two new Drosophila protein kinase RT C genes, including one specifically expressed in photoreceptor RT cells."; RL Cell 57:403-412(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PKC IS ACTIVATED BY DIACYLGLYCEROL WHICH IN TURN CC PHOSPHORYLATES A RANGE OF CELLULAR PROTEINS. PKC ALSO SERVES AS CC THE RECEPTOR FOR PHORBOL ESTERS, A CLASS OF TUMOR PROMOTERS. CC -!- MISCELLANEOUS: THIS IS A CALCIUM-ACTIVATED, PHOSPHOLIPID- CC DEPENDENT, SERINE- AND THREONINE-SPECIFIC ENZYME. CC -!- SIMILARITY: CONTAINS 2 ZINC-DEPENDENT PHORBOL-ESTER AND DAG CC BINDING DOMAINS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. PKC CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04848; AAA28818.1; -. DR EMBL; AE003768; AAF56846.1; ALT_INIT. DR PIR; B32392; B32392. DR HSSP; P28867; 1PTQ. DR FlyBase; FBgn0003093; Pkc98E. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR002219; DAG_PE-bind. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00130; DAG_PE-bind; 2. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00433; pkinase_C; 1. DR PRINTS; PR00008; DAGPEDOMAIN. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00109; C1; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 2. DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Calcium-binding; Repeat; ATP-binding; Transferase; KW Serine/threonine-protein kinase; Multigene family; Zinc; KW Phorbol-ester binding. FT DOMAIN 72 121 PHORBOL-ESTER AND DAG BINDING 1. FT DOMAIN 147 196 PHORBOL-ESTER AND DAG BINDING 2. FT DOMAIN 303 560 PROTEIN KINASE. FT NP_BIND 309 317 ATP (BY SIMILARITY). FT BINDING 332 332 ATP (BY SIMILARITY). FT ACT_SITE 427 427 BY SIMILARITY. SQ SEQUENCE 634 AA; 71156 MW; 3AE3A3D6B7A276BA CRC64; MQSETAVQDL WVNLEPQGKI HVIIELKNRT DKAKAEAVVE HTVAVNKEFK ERAGFNRRRG AMRRRVHQVN GHKFMATFLR QPTFCSHCRE FIWGIGKQGY QCQVCTLVVH KKCHLSVVSK CPGMRDEQPA KVEMVPAGQR FNVNLPHRFV VHSYKRFTFC DHCGSLLYGL IKQGLQCETC GMNVHKRCQK NVANTCGINT KQMAEILSSL GISPDKQQPR RSKYLNQQGG EDNYGASLGA DGDGAPGQSF RSCALSVDSL ATSTTTMTSG YNSSSCMSLA VTGSGGVGAT GETRPGKCSL LDFNFIKVLG KGSFGKVMLA EKKGTDEIYA IKVLKKDAII QDDDVDCTMT EKRILALAAN HPFLTALHSC FQTPDRLFFV MEYVNGGDLM FQIQKARRFE ASRAAFYAAE VTLALQFLHT HGVIYRDLKL DNILLDQEGH CKLADFGMCK EGIMNGMLTT TFCGTPDYIA PEILKEQEYG ASVDWWALGV LMYEMMAGQP PFEADNEDEL FDSIMHDDVL YPVWLSREAV SILKGFLTKN PEQRLGCTGD ENEIRKHPFF AKLDWKELEK RNIKPPFRPK MKNPRDANNF DAEFTKEDPV LTPIGNEVVR CINQDEFAGF SFVNPKFGPE RKVY // ID KPC4_DROME STANDARD; PRT; 643 AA. AC P83099; Q9VYN2; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative protein kinase C, delta type homolog (EC 2.7.1.37). GN PKC-DELTA OR PKCDELTA OR CG10524. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- SIMILARITY: CONTAINS 2 ZINC-DEPENDENT PHORBOL-ESTER AND DAG CC BINDING DOMAINS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. PKC CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003489; AAF48160.2; -. DR FlyBase; FBgn0030387; Pkc-delta. DR InterPro; IPR000008; C2. DR InterPro; IPR002219; DAG_PE-bind. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00130; DAG_PE-bind; 2. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00433; pkinase_C; 1. DR PRINTS; PR00008; DAGPEDOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00109; C1; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 2. DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Hypothetical protein; ATP-binding; Transferase; KW Serine/threonine-protein kinase; Phorbol-ester binding; Metal-binding; KW Zinc; Repeat. FT DOMAIN 144 194 PHORBOL-ESTER AND DAG BINDING 1. FT DOMAIN 216 266 PHORBOL-ESTER AND DAG BINDING 2. FT DOMAIN 315 573 PROTEIN KINASE. FT NP_BIND 321 329 ATP (BY SIMILARITY). FT BINDING 344 344 ATP (BY SIMILARITY). FT ACT_SITE 439 439 BY SIMILARITY. SQ SEQUENCE 643 AA; 73325 MW; 2769D0869EC5E9A4 CRC64; MMFTRAQVRK QKTSNSSSQR PRSSGGSTRH ETRYKQSSTS SSGAGSGLSG ASGASGARRD QYRDRDHYGK HSFELPRQHS KEEAYHRDRE SSAGGVDRGE RSGIGGNGGG VTGGGVYVDR RTRPRSITNR RGAIKHQKTH DINGHRFVAK FFRQPTFCAF CNLFLWGFGK QGYQCIICQT VVHKKCHDKL LGKCSGSVFT SASTILLRER FKIDMPHRFK PHTFMSPTFC DHCGSLMGGF FIQGLKCEEC DVNCHKKCER LTANLCGVNQ KLIVEALNHV KRETSYTYSQ FQKSGRFTAP ATVIPRFKNY SVDDFHFLAV LGKGSFGKVL LAELRDTTYY YAIKCLKKDV VLEDDDVDST LIERKVLALG TKHPYLCHLF CTFQTESHLF FVMEYLNGGD LMFHIQESGR FSEERARFYG AEIISGLKFL HKKGIIYRDL KLDNVLLDYE GHVRIADFGM CKLQIYLDKT ADSFCGTPDY MAPEIIKGEK YNQNVDWWSF GVLLYEMLIG QSPFSGCDED ELFWSICNEI PWFPVYISAE ATGILKGLLE KDYTKRIGSQ YSPAGDIADH IFFRPIDWGL LEKRQIEPPF KPQVKHPLDT QYFDRVFTRE RVRLTPIDKE ILASMDQKQF HGFTYTNPHI TLD // ID KPEL_DROME STANDARD; PRT; 501 AA. AC Q05652; Q9VB57; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable serine/threonine-protein kinase pelle (EC 2.7.1.37). GN PLL OR CG5974. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND MUTAGENESIS. RX MEDLINE=93177834; PubMed=8440018; RA Shelton C.A., Wasserman S.A.; RT "Pelle encodes a protein kinase required to establish dorsoventral RT polarity in the Drosophila embryo."; RL Cell 72:515-525(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP INTERACTION WITH PLI. RX MEDLINE=99264282; PubMed=10330490; RA Grosshans J., Schnorrer F., Nuesslein-Volhard C.; RT "Oligomerisation of Tube and Pelle leads to nuclear localisation of RT dorsal."; RL Mech. Dev. 81:127-138(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 26-129 IN COMPLEX WITH TUBE. RX MEDLINE=20055599; PubMed=10589682; RA Xiao T., Towb P., Wasserman S.A., Sprang S.R.; RT "Three-dimensional structure of a complex between the death domains RT of Pelle and Tube."; RL Cell 99:545-555(1999). CC -!- FUNCTION: REQUIRED FOR THE NUCLEAR IMPORT OF THE DORSAL PROTEIN CC WHICH ESTABLISHES DORSOVENTRAL POLARITY IN DROSOPHILA EMBRYOS. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- SUBUNIT: INTERACTS WITH TUBE THROUGH THEIR RESPECTIVE N-TERMINAL CC DEATH DOMAINS. INTERACTS WITH PELLINO (PLI). CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT THE LIFE CYCLE WITH CC HIGHEST LEVELS IN 0-3 HOUR-OLD EMBRYOS AND ADULT FEMALES. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC PELLE SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 DEATH DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08476; AAA28750.1; -. DR EMBL; AE003760; AAF56686.1; -. DR PIR; A45775; A45775. DR PDB; 1D2Z; 29-NOV-99. DR PDB; 1IK7; 25-SEP-02. DR FlyBase; FBgn0010441; pll. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0006966; P:antifungal humoral response (sensu Inverteb...; IMP. DR GO; GO:0007352; P:zygotic determination of dorsal/ventral axis; IMP. DR InterPro; IPR000488; Death. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00531; death; 1. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00005; DEATH; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW 3D-structure. FT DOMAIN 55 121 DEATH. FT DOMAIN 213 499 PROTEIN KINASE. FT NP_BIND 219 227 ATP (BY SIMILARITY). FT BINDING 240 240 ATP. FT ACT_SITE 346 346 FT MUTAGEN 240 240 K->R: ABOLISHES ACTIVITY. FT MUTAGEN 346 346 D->A: REDUCED ACTIVITY. FT MUTAGEN 350 350 A->E: REDUCED ACTIVITY. FT STRAND 33 33 FT TURN 35 36 FT HELIX 39 52 FT TURN 53 53 FT HELIX 55 61 FT TURN 62 63 FT HELIX 66 77 FT TURN 78 79 FT HELIX 82 90 FT TURN 91 94 FT STRAND 97 97 FT HELIX 98 107 FT TURN 108 109 FT HELIX 111 116 FT TURN 117 117 FT HELIX 118 120 FT HELIX 123 128 SQ SEQUENCE 501 AA; 56160 MW; 4B29E2B40ACB81A8 CRC64; MSGVQTAEAE AQAQNQANGN RTRSRSHLDN TMAIRLLPLP VRAQLCAHLD ALDVWQQLAT AVKLYPDQVE QISSQKQRGR SASNEFLNIW GGQYNHTVQT LFALFKKLKL HNAMRLIKDY VSEDLHKYIP RSVPTISELR AAPDSSAKVN NGPPFPSSSG VSNSNNNRTS TTATEEIPSL ESLGNIHIST VQRAAESLLE IDYAELENAT DGWSPDNRLG QGGFGDVYRG KWKQLDVAIK VMNYRSPNID QKMVELQQSY NELKYLNSIR HDNILALYGY SIKGGKPCLV YQLMKGGSLE ARLRAHKAQN PLPALTWQQR FSISLGTARG IYFLHTARGT PLIHGDIKPA NILLDQCLQP KIGDFGLVRE GPKSLDAVVE VNKVFGTKIY LPPEFRNFRQ LSTGVDVYSF GIVLLEVFTG RQVTDRVPEN ETKKNLLDYV KQQWRQNRME LLEKHLAAPM GKELDMCMCA IEAGLHCTAL DPQDRPSMNA VLKRFEPFVT D // ID KPYK_DROME STANDARD; PRT; 533 AA. AC O62619; Q86PE3; Q8MT14; Q9VD24; DT 15-DEC-1998 (Rel. 37, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pyruvate kinase (EC 2.7.1.40) (PK). GN PYK OR CG7070. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Canton-S; RA Chien Y.-C., Zhu Y.-J., Chuen C.-M.; RT "Complementary DNA cloning and analysis of gene structure of pyruvate RT kinase from Drosophila melanogaster."; RL Zool. Stud. 38:322-332(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=85158818; PubMed=3920304; RA Rust K.J., Collier G.E.; RT "Localization of a dosage sensitive region for pyruvate kinase in RT Drosophila melanogaster."; RL J. Hered. 76:39-44(1985). CC -!- CATALYTIC ACTIVITY: ATP + PYRUVATE = ADP + PHOSPHOENOLPYRUVATE. CC -!- COFACTOR: REQUIRES MAGNESIUM AND POTASSIUM. CC -!- PATHWAY: GLYCOLYSIS; FINAL STEP. CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=O62619-1; Sequence=Displayed; CC Name=B; CC IsoId=O62619-2; Sequence=VSP_002885; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: IN ADULTS EXPRESSED PREDOMINANTLY IN THE CC THORAX. CC -!- DEVELOPMENTAL STAGE: LOW LEVELS IN LARVAE AND PUPAE, BUT INCREASES CC IN YOUNG ADULTS, BECOMING RELATIVELY STABLE IN TWO-DAY-OLD FLIES. CC -!- SIMILARITY: BELONGS TO THE PYRUVATE KINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF062478; AAC16244.1; -. DR EMBL; AF061507; AAC15808.1; -. DR EMBL; AE003738; AAF55979.3; -. DR EMBL; AE003738; AAN14373.1; -. DR EMBL; AY118442; AAM48471.1; -. DR EMBL; BT003180; AAO24935.1; -. DR HSSP; P14178; 1E0T. DR FlyBase; FBgn0003178; PyK. DR GO; GO:0004743; F:pyruvate kinase activity; NAS. DR GO; GO:0006096; P:glycolysis; NAS. DR InterPro; IPR001697; Pyruvate_kinase. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR ProDom; PD001009; Pyruvate_kinase; 1. DR TIGRFAMs; TIGR01064; pyruv_kin; 1. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. KW Transferase; Kinase; Glycolysis; Magnesium; Alternative splicing. FT ACT_SITE 273 273 BY SIMILARITY. FT METAL 275 275 MAGNESIUM (BY SIMILARITY). FT METAL 296 296 MAGNESIUM (BY SIMILARITY). FT METAL 297 297 MAGNESIUM (BY SIMILARITY). FT VARSPLIC 1 21 Missing (in isoform B). FT /FTId=VSP_002885. FT CONFLICT 180 180 D -> N (IN REF. 1). FT CONFLICT 271 271 I -> F (IN REF. 4; AAO24935). FT CONFLICT 397 397 L -> F (IN REF. 1). SQ SEQUENCE 533 AA; 57440 MW; A8376B72F040EEDB CRC64; MVNVTIYDEA PQLKPNEVPQ NMAAGADTQL EHMCRLQFDS PVPHVRLSGI VCTIGPASSS VEMLEKMMAT GMNIARMNFS HGSHEYHAAT VANVRQAVKN YSAKLGYEHP VAIALDTKGP EIRTGLIGGS GTAEIELKKG EKIKLTTNKE FLEKGSLEIV YVDYENIVNV VKPGNRVFVD DGLISLIVRE VGKDSLTCEV ENGGSLGSRK GVNLPGVPVD LPAVSEKDKS DLLFGVEQEV DMIFASFIRN AAALTEIRKV LGEKGKNIKI ISKIENQQGM HNLDEIIEAG DGIMVARGDL GIEIPAEKVF LAQKAMIARC NKAGKPVICA TQMLESMVKK PRPTRAEISD VANAVLDGAD CVMLSGETAK GEYPLECVLT MAKTCKEAEA ALWHQNLFND LVRGAGTIDA SHAAAIAAVE AATKAKASAI VVITTSGKSA FQVSKYRPRC PIIAVTRFAQ TARQAHLYRG LVPLIYKEPG LGDWLKDVDV RVQFGLQVGK KNGFIKTGDS VVVVTGWKQG SGFTNTIRIV TVE // ID KRAF_DROME STANDARD; PRT; 781 AA. AC P11346; DT 01-JUL-1989 (Rel. 11, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE RAF homolog serine/threonine-protein kinase dRAF-1 (EC 2.7.1.37) DE (Pole-hole protein). GN PHL OR DRAF-1 OR D-RAF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88283647; PubMed=3135183; RA Nishida Y., Hata M., Ayaki T., Ryo H., Yamagata M., Shimizu K., RA Nishizuka Y.; RT "Proliferation of both somatic and germ cells is affected in the RT Drosophila mutants of raf proto-oncogene."; RL EMBO J. 7:775-781(1988). RN [2] RP SEQUENCE OF 465-753 FROM N.A. RX MEDLINE=87257926; PubMed=3037346; RA Mark G.E., Macintyre R.J., Digan M.E., Ambrosio L., Perrimon N.; RT "Drosophila melanogaster homologs of the raf oncogene."; RL Mol. Cell. Biol. 7:2134-2140(1987). RN [3] RP CHARACTERIZATION. RX MEDLINE=93140754; PubMed=8423783; RA Sprenger F., Torsoclair M.M., Morrison D.K.; RT "Biochemical analysis of torso and D-raf during Drosophila RT embryogenesis: implications for terminal signal transduction."; RL Mol. Cell. Biol. 13:1163-1172(1993). CC -!- FUNCTION: SERINE/THREONINE KINASE REQUIRED IN THE EARLY EMBRYO CC FOR THE FORMATION OF TERMINAL STRUCTURE. ALSO REQUIRED DURING CC THE PROLIFERATION OF IMAGINAL CELLS. MAY ACT DOWNSTREAM OF RAS1 CC IN THE SEV SIGNAL TRANSDUCTION PATHWAY. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- COFACTOR: BINDS 2 ZINC IONS PER SUBUNIT (BY SIMILARITY). CC -!- PTM: EXTENSIVELY PHOSPHORYLATED AT 1 TO 2 H AFTER EGG LAYING. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. RAF CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 ZINC-DEPENDENT PHORBOL-ESTER AND DAG CC BINDING DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RAS-BINDING (RBD) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07181; CAA30166.1; ALT_INIT. DR EMBL; M16598; -; NOT_ANNOTATED_CDS. DR HSSP; P04049; 1RFA. DR FlyBase; FBgn0003079; phl. DR GO; GO:0008069; P:dorsal/ventral axis determination, follicul...; IMP. DR GO; GO:0007369; P:gastrulation; NAS. DR GO; GO:0007165; P:signal transduction; IGI. DR GO; GO:0007283; P:spermatogenesis; IMP. DR GO; GO:0007362; P:terminal region determination; IMP. DR InterPro; IPR002219; DAG_PE-bind. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR003116; RBD. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00130; DAG_PE-bind; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF02196; RBD; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00455; RBD; 1. DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 1. DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50898; RBD; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Metal-binding; Zinc; Phorbol-ester binding; Phosphorylation. FT DOMAIN 183 254 RAS-BINDING. FT DOMAIN 265 310 PHORBOL-ESTER AND DAG BINDING. FT DOMAIN 471 732 PROTEIN KINASE. FT NP_BIND 477 485 ATP (BY SIMILARITY). FT METAL 262 262 ZINC 1 (BY SIMILARITY). FT METAL 278 278 ZINC 2 (BY SIMILARITY). FT METAL 281 281 ZINC 2 (BY SIMILARITY). FT METAL 291 291 ZINC 1 (BY SIMILARITY). FT METAL 294 294 ZINC 1 (BY SIMILARITY). FT METAL 299 299 ZINC 2 (BY SIMILARITY). FT METAL 302 302 ZINC 2 (BY SIMILARITY). FT METAL 310 310 ZINC 1 (BY SIMILARITY). FT BINDING 497 497 ATP (BY SIMILARITY). FT ACT_SITE 590 590 BY SIMILARITY. FT CONFLICT 495 495 P -> A (IN REF. 2). FT CONFLICT 520 522 KKT -> RKA (IN REF. 2). FT CONFLICT 571 571 G -> R (IN REF. 2). FT CONFLICT 700 703 RRHS -> PQAL (IN REF. 2). SQ SEQUENCE 781 AA; 88794 MW; DEAD54762249EADC CRC64; MSSESSPKRQ DLYDPLAEEL HNVQLVKHVT RENIDALNAK FANLQEPPAM YLIGESSKAE LNTTWVLGNP TPTSKLFIKY PTYVYVCISR LWFLPTEYQE LTSKLHELEA KEQELMERLN SQDQQEDSSL VERFKEQPHY QNQTQILQQQ RQLARVHHGT DLTDSLGSQP GSQCGTLTRQ PKILLRAHLP NQQRTSVEVI SGVRLCDALM KALKLRQLTP DMCEVSTTHS GRHIIPWHTD IGTLHVEEIF VRLLDKFPIR THIKHQIIRK TFFSLVFCEG CRRLLFTGFY CSQCNFRFHQ RCANRVPMLC QPFPMDSYYQ LLLAENPDNG VGFPGRGTAV RFNMSSRSRS RRCSSSGSSS SSKPPSSSSG NHRQGRPPRI SQDDRSNSAP NVCINNIRSV TSEVQRSLIM QARPPLPHPC TDHSNSTQAS PTSTLKHNRP RARSADESNK NLLLRDAKSS EENWNILAEE ILIGPRIGSG SFGTVYRAHW HGPVPVKTLN VKTPSPAQLQ AFKNEVAMLK KTRHCNILLF MGCVSKPSLA IVTQWCEGSS LYKHVHVSET KFKLNTLIDI GRQVAQGMDY LHAKNIIHRD LKSNNIFLHE DLSVKIGDFG LATAKTRWSG EKQANQPTGS ILWMAPEVIR MQELNPYSFQ SDVYAFGIVM YELLAECLPY GHISNKDQIL FMVGRGLLRP DMSQVRSDAR RHSKRLAEDC IKYTPKDRPL FRPLLNMLEN MLRTLPKIHR SASEPNLTQS QLQNDEFLYL PSPKTPVNFN NFQFFGSAGN I // ID KRAK_DROME STANDARD; PRT; 331 AA. AC O18391; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable serine hydrolase (EC 3.1.-.-) (Kraken protein). GN KRAKEN OR CG3943. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=99051329; PubMed=9831651; RA Chan H.Y.E., Harris S.J., O'Kane C.J.; RT "Identification and characterization of kraken, a gene encoding a RT putative hydrolytic enzyme in Drosophila melanogaster."; RL Gene 222:195-201(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY HAVE A ROLE IN DETOXIFICATION AND DIGESTION DURING CC EMBRYOGENESIS AND LARVAL DEVELOPMENT. CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED BEFORE EMBRYONIC STAGE CC 11. AT STAGE 11, EXPRESSION IS CONCENTRATED IN THE FOREGUT AND CC POSTERIOR MIDGUT. BY STAGE 15, IN GASTRIC CAECAE, PHARYNX, CC POSTERIOR SPIRACLES AND ANTERIOR EDGE OF MIDGUT. AT THE END OF CC EMBRYOGENESIS, EXPRESSION IS CONFINED TO GASTRIC CAECAE. DURING CC THIRD INSTAR LARVAE, EXPRESSED AT LOW LEVELS IN GASTRIC CAECAE, CC MIDGUT AND HINDGUT AND HIGH LEVEL IN FAT BODY. CC -!- DEVELOPMENTAL STAGE: PROBABLY EXPRESSED BOTH MATERNALLY AND CC ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE AB HYDROLASE SUPERFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ000516; CAA04153.1; -. DR EMBL; AE003588; AAF51445.1; -. DR EMBL; AY095092; AAM11420.1; -. DR EMBL; AY118303; AAM48332.1; -. DR FlyBase; FBgn0020545; kraken. DR GO; GO:0017171; F:serine hydrolase activity; NAS. DR GO; GO:0007586; P:digestion; IEP. DR GO; GO:0009636; P:response to toxin; IEP. DR InterPro; IPR000073; A/b_hydrolase. DR InterPro; IPR003089; AB_hydrolase. DR InterPro; IPR008262; Lipase_AS. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00561; abhydrolase; 1. DR PRINTS; PR00111; ABHYDROLASE. DR PROSITE; PS00120; LIPASE_SER; 1. KW Detoxification; Digestion; Developmental protein; Hydrolase. FT ACT_SITE 138 138 BY SIMILARITY. SQ SEQUENCE 331 AA; 37093 MW; 1FE39BC42AED4E69 CRC64; MGQTRVAATT AAQSPAAELS PETNGQTEEP LQLLGEDSWE EFSIAVPWGT VEAKWWGSKE RQPIIALHGW QDNCGSFDRL CPLLPADTSI LAIDLPGHGK SSHYPMGMQY FIFWDGICLI RRIVRKYNWK NVTLLGHSLG GALTFMYAAS FPTEVEKLIN IDIAGPTVRG TQRMAEGTGR ALDKFLDYET LPESKQPCYS YDEMIKLVLD AYDGSVDEPS VRVLMNRGMR HNPSKNGYLF ARDLRLKVSL LGMFTAEQTL AYARQIRCRV LNIRGIPGMK FETPQVYADV IATLRENAAK VVYVEVPGTH HLHLVTPDRV APHIIRFLKE A // ID KRH2_DROME STANDARD; PRT; 276 AA. AC Q9V447; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Kr-h2 protein. GN KR-H2 OR CG9159. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Benevolenskaya E.V., Frolov M.V., Birchler J.A.; RT "Kruppel homolog (Kr h) is a dosage-dependent modifier of gene RT expression in Drosophila."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE UPF0121 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF148686; AAD45272.1; -. DR EMBL; AE003612; AAF52341.1; -. DR FlyBase; FBgn0028419; Kr-h2. DR InterPro; IPR005344; UPF0121. DR Pfam; PF03661; UPF0121; 1. KW Transmembrane. FT TRANSMEM 53 73 POTENTIAL. FT TRANSMEM 125 145 POTENTIAL. FT TRANSMEM 181 201 POTENTIAL. SQ SEQUENCE 276 AA; 31215 MW; 1430CC39A1429140 CRC64; MSAPTDQPPR SEGAQTNSSE RSSQQQEQPQ QSQSQNVPAK LLQHFQTNRI DSALWALRLL VIFFTVSYVL PIFTSQQSAF SKVMLANAAI SALRLHQRLP AFAFSREFLA RLFAEDSCHY MMYSLIFFNI RPSLLVLIPV LLYSVLHASS YSLKLLDLIG QNSWWGARFI ISIVEFQAAN ILKATAFCEI FIMPYAIVLA FMNHAGLMTP VIYYHYLVMR YSSRRNPYPR NAFAELRITF EALAARSPPA FAKIIRGGIG FVNRLAPQLQ PAAAQE // ID KRUH_DROME STANDARD; PRT; 845 AA. AC P08155; Q9VMH5; DT 01-AUG-1988 (Rel. 08, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Krueppel homologous protein 1. GN KR-H1 OR KR-H OR CG9167. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; TISSUE=Embryo, Larva, and Pupae; RX MEDLINE=20237577; PubMed=10772791; RA Pecasse F., Beck Y., Ruiz C., Richards G.; RT "Kruppel-homolog, a stage-specific modulator of the prepupal ecdysone RT response, is essential for Drosophila metamorphosis."; RL Dev. Biol. 221:53-67(2000). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS ALPHA AND BETA). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM BETA). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 289-367 FROM N.A. RX MEDLINE=87051757; PubMed=3096579; RA Schuh R., Aicher W., Gaul U., Cote S., Preiss A., Maier D., RA Seifert E., Nauber U., Schroeder C., Kemler R., Jaeckle H.; RT "A conserved family of nuclear proteins containing structural RT elements of the finger protein encoded by Kruppel, a Drosophila RT segmentation gene."; RL Cell 47:1025-1032(1986). CC -!- FUNCTION: PLAYS A GENERAL ROLE IN THE HIERARCHIES OF GENE CC EXPRESSION LEADING TO METAMORPHOSIS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Beta; CC IsoId=P08155-1; Sequence=Displayed; CC Name=Alpha; CC IsoId=P08155-2; Sequence=VSP_006830; CC -!- DEVELOPMENTAL STAGE: BETA ISOFORM IS EXPRESSED DURING CC EMBRYOGENESIS, MOST ABUNDANT IN MIDEMBRYOGENESIS, AND IN ADULTS. CC ALPHA ISOFORM IS EXPRESSED FROM EMBRYOGENESIS TO 8 HOURS AFTER CC PUPARIATION, MAJOR PERIOD OF EXPRESSION IS DURING SECOND INSTAR. CC -!- SIMILARITY: BELONGS TO THE KRUEPPEL FAMILY OF C2H2-TYPE ZINC- CC FINGER PROTEINS. CC -!- SIMILARITY: CONTAINS 8 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ005440; CAA06543.2; -. DR EMBL; AJ005441; CAA06544.2; -. DR EMBL; AE003612; AAF52343.2; -. DR EMBL; AE003612; AAG22417.1; -. DR EMBL; AY051816; AAK93240.1; -. DR EMBL; M14940; AAA28660.1; -. DR HSSP; P08047; 1SP2. DR FlyBase; FBgn0028420; Kr-h1. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 8. DR ProDom; PD000003; Znf_C2H2; 4. DR SMART; SM00355; ZnF_C2H2; 8. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8. KW Zinc-finger; Metal-binding; DNA-binding; Repeat; Alternative splicing; KW Developmental protein. FT DOMAIN 108 148 GLN-RICH. FT DOMAIN 482 515 SER/THR-RICH. FT DOMAIN 538 565 SER/THR-RICH. FT ZN_FING 194 216 C2H2-TYPE 1. FT ZN_FING 271 293 C2H2-TYPE 2. FT ZN_FING 299 321 C2H2-TYPE 3. FT ZN_FING 327 349 C2H2-TYPE 4. FT ZN_FING 355 377 C2H2-TYPE 5. FT ZN_FING 383 407 C2H2-TYPE 6. FT ZN_FING 413 435 C2H2-TYPE 7. FT ZN_FING 441 463 C2H2-TYPE 8. FT VARSPLIC 1 54 Missing (in isoform Alpha). FT /FTId=VSP_006830. FT CONFLICT 313 313 N -> D (IN REF. 4). SQ SEQUENCE 845 AA; 91451 MW; A4D878E98DC8E372 CRC64; MTESKNDTKS WAPKQIWIKD VLKKSGTELL DISKSPAKAV AVKKSPAKDS ATTKMVYYSA NQLLIKTEQS SQAQFCLQVP PPLTATTTSV GLGVPPSGGQ QEHFELLQTP QQRQMQLQLQ DQHQQEQQQF VSYQLAIQQH QKQQQQQQHE SITNAAPTAA PSAQRIKTEP VGGFPASAAV VSQVRKPSAS KPQFKCDQCG MTFGSKSAHT SHTKSHSKNQ DLSLNGASGA GVAAPVSTAA IELNDAGLPV GIPKSPTIKP LANVAAGADP YQCNVCQKTF AVPARLIRHY RTHTGERPFE CEFCHKLFSV KENLQVHRRI HTKERPYKCD VCGRAFEHSG KLHRHMRIHT GERPHKCSVC EKTFIQSGQL VIHMRTHTGE KPYKCPEPGC GKGFTCSKQL KVHSRTHTGE KPYHCDICFR DFGYNHVLKL HRVQHYGSKC YKCTICDETF KNKKEMEAHI KGHANEVPDD EAEAAAASAA ASTSAGSSAG SPSLQGVSSN SESSNHSPPS SPPATKKPRQ ARQPRVSKTV AATLSIPTSS PLSPSSLSST YSPSASSMAS PPPTSAHYLP VQMEADALSR DSGVSSAQPA HSTYADEEPT DLSMQQVQGQ LPESTVDYYQ APPSLLELQP QPAGLTINPA LLEAASIARR HDDNDDQVQD EDVHAAAWQM MQLCRGHGSL PPTEQPAPSH QPQVPTLHVS DLAANYDDTH EATVLIEHFK RGDLARHGLH KGYAPVPKYE SALPNPDVVR RVEAAIGLRS STESPERSSS PESDSLMMAD RNVMTLPLRK RKHYMNKGDD GQVDSEKASG DGTSAAGGAA SVGAGDGPGS KVMRMSSVIQ FAKAS // ID KRUP_DROME STANDARD; PRT; 466 AA. AC P07247; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Krueppel protein. GN KR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Rosenberg U.B., Schroeder C., Preiss A., Kienlin A., Cote S., RA Riede I., Jaeckle H.; RT "Structural homology of the product of the Drosophila Krueppel gene RT with Xenopus transcription factor IIIA."; RL Nature 319:336-339(1986). RN [2] RP SEQUENCE OF 240-314 FROM N.A. RX MEDLINE=93066327; PubMed=1438276; RA Sommer R.J., Retzlaff M., Goerlich K., Sander K., Tautz D.; RT "Evolutionary conservation pattern of zinc-finger domains of RT Drosophila segmentation genes."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10782-10786(1992). RN [3] RP SUBCELLULAR LOCATION, DNA-BINDING, AND PHOSPHORYLATION. RX MEDLINE=87289672; PubMed=3112773; RA Ollo R., Maniatis T.; RT "Drosophila Kruppel gene product produced in a baculovirus expression RT system is a nuclear phosphoprotein that binds to DNA."; RL Proc. Natl. Acad. Sci. U.S.A. 84:5700-5704(1987). CC -!- FUNCTION: KRUEPPEL IS A GAP CLASS SEGMENTATION PROTEIN. IT IS CC INVOLVED IN THE SEGMENTATION OF THE EMBRYO AND IN THE CC DIFFERENTIATION OF THE MALPIGHIAN TUBULES. CC -!- SUBCELLULAR LOCATION: NUCLEAR, CHROMATIN ASSOCIATED. CC -!- SIMILARITY: BELONGS TO THE KRUEPPEL FAMILY OF C2H2-TYPE ZINC- CC FINGER PROTEINS. CC -!- SIMILARITY: CONTAINS 5 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03414; CAA27148.1; -. DR PIR; A24566; TWFF. DR HSSP; P25490; 1ZNM. DR TRANSFAC; T00456; -. DR FlyBase; FBgn0001325; Kr. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0016564; F:transcriptional repressor activity; IDA. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR GO; GO:0007400; P:neuroblast cell fate determination; IEP. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 4. DR ProDom; PD000003; Znf_C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. KW Developmental protein; Gap protein; Zinc-finger; KW Metal-binding; DNA-binding; Repeat; Nuclear protein; Phosphorylation. FT ZN_FING 222 244 C2H2-TYPE 1. FT ZN_FING 250 272 C2H2-TYPE 2. FT ZN_FING 278 300 C2H2-TYPE 3. FT ZN_FING 306 328 C2H2-TYPE 4. FT ZN_FING 334 354 C2H2-TYPE 5. SQ SEQUENCE 466 AA; 50798 MW; 301D1F0C4398EBE9 CRC64; MSISMLQDAQ TRTLAAALAG IKQEDVHLDR SMSLSPPMSA NTSATSAAAI YPAMGLQQAA AASAFGMLSP TQLLAANRQA AAFMAQLPMS TLANTLFPHN PAALFGAWAA QQSLPPQGTH LHSPPASPHS PLSTPLGSGK HPLNSPNSTP QHHEPAKKAR KLSVKKEFQT EISMSVNDMY LSSGGPISPP SSGSSPNSTH DGAGGNAGCV GVSKDPSRDK SFTCKICSRS FGYKHVLQNH ERTHTGEKPF ECPECDKRFT RDHHLKTHMR LHTGEKPYHC SHCDRQFVQV ANLRRHLRVH TGERPYTCEI CDGKFSDSNQ LKSHMLVHTG EKPFECERCH MKFRRRHHLM NHKCGIQSPP TPALSPAMSG DYPVAISAIA IEASTNRFAA MCATYGSSNE SVDMEKATPE TMVHWICLKM EPALWMAITA TSHGARHRTF VGFSGCLHRK SLTYPVICLS KPSQRI // ID KU70_DROME STANDARD; PRT; 631 AA. AC Q23976; Q24006; Q9VGP5; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Yolk protein factor 1 beta subunit (Inverted repeat-binding protein). GN IRBP OR YPF1B OR DP70 OR CG5247. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Ovary; RX MEDLINE=94209330; PubMed=8157678; RA Jacoby D.B., Wensink P.C.; RT "Yolk protein factor 1 is a Drosophila homolog of Ku, the DNA-binding RT subunit of a DNA-dependent protein kinase from humans."; RL J. Biol. Chem. 269:11484-11491(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=SB2040; TISSUE=Embryo; RX MEDLINE=95108022; PubMed=7809101; RA Beall E.L., Admon A., Rio D.C.; RT "A Drosophila protein homologous to the human p70 Ku autoimmune RT antigen interacts with the P transposable element inverted repeats."; RL Proc. Natl. Acad. Sci. U.S.A. 91:12681-12685(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: SEQUENCE-SPECIFIC DNA-BINDING PROTEIN THAT HAS A HIGH CC AFFINITY FOR A 31 BP SEQUENCE IN THE YP1 GENE. SITE-SPECIFIC DNA CC BINDING TO 31 BP P ELEMENT INVERTED REPEATS. CC -!- SUBUNIT: HETERODIMER OF A 70 KDA AND A 80 KDA SUBUNIT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ATP-DEPENDENT DNA HELICASE II 70 KDA CC SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05208; AAA20644.1; -. DR EMBL; U15004; AAC46492.1; -. DR EMBL; AE003691; AAF54631.1; -. DR PIR; A53623; A53623. DR FlyBase; FBgn0011774; Irbp. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0004677; F:DNA-dependent protein kinase activity; IDA. DR InterPro; IPR006164; Ku. DR InterPro; IPR006165; Ku70. DR InterPro; IPR005160; Ku_C. DR InterPro; IPR005161; Ku_N. DR Pfam; PF02735; ku; 1. DR Pfam; PF03730; Ku_C; 1. DR Pfam; PF03731; Ku_N; 1. DR TIGRFAMs; TIGR00578; ku70; 1. KW Helicase; Nuclear protein; DNA-binding. FT CONFLICT 174 174 R -> S (IN REF. 1). FT CONFLICT 244 244 S -> P (IN REF. 1). FT CONFLICT 553 553 P -> H (IN REF. 3). SQ SEQUENCE 631 AA; 72495 MW; E5028FAA1974013C CRC64; MSTWNPENDV DLLSGSEDEE DVSMKRDYHG REAILFVVDA NLQTAGVERL LEALNIIRTA FISGLLVNDK DLIGLIFANT KHSPPPLEAS ALDNIVMPDN CAVFLPLRQL TKPIVEHYLE FMGGVETQFA DVYGLAEPDG RGRFDLMIRL CIEMLEKCGK KLNNAKIAYV TDVREPHPSN SNHFQAALQK ASDLEGKEFE FHVIPMVDDF DYEPFYKEFI TLSRAIELDA FQVPDAQMLR EILSDRKLKQ DFLRRCLGHF SFYLGPNLSM SVQYYNYFQR RAYPRKVQIL RRDNSVVRTK RVITVQKQKD DGSQDIEHEY QIKVTGGWYT CNVGERDLRI SMDQLNRVRN LHKPQMMLLG FKHRSSLPEV SYIKPANFMY PDDQSIIGSK RLFRALWERC LVRDKIAICL FMCKRKSIPR YVALVPVEAP DNGEDKNYRS LLCGDGFKIV YLPEAKHIRH LDLQDWNNTE NTADEQKVEF FQKIIKKLRV DYQPNLINDP SLDALQANLL ALSLDFSTDT KGLDNLLDTS QQDKRIEKLL PDYEMFAPEA EPPKKRAAKS TTAGASGPKM AKIDDDQLKE FEFVKSLNKD EALTSCTAAQ LHFILQHHFD VTMPKSSKKA KLVAKIEELH K // ID KZ_DROME STANDARD; PRT; 1192 AA. AC O46072; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable ATP-dependent helicase kurz. GN KZ OR EG:30B8.2 OR CG3228. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP PRELIMINARY SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92253387; PubMed=1579473; RA Tirronen M., Roos C.; RT "The kurz locus of Drosophila melanogaster shares conserved motifs RT with a family of yeast ATP dependent splicing factors."; RL Nucleic Acids Res. 20:1802-1802(1992). RN [2] RP REVISIONS. RA Roos C.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP DEVELOPMENTAL STAGE. RA Haenlin M., Roos C., Cassab A., Mohier E.; RT "Oocyte-specific transcription of fs(1)K10: a Drosophila gene RT affecting dorsal-ventral developmental polarity."; RL EMBO J. 6:801-807(1987). CC -!- DEVELOPMENTAL STAGE: MATERNAL PROTEIN DETECTABLE UP TO 6 HOURS OF CC EMBRYONIC DEVELOPMENT. CC -!- MISCELLANEOUS: 'KURZ' MEANS 'SHORT' IN GERMAN. CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. DEAH CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64418; CAB55570.1; -. DR EMBL; AL009195; CAA15706.1; -. DR EMBL; AE003423; AAF45757.1; -. DR PIR; T13424; T13424. DR FlyBase; FBgn0001330; kz. DR InterPro; IPR001410; DEAD. DR InterPro; IPR002464; DEAH_box. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR007502; Helicase_dom. DR Pfam; PF04408; HA2; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. KW ATP-binding; RNA-binding; Helicase; Nuclear protein. FT NP_BIND 283 290 ATP (BY SIMILARITY). FT SITE 379 382 DEAH BOX. SQ SEQUENCE 1192 AA; 134120 MW; 569D4477D2EF8095 CRC64; MGKKVHNAKA RQNPQTIVDN SAVKKIQIDV DAVAGGNQVG YDEANALVLP SEKRATKIKV DKVQHVKILS KKQRKHLQAI VDKKKKKEGR AQLLGDLAAV QIPEEELQQY TSISQVQTVG LKRLPTLDEY LAKKKERQAQ VLAEKSSASG LRVNAIKGSK RKLLVEEEEE LQAKRKNPNV ISVEEDDEDS SSSDEDDEEA PAQSAPIAIP TPVSIAPPQI AVKPPIKKLK PEPNPPACIH QTVYVPVHRT TEVQNARLRL PILAEEQQVM ETINENPIVI VAGETGSGKT TQLPQFLYEA GYAQHKMIGV TEPRRVAAIA MSKRVAHEMN LPESEVSYLI RFEGNVTPAT RIKFMTDGVL LKEIETDFLL SKYSVIILDE AHERSVYTDI LVGLLSRIVP LRHKRGQPLK LIIMSATLRV SDFTENTRLF KIPPPLLKVE ARQFPVTIHF QKRTPDDYVA EAYRKTLKIH NKLPEGGILI FVTGQQEVNQ LVRKLRRTFP YHHAPTKDVA KNGKVSEEEK EETIDDAAST VEDPKELEFD MKRVIRNIRK SKKKFLAQMA LPKINLDDYK LPGDDTEADM HEQPDEDDEQ EGLEEDNDDE LGLEDESGMG SGQRQPLWVL PLYSLLSSEK QNRIFLPVPD GCRLCVVSTN VAETSLTIPH IKYVVDCGRQ KTRLYDKLTG VSAFVVTYTS KASADQRAGR AGRISAGHCY RLYSSAVYND CFEDFSQPDI QKKPVEDLML QMRCMGIDRV VHFPFPSPPD QVQLQAAERR LIVLGALEVA KTENTDLPPA VTRLGHVISR FPVAPRFGKM LALSHQQNLL PYTVCLVAAL SVQEVLIETG VQRDEDVAPG ANRFHRKRQS WAASGNYQLL GDPMVLLRAV GAAEYAGSQG RLPEFCAANG LRQKAMSEVR KLRVQLTNEI NLNVSDVELG VDPELKPPTD AQARFLRQIL LAGMGDRVAR KVPLADIADK EERRRLKYAY NCADMEEPAF LHVSSVLRQK APEWVIYQEA YELQNGDSTK MFIRGITAIE PEWLLLYVPL LCNIREVRED PAPRFDKTSG KIFCHVDATF GKSGWELPLG EVEMPLSEKA CCYFGMFLLD GEVCSRLADF RSKLKSTPAS VIKSWSSMNN KVLRFKRALI TKQIHNRQAL IDQWNSDPHF LLEEYQNLLY DVALSELTPL WPPVDKKEPQ RQ // ID L259_DROME STANDARD; PRT; 1290 AA. AC P91660; Q9V571; Q9V572; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable multidrug resistance-associated protein lethal(2)03659 (Wunen DE region A protein). GN L(2)03659 OR CG8799/CG11803. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 808-921 FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=97138220; PubMed=8985246; RA Zhang N., Zhang J.P., Purcell K.J., Chen Y., Howard K.; RT "The Drosophila protein Wunen repels migrating germ cells."; RL Nature 385:64-67(1997). CC -!- FUNCTION: VITAL FOR DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: UNIFORM EXPRESSION IN EMBRYOS. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MRP SUBFAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003833; AAF58947.1; ALT_SEQ. DR EMBL; U73821; AAC47448.1; ALT_SEQ. DR FlyBase; FBgn0010549; l(2)03659. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0005524; F:ATP binding; NAS. DR GO; GO:0004009; F:ATP-binding cassette (ABC) transporter acti...; NAS. DR GO; GO:0007275; P:development; IMP. DR GO; GO:0006810; P:transport; NAS. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR001140; ABC_TM_transpt. DR InterPro; IPR003439; ABC_transporter. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR ProDom; PD000006; ABC_transporter; 2. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. KW Transport; Developmental protein; ATP-binding; Transmembrane; KW Glycoprotein; Repeat. FT TRANSMEM 76 96 POTENTIAL. FT TRANSMEM 122 142 POTENTIAL. FT TRANSMEM 199 219 POTENTIAL. FT TRANSMEM 222 242 POTENTIAL. FT TRANSMEM 321 341 POTENTIAL. FT TRANSMEM 343 363 POTENTIAL. FT TRANSMEM 704 724 POTENTIAL. FT TRANSMEM 762 782 POTENTIAL. FT TRANSMEM 830 850 POTENTIAL. FT TRANSMEM 855 875 POTENTIAL. FT TRANSMEM 942 962 POTENTIAL. FT DOMAIN 416 639 ABC TRANSPORTER 1. FT DOMAIN 1036 1269 ABC TRANSPORTER 2. FT NP_BIND 451 458 ATP (POTENTIAL). FT NP_BIND 1070 1077 ATP (POTENTIAL). FT CARBOHYD 478 478 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1171 1171 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1270 1270 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 779 779 F -> I (IN REF. 2). FT CONFLICT 783 783 K -> P (IN REF. 2). SQ SEQUENCE 1290 AA; 144007 MW; 73E4B2C193177B26 CRC64; MSFIHSYIFY TFSRLFNKYR YTIPIFRKGY RKTLDSTDLY RPLEEQKSDI LGNRLCASWE RELKNDGRSP SLVRALLRVF GWQLGFPGLA IFVVELGLRT LQPIFLVKLI SYFSGEPDAA NAGFYYAVAQ IVISALTVMI LTPTTFGIHH VCFKMRVAMG SMIFRKALRL TKGALGDTTS GHVVNLISND IPRLDSAPYT VHYLWVGPLQ VLVITYLMYQ EIGISAVFGV LFMLLFMPIQ MYLGTRTSAI QLKAAERTDN RIRMVNEIIS AIQVLKMYAW EQPFEQMVTH AREKEMNTIR QGQYIRGFDF ARRIVLSRVA IFLSLVGYVI LGKVFTPEIA FMITAYYNVL LAAMSIYVPS AIIQTAQFLT SIRRVEQFMQ SEELGSSDKS EGPSKDTVPG NPPSNNNEAD LLKSAISIRD LKAKWDPNSP DYTLSGINLE IKPGSVVAVI GLTGSGKSSL IQAILGELKA NSGQLQVNGS LSYTSQESWL FSGTVRQNIL FGQPMDSQRY EEVVKKCALE RDFDLLPLRD NTIVGERGAT LSGGQKARIS LARSVYRKAS IYLLDDPLSA VDASVARHLF DQCVRGHLRG STVVLVTHQE QFLPHVDQIV ILANGQIKAL GDYESLLKTG LITGLGSLSK TDKAKTEEQE PLNLNSPDNK NEVTPIKENS EQTVGGSSSG KEHVERQESG GISLALYRKY FQAGGGLVAF LVMLSSSVLA QVAVTGGDYF LTYWVKKEST AAGHGEMEDM ESKSMDVYKY TLIIILSVIM NLSSSFLLFN IAKKASIRLH NTIFNRVTRA DMHFFSINKH GSILNRFTKD MSQVDEVLPV VLVDVMQIAL WLAGIIIVIA NVNPLLLVPT LMLSVIFYHL RNLYLKTSRD LKRVEAINRS PVYSHLAASL NGLTTIRALD AQRVLEKEFD SYQDAHSSAF FMYISTSQAF GYCMNCICVI YISIITLSFF AFPPGNGADV GLVITQAMGL IDMVQWGVRQ TAELENTMTA VERVVEYESI EPEGMLEAPD DKKPPKTWPE QGEIIFKELN LRYTPNAKAE NVLKSLSFVI QPREKVGIVG RTGAGKSSLI NALFRLSYTD GSVLIDTRDT RQMGLHDLRR QISIIPQEPV LFSGTMRYNL DPFDEYSDEK LWGCLEEVKL KEVVSDLPDG LASKISEGGT NFSVGQRQLV CLARAILREN RILVMDEATA NVDPQTDGLI QATIRSKFRD CTVLTIAHRL HTIIDSDKVM VMDAGRVVEF GSPYELMTKS DSKVFHNLVN QSGRASYEGL LKIAQEVRFN // ID L2AM_DROME STANDARD; PRT; 510 AA. AC P18486; Q9VIZ8; DT 01-NOV-1990 (Rel. 16, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-methyldopa hypersensitive protein (EC 4.1.1.-). GN AMD OR L(2)AMD OR CG10501. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87031534; PubMed=3021571; RA Marsh J.L., Erfle M.P., Leeds C.A.; RT "Molecular localization, developmental expression and nucleotide RT sequence of the alpha-methyldopa hypersensitive gene of Drosophila."; RL Genetics 114:453-467(1986). RN [2] RP REVISIONS. RA Marsh J.L.; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PARTICIPATES IN CATECHOLAMINE METABOLISM. IT PLAYS A CC VITAL ROLE IN CUTICLE DEVELOPMENT. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: REACHES A MAXIMUM IN MID-EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE GROUP II DECARBOXYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04695; CAA28400.1; -. DR EMBL; AE003661; AAF53760.1; -. DR PIR; A28569; A28569. DR FlyBase; FBgn0000075; amd. DR GO; GO:0016831; F:carboxy-lyase activity; NAS. DR GO; GO:0006584; P:catecholamine metabolism; IMP. DR GO; GO:0040003; P:cuticle biosynthesis (sensu Insecta); IMP. DR InterPro; IPR002129; Pyridoxal_deC. DR Pfam; PF00282; pyridoxal_deC; 1. DR PRINTS; PR00800; YHDCRBOXLASE. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. KW Catecholamine metabolism; Lyase; Decarboxylase; Pyridoxal phosphate; KW Cuticle. FT BINDING 303 303 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT CONFLICT 71 72 WQ -> SE (IN REF. 1). FT CONFLICT 370 370 G -> E (IN REF. 1). FT CONFLICT 379 379 R -> A (IN REF. 1). FT CONFLICT 477 478 EQ -> DE (IN REF. 1). FT CONFLICT 493 494 QH -> HD (IN REF. 1). SQ SEQUENCE 510 AA; 57021 MW; 94464F49896E7654 CRC64; MDAKEFREFG KAAIDYIADY LENIRDDDVL PNVEPGYLLD LLPTEMPEEP EAWKDVLGDI SRVIKPGLTH WQSPHMHAYY PTSTSYPSIV GEMLASGFGV IGFSWICSPA CTELEVVVMD WLAKFLKLPA HFQHASDGPG GGVIQGSASE AVLVAVLAAR EQAVANYRES HPELSESEVR GRLVAYSSDQ SNSCIEKAGV LAAMPIRLLP AGEDFVLRGD TLRGAIEEDV AAGRIPVICV ATLGTTGTCA YDDIESLSAV CEEFKVWLHV DAAYAGGAFA LEECSDLRKG LDRVDSLNFN LHKFMLVNFD CSAMWLRDAN KVVDSFNVDR IYLKHKHEGQ SQIPDFRHWQ IPLGRRFRAL KVWITFRTLG AEGLRNHVRK HIELAKQFEQ LVLKDSRFEL VAPRALGLVC FRPKGDNEIT TQLLQRLMDR KKIYMVKAEH AGRQFLRFVV CGMDTKASDI DFAWQEIESQ LTDLQAEQSL VARKSGNVGD LAQHFQIHLS TENATHEKSQ // ID L2CC_DROME STANDARD; PRT; 203 AA. AC P24156; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE L(2)37CC protein. GN L(2)37CC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86312887; PubMed=3092183; RA Eveleth D.D. Jr., Marsh J.L.; RT "Sequence and expression of the Cc gene, a member of the dopa RT decarboxylase gene cluster of Drosophila: possible translational RT regulation."; RL Nucleic Acids Res. 14:6169-6183(1986). CC -!- FUNCTION: REQUIRED FOR LARVAL METABOLISM OR FOR THE PROGRESSION CC OF THE LARVA INTO A PUPA. CC -!- SIMILARITY: BELONGS TO THE PROHIBITIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04228; CAA27810.1; -. DR EMBL; X04227; CAA27807.1; -. DR PIR; C25511; C25511. DR FlyBase; FBgn0002031; l(2)37Cc. DR InterPro; IPR001107; Band_7. DR InterPro; IPR000163; Prohibitin. DR Pfam; PF01145; Band_7; 1. DR PRINTS; PR00679; PROHIBITIN. DR SMART; SM00244; PHB; 1. KW Developmental protein. SQ SEQUENCE 203 AA; 22817 MW; B15D085CC0862A11 CRC64; MGAAAHHLRT IRSQPRNVPE ITGSKDLQNV NITLRILYRP IPDQLPKIYT ILGQDYDERV LPSIAPEMVS QRVSQELTVR AKQFGFILDD ISLTHLTFGR EFTLAVEMKQ VAQQEAEKAR FVVEKAEQQK LASIISAEGD AERACVGQVI ARPETVWWSL RLIDRPRYRL TSYPRSRGVA YLPSGQSHAA QSAIDHRAVA GCI // ID L2DT_DROME STANDARD; PRT; 758 AA. AC Q24371; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Lethal(2)denticleless protein (DTL83 protein). GN L(2)DTL OR DTL83. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96257214; PubMed=8666267; RA Kurzik-Dumke U., Neubauer M., Debes A.; RT "Identification of a novel Drosophila melanogaster heat-shock gene, RT lethal(2)denticleless [l(2)dtl], coding for an 83-kDa protein."; RL Gene 171:163-170(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-2; RA Gunacker S., Neubhuer M., Kurzik-Dumke U.; RT "Sequence of a 10291 nt genomic region of Drosophila melanogaster RT harbouring the genes l(2)tid, l(2)not, l(2)rot, and l(2)dtl."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED DURING EMBRYOGENESIS CC WITH NO SIGN OF TISSUE SPECIFICITY IN EXPRESSION UP TO STAGE 17. CC -!- DEVELOPMENTAL STAGE: DETECTED AT ALL DEVELOPMENTAL STAGES. THE CC EXTREMELY HIGH LEVEL OF TRANSCRIPTION DETECTED IN THE EARLY EMBRYO CC AND IN ADULTS IS CAUSED BY MATERNAL MESSAGE. CC -!- INDUCTION: BY HEAT SHOCK. CC -!- SIMILARITY: CONTAINS 6 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X83414; CAA58441.1; -. DR EMBL; X98094; CAA66723.1; -. DR PIR; S51748; S51748. DR FlyBase; FBgn0013548; l(2)dtl. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 5. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Heat shock; Repeat; WD repeat. FT REPEAT 88 118 WD 1. FT REPEAT 132 163 WD 2. FT REPEAT 183 238 WD 3. FT REPEAT 253 292 WD 4. FT REPEAT 309 338 WD 5. FT REPEAT 351 382 WD 6. FT DOMAIN 558 567 POLY-ALA. FT DOMAIN 672 675 POLY-GLY. FT DOMAIN 721 724 POLY-THR. SQ SEQUENCE 758 AA; 82352 MW; 3A05FEF78D0502F1 CRC64; MATAMRGPTT SPCAAFPVAK EDSWRGIAPA NYCPDFNPEP PIFSAKFANC DGYRHILAIA NEDGKITLQD TTQRNHQPEE QSLVGPQCHF NAVFDLEWAP GQMRFVSASG DHTARLWEVA GSGIRGLNSY VGHTRSVKSA AFKRTDPAVF ATGGRDGAIL IWDIRANLNM DLTSRVDNCI YSGHTGGPGT PVSQRKQRTR TPKMAGGTTS SSITGLAFQD NDTLISCGAG DGVIKVWDLR RNYTAYKKEP LPRHKLPYAG SSTFRGFTNL IVDASGTRLY ANCMDNTIYC YNLASYSPRP LACYKGLLNS TFYIKSCLSP DGKYLLSGSS DERAYIWNLD HAEEPLVALA GHTVEVTCVA WGSSHDCPIV TCSDDARHKI WRIGPDLDGL SEAERAEKYR GTASYVREFG KKAFGPSSGN HKYNLRDLES TPRSLKRLMD QNERTPGSVE KTTTKRSFLE MLGVAGQETE ATEQPQKRAK PLESRGRRLF GPSSQETACR HIQLQSINEE DASPSKRQKE NSAAEDVSPL HKLLSTPSHS PLSENVNHVY TSPPTTSAAA AAVAADALNP PPISAAIYSP TSNLPNYVLD GEAPHLGIMS PKRKAKEKVD WLTNIRKQKL MSGRAHVTLS EKISEEQQAD VLASPRLQSL RQSECSPRIH ASPRRRISHT DGGGGTPAGS SSHSHSQSQP KTPTSSRRNS ETTLLRFFSI QRSSSVPAEE TTTTNAAPSS SDPHPPAVTA PAATPLSMRT PTTAVGSD // ID L2GL_DROME STANDARD; PRT; 1161 AA. AC P08111; Q24377; Q9VPI1; DT 01-AUG-1988 (Rel. 08, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lethal(2) giant larvae protein. GN L(2)GL OR CG2671. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM P127). RA Luetzelschwab R., Klaembt C., Rossa R., Schmidt O.; RT "A protein product of the Drosophila recessive tumor gene, l(2) RT giant gl, potentially has cell adhesion properties."; RL EMBO J. 6:1791-1797(1987). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=87244337; PubMed=3036370; RA Jacob L., Opper M., Metzroth B., Phannavong B., Mechler B.M.; RT "Structure of the l(2)gl gene of Drosophila and delimitation of its RT tumor suppressor domain."; RL Cell 50:215-225(1987). RN [3] RP SEQUENCE FROM N.A. (ISOFORM P127). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM P127). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ISOFORM P78 HAS AN ESSENTIAL ROLE IN CONTROL OF CELL CC PROLIFERATION AND DIFFERENTIATION DURING DEVELOPMENT AND COULD ACT CC AS TUMOR SUPPRESSOR. ISOFORM P217 HAS AN ACCESSORY FUNCTION IN CC THIS RESPECT. CC -!- SUBUNIT: MAY FORM MULTIMERIC COMPLEXES. CC -!- SUBCELLULAR LOCATION: CELLULAR MEMBRANE OR INTERCELLULAR MATRIX. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=p127; CC IsoId=P08111-1; Sequence=Displayed; CC Name=p78; Synonyms=EC371; CC IsoId=P08111-2; Sequence=VSP_004299, VSP_004300; CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE EPITHELIAL CELLS OF THE CC DIGESTIVE TRACT AND IN GONADS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED ABUNDANTLY IN EARLY EMBRYOGENESIS. CC MODERATE EXPRESSION IS FOUND IN LARVAL AND ADULT STAGES. CC -!- SIMILARITY: BELONGS TO THE L(2)GL FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05426; CAA29007.1; -. DR EMBL; M17022; AAA28671.1; -. DR EMBL; M17022; AAA28672.1; -. DR EMBL; AE003590; AAF51570.1; -. DR EMBL; AY051654; AAK93078.1; -. DR PIR; A27069; A27069. DR PIR; A27868; A27868. DR FlyBase; FBgn0002121; l(2)gl. DR GO; GO:0016327; C:apicolateral plasma membrane; IDA. DR GO; GO:0005938; C:cell cortex; IDA. DR GO; GO:0005856; C:cytoskeleton; NAS. DR GO; GO:0005578; C:extracellular matrix; IDA. DR GO; GO:0005918; C:septate junction; NAS. DR GO; GO:0008021; C:synaptic vesicle; NAS. DR GO; GO:0045159; F:myosin II binding; IGI. DR GO; GO:0045175; P:basal protein localization; IMP. DR GO; GO:0045197; P:establishment and/or maintenance of epithel...; NAS. DR GO; GO:0016334; P:establishment and/or maintenance of polarit...; IGI. DR GO; GO:0045184; P:establishment of protein localization; IMP. DR GO; GO:0007399; P:neurogenesis; IMP. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0008360; P:regulation of cell shape; NAS. DR GO; GO:0016082; P:synaptic vesicle priming; NAS. DR GO; GO:0007179; P:TGFbeta receptor signaling pathway; IGI. DR InterPro; IPR000664; Lethal2_giant. DR PRINTS; PR00962; LETHAL2GIANT. KW Anti-oncogene; Repeat; Developmental protein; Alternative splicing. FT REPEAT 524 538 1. FT REPEAT 613 627 2. FT VARSPLIC 708 708 V -> F (in isoform p78). FT /FTId=VSP_004299. FT VARSPLIC 709 1161 Missing (in isoform p78). FT /FTId=VSP_004300. FT CONFLICT 2 2 L -> F (IN REF. 2). FT CONFLICT 37 38 KP -> A (IN REF. 1). FT CONFLICT 185 185 G -> S (IN REF. 1). FT CONFLICT 227 227 G -> R (IN REF. 1). FT CONFLICT 243 245 FTW -> RYL (IN REF. 1). FT CONFLICT 304 304 Y -> N (IN REF. 1). FT CONFLICT 331 331 F -> I (IN REF. 1). FT CONFLICT 338 338 N -> S (IN REF. 1). FT CONFLICT 366 366 I -> T (IN REF. 1). FT CONFLICT 388 388 V -> L (IN REF. 1). FT CONFLICT 512 515 VKKI -> SEEN (IN REF. 1). FT CONFLICT 667 675 KLRKGRSTR -> SFARVDQTK (IN REF. 1). FT CONFLICT 727 727 T -> S (IN REF. 1). FT CONFLICT 959 959 R -> G (IN REF. 2). FT CONFLICT 1095 1095 A -> G (IN REF. 1). SQ SEQUENCE 1161 AA; 126892 MW; 979F73A01DA62A1A CRC64; MLKFIRGKGQ QPSADRHRLQ KDLFAYRKTA QHGFPHKPSA LAYDPVLKLM AIGTQTGALK VFGQPGVELY GQHTLLNNSA SELNVQLLEW VYGTGRILSL TAANQLILWE PVGATLLPIK TLPFDGKLKK VSSLCCSLSK DLLWIGTEGG NIYQLDLHTF TIKEPVIYHD VVLEQVPPAY KLNPGAIESI RQLPNSPSKL LVAYNRGLCV LWDFESASVQ RAYIAPGHGQ SVGLTVNFEG SEFTWYHADG SYATWSIDNP EPPSNVNYVP YGPDPCKSIN RLYKGKRRSN DVIVFSGGMP RSAYGDHNCV SVHASDGHKV CLDFTSKVID FFVTFENNRD VAEVLVVLLE EELCAYDLTD PNICAIKAPY LHSVHASAVT CNYLASEVVQ SVYESILRAG DEQDIDYSNI SWPITGGTLP DNLEESVEED ATKLYEILLT GHEDGSVKFW DCTGVLLKPI YNFKTSSIFG SESDFRDDAA ADMSAEQVDE GEPPFRKSGL FDPYSDDPRL AVKKIAFCPK TGQLIVGGTA GQIVIADFID LPEKVSLKYI SMNLVSDRDG FVWKGHDQLN VRSNLLDGEA IPTTERGVNI SGVLQVLPPA SITCMALEAS WGLVSGGTAH GLVLFDFKNF VPVFHRCTLN PNDLTGAGEQ LSRRKSFKKS LRESFRKLRK GRSTRTNQSN QVPTTLEARP VERQIEARCA DDGLGSMVRC LLFAKTYVTN VNITSPTLWS ATNASTVSVF LLHLPPAQTA ATAVPSASGN APPHMPRRIS AQLAKEIQLK HRAPVVGISI FDQAGSPVDQ LNAGENGSPP HRVLIASEEQ FKVFSLPQLK PINKYKLTAN EGARIRRIHF GSFSCRISPE TLQSMHGCSP TKSTRSHGDG EADPNISGSL AVSRGDVYNE TALICLTNMG DIMVLSVPEL KRQLNAAAVR REDINGVSSL CFTNSGEALY MMSSSELQRI ALATSRVVQP TGVVPVEPLE NEESVLEEND AENNKETYAC DEVVNTYEIK NPSGISICTR PAEENVGRNS VQQVNGVNIS NSPNQANETI SSSIGDITVD SVRDHLNMTT TTLCSINTEE TIGRLSVLST QTNKASTTVN MSEIPNINIS NLEDLESKRN TTETSTSSVV IKSIITNISH EKTNGDNKIG TPKTAPEESQ F // ID L2K1_DROME STANDARD; PRT; 221 AA. AC Q9V574; P91662; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lethal(2)k10201 protein (Wunen region B protein). GN L(2)K10201 OR CG13951/CG8803. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RX MEDLINE=97138220; PubMed=8985246; RA Zhang N., Zhang J.P., Purcell K.J., Chen Y., Howard K.; RT "The Drosophila protein Wunen repels migrating germ cells."; RL Nature 385:64-67(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: VITAL FOR DEVELOPMENT. CC -!- SIMILARITY: CONTAINS 2 C2H2-TYPE ZINC FINGERS. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U73823; AAC47450.1; ALT_SEQ. DR EMBL; AE003833; AAF58944.2; -. DR FlyBase; FBgn0016970; l(2)k10201. DR GO; GO:0007275; P:development; IMP. DR InterPro; IPR007087; Znf_C2H2. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG. KW Developmental protein; Metal-binding; Zinc; Zinc-finger; Repeat. FT ZN_FING 74 97 C2H2-TYPE 1. FT ZN_FING 113 138 C2H2-TYPE 2. SQ SEQUENCE 221 AA; 24962 MW; CC906EC62398DAD9 CRC64; MDSEAAGVAL LSREQIIRIL SEVPAGFIKP TDPPAPSLAP FKKLGVLVDI DDILGEQDAA AARIRDNIDK EQSYSCVECR KMLPTAHLLD LHITEQHDCY FAASVERGDK PMFSCFLEEC TIKFHTARQR KDHCIITHKL PANYRFDHSK NRGKQKHQGK SKPNSMEVDE VIEETKSLPY VKAFSFGHQT QRSFYTGKDQ RSGKTLDDVQ AMKEAINDIL D // ID LACH_DROME STANDARD; PRT; 359 AA. AC Q24372; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lachesin precursor. GN LAC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94038693; PubMed=8223276; RA Karlstrom R.O., Wilder L.P., Bastiani M.J.; RT "Lachesin: an immunoglobulin superfamily protein whose expression RT correlates with neurogenesis in grasshopper embryos."; RL Development 118:509-522(1993). CC -!- FUNCTION: MAY PLAY A ROLE IN EARLY NEURONAL DIFFERENTIATION AND CC AXON OUTGROWTH. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR (BY CC SIMILARITY). CC -!- DEVELOPMENTAL STAGE: EXPRESSED ON DIFFERENTIATING NEURONAL CELLS CC FROM THE ONSET OF NEUROGENESIS IN BOTH THE CENTRAL AND PERIPHERAL CC NERVOUS SYSTEMS. CC -!- SIMILARITY: CONTAINS 2 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 IMMUNOGLOBULIN-LIKE V-TYPE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13255; AAC37184.1; -. DR HSSP; P56276; 1TLK. DR FlyBase; FBgn0010238; Lac. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR Pfam; PF00047; ig; 3. DR SMART; SM00408; IGc2; 2. DR PROSITE; PS50835; IG_LIKE; 3. KW Immunoglobulin domain; Cell adhesion; Glycoprotein; GPI-anchor; KW Repeat; Signal; Lipoprotein. FT SIGNAL 1 25 POTENTIAL. FT CHAIN 26 336 LACHESIN. FT PROPEP 337 359 REMOVED IN MATURE FORM (POTENTIAL). FT DOMAIN 29 130 IG-LIKE V-TYPE. FT DOMAIN 135 221 IG-LIKE C2-TYPE 1. FT DOMAIN 226 317 IG-LIKE C2-TYPE 2. FT DISULFID 50 113 POTENTIAL. FT DISULFID 157 204 POTENTIAL. FT DISULFID 247 303 POTENTIAL. FT CARBOHYD 92 92 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 140 140 N-LINKED (GLCNAC...) (POTENTIAL). FT LIPID 336 336 GPI-anchor amidated alanine (Potential). SQ SEQUENCE 359 AA; 39998 MW; D1F513E2B9D886E6 CRC64; MWRPSISNCV WSTLLLAIFV QQTLAQRTPT ISYITQEQIK DIGGTVEFDC SVQYAKEYNV LFLKTDSDPV FLSTGSTLVI KDSRFSLRYD PNSSTYKLQI KDIQETDAGT YTCQVVISTV HKVSAEVKLS VRRPPVISDN STQSVVASEG SEVQMECYAS GYPTPTITWR RENNAILPTD SATYVGNTLR IKSVKKEDRG TYYCVADNGV SKGDRRNINV EVEFAPVITV PRPRLGQALQ YDMDLECHIE AYPPPAIVWT KDDIQLANNQ HYSISHFATA DEYTDSTLRV ITVEKRQYGD YVCKATNRFG EAEARVNLFE TIIPVCPPAC GQAYIAGAED VSATSFALVG ISARLLFAR // ID LAM0_DROME STANDARD; PRT; 622 AA. AC P08928; DT 01-NOV-1988 (Rel. 09, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lamin Dm0. GN LAM. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91065636; PubMed=2123469; RA Osman M., Paz M., Landesman Y., Fainsod A., Gruenbaum Y.; RT "Molecular analysis of the Drosophila nuclear lamin gene."; RL Genomics 8:217-224(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88153889; PubMed=3126192; RA Gruenbaum Y., Landesman Y., Drees B., Bare J.W., Saumweber H., RA Paddy M.R., Sedat J.W., Smith D.E., Benton B.M., Fisher P.A.; RT "Drosophila nuclear lamin precursor Dm0 is translated from either of RT two developmentally regulated mRNA species apparently encoded by a RT single gene."; RL J. Cell Biol. 106:585-596(1988). RN [3] RP REVISIONS TO 24-39 AND 254-263. RA Stuurman N., Maus N., Fisher P.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: LAMINS ARE COMPONENTS OF THE NUCLEAR LAMINA, A FIBROUS CC LAYER ON THE NUCLEOPLASMIC SIDE OF THE INNER NUCLEAR MEMBRANE, CC WHICH IS THOUGHT TO PROVIDE A FRAMEWORK FOR THE NUCLEAR ENVELOPE CC AND MAY ALSO INTERACT WITH CHROMATIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: THREE FORMS OF LAMIN HAVE BEEN IDENTIFIED IN D.MELANOGASTER, CC LAMIN DM0 IS RAPIDLY PROCESSED TO LAMIN DM1 IN THE CYTOPLASM, CC DM1 IS THEN ASSEMBLED IN THE NUCLEAR ENVELOPE AND IS THEN CC PHOSPHORYLATED, FORMING LAMIN DM2. CC -!- SIMILARITY: BELONGS TO THE INTERMEDIATE FILAMENT FAMILY. CC THIS IS A B TYPE LAMIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16275; CAA34351.1; -. DR EMBL; X07278; CAA30259.1; -. DR PIR; A29965; A29965. DR PIR; A37103; A37103. DR HSSP; P36956; 1AM9. DR FlyBase; FBgn0002525; Lam. DR GO; GO:0007084; P:nuclear envelope reassembly; IDA. DR GO; GO:0007430; P:terminal branching of trachea, cytoplasmic ...; IMP. DR InterPro; IPR001664; IF. DR InterPro; IPR001322; IF_tail_C. DR Pfam; PF00038; filament; 1. DR Pfam; PF00932; IF_tail; 1. DR PROSITE; PS00226; IF; FALSE_NEG. KW Intermediate filament; Coiled coil; Nuclear protein; Lipoprotein; KW Prenylation; Phosphorylation. FT DOMAIN 1 56 HEAD. FT DOMAIN 57 408 ROD. FT DOMAIN 409 622 TAIL. FT DOMAIN 55 91 COIL 1A. FT DOMAIN 92 103 LINKER 1. FT DOMAIN 104 241 COIL 1B. FT DOMAIN 242 265 LINKER 2. FT DOMAIN 266 408 COIL 2. FT SITE 289 289 HEPTAD CHANGE OF PHASE. FT SITE 353 353 HEPTAD CHANGE OF PHASE. FT DOMAIN 446 451 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT LIPID 619 619 S-farnesyl cysteine (By similarity). FT CONFLICT 24 39 PSAGPQPPPPSTHSQT -> AIGSAAAAAVHSLAD (IN FT REF. 1). FT CONFLICT 135 135 R -> E (IN REF. 1). FT CONFLICT 255 263 RLSSEYDAK -> SPQLRVRCQ (IN REF. 1). FT CONFLICT 270 271 DV -> EL (IN REF. 1). SQ SEQUENCE 622 AA; 71249 MW; DC8F0187CCF2E2A8 CRC64; MSSKSRRAGT ATPQPGNTST PRPPSAGPQP PPPSTHSQTA SSPLSPTRHS RVAEKVELQN LNDRLATYID RVRNLETENS RLTIEVQTTR DTVTRETTNI KNIFEAELLE TRRLLDDTAR DRARAEIDIK RLWERNEELK NKLDKKTKEC TTAEGNVRMY ESRANELNNK YNQANADRKK LNEDLNEALK ELERLRKQFE ETRKNLEQET LSRVDLENTI QSLREELSFK DQIHSQEINE SRRIKQTEYS EIDGRLSSEY DAKLKQSLQD VRAQYEEQMQ INRDEIQSLI EDKIQRLQEA AARTSNSTHK SIEELRSTRV RIDALNANIN ELEQANADLN ARIRDLERQL DNDRERHGQE IDLLEKELIR LREEMTQQLK EYQDLMDIKV SLDLEIAAYD KLLVGEEARL NITPATNTAT VQSFSQSLRN STRATPSRRT PSAAVKRKRA VVDESEDHSV ADYYVSASAK GNVEIKEIDP EGKFVRLFNK GSEEVAIGGW QLQRLINEKG PSTTYKFHRS VRIEPNGVIT VWSADTKASH EPPSSLVMKS QKWVSADNTR TILLNSEGEA VANLDRIKRI VSQHTSSSRL SRRRSVTAVD GNEQLYHQQG DPQQSNEKCA IM // ID LAMC_DROME STANDARD; PRT; 621 AA. AC Q03427; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Lamin C (PG-IF). GN LAMC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=93300998; PubMed=8314904; RA Bossie C.A., Sanders M.M.; RT "A cDNA from Drosophila melanogaster encodes a lamin C-like RT intermediate filament protein."; RL J. Cell Sci. 104:1263-1272(1993). CC -!- FUNCTION: LAMINS ARE COMPONENTS OF THE NUCLEAR LAMINA, A FIBROUS CC LAYER ON THE NUCLEOPLASMIC SIDE OF THE INNER NUCLEAR MEMBRANE, CC WHICH IS THOUGHT TO PROVIDE A FRAMEWORK FOR THE NUCLEAR ENVELOPE CC AND MAY ALSO INTERACT WITH CHROMATIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN 0-20 HOUR EMBRYOS. CC -!- POLYMORPHISM: THERE IS AT LEAST ONE ISOFORM OF THIS PROTEIN. CC -!- SIMILARITY: BELONGS TO THE INTERMEDIATE FILAMENT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L07933; AAA28666.1; -. DR FlyBase; FBgn0010397; LamC. DR GO; GO:0005638; C:lamin filament; NAS. DR InterPro; IPR001664; IF. DR InterPro; IPR001322; IF_tail_C. DR Pfam; PF00038; filament; 1. DR Pfam; PF00932; IF_tail; 1. DR PROSITE; PS00226; IF; FALSE_NEG. KW Intermediate filament; Coiled coil; Nuclear protein; Phosphorylation; KW Polymorphism. FT DOMAIN 1 47 HEAD. FT DOMAIN 48 403 ROD. FT DOMAIN 404 621 TAIL. FT DOMAIN 47 85 COIL 1A. FT DOMAIN 86 95 LINKER 1. FT DOMAIN 96 233 COIL 1B. FT DOMAIN 234 257 LINKER 2. FT DOMAIN 258 403 COIL 2. FT DOMAIN 453 458 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT SITE 281 281 HEPTAD CHANGE OF PHASE. FT SITE 345 345 HEPTAD CHANGE OF PHASE. FT VARIANT 166 166 S -> A (IN PG-9). FT VARIANT 528 528 I -> V (IN PG-9). SQ SEQUENCE 621 AA; 69855 MW; 7EFB7375803C2C87 CRC64; MSARRVTLNT RVSRASTSTP VGGASTSSRV GATSPTSPTR TSRQQEKEEL QHLNDRLACY IDRMRNLENE NSRLTQELNL AQDTVNRETS NLKAVYEKEL AAARKLLDET AKEKAKLEID IKRLWEENDD LKPRLDKKTK EATVAENNAR LYENRYNEVN GKYNQSLADR KKFEDQAKEL ALENERLRRQ LDDLRKQLEA ETLARVDLEN QNQSLREELA FKDQVHTQEL TETRSRRQIE ISEIDGRLSR QYEAKLQQSL QELRDQYEGQ MRINREEIEL LYDNEIQNLK AAANRAAQGS ALATEEVRLM RTKIDGLNAK LQNLEDTNAG LNARIRELEN LLDTERQRHN QYIASLEAEL QRIRDEMAHQ LQEYQGLMDI KVSLDLEIAA YDKLLCGEER RLNIESPGRP TTDSGISSNG SHLTASASSR SGRVTPSGRR SATPGISGSS AVKRRRTVID ESEDRTLSEY SVNAAAKGDL EIIEADVEGR FIKLHNKGTE EINLTGWQLT RIAGDEELAF KFSRGSKILG GASVTIWSVD AGTAHDPPNN LVMKKKWPVA NSMRSVLANA DKEDVASYDR VRANVSSHTS RHRSSGTPST GFTLGSGAGS TGVRSLFSLL F // ID LAR_DROME STANDARD; PRT; 2029 AA. AC P16621; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein-tyrosine phosphatase Lar precursor (EC 3.1.3.48) (Protein- DE tyrosine-phosphate phosphohydrolase) (dLAR). GN LAR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90046860; PubMed=2554325; RA Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.; RT "A family of receptor-linked protein tyrosine phosphatases in humans RT and Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96178473; PubMed=8598047; RA Krueger N.X., van Vactor D., Wan H.I., Gelbart W.M., Goodman C.S., RA Saito H.; RT "The transmembrane tyrosine phosphatase DLAR controls motor axon RT guidance in Drosophila."; RL Cell 84:611-622(1996). CC -!- FUNCTION: IT IS POSSIBLE THAT DLAR IS A CELL ADHESION RECEPTOR. CC IT POSSESSES AN INTRINSIC PROTEIN TYROSINE PHOSPHATASE ACTIVITY CC (PTPASE). IT CONTROLS MOTOR AXON GUIDANCE. CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: SELECTIVELY EXPRESSED IN A SUBSET OF AXONS AND CC PIONEER NEURONS IN THE EMBRYO. CC -!- SIMILARITY: CONTAINS 3 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -!- SIMILARITY: CONTAINS 9 FIBRONECTIN TYPE III DOMAINS. CC -!- SIMILARITY: CONTAINS 2 PROTEIN-TYROSINE PHOSPHATASE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27700; AAA28668.1; -. DR EMBL; U36857; AAC47002.1; -. DR EMBL; U36849; AAC47002.1; JOINED. DR EMBL; U36850; AAC47002.1; JOINED. DR EMBL; U36851; AAC47002.1; JOINED. DR EMBL; U36852; AAC47002.1; JOINED. DR EMBL; U36853; AAC47002.1; JOINED. DR EMBL; U36854; AAC47002.1; JOINED. DR EMBL; U36855; AAC47002.1; JOINED. DR EMBL; U36856; AAC47002.1; JOINED. DR PIR; A36182; TDFFLK. DR HSSP; P28827; 1RPM. DR FlyBase; FBgn0000464; Lar. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA. DR GO; GO:0008045; P:motor axon guidance; IMP. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003961; FN_III. DR InterPro; IPR003962; FnIII_subd. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR InterPro; IPR000387; TYR_phosphatase. DR InterPro; IPR000242; Tyr_PP. DR Pfam; PF00041; fn3; 9. DR Pfam; PF00047; ig; 3. DR Pfam; PF00102; Y_phosphatase; 2. DR PRINTS; PR00014; FNTYPEIII. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 9. DR SMART; SM00408; IGc2; 3. DR SMART; SM00194; PTPc; 2. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. KW Hydrolase; Receptor; Glycoprotein; Signal; Transmembrane; KW Cell adhesion; Immunoglobulin domain; Repeat. FT SIGNAL 1 32 FT CHAIN 33 2029 PROTEIN-TYROSINE PHOSPHATASE LAR. FT DOMAIN 33 1377 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1378 1402 POTENTIAL. FT DOMAIN 1403 2029 CYTOPLASMIC (POTENTIAL). FT DOMAIN 36 128 IG-LIKE C2-TYPE 1. FT DOMAIN 140 224 IG-LIKE C2-TYPE 2. FT DOMAIN 234 316 IG-LIKE C2-TYPE 3. FT DOMAIN 320 417 FIBRONECTIN TYPE-III 1. FT DOMAIN 418 512 FIBRONECTIN TYPE-III 2. FT DOMAIN 513 607 FIBRONECTIN TYPE-III 3. FT DOMAIN 608 706 FIBRONECTIN TYPE-III 4. FT DOMAIN 707 809 FIBRONECTIN TYPE-III 5. FT DOMAIN 810 906 FIBRONECTIN TYPE-III 6. FT DOMAIN 907 1007 FIBRONECTIN TYPE-III 7. FT DOMAIN 1008 1102 FIBRONECTIN TYPE-III 8. FT DOMAIN 1103 1207 FIBRONECTIN TYPE-III 9. FT DOMAIN 1492 1738 PROTEIN-TYROSINE PHOSPHATASE 1. FT DOMAIN 1781 2029 PROTEIN-TYROSINE PHOSPHATASE 2. FT ACT_SITE 1670 1670 PHOSPHOCYSTEINE INTERMEDIATE (BY FT SIMILARITY). FT ACT_SITE 1961 1961 PHOSPHOCYSTEINE INTERMEDIATE (BY FT SIMILARITY). FT DISULFID 57 111 POTENTIAL. FT DISULFID 161 209 POTENTIAL. FT DISULFID 256 301 POTENTIAL. FT CARBOHYD 176 176 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 253 253 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 298 298 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 553 553 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 616 616 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 666 666 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 721 721 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 774 774 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 915 915 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 962 962 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1183 1183 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1304 1304 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 2029 AA; 229027 MW; 536A0C794D3DC800 CRC64; MGLQMTAARP IAALSLLVLS LLTWTHPTIV DAAHPPEIIR KPQNQGVRVG GVASFYCAAR GDPPPSIVWR KNGKKVSGTQ SRYTVLEQPG GISILRIEPV RAGRDDAPYE CVAENGVGDA VSADATLTIY EGDKTPAGFP VITQGPGTRV IEVGHTVLMT CKAIGNPTPN IYWIKNQTKV DMSNPRYSLK DGFLQIENSR EEDQGKYECV AENSMGTEHS KATNLYVKVR RVPPTFSRPP ETISEVMLGS NLNLSCIAVG SPMPHVKWMK GSEDLTPENE MPIGRNVLQL INIQESANYT CIAASTLGQI DSVSVVKVQS LPTAPTDVQI SEVTATSVRL EWSYKGPEDL QYYVIQYKPK NANQAFSEIS GIITMYYVVR ALSPYTEYEF YVIAVNNIGR GPPSAPATCT TGETKMESAP RNVQVRTLSS STMVITWEPP ETPNGQVTGY KVYYTTNSNQ PEASWNSQMV DNSELTTVSD VTPHAIYTVR VQAYTSMGAG PMSTPVQVKA QQGVPSQPSN FRATDIGETA VTLQWTKPTH SSENIVHYEL YWNDTYANQA HHKRISNSEA YTLDGLYPDT LYYIWLAARS QRGEGATTPP IPVRTKQYVP GAPPRNITAI ATSSTTISLS WLPPPVERSN GRIIYYKVFF VEVGREDDEA TTMTLNMTSI VLDELKRWTE YKIWVLAGTS VGDGPRSHPI ILRTQEDVPG DPQDVKATPL NSTSIHVSWK PPLEKDRNGI IRGYHIHAQE LRDEGKGFLN EPFKFDVVDT LEFNVTGLQP DTKYSIQVAA LTRKGDGDRS AAIVVKTPGG VPVRPTVSLK IMEREPIVSI ELEWERPAQT YGELRGYRLR WGVKDQALKE EMLSGPQMTK KRFDNLERGV EYEFRVAGSN HIGIGQETVK IFQTPEGTPG GPPSNITIRF QTPDVLCVTW DPPTREHRNG IITRYDVQFH KKIDHGLGSE RNMTLRKAVF TNLEENTEYI FRVRAYTKQG AGPFSDKLIV ETERDMGRAP MSLQAEATSE QTAEIWWEPV TSRGKLLGYK IFYTMTAVED LDDWQTKTVG LTESADLVNL EKFAQYAVAI AARFKNGLGR LSEKVTVRIK PEDVPLNLRA HDVSTHSMTL SWSPPIRLTP VNYKISFDAM KVFVDSQGFS QTQIVPKREI ILKHYVKTHT INELSPFTTY NVNVSAIPSD YSYRPPTKIT VTTQMAAPQP MVKPDFYGVV NGEEILVILP QASEEYGPIS HYYLVVVPED KSNLHKIPDQ FLTDDLLPGR NKPERPNAPY IAAKFPQRSI PFTFHLGSGD DYHNFTNRKL EREKRYRIFV RAVVDTPQKH LYTSSPFSEF LSLDMREAPP GERPHRPDPN WPAEPEVSVN RNKDEPEILW VVLPLMVSTF IVSTALIVLC VVKRRRQPCK TPDQAAVTRP LMAADLGAGP TPSDPVDMRR LNFQTPGMIS HPPIPISEFA NHIERLKSND NQKFSQEYES IEPGQQFTWD NSNLEHNKSK NRYANVTAYD HSRVQLPAVE GVVGSDYINA NYCDGYRKHN AYVATQGPLQ ETFVDFWRMC WELKTATIVM MTRLEERTRI KCDQYWPTRG TETYGQIFVT ITETQELATY SIRTFQLCRQ GFNDRREIKQ LQFTAWPDHG VPDHPAPFLQ FLRRCRALTP PESGPVIVHC SAGVGRTGCY IVIDSMLERM KHEKIIDIYG HVTCLRAQRN YMVQTEDQYI FIHDAILEAI ICGVTEVPAR NLHTHLQKLL ITEPGETISG MEVEFKKLSN VKMDSSKFVT ANLPCNKHKN RLVHILPYES SRVYLTPIHG IEGSDYVNAS FIDGYRYRSA YIAAQGPVQD AAEDFWRMLW EHNSTIVVML TKLKEMGREK CFQYWPHERS VRYQYYVVDP IAEYNMPQYK LREFKVTDAR DGSSRTVRQF QFIDWPEQGV PKSGEGFIDF IGQVHKTKEQ FGQDGPITVH CSAGVGRSGV FITLSIVLER MQYEGVLDVF QTVRILRSQR PAMVQTEDQY HFCYRAALEY LGSFDNYTN // ID LA_DROME STANDARD; PRT; 390 AA. AC P40796; Q24375; Q9VIN2; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE La protein homolog (La ribonucleoprotein) (La autoantigen homolog). GN LA OR CG10922. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Ovary; RX MEDLINE=94309632; PubMed=8035794; RA Bai C., Li Z., Tolias P.P.; RT "Developmental characterization of a Drosophila RNA-binding protein RT homologous to the human systemic lupus erythematosus-associated RT La/SS-B autoantigen."; RL Mol. Cell. Biol. 14:5123-5129(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94309661; PubMed=8035818; RA Yoo C.J., Wolin S.L.; RT "La proteins from Drosophila melanogaster and Saccharomyces RT cerevisiae: a yeast homolog of the La autoantigen is dispensable for RT growth."; RL Mol. Cell. Biol. 14:5412-5424(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN TRANSCRIPTION TERMINATION BY RNA CC POLYMERASE III. BINDS RNA AND DNA. BINDS TO PRECURSORS OF RNA CC POLYMERASE III TRANSCRIPTS. MAY PLAY A SPECIALIZED ROLE DURING FLY CC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYONIC, LARVAL, CC PUPAL, AND ADULT DEVELOPMENT. EXPRESSION THROUGHOUT THE EMBRYO IS CC FOLLOWED BY A RESTRICTED PATTERN OF MESODERMAL EXPRESSION THAT IS CC LATER CONFINED TO THE VISCERAL MESODERM, GONADS, GUT, AND SALIVARY CC GLANDS. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -!- SIMILARITY: TO VERTEBRATE PROTEIN LA. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U07652; AAA20518.1; -. DR EMBL; L32988; AAA21776.1; -. DR EMBL; AE003666; AAF53885.1; -. DR PIR; A53773; A53773. DR PIR; A53781; A53781. DR FlyBase; FBgn0011638; La. DR GO; GO:0008098; F:5S rRNA primary transcript binding; IDA. DR GO; GO:0003723; F:RNA binding; NAS. DR InterPro; IPR002344; Lupus_La. DR InterPro; IPR006630; Lupus_La_dom. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF05383; La; 1. DR Pfam; PF00076; rrm; 1. DR PRINTS; PR00302; LUPUSLA. DR SMART; SM00715; LA; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; 1. KW RNA-binding; Nuclear protein; DNA-binding. FT DOMAIN 149 234 RNA-BINDING (RRM). FT CONFLICT 169 169 A -> T (IN REF. 1). FT CONFLICT 182 183 KH -> NS (IN REF. 1). FT CONFLICT 283 283 A -> R (IN REF. 1). FT CONFLICT 329 329 K -> N (IN REF. 1). SQ SEQUENCE 390 AA; 44884 MW; A8099288B90446A5 CRC64; MAEVAETPSV EAQEEVAQPA EAQVLEAKNG DAKKDPAPAA EEAAGGFTKQ ERAIIRQVEY YFGDANLNRD KFLREQIGKN EDGWVPLSVL VTFKRLASLS TDLSEIVAAL NKSEEGLVEI SEDKLSLRRH PERPIPEHNE ERRKEIQERT AYAKGFPLDS QISELLDFAA NYDKVVNLTM RKHYDKPTKS YKFKGSIFLT FETKDQAKAF LEQEKIVYKE RELLRKWQVD YLKEKQEEYA QKNEKRKNKK EAKPEPAFEL PKNAIVVFEG APETSSREEI REAFEKIKDF EVAYIEFAKG ETKGSVRLTE ADAAEKYIAK VEEGKLKFKD EVSLSLRKAT EEEEKEFIDK AIEFMKKRRD FTRNKGKRFN RKRHGGNDHK HGGGKKARGD // ID LBM_DROME STANDARD; PRT; 208 AA. AC Q24188; Q9V4H0; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Late bloomer protein. GN LBM OR LBL OR CG2374. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96175586; PubMed=8596956; RA Kopczynski C.C., Davis G.W., Goodman C.S.; RT "A neural tetraspanin, encoded by late bloomer, that facilitates RT synapse formation."; RL Science 271:1867-1870(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: FACILITATES SYNAPSE FORMATION. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE TETRASPANIN (TM4SF) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U49081; AAA98512.1; -. DR EMBL; AE003842; AAF59302.1; -. DR FlyBase; FBgn0016032; lbm. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0007416; P:synaptogenesis; IMP. DR InterPro; IPR000301; Transmem_4. DR Pfam; PF00335; transmembrane4; 1. KW Transmembrane. FT TRANSMEM 10 30 POTENTIAL. FT TRANSMEM 41 61 POTENTIAL. FT TRANSMEM 67 87 POTENTIAL. FT TRANSMEM 174 194 POTENTIAL. SQ SEQUENCE 208 AA; 23005 MW; 5EC36525287B7AC9 CRC64; MGCATTSVKI ASIVLNAVLG FLAAGAIGWI AYNADTETEE FVIAAYIACS LILVFALLGI FAAIRESVVL TATSAVFLLI LAILQIVSTC LFLHEFDVKS GRDMVEVAWQ ANNMDSLQQK HECCGQSSAQ DYIHLSLLIP PSCYADLQQT PDHLYLDGCI EKVQSFYESD KLRFIIVSWV LVAFELICFA LAVFLAISFK NKQRRMEF // ID LCK_DROME STANDARD; PRT; 160 AA. AC P81829; Q9U4A5; Q9VUF4; DT 30-MAY-2000 (Rel. 39, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Leucokinin precursor (DLK). GN LK OR PP OR CG13480. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE OF 117-160 FROM N.A., SEQUENCE OF 133-147, AND AMIDATION. RC STRAIN=Oregon-R; TISSUE=Neurosecretory cell; RX MEDLINE=20044845; PubMed=10574744; RA Terhzaz S., O'Connell F.C., Pollock V.P., Kean L., Davies S.A., RA Veenstra J.A., Dow J.A.T.; RT "Isolation and characterization of a leucokinin-like peptide of RT Drosophila melanogaster."; RL J. Exp. Biol. 202:3667-3676(1999). RN [4] RP SEQUENCE OF 133-147, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- FUNCTION: ACTS THROUGH INTRACELLULAR CALCIUM IN MALPIGHIAN TUBULE CC STELLATE CELLS TO RAISE CHLORIDE CONDUCTANCE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003534; AAF49731.2; -. DR EMBL; AF192342; AAF20066.1; -. DR FlyBase; FBgn0028418; Leucokinin. DR GO; GO:0008613; F:diuretic hormone activity; NAS. DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS. KW Neuropeptide; Amidation; Cleavage on pair of basic residues; Signal. FT SIGNAL 1 19 POTENTIAL. FT PROPEP 20 130 FT PEPTIDE 133 147 LEUCOKININ. FT PROPEP 151 160 FT MOD_RES 147 147 AMIDATION (G-148 PROVIDE AMIDE GROUP). SQ SEQUENCE 160 AA; 18277 MW; 8E9C41B2086407EA CRC64; MAKIVLCMVL LAFGRQVYGA SLVPAPISEQ DPELATCELQ LSKYRRFILQ AILSFEDVCD AYSSRPGGQD SDSEGWPFRH YAPPPTSQRG EIWAFFRLLM AQFGDKEFSP IIRDAVIERC RIKSQLQRDE KRNSVVLGKK QRFHSWGGKR SPEPPILPDY // ID LCP5_DROME STANDARD; PRT; 104 AA. AC P92192; O96905; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval cuticle protein V precursor. GN (LCP65AB1 OR LCP5 OR DCP3-ALPHA OR CG18776) AND GN (LCP65AB2 OR LCP5 OR DCP3-BETA OR CG18773). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Mandalaparthy P., Jiang S., Schneider G., Chihara C.; RT "The cuticle proteins of Drosophila melanogaster: sequence of Lcp5 in RT the third chromosome cluster."; RL Dros. Info. Service 77:49-51(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1; RX MEDLINE=98043412; PubMed=9383064; RA Charles J.-P., Chihara C., Nejad S., Riddiford L.M.; RT "A cluster of cuticle genes of Drosophila at 65A: sequence, structure RT and evolution."; RL Genetics 147:1213-1224(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 19-32. RC STRAIN=Oregon-R; TISSUE=Larva; RX MEDLINE=98318806; PubMed=9654737; RA Charles J.-P., Chihara C., Nejad S., Riddiford L.M.; RT "Identification of proteins and developmental expression of RNAs RT encoded by the 65A cuticle protein gene cluster in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 28:131-138(1998). CC -!- FUNCTION: COMPONENT OF THE CUTICLE OF THE LARVA. CC -!- SIMILARITY: CONTAINS 1 CUTICLE CONSENSUS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U81550; AAD00301.1; -. DR EMBL; U84746; AAB88065.1; -. DR EMBL; U84747; AAB88066.1; -. DR EMBL; AE003563; AAG22328.1; -. DR EMBL; AE003563; AAG22331.1; -. DR EMBL; AY071366; AAL48988.1; -. DR FlyBase; FBgn0020644; Lcp65Ab1. DR FlyBase; FBgn0020643; Lcp65Ab2. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. DR PROSITE; PS00233; CUTICLE; FALSE_NEG. KW Structural protein; Cuticle; Signal. FT SIGNAL 1 18 FT CHAIN 19 104 LARVAL CUTICLE PROTEIN V. FT CONFLICT 62 72 AAVVHGSFTWV -> CRCRPRILHLG (IN REF. 1). SQ SEQUENCE 104 AA; 11267 MW; BA60DD9483DD6992 CRC64; MKFLIVFVAL FAMAVARPNL AEIVRQVSDV EPEKWSSDVE TSDGTSIKQE GVLKNAGTDN EAAVVHGSFT WVDEKTGEKF TITYVADENG YQPQGAHLPV APVA // ID LDH_DROME STANDARD; PRT; 332 AA. AC Q95028; Q9VRW6; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE L-lactate dehydrogenase (EC 1.1.1.27) (LDH). GN IMPL3 OR IMP-L3 OR CG10160. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=97248084; PubMed=9094207; RA Abu-Shumays R.L., Fristrom J.W.; RT "IMP-L3, A 20-hydroxyecdysone-responsive gene encodes Drosophila RT lactate dehydrogenase: structural characterization and developmental RT studies."; RL Dev. Genet. 20:11-22(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: (S)-LACTATE + NAD(+) = PYRUVATE + NADH. CC -!- PATHWAY: ANAEROBIC GLYCOLYSIS; FINAL STEP. CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE LDH FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U68038; AAB07594.1; -. DR EMBL; AE003563; AAF50666.1; -. DR HSSP; P00336; 5LDH. DR FlyBase; FBgn0001258; ImpL3. DR InterPro; IPR001557; L_LDH. DR InterPro; IPR001236; ldh. DR Pfam; PF00056; ldh; 1. DR Pfam; PF02866; ldh_C; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR PROSITE; PS00064; L_LDH; 1. KW Oxidoreductase; NAD; Glycolysis. FT ACT_SITE 193 193 ACCEPTS A PROTON DURING CATALYSIS FT (BY SIMILARITY). SQ SEQUENCE 332 AA; 35537 MW; E49F1EE2399440F1 CRC64; MAAIKDSLLA QVAEVLPSSG HKVTIVGIGQ VGMASAFSIL AQNVSKEVCL IDVCADKLQG ELMDLQHGSN FLKNPQITAS TDFAASANSR LCIVTAGVRQ KEGESRLSLV QRNTDILKNI IPKLVEYSPD TILLMVSNPV DIMTYVAWKL SGLPKNRVIG SGTNLDSSRF RFLMSQRLGV APTSCHGWII GEHGDSSVPV WSGVNIAGVR LRELNPILGT GEDPEKWNEL HKQVVDSAYE VIKLKGYTSW AIGLSTASLA SAILRNTSSV AAVSTSVLGE HGIDKDVFLS LPCVLNANGV TSVVKQILTP TEVEQLQKSA NIMSDVQAGL KF // ID LDS_DROME STANDARD; PRT; 1061 AA. AC P34739; Q9VHY1; DT 01-FEB-1994 (Rel. 28, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable helicase lodestar. GN LDS OR CG2684. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92009170; PubMed=1916263; RA Girdham C.G., Glover D.M.; RT "Chromosome tangling and breakage at anaphase result from mutations RT in lodestar, a Drosophila gene encoding a putative nucleoside RT triphosphate-binding protein."; RL Genes Dev. 5:1786-1799(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE SNF2/RAD54 HELICASE FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 946. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62629; CAA44496.1; ALT_FRAME. DR EMBL; AE003676; AAF54167.1; -. DR PIR; A40580; A40580. DR FlyBase; FBgn0002542; lds. DR GO; GO:0008094; F:DNA dependent ATPase activity; IDA. DR GO; GO:0006353; P:transcription termination; IDA. DR InterPro; IPR001410; DEAD. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR000330; SNF2_N. DR Pfam; PF00271; helicase_C; 1. DR Pfam; PF00176; SNF2_N; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. KW Nuclear protein; Helicase; ATP-binding. FT NP_BIND 465 472 ATP (POTENTIAL). FT SITE 603 606 DEAH BOX. FT CONFLICT 167 167 R -> G (IN REF. 1). SQ SEQUENCE 1061 AA; 118374 MW; 536BC893B1A90509 CRC64; MSSENSEYYS DKEEDSVVNN SSLGRSRKSS RLSKSSRLSK SSRPSSAGVV IDETQSEEEE SQSSETAESE KSDESDNSQN SQESEDSEDD SVRPSARNTK RKPLGIPSDS EDEEDELEQR ALSPSTRMSI TGVRPQDLSD DDSEIEYSDE VQEGPTEAPT AEAVVPRYTT QFAGNIQNDL HSTIGAADSE VLDDSSGSDV LILSNKETPI EILSSTDDDA TTNKENMSGP PFERPSKSLS PRSSAGASVV KTSKNLSQPT IQAVLKQKTS PAAPRRSRIK SEDQKVVSQV VYDEEMRKLA EKRVQVSDAE KLFEKVAHKL PDKGSQIMKR IDTLRRELAM DEQWISALRV QQSNVPAVRV VKPTLNPPRA PSIDTLDWDE LSEAVNEIKP VYTGAQGMAT FNNQKALTLE SLKDLHVSLE DLPGPEVLAE DPVGLKVSLM NHQKHALAWM SWRERKLPRG GILADDMGLG KTLTMISSVL ACKNGQEMSE GKDESSDSDS EDDKNKKRKS VTGWKSKGRK DTRRGGTLVV CPASLLRQWE SEVESKVSRQ KLTVCVHHGN NRETKGKYLR DYDIVVTTYQ IVAREHKSLS AVFGVKWRRI ILDEAHVVRN HKSQSSLAVC DLRGKYRWAL TGTPIQNKEL DVYALLKFLR CSPFDDLHTW KKWIDNKSAG GQNRLNLLMK SLMLRRTKAQ LQSDGKLNSL PNKELRLIEI SLDKEEMNVY QTVMTYSRTL FAQFLHQRAE RETDFNYRSD ANKPTYNQIK DPNGAYYKMH EKFARMAGSK KEVKSHDILV LLLRLRQICC HPGLIDAMLD GEESQTMGDH SSDSDTPEID LLAQLNKLAI TDTSTDGQQS VANAGDDGPP LLPDEARIAK ASKNLLKRSN PVFNLHRPSS KINMVIQILK TSILKSSDDK AIVVSQWTSV LDILRDHLSK DGVATLSLNG TIPVKNRQDI VNEFNDRNNQ KRVLLLSLTA GGVGLNLIGA NHLLLLDLHW NPQLEAQAQD RIYRVGQKKN VIIYKFMCVD TVEQRIKGLQ DKKLDLADGV LTGAKVSSKL TIDDLKGLFG M // ID LIP1_DROME STANDARD; PRT; 439 AA. AC O46107; Q9VKR6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lipase 1 precursor (EC 3.1.1.-) (DmLip1). GN LIP1 OR CG7279. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Canton-S; RX MEDLINE=98227315; PubMed=9566193; RA Pistillo D., Manzi A., Tino A., Pilo Boyl P., Graziani F., Malva C.; RT "The Drosophila melanogaster lipase homologs: a gene family with RT tissue and developmental specific expression."; RL J. Mol. Biol. 276:877-885(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COULD BE A DIGESTIVE ENZYME. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: IN 14 HOUR EMBRYOS EXPRESSION IS SEEN IN THE CC FOREGUT/MIDGUT BOUNDARY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM 14 HOUR EMBRYOS THROUGH TO CC ADULTHOOD. THERE IS A WEAK MATERNAL CONTRIBUTION TO EARLY EMBRYOS. CC -!- SIMILARITY: BELONGS TO THE AB HYDROLASE SUPERFAMILY. LIPASE CC FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-7 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y14366; CAA74736.1; ALT_INIT. DR EMBL; AE003629; AAF52994.1; -. DR EMBL; AY075506; AAL68315.1; -. DR FlyBase; FBgn0023496; Lip1. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0016298; F:lipase activity; IEP. DR GO; GO:0007586; P:digestion; IEP. DR InterPro; IPR000073; A/b_hydrolase. DR InterPro; IPR006693; abhydro_lipase. DR InterPro; IPR008262; Lipase_AS. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF04083; abhydro_lipase; 1. DR Pfam; PF00561; abhydrolase; 1. DR PROSITE; PS00120; LIPASE_SER; FALSE_NEG. KW Hydrolase; Lipid degradation; Signal; Glycoprotein. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 439 LIPASE 1. FT DOMAIN 30 44 POLY-GLU. FT ACT_SITE 197 197 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 393 393 CHARGE RELAY SYSTEM (BY SIMILARITY). FT CARBOHYD 124 124 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 151 151 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 346 346 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 379 379 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 426 426 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 10 10 L -> I (IN REF. 1). FT CONFLICT 213 213 Y -> F (IN REF. 1). FT CONFLICT 412 412 Q -> E (IN REF. 1). SQ SEQUENCE 439 AA; 50660 MW; 9E32E20BEAE93E3F CRC64; MRCSLRMQLL LLLGLCVFIS RIQGQLIGGE EDEEDEEEEE EEEESVEDET PEDRLQRKNI KQDSTLSVDK LIAKYGYESE VHHVTTEDGY ILTMHRIRKQ GAPPFLLQHG LVDSSAGFVV MGPNVSLAYL LADHNYDVWL GNARGNRYSR NHTTLDPDES KFWDFSWHEI GMYDLPAMID HVLKVTGFPK LHYAGHSQGC TSFFVMCSMR PAYNDKVVSM QALAPAVYAK ETEDHPYIRA ISLYFNSLVG SSIREMFNGE FRFLCRMTEE TERLCIEAVF GIVGRNWNEF NRKMFPVILG HYPAGVAAKQ VKHFIQIIKS GRFAPYSYSS NKNMQLYRDH LPPRYNLSLV TVPTFVYYST NDLLCHPKDV ESMCDDLGNV TGKYLVPQKE FNHMDFLWAI DVRKMLYRRM LQVLGKVPEG SPEEANRSRR EIRGKFIRS // ID LIP3_DROME STANDARD; PRT; 394 AA. AC O46108; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lipase 3 precursor (EC 3.1.1.-) (DmLip3). GN LIP3 OR CG8823. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98227315; PubMed=9566193; RA Pistillo D., Manzi A., Tino A., Pilo Boyl P., Graziani F., Malva C.; RT "The Drosophila melanogaster lipase homologs: a gene family with RT tissue and developmental specific expression."; RL J. Mol. Biol. 276:877-885(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: FAT BODY. CC -!- DEVELOPMENTAL STAGE: ONLY AT LARVAL STAGES. CC -!- SIMILARITY: BELONGS TO THE AB HYDROLASE SUPERFAMILY. LIPASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y14367; CAA74737.1; -. DR EMBL; AE003699; AAF54935.1; -. DR FlyBase; FBgn0023495; Lip3. DR InterPro; IPR000073; A/b_hydrolase. DR InterPro; IPR006693; abhydro_lipase. DR InterPro; IPR008262; Lipase_AS. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF04083; abhydro_lipase; 1. DR Pfam; PF00561; abhydrolase; 1. DR PROSITE; PS00120; LIPASE_SER; 1. KW Hydrolase; Lipid degradation; Signal; Glycoprotein. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 394 LIPASE 3. FT ACT_SITE 164 164 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 369 369 CHARGE RELAY SYSTEM (BY SIMILARITY). FT CARBOHYD 131 131 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 394 AA; 44901 MW; A718D1D743673802 CRC64; MTRGALKVTI LLVGLGLVLA GSRPISDCGE RIEDDGYPME RHEVVTSDNY ILTMHRIPYS PKTGESSNRP VAFLMHGMLS SSSDWVLMGP ERSLAYMLAD AGYDVWMGNA RGNTYSKAHK YWPTYWQIFW NFSWNEIGMY DVPAMIDYVL AKTGQQQVQY VGHSQGTTVY LVMVSERPEY NDKIKSAHLL GPAAYMGNMK SPLTRAFAPI LGQPNAIVEV CGSMEFMPSN KFKQDLGIEM CQATSPYADM CANEIFLIGG YDTEQLDYEL LEHIKATSPA GASVNQNLHF CQEYNSGKFR KFDYTALRNP YEYGSYFPPD YKLKNAKAPV LLYYGANDWM CDVSDVRKLR DELPNMALDY LVPFEKWAHL DFIWGTEARK YVYDEVLKQM QSYE // ID LMA_DROME STANDARD; PRT; 3712 AA. AC Q00174; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Laminin alpha chain precursor. GN LANA OR LAMA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93049203; PubMed=1425586; RA Kusche-Gullberg M., Garrison K., Mackrell A.J., Fessler L.I., RA Fessler J.H.; RT "Laminin A chain: expression during Drosophila development and RT genomic sequence."; RL EMBO J. 11:4519-4527(1992). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=94038678; PubMed=8223265; RA Henchcliffe C., Garcia-Alonso L., Tang J., Goodman C.S.; RT "Genetic analysis of laminin A reveals diverse functions during RT morphogenesis in Drosophila."; RL Development 118:325-337(1993). RN [3] RP SEQUENCE OF 1762-3712 FROM N.A. RX MEDLINE=92078147; PubMed=1744083; RA Garrison K., Mackrell A.J., Fessler J.H.; RT "Drosophila laminin A chain sequence, interspecies comparison, and RT domain structure of a major carboxyl portion."; RL J. Biol. Chem. 266:22899-22904(1991). CC -!- FUNCTION: BINDING TO CELLS VIA A HIGH AFFINITY RECEPTOR, LAMININ CC IS THOUGHT TO MEDIATE THE ATTACHMENT, MIGRATION AND ORGANIZATION CC OF CELLS INTO TISSUES DURING EMBRYONIC DEVELOPMENT BY INTERACTING CC WITH OTHER EXTRACELLULAR MATRIX COMPONENTS. CC -!- FUNCTION: DIVERSE FUNCTIONS DURING MORPHOGENESIS IN DROSOPHILA. CC COMPLETE LOSS-OF-FUNCTION MUTATIONS LEAD TO LATE EMBRYONIC CC LETHALITY. CERTAIN PARTIAL LOSS-OF-FUNCTION MUTATIONS GIVE RAISE CC TO ESCAPER ADULTS, WHICH HAVE ROUGH EYES ASSOCIATED WITH CHANGES CC IN CELL FATE AND PATTERN, MISSHAPPEN LEGS AND DEFECTS IN WING CC STRUCTURE. CC -!- SUBUNIT: LAMININ IS A COMPLEX GLYCOPROTEIN, CONSISTING OF THREE CC DIFFERENT POLYPEPTIDE CHAINS (ALPHA, BETA, GAMMA), WHICH ARE BOUND CC TO EACH OTHER BY DISULFIDE BONDS INTO A CROSS-SHAPED MOLECULE CC COMPRISING ONE LONG AND THREE SHORT ARMS WITH GLOBULES AT EACH CC END. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR; FOUND IN THE BASEMENT CC MEMBRANES (MAJOR COMPONENT). CC -!- TISSUE SPECIFICITY: NEWLY FORMED MESODERM AND LATER PROMINENTLY CC EXPRESSED IN HEMOCYTES, WHICH ALSO SYNTHESIZE COLLAGEN IV. CC -!- DEVELOPMENTAL STAGE: DURING MORPHOGENESIS, MOSTLY IN EMBRYO CC DEVELOPMENT AT 10-12 HOURS. CC -!- DOMAIN: THE ALPHA-HELICAL DOMAINS I AND II ARE THOUGHT TO INTERACT CC WITH OTHER LAMININ CHAINS TO FORM A COILED COIL STRUCTURE. CC -!- DOMAIN: DOMAINS VI, IV AND G ARE GLOBULAR. CC -!- SIMILARITY: CONTAINS 1 LAMININ N-TERMINAL DOMAIN. CC -!- SIMILARITY: CONTAINS 22 LAMININ EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 LAMININ IV DOMAIN. CC -!- SIMILARITY: CONTAINS 5 LAMININ G-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96388; AAA28662.1; -. DR EMBL; L07288; AAC37178.1; -. DR EMBL; M75882; AAA28661.1; -. DR PIR; S28399; S18253. DR HSSP; P02468; 1TLE. DR FlyBase; FBgn0002526; LanA. DR GO; GO:0005605; C:basal lamina; IDA. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR000034; Laminin_B. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR008211; LamNT. DR Pfam; PF00052; laminin_B; 1. DR Pfam; PF00053; laminin_EGF; 18. DR Pfam; PF00054; laminin_G; 5. DR Pfam; PF00055; laminin_Nterm; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00180; EGF_Lam; 19. DR SMART; SM00281; LamB; 1. DR SMART; SM00282; LamG; 5. DR SMART; SM00136; LamNT; 1. DR PROSITE; PS00022; EGF_1; 17. DR PROSITE; PS01186; EGF_2; 5. DR PROSITE; PS01248; LAMININ_TYPE_EGF; 19. DR PROSITE; PS50025; LAM_G_DOMAIN; 5. KW Glycoprotein; Basement membrane; Extracellular matrix; Coiled coil; KW Laminin EGF-like domain; Cell adhesion; Repeat; Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 3712 LAMININ ALPHA CHAIN. FT DOMAIN 25 272 LAMININ N-TERMINAL (DOMAIN VI). FT DOMAIN 273 332 LAMININ EGF-LIKE 1. FT DOMAIN 333 402 LAMININ EGF-LIKE 2. FT DOMAIN 403 447 LAMININ EGF-LIKE 3. FT DOMAIN 448 494 LAMININ EGF-LIKE 4. FT DOMAIN 495 540 LAMININ EGF-LIKE 5. FT DOMAIN 541 586 LAMININ EGF-LIKE 6. FT DOMAIN 587 631 LAMININ EGF-LIKE 7. FT DOMAIN 632 676 LAMININ EGF-LIKE 8. FT DOMAIN 677 731 LAMININ EGF-LIKE 9. FT DOMAIN 732 784 LAMININ EGF-LIKE 10. FT DOMAIN 785 815 LAMININ EGF-LIKE 11 (INCOMPLETE). FT DOMAIN 816 1374 DOMAIN IV''. FT DOMAIN 1375 1420 LAMININ EGF-LIKE 12. FT DOMAIN 1421 1465 LAMININ EGF-LIKE 13. FT DOMAIN 1466 1513 LAMININ EGF-LIKE 14. FT DOMAIN 1514 1564 LAMININ EGF-LIKE 15. FT DOMAIN 1565 1574 LAMININ EGF-LIKE 16 (N-TERMINAL). FT DOMAIN 1575 1775 LAMININ DOMAIN IV. FT DOMAIN 1776 1808 LAMININ EGF-LIKE 16 (C-TERMINAL). FT DOMAIN 1809 1858 LAMININ EGF-LIKE 17. FT DOMAIN 1859 1916 LAMININ EGF-LIKE 18. FT DOMAIN 1917 1969 LAMININ EGF-LIKE 19. FT DOMAIN 1970 2016 LAMININ EGF-LIKE 20. FT DOMAIN 2017 2063 LAMININ EGF-LIKE 21. FT DOMAIN 2064 2111 LAMININ EGF-LIKE 22. FT DOMAIN 2112 2671 DOMAIN II AND I. FT DOMAIN 2672 2868 LAMININ G-LIKE 1. FT DOMAIN 2876 3048 LAMININ G-LIKE 2. FT DOMAIN 3055 3223 LAMININ G-LIKE 3. FT DOMAIN 3349 3528 LAMININ G-LIKE 4. FT DOMAIN 3534 3709 LAMININ G-LIKE 5. FT DOMAIN 2178 2249 COILED COIL (POTENTIAL). FT DOMAIN 2301 2321 COILED COIL (POTENTIAL). FT DOMAIN 2376 2450 COILED COIL (POTENTIAL). FT DOMAIN 2541 2676 COILED COIL (POTENTIAL). FT DOMAIN 3270 3296 POLY-THR. FT DISULFID 273 282 BY SIMILARITY. FT DISULFID 275 296 BY SIMILARITY. FT DISULFID 298 307 BY SIMILARITY. FT DISULFID 310 330 BY SIMILARITY. FT DISULFID 333 342 BY SIMILARITY. FT DISULFID 335 367 BY SIMILARITY. FT DISULFID 370 379 BY SIMILARITY. FT DISULFID 382 400 BY SIMILARITY. FT DISULFID 403 414 BY SIMILARITY. FT DISULFID 405 421 BY SIMILARITY. FT DISULFID 423 432 BY SIMILARITY. FT DISULFID 435 445 BY SIMILARITY. FT DISULFID 448 460 BY SIMILARITY. FT DISULFID 450 468 BY SIMILARITY. FT DISULFID 470 479 BY SIMILARITY. FT DISULFID 482 492 BY SIMILARITY. FT DISULFID 495 507 BY SIMILARITY. FT DISULFID 497 514 BY SIMILARITY. FT DISULFID 516 525 BY SIMILARITY. FT DISULFID 528 538 BY SIMILARITY. FT DISULFID 541 553 BY SIMILARITY. FT DISULFID 543 560 BY SIMILARITY. FT DISULFID 562 571 BY SIMILARITY. FT DISULFID 574 584 BY SIMILARITY. FT DISULFID 587 599 BY SIMILARITY. FT DISULFID 589 605 BY SIMILARITY. FT DISULFID 607 616 BY SIMILARITY. FT DISULFID 619 629 BY SIMILARITY. FT DISULFID 632 644 BY SIMILARITY. FT DISULFID 634 650 BY SIMILARITY. FT DISULFID 652 661 BY SIMILARITY. FT DISULFID 664 674 BY SIMILARITY. FT DISULFID 677 691 BY SIMILARITY. FT DISULFID 679 700 BY SIMILARITY. FT DISULFID 702 711 BY SIMILARITY. FT DISULFID 714 729 BY SIMILARITY. FT DISULFID 732 746 BY SIMILARITY. FT DISULFID 734 753 BY SIMILARITY. FT DISULFID 755 764 BY SIMILARITY. FT DISULFID 767 782 BY SIMILARITY. FT DISULFID 1375 1387 BY SIMILARITY. FT DISULFID 1377 1394 BY SIMILARITY. FT DISULFID 1396 1405 BY SIMILARITY. FT DISULFID 1408 1418 BY SIMILARITY. FT DISULFID 1421 1429 BY SIMILARITY. FT DISULFID 1423 1436 BY SIMILARITY. FT DISULFID 1438 1447 BY SIMILARITY. FT DISULFID 1450 1463 BY SIMILARITY. FT DISULFID 1466 1480 BY SIMILARITY. FT DISULFID 1468 1487 BY SIMILARITY. FT DISULFID 1489 1498 BY SIMILARITY. FT DISULFID 1501 1511 BY SIMILARITY. FT DISULFID 1514 1526 BY SIMILARITY. FT DISULFID 1516 1533 BY SIMILARITY. FT DISULFID 1535 1544 BY SIMILARITY. FT DISULFID 1547 1562 BY SIMILARITY. FT DISULFID 1859 1874 BY SIMILARITY. FT DISULFID 1861 1885 BY SIMILARITY. FT DISULFID 1887 1896 BY SIMILARITY. FT DISULFID 1899 1914 BY SIMILARITY. FT DISULFID 1917 1931 BY SIMILARITY. FT DISULFID 1919 1938 BY SIMILARITY. FT DISULFID 1941 1950 BY SIMILARITY. FT DISULFID 1953 1967 BY SIMILARITY. FT DISULFID 1970 1980 BY SIMILARITY. FT DISULFID 1972 1987 BY SIMILARITY. FT DISULFID 1989 1998 BY SIMILARITY. FT DISULFID 2001 2014 BY SIMILARITY. FT DISULFID 2017 2028 BY SIMILARITY. FT DISULFID 2019 2035 BY SIMILARITY. FT DISULFID 2037 2046 BY SIMILARITY. FT DISULFID 2049 2061 BY SIMILARITY. FT DISULFID 2064 2076 BY SIMILARITY. FT DISULFID 2066 2083 BY SIMILARITY. FT DISULFID 2085 2094 BY SIMILARITY. FT DISULFID 2097 2109 BY SIMILARITY. FT DISULFID 2112 2112 INTERCHAIN (PROBABLE). FT DISULFID 2115 2115 INTERCHAIN (PROBABLE). FT CARBOHYD 116 116 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 219 219 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 395 395 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 453 453 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 508 508 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 588 588 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 722 722 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 897 897 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1352 1352 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1484 1484 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1583 1583 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1617 1617 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1847 1847 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1943 1943 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2024 2024 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2196 2196 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2215 2215 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2267 2267 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2301 2301 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2323 2323 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2482 2482 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2524 2524 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2538 2538 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2569 2569 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2699 2699 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2720 2720 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2890 2890 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2938 2938 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3010 3010 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3070 3070 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3491 3491 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 3612 3612 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 45 45 P -> Q (IN REF. 2). FT CONFLICT 1032 1032 L -> R (IN REF. 2). FT CONFLICT 1407 1407 R -> A (IN REF. 2). FT CONFLICT 1559 1559 P -> Q (IN REF. 2). FT CONFLICT 1598 1598 H -> Q (IN REF. 2). FT CONFLICT 1912 1912 Q -> E (IN REF. 2). SQ SEQUENCE 3712 AA; 411204 MW; 8FDA0E19A86AC527 CRC64; MGHGVASIGA LLVILAISYC QAELTPPYFN LATGRKIYAT ATCGPDTDGP ELYCKLVGAN TEHDHIDYSV IQGQVCDYCD PTVPERNHPP ENAIDGTEAW WQSPPLSRGM KFNEVNLTIN FEQEFHVAYL FIRMGNSPRP GLWTLEKSTD YGKTWTPWQH FSDTPADCET YFGKDTYKPI TRDDDVICTT EYSKIVPLEN GEIPVMLLNE RPSSTNYFNS TVLQEWTRAT NVRIRLLRTK NLLGHLMSVA RQDPTVTRRY FYSIKDISIG GRCMCNGHAD TCDVKDPKSP VRILACRCQH HTCGIQCNEC CPGFEQKKWR QNTNARPFNC EPCNCHGHSN ECKYDEEVNR KGLSLDIHGH YDGGGVCQNC QHNTVGINCN KCKPKYYRPK GKHWNETDVC SPCQCDYFFS TGHCEEETGN CECRAAFQPP SCDSCAYGYY GYPNCRECEC NLNGTNGYHC EAESGQQCPC KINFAGAYCK QCAEGYYGFP ECKACECNKI GSITNDCNVT TGECKCLTNF GGDNCERCKH GYFNYPTCSY CDCDNQGTES EICNKQSGQC ICREGFGGPR CDQCLPGFYN YPDCKPCNCS STGSSAITCD NTGKCNCLNN FAGKQCTLCT AGYYSYPDCL PCHCDSHGSQ GVSCNSDGQC LCQPNFDGRQ CDSCKEGFYN FPSCEDCNCD PAGVIDKFAG CGSVPVGELC KCKERVTGRI CNECKPLYWN LNISNTEGCE ICDCWTDGTI SALDTCTSKS GQCPCKPHTQ GRRCQECRDG TFDLDSASLF GCKDCSCDVG GSWQSVCDKI SGQCKCHPRI TGLACTQPLT THFFPTLHQF QYEYEDGSLP SGTQVRYDYD EAAFPGFSSK GYVVFNAIQN DVRNEVNVFK SSLYRIVLRY VNPNAENVTA TISVTSDNPL EVDQHVKVLL QPTSEPQFVT VAGPLGVKPS AIVLDPGRYV FTTKANKNVM LDYFVLLPAA YYEAGILTRH ISNPCELGNM ELCRHYKYAS VEVFSPAATP FVIGENSKPT NPVETYTDPE HLQIVSHVGD IPVLSGSQNE LHYIVDVPRS GRYIFVIDYI SDRNFPDSYY INLKLKDNPD SETSVLLYPC LYSTICRTSV NEDGMEKSFY INKEDLQPVI ISADIEDGSR FPIISVTAIP VDQWSIDYIN PSPVCVIHDQ QCATPKFRSV PDSKKIEFET DHEDRIATNK PPYASLDERV KLVHLDSQNE ATIVIESKVD ATKPNLFVIL VKYYQPSHPK YQVYYTLTAG KNQYDGKFDI QHCPSSSGCR GVIRPAGEGS FEIDDEFKFT ITTDRSQSVW LDYLVVVPLK QYNDDLLVEE TFDQTKEFIQ NCGHDHFHIT HNASDFCKKS VFSLTADYNS GALPCNCDYA GSTSFECHPF GGQCQCKPNV IERTCGRCRS RYYGFPDCKP CKCPNSAMCE PTTGECMCPP NVIGDLCEKC APNTYGFHQV IGCEECACNP MGIANGNSQC DLFNGTCECR QNIEGRACDV CSNGYFNFPH CEQCSCHKPG TELEVCDKID GACFCKKNVV GRDCDQCVDG TYNLQESNPD GCTTCFCFGK TSRCDSAYLR VYNVSLLKHV SITTPEFHEE SIKFDMWPVP ADEILLNETT LKADFTLREV NDERPAYFGV LDYLLNQNNH ISAYGGDLAY TLHFTSGFDG KYIVAPDVIL FSEHNALVHT SYEQPSRNEP FTNRVNIVES NFQTISGKPV SRADFMMVLR DLKVIFIRAN YWEQTLVTHL SDVYLTLADE DADGTGEYQF LAVERCSCPP GYSGHSCEDC APGYYRDPSG PYGGYCIPCE CNGHSETCDC ATGICSKCQH GTEGDHCERC VSGYYGNATN GTPGDCMICA CPLPFDSNNF ATSCEISESG DQIHCECKPG YTGPRCESCA NGFYGEPESI GQVCKPCECS GNINPEDQGS CDTRTGECLR CLNNTFGAAC NLCAPGFYGD AIKLKNCQSC DCDDLGTQTC DPFVGVCTCH ENVIGDRCDR CKPDHYGFES GVGCRACDCG AASNSTQCDP HTGHCACKSG VTGRQCDRCA VDHWKYEKDG CTPCNCNQGY SRGFGCNPNT GKCQCLPGVI GDRCDACPNR WVLIKDEGCQ ECNNCHHALL DVTDRMRYQI DSVLEDFNSV TLAFFTSQKL NYYDQLADEL EPKVKLLDPN SVDLSPSKKA NSELESDAKS YAKQVNQTLA NAFDIRERSS TTLGNITVAY DEAVKSADQA KEAIASVEAL SKNLEAAAST KIDAALEQAQ HILGQINGTS IELTPNEQVL EKARKLYEEV NTLVLPIKAQ NKSLNALKND IGEFSDHLED LFNWSEASQA KSADVERRNV ANQKAFDNSK FDTVSEQKLQ AEKNIKDAGN FLINGDLTLN QINQKLDNLR DALNELNSFN KNVDEELPVR EDQHKEADAL TDQAEQKAAE LAIKAQDLAA QYTDMTASAE PAIKAATAYS GIVEAVEAAQ KLSQDAISAA GNATDKTDGI EERAHLADTG STDLLQRARQ SLQKVQDDLE PRLNASAGKV QKISAVNNAT EHQLKDINKL IDQLPAESQR DMWKNSNANA SDALEILKNV LEILEPVSVQ TPKELEKAHG INRDLDLTNK DVSQANKQLD DVEGSVSKLN ELAEDIEEQQ HRVGSQSRQL GQEIENLKAQ VEAARQLANS IKVGVNFKPS TILELKTPEK TKLLATRTNL STYFRTTEPS GFLLYLGNDN KTAQKNNDFV AVEIVNGYPI LTIDLGNGPE RITSDKYVAD GRWYQAVVDR MGPNAKLTIR EELPNGDVVE HSKSGYLEGS QNILHVDKNS RLFVGGYPGI SDFNAPPDLT TNSFSGDIED LKIGDESVGL WNFVYGDDND QGARERDVLL EKKKPVTGLR FKGNGYVQLN ATSNLKSRSS IQFSFKADKD TSNGLLFFYG RDKHYMSIEM IDGAIFFNIS LGEGGGVQSG SQDRYNDNQW HKVQAERENR NGLLKVDDIV ISRTNAPLEA DLELPKLRRL YFGGHPRRLN TSISLQPNFD GCIDNVVINQ GVVDLTEYVT GGGVEEGCSA KFSTVVSYAP HEYGFLRMNN VSSDNNLHVV LHFKTTQPNG VLFYAANHDQ SSTIGLSLQD GLLKLNSMGS QLVIDDRILN DGEDHVVTVQ HTQGELRLTV DDVDNKRLGS PQPLILEGGD IFFAGLPDNY RTPRNALASL AYFVGCISDV TVNEEIINFA NSAEKKNGNI NGCPPHVLAY EPSLVPSYYP SGDNEVESPW SNADTLPPLK PDIESTLPPT TPTTTTTTTT TTTSTTTTST TTTTTTPSPI VIDEEKEIEA KTPQKILTTR PPAKLNLPSD ERCKLPEQPN FDVDFTEAGY RFYGLREQRL QINSLPVKVR RHHDIGISFR TERPNGLLIY AGSKQRDDFI AVYLLDGRVT YEIRVGAQLQ AKITTEAELN DGTWHTVEVV RTQRKVSLLI DKLEQPGSVD LNAERSAPVL AVELPIYLGG VNKFLESEVK NLTDFKTEVP YFNGCLKNIK FDAMDLETPP EEFGVVPCSE QVERGLFFNN QKAFVKIFDH FDVGTEMKIS FDFRPRDPNG LLFSVHGKNS YAILELVDNT LYFTVKTDLK NIVSTNYKLP NNESFCDGKT RNVQAIKSKF VINIAVDFIS SNPGVGNEGS VITRTNRPLF LGGHVAFQRA PGIKTKKSFK GCISKVEVNQ RMINITPNMV VGDIWQGYCP LN // ID LMB1_DROME STANDARD; PRT; 1790 AA. AC P11046; Q26328; Q9VLW6; Q9XZT4; DT 01-JUL-1989 (Rel. 11, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Laminin beta-1 chain precursor (Laminin B1 chain). GN LANB1 OR LAMB1 OR CG7123. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94000382; PubMed=8397815; RA Gow C.-H., Chang H.-Y., Lih C.-J., Chang T.-W., Hui C.-F.; RT "Analysis of the Drosophila gene for the laminin B1 chain."; RL DNA Cell Biol. 12:573-587(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88210471; PubMed=3365769; RA Montell D.J., Goodman C.S.; RT "Drosophila substrate adhesion molecule: sequence of laminin B1 chain RT reveals domains of homology with mouse."; RL Cell 53:463-473(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDING TO CELLS VIA A HIGH AFFINITY RECEPTOR, LAMININ CC IS THOUGHT TO MEDIATE THE ATTACHMENT, MIGRATION AND ORGANIZATION CC OF CELLS INTO TISSUES DURING EMBRYONIC DEVELOPMENT BY INTERACTING CC WITH OTHER EXTRACELLULAR MATRIX COMPONENTS. CC -!- SUBUNIT: LAMININ IS A COMPLEX GLYCOPROTEIN, CONSISTING OF THREE CC DIFFERENT POLYPEPTIDE CHAINS (ALPHA, BETA, GAMMA), WHICH ARE BOUND CC TO EACH OTHER BY DISULFIDE BONDS INTO A CROSS-SHAPED MOLECULE CC COMPRISING ONE LONG AND THREE SHORT ARMS WITH GLOBULES AT EACH CC END. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: FOUND IN THE BASEMENT MEMBRANES (MAJOR CC COMPONENT). CC -!- DOMAIN: THE ALPHA-HELICAL DOMAINS I AND II ARE THOUGHT TO INTERACT CC WITH OTHER LAMININ CHAINS TO FORM A COILED COIL STRUCTURE. CC -!- DOMAIN: DOMAINS VI AND IV ARE GLOBULAR. CC -!- SIMILARITY: CONTAINS 1 LAMININ N-TERMINAL DOMAIN. CC -!- SIMILARITY: CONTAINS 13 LAMININ EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 2 LAMININ IV DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95811; AAD19752.1; -. DR EMBL; M19525; AAA28663.1; -. DR EMBL; AE003618; AAF52563.1; -. DR PIR; A28783; MMFFB1. DR HSSP; P02468; 1TLE. DR FlyBase; FBgn0002527; LanB1. DR GO; GO:0005605; C:basal lamina; IDA. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR008211; LamNT. DR Pfam; PF00053; laminin_EGF; 13. DR Pfam; PF00055; laminin_Nterm; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00180; EGF_Lam; 12. DR SMART; SM00136; LamNT; 1. DR PROSITE; PS00022; EGF_1; 10. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS01248; LAMININ_TYPE_EGF; 12. KW Glycoprotein; Basement membrane; Extracellular matrix; Coiled coil; KW Laminin EGF-like domain; Cell adhesion; Repeat; Signal. FT SIGNAL 1 25 FT CHAIN 26 1790 LAMININ BETA-1 CHAIN. FT DOMAIN 43 289 LAMININ N-TERMINAL (DOMAIN VI). FT DOMAIN 290 356 LAMININ EGF-LIKE 1. FT DOMAIN 357 419 LAMININ EGF-LIKE 2. FT DOMAIN 420 479 LAMININ EGF-LIKE 3. FT DOMAIN 480 530 LAMININ EGF-LIKE 4. FT DOMAIN 531 561 LAMININ EGF-LIKE 5 (INCOMPLETE). FT DOMAIN 562 789 LAMININ DOMAIN IV. FT DOMAIN 791 838 LAMININ EGF-LIKE 6. FT DOMAIN 839 884 LAMININ EGF-LIKE 7. FT DOMAIN 885 934 LAMININ EGF-LIKE 8. FT DOMAIN 935 992 LAMININ EGF-LIKE 9. FT DOMAIN 993 1044 LAMININ EGF-LIKE 10. FT DOMAIN 1045 1095 LAMININ EGF-LIKE 11. FT DOMAIN 1096 1143 LAMININ EGF-LIKE 12. FT DOMAIN 1144 1190 LAMININ EGF-LIKE 13. FT DOMAIN 1191 1407 DOMAIN II. FT DOMAIN 1408 1434 DOMAIN ALPHA. FT DOMAIN 1435 1790 DOMAIN I. FT DOMAIN 1257 1407 COILED COIL (POTENTIAL). FT DOMAIN 1455 1507 COILED COIL (POTENTIAL). FT DOMAIN 1542 1563 COILED COIL (POTENTIAL). FT DOMAIN 1610 1764 COILED COIL (POTENTIAL). FT DISULFID 290 299 BY SIMILARITY. FT DISULFID 292 320 BY SIMILARITY. FT DISULFID 322 331 BY SIMILARITY. FT DISULFID 334 354 BY SIMILARITY. FT DISULFID 357 366 BY SIMILARITY. FT DISULFID 359 384 BY SIMILARITY. FT DISULFID 387 396 BY SIMILARITY. FT DISULFID 399 417 BY SIMILARITY. FT DISULFID 420 433 BY SIMILARITY. FT DISULFID 422 448 BY SIMILARITY. FT DISULFID 450 459 BY SIMILARITY. FT DISULFID 462 477 BY SIMILARITY. FT DISULFID 480 493 BY SIMILARITY. FT DISULFID 482 500 BY SIMILARITY. FT DISULFID 502 511 BY SIMILARITY. FT DISULFID 514 528 BY SIMILARITY. FT DISULFID 791 803 BY SIMILARITY. FT DISULFID 793 810 BY SIMILARITY. FT DISULFID 812 821 BY SIMILARITY. FT DISULFID 824 836 BY SIMILARITY. FT DISULFID 839 851 BY SIMILARITY. FT DISULFID 841 858 BY SIMILARITY. FT DISULFID 860 869 BY SIMILARITY. FT DISULFID 872 882 BY SIMILARITY. FT DISULFID 885 894 BY SIMILARITY. FT DISULFID 887 901 BY SIMILARITY. FT DISULFID 904 913 BY SIMILARITY. FT DISULFID 916 932 BY SIMILARITY. FT DISULFID 935 951 BY SIMILARITY. FT DISULFID 937 962 BY SIMILARITY. FT DISULFID 964 973 BY SIMILARITY. FT DISULFID 976 990 BY SIMILARITY. FT DISULFID 993 1007 BY SIMILARITY. FT DISULFID 995 1014 BY SIMILARITY. FT DISULFID 1017 1026 BY SIMILARITY. FT DISULFID 1029 1042 BY SIMILARITY. FT DISULFID 1045 1059 BY SIMILARITY. FT DISULFID 1047 1066 BY SIMILARITY. FT DISULFID 1068 1077 BY SIMILARITY. FT DISULFID 1080 1093 BY SIMILARITY. FT DISULFID 1096 1108 BY SIMILARITY. FT DISULFID 1098 1115 BY SIMILARITY. FT DISULFID 1117 1126 BY SIMILARITY. FT DISULFID 1129 1141 BY SIMILARITY. FT DISULFID 1144 1156 BY SIMILARITY. FT DISULFID 1146 1163 BY SIMILARITY. FT DISULFID 1165 1174 BY SIMILARITY. FT DISULFID 1177 1188 BY SIMILARITY. FT DISULFID 1191 1191 INTERCHAIN (PROBABLE). FT DISULFID 1194 1194 INTERCHAIN (PROBABLE). FT DISULFID 1788 1788 INTERCHAIN (PROBABLE). FT SITE 643 645 CELL ATTACHMENT SITE (POTENTIAL). FT CARBOHYD 140 140 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 203 203 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 234 234 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 489 489 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 593 593 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1053 1053 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1248 1248 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1303 1303 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1332 1332 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1343 1343 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1475 1475 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1495 1495 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1517 1517 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1583 1583 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1646 1646 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1705 1705 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 15 16 MISSING (IN REF. 3). FT CONFLICT 668 668 L -> H (IN REF. 1). FT CONFLICT 726 727 DS -> VT (IN REF. 2). FT CONFLICT 768 769 KS -> NA (IN REF. 1 AND 2). FT CONFLICT 948 949 MISSING (IN REF. 1 AND 2). FT CONFLICT 1358 1375 SDRIAREWKICLIRFRPN -> TDRNCKRVENLSNKIQAE FT (IN REF. 3). SQ SEQUENCE 1790 AA; 198672 MW; 9B04CA31869C9A3B CRC64; MLELRLIVVI VLALALLSWQ WDPVDSQRPP QHGRRDRPKY PPNKFIKTHP CERSSCYPAT GNLLIGRENR LTASSTCGLH SPERFCILSH LQDKKCFLCD TREETKHDPY KNHRIGQIIY KTKPGTNIPT WWQSENGKEN ATIQLDLEAE FHFTHLIITF TTFRPAAMYI ERSFDFGQTW HIYRYFAYDC KESFPGVPTV LENITDVMCT SRYSNVEPSR NGEVIFRVLP PNINVTDPYA EHVQNQLKMT NLRIQMTKLH KLGDNLLDSR LENEEKYYYG ISNMVVRGSC SCYGHASQCL PLDPAFSQAD NEDGMVHGRC ECTHNTKGMN CEECEDFFND LPWKPAFGKK TNACKKCECN DHAVSCHFDE AVFTASGFVS GGVCDNCLHN TRGQHCEECM PYFYRDPEQD ITSERVCQPC DCDPQGSSDD GICDSLNELE EGAVAGACHC KAFVTGRRCN QCKDGYWNLQ SDNPEGCEPC TCNPLGTLNN SGCVMRTGEC KCKKYVTGKD CNQCMPETYG LSESPEGCSL CNCDAGGSYD NYCDVISGQC RCRPHMTGRS CSQPKQNYFI PLLPEVHEAE VVDECISYGA NGNCSLVAET PDGSFTGIGF TRVPENSELV FTVGDIPRSM PYDAVIRYQS TSRGDWENAF ITLVRPDQVD PEGGCGELAA ATSSETRIPF SLPDRSRQVV ALNEVCLEAG KVYKFRIYFE RKRHDVDSPT ATILVDSLTL IPRIDVTPIF QGSVLADIRK KDYEKYNCKS SLYDMNYKSD PKCQNLDNIL SVFVHDGASM CNCNPTGSLS KVCESNGGYC QCKPNVVGRQ CDQCAPGTYG FGPEGCKACD CNSIGSKDKY CDLITGQCQC VPNTYGRECN QCQPGYWNFP ECRVCQCNGH AATCDPIQGT CIDCQDSTTG YSCDSCLDGY YGNPLFGSEI GCRPCRCPET VASGLAHADG CSLDTRNNNM LCHCQEGYSG SRCEICADNF FGNPDNGGTC SKCECSNNVD LYDTGNCDRQ TGACLKCLYQ TTGDHCELCK DGFFGDALQQ NCQQCECDFL GTNNTIAHCD RFTGQCPCLP NVQGVRCDQC AENHWKIASG EGCESCNCDP IGALHEQCNS YTGQCQCKPG FGGRACNQCQ AHYWGNPNEK CQPCECDQFG AADFQCDRET GNCVCHEGIG GYKCNECARG YIGQFPHCSP CGECFNNWDL ILSALEDATT ATILRAKEIK QVGATGAYTS EFSELDKKLQ HIRNLLQNTS VSLVDIEKLD YETQSLRDQL QASHGRLSET EQNLDDIYNS LSLSGVELES LQNHSRLVQQ LSKELKENGI QLQESNIEGA LNLTRHAYER VSNLSTLKDE ANELASNSDR IAREWKICLI RFRPNADDLA NNNKLIEDYR AELTSLTSQI PELNNQVCGK PGDPCDSLCG GAGCGHCGGF LSCEHGAKTH SEEALKVAKD AETAITSKKD QADQTIRALT QAKLNASEAY EKAKRGFEQS ERYLNQTNAN IKLAENLFIA LNNFQENKTA SPSESKELAQ KTLDLDLKLE PEEIETLGDQ INRAVSSLKN VEAIIYRTKP DLDRVNNLQS IANATKEKAD KILDSANSVV ESLAAADESQ GKAKDAIQQA NSNIELAGQD LEKIDEETYS AEAPANNTAQ QVEKLAKKVQ KLQNNIMKND RDAKEITKEA GSVKLEAMRA RGEANNLQSA TSATNQTLTD RASRSENARE RAKQLLQRAS KLTVDTNAKL KDLNDLQTVY LNKNQQLLRL QAEIGPLNKE LNEHLIHIKE RGSHYRQCYT // ID LMG1_DROME STANDARD; PRT; 1639 AA. AC P15215; Q24373; Q9VT18; DT 01-APR-1990 (Rel. 14, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Laminin gamma-1 chain precursor (Laminin B2 chain). GN LANB2 OR LAMC1 OR LAMG1 OR CG3322. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=91299161; PubMed=1840513; RA Chi H.-C., Juminaga D., Wang S.Y., Hui C.-F.; RT "Structure of the Drosophila gene for the laminin B2 chain."; RL DNA Cell Biol. 10:451-466(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=89109164; PubMed=2912972; RA Chi H.-C., Hui C.-F.; RT "Primary structure of the Drosophila laminin B2 chain and comparison RT with human, mouse, and Drosophila laminin B1 and B2 chains."; RL J. Biol. Chem. 264:1543-1550(1989). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=90037237; PubMed=2808533; RA Montell D.J., Goodman C.S.; RT "Drosophila laminin: sequence of B2 subunit and expression of all RT three subunits during embryogenesis."; RL J. Cell Biol. 109:2441-2453(1989). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 344-1639 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=88303364; PubMed=3405777; RA Chi H.-C., Hui C.-F.; RT "cDNA and amino acid sequences of Drosophila laminin B2 chain."; RL Nucleic Acids Res. 16:7205-7205(1988). CC -!- FUNCTION: BINDING TO CELLS VIA A HIGH AFFINITY RECEPTOR, LAMININ CC IS THOUGHT TO MEDIATE THE ATTACHMENT, MIGRATION AND ORGANIZATION CC OF CELLS INTO TISSUES DURING EMBRYONIC DEVELOPMENT BY INTERACTING CC WITH OTHER EXTRACELLULAR MATRIX COMPONENTS. CC -!- SUBUNIT: LAMININ IS A COMPLEX GLYCOPROTEIN, CONSISTING OF THREE CC DIFFERENT POLYPEPTIDE CHAINS (ALPHA, BETA, GAMMA), WHICH ARE BOUND CC TO EACH OTHER BY DISULFIDE BONDS INTO A CROSS-SHAPED MOLECULE CC COMPRISING ONE LONG AND THREE SHORT ARMS WITH GLOBULES AT EACH CC END. CC -!- SUBCELLULAR LOCATION: BASEMENT MEMBRANES (MAJOR COMPONENT). CC -!- DOMAIN: THE ALPHA-HELICAL DOMAINS I AND II ARE THOUGHT TO INTERACT CC WITH OTHER LAMININ CHAINS TO FORM A COILED COIL STRUCTURE. CC -!- DOMAIN: DOMAINS VI AND IV ARE GLOBULAR. CC -!- SIMILARITY: CONTAINS 1 LAMININ N-TERMINAL DOMAIN. CC -!- SIMILARITY: CONTAINS 11 LAMININ EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 LAMININ IV DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M58417; AAA28665.1; -. DR EMBL; M25063; AAA28664.1; -. DR EMBL; AE003551; AAF50238.1; -. DR PIR; A31483; MMFFB2. DR HSSP; P02468; 1TLE. DR FlyBase; FBgn0002528; LanB2. DR GO; GO:0005605; C:basal lamina; IDA. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR000034; Laminin_B. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR008211; LamNT. DR InterPro; IPR008212; Lam_N2. DR Pfam; PF00052; laminin_B; 1. DR Pfam; PF00053; laminin_EGF; 10. DR Pfam; PF00055; laminin_Nterm; 1. DR PRINTS; PR00011; EGFLAMININ. DR ProDom; PD002082; Lam_N2; 1. DR SMART; SM00180; EGF_Lam; 9. DR SMART; SM00281; LamB; 1. DR SMART; SM00136; LamNT; 1. DR PROSITE; PS00022; EGF_1; 8. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS01248; LAMININ_TYPE_EGF; 11. KW Glycoprotein; Basement membrane; Extracellular matrix; Coiled coil; KW Laminin EGF-like domain; Cell adhesion; Repeat; Signal. FT SIGNAL 1 33 POTENTIAL. FT CHAIN 34 1639 LAMININ GAMMA-1 CHAIN. FT DOMAIN 34 298 LAMININ N-TERMINAL (DOMAIN VI). FT DOMAIN 299 358 LAMININ EGF-LIKE 1. FT DOMAIN 359 413 LAMININ EGF-LIKE 2. FT DOMAIN 414 460 LAMININ EGF-LIKE 3. FT DOMAIN 461 513 LAMININ EGF-LIKE 4. FT DOMAIN 514 523 LAMININ EGF-LIKE 5 (N-TERMINAL). FT DOMAIN 524 709 LAMININ DOMAIN IV. FT DOMAIN 710 743 LAMININ EGF-LIKE 5 (C-TERMINAL). FT DOMAIN 744 792 LAMININ EGF-LIKE 6. FT DOMAIN 793 846 LAMININ EGF-LIKE 7. FT DOMAIN 847 901 LAMININ EGF-LIKE 8. FT DOMAIN 902 955 LAMININ EGF-LIKE 9. FT DOMAIN 956 1003 LAMININ EGF-LIKE 10. FT DOMAIN 1004 1049 LAMININ EGF-LIKE 11. FT DOMAIN 1050 1609 DOMAIN II AND I. FT DOMAIN 1087 1109 COILED COIL (POTENTIAL). FT DOMAIN 1144 1247 COILED COIL (POTENTIAL). FT DOMAIN 1306 1627 COILED COIL (POTENTIAL). FT DISULFID 299 308 BY SIMILARITY. FT DISULFID 301 322 BY SIMILARITY. FT DISULFID 324 333 BY SIMILARITY. FT DISULFID 336 356 BY SIMILARITY. FT DISULFID 359 368 BY SIMILARITY. FT DISULFID 361 384 BY SIMILARITY. FT DISULFID 387 396 BY SIMILARITY. FT DISULFID 399 411 BY SIMILARITY. FT DISULFID 414 426 BY SIMILARITY. FT DISULFID 416 432 BY SIMILARITY. FT DISULFID 434 443 BY SIMILARITY. FT DISULFID 446 458 BY SIMILARITY. FT DISULFID 461 475 BY SIMILARITY. FT DISULFID 463 482 BY SIMILARITY. FT DISULFID 484 493 BY SIMILARITY. FT DISULFID 496 511 BY SIMILARITY. FT DISULFID 744 753 BY SIMILARITY. FT DISULFID 746 760 BY SIMILARITY. FT DISULFID 762 771 BY SIMILARITY. FT DISULFID 774 790 BY SIMILARITY. FT DISULFID 793 801 BY SIMILARITY. FT DISULFID 795 811 BY SIMILARITY. FT DISULFID 814 823 BY SIMILARITY. FT DISULFID 826 844 BY SIMILARITY. FT DISULFID 847 861 BY SIMILARITY. FT DISULFID 849 868 BY SIMILARITY. FT DISULFID 871 880 BY SIMILARITY. FT DISULFID 883 899 BY SIMILARITY. FT DISULFID 902 919 BY SIMILARITY. FT DISULFID 904 926 BY SIMILARITY. FT DISULFID 928 937 BY SIMILARITY. FT DISULFID 940 953 BY SIMILARITY. FT DISULFID 956 968 BY SIMILARITY. FT DISULFID 958 975 BY SIMILARITY. FT DISULFID 977 986 BY SIMILARITY. FT DISULFID 989 1001 BY SIMILARITY. FT DISULFID 1004 1016 BY SIMILARITY. FT DISULFID 1006 1022 BY SIMILARITY. FT DISULFID 1024 1033 BY SIMILARITY. FT DISULFID 1036 1047 BY SIMILARITY. FT DISULFID 1050 1050 INTERCHAIN (PROBABLE). FT DISULFID 1053 1053 INTERCHAIN (PROBABLE). FT DISULFID 1631 1631 INTERCHAIN (PROBABLE). FT CARBOHYD 147 147 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 376 376 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 669 669 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 862 862 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 965 965 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1070 1070 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1156 1156 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1394 1394 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1479 1479 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1584 1584 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 831 831 F -> Y. FT VARIANT 892 892 L -> P (IN OREGON-R). FT CONFLICT 1026 1027 DN -> EY (IN REF. 3). SQ SEQUENCE 1639 AA; 182338 MW; 8F510AC6933A52BC CRC64; MKRSRWSHSG SSTARLLLIG VLFASCSTAI LGAQRPPINS AGGHELRGTT FMPALECYDP YGRPQKCLPE FINAAYQLQI ESTNTCGEQN DNHFCIQTMN QNHKNCEFCK YNDHNPSFLT DLHDPQSPTW WQSETMFEGI QHPNYVNLTL HLGKSYDITY VRILFRSPRP ESFTIYKRTS ESGPWIPYQF YSATCRDTYS LPDSRAIRKG EGEAHALCTS EYSDISPLRD GEIAFSTLEG RPSGINFERS GELQEWVTAT DIRITLDRLN TFGDELFGDS QVLKSYFYAI SDIAVGARCK CNGHASKCVP STGMHGERTL VCECRHNTDG PDCDRCLPLY NDLKWKRSTS TEVNECKACN CNGLADKCFF DANLFNRTGH GGHCLDCREN RDGPNCERCK ENFYMRDDGY CVNCACDPVG SRSLQCNSHG KCQCKPGVTG DKCDRCDNNY YQFGPHGCQQ CGCDSGGSHQ NTPACDTETG ICFCKENVEG RRCNECKPGF FNLDKNNRFG CTPCFCYGHT SECMTAPGYS IVSVTSNFNK FKERWTAADL NQREVDIKYN QYSRSIGTTA QGNEHVYFQA PDRFLGDQRA SYNRDLKFKL QLVGQVANTG VSDVILEGAG SRISLPIFAQ GNGIPDQGVK EYTFRLHEHH DYQWQPSQSA RGFLSILSNL TAIKIRATYS VQGEAILDDV ELQTAHRGAA GHPATWIEQC TCPEGYLGQF CESCAPGYRH SPARGGPFMP CIPCDCHGHA DICDSETGRC ICQHNTHGDN CDQCAKGFYG NALGGTPNDC KRCPCPNDGA CLQINEDTVI CTECPKGYFG SRCEQCSDGF FGDPTGLLGE VQTCKSCDCN GNVDPNAVGN CNRTTGECLK CIHNTAGEHC DQCLSGHFGD PLALPHGRCD RCSCYEAGTE QDEQSITRCD QVTGQCQCKP NVIGRDCGEC QPGYFNIRSG NGCENCLCDP VGSYNSTCDR YSGQCHCRPG VMGQRCDQCE NYFYGFSSEG CKPCECDESG SKGFQCDQNG QCPCNDNVEG RRCDRCKENK YDRHRGCIDC PDCYNLVQDA ADLHRAKLFN LSQTLDEIAR TPVTNDDEFE AKLKAVQEKV AVLAQDARDN SGDGGQTYAE VIDDLHKHLD SVREHLVSAD KFQADANGEI DRARQNYTIL DQITENAKKE LQQALDLLND EGAQALARAK EKSVEFGQQS EQISDISREA RALADKLESE AQFDLKNAKD AKDAVEKAHQ LAKSAIDLQL KIGTELRSEV GLELSHVKQS LGTVVQTSKE ALRKANEVYD TALTLLNDVN RQTQPEIDIS QLKKDAVAAN ERADELLKQI TELSNSNGEL FADFETEQEL TEALLKRAEQ QQLEDIELLE RAKAAHDKAT KAVEQGDNTL KEANNTYEKL AGFQSDVQRS SESAEKALQT VPNIEKEIQN AESLISQAEE ALDGANKNAN EAKKNAQEAQ LKYAEQASKD AELIRRKANE TKVAARNLRE EADQLNHRVK LTEMDIFKLE ESSTKDDNLV DDAKRKVGQA KADTQEAQKQ IEKANADLTA IKDELENLKD INTGDLDRLE NRLATVEGEI NRVNLTGRIE KYREQRTIQK NLIDKYDAEL RELKDEVQNI GLISKALPDS CFSRNRLEP // ID LOK_DROME STANDARD; PRT; 476 AA. AC O61267; O61268; P91876; Q8SZS3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ovarian-specific serine/threonine-protein kinase Lok (EC 2.7.1.-) DE (Loki protein) (dMNK). GN LOK OR CG10895. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=98175876; PubMed=9507063; RA Oishi I., Sugiyama S., Otani H., Yamamura H., Nishida Y., Minami Y.; RT "A novel Drosophila nuclear protein serine/threonine kinase expressed RT in the germline during its establishment."; RL Mech. Dev. 71:49-63(1998). RN [2] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Oregon-R; TISSUE=Ovary; RA Larochelle S., Suter B.; RT "Identification of a novel ovarian specific protein kinase."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY HAVE A ROLE IN GERM LINE ESTABLISHMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR; SPECKLED SUBNUCLEAR COMPARTMENT. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=O61267-1; Sequence=Displayed; CC Name=Short; CC IsoId=O61267-2; Sequence=VSP_004865; CC -!- TISSUE SPECIFICITY: IN STAGE 3 EMBRYOS, BOTH ISOFORMS ARE CC EXPRESSED IN BOTH SOMATIC AND POLE CELL NUCLEI. EXPRESSION IN POLE CC CELL NUCLEI IS SUSTAINED UNTIL STAGE 9 AND WEAKLY EXPRESSED AFTER CC POLE CELL INVAGINATION INTO THE ABDOMINAL CAVITY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY IN CC ADULT FEMALES. LEVELS OF THE LONG ISOFORM REMAIN FAIRLY CONSTANT CC FROM OVARIES TO EMBRYOS, THE LEVELS OF SHORT ISOFORM DECREASE CC DRAMATICALLY. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CDS1 CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 FHA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB007821; BAA28755.1; -. DR EMBL; AB007822; BAA28756.1; -. DR EMBL; U87984; AAB49642.1; -. DR EMBL; AE003665; AAF53867.2; -. DR EMBL; AE003665; AAN11062.1; -. DR EMBL; AY070549; AAL48020.1; -. DR HSSP; Q63450; 1A06. DR FlyBase; FBgn0019686; lok. DR GO; GO:0005634; C:nucleus; IEP. DR GO; GO:0004674; F:protein serine/threonine kinase activity; NAS. DR GO; GO:0008630; P:DNA damage response, signal transduction re...; IMP. DR GO; GO:0000077; P:DNA damage response, signal transduction re...; IMP. DR GO; GO:0007281; P:germ-cell development; IEP. DR GO; GO:0006468; P:protein amino acid phosphorylation; NAS. DR InterPro; IPR000253; FHA. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR008984; SMAD_FHA. DR Pfam; PF00498; FHA; 1. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00240; FHA; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Nuclear protein; Alternative splicing. FT DOMAIN 69 129 FHA. FT DOMAIN 174 441 PROTEIN KINASE. FT NP_BIND 180 188 ATP (BY SIMILARITY). FT BINDING 203 203 ATP (BY SIMILARITY). FT ACT_SITE 303 303 BY SIMILARITY. FT VARSPLIC 46 62 Missing (in isoform Short). FT /FTId=VSP_004865. SQ SEQUENCE 476 AA; 54261 MW; 58D583E015C4E626 CRC64; MARDTQGTQG TQSQASNIWT QVESQPMEKI VWGRLYGKNI KIKSLGTSSK YRIIYTHSSF SVDLNNDEFT AGRGEANDLI LTLNDLPEKI LTRISKVHFI IKRANCELTN PVYIQDLSRN GTFVNNEKIG TNRMRILKND DVISLSHPTY KAFVFKDLSP NESIGLPEEI NKTYYVNRKL GSGAYGLVRL VYDTRTCQQF AMKIVKKNML SGARPSTNFS DPDRVLNEAK IMKNLSHPCV VRMHDIVDKP DSVYMVLEFM RGGDLLNRII SNKLLSEDIS KLYFYQMCHA VKYLHDRGIT HRDLKPDNVL LETNDEETLL KVSDFGLSKF VQKDSVMRTL CGTPLYVAPE VLITGGREAY TKKVDIWSLG VVLFTCLSGT LPFSDEYGTP AAQQIKKGRF AYGHPSWKSV SQRAKLLINQ MLIVDPERRP SIDDVLQSSW LRDAPMLQKA KRLMKLDGME IEEENFLEPP TKRSRR // ID LOLL_DROME STANDARD; PRT; 894 AA. AC P42283; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lola protein, long isoform (Longitudinals lacking protein). GN LOLA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94326639; PubMed=8050351; RA Giniger E., Tietje K., Jan L.Y., Jan Y.N.; RT "Lola encodes a putative transcription factor required for axon RT growth and guidance in Drosophila."; RL Development 120:1385-1398(1994). CC -!- FUNCTION: PUTATIVE TRANSCRIPTION FACTOR REQUIRED FOR AXON GROWTH CC AND GUIDANCE IN THE CENTRAL AND PERIPHERAL NERVOUS SYSTEMS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P42283-1; Sequence=Displayed; CC Name=Short; CC IsoId=P42284-1; Sequence=External; CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U07607; AAA19593.1; -. DR FlyBase; FBgn0005630; lola. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007411; P:axon guidance; IMP. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. KW Transcription regulation; Zinc-finger; Metal-binding; DNA-binding; KW Nuclear protein; Alternative splicing. FT DOMAIN 32 97 BTB. FT ZN_FING 794 817 C2H2-TYPE (ATYPICAL). FT ZN_FING 824 846 C2H2-TYPE. SQ SEQUENCE 894 AA; 96539 MW; 978D09062E1AE833 CRC64; MDDDQQFCLR WNNHQSTLIS VFDTLLENET LVDCTLAAEG KFLKAHKVVL SACSPYFATL LQEQYDKHPI FILKDVKYQE LRAMMDYMYR GEVNISQDQL AALLKAAESL QIKGLSDNRT GGGVAPKPES SGHHRGGKLS GAYTLEQTKR ARLATGGAMD TSGDVSGSRE GSSSPSRRRR KVRRRSMEND AHDNSNSSVL QAAASNQSIL QQTGAGLAVS ALVTTQLSSG PAAGTSSQAS STQQQQPLTS TNVTKKTESA KLTSSTAAPA SGASASAAVQ QAHLHQQQAQ TTSDAINTEN VQAQSQGGAQ GVQGDDEDID EGSAVGGPNS ATGPNPASAS ASAVHAGVVV KQLASVVDKS SSNHKHKIKD NSVSSVGSEM VIEPKAEYDD DAHDENVEDL TLDEEDMTME ELDQTAGTSQ GGEGSSQTYA TWQHDRSQDE LGLMAQDAQQ RDPQDLSRKE NTAPDVASTA EIQRSFQRSI LNGKQRDEQK IQLPGSRRKR LSVTEVSDML FEFYKTKSAK VPKAEQPHRQ VSPTSGEILD PSTISAIAVY GTASETASKN LNADEVMRVQ NATATRVVGA AAGAAASFHP RPKYTLKTAA SSTEQLGVVK AIPTSVLVAN SAAALTPKPQ AAVIAEALMR NGLHNFQQQL RAQEILRQQT PHRRIKEEND VEIAGGDITP TKILENLLRK QQERDLRHSE CENEPGYSTE DDEEGRYHAF DDIHLMEQSG GKFGNNSGMG MFNANAHGGS ASSILDAHQA FRNLEFTLSD YGGSSSNGST TSPNGIGLDG EPVYECRHCG KKYRWKSTLR RHENVECGGK EPSHQCPYCP YKSKQRGNLG VHVRKHHTDL PQLPSKRRSK YSMNRENGMS GSMSDDSQGK LIIDFNGKGE LETK // ID LOLS_DROME STANDARD; PRT; 467 AA. AC P42284; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lola protein, short isoform (Longitudinals lacking protein). GN LOLA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94326639; PubMed=8050351; RA Giniger E., Tietje K., Jan L.Y., Jan Y.N.; RT "Lola encodes a putative transcription factor required for axon RT growth and guidance in Drosophila."; RL Development 120:1385-1398(1994). CC -!- FUNCTION: PUTATIVE TRANSCRIPTION FACTOR REQUIRED FOR AXON GROWTH CC AND GUIDANCE IN THE CENTRAL AND PERIPHERAL NERVOUS SYSTEMS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Short; CC IsoId=P42284-1; Sequence=Displayed; CC Name=Long; CC IsoId=P42283-1; Sequence=External; CC -!- TISSUE SPECIFICITY: MOSTLY NEURONAL. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U07606; AAA19592.1; -. DR FlyBase; FBgn0005630; lola. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007411; P:axon guidance; IMP. DR InterPro; IPR000210; BTB_POZ. DR Pfam; PF00651; BTB; 1. DR SMART; SM00225; BTB; 1. DR PROSITE; PS50097; BTB; 1. KW Transcription regulation; Nuclear protein; Alternative splicing. FT DOMAIN 32 97 BTB. SQ SEQUENCE 467 AA; 49612 MW; 24C657D2FA1169C4 CRC64; MDDDQQFCLR WNNHQSTLIS VFDTLLENET LVDCTLAAEG KFLKAHKVVL SACSPYFATL LQEQYDKHPI FILKDVKYQE LRAMMDYMYR GEVNISQDQL AALLKAAESL QIKGLSDNRT GGGVAPKPES SGHHRGGKLS GAYTLEQTKR ARLATGGAMD TSGDVSGSRE GSSSPSRRRR KVRRRSMEND AHDNSNSSVL QAAASNQSIL QQTGAGLAVS ALVTTQLSSG PAAGTSSQAS STQQQQPLTS TNVTKKTESA KLTSSTAAPA SGASASAAVQ QAHLHQQQAQ TTSDAINTEN VQAQSQGGAQ GVQGDDEDID EGSAVGGPNS ATGPNPASAS ASAVHAGVVV KQLASVVDKS SSNHKHKIKD NSVSSVGSEM VIEPKAEYDD DAHDENVEDL TLDEEDMTME ELDQTAGTSQ GGEGSSQTYA TWQHDRSQDE LGLMAQDAQQ RDPQGECLLP LKSIYEL // ID LP1A_DROME STANDARD; PRT; 789 AA. AC P11995; Q9VYM4; DT 01-OCT-1989 (Rel. 12, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval serum protein 1 alpha chain precursor (Hexamerin 1 alpha). GN LSP1-ALPHA OR LSP1-A OR CG2559. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-84 FROM N.A. RX MEDLINE=87060914; PubMed=3097321; RA Delaney S.J., Smith D.F., McClelland A., Sunkel C., Glover D.M.; RT "Sequence conservation around the 5' ends of the larval serum protein RT 1 genes of Drosophila melanogaster."; RL J. Mol. Biol. 189:1-11(1986). RN [3] RP SEQUENCE OF 1-52 FROM N.A. RA Jowett T.; RT "The regulatory domain of a larval serum protein gene in Drosophila RT melanogaster."; RL EMBO J. 4:3789-3795(1985). CC -!- FUNCTION: LARVAL STORAGE PROTEIN (LSP) WHICH MAY SERVE AS A STORE CC OF AMINO ACIDS FOR SYNTHESIS OF ADULT PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: HETEROHEXAMER, COMPOSED OF THREE SUBUNITS, ALPHA, BETA CC AND GAMMA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: LARVAL HEMOLYMPH. CC -!- SIMILARITY: TO ARYLPHORINS AND TO ARTHROPOD HEMOCYANINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003489; AAF48168.1; -. DR EMBL; X03872; CAA27506.1; -. DR EMBL; X03368; CAA27066.1; -. DR PIR; A27144; A27144. DR HSSP; P04253; 1LLA. DR FlyBase; FBgn0002562; Lsp1-alpha. DR GO; GO:0005616; C:larval serum protein complex; IDA. DR InterPro; IPR008922; Di-copper_centre. DR InterPro; IPR000896; Hemocyanin. DR InterPro; IPR005203; hemocyanin_C. DR InterPro; IPR005204; hemocyanin_N. DR InterPro; IPR007110; Ig-like. DR Pfam; PF00372; hemocyanin; 1. DR Pfam; PF03723; hemocyanin_C; 1. DR Pfam; PF03722; hemocyanin_N; 1. DR PRINTS; PR00187; HAEMOCYANIN. DR PROSITE; PS00209; HEMOCYANIN_1; FALSE_NEG. DR PROSITE; PS00210; HEMOCYANIN_2; 1. KW Signal; Hemolymph; Storage protein; Glycoprotein; Multigene family. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 789 LARVAL SERUM PROTEIN 1 ALPHA CHAIN. SQ SEQUENCE 789 AA; 95883 MW; 47F3F21B05D53795 CRC64; MKFAIAFLAC VAVVTATAYH KTHDIKVADK AFLMKQKFLF EIVYRVEDPL MFEEYIAMGK QFYFDKEHYT HFDLYMEKFF EAHKAHALLP KGEFFGALVK HHAKQARGLF NFFYYAKDWE TFMTNVAFAR MHFNEGMFVY ALTLAVIHRD DFHGLVLPAI HEIFPQFFFN SKFVMEAEKF DYEMWMKTSL YEKEYMDVYH KTYEHEFGSM YQTSDYMYMK DFKTWQWWKL MGLGEHWYSE SNYILRENIY EYNQESNWLT MMKDVKKFYM PVDYSRDLYL YNEESKLSYF TEDLGWNSYW YYLNMDYSFF LDGKTFGLQN DRRGEWWLYN VHQLLSRYHM ERLSHGLGEI PQFSWFHQIE MGYDPQLIYY NGIGYSYRKN YYELETYGNF EMLDKITGFQ QRIQNIVELG YYQTTDGHMI DLRKPESIEI IGNMLQGNVD AIDNIFFQFW YMLAHMYFAD THYYQMEVYP NVMLNFETMM RDPMFYMFYK SIAQVYFQFM HHLPKYTKEQ LLMPGVTLKH VEVSELVTYF DLVDFDVTNM LNGKMVFHEG QFLWDKSLFA RQMRLNHKPF SYTYTIDSAR DEKVVIRAFL GPKFDEYGRM ISLTDNRMNF MEIDEFTYTL KTGSNLITRK STDFAWTVKD RTTYTELYYY TMMAFDGKYD YPLDLTEPHC GFPDRLVLPM GWKKGMPMQM FFMVVPYMAP QHEQFSTFDY TYSCGIGSGA RHVDSLPFGY PFDREINEYE FHVPNMYFKD VTIYHADTME KYYNYKEYTN YGHFDYSFFN DYYTKYFKL // ID LP1B_DROME STANDARD; PRT; 789 AA. AC P11996; Q9VPV2; DT 01-OCT-1989 (Rel. 12, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Larval serum protein 1 beta chain precursor (Hexamerin 1 beta). GN LSP1-BETA OR LSP1-B OR CG4178. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97274657; PubMed=9128742; RA Massey H.C. Jr., Kejzlarova-Lepesant J., Willis R.L., RA Castleberry A.B., Benes H.; RT "The Drosophila Lsp-1 beta gene. A structural and phylogenetic RT analysis."; RL Eur. J. Biochem. 245:199-207(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 1-100 FROM N.A. RX MEDLINE=87060914; PubMed=3097321; RA Delaney S.J., Smith D.F., McClelland A., Sunkel C., Glover D.M.; RT "Sequence conservation around the 5' ends of the larval serum protein RT 1 genes of Drosophila melanogaster."; RL J. Mol. Biol. 189:1-11(1986). CC -!- FUNCTION: LARVAL STORAGE PROTEIN (LSP) WHICH MAY SERVE AS A STORE CC OF AMINO ACIDS FOR SYNTHESIS OF ADULT PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: HETEROHEXAMER, COMPOSED OF THREE SUBUNITS, ALPHA, BETA CC AND GAMMA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: LARVAL HEMOLYMPH. CC -!- SIMILARITY: TO ARYLPHORINS AND TO ARTHROPOD HEMOCYANINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U63556; AAB58821.1; -. DR EMBL; AE003588; AAF51434.1; -. DR EMBL; AY069163; AAL39308.1; -. DR EMBL; X03873; CAA27507.1; -. DR PIR; B27144; B27144. DR HSSP; P04253; 1OXY. DR FlyBase; FBgn0002563; Lsp1-beta. DR GO; GO:0005616; C:larval serum protein complex; IDA. DR InterPro; IPR008922; Di-copper_centre. DR InterPro; IPR000896; Hemocyanin. DR InterPro; IPR005203; hemocyanin_C. DR InterPro; IPR005204; hemocyanin_N. DR InterPro; IPR007110; Ig-like. DR Pfam; PF00372; hemocyanin; 1. DR Pfam; PF03723; hemocyanin_C; 1. DR Pfam; PF03722; hemocyanin_N; 1. DR PRINTS; PR00187; HAEMOCYANIN. DR PROSITE; PS00209; HEMOCYANIN_1; FALSE_NEG. DR PROSITE; PS00210; HEMOCYANIN_2; 1. KW Signal; Hemolymph; Storage protein; Glycoprotein; Multigene family. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 789 LARVAL SERUM PROTEIN 1 BETA CHAIN. FT CONFLICT 275 275 T -> N (IN REF. 1). FT CONFLICT 725 725 S -> R (IN REF. 1). SQ SEQUENCE 789 AA; 95913 MW; AE12594515806A5B CRC64; MKIAIALLAC LGLAAAASFH QTHEVKIADK AFLMKQKFLF EIVYRVEDPL MFEDHIKQGE KFYFEESYYT HYDMYMKKFF EAYKAHALLP KGEFFGALVM SHAKQARGLF NFFYYAKDWE TFAANVAWAR MHVNEGMFVY ALTMAVIHRN DFHGLMLPSI YEIFPQFFFN SKFVFEAEKF DYEMWMKMTM YEKEYMDVYY KTNGYDYSTM YRSSDYTYMK DFKTWQWWKL MGLGEHWYTE DKFILRENIY EFNQETKWLS MMKDVKKFYM PVDYTRDLNL YNKESKLSYF TEDLGWNAYW YYLNMDYSFF LDGNTFDLKN DRRGEWWLYN VHQLLSRYYM ERLSHGFGEI PEFSWYQQIE MGYDPQLIYY NGIGYSFRKN YYEMETYANY DMLDKITGFL KRIHNIVEMG YYKTADGHTI DLRKPEAIEF IGNMLQGNVD AMDKMFYQFW YMLAHMYFAD ADYYQMDVYP NVMLNFETMM RDPMYYMFYK SIAQVYFQFM HYLPKYTKEQ LLMPGVTMKN VEVSDLTTYF DLVDFDVTNM LNDKMIFQDG KFVWDMSLFA RQMRLNHKPF TYTYTIESEK VEKVVIRAFL GPKFDEFGKV ISLAENRMNF MEIDEFYYEL KAGTNKITRK SSEFYWTVKD RTTYTELYYY TMMAFDGKYD FPLDISEPHC GFPDRLVLPM GWQKGMPMQM FFMVVPYVAP AHEQFSTFDY TYSCGIGSGA RYVDSLPFGY PFDRAIDEYE FFVPNMYFKD VSIYHADTME PYYKYKSYSN YGHFDYTFFN DYYTKYFKF // ID LP1G_DROME STANDARD; PRT; 772 AA. AC P11997; O16162; Q9W0V6; DT 01-OCT-1989 (Rel. 12, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Larval serum protein 1 gamma chain precursor (Hexamerin 1 gamma). GN LSP1-GAMMA OR LSP1-G OR CG6821. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-711 FROM N.A. RX MEDLINE=98066355; PubMed=9402735; RA Bauer V.L., Aquadro C.F.; RT "Rates of DNA sequence evolution are not sex-biased in Drosophila RT melanogaster and D. simulans."; RL Mol. Biol. Evol. 14:1252-1257(1997). RN [3] RP SEQUENCE OF 1-105 FROM N.A. RX MEDLINE=87060914; PubMed=3097321; RA Delaney S.J., Smith D.F., McClelland A., Sunkel C., Glover D.M.; RT "Sequence conservation around the 5' ends of the larval serum protein RT 1 genes of Drosophila melanogaster."; RL J. Mol. Biol. 189:1-11(1986). CC -!- FUNCTION: LARVAL STORAGE PROTEIN (LSP) WHICH MAY SERVE AS A STORE CC OF AMINO ACIDS FOR SYNTHESIS OF ADULT PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: HETEROHEXAMER, COMPOSED OF THREE SUBUNITS, ALPHA, BETA CC AND GAMMA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: LARVAL HEMOLYMPH. CC -!- SIMILARITY: TO ARYLPHORINS AND TO ARTHROPOD HEMOCYANINS. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 101. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003467; AAF47324.1; -. DR EMBL; AF016033; AAB71666.1; -. DR EMBL; X03874; CAA27508.1; ALT_FRAME. DR PIR; C27144; C27144. DR HSSP; P04253; 1OXY. DR FlyBase; FBgn0002564; Lsp1-gamma. DR GO; GO:0005616; C:larval serum protein complex; IDA. DR InterPro; IPR008922; Di-copper_centre. DR InterPro; IPR000896; Hemocyanin. DR InterPro; IPR005203; hemocyanin_C. DR InterPro; IPR005204; hemocyanin_N. DR InterPro; IPR007110; Ig-like. DR Pfam; PF00372; hemocyanin; 1. DR Pfam; PF03723; hemocyanin_C; 1. DR Pfam; PF03722; hemocyanin_N; 1. DR PRINTS; PR00187; HAEMOCYANIN. DR PROSITE; PS00209; HEMOCYANIN_1; FALSE_NEG. DR PROSITE; PS00210; HEMOCYANIN_2; 1. KW Signal; Hemolymph; Storage protein; Glycoprotein; Multigene family. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 772 LARVAL SERUM PROTEIN 1 GAMMA CHAIN. FT CONFLICT 326 328 QQI -> SRS (IN REF. 2). FT CONFLICT 624 624 S -> T (IN REF. 2). SQ SEQUENCE 772 AA; 93408 MW; FC2BC0A7336F636D CRC64; MKLTLVILAL VACVTAFSVP TQKVKIADKN FLEKQKFLFE IVHRIDEPLM FEEWIKMGQK LITDKAQYET FDFYMEKLWE SYKLGALLPK GEFFGALVKT HHKQAYGLFN FFYYAKDWET FVRNVAWARI HVNEGMFVYA LTLAVIHKPE FEGLILPQIY EIFPQYFFNS KFVYAAEKFD YEVFSKLTMY EKEYKDILYK DYSEFTGNFY FYTKDWKTWQ WYKMMGLDQE WYVEDKYFLR ENLSQFVNDP KYVDVVKGLK KFYMPVDYTR DIDFFNDETK MTYFTEDLGW NAYWYYLNMD YAFFLNGKQF GLDKDRRGEY WIYNVQQILA RYYQERLANG FGEIPEFFWY KQIEYGYDPQ LIYYNGIGYS YRKNYYDFYT YGKFEMYSQI QNFFSRVYKV LETGFYKTAD GQVFDLHKPE AIKIVGNYLQ GNADTFDKYF FNYYYLLAHM YFADVDYNDM EVFPNVFLNF ETMLRDPFFY TFYKKFTDVF YTFKYYLKPY TQKDLFYEGI TIKDVSVSKL VTYYDIVDFD VTNLLNDKMT FVDGQYIWDK ALLARQARLN HKPFNFEFTI DSDKVQKGVV RVFLGPKFDE YGRVIPLDYN RKNFVQIDSF VYPFIAGTNT IKRSSKEFSW TAEDRITYTE LYKYVMLASE GKYDFPLDIS EPHNAFPDRL VLPKGWEQGM PMQFYFFVSP FAETYEQFSN FDYTYSSGVG SGTRFVDTKP FGYPFDRQID ESDFFVPNGF FKDVKVYYVD TFAKYFEKKY TQFGTFDYSI EY // ID LSP2_DROME STANDARD; PRT; 718 AA. AC Q24388; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Larval serum protein 2 precursor (LSP-2) (Hexamerin 2). GN LSP2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97274656; PubMed=9128741; RA Mousseron-Grall S., Kejzlarova-Lepesant J., Burmester T., Chihara C., RA Barray M., Delain E., Pictet R., Lepesant J.-A.; RT "Sequence, structure and evolution of the ecdysone-inducible Lsp-2 RT gene of Drosophila melanogaster."; RL Eur. J. Biochem. 245:191-198(1997). CC -!- FUNCTION: LARVAL STORAGE PROTEIN (LSP) WHICH MAY SERVE AS A STORE CC OF AMINO ACIDS FOR SYNTHESIS OF ADULT PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: HOMOHEXAMER. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: TO ARYLPHORINS AND TO ARTHROPOD HEMOCYANINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X97770; CAA66371.1; -. DR HSSP; P04254; 1HC2. DR FlyBase; FBgn0002565; Lsp2. DR GO; GO:0005616; C:larval serum protein complex; IDA. DR InterPro; IPR008922; Di-copper_centre. DR InterPro; IPR000896; Hemocyanin. DR InterPro; IPR005203; hemocyanin_C. DR InterPro; IPR005204; hemocyanin_N. DR InterPro; IPR007110; Ig-like. DR Pfam; PF00372; hemocyanin; 1. DR Pfam; PF03723; hemocyanin_C; 1. DR Pfam; PF03722; hemocyanin_N; 1. DR PRINTS; PR00187; HAEMOCYANIN. DR PROSITE; PS00209; HEMOCYANIN_1; FALSE_NEG. DR PROSITE; PS00210; HEMOCYANIN_2; 1. KW Signal; Storage protein; Glycoprotein; Multigene family. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 718 LARVAL SERUM PROTEIN 2. FT CARBOHYD 204 204 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 699 699 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 718 AA; 85479 MW; 6366B7FD54CD475E CRC64; MKSFTVIALA AVALLATLGQ AKHLDSKVAD KDFLMKQKFM YQILQHIYQD DVFTTPFGGS YVEYKPWEHV ADYVHPEMLE HFFELWQHQP FTDDMVWSVM YDKHEEYVVG LVRLFYFAKN WETFQHVVYW ARQHVNKQLF VYAVTIASLF RDDMQGVVLP AHYEIHPWSY FDSQALEWAE HYKMHGFHHV KQMDNIYNVV IRTNYSNVHG SLNYDHDLAY YLEDVGFNAF YYYFNLDYPF WTKGGEEHVL NKDRRGELYL YVHWQLLARW HLERLSHDLG EVPAFNMYVP TESGYASNLR TYYGVPQWHR ENHHSFYHEH NYEHIEHVEM YTQRLMDWIH KNEKFDVETI NVLGNIIQGN ADSVDKKFYG SLDKLYRFIV NEGHHYGHGD ESFPGLFMHY DTSMRDPIFY EVYKTIVSHY WHLMETYPEY HKKDYAFEGV HIDAVHMPES LTTYFEHFDS DISNAVNVEP AVEGSADPLY TFGRNSHYKG SSYVIKARQQ RLNHKPFEFT LDVTSDKAQD AVVKVFIGPK YDEHGHEIPL EHNYQNFFEL EHFKVHLEAG VNHIKRASGD FSFWVNDRTT YLELYQKLMD ATNSDYKFKL DQSEAHCGVP NRMMLPRGKK GGQVFQFFYM VYPYHQPEVA QFTGYDPVVS CGVGHGSRYV DALPFGFPFN RPVKHDYYFD VHNFKFVDVK IFHRDEHTNW SRSWTQRIRT PKRTNDIG // ID LVA_DROME STANDARD; PRT; 2779 AA. AC Q8MSS1; Q9W4N7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lava lamp protein. GN LVA OR CG6450. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 980-2779 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX MEDLINE=20530668; PubMed=11076973; RA Sisson J.C., Field C., Ventura R., Royou A., Sullivan W.; RT "Lava lamp, a novel peripheral golgi protein, is required for RT Drosophila melanogaster cellularization."; RL J. Cell Biol. 151:905-918(2000). CC -!- FUNCTION: LVA AND SPECTRIN MAY FORM A GOLGI-BASED SCAFFOLD THAT CC MEDIATES INTERACTION OF GOLGI BODIES WITH MICROTUBUBLES AND CC FACILITATES GOLGI-DERIVED MEMBRANE SECRETION REQUIRED FOR THE CC FORMATION OF FURROWS DURING CELLULARIZATION. CC -!- SUBUNIT: INTERACTS WITH CLIP-190 AND SPECTRIN SEPARATELY. CC -!- SUBCELLULAR LOCATION: LVA-ALPHA-SPECTRIN AND LVA-CLIP-190 CC COMPLEXES ARE FOUND AT THE GOLGI. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003429; AAF45910.1; -. DR EMBL; AY118638; AAM50007.1; ALT_INIT. DR FlyBase; FBgn0029688; lva. KW Developmental protein; Golgi stack; Coiled coil. FT DOMAIN 52 85 COILED COIL (POTENTIAL). FT DOMAIN 141 175 COILED COIL (POTENTIAL). FT DOMAIN 220 607 COILED COIL (POTENTIAL). FT DOMAIN 659 716 COILED COIL (POTENTIAL). FT DOMAIN 751 1733 COILED COIL (POTENTIAL). FT DOMAIN 1785 1863 COILED COIL (POTENTIAL). FT DOMAIN 1941 2433 COILED COIL (POTENTIAL). FT DOMAIN 2504 2544 COILED COIL (POTENTIAL). FT DOMAIN 2600 2641 COILED COIL (POTENTIAL). FT CONFLICT 1211 1211 E -> K (IN REF. 2). FT CONFLICT 1424 1424 A -> S (IN REF. 2). FT CONFLICT 1506 1506 E -> D (IN REF. 2). FT CONFLICT 2034 2034 A -> V (IN REF. 2). FT CONFLICT 2069 2069 Q -> H (IN REF. 2). FT CONFLICT 2133 2133 G -> E (IN REF. 2). FT CONFLICT 2154 2154 Q -> E (IN REF. 2). FT CONFLICT 2160 2160 E -> V (IN REF. 2). FT CONFLICT 2200 2200 L -> P (IN REF. 2). FT CONFLICT 2217 2217 A -> T (IN REF. 2). FT CONFLICT 2271 2271 E -> D (IN REF. 2). SQ SEQUENCE 2779 AA; 315897 MW; 1CB3965102018AEE CRC64; MAEDSGALES SYDFSIVQPD DHEYGEADIR LAGSSNDLSS LQNVSASTTR GTKGKGRLDS LKENLYKQQE RLTALKERAL RKSQDERHKS SMSDSMESLK TLGQKLTVLK TRSGDSSTPL VSPTKDSDPG DVSLLQTSGS EKLLMLTQRT EQNRALLEQR KRDLAKSLLS VKSNIGHQTT AELGSSMTDL RHAASVSNPP VSRHRSALDL EAQGQEAVDE SRVKLLRSRM KLTELKQGRQ EQELNELRTE LAKRAKLIER LELSGAELQR TLTQRNEELE QLRVVQAEED SLKVQENSRL QGEVLVLRER LAELENVNDL LETTRCELQE ELTTARERQR NLELEQEQEK ASRSPQSEAA HTDAQVSAEL AKQLQELTNQ LADLQATNEE LRQQVAAQAK LQVTDEIVSQ RLEELEATIA AQLLELQEQK SAMAAQNEEL AEKTTELNVL NVNLRLLEEK LAQSSRSKPL FLEDHSEDSA ASKQMQEDLQ QLKLKLDETN KANIKLKLKC KQAEKKLQKF QSQDGQQQLA SLLADNEELQ QRIAVLEDEK GQWQLANMQE DDRQPEQSTE SNNPLQLETI RLLEEQKLEL QQALEALLSS SSSAESIEIV ERHHLECLGQ RRPASEGDAQ EQKQVHPPGP SHVSELTQTE QTEEEDSSGE TLSQLRERLE LFTQERGEVL DKLEQLSAEN LQLQARLEES SSSLQLLQRE REKDLISSTS TSSNLSQELS SMQRSSEVVA TLDAGEGGPV LFEKCEKSLS KLNSELEAYR KANDRQAKFN VSKKLAKEAK NCHTQLSELL HKVKEASTAV ETVTVVETVV AVTAPNGKAL AEYEQLNAQN AELKAVISRL RQELDELRES YPETEAPLAI VGSDSQREDE ILQLQSQLED ARSLQAEQRQ QIEEQVDQIK ELRQTEAEQL QLVARQSAEI TQLQLQSEQF DQLLNSKEMS HEKQLEQQTR IRRELEARAE SLEGELSILQ TLVAEQKQQL IESVSESEHA LNLKMLELQS AQEELRELRA KEDPDQLREA LRVSKSLVAQ QVRELTSSQE TVDALNQQIQ EYQGLEHAHK EEQFKNRELR EKLKKYALNL KKRTQDNADL EQKVQELTSQ LQEQQELVKQ KEEVEREPIV DNHRVEQLQQ QVSKLNEDLK AKIHLNLENR DALRQLKQQI QEQEQLIQER DAELQDANLV SKELRRERQE ADQEVFQLGQ ENSRLREEIS KLQEEIHNLG QRVNEEPTAV EDLRRQLEAK SKKFEKSKEL IKLRNATIQS LQRELQQLQQ DQDSEVEHVR NARAAHEQLR LEKDAEITAL RQEILKLERS RAAGEGDDTI TKTSHQLLES QSQQQAESLQ VAERELQQLR VQLTAAQEQH ALLAQQYASD KANFEMTIAR LETLHEGIQA KLQEDASYIE SLEAQNTELQ ARSAALEEQA ASQANQQAAS QDKVQILEQQ LKEQREQEEQ KRQQDQQLQE RFYELGQREQ AQSRQLELLT SEAEESRQQL AGLRTEYESL LAKHSQLTAT AQAEREQMSS HSQEELAELR QQLDVKEADL HRQRQVYDAK LAAKATELDE LECDLNSHVE RAAAETRELC QQLERSQELV AQRTEELQRL NEEFQEVERE RSTLSREVTL LRLQHDSAEQ DVLELQELRM QAMQDKTEMD NLRTQIDALC ANHSQELQAL QQRIAELDTL GQNQTDDQVY IETENKRLAE QLSELQAQLA RQQHQQQQQQ HHHPAVQSQQ HPPPASLFFG GDALAAPSPF DEIAQPLRVS SLAASAPPPI SPPPTIEDLQ RNVSDLEKHA QDLETKLLAR NQNLAEQEER RLQLEQRLSE VERLLSERTQ QLADIQTANE ERDRLAALEK LIQPAAAPTL DMFFGGQAEE TVPDAVSHHL DLGLPQTEPV VEPLIQPKKA YLCQPKQEIQ EQTAQTIDWG VDEDPWASAA NEAPQTDVEH LHTRIAQLEL QLSNAEQQKT ELQTKAAKLM KRLKEYKTKA TTTATPTVTV DNDLDSTIIE ELKHQLQLQE SRLSKAEEIS QQHALEKEKL AKRIDVLTAG NDRMAEMKER QDMDVQMYQA RIRELQEKLS QLDQWGEPAA TVSSSLDGDE AARIESLQQE IQQLRQQVSE LEDERTRDQA ELGALRQSSQ GYDEAEDNQK LELQQLRQQE SELEALRTRD QSELEALRQS CQGHDETVRI ATLQQDNQQL ELQQLRQAII ELETLRARDQ TELEALRQSS QGHDEAARIA IEQRDNQQLE LQQLRQQLIE LEALRARDQA ELEALRQSCQ GQQLSVDMAS RNDEQMAQLQ EKESEIVHLK QRIEELMRED QTEKLVFEIL TKNQELQLLR MQVKQLEEDK EDQQVSAAPP KDDGETVEKL KSLCQQLQQE KSDMEEELRV LNNHVLSSLE LEDRMKQTLL QLDTKNIEIT ELRRSLEILQ SQNLGQNSAA EQIPDLSAIN QQWEQLVEQK CGEVASIWQE HLSQREAAFK AQLEEVTQQQ QRELPQSQQS TQGEATSDIM QKMQKALETQ EMEIVTLKEQ LAIRSAEYAR LAAQYDPFRL QNRGGASGGN PASTTVSAGG PPSLTANEPL PEYVLKADLD YALMMLHQRD MRVEEMIVEL VQLLEERDHL QLKLSDTLRQ LETERSRVSD EPSATASSSA ASSSSPSKIS SAGSNSELLG TTSAAGSDLK QKLAELQTVK HSKDKVIVDE REQRLQQMLQ LQKDMAKQGS GSQSGAGAVA AVAAPTSAAP TAIGVDLSQS GLRSPSMMLM DWILGNNNKE EEAGHQTTG // ID LYSA_DROME STANDARD; PRT; 140 AA. AC P37157; P29614; Q9W0J6; Q9W0J7; DT 01-OCT-1994 (Rel. 30, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lysozyme A/C/D precursor (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase DE A/C). GN LYSA AND (LYSC OR CG9111) AND (LYSD OR CG9118). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94211204; PubMed=8159165; RA Daffre S., Kylsten P., Samakovlis C., Hultmark D.; RT "The lysozyme locus in Drosophila melanogaster: an expanded gene RT family adapted for expression in the digestive tract."; RL Mol. Gen. Genet. 242:152-162(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: UNLIKELY TO PLAY AN ACTIVE ROLE IN THE HUMORAL IMMUNE CC DEFENSE. MAY HAVE A FUNCTION IN THE DIGESTION OF BACTERIA IN THE CC FOOD. CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 1,4-BETA-LINKAGES BETWEEN N- CC ACETYL-D-GLUCOSAMINE AND N-ACETYLMURAMIC ACID IN PEPTIDOGLYCAN CC HETEROPOLYMERS OF THE PROKARYOTES CELL WALLS. CC -!- TISSUE SPECIFICITY: FOUND IN THE MIDGUT. CC -!- DEVELOPMENTAL STAGE: MAXIMAL EXPRESSION IS FOUND DURING THE THIRD CC LARVAL INSTAR, IT DROPS TO BECOME UNDETECTABLE IN THE LATE PUPAL CC STAGE. THE EXPRESSION IN ADULTS IS SIMILAR TO THAT OF FIRST AND CC SECOND LARVAL INSTARS. CC -!- SIMILARITY: BELONGS TO FAMILY 22 OF GLYCOSYL HYDROLASES. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z22223; CAA80225.1; -. DR EMBL; Z22226; CAA80228.1; -. DR EMBL; X58382; CAA41272.1; -. DR EMBL; AE003470; AAF47449.1; ALT_SEQ. DR EMBL; AE003470; AAF47450.1; -. DR EMBL; AE003470; -; NOT_ANNOTATED_CDS. DR PIR; S20914; S20914. DR PIR; S41573; S41573. DR HSSP; P00695; 1LZ5. DR FlyBase; FBgn0011201; LysA. DR FlyBase; FBgn0004426; LysC. DR FlyBase; FBgn0004427; LysD. DR GO; GO:0004568; F:chitinase activity; IDA. DR GO; GO:0003796; F:lysozyme activity; IDA. DR InterPro; IPR001916; Glyco_hydro_22. DR Pfam; PF00062; lys; 1. DR PRINTS; PR00135; LYZLACT. DR SMART; SM00263; LYZ1; 1. DR PROSITE; PS00128; LACTALBUMIN_LYSOZYME; 1. KW Hydrolase; Glycosidase; Bacteriolytic enzyme; Signal; KW Multigene family. FT SIGNAL 1 18 BY SIMILARITY. FT CHAIN 19 140 LYSOZYME A/C/D. FT DISULFID 24 139 BY SIMILARITY. FT DISULFID 45 129 BY SIMILARITY. FT DISULFID 80 96 BY SIMILARITY. FT DISULFID 92 110 BY SIMILARITY. FT ACT_SITE 50 50 BY SIMILARITY. FT ACT_SITE 68 68 BY SIMILARITY. FT CONFLICT 41 42 AR -> NK (IN REF. 1). SQ SEQUENCE 140 AA; 15635 MW; 75C24CA6F85DF903 CRC64; MKAFIVLVAL ACAAPAFGRT MDRCSLAREM SNLGVPRDQL ARWACIAEHE SSYRTGVVGP ENYNGSNDYG IFQINDYYWC APPSGRFSYN ECGLSCNALL TDDITHSVRC AQKVLSQQGW SAWSTWHYCS GWLPSIDDCF // ID LYSB_DROME STANDARD; PRT; 140 AA. AC Q08694; P37158; Q9W0J8; DT 01-OCT-1994 (Rel. 30, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lysozyme B precursor (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase B). GN LYSB OR CG1179. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94211204; PubMed=8159165; RA Daffre S., Kylsten P., Samakovlis C., Hultmark D.; RT "The lysozyme locus in Drosophila melanogaster: an expanded gene RT family adapted for expression in the digestive tract."; RL Mol. Gen. Genet. 242:152-162(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: UNLIKELY TO PLAY AN ACTIVE ROLE IN THE HUMORAL IMMUNE CC DEFENSE. MAY HAVE A FUNCTION IN THE DIGESTION OF BACTERIA IN THE CC FOOD. CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 1,4-BETA-LINKAGES BETWEEN N- CC ACETYL-D-GLUCOSAMINE AND N-ACETYLMURAMIC ACID IN PEPTIDOGLYCAN CC HETEROPOLYMERS OF THE PROKARYOTES CELL WALLS. CC -!- TISSUE SPECIFICITY: FOUND IN THE MIDGUT. CC -!- DEVELOPMENTAL STAGE: MAXIMAL EXPRESSION IS FOUND DURING THE THIRD CC LARVAL INSTAR, IT DROPS TO BECOME UNDETECTABLE IN THE LATE PUPAL CC STAGE. THE EXPRESSION IN ADULTS IS SIMILAR TO THAT OF FIRST AND CC SECOND LARVAL INSTARS. CC -!- SIMILARITY: BELONGS TO FAMILY 22 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z22225; CAA80227.1; -. DR EMBL; AE003470; AAF47448.1; -. DR PIR; S41574; S41574. DR HSSP; P00695; 1LZ5. DR FlyBase; FBgn0004425; LysB. DR InterPro; IPR001916; Glyco_hydro_22. DR Pfam; PF00062; lys; 1. DR PRINTS; PR00135; LYZLACT. DR SMART; SM00263; LYZ1; 1. DR PROSITE; PS00128; LACTALBUMIN_LYSOZYME; 1. KW Hydrolase; Glycosidase; Bacteriolytic enzyme; Signal; KW Multigene family. FT SIGNAL 1 18 BY SIMILARITY. FT CHAIN 19 140 LYSOZYME B. FT DISULFID 24 139 BY SIMILARITY. FT DISULFID 45 129 BY SIMILARITY. FT DISULFID 80 96 BY SIMILARITY. FT DISULFID 92 110 BY SIMILARITY. FT ACT_SITE 50 50 BY SIMILARITY. FT ACT_SITE 68 68 BY SIMILARITY. FT CONFLICT 12 13 LA -> SG (IN REF. 1). SQ SEQUENCE 140 AA; 15611 MW; 70AFA5321857F093 CRC64; MKAFIVLVAL ALAAPALGRT MDRCSLAREM SNLGVPRDQL ARWACIAEHE SSYRTGVVGP ENYNGSNDYG IFQINDYYWC APPSGRFSYN ECGLSCNALL TDDITHSVRC AQKVLSQQGW SAWSTWHYCS GWLPSIDDCF // ID LYSE_DROME STANDARD; PRT; 140 AA. AC P37159; Q9W0J5; DT 01-OCT-1994 (Rel. 30, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lysozyme E precursor (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase E). GN LYSE OR CG1180. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94211204; PubMed=8159165; RA Daffre S., Kylsten P., Samakovlis C., Hultmark D.; RT "The lysozyme locus in Drosophila melanogaster: an expanded gene RT family adapted for expression in the digestive tract."; RL Mol. Gen. Genet. 242:152-162(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: UNLIKELY TO PLAY AN ACTIVE ROLE IN THE HUMORAL IMMUNE CC DEFENSE. MAY HAVE A FUNCTION IN THE DIGESTION OF BACTERIA IN THE CC FOOD. CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 1,4-BETA-LINKAGES BETWEEN N- CC ACETYL-D-GLUCOSAMINE AND N-ACETYLMURAMIC ACID IN PEPTIDOGLYCAN CC HETEROPOLYMERS OF THE PROKARYOTES CELL WALLS. CC -!- TISSUE SPECIFICITY: FOUND IN THE MIDGUT. CC -!- DEVELOPMENTAL STAGE: MAXIMAL EXPRESSION IS FOUND DURING THE THIRD CC LARVAL INSTAR, IT DROPS TO BECOME UNDETECTABLE IN THE LATE PUPAL CC STAGE. THE EXPRESSION IN ADULTS IS SIMILAR TO THAT OF FIRST AND CC SECOND LARVAL INSTARS. CC -!- SIMILARITY: BELONGS TO FAMILY 22 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z22227; CAA80229.1; -. DR EMBL; AE003470; AAF47451.1; -. DR PIR; S41577; S41577. DR HSSP; P00695; 1OUE. DR FlyBase; FBgn0004428; LysE. DR InterPro; IPR001916; Glyco_hydro_22. DR Pfam; PF00062; lys; 1. DR PRINTS; PR00135; LYZLACT. DR SMART; SM00263; LYZ1; 1. DR PROSITE; PS00128; LACTALBUMIN_LYSOZYME; 1. KW Hydrolase; Glycosidase; Bacteriolytic enzyme; Signal; KW Multigene family. FT SIGNAL 1 18 BY SIMILARITY. FT CHAIN 19 140 LYSOZYME E. FT DISULFID 24 139 BY SIMILARITY. FT DISULFID 45 129 BY SIMILARITY. FT DISULFID 80 96 BY SIMILARITY. FT DISULFID 92 110 BY SIMILARITY. FT ACT_SITE 50 50 BY SIMILARITY. FT ACT_SITE 68 68 BY SIMILARITY. FT CONFLICT 12 12 M -> L (IN REF. 1). FT CONFLICT 76 76 N -> D (IN REF. 1). FT CONFLICT 138 138 G -> D (IN REF. 1). SQ SEQUENCE 140 AA; 15552 MW; CEB5465CF6B6F123 CRC64; MKAFIVLVAL AMAAPALGRT LDRCSLAREM SNLGVPRDQL ARWACIAEHE SSYRTGVVGP ENYNGSNDYG IFQINNYYWC APPSGRFSYN ECGLSCNALL TDDITHSVRC AQKVLSQQGW SAWSTWHYCS GWLPSIDGCF // ID LYSP_DROME STANDARD; PRT; 141 AA. AC P29615; Q9W0J4; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lysozyme P precursor (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase P). GN LYSP OR CG9116. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92269751; PubMed=1588905; RA Kylsten P., Kimbrell D.A., Daffre S., Samakovlis C., Hultmark D.; RT "The lysozyme locus in Drosophila melanogaster: different genes are RT expressed in midgut and salivary glands."; RL Mol. Gen. Genet. 232:335-343(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: UNLIKELY TO PLAY AN ACTIVE ROLE IN THE HUMORAL IMMUNE CC DEFENSE. MAY HAVE A FUNCTION IN THE DIGESTION OF BACTERIA IN THE CC FOOD. CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 1,4-BETA-LINKAGES BETWEEN N- CC ACETYL-D-GLUCOSAMINE AND N-ACETYLMURAMIC ACID IN PEPTIDOGLYCAN CC HETEROPOLYMERS OF THE PROKARYOTES CELL WALLS. CC -!- TISSUE SPECIFICITY: SALIVARY GLAND. CC -!- DEVELOPMENTAL STAGE: ONLY EXPRESSED IN ADULTS. CC -!- SIMILARITY: BELONGS TO FAMILY 22 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58383; CAA41273.1; -. DR EMBL; AE003470; AAF47452.1; -. DR PIR; S20915; S20915. DR HSSP; P00695; 1LZ5. DR FlyBase; FBgn0004429; LysP. DR InterPro; IPR001916; Glyco_hydro_22. DR Pfam; PF00062; lys; 1. DR PRINTS; PR00135; LYZLACT. DR SMART; SM00263; LYZ1; 1. DR PROSITE; PS00128; LACTALBUMIN_LYSOZYME; 1. KW Hydrolase; Glycosidase; Bacteriolytic enzyme; Signal; KW Multigene family. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 141 LYSOZYME P. FT DISULFID 25 140 BY SIMILARITY. FT DISULFID 46 130 BY SIMILARITY. FT DISULFID 81 97 BY SIMILARITY. FT DISULFID 93 111 BY SIMILARITY. FT ACT_SITE 51 51 BY SIMILARITY. FT ACT_SITE 69 69 BY SIMILARITY. SQ SEQUENCE 141 AA; 15648 MW; 4D7C51B018FD5417 CRC64; MKAFLVICAL TLTAVATQAR TMDRCSLARE MSKLGVPRDQ LAKWTCIAQH ESSFRTGVVG PANSNGSNDY GIFQINNKYW CKPADGRFSY NECGLSCNAL LTDDITNSVK CARKIQRQQG WTAWSTWKYC SGSLPSINSC F // ID LYSS_DROME STANDARD; PRT; 140 AA. AC P37160; Q9W0J3; DT 01-OCT-1994 (Rel. 30, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lysozyme S precursor (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase S). GN LYSS OR CG1165. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94211204; PubMed=8159165; RA Daffre S., Kylsten P., Samakovlis C., Hultmark D.; RT "The lysozyme locus in Drosophila melanogaster: an expanded gene RT family adapted for expression in the digestive tract."; RL Mol. Gen. Genet. 242:152-162(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: UNLIKELY TO PLAY AN ACTIVE ROLE IN THE HUMORAL IMMUNE CC DEFENSE. MAY HAVE A FUNCTION IN THE DIGESTION OF BACTERIA IN THE CC FOOD. CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 1,4-BETA-LINKAGES BETWEEN N- CC ACETYL-D-GLUCOSAMINE AND N-ACETYLMURAMIC ACID IN PEPTIDOGLYCAN CC HETEROPOLYMERS OF THE PROKARYOTES CELL WALLS. CC -!- TISSUE SPECIFICITY: FOUND IN THE MIDGUT, ESPECIALLY THE EPITHELIUM CC OF THE GASTRIC CAECAE. CC -!- DEVELOPMENTAL STAGE: EXPRESSED ONLY DURING THE LARVAL STAGE, THE CC HIGHEST LEVEL IS REACHED DURING THE THIRD LARVAL INSTAR. CC -!- SIMILARITY: BELONGS TO FAMILY 22 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003470; AAF47453.1; -. DR EMBL; Z22228; CAA80230.1; -. DR PIR; S41579; S41579. DR HSSP; P00695; 1C46. DR FlyBase; FBgn0004430; LysS. DR InterPro; IPR001916; Glyco_hydro_22. DR Pfam; PF00062; lys; 1. DR PRINTS; PR00135; LYZLACT. DR SMART; SM00263; LYZ1; 1. DR PROSITE; PS00128; LACTALBUMIN_LYSOZYME; 1. KW Hydrolase; Glycosidase; Bacteriolytic enzyme; Signal; KW Multigene family. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 140 LYSOZYME S. FT DISULFID 25 139 BY SIMILARITY. FT DISULFID 46 129 BY SIMILARITY. FT DISULFID 81 96 BY SIMILARITY. FT DISULFID 92 110 BY SIMILARITY. FT ACT_SITE 51 51 BY SIMILARITY. FT ACT_SITE 69 69 BY SIMILARITY. FT CONFLICT 11 16 AIAAPA -> PLPLC (IN REF. 1). SQ SEQUENCE 140 AA; 15651 MW; ACD139CC656EF8FC CRC64; MKAFFALVLL AIAAPALAGR TLDRCSLARE MADLGVPRDQ LDKWTCIAQH ESDYRTWVVG PANSDGSNDY GIFQINDLYW CQADGRFSYN ECGLSCNALL TDDITNSVRC AQKVLSQQGW SAWAVWHYCS GWLPSIDECF // ID LYSX_DROME STANDARD; PRT; 142 AA. AC P37161; Q9W0K1; DT 01-OCT-1994 (Rel. 30, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lysozyme X precursor (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase X). GN LYSX OR CG9120. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 62-142 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94211204; PubMed=8159165; RA Daffre S., Kylsten P., Samakovlis C., Hultmark D.; RT "The lysozyme locus in Drosophila melanogaster: an expanded gene RT family adapted for expression in the digestive tract."; RL Mol. Gen. Genet. 242:152-162(1994). CC -!- FUNCTION: UNLIKELY TO PLAY AN ACTIVE ROLE IN THE HUMORAL IMMUNE CC DEFENSE. MAY HAVE A FUNCTION IN THE DIGESTION OF BACTERIA IN THE CC FOOD. MAY BE INVOLVED IN THE CLEARANCE OF BACTERIA FROM THE LARVAL CC GUT BEFORE METAMORPHOSIS. CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 1,4-BETA-LINKAGES BETWEEN N- CC ACETYL-D-GLUCOSAMINE AND N-ACETYLMURAMIC ACID IN PEPTIDOGLYCAN CC HETEROPOLYMERS OF THE PROKARYOTES CELL WALLS. CC -!- TISSUE SPECIFICITY: FOUND IN THE MIDGUT. CC -!- DEVELOPMENTAL STAGE: RISES DRAMATICALLY IN THE LATE THIRD INSTAR, CC THEN DECREASES GRADUALLY DURING THE PUPAL STAGES. LOW EXPRESSION CC IS FOUND IN ADULTS. CC -!- SIMILARITY: BELONGS TO FAMILY 22 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003470; AAF47445.1; -. DR EMBL; Z22224; CAA80226.1; -. DR PIR; S41580; S41580. DR HSSP; P00698; 1AT5. DR FlyBase; FBgn0004431; LysX. DR InterPro; IPR001916; Glyco_hydro_22. DR Pfam; PF00062; lys; 1. DR PRINTS; PR00135; LYZLACT. DR SMART; SM00263; LYZ1; 1. DR PROSITE; PS00128; LACTALBUMIN_LYSOZYME; 1. KW Hydrolase; Glycosidase; Bacteriolytic enzyme; Signal; KW Multigene family. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 142 LYSOZYME X. FT DISULFID 25 140 BY SIMILARITY. FT DISULFID 46 130 BY SIMILARITY. FT DISULFID 81 97 BY SIMILARITY. FT DISULFID 93 111 BY SIMILARITY. FT ACT_SITE 51 51 BY SIMILARITY. FT ACT_SITE 69 69 BY SIMILARITY. FT CONFLICT 78 78 M -> L (IN REF. 2). SQ SEQUENCE 142 AA; 15591 MW; 2A48035364B995BC CRC64; MRALLGICVL ALVTPAVLGR TMDRCSLARE MANMGVSRDQ LSKWACIAEH ESSYRTGVVG PPNTDGSNDY GIFQINDMYW CQPSSGKFSH NGCDVSCNAL LTDDIKSSVR CALKVLGQQG WSAWSTWHYC SGYLPPIDDC FV // ID M121_DROME STANDARD; PRT; 667 AA. AC P53624; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform 1 DE (EC 3.2.1.113) (Man(9)-alpha-mannosidase). GN ALPHA-MAN-1 OR MAS-1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=95246933; PubMed=7729592; RA Kerscher S., Albert S., Wucherpfennig D., Heisenberg M., Schneuwly S.; RT "Molecular and genetic analysis of the Drosophila mas-1 RT (mannosidase-1) gene which encodes a glycoprotein processing alpha RT 1,2-mannosidase."; RL Dev. Biol. 168:613-626(1995). CC -!- FUNCTION: INVOLVED IN THE MATURATION OF ASN-LINKED CC OLIGOSACCHARIDES. PROGRESSIVELY TRIM ALPHA-1,2-LINKED MANNOSE CC RESIDUES FROM MAN(9)GLCNAC(2) TO PRODUCE MAN(5)GLCNAC(2). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE TERMINAL 1,2-LINKED ALPHA-D- CC MANNOSE RESIDUES IN THE OLIGO-MANNOSE OLIGOSACCHARIDE CC MAN(9)(GLCNAC)(2). CC -!- COFACTOR: CALCIUM (BY SIMILARITY). CC -!- PATHWAY: N-GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P53624-1; Sequence=Displayed; CC Name=2; CC IsoId=P53625-1; Sequence=External; CC -!- TISSUE SPECIFICITY: COMPLEX SPATIAL DISTRIBUTION DURING CC EMBRYOGENESIS, INCLUDING EXPRESSION IN LOBULA PLATE GIANT NEURONS. CC ALSO EXPRESSED IN ADULT WING AND EYES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC DURING EMBRYONIC STAGES. CC -!- SIMILARITY: BELONGS TO FAMILY 47 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X82640; CAA57962.1; -. DR EMBL; X82641; CAA57963.1; -. DR PIR; S60709; S60709. DR HSSP; P32906; 1DL2. DR FlyBase; FBgn0010338; alpha-Man-I. DR InterPro; IPR001382; Glyco_hydro_47. DR Pfam; PF01532; Glyco_hydro_47; 1. DR PRINTS; PR00747; GLYHDRLASE47. DR ProDom; PD003239; Glyco_hydro_47; 1. KW Hydrolase; Glycosidase; Glycoprotein; Transmembrane; Calcium-binding; KW Signal-anchor; Golgi stack; Alternative splicing. FT DOMAIN 1 18 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 19 39 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 40 667 LUMENAL (POTENTIAL). FT CA_BIND 275 287 POTENTIAL. FT CARBOHYD 278 278 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 667 AA; 74967 MW; 8F49C7D94A88F9D0 CRC64; MYRISPIGRK SNFHSREKCL TGLVLVTLCF LCFGGIFLLP DNFGSDRVLR VYKHFRKAGP EIFIPAPPLA AHAPHRSEDP HFIGDRQRLE QKIRAELGDM LDEPPAAGGG EPGQFQVLAQ QAQAPAPVAA LADQPLDQDE GHAAIPVLAA PVQGDNAASQ ASSHPQSSAQ QHNQQQPQLP LGGGGNDQAP DTLDATLEER RQKVKEMMEH AWHNYKLYAW GKNELRPLSQ RPHSASIFGS YDLGATIVDG LDTLYIMGLE KEYREGRDWI ERKFSLDNIS AELSVFETNI RFVGGMLTLY AFTGDPLYKE KAQHVADKLL PAFQTPTGIP YALVNTKTGV AKNYGWASGG SSILSEFGTL HLEFAYLSDI TGNPLYRERV QTIRQVLKEI EKPKGLYPNF LNPKTGKWGQ LHMSLGALGD SYYEYLLKAW LQSGQTDEEA REMFDEAMLA ILDKMVRTSP GGLTYVSDLK FDRLEHKMDH LACFSGGLFA LGAATRQNDY TDKYMEVGKG ITNTCHESYI RAPTQLGPEA FRFSEAVEAR ALRSQEKYYI LRPETFESYF VLWRLTHEQK YRDWGWEAVL ALEKHCRTAH GYCGLRNVYQ QEPQKDDVQQ SFFLAETLKY LYLLFSDDSV LPLDEWVFNT EAHPLPIKGA NAYYRQAPVT LPVSNAS // ID M122_DROME STANDARD; PRT; 643 AA. AC P53625; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform 2 DE (EC 3.2.1.113) (Man(9)-alpha-mannosidase). GN ALPHA-MAN-1 OR MAS-1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berlin; TISSUE=Head; RX MEDLINE=95246933; PubMed=7729592; RA Kerscher S., Albert S., Wucherpfennig D., Heisenberg M., RA Schneuwly S.; RT "Molecular and genetic analysis of the Drosophila mas-1 RT (mannosidase-1) gene which encodes a glycoprotein processing alpha RT 1,2-mannosidase."; RL Dev. Biol. 168:613-626(1995). CC -!- FUNCTION: INVOLVED IN THE MATURATION OF ASN-LINKED CC OLIGOSACCHARIDES. PROGRESSIVELY TRIM ALPHA-1,2-LINKED MANNOSE CC RESIDUES FROM MAN(9)GLCNAC(2) TO PRODUCE MAN(5)GLCNAC(2). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE TERMINAL 1,2-LINKED ALPHA-D- CC MANNOSE RESIDUES IN THE OLIGO-MANNOSE OLIGOSACCHARIDE CC MAN(9)(GLCNAC)(2). CC -!- COFACTOR: CALCIUM (BY SIMILARITY). CC -!- PATHWAY: N-GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; CC IsoId=P53625-1; Sequence=Displayed; CC Name=1; CC IsoId=P53624-1; Sequence=External; CC -!- TISSUE SPECIFICITY: COMPLEX SPATIAL DISTRIBUTION DURING CC EMBRYOGENESIS, INCLUDING EXPRESSION IN LOBULA PLATE GIANT NEURONS. CC ALSO EXPRESSED IN ADULT WING AND EYES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC DURING EMBRYONIC STAGES. CC -!- SIMILARITY: BELONGS TO FAMILY 47 OF GLYCOSYL HYDROLASES. DR PIR; S60710; S60710. DR HSSP; P32906; 1DL2. DR FlyBase; FBgn0010338; alpha-Man-I. DR InterPro; IPR001382; Glyco_hydro_47. DR Pfam; PF01532; Glyco_hydro_47; 1. DR PRINTS; PR00747; GLYHDRLASE47. DR ProDom; PD003239; Glyco_hydro_47; 1. KW Hydrolase; Glycosidase; Glycoprotein; Transmembrane; Calcium-binding; KW Signal-anchor; Golgi stack; Alternative splicing. FT DOMAIN 1 11 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 12 32 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 33 643 LUMENAL (POTENTIAL). FT CA_BIND 251 263 POTENTIAL. FT CARBOHYD 36 36 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 77 77 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 166 166 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 254 254 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 643 AA; 72539 MW; 7375AC9C9B6FD1D9 CRC64; MCPKTSKTTP LLLIGGICFV IVLVGITGIT LINNINLSNI IRLNEKVASD SVSNNENQIK ELNYVNNHPR NVYLKLNASS RDDEDDEQMQ KEQEQLELPK ISAVIGGSKP KVEDNQVKES SEVISPSTST FSMRSSAGEL TSTSAPLSSI VSVTAPPMPF GGVKYNQSSG LIDYEKRNQV VKMMEHAWHN YKLYAWGKNE LRPLSQRPHS ASIFGSYDLG ATIVDGLDTL YIMGLEKEYR EGRDWIERKF SLDNISAELS VFETNIRFVG GMLTLYAFTG DPLYKEKAQH VADKLLPAFQ TPTGIPYALV NTKTGVAKNY GWASGGSSIL SEFGTLHLEF AYLSDITGNP LYRERVQTIR QVLKEIEKPK GLYPNFLNPK TGKWGQLHMS LGALGDSYYE YLLKAWLQSG QTDEEAREMF DEAMLAILDK MVRTSPGGLT YVSDLKFDRL EHKMDHLACF SGGLFALGAA TRQNDYTDKY MEVGKGITNT CHESYIRAPT QLGPEAFRFS EAVEARALRS QEKYYILRPE TFESYFVLWR LTHEQKYRDW GWEAVLALEK HCRTAHGYCG LRNVYQQEPQ KDDVQQSFFL AETLKYLYLL FSDDSVLPLD EWVFNTEAHP LPIKGANAYY RQAPVTLPVS NAS // ID M14A_DROME STANDARD; PRT; 366 AA. AC O62618; O46216; Q9TXB4; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitogen-activated protein kinase 14A (EC 2.7.1.37) (MAP kinase p38a) DE (p38 MAPK) (Dp38) (D-p38a). GN MPK2 OR P38A OR CG5475. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, DEVELOPMENTAL STAGE, AND ENZYME RP REGULATION. RC TISSUE=Embryo; RX MEDLINE=98252940; PubMed=9584193; RA Han Z.S., Enslen H., Hu X., Meng X., Wu I.-H., Barrett T., Davis R.J., RA Ip Y.T.; RT "A conserved p38 mitogen-activated protein kinase pathway regulates RT Drosophila immunity gene expression."; RL Mol. Cell. Biol. 18:3527-3539(1998). RN [2] RP SEQUENCE FROM N.A., PHOSPHORYLATION OF TYR-186, FUNCTION, SUBCELLULAR RP LOCATION, AND ENZYME REGULATION. RC TISSUE=Hemocyte; RX MEDLINE=98079070; PubMed=9417090; RA Han S.-J., Choi K.-Y., Brey P.T., Lee W.-J.; RT "Molecular cloning and characterization of a Drosophila p38 mitogen- RT activated protein kinase."; RL J. Biol. Chem. 273:369-374(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 38-188 FROM N.A. RC TISSUE=Imaginal disks; RX MEDLINE=92335284; PubMed=1378625; RA Biggs W.H. III, Zipursky S.L.; RT "Primary structure, expression, and signal-dependent tyrosine RT phosphorylation of a Drosophila homolog of extracellular signal- RT regulated kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992). CC -!- FUNCTION: KINASE INVOLVED IN A SIGNAL TRANSDUCTION PATHWAY. MAY CC DOWN REGULATE INSECT IMMUNITY GENE EXPRESSION AFTER PROLONGED CC INFECTION. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- COFACTOR: MAGNESIUM (BY SIMILARITY). CC -!- ENZYME REGULATION: ACTIVATED BY MKK3 AND BY PHOSPHORYLATION ON CC TYR-186 IN RESPONSE TO ENVIRONMENTAL STRESS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC LEVELS ARE HIGHEST AT THE PREBLASTODERM STAGE BUT LOW LEVELS ARE CC PRESENT THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. MAP CC KINASE SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF035546; AAC39030.1; -. DR EMBL; AF035547; AAC39031.1; -. DR EMBL; U86867; AAB97138.1; -. DR EMBL; AE003746; AAF56244.1; -. DR HSSP; Q16539; 1WFC. DR FlyBase; FBgn0015765; Mpk2. DR GO; GO:0004707; F:MAP kinase activity; IDA. DR GO; GO:0008348; P:attenuation of antimicrobial humoral response; IMP. DR GO; GO:0006955; P:immune response; IDA. DR GO; GO:0000165; P:MAPKKK cascade; NAS. DR GO; GO:0006970; P:response to osmotic stress; IDA. DR InterPro; IPR008351; JNK_MAPK. DR InterPro; IPR003527; MAP_kin. DR InterPro; IPR008352; p38_MAPK. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR01772; JNKMAPKINASE. DR PRINTS; PR01773; P38MAPKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Nuclear protein; Phosphorylation. FT DOMAIN 25 312 PROTEIN KINASE. FT NP_BIND 31 39 ATP (BY SIMILARITY). FT BINDING 54 54 ATP (BY SIMILARITY). FT ACT_SITE 154 154 BY SIMILARITY. FT MOD_RES 184 184 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 186 186 PHOSPHORYLATION. FT CONFLICT 27 27 D -> G (IN REF. 2). FT CONFLICT 77 77 K -> R (IN REF. 4). FT CONFLICT 80 80 D -> A (IN REF. 2). FT CONFLICT 108 108 L -> LL (IN REF. 4). FT CONFLICT 124 124 Q -> QQ (IN REF. 4). FT CONFLICT 149 149 MISSING (IN REF. 4). FT CONFLICT 163 163 N -> NN (IN REF. 4). SQ SEQUENCE 366 AA; 42255 MW; B3592B869F97990E CRC64; MSVSITKKFY KLDINRTEWE IPDIYQDLQP VGSGAYGQVS KAVVRGTNMH VAIKKLARPF QSAVHAKRTY RELRLLKHMD HENVIGLLDI FHPHPANGSL ENFQQVYLVT HLMDADLNNI IRMQHLSDDH VQFLVYQILR GLKYIHSAGV IHRDLKPSNI AVNEDCELRI LDFGLARPTE NEMTGYVATR WYRAPEIMLN WMHYDQTVDI WSVGCIMAEL ITRRTLFPGT DHIHQLNLIM EMLGTPPAEF LKKISSESAR SYIQSLPPMK GRSFKNVFKN ANPLAIDLLE KMLELDAEKR ITAEEALSHP YLEKYAEPSV EQTSPPYDHS FEDMDLPVDK WKELIYKEVT NFKPPPSYAQ VLKDVK // ID M14B_DROME STANDARD; PRT; 365 AA. AC O61443; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitogen-activated protein kinase 14B (EC 2.7.1.37) (MAP kinase p38b) DE (D-p38b). GN P38B OR CG7393. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND ENZYME REGULATION. RC TISSUE=Embryo; RX MEDLINE=98252940; PubMed=9584193; RA Han Z.S., Enslen H., Hu X., Meng X., Wu I.-H., Barrett T., Davis R.J., RA Ip Y.T.; RT "A conserved p38 mitogen-activated protein kinase pathway regulates RT Drosophila immunity gene expression."; RL Mol. Cell. Biol. 18:3527-3539(1998). RN [2] RP SEQUENCE FROM N.A., AND FUNCTION. RC TISSUE=Imaginal disks; RX MEDLINE=99147066; PubMed=10022918; RA Adachi-Yamada T., Nakamura M., Irie K., Tomoyasu Y., Sano Y., Mori E., RA Goto S., Ueno N., Nishida Y., Matsumoto K.; RT "p38 mitogen-activated protein kinase can be involved in transforming RT growth factor beta superfamily signal transduction in Drosophila wing RT morphogenesis."; RL Mol. Cell. Biol. 19:2322-2329(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: KINASE INVOLVED IN DPP SIGNAL TRANSDUCTION PATHWAY IN CC THE PROCESS OF WING MORPHOGENESIS WHEN THE LEVELS OF DPP ARE CC ENHANCED OR INHIBITED. MAY DOWN REGULATE INSECT IMMUNITY GENE CC EXPRESSION AFTER PROLONGED INFECTION. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- COFACTOR: MAGNESIUM (BY SIMILARITY). CC -!- ENZYME REGULATION: ACTIVATED BY MKK3. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: AT MID-EMBRYOGENESIS, HIGHEST EXPRESSION IS CC SEEN IN DEVELOPING ANTERIOR AND POSTERIOR MIDGUTS. ALMOST CC UBIQUITOUS EXPRESSION THROUGHOUT ALL DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY IN CC THE EMBRYO, EXPRESSION SEEN IN ALL DEVELOPMENTAL STAGES. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. MAP CC KINASE SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF035548; AAC39032.1; -. DR EMBL; AB006364; BAA35141.1; -. DR EMBL; AE003407; AAF44812.1; -. DR EMBL; AE003641; AAF53326.1; -. DR EMBL; AY058548; AAL13777.1; -. DR HSSP; Q16539; 1WFC. DR FlyBase; FBgn0024846; p38b. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0004674; F:protein serine/threonine kinase activity; NAS. DR GO; GO:0016909; F:SAP kinase activity; NAS. DR GO; GO:0000165; P:MAPKKK cascade; NAS. DR GO; GO:0030510; P:regulation of BMP signaling pathway; IDA. DR GO; GO:0045088; P:regulation of innate immune response; IDA. DR GO; GO:0007476; P:wing morphogenesis; IDA. DR InterPro; IPR008351; JNK_MAPK. DR InterPro; IPR003527; MAP_kin. DR InterPro; IPR008352; p38_MAPK. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR01772; JNKMAPKINASE. DR PRINTS; PR01773; P38MAPKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Nuclear protein; Phosphorylation. FT DOMAIN 24 311 PROTEIN KINASE. FT NP_BIND 30 38 ATP (BY SIMILARITY). FT BINDING 53 53 ATP (BY SIMILARITY). FT ACT_SITE 153 153 BY SIMILARITY. FT MOD_RES 183 183 PHOSPHORYLATION (ACTIVATES THE KINASE) FT (BY SIMILARITY). FT MOD_RES 185 185 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 365 AA; 42098 MW; 3B3F217E467BAD53 CRC64; MSRKMAKFYK LDINRTEWEI PETYQNLQPV GQGAYGQVCK AVVRGTSTKV AIKKLARPFQ SAVHAKRTYR ELRLLKHMDH ENVIGLLDVF HPGQPADSLD QFQQVYMVTH LMDADLNNII RTQKLSDDHV QFLVYQILRG LKYIHSAGVI HRDLKPSNIA VNEDCELRIL DFGLARPAES EMTGYVATRW YRAPEIMLNW MHYNQTADIW SVGCIMAELL TGRTLFPGTD HIHQLNLIME VLGTPADEFM SRISSESARN YIRSLPVMPR RNFRDIFRGA NPLAIDLLEK MLELDADKRI TAEQALAHPY MEKYHDPTDE QTAALYDQSF EENELPVEKW REMVFSEVTA FKPTAAFAEL LPKEQ // ID M14C_DROME STANDARD; PRT; 356 AA. AC P83100; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative mitogen-activated protein kinase 14C (EC 2.7.1.37) (MAP DE kinase p38c). GN P38C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Manning G., Sudarsanam S., Plowman G.; RT "Prediction of novel protein kinases from the Drosophila genome RT project and EST sequences."; RL Unpublished observations (AUG-2001). CC -!- FUNCTION: KINASE INVOLVED IN A SIGNAL TRANSDUCTION PATHWAY. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- COFACTOR: MAGNESIUM (BY SIMILARITY). CC -!- ENZYME REGULATION: ACTIVATED BY TYROSINE AND THREONINE CC PHOSPHORYLATION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. MAP CC KINASE SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003746; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0046322; p38c. DR InterPro; IPR003527; MAP_kin. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS01351; MAPK; FALSE_NEG. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. KW Hypothetical protein; Transferase; Serine/threonine-protein kinase; KW ATP-binding; Phosphorylation. FT DOMAIN 20 305 PROTEIN KINASE. FT NP_BIND 26 34 ATP (BY SIMILARITY). FT BINDING 49 49 ATP (BY SIMILARITY). FT ACT_SITE 147 147 BY SIMILARITY. FT MOD_RES 177 177 PHOSPHORYLATION (ACTIVATES THE KINASE) FT (BY SIMILARITY). SQ SEQUENCE 356 AA; 41968 MW; F90340860375BAF9 CRC64; MPEFVRVAIN ESLWEFPDIY EFVRFLGGGS FGQVAKVRLR GTENYFAMKR LMRPFEREED AKGTYREIRL LKHMNHRNVI SLLNVFHPPA HNMMEFQQVY LVTHLMDADL HRYSRSKRMS DQEIRIILYQ ILRGLKYIHS AGVVHRDLKP CNIAVNGNSE VRILDFGLSR MCADKMTDHV GTMWYLAPEI IFLRGQYTKA IDVWSVGCIL AELITDRVLF RGENYVSQIR CLINIMGTPT REFITGISME RSRNYLEGYP LRQRCDFHHL FMGYDVQAID LMEKMLEMVP EKRITAAEAM LHPYLRDLIE PHHHAEDTAP VYDQNFENMV LPVKCWKELV SHEIRNFRPD QLDLHF // ID M3K7_DROME STANDARD; PRT; 393 AA. AC P83104; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative mitogen-activated protein kinase kinase kinase 7 DE (EC 2.7.1.-). GN TAKL1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Manning G., Sudarsanam S., Plowman G.; RT "Prediction of novel protein kinases from the Drosophila genome RT project and EST sequences."; RL Unpublished observations (AUG-2001). CC -!- FUNCTION: CAN PHOSPHORYLATE AND ACTIVATE YET UNDEFINED MAPKKS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. MAP CC KINASE KINASE KINASE SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003732; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0046689; Takl1. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Hypothetical protein; Transferase; Serine/threonine-protein kinase; KW Tyrosine-protein kinase; ATP-binding. FT DOMAIN 11 266 PROTEIN KINASE. FT NP_BIND 17 25 ATP (By similarity). FT BINDING 38 38 ATP (By similarity). FT ACT_SITE 133 133 BY SIMILARITY. SQ SEQUENCE 393 AA; 45238 MW; 43370C98490F0384 CRC64; MVKQVDFAEV KLSEKFLGAG SGGAVRKATF QNQEIAVKIF DFLEETIKKN AEREITHLSE IDHENVIRVI GRASNGKKDY LLMEYLEEGS LHNYLYGDDK WEYTVEQAVR WALQCAKALA YLHSLDRPIV HRDIKPQNML LYNQHEDLKI CDFGLATDMS NNKTDMQGTL RYMAPEAIKH LKYTAKCDVY SFGIMLWELM TRQLPYSHLE NPNSQYAIMK AISSGEKLPM EAVRSDCPEG IKQLMECCMD INPEKRPSMK EIEKFLGEQY ESGTDEDFIK PLDEDTVAVV TYHVDSSGSR IMRVDFWRHQ LPSIRMTFPI VKREAERLGK TVVREMAKAA ADGDREVRRA EKDTERETSR AAHNGERETR RAGQDVGRET VRAVKKIGKK LRF // ID M84A_DROME STANDARD; PRT; 63 AA. AC Q01642; Q9VIA3; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Male specific sperm protein Mst84Da. GN MST84DA OR CG17946. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92102953; PubMed=1684716; RA Kuhn R., Kuhn C., Boersch D., Glaetzer K.H., Schaefer U., RA Schaefer M.; RT "A cluster of four genes selectively expressed in the male germ line RT of Drosophila melanogaster."; RL Mech. Dev. 35:143-151(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- DEVELOPMENTAL STAGE: PRIMARY SPERMATOCYTES. CC -!- DOMAIN: THIS PROTEIN IS MOSTLY COMPOSED OF REPETITIVE C-G-P CC MOTIFS. CC -!- SIMILARITY: BELONGS TO THE MST(3)CGP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67703; CAA47937.1; -. DR EMBL; AE003672; AAF54022.1; -. DR PIR; S25772; S25772. DR FlyBase; FBgn0004172; Mst84Da. DR InterPro; IPR005634; MSSP. DR Pfam; PF03940; MSSP; 1. KW Spermatogenesis; Repeat; Multigene family. SQ SEQUENCE 63 AA; 5806 MW; BF84CD74CBCEFD3F CRC64; MYMYVNPNYV LVGGPCCGPC GGCGPCGGCG PCCGGCGPCC GPCGGCGPCC GGTSSFCGCG PCC // ID M84B_DROME STANDARD; PRT; 74 AA. AC Q01643; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Male specific sperm protein Mst84Db. GN MST84DB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92102953; PubMed=1684716; RA Kuhn R., Kuhn C., Boersch D., Glaetzer K.H., Schaefer U., RA Schaefer M.; RT "A cluster of four genes selectively expressed in the male germ line RT of Drosophila melanogaster."; RL Mech. Dev. 35:143-151(1991). CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- DEVELOPMENTAL STAGE: PRIMARY SPERMATOCYTES. CC -!- DOMAIN: THIS PROTEIN IS MOSTLY COMPOSED OF REPETITIVE C-G-P CC MOTIFS. CC -!- SIMILARITY: BELONGS TO THE MST(3)CGP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67703; CAA47938.1; -. DR PIR; S25773; S25773. DR HSSP; P01180; 1NPO. DR FlyBase; FBgn0004173; Mst84Db. DR InterPro; IPR005634; MSSP. DR Pfam; PF03940; MSSP; 1. KW Spermatogenesis; Repeat; Multigene family. SQ SEQUENCE 74 AA; 6824 MW; D0793137A7E7D1D0 CRC64; MCCGPLGFCG PCSPCGGPCG PCGPCGPCGS CCSPCGSCCA PWGPCGPCGP CCGGCGPCGL CGPCCGPCRP YCGC // ID M84C_DROME STANDARD; PRT; 55 AA. AC Q01644; Q9VIA0; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Male specific sperm protein Mst84Dc. GN MST84DC OR CG17945. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92102953; PubMed=1684716; RA Kuhn R., Kuhn C., Boersch D., Glaetzer K.H., Schaefer U., RA Schaefer M.; RT "A cluster of four genes selectively expressed in the male germ line RT of Drosophila melanogaster."; RL Mech. Dev. 35:143-151(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- DEVELOPMENTAL STAGE: PRIMARY SPERMATOCYTES. CC -!- DOMAIN: THIS PROTEIN IS MOSTLY COMPOSED OF REPETITIVE C-G-P CC MOTIFS. CC -!- SIMILARITY: BELONGS TO THE MST(3)CGP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67703; CAA47939.1; -. DR EMBL; AE003672; AAF54025.1; -. DR PIR; S25774; S25774. DR FlyBase; FBgn0004174; Mst84Dc. DR InterPro; IPR005634; MSSP. DR Pfam; PF03940; MSSP; 1. KW Spermatogenesis; Repeat; Multigene family. SQ SEQUENCE 55 AA; 5225 MW; 95A12F3AEC88BD6C CRC64; MCCGPCGSCC GYYCCGPCCG PCGPRCGPCG SCCGPCGPCG PCCGPFGSCC GGCWC // ID M84D_DROME STANDARD; PRT; 68 AA. AC Q01645; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Male specific sperm protein Mst84Dd. GN MST84DD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92102953; PubMed=1684716; RA Kuhn R., Kuhn C., Boersch D., Glaetzer K.H., Schaefer U., RA Schaefer M.; RT "A cluster of four genes selectively expressed in the male germ line RT of Drosophila melanogaster."; RL Mech. Dev. 35:143-151(1991). CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- DEVELOPMENTAL STAGE: PRIMARY SPERMATOCYTES. CC -!- DOMAIN: THIS PROTEIN IS MOSTLY COMPOSED OF REPETITIVE C-G-P CC MOTIFS. CC -!- SIMILARITY: BELONGS TO THE MST(3)CGP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67703; CAA47940.1; -. DR PIR; S25775; S25775. DR FlyBase; FBgn0004175; Mst84Dd. DR InterPro; IPR005634; MSSP. DR Pfam; PF03940; MSSP; 1. KW Spermatogenesis; Repeat; Multigene family. SQ SEQUENCE 68 AA; 6480 MW; 2F2BD26128DE3DEF CRC64; MGCAPGGPCC GPCGPCCGPC CGPCCGPCCG PCGPCCGPCG PRCGPCGPCG PCCGTMEKRN GLQRCCPF // ID M87F_DROME STANDARD; PRT; 56 AA. AC P08175; Q9VFQ6; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Male specific sperm protein Mst87F. GN MST87F OR MST(3)GL-9 OR CG17956. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=88211557; PubMed=2835228; RA Kuhn R., Schaefer U., Schaefer M.; RT "Cis-acting regions sufficient for spermatocyte-specific RT transcriptional and spermatid-specific translational control of the RT Drosophila melanogaster gene mst(3)gl-9."; RL EMBO J. 7:447-454(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- DEVELOPMENTAL STAGE: PRIMARY SPERMATOCYTES. CC -!- DOMAIN: THIS PROTEIN IS MOSTLY COMPOSED OF REPETITIVE C-G-P CC MOTIFS. CC -!- SIMILARITY: BELONGS TO THE MST(3)CGP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00831; CAA68761.1; -. DR EMBL; AE003702; AAF54994.1; -. DR PIR; S00340; WTFF. DR HSSP; P01180; 1NPO. DR FlyBase; FBgn0002862; Mst87F. KW Spermatogenesis; Repeat; Multigene family. SQ SEQUENCE 56 AA; 5233 MW; 830CD13212C34A47 CRC64; MCCGPCGPCC GPCCGPCCGP CGPCGGGCGP CYGPNVCGPC YACGPCGGCY CGYPCC // ID MAD_DROME STANDARD; PRT; 455 AA. AC P42003; Q9VQM3; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mothers against dpp protein. GN MAD OR CG12399. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95286061; PubMed=7768443; RA Sekelsky J.J., Newfeld S.J., Raftery L.A., Chartoff E.H., RA Gelbart W.M.; RT "Genetic characterization and cloning of mothers against dpp, a gene RT required for decapentaplegic function in Drosophila melanogaster."; RL Genetics 139:1347-1358(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE FUNCTION OF DECAPENTAPLEGIC. MAY PLAY CC AN IMPORTANT ROLE IN MEDIATING DPP SIGNALING. CC -!- DEVELOPMENTAL STAGE: IS DETECTED IN ALL DEVELOPMENTAL STAGES, CC THOUGH IT APPEARS MOST ABUNDANT IN PUPAE, ADULT STAGES AND EARLY CC EMBRYOS. ITS ABUNDANCE DECREASES THROUGHOUT EMBRYONIC AND LARVAL CC DEVELOPMENT AND THEN RETURNS TO HIGH LEVELS IN PUPAE AND ADULT CC FEMALES. CC -!- SIMILARITY: BELONGS TO THE DWARFIN/SMAD FAMILY. CC -!- SIMILARITY: CONTAINS 1 DWA/MH1 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 DWB/MH2 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U10328; AAB60230.1; -. DR EMBL; AE003580; AAF51142.1; -. DR PIR; S55019; S55019. DR HSSP; Q15796; 1DEV. DR TRANSFAC; T04378; -. DR FlyBase; FBgn0011648; Mad. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IDA. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0007480; P:leg morphogenesis (sensu Holometabola); IMP. DR GO; GO:0006357; P:regulation of transcription from Pol II pro...; NAS. DR GO; GO:0007179; P:TGFbeta receptor signaling pathway; IGI. DR GO; GO:0008586; P:wing vein morphogenesis; IMP. DR InterPro; IPR001132; Dwarfin. DR InterPro; IPR003619; Dwarfin_A. DR InterPro; IPR008984; SMAD_FHA. DR Pfam; PF03165; MH1; 1. DR Pfam; PF03166; MH2; 1. DR SMART; SM00523; DWA; 1. DR SMART; SM00524; DWB; 1. KW Transcription regulation. FT DOMAIN 39 148 DWA. FT DOMAIN 259 431 DWB. FT MUTAGEN 409 409 G->S: IN ALLELE MAD-10; PUPAL LETHAL. FT MUTAGEN 421 421 S->L: IN ALLELE MAD-9; LETHAL. SQ SEQUENCE 455 AA; 50504 MW; 6C8570674C3AB9D8 CRC64; MDTDDVESNT SSAMSTLGSL FSFTSPAVKK LLGWKQGDEE EKWAEKAVDS LVKKLKKRKG AIEELERALS CPGQPSKCVT IPRSLDGRLQ VSHRKGLPHV IYCRVWRWPD LQSHHELKPL ELCQYPFSAK QKEVCINPYH YKRVESPVLP PVLVPRHSEF APGHSMLQFN HVAEPSMPHN VSYSNSGFNS HSLSTSNTSV GSPSSVNSNP NSPYDSLAGT PPPAYSPSED GNSNNPNDGG QLLDAQMGDV AQVSYSEPAF WASIAYYELN CRVGEVFHCN NNSVIVDGFT NPSNNSDRCC LGQLSNVNRN STIENTRRHI GKGVHLYYVT GEVYAECLSD SAIFVQSRNC NYHHGFHPST VCKIPPGCSL KIFNNQEFAQ LLSQSVNNGF EAVYELTKMC TIRMSFVKGW GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPHNA ISSVS // ID MAL1_DROME STANDARD; PRT; 508 AA. AC P07191; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Possible maltase D precursor (EC 3.2.1.20) (Larval visceral protein DE D). GN LVPD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83216126; PubMed=6854639; RA Snyder M., Davidson N.; RT "Two gene families clustered in a small region of the Drosophila RT genome."; RL J. Mol. Biol. 166:101-118(1983). RN [2] RP POSSIBLE FUNCTION. RX MEDLINE=88289361; PubMed=3135536; RA Henikoff S., Wallace J.C.; RT "Detection of protein similarities using nucleotide sequence RT databases."; RL Nucleic Acids Res. 16:6191-6204(1988). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF TERMINAL, NON-REDUCING 1,4- CC LINKED D-GLUCOSE RESIDUES WITH RELEASE OF D-GLUCOSE. CC -!- DEVELOPMENTAL STAGE: ONE OF THE PROTEINS EXPRESSED BY THE 44D CC CUTICLE GENE CLUSTER. EXPRESSED IN FIRST, SECOND AND EARLY 3RD CC INSTAR LARVAE AND IN ADULTS, BUT NOT IN EMBRYOS OR PUPAE. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00204; CAA23492.1; -. DR PIR; S08597; S08597. DR HSSP; P21332; 1UOK. DR FlyBase; FBgn0002569; LvpD. DR InterPro; IPR006589; Alp_amyl_cat_sub. DR InterPro; IPR006047; Alpha_amyl_cat. DR Pfam; PF00128; alpha-amylase; 1. DR SMART; SM00642; Aamy; 1. KW Hydrolase; Glycosidase; Signal. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 508 POSSIBLE MALTASE D. FT CARBOHYD 30 30 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 124 124 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 198 198 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 312 312 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 508 AA; 57941 MW; C08411DED5A4DCEA CRC64; MPKWAHLGLA ALLLISTTQE GTADIDWWEN ASLYQIYPRS FQDSDGDGIG DLKGITSRLG YLKEIGITAT WLSPIFTSPM SDFGYDISNF YDIDPIFGTL EDFDDLIVEA KSLGVKIILD FVPNHSSDEN VWFEKSVNRE DGYDDFYVWD DGKLNEETGA RDPPSNWVSV FSGPMWTWNE KRQQYFLHQF QVKQPDLNFT NPMVREHMLD VLKFWLDRGV DGFRIDAVPH IYEHRNADGS YPDEPVSGWG SDPNAYDYHD HIYTKDQPAT VDLMYEWREF LDNYRAQNGG DSRVLLAEAY SSVETLSAYF GNSTHQGTQL PMNFQLMYLS GYSTAKDVVG SIDYWMNTMW KEHQTANWVV GNHDTNRVAD RMGAHKVDLL NVIVNALPGA SVTYYGEEIG MSNVDVECTG DSCEDRDGER TPMQWTAGKN ADFSDGESTW LPLSPEYQRY NVQTERGVSR SSLNIFKGLQ ELKSSSAFLA FKEDGGFSYE AVTEQVLQII RYVKQILF // ID MAL2_DROME STANDARD; PRT; 522 AA. AC P07190; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Possible maltase H precursor (EC 3.2.1.20) (Larval visceral protein DE H). GN LVPH. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83216126; PubMed=6854639; RA Snyder M., Davidson N.; RT "Two gene families clustered in a small region of the Drosophila RT genome."; RL J. Mol. Biol. 166:101-118(1983). RN [2] RP POSSIBLE FUNCTION. RX MEDLINE=88289361; PubMed=3135536; RA Henikoff S., Wallace J.C.; RT "Detection of protein similarities using nucleotide sequence RT databases."; RL Nucleic Acids Res. 16:6191-6204(1988). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF TERMINAL, NON-REDUCING 1,4- CC LINKED D-GLUCOSE RESIDUES WITH RELEASE OF D-GLUCOSE. CC -!- DEVELOPMENTAL STAGE: ONE OF THE PROTEINS EXPRESSED BY THE 44D CC CUTICLE GENE CLUSTER. EXPRESSED IN FIRST, SECOND AND EARLY 3RD CC INSTAR LARVAE AND IN ADULTS, BUT NOT IN EMBRYOS OR PUPAE. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00204; CAA23491.1; -. DR PIR; S07253; S07253. DR HSSP; P21332; 1UOK. DR FlyBase; FBgn0002570; LvpH. DR InterPro; IPR006589; Alp_amyl_cat_sub. DR InterPro; IPR006047; Alpha_amyl_cat. DR Pfam; PF00128; alpha-amylase; 1. DR SMART; SM00642; Aamy; 1. KW Hydrolase; Glycosidase; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 522 POSSIBLE MALTASE H. FT CARBOHYD 119 119 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 151 151 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 244 244 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 315 315 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 331 331 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 522 AA; 60638 MW; 1D3683C2F6594F22 CRC64; MRPQSAACLL LAIVGFVGAT EWWESGNYYQ IYPRSFRDSD GDGIGDLNGV TEKLQYLKDI GFTGTWLSPI FKSPMVDFGY DISDFYQIHP EYGTMEDFER MIAKAKEVGI KIILDFVPNH SSTENEWFTK SVDSDPVYKD FYIWHDGKIN NETGEREPPS NWNSEFRYSA WEWNEVRQQY YLHQFAIQQA DLNYRNPAVV NEMKNVIRFW LGKGVSGFRI DAVPYLFEVD LDRYNQYPDE PLTNDSVNCP DPDDHCYTQH IYTQDMPETI DMVYQWRELV DEFHVENGGD KRLLMTEAYT SFENIMTYYG NGVRNGSHIP FNFDFLTSIN NASKAGEYVK HIKKWMDASP EGVYANWVLG NHDNKRVASR FGVQRTDLIN ILLQTLPGHA VTYNGEELGM TDVWISWEDT VDPNACNSDP DNYYARSRDP ARSPYQWDAS SKAGFTSADH TWLPVADDYK TNNALQQLRA PRSHLQIFKK LXRVRKEPSF RQGELNIQAI DDDVIIYSRQ VYQSLRSLSF DY // ID MAL3_DROME STANDARD; PRT; 505 AA. AC P07192; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Possible maltase L precursor (EC 3.2.1.20) (Larval visceral protein DE L). GN LVPL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83216126; PubMed=6854639; RA Snyder M., Davidson N.; RT "Two gene families clustered in a small region of the Drosophila RT genome."; RL J. Mol. Biol. 166:101-118(1983). RN [2] RP POSSIBLE FUNCTION. RX MEDLINE=88289361; PubMed=3135536; RA Henikoff S., Wallace J.C.; RT "Detection of protein similarities using nucleotide sequence RT databases."; RL Nucleic Acids Res. 16:6191-6204(1988). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF TERMINAL, NON-REDUCING 1,4- CC LINKED D-GLUCOSE RESIDUES WITH RELEASE OF D-GLUCOSE. CC -!- DEVELOPMENTAL STAGE: ONE OF THE PROTEINS EXPRESSED BY THE 44D CC CUTICLE GENE CLUSTER. EXPRESSED IN FIRST, SECOND AND EARLY 3RD CC INSTAR LARVAE AND IN ADULTS, BUT NOT IN EMBRYOS OR PUPAE. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00204; CAA23493.1; -. DR PIR; S08598; S08598. DR HSSP; P21332; 1UOK. DR FlyBase; FBgn0002571; LvpL. DR InterPro; IPR006589; Alp_amyl_cat_sub. DR InterPro; IPR006047; Alpha_amyl_cat. DR Pfam; PF00128; alpha-amylase; 1. DR SMART; SM00642; Aamy; 1. KW Hydrolase; Glycosidase; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 505 POSSIBLE MALTASE L. FT CARBOHYD 120 120 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 307 307 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 443 443 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 505 AA; 57565 MW; 116F4FB3CB256178 CRC64; MFKLLVLSCL LALALPSLAE VGWWKTGQFY QIYPRSFKDS DGDGVGDLIG ITQQLPYLKE IGITATWLSP IFTSPMADFG YDVADLKGID PIFGTMEDFE ALLARAKELD IKIILDFVPN HTSDECDWFI RSAAGEEEYK DFYVWPTGKV VNGIRQPPTN WVSVFRGSMW TWNEERQAYY LHQFHAKQPD LNYRNPKVVE AMKDVLRFWL RKGAYGFRID AVPHVYEIPA DADGNWPDEP RNEAVSDPED YTYLQHIYTT DQPETLELVY AFRDVIEEID AELGGDDRVL LTEAYSPLEV LMQYYGNGTH LGSQIPFNFE LLAQISYSSD AYHYSELIHN WLDNMPEGQV ANWVFGNHDQ SRIGSRLGAD RIDACNMIIL GLPGVSVTYQ GEEMGMTDVW ISWEDTVDPQ ACQSNEQEFE RLTRDPVRTP FQWSDEVNAG FSNASVTWLP VASNYKLVNV KKERGIALSH LNVYKQLRAL RDEPTLKQGD VSVTAIGPNV LAFKR // ID MAM_DROME STANDARD; PRT; 1596 AA. AC P21519; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 01-MAR-1992 (Rel. 21, Last annotation update) DE Neurogenic protein mastermind. GN MAM. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=91065516; PubMed=1701150; RA Smoller D., Friedel C., Schmid A., Bettler D., Lam L., RA Yedvobnick B.; RT "The Drosophila neurogenic locus mastermind encodes a nuclear protein RT unusually rich in amino acid homopolymers."; RL Genes Dev. 4:1688-1700(1990). CC -!- FUNCTION: MAY HAVE A REGULATORY FUNCTION POSSIBLY IN ASSOCIATION CC WITH THE N GENE PRODUCT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: DURING EARLY NEUROGENESIS MAM PRODUCTS ARE CC UBIQUITOUSLY LOCATED. DURING LATER STAGES THEY ACCUMULATE IN THE CC CENTRAL NERVOUS SYSTEM. CC -!- MISCELLANEOUS: THE PROTEIN HAS MANY AA HOMOPOLYMERIC DOMAINS: 21 CC POLY-GLN RUNS (FROM 5 TO 16 AA IN LENGTH), 4 POLY-GLY (6 TO 10 CC AA), 3 POLY-ASN (3 X 5 AA), 1 POLY-ALA (10 AA) AND 1 POLY-THR (5 CC AA) RUNS. CC -!- SIMILARITY: TO OTHER NUCLEAR PROTEINS OF DROSOPHILA, TO CERTAIN CC YEAST AND MAMMALIAN REGULATORY PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54251; CAA38152.1; -. DR PIR; A36391; A33106. DR FlyBase; FBgn0002643; mam. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007500; P:mesoderm cell fate determination; IMP. DR GO; GO:0007399; P:neurogenesis; NAS. KW Neurogenesis; Nuclear protein; Repeat. FT DOMAIN 20 84 GLN-RICH. FT DOMAIN 127 190 ARG/LYS-RICH (BASIC). FT DOMAIN 196 219 GLN-RICH. FT DOMAIN 259 304 ASN-RICH. FT DOMAIN 355 388 GLY/ASN-RICH. FT DOMAIN 392 406 GLN-RICH. FT DOMAIN 407 440 GLY-RICH. FT DOMAIN 651 671 GLN-RICH. FT DOMAIN 700 714 GLN-RICH. FT DOMAIN 759 816 GLN-RICH. FT DOMAIN 987 996 5 X 2 AA TANDEM REPEATS OF G-V. FT DOMAIN 1060 1079 ALA-RICH. FT DOMAIN 1092 1107 8 X 2 AA TANDEM REPEATS OF V-G. FT DOMAIN 1237 1252 7 X 2 AA TANDEM REPEATS OF G-V. FT DOMAIN 1492 1496 POLY-THR. FT DOMAIN 1559 1592 ASP/GLU-RICH (ACIDIC). SQ SEQUENCE 1596 AA; 167717 MW; B944D86EF359D605 CRC64; MDAGGLPVFQ SASQAAAVAQ QQQQQQQQQH LNLQLHQQHL GLHLQQQQQL QLQQQQHNAQ AQQQQIQVQQ QQQQQQQQQQ QQQQHSPYNA NLGATGGIAG ITGGNGAGGP TNPGAVPTAP GDTMPTKRMP VVDRLRRRME NYRRRQTDCV PRYEQAFNTV CEQQNQETTV LQKRFLESKN KRAAKKTDKK LPDPSQQHQQ QQHQQQQQHQ QHQQHQQAQT MLAGQLQSSV HVQQKFLKRP AEDVDNGPDS FEPPHKLPNN NNNSNSNNNN GNANANNGGN GSNTGNNTNN NGNSTNNNGG SNNNGSENLT KFSVEIVQQL EFTTSPANSQ PQQISTNVTV KALTNTSVKS EPGVGGGGGG GGGGNSGNNN NNGGGGGGGN GNNNNNGGDH HQQQQQHQHQ QQQQQQGGGL GGLGNNGRGG GPGGMATGPG GVAGGLGGMG MPPNMMSAQQ KSALGNLANL VECKREPDHD FPDLGSLDKD GGGGQFPGFP DLLGDDNSEN NDTFKDLINN LQDFNPSFLD GFDEKPLLDI KTEDGIKVEP PNAQDLINSL NVKSEGGLGH GFGGFGLGLD NPGMKMRGGN PGNQGGFPNG PNGGTGGAPN AGGNGGNSGN LMSEHPLAAQ TLKQMAEQHQ HKNAMGGMGG FPRPPHGMNP QQQQQQQQQQ QQQQAQQQHG QMMGQGQPGR YNDYGGGFPN DFGLGPNGPQ QQQQQAQQQQ PQQQHLPPQF HQQKGPGPGA GMNVQQNFLD IKQELFYSSQ NDFDLKRLQQ QQAMQQQQQQ QHHQQQQPKM GGVPNFNKQQ QQQQVPQQQL QQQQQQQQQQ QQQQQQYSPF SNQNPNAAAN FLNCPPRGGP NGNQQPGNLA QQQQQPGAGP QQQQQRGNAG NGQQNNPNTG PGGNTPNAPQ QQQQQQSTTT TLQMKQTQQL HISQQGGGAQ GIQVSAGQHL HLSGDMKSNV SVAAQQGVFF SQQQAQQQQQ QQQPGGTNGP NPQQQQQQPH GGNAGGGVGV GVGVGVGNGG PNPGQQQQQP NQNMSNANVP SDGFSLSQSQ SMNFNQQQQQ QAAAQQQQVQ PNMRQRQTQA QAAAAAAAAA AQAQAAANAS GPNVPLMQQP QVGVGVGVGV GVGVGVGNGG VVGGPGSGGP NNGAMNQMGG PMGGMPGMQM GGPMNPMQMN PNAAGPTAQQ MMMGSGAGGP GQVPGPGQGP NPNQAKFLQQ QQMMRAQAMQ QQQQHMSGAR PPPPEYNATK AQLMQAQMMQ QTVGGGGVGV GGVGVGVGVG GVGGANGGRF PNSAAQAAAM RRMTQQPIPP SGPMMRPQHA MYMQQHGGAG GGPRTGMGVP YGGGRGGPMG GPQQQQRPPN VQVTPDGMPM GSQQEWRHMM MTQQQTQMGF GGPGPGGPMR QGPGGFNGGN FMPNGAPNGA AGSGPNAGGM MTGPNVPQMQ LTPAQMQQQL MRQQQQQQQQ QQQQHMGPGA ANNMQMQQLL QQQQSGGGGN MMASQMQMTS MHMTQTQQQI TMQQQQQFVQ STTTTTHQQQ QMMQMGPGGG GGGGGPGSAN NNNGGGGGGA AGGGNSASTI ASASSISQTI NSVVANSNDF GLEFLDNLPV DSNFSTQDLI NSLDNDNFNL QDFNMP // ID MAN2_DROME STANDARD; PRT; 1108 AA. AC Q24451; Q9TYG5; Q9VHD8; Q9VHD9; DT 15-JUL-1998 (Rel. 36, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-mannosidase II (EC 3.2.1.114) (Mannosyl-oligosaccharide DE 1,3-1,6-alpha-mannosidase) (MAN II) (Golgi alpha-mannosidase II) DE (AMAN II). GN ALPHA-MAN-II OR GMII OR CG18474/CG18802/CG8139. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95196999; PubMed=7890162; RA Foster J.M., Yudkin B., Lockyer A.E., Roberts D.B.; RT "Cloning and sequence analysis of GmII, a Drosophila melanogaster RT homologue of the cDNA encoding murine Golgi alpha-mannosidase II."; RL Gene 154:183-186(1995). RN [2] RP SEQUENCE FROM N.A., ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND RP INDUCTION. RX MEDLINE=99436189; PubMed=10504337; RA Rabouille C., Kuntz D.A., Lockyer A.E., Watson R., Signorelli T., RA Rose D.R., van den Heuvel M., Roberts D.B.; RT "The Drosophila GMII gene encodes a Golgi alpha-mannosidase II."; RL J. Cell Sci. 112:3319-3330(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CATALYZES THE FIRST COMMITTED STEP IN THE BIOSYNTHESIS CC OF COMPLEX N-GLYCANS. IT CONTROLS CONVERSION OF HIGH MANNOSE TO CC COMPLEX N-GLYCANS; THE FINAL HYDROLYTIC STEP IN THE N-GLYCAN CC MATURATION PATHWAY (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE TERMINAL 1,3- AND 1,6-LINKED CC ALPHA-D-MANNOSE RESIDUES IN THE MANNOSYL-OLIGOSACCHARIDE CC MAN(5)(GLCNAC)(3). CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBUNIT: HOMODIMER; DISULFIDE-LINKED (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI. CC -!- INDUCTION: INHIBITED BY SWAINSONINE AND BY COPPER SULFATE. CC -!- SIMILARITY: BELONGS TO FAMILY 38 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X77652; CAA54732.1; -. DR EMBL; AJ132715; CAA10755.1; -. DR EMBL; AE003682; AAF54375.1; -. DR EMBL; AY119464; AAM50118.1; -. DR PDB; 1HTY; 02-JAN-02. DR PDB; 1HWW; 10-JAN-02. DR PDB; 1HXK; 16-JAN-02. DR FlyBase; FBgn0011740; alpha-Man-II. DR GO; GO:0005783; C:endoplasmic reticulum; NAS. DR GO; GO:0005795; C:Golgi stack; NAS. DR InterPro; IPR000602; Glyco_hydro_38. DR Pfam; PF01074; Glyco_hydro_38; 1. KW Hydrolase; Glycosidase; Transmembrane; Signal-anchor; Golgi stack; KW 3D-structure. FT DOMAIN 1 9 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 10 30 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 31 1108 LUMENAL (POTENTIAL). FT CONFLICT 71 71 E -> K (IN REF. 1). FT CONFLICT 305 306 QL -> HV (IN REF. 2). FT CONFLICT 397 397 L -> V (IN REF. 2). FT CONFLICT 970 970 E -> K (IN REF. 1). SQ SEQUENCE 1108 AA; 126720 MW; 55E370EC8CAC6D4A CRC64; MLRIRRRFAL VICSGCLLVF LSLYIILNFA APAATQIKPN YENIENKLHE LENGLQEHGE EMRNLRARLA ETSNRDDPIR PPLKVARSPR PGQCQDVVQD VPNVDVQMLE LYDRMSFKDI DGGVWKQGWN IKYDPLKYNA HHKLKVFVVP HSHNDPGWIQ TFEEYYQHDT KHILSNALRH LHDNPEMKFI WAEISYFARF YHDLGENKKL QMKSIVKNGQ LEFVTGGWVM PDEANSHWRN VLLQLTEGQT WLKQFMNVTP TASWAIDPFG HSPTMPYILQ KSGFKNMLIQ RTHYSVKKEL AQQRQLEFLW RQIWDNKGDT ALFTHMMPFY SYDIPHTCGP DPKVCCQFDF KRMGSFGLSC PWKVPPRTIS DQNVAARSDL LVDQWKKKAE LYRTNVLLIP LGDDFRFKQN TEWDVQRVNY ERLFEHINSQ AHFNVQAQFG TLQEYFDAVH QAERAGQAEF PTLSGDFFTY ADRSDNYWSG YYTSRPYHKR MDRVLMHYVR AAEMLSAWHS WDGMARIEER LEQARRELSL FQHHDGITGT AKTHVVVDYE QRMQEALKAC QMVMQQSVYR LLTKPSIYSP DFSFSYFTLD DSRWPGSGVE DSRTTIILGE DILPSKHVVM HNTLPHWREQ LVDFYVSSPF VSVTDLANNP VEAQVSPVWS WHHDTLTKTI HPQGSTTKYR IIFKARVPPM GLATYVLTIS DSKPEHTSYA SNLLLRKNPT SLPLGQYPED VKFGDPREIS LRVGNGPTLA FSEQGLLKSI QLTQDSPHVP VHFKFLKYGV RSHGDRSGAY LFLPNGPASP VELGQPVVLV TKGKLESSVS VGLPSVVHQT IMRGGAPEIR NLVDIGSLDN TEIVMRLETH IDSGDIFYTD LNGLQFIKRR RLDKLPLQAN YYPIPSGMFI EDANTRLTLL TGQPLGGSSL ASGELEIMQD RRLASDDERG LGQGVLDNKP VLHIYRLVLE KVNNCVRPSE LHPAGYLTSA AHKASQSLLD PLDKFIFAEN EWIGAQGQFG GDHPSAREDL DVSVMRRLTK SSAKTQRVGY VLHRTNLMQC GTPEEHTQKL DVCHLLPNVA RCERTTLTFL QNLEHLDGMV APEVCPMETA AYVSSHSS // ID MAPX_DROME STANDARD; PRT; 1185 AA. AC P23226; Q9V9S1; DT 01-NOV-1991 (Rel. 20, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 205 kDa microtubule-associated protein. GN MAP205 OR CG1483. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91115949; PubMed=1703540; RA Irminger-Finger I., Laymon R.A., Goldstein L.S.B.; RT "Analysis of the primary sequence and microtubule-binding region of RT the Drosophila 205K MAP."; RL J. Cell Biol. 111:2563-2572(1990). RN [2] RP SEQUENCE FROM N.A. (ISOFORM B3). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY PLAY AN IMPORTANT ROLE IN THE REGULATION OF CC MICROTUBULE ASSEMBLY AND INTERACTION. CC -!- SUBCELLULAR LOCATION: ASSOCIATED WITH CYTOPLASMIC MICROTUBULES AND CC WITH THE MITOTIC SPINDLE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=J5; CC IsoId=P23226-1; Sequence=Displayed; CC Name=C2; CC IsoId=P23226-2; Sequence=VSP_004319, VSP_004320, VSP_004321; CC Name=B3; CC IsoId=P23226-3; Sequence=VSP_004319; CC -!- MISCELLANEOUS: PHOSPHORYLATION OF VARIOUS SERINE RESIDUES MAY PLAY CC A REGULATORY ROLE. THE BASIC DOMAIN CONTAINS NUMEROUS SEQUENCES CC THAT MATCH KNOWN CONSENSUS SEQUENCES OF SEVERAL DIFFERENT PROTEIN CC KINASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54061; CAA37996.1; -. DR EMBL; AE003780; AAF57214.1; -. DR PIR; A36685; A36685. DR FlyBase; FBgn0002645; Map205. DR GO; GO:0005875; C:microtubule associated complex; IDA. KW Microtubule; Alternative splicing; Phosphorylation. FT DOMAIN 1 784 ASP/GLU-RICH (ACIDIC). FT DOMAIN 785 1124 ARG/LYS-RICH (BASIC). FT DOMAIN 1125 1185 ASP/GLU-RICH (ACIDIC). FT BINDING 745 977 MICROTUBULES (POTENTIAL). FT VARSPLIC 557 578 Missing (in isoform B3 and isoform C2). FT /FTId=VSP_004319. FT VARSPLIC 650 703 Missing (in isoform C2). FT /FTId=VSP_004320. FT VARSPLIC 704 704 D -> N (in isoform C2). FT /FTId=VSP_004321. SQ SEQUENCE 1185 AA; 126669 MW; 47B422E2CEE03F70 CRC64; MEHHEDNAQL DNYLQNRLAE SLQICGGAGE HNPHLADATG GNGCAPGIAP SKSDEVDGEE DEEWKYIHEV RQSEKLQQEK LPLTKETGNG FGPGRDSDNQ VHGNGAAAVF NLYEEDVEVI KNDGDFSTNS NTTTSTDEVV ARQAQEPNQL PEQLQQQQQI ESQGVHEDPR QEDEDEHSSV ATTYGTSSLS ENNSSPLDQE EVVMVAQTVG QEQLVDFDNK ENSYFVKNLE ENHSQLNPNA VAFVPGVGSQ SSSPLPAAED PLPGVQPRPF LPGGTLDDLV AESPRKEFAR INMDGIAVPD EREFDIEADM RPHELEQESD TFGAGHLEMQ LLNGIGTADQ AALRDVLDHG PETSVDMELP LDQVPNDADI MKQSIYAEHN SSIEDILNSV QPLPIQTCDD KELIHVEEKE HVSKSPSTEE LQFQSDFPNN QESHTLFNNT EQDPMQASFY LEHTSQKAQE GCQEQMQLPA ECSDIFADQS LLLDTSAPQL SSEADSPVAK LELESQQAGI VDITPSPLSS TAEKHLVEDT KELVEEYTLD PESHFFGVVS SQAPLQLFGK HTLPSIIHSC KHRVASEQND EENAVFESVS GYETQNFDEI SSPPEGINPF AQPFTPAHLV IEQANTMMED VGGMPIPASE DFAICDKVAS KSSNEVEDHR SEQQAFVKEE LLHPVGDVVA QVENLGTEKN FVVEEERLPI SVSDEIPLSS ASKEKLLPDT TDEQLLTSAL EEKLRSVAPE ESVSTAADGQ SISQFDEYVI ASNKPLEDIL EPEKDVEVAK SLSEKTSVAT VAGGAVVGAT KTHSATKAGS TAASAKSKTE TLVMKKTTAS STSVYGANKS AAPRPSTARL GIKSTSIATK TSTTSSLTGN PRKSLSSNVG STVKPPTKLS GTRPATAPVS KVTLGAKTIT NKPTASGTAS DNVTRTTLRP LVSTNARRPA TSGTGSVASS TARRPVTNAK GSAPGSAAST KVRPAATMTA PVKPKVLSPR STISSTTTVR KVPSTSTPSF STRSPNKQQS NGLGKNTSST TTSTATATIT KSFTARSAPK FTHSASLTYN NGSTSRRLLV PGSSSTTTTS SLRKSSPLKA APGKAASKPL TPQSKDGTAK SSPAVLKARN STLMGGEGVA PSNECVPTPN GQINAEEVVK LKGKGLAEEV KIIEEQKLHE QDVPAHNAEV PLLDF // ID MBL_DROME STANDARD; PRT; 297 AA. AC O16011; O16009; O16010; Q9V803; Q9V804; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mindmelt protein (Muscleblind protein). GN MM OR MBL OR CG14477/CG10941. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND ALTERNATIVE RP SPLICING. RC TISSUE=Imaginal disks; RX MEDLINE=98043867; PubMed=9334280; RA Begemann G., Paricio N., Artero R., Kiss I., Perez-Alonso M., RA Mlodzik M.; RT "Muscleblind, a gene required for photoreceptor differentiation in RT Drosophila, encodes novel nuclear Cys3His-type zinc-finger-containing RT proteins."; RL Development 124:4321-4331(1997). RN [2] RP SEQUENCE OF 64-297 FROM N.A. (ISOFORM C). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: REQUIRED FOR TERMINAL DIFFERENTIATION OF PHOTORECEPTOR CC CELLS. VITAL FOR EMBRYONIC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=B; CC IsoId=O16011-1; Sequence=Displayed; CC Name=A; CC IsoId=O16011-2; Sequence=VSP_006425, VSP_006426; CC Name=C; CC IsoId=O16011-3; Sequence=VSP_006427, VSP_006428; CC -!- TISSUE SPECIFICITY: EXPRESSED IN EMBRYONIC MUSCLE CELLS. CC -!- SIMILARITY: CONTAINS 2 C3H1-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF001625; AAC47757.1; -. DR EMBL; AF001626; AAC47758.1; -. DR EMBL; AF001536; AAC01949.1; -. DR EMBL; AE003803; AAF57880.2; -. DR FlyBase; FBgn0053197; mm. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003676; F:nucleic acid binding; NAS. DR GO; GO:0009790; P:embryonic development; IMP. DR GO; GO:0007517; P:muscle development; IMP. DR GO; GO:0007467; P:photoreceptor differentiation (sensu Drosop...; IMP. DR InterPro; IPR000571; Znf_CCCH. DR Pfam; PF00642; zf-CCCH; 1. DR SMART; SM00356; ZnF_C3H1; 2. KW Developmental protein; Metal-binding; Zinc-finger; Repeat; KW Nuclear protein; Vision; Alternative splicing. FT ZN_FING 18 45 C3H1-TYPE 1. FT ZN_FING 52 79 C3H1-TYPE 2. FT DOMAIN 210 240 ALA-RICH. FT VARSPLIC 180 203 TSPLAAHHHQQQQQLQHQLNNINN -> VSFGLMPTTIYIS FT RYMFMYPMKSI (in isoform A). FT /FTId=VSP_006425. FT VARSPLIC 204 297 Missing (in isoform A). FT /FTId=VSP_006426. FT VARSPLIC 180 243 TSPLAAHHHQQQQQLQHQLNNINNNNNHSTAGAAATSTTAT FT TTTNNAAAAAAAAAAAAAAAVMG -> MDVKTVGSFYYDNF FT QFSGMVPFKRPAAEKSGIPVYQPGATAYQQLMQPYVPVSFT FT GHPPGVPRF (in isoform C). FT /FTId=VSP_006427. FT VARSPLIC 244 297 Missing (in isoform C). FT /FTId=VSP_006428. FT CONFLICT 189 189 MISSING (IN REF. 1; AAC47758). FT CONFLICT 247 297 LEVGKKRAADTTDMFPLVFFCSFPSPCVFAFLNCSIFGFLR FT LWFSLFNLRH -> GSGQEAGGGHDRHVSTGIFLFFSFTMC FT FCVFELFHIWILAFMVFFIQFTTLVCYPHSFEILTEFAFFV FT ACF (IN REF. 1; AAC47758). SQ SEQUENCE 297 AA; 32330 MW; 37D430C798D91185 CRC64; MANVVNMNSL LNGKDSRWLQ LEVCREFQRN KCSRQDTECK FAHPPANVEV QNGKVTACYD SIKGRCNRDK PPCKYFHPPQ HLKDQLLING RNHLALKNAL MQQMGIAPGQ PVISGQVPAV ATNPYLTGIP ANSYSPYYTT GHLVPALLGP DPVTSQLGPV VPQTVQVAQQ KIPRSDRLET SPLAAHHHQQ QQQLQHQLNN INNNNNHSTA GAAATSTTAT TTTNNAAAAA AAAAAAAAAA VMGHHTLEVG KKRAADTTDM FPLVFFCSFP SPCVFAFLNC SIFGFLRLWF SLFNLRH // ID MBN_DROME STANDARD; PRT; 796 AA. AC P52302; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Lethal(3)malignant blood neoplasm-1 protein (Mbn(83)). GN L(3)MBN OR L(3)MBN-1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94229362; PubMed=8174791; RA Konrad L., Becker G., Schmidt A., Kloeckner T., RA Kaufer-Stillger G., Dreschers S., Edstroem J.-E., Gateff E.; RT "Cloning, structure, cellular localization, and possible function of RT the tumor suppressor gene lethal(3)malignant blood neoplasm-1 of RT Drosophila melanogaster."; RL Dev. Biol. 163:98-111(1994). CC -!- FUNCTION: REQUIRED FOR DIFFERENTIATION OF THE PHAGOCYTIC BLOOD- CC CELL TYPE, THE PLASMATOCYTE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC; MAINLY AROUND THE NUCLEUS. CC -!- TISSUE SPECIFICITY: BLOOD CELLS AND OTHER TISSUES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z47722; CAA87654.1; -. DR PIR; S57844; S57844. DR FlyBase; FBgn0002440; l(3)mbn. DR InterPro; IPR000618; Insect_cuticle. DR Pfam; PF00379; Chitin_bind_4; 1. KW Repeat. FT DOMAIN 225 314 2 X 37 AA REPEATS. FT REPEAT 225 261 1-1. FT REPEAT 278 314 1-2. FT DOMAIN 471 512 2 X 21 AA REPEATS. FT REPEAT 471 491 2-1. FT REPEAT 492 512 2-2. FT DOMAIN 576 711 7 X APPROXIMATE TANDEM REPEATS, FT GLY-SER-RICH. FT REPEAT 576 598 3-1. FT REPEAT 599 618 3-2. FT REPEAT 619 640 3-3. FT REPEAT 641 658 3-4. FT REPEAT 659 676 3-5. FT REPEAT 677 694 3-6. FT REPEAT 695 711 3-7. SQ SEQUENCE 796 AA; 83348 MW; 6B1D593961FFF370 CRC64; MHFTRTQSTN KSIRTKNTQE LLYKKYRGCK LLSSRGVMRS GQCYQLCDPT WAKYTTCRRQ RFARTLGQQA AAGSRPPLMF YNVYLILLTL SIRCRTSWGV FILRRLLRAD NLAPKIDGVC LCSAAPVTLT HVLSAATTVR PYKFGFTIDE QQHRAEKRDE RGIIMGQFGF ITADGIYQVT VYPTDEEGKF RIISMKSYPY AGPVGSKSVP VTTTPKVLLH AAPVALPKYN FNSEACSGCF LKKSPPKTEI RTLSQPLAPV QCSCDNDSKG PASCSSGALP KYNFNSEACS GCFLKKSPPK TEIRTLSQPL APVQPGKPDG SSDIGLNVQL PFRESIAQTV ASRLGLLQDT LQASNTNTNA PNTKTIELGL NLAMSTYYTT KNAVTGHVSR QTSNSQTPSA NTKIDYNVGV VEKASPPVYR PLNIRLNEDV MRQAITYGNT IPGHVPLPNQ PLVETSLLPA SQVKIFALDG NAKVPLASNI QSVAQHPNAG LNAKVPLASN IQSVAQHPNA GLKNINRSGV SSAKTLANTK TRPPHTFNPH QTPLLSSATA PGISGVTANT PTGNAPSNGG GIAAGKAPGN PQAGGSGGII GAGAPGGRKV SAGGIGSGSA IGGVSGGSKA SGNGGAIGSG SAIGGGATGS KASGFGFGSN IGGGVSGSKP SGFGSESKIG GADSGSKASG FGSGSKIGGG ITGTKASGLG GEIGSGRGSA SSATGDLYKF KYILDYNGHE ETGGRNGDKQ GSYFAIGEDA VQRTIEYIAN EFGFQPHVSW RKLDAKEALP EENSLKHYEF KWFNQE // ID MCM2_DROME STANDARD; PRT; 887 AA. AC P49735; Q9VHU2; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA replication licensing factor MCM2. GN MCM2 OR CG7538. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye-antennal disk; RX MEDLINE=95347580; PubMed=7622035; RA Treisman J.E., Follette P.J., O'Farrell P.H., Rubin G.M.; RT "Cell proliferation and DNA replication defects in a Drosophila MCM2 RT mutant."; RL Genes Dev. 9:1709-1715(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTS AS A FACTOR THAT ALLOWS THE DNA TO UNDERGO A CC SINGLE ROUND OF REPLICATION PER CELL CYCLE. REQUIRED FOR DNA CC REPLICATION AND CELL PROLIFERATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE MCM FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L42762; AAB36617.1; -. DR EMBL; AE003678; AAF54207.1; -. DR FlyBase; FBgn0014861; Mcm2. DR InterPro; IPR001208; MCM. DR InterPro; IPR008045; MCM_2. DR Pfam; PF00493; MCM; 1. DR PRINTS; PR01657; MCMFAMILY. DR PRINTS; PR01658; MCMPROTEIN2. DR ProDom; PD001041; MCM; 1. DR SMART; SM00350; MCM; 1. DR PROSITE; PS00847; MCM_1; 1. DR PROSITE; PS50051; MCM_2; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW DNA replication; Zinc-finger; ATP-binding; Cell cycle. FT ZN_FING 314 340 C4-TYPE (POTENTIAL). FT DOMAIN 458 665 MCM. FT NP_BIND 508 515 ATP (POTENTIAL). SQ SEQUENCE 887 AA; 100414 MW; 26A7092109F09CBE CRC64; MDNPSSPPPN TPSDAAERRD LRAAMTSPVG DFEPFENEDE ILGDQTVRDE AEEEDGEELF GDNMENDYRP MPELDHYDPA LLDDEDDFSE MSQGDRFAAE SEMRRRDRAA GIHRDDRDLG FGQSDDEDDV GPRAKRRAGE KAAVGEVEDT EMVESIENLE DTKGHSTKEW VSMLGPRTEI ANRFQSFLRT FVDERGAYTY RDRIRRMCEQ NMSSFVVSYT DLANKEHVLA YFLPEAPFQM LEIFDKVAKD MVLSIFPTYE RVTTEIHVRI SELPLIEELR TFRKLHLNQL VRTLGVVTAT TGVLPQLSVI KYDCVKCGYV LGPFVQSQNT EIKPGSCPEC QSTGPFSINM EQTLYRNYQK ITLQESPGRI PAGRIPRSKD VILLADLCDQ CKPGDELEVT GIYTNNYDGS LNTDQGFPVF ATVIIANHVV VKDSKQVVQS LTDEDIATIQ KLSKDPRIVE RVVASMAPSI YGHDYIKRAL ALALFGGESK NPGEKHKVRG DINLLICGDP GTAKSQFLKY TEKVAPRAVF TTGQGASAVG LTAYVRRNPV SREWTLEAGA LVLADQGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG IVTSLQARCT VIAAANPIGG RYDPSMTFSE NVNLSEPILS RFDVLCVVKD EFDPMQDQQL AKFVVHSHMK HHPSEEEQPE LEEPQLKTVD EIPQDLLRQY IVYAKENIRP KLTNIDEDKI AKMYAQLRQE SFATGSLPIT VRHIESVIRM SEAHARMHLR ENVMEADVSM AIRMMLESFI EAQKFSVMKK MRSTFQKYLS FQKDHSELLF FILRQLTLDQ LAYIRCKDGP GATHVEIMER DLIERAKQLD IVNLKPFYES DLFRTNGFSY DPKRRIILQI VVDGNTA // ID MCM4_DROME STANDARD; PRT; 866 AA. AC Q26454; Q9V4M5; DT 01-NOV-1997 (Rel. 35, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA replication licensing factor MCM4 (Disc proliferation abnormal DE protein). GN DPA OR CG1616. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96080174; PubMed=7489728; RA Feger G., Vaessin H., Su T.T., Wolff E., Jan L.Y., Jan Y.N.; RT "dpa, a member of the MCM family, is required for mitotic DNA RT replication but not endoreplication in Drosophila."; RL EMBO J. 14:5387-5398(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ESSENTIAL ROLE IN MITOTIC DNA REPLICATION BUT NOT IN CC ENDOREPLICATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE MCM FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S80255; AAB35644.1; -. DR EMBL; AE003841; AAF59242.1; -. DR PIR; S59872; S59872. DR FlyBase; FBgn0015929; dpa. DR GO; GO:0006260; P:DNA replication; IMP. DR GO; GO:0007052; P:mitotic spindle assembly; IMP. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR001208; MCM. DR InterPro; IPR008047; MCM_4. DR Pfam; PF00493; MCM; 1. DR PRINTS; PR01657; MCMFAMILY. DR PRINTS; PR01660; MCMPROTEIN4. DR ProDom; PD001041; MCM; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00350; MCM; 1. DR PROSITE; PS00847; MCM_1; 1. DR PROSITE; PS50051; MCM_2; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW DNA replication; ATP-binding. FT DOMAIN 460 669 MCM. FT NP_BIND 512 519 ATP (POTENTIAL). FT CONFLICT 435 435 D -> E (IN REF. 1). SQ SEQUENCE 866 AA; 96610 MW; CF6ED69D2ADDA04E CRC64; MSSPARSPSV GGATPKQGAR TPTRGIASQD VETPMRMGPG RAVRPSDNIS LPPTSPGNIS LPATSPARGL GANMSEIDLS SPLNYGTPSS MGSIRTPRSG IRGTPLRARP DIRTDKRIRQ VAIGGGSGLE PIPEKGSETT DPVSESSQAP QLVVWGTNVV VSQCKSKFKS FIMRFIDPSA EQDEISENID VNQPLYLQKL EEIHTLEEPY LNLNCAHLKT FDQDLYRQLI CYPQEVIPGF DMAINEMFFE RYPAALLEHQ IQVRPFNADK TRNMRSLNPE DMDQLISISG MVIRSSNVIP EMREAFFSCN ICSFSTTVEV DRGRINQPTL CTNCNTNHCF RLIHNRSEFT DKQLVKLQES PDDMAAGQTP HNVLLYAHND LVDKVQPGDR VTVTGIYRAT PLKTGGLSSS VKSVYKTHVD VVHFRKVDNK RLYEDEEGKD HIFPPERVEL LQLLAKKPDI YDRLARAIAP SIYENDDIKK GILLQLFGGT KKKHATLGRQ NFRSEIHLLL CGDPGTSKSQ MLQYVFNLVP RSQYTSGRGS SAVGLTAYVT KDPETRQLVL QTGALVLADN GVCCIDEFDK MNDSTRSVLH EVMEQQTLSI AKAGIICQLN ARTSILAAAN PAESQWNKRK NIIDNVQLPH TLLSRFDLIF LVLDPQDEIF DKRLASHLVS LYYVTRHEEE DTMFDMSVLR DYIAYAREHL SPTLSDEAQQ RLIQAYVDMR KVGAGRGQIS AYPRQLESLI RLSEAHAKVR LSNQVELLDV EEAWRLHREA LKQSATDPLS GKIDVGILTT GLSTAARKKR ADLVAAIKEN LKKKGKVLTV PYQKLFSDIK EGSQIMITRE QFEDALKEVQ DEGAIVVMGK NTIRIC // ID MDR4_DROME STANDARD; PRT; 1302 AA. AC Q00449; Q9V6I6; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Multidrug resistance protein homolog 49 (P-glycoprotein 49). GN MDR49 OR CG3879. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=91304385; PubMed=2072901; RA Wu C.-T., Budding M., Griffin M.S., Croop J.M.; RT "Isolation and characterization of Drosophila multidrug resistance RT gene homologs."; RL Mol. Cell. Biol. 11:3940-3948(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59076; AAA28679.1; -. DR EMBL; AE003820; AAF58437.2; -. DR EMBL; AY058791; AAL14020.1; -. DR PIR; A41249; A41249. DR FlyBase; FBgn0004512; Mdr49. DR GO; GO:0005887; C:integral to plasma membrane; NAS. DR GO; GO:0015239; F:multidrug transporter activity; NAS. DR GO; GO:0006855; P:multidrug transport; NAS. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR001140; ABC_TM_transpt. DR InterPro; IPR003439; ABC_transporter. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR ProDom; PD000006; ABC_transporter; 2. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. KW ATP-binding; Glycoprotein; Transmembrane; Transport; Repeat; KW Multigene family. FT DOMAIN 1 46 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 47 67 POTENTIAL. FT TRANSMEM 117 145 POTENTIAL. FT TRANSMEM 193 213 POTENTIAL. FT TRANSMEM 221 240 POTENTIAL. FT TRANSMEM 301 322 POTENTIAL. FT TRANSMEM 340 360 POTENTIAL. FT DOMAIN 361 734 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 735 756 POTENTIAL. FT TRANSMEM 780 801 POTENTIAL. FT TRANSMEM 856 876 POTENTIAL. FT TRANSMEM 878 897 POTENTIAL. FT TRANSMEM 960 980 POTENTIAL. FT TRANSMEM 997 1017 POTENTIAL. FT DOMAIN 1018 1302 CYTOPLASMIC (POTENTIAL). FT NP_BIND 437 444 ATP (POTENTIAL). FT NP_BIND 1094 1101 ATP (POTENTIAL). FT REPEAT 1 670 FT REPEAT 671 1302 FT CARBOHYD 101 101 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 697 697 S -> N. FT VARIANT 712 712 D -> N. FT VARIANT 952 952 V -> I. SQ SEQUENCE 1302 AA; 142724 MW; 4720C169455C28CD CRC64; MVKKEESRLP QAGDFQLKEG SVVDATRKYS YFDLFRYSTR CERFLLVVSL LVATAASAFI PYFMIIYGEF TSLLVDRTVG VGTSSPAFAL PMFGGGQQLT NASKEENNQA IIDDATAFGI GSLVGSVAMF LLITLAIDLA NRIALNQIDR IRKLFLEAML RQDIAWYDTS SGSNFASKMT EDLDKLKEGI GEKIVIVVFL IMTFVIGIVS AFVYGWKLTL VVLSCVPFII AATSVVARLQ GSLAEKELKS YSDAANVVEE VFSGIRTVFA FSGQEKEKER FGKLLIPAEN TGRKKGLYSG MGNALSWLII YLCMALAIWY GVTLILDERD LPDRVYTPAV LVIVLFAVIM GAQNLGFASP HVEAIAVATA AGQTLFNIID RPSQVDPMDE KGNRPENTAG HIRFEGIRFR YPARPDVEIL KGLTVDVLPG QTVAFVGASG CGKSTLIQLM QRFYDPEAGS VKLDGRDLRT LNVGWLRSQI GVVGQEPVLF ATTIGENIRY GRPSATQADI EKAARAANCH DFITRLPKGY DTQVGEKGAQ ISGGQKQRIA IARALVRQPQ VLLLDEATSA LDPTSEKRVQ SALELASQGP TTLVVAHRLS TITNADKIVF LKDGVVAEQG THEELMERRG LYCELVSITQ RKEATEADEG AVAGRPLQKS QNLSDEETDD DEEDEEEDEE PELQTSGSSR DSGFRASTRR KRRSQRRKKK KDKEVVSKVS FTQLMKLNSP EWRFIVVGGI ASVMHGATFP LWGLFFGDFF GILSDGDDDV VRAEVLKISM IFVGIGLMAG LGNMLQTYMF TTAGVKMTTR LRKRAFGTII GQDIAYFDDE RNSVGALCSR LASDCSNVQG ATGARVGTML QAVATLVVGM VVGFVFSWQQ TLLTLVTLPL VCLSVYLEGR FIMKSAQKAK ASIEEASQVA VEAITNIRTV NGLCLERQVL DQYVQQIDRV DVACRRKVRF RGLVFALGQA APFLAYGISM YYGGILVAEE RMNYEDIIKV AEALIFGSWM LGQALAYAPN VNDAILSAGR LMDLFKRTST QPNPPQSPYN TVEKSEGDIV YENVGFEYPT RKGTPILQGL NLTIKKSTTV ALVGPSGSGK STCVQLLLRY YDPVSGSVNL SGVPSTEFPL DTLRSKLGLV SQEPVLFDRT IAENIAYGNN FRDDVSMQEI IEAAKKSNIH NFISALPQGY DTRLGKTSQL SGGQKQRIAI ARALVRNPKI LILDEATSAL DLESEKVVQQ ALDEARSGRT CLTIAHRLTT VRNADLICVL KRGVVVEHGT HDELMALNKI YANLYLMQQV SG // ID MDR5_DROME STANDARD; PRT; 1302 AA. AC Q00748; Q9VRW3; DT 01-APR-1993 (Rel. 25, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Multidrug resistance protein homolog 65 (P-glycoprotein 65). GN MDR65 OR CG10181. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=91304385; PubMed=2072901; RA Wu C.-T., Budding M., Griffin M.S., Croop J.M.; RT "Isolation and characterization of Drosophila multidrug resistance RT gene homologs."; RL Mol. Cell. Biol. 11:3940-3948(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=WSIII27, and WSIII25; RX MEDLINE=20467314; PubMed=11012721; RA Begun D.J., Whitley P.; RT "Genetics of alpha-amanitin resistance in a natural population of RT Drosophila melanogaster."; RL Heredity 85:184-190(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59077; AAA28680.1; -. DR EMBL; AF251287; AAF69147.1; -. DR EMBL; AF251286; AAF69146.1; -. DR EMBL; AE003563; AAF50669.1; -. DR PIR; B41249; B41249. DR FlyBase; FBgn0004513; Mdr65. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR001140; ABC_TM_transpt. DR InterPro; IPR003439; ABC_transporter. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR ProDom; PD000006; ABC_transporter; 2. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. KW ATP-binding; Glycoprotein; Transmembrane; Transport; Repeat; KW Multigene family. FT DOMAIN 1 48 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 49 69 1 (POTENTIAL). FT DOMAIN 70 118 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 119 147 2 (POTENTIAL). FT DOMAIN 148 194 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 195 215 3 (POTENTIAL). FT DOMAIN 216 223 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 224 242 4 (POTENTIAL). FT DOMAIN 243 302 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 303 323 5 (POTENTIAL). FT DOMAIN 324 341 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 342 362 6 (POTENTIAL). FT DOMAIN 363 731 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 732 753 7 (POTENTIAL). FT DOMAIN 754 776 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 777 798 8 (POTENTIAL). FT DOMAIN 799 852 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 853 873 9 (POTENTIAL). FT DOMAIN 874 874 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 875 894 10 (POTENTIAL). FT DOMAIN 895 956 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 957 977 11 (POTENTIAL). FT DOMAIN 978 993 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 994 1014 12 (POTENTIAL). FT DOMAIN 1015 1302 CYTOPLASMIC (POTENTIAL). FT NP_BIND 440 447 ATP (POTENTIAL). FT NP_BIND 1094 1101 ATP (POTENTIAL). FT REPEAT 1 673 1. FT REPEAT 674 1302 2. FT CARBOHYD 103 103 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 369 369 T -> S (IN REF. 1). FT CONFLICT 678 678 F -> L (IN REF. 1). SQ SEQUENCE 1302 AA; 143784 MW; 39A7BCABFA31924A CRC64; MERDEVSTSS SEGKSQEEAP MAEGLEPTEP IAFLKLFRFS TYGEIGWLFF GFIMCCIKAL TLPAVVIIYS EFTSMLVDRA MQFGTSSNVH ALPLFGGGKT LTNASREENN EALYDDSISY GILLTIASVV MFISGIFSVD VFNMVALRQV TRMRIKLFSS VIRQDIGWHD LASKQNFTQS MVDDVEKIRD GISEKVGHFV YLVVGFIITV AISFSYGWKL TLAVSSYIPL VILLNYYVAK FQGKLTAREQ ESYAGAGNLA EEILSSIRTV VSFGGEKSEV QRYENFLVPA RKASQWKGAF SGLSDAVLKS MLYLSCAGAF WYGVNLIIDD RNVENKEYTP AILMIAFFGI IVGADNIART APFLESFATA RGCATNLFKV IDLTSKIDPL STDGKLLNYG LRGDVEFQDV FFRYPSRPEV IVHRGLNIRI RAGQTVALVG SSGCGKSTCV QLLQRFYDPV FGSVLLDDLD IRKYNIQWLR SNIAVVGQEP VLFLGTIAQN ISYGKPGATQ KEIEAAATQA GAHEFITNLP ESYRSMIGER GSQLSGGQKQ RIAIARALIQ NPKILLLDEA TSALDYQSEK QVQQALDLAS KGRTTIVVSH RLSAIRGADK IVFIHDGKVL EEGSHDDLMA LEGAYYNMVR AGDINMPDEV EKEDSIEDTK QKSLALFEKS FETSPLNFEK GQKNSVQFEE PIIKALIKDT NAQSAEAPPE KPNFFRTFSR ILQLAKQEWC YLILGTISAV AVGFLYPAFA VIFGEFYAAL AEKDPEDALR RTAVLSWACL GLAFLTGLVC FLQTYLFNYA GIWLTTRMRA MTFNAMVNQE VGWFDDENNS VGALSARLSG EAVDIQGAIG YPLSGMIQAL SNFISSVSVA MYYNWKLALL CLANCPIIVG SVILEAKMMS NAVVREKQVI EEACRIATES ITNIRTVAGL RREADVIREY TEEIQRVEVL IRQKLRWRGV LNSTMQASAF FAYAVALCYG GVLVSEGQLP FQDIIKVSET LLYGSMMLAQ SLAFTPAFSA ALIAGHRLFQ ILDRKPKIQS PMGTIKNTLA KQLNLFEGVR YRGIQFRYPT RPDAKILNGL DLEVLKGQTV ALVGHSGCGK STCVQLLQRY YDPDEGTIHI DHDDIQHDLT LDGVRTKLGI VSQEPTLFER SIAENIAYGD NRRSVSMVEI IAAAKSANAH SFIISLPNGY DTRMGARGTQ LSGGQKQRIA IARALVRNPK ILLLDEATSA LDLQSEQLVQ QALDTACSGR TCIVIAHRLS TVQNADVICV IQNGQVVEQG NHMQLISQGG IYAKLHKTQK DH // ID ME31_DROME STANDARD; PRT; 458 AA. AC P23128; Q9VL17; DT 01-NOV-1991 (Rel. 20, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative ATP-dependent RNA helicase me31b. GN ME31B OR CG4916. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91172763; PubMed=1900936; RA de Valoir T., Tucker M.A., Belikoff E.J., Camp L.A., Bolduc C., RA Beckingham K.; RT "A second maternally expressed Drosophila gene encodes a putative RNA RT helicase of the 'DEAD box' family."; RL Proc. Natl. Acad. Sci. U.S.A. 88:2113-2117(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: UNWINDS RNA IN AN ATP-DEPENDENT FASHION (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: MATERNALLY EXPRESSED (DURING OOGENESIS). CC FUNCTION DURING EARLY EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. CC DDX6/ME31B SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59926; AAA28603.1; ALT_INIT. DR EMBL; AE003628; AAF52881.1; -. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0004419; me31B. DR GO; GO:0004004; F:ATP dependent RNA helicase activity; NAS. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. KW Helicase; ATP-binding; RNA-binding. FT NP_BIND 101 108 ATP (BY SIMILARITY). FT SITE 206 209 DEAD BOX. FT CONFLICT 38 44 KLPPKDN -> NCRQRTT (IN REF. 1). SQ SEQUENCE 458 AA; 51814 MW; 4CA15289432DE9FD CRC64; MTEKLNSGHT NLTSKGIIND LQIAGNTSDD MGWKSKLKLP PKDNRFKTTD VTDTRGNEFE EFCLKRELLM GIFEKGWERP SPIQEAAIPI ALSGKDVLAR AKNGTGKTGA YCIPVLEQID PTKDYIQALV MVPTRELALQ TSQICIELAK HLDIRVMVTT GGTILKDDIL RIYQKVQLII ATPGRILDLM DKKVADMSHC RILVLDEADK LLSLDFQGML DHVILKLPKD PQILLFSATF PLTVKNFMEK HLREPYEINL MEELTLKGVT QYYAFVQERQ KVHCLNTLFS KLQINQSIIF CNSTQRVELL AKKITELGYC CYYIHAKMAQ AHRNRVFHDF RQGLCRNLVC SDLFTRGIDV QAVNVVINFD FPRMAETYLH RIGRSGRFGH LGIAINLITY EDRFDLHRIE KELGTEIKPI PKVIDPALYV ANVGASVGDT CNNSDLNNSA NEEGNVSK // ID MEF2_DROME STANDARD; PRT; 539 AA. AC P40791; Q24394; Q95R70; Q9U5I8; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Myocyte-specific enhancer factor 2 (MADS domain transcription factor DE D-mef2). GN MEF2 OR CG1429. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS C AND D). RC TISSUE=Embryo; RX MEDLINE=94261646; PubMed=8202544; RA Lilly B., Galewsky S., Firulli A.B., Schulz R.A., Olson E.N.; RT "D-MEF2: a MADS box transcription factor expressed in differentiating RT mesoderm and muscle cell lineages during Drosophila embryogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5662-5666(1994). RN [2] RP SEQUENCE FROM N.A. (ISOFORM C). RC TISSUE=Embryo; RX MEDLINE=94329547; PubMed=8052612; RA Nguyen H.T., Bodmer R., Abmayr S.M., McDermott J.C., Spoerel N.A.; RT "D-mef2: a Drosophila mesoderm-specific MADS box-containing gene with RT a biphasic expression profile during embryogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7520-7524(1994). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS A; C AND D), AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=95329426; PubMed=7605749; RA Taylor M.V., Beatty K.E., Hunter H.K., Baylies M.K.; RT "Drosophila MEF2 is regulated by twist and is expressed in both the RT primordia and differentiated cells of the embryonic somatic, visceral RT and heart musculature."; RL Mech. Dev. 50:29-41(1995). RN [4] RP SEQUENCE FROM N.A. (ISOFORM C). RX MEDLINE=95141075; PubMed=7839146; RA Lilly B., Zhao B., Ranganayakulu G., Paterson B.M., Schulz R.A., RA Olson E.N.; RT "Requirement of MADS domain transcription factor D-MEF2 for muscle RT formation in Drosophila."; RL Science 267:688-693(1995). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [7] RP SEQUENCE FROM N.A. (ISOFORM E). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: TRANSCRIPTION FACTOR THAT COULD BE A KEY PLAYER IN EARLY CC MESODERM DIFFERENTIATION AND MAY BE REQUIRED FOR SUBSEQUENT CELL CC FATE SPECIFICATIONS WITHIN THE SOMATIC AND VISCERAL/HEART CC MESODERMAL LAYERS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=D; Synonyms=1; CC IsoId=P40791-1; Sequence=Displayed; CC Name=A; Synonyms=3; CC IsoId=P40791-2; Sequence=VSP_006237, VSP_006238; CC Name=B; CC IsoId=P40791-3; Sequence=VSP_006237, VSP_006239; CC Name=C; Synonyms=2; CC IsoId=P40791-4; Sequence=VSP_006239; CC Name=E; CC IsoId=P40791-5; Sequence=VSP_006235, VSP_006236; CC -!- DEVELOPMENTAL STAGE: FIRST DETECTABLE IN THE PRESUMPTIVE MESODERM CC AT LATE CELLULAR BLASTODERM STAGE. EXPRESSED IN ALL PRESUMPTIVE CC MESODERM PRIOR TO THE SPLITTING PROCESS THAT GENERATES THE SOMATIC CC AND VISCERAL/ HEART MESODERM. AFTER THE SUBDIVISION, IT IS FOUND CC IN BOTH THE SOMATIC AND THE VISCERAL/HEART MESODERM. CC -!- INDUCTION: TWI ACTIVITY IS REQUIRED FOR MEF2 EXPRESSION. SNA CC ACTIVITY IS NEEDED FOR MAINTAINING MEF2 EXPRESSION. CC -!- SIMILARITY: BELONGS TO THE MEF2 FAMILY. CC -!- SIMILARITY: CONTAINS 1 MADS-BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03292; AAA19957.1; -. DR EMBL; U07422; AAA20463.1; -. DR EMBL; X83527; CAA58508.1; -. DR EMBL; U19493; AAF06817.1; -. DR EMBL; AE003831; AAF58872.1; -. DR EMBL; AE003831; AAM71042.1; -. DR EMBL; AE003831; AAM71043.1; -. DR EMBL; AE003831; AAM71044.1; -. DR EMBL; AE003831; AAM71045.1; -. DR EMBL; AY061589; AAL29137.1; -. DR HSSP; P11831; 1SRS. DR TRANSFAC; T01772; -. DR FlyBase; FBgn0011656; Mef2. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007498; P:mesoderm development; IMP. DR InterPro; IPR002100; TF_MADSbox. DR Pfam; PF00319; SRF-TF; 1. DR PRINTS; PR00404; MADSDOMAIN. DR SMART; SM00432; MADS; 1. DR PROSITE; PS00350; MADS_BOX_1; 1. DR PROSITE; PS50066; MADS_BOX_2; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW Developmental protein; Differentiation; Activator; KW Alternative splicing. FT DOMAIN 3 57 MADS-box. FT DNA_BIND 58 86 MEF2-TYPE (POTENTIAL). FT DOMAIN 380 386 POLY-SER. FT DOMAIN 390 396 POLY-GLY. FT DOMAIN 419 428 POLY-GLY. FT DOMAIN 377 431 GLY-RICH. FT DOMAIN 508 513 POLY-GLN. FT DOMAIN 516 519 POLY-GLN. FT VARSPLIC 193 193 I -> S (in isoform E). FT /FTId=VSP_006235. FT VARSPLIC 194 539 Missing (in isoform E). FT /FTId=VSP_006236. FT VARSPLIC 187 193 GGMSLII -> V (in isoform A and isoform FT B). FT /FTId=VSP_006237. FT VARSPLIC 468 490 HDKYEGYPYRALMGHNPRWNLNF -> DFIILN (in FT isoform A). FT /FTId=VSP_006238. FT VARSPLIC 468 491 Missing (in isoform B and isoform C). FT /FTId=VSP_006239. FT CONFLICT 97 97 D -> E (IN REF. 4). FT CONFLICT 101 101 A -> G (IN REF. 4). FT CONFLICT 112 114 EAK -> GGM (IN REF. 4). FT CONFLICT 338 338 S -> R (IN REF. 2). FT CONFLICT 364 377 ASGHQQNSNGSTGS -> PAVISRIAMVPRAG (IN REF. FT 1 AND 4). FT CONFLICT 429 429 S -> T (IN REF. 4). FT CONFLICT 467 467 P -> PG (IN REF. 5; AAM71044). SQ SEQUENCE 539 AA; 57115 MW; 252879CA0741A40B CRC64; MGRKKIQISR ITDERNRQVT FNKRKFGVMK KAYELSVLCD CEIALIIFSS SNKLYQYAST DMDRVLLKYT EYNEPHESLT NKNIIEKENK NGVMSPDSPE AETDYTLTPR TEAKYNKIDE EFQNMMQRNQ MAIGGAGAPR QLPNSSYTLP VSVPVPGSYG DNLLQASPQM SHTNISPRPS SSETDSGGMS LIIYPSGSML EMSNGYPHSH SPLVGSPSPG PSPGIAHHLS IKQQSPGSQN GRASNLRVVI PPTIAPIPPN MSAPDDVGYA DQRQSQTSLN TPVVTLQTPI PALTSYSFGA QDFSSSGVMN SADIMSLNTW HQGLVPHSSL SHLAVSNSTP PPATSPVSIK VKAEPQSPPR DLSASGHQQN SNGSTGSGGS SSSTSSNASG GAGGGGAVSA ANVITHLNNV SVLAGGPSGQ GGGGGGGGSN GNVEQATNLS VLSHAQQHHL GMPNSRPSST GHITPTPHDK YEGYPYRALM GHNPRWNLNF AGAPSSDQDV RLAAVAVQQQ QQQPHQQQQL GDYDAPNHKR PRISGGWGT // ID MEI9_DROME STANDARD; PRT; 926 AA. AC Q24087; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mei-9 protein (Meiotic-9 protein). GN MEI-9. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96109608; PubMed=8647398; RA Sekelsky J.J., McKim K.S., Chin G.M., Hawley R.S.; RT "The Drosophila meiotic recombination gene mei-9 encodes a homologue RT of the yeast excision repair protein Rad1."; RL Genetics 141:619-627(1995). CC -!- FUNCTION: IMPLICATED IN RECOMBINATION EVENTS DURING MEIOSIS, CC MOSTLY IN MEIOTIC EXCHANGE. MAY DIRECTLY RESOLVE HOLLIDAY CC JUNCTIONS WITHIN RECOMBINATION INTERMEDIATES LEADING TO DNA CC EXCHANGE. ALSO REQUIRED FOR THE REPAIR OF MISMATCHES WITHIN CC MEIOTIC HETERODUPLEX DNA AND FOR NUCLEOTIDE EXCISION REPAIR. CC -!- SUBUNIT: HETERODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE XPF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U27181; AAC46917.1; -. DR PIR; S58936; S58936. DR FlyBase; FBgn0002707; mei-9. DR GO; GO:0007059; P:chromosome segregation; IMP. DR GO; GO:0007131; P:meiotic recombination; IMP. DR GO; GO:0006298; P:mismatch repair; IMP. DR GO; GO:0006289; P:nucleotide-excision repair; IMP. DR InterPro; IPR006166; ERCC4. DR InterPro; IPR006167; Rad_1. DR Pfam; PF02732; ERCC4; 1. DR TIGRFAMs; TIGR00596; rad1; 1. KW Meiosis; DNA repair; DNA-binding; Nuclear protein; Hydrolase; KW Nuclease; Endonuclease. SQ SEQUENCE 926 AA; 105685 MW; 342C2C91BB3AFD91 CRC64; MVLLDYEKQM FLDLVEADGL LVCAKGLSYD RVVISILKAY SDSGNLVLVI NSSDWEEQYY KSKIEPKYVH EGASTATERE RVYLEGGLQF ISTRILVVDL LKQRIPIELI SGIIVLRAHT IIESCQEAFA LRLFRQKNKT GFVKAFSSSP EAFTIGYSHV ERTMRNLFVK HLYIWPRFHE SVRTVLQPWK IQSIEMHVPI SQNITSIQSH ILEIMNFLVQ EIKRINRTVD MEAVTVENCV TKTFHKILQA QLDCIWHQLN SQTKLIVADL KILRTLMIST MYHDAVSAYA FMKRYRSTEY ALSNSGWTLL DAAEQIFKLS RQRVFNGQQE FEPEPCPKWQ TLTDLLTKEI PGDMRRSRRS EQQPKVLILC QDARTCHQLK QYLTQGGPRF LLQQALQHEV PVGKLSDNYA KESQTRSAPP KNVSSNKELR REEVSGSQPP LAGMDELAQL LSESETEGQH FEESYMLTMT QPVEVGPAAI DIKPDPDVSI FETIPELEQF DVTAALASVP HQPYICLQTF KTEREGSMAL EHMLEQLQPH YVVMYNMNVT PIRQLEVFEA RRRLPPADRM KVYFLIHART VEEQAYLTSL RREKAAFEFI IDTKSKMVIP KYQDGKTDEA FLLLKTYDDE PTDENAKSRQ AGGQAPQATK ETPKVIVDMR EFRSDLPCLI HKRGLEVLPL TITIGDYILT PDICVERKSI SDLIGSLNSG RLYNQCVQMQ RHYAKPILLI EFDQNKPFHL QGKFMLSQQT SMANRDIVQK LQLLTLHFPK LRLIWSPSPY ATAQLFEELK LGKPEPDPQT AAALGSDEPM AGEQLHFNSG IYDFLLRLPG VHTRNIHGLL RKGGSLRQLL LRSQKELEEL LQSQESAKLL YDILHVAHLP EKDEVTGSTA LLAASKQFGA GSHNRFRMAA RIAKGSPMML SSKDGP // ID MEIS_DROME STANDARD; PRT; 401 AA. AC Q24141; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Meiotic protein mei-S332. GN MEI-S332 OR CG5303. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Testis; RX MEDLINE=96028099; PubMed=7585942; RA Kerrebrock A.W., Moore D.P., Wu J.S., Orr-Weaver T.L.; RT "Mei-S332, a Drosophila protein required for sister-chromatid RT cohesion, can localize to meiotic centromere regions."; RL Cell 83:247-256(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED TO MAINTAIN SISTER-CHROMATID COHESION DURING CC MEIOSIS IN BOTH MALES AND FEMALES. RELEASE OF THE PROTEIN IS CC REQUIRED FOR SISTER-CHROMATID SEPARATION DURING ANAPHASE II OF CC MEIOSIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR; CENTROMERE REGION OF MEIOTIC CC CHROMOSOMES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36583; AAA87038.1; -. DR EMBL; AE003456; AAF46802.1; -. DR EMBL; AY058633; AAL13862.1; -. DR PIR; A57226; A57226. DR GermOnline; 210188; -. DR FlyBase; FBgn0002715; mei-S332. DR GO; GO:0007062; P:sister chromatid cohesion; IMP. KW Meiosis; Nuclear protein; Centromere; Cell cycle; Coiled coil. FT DOMAIN 3 49 COILED COIL (POTENTIAL). SQ SEQUENCE 401 AA; 44401 MW; 76D3EA53577B315F CRC64; MGSKVEQQYK LLNAELMDQV QKQRLEIGEY RKRVISLERE IMDIREEHVL QNHRQRMENI SIVRSLMLSL NVDSDSLAVR QEPAPAAQIN RPSGPRRSSR EICKDMRRTC ALARTTRPIS PRRSSSVTST VSSTSRRSSA EVQSEVVTTR IPEDRRANKP TPPPRRPAEL VFDEDDSDDD FDEAVSPVEE TQTEQNEENN RLFSIIEENG SEGESTDSSS SCEAIYCDTT FESSPPNAQV TVTPSGRALR EVDTNIPVAV SLSRGKETGK GSWLAISVAV EDSPQEPSIQ CPRLAVTRPS QSSGIFPDVN GLTPRRSLFN GIGKMAGSTS TPKSFLVEEM PSIRTRSRTA ANKKSENTDM SSSFCNNSAR PSRSCRPTSL VEPSLKNKLR NGSKGKAKAK K // ID MERH_DROME STANDARD; PRT; 635 AA. AC Q24564; Q24054; Q8SWY3; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Moesin/ezrin/radixin homolog 2 (Ezrin-moesin-radixin-2) (Merlin DE protein) (dMerlin). GN MER OR EMR2 OR CG14228. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=96234672; PubMed=8666669; RA McCartney B.M., Fehon R.G.; RT "Distinct cellular and subcellular patterns of expression imply RT distinct functions for the Drosophila homologues of moesin and the RT neurofibromatosis 2 tumor suppressor, merlin."; RL J. Cell Biol. 133:843-852(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 218-307 FROM N.A. RA Winge P., Fleming J.T., Gobel V.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY HAVE A ROLE IN REGULATION OF CELLULAR GROWTH AND CC SIGNALING, POSSIBLY BY HAVING A ROLE IN ENDOCYTIC PROCESSES. CC -!- SUBUNIT: INTERACTS WITH MOE AND ARM AT THE ADHERENS JUNCTION. CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED; ADHERENS JUNCTIONS AND CC ENDOCYTIC COMPARTMENTS. CYTOPLASMIC; PUNCTATE. CC -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN THE GERM LINE. CC EXPRESSED IN THE DEVELOPING OOCYTE FROM STAGE 6 TO THE END OF CC OOGENESIS AND IN THE APICAL ENDS OF FOLLICAL CELLS FROM STAGE 10. CC UBIQUITOUS EXPRESSION THROUGHOUT EMBRYOGENESIS WITH ENHANCED CC EXPRESSION IN MESODERM OF EARLY EMBRYOS AND MIDGUT OF LATE CC EMBRYOS. IN EMBRYONIC CNS, EXPRESSION IS SEEN IN NEUROPIL AND CC DEVELOPING BRAIN AND IS ENHANCED IN NEURONAL CELL BODIES. IN CC EMBRYONIC PNS, EXPRESSION IS SEEN WITHIN THE CELL BODY. IN THIRD CC INSTAR LARVAE, EXPRESSION IS UNIFORM IN THE EYE IMAGINAL DISK AND CC IS ENHANCED AT THE MORPHOGENETIC FURROW. IN PUPAL EYES, EXPRESSION CC IS SEEN IN THE CYTOPLASM OF SECONDARY AND TERTIARY PIGMENT CELLS, CC BRISTLE PRECURSOR CELLS AND RHABDOMERES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MATERNALLY AND ZYGOTICALLY IN CC EMBRYOS. CC -!- SIMILARITY: CONTAINS 1 FERM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U49724; AAB08449.1; -. DR EMBL; AE003512; AAF49005.1; -. DR EMBL; AY094998; AAM11326.1; -. DR EMBL; U23799; AAA65060.1; -. DR FlyBase; FBgn0013951; Mer. DR GO; GO:0005912; C:adherens junction; IDA. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0009798; P:axis specification; IMP. DR GO; GO:0007267; P:cell-cell signaling; IEP. DR GO; GO:0006897; P:endocytosis; IEP. DR GO; GO:0001558; P:regulation of cell growth; IEP. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR008954; Moesin. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF00769; ERM; 1. DR PRINTS; PR00935; BAND41. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; FALSE_NEG. DR PROSITE; PS50057; FERM_3; 1. KW Endocytosis; Membrane. FT DOMAIN 12 305 FERM. FT CONFLICT 166 166 G -> R (IN REF. 3). SQ SEQUENCE 635 AA; 74492 MW; 940D6B8A0D160A3F CRC64; MSPFGSKKNR SLSVRVSTFD SELEFKLEPR ASGQDLFDLV CRTIGLRESW YFGLQYVDTR SNVSWLKMEK RVRDQRVELH ASNNVYVFSF YAKFFPENVS EELIQEITQH LFFLQVKQSI LSMDIYCRPE ASVLLASYAV HVQYGPYDYE TYKDGMLAGG ELLPKGVTDQ YQMTPEMWEE RIKTWYMDHE PMTRDEVEME YLKIAQDLDM YGVNYFPITN KNKTKLWLGV TSVGLNIYDE RDKLTPKTTF QWNEIRHVSF DDKKFTIRLV DAKVSNFIFY SQDLHINKMI LDLCKGNHDL YMRRRKPDTM EIQQMKAQAK EEKQRRQIER KKFIREKKLR EKAEHERYEL EKSMEHLQNE MRMANDALRR SEETKELYFE KSRVNEEQMQ LTECKANHFK TEMDRLRERQ MKIEREKHDL EKKIRDADFY VHQLTVENDK REAETEKLRK ELICAKMAER EATARLLEFL NSGRKSSTDS LLTASSVSHA ANTASSMAAI STPSLITSSS TNDLETAGGA ELTTHSSHYL VQGDNSSGIS DDFEPKEFIL TDNEMEQITN EMERNHLDYL RNSKQVQSQL QTLRSEIAPH KIEENQSNLD ILSEAQIKAG ENKYSTLKKL KSGSTKARVA FFEEL // ID MES4_DROME STANDARD; PRT; 1427 AA. AC Q8MT36; Q9VAY5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Potential histone methyltransferase Mes-4 (Maternal-effect sterile 4). GN MES-4 OR CG4976. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: POTENTIAL HISTONE METHYLTRANSFERASE. HISTONE METHYLATION CC GIVES SPECIFIC TAGS FOR EPIGENETIC TRANSCRIPTIONAL ACTIVATION OR CC REPRESSION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: CONTAINS 3 PHD-TYPE ZINC FINGERS. CC -!- SIMILARITY: CONTAINS 1 POST-SET DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PWWP DOMAINS. CC -!- SIMILARITY: CONTAINS 1 SET DOMAIN. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 348. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003763; AAF56762.2; -. DR EMBL; AY118404; AAM48433.1; ALT_FRAME. DR FlyBase; FBgn0039559; Mes-4. DR GO; GO:0000228; C:nuclear chromosome; ISS. DR GO; GO:0042054; F:histone methyltransferase activity; ISS. DR GO; GO:0016458; P:gene silencing; ISS. DR GO; GO:0018992; P:germ-line sex determination; ISS. DR InterPro; IPR006560; AWS. DR InterPro; IPR003616; PostSET. DR InterPro; IPR000313; PWWP_domain. DR InterPro; IPR001214; SET. DR InterPro; IPR001965; Znf_PHD. DR Pfam; PF00628; PHD; 1. DR Pfam; PF00855; PWWP; 1. DR Pfam; PF00856; SET; 1. DR SMART; SM00570; AWS; 1. DR SMART; SM00249; PHD; 3. DR SMART; SM00293; PWWP; 2. DR SMART; SM00317; SET; 1. DR PROSITE; PS50868; POST_SET; 1. DR PROSITE; PS50812; PWWP; 2. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. KW Nuclear protein; Zinc-finger; Metal-binding; Repeat. FT DOMAIN 395 468 PWWP 1. FT ZN_FING 777 862 PHD-TYPE 1. FT ZN_FING 864 932 PHD-TYPE 2. FT ZN_FING 999 1044 PHD-TYPE 3. FT DOMAIN 1049 1111 PWWP 2. FT DOMAIN 1233 1355 SET. FT DOMAIN 1359 1375 POST-SET. FT DOMAIN 95 100 POLY-GLN. FT DOMAIN 174 181 POLY-GLY. SQ SEQUENCE 1427 AA; 159027 MW; FB6EFD62E814BEF3 CRC64; MKLSTDAHSE IEGDAAHGNV LCNSASDSLT ATDEVAAGND ESVATEGDDV EIPRDTNNST PVRLLDKPGQ NPVQNGAQPA AEESELESQR QTPVQKQQQQ RVSMVNRKRD LINLQSALSP KYIGYANANS PTPLSDSDDT IRTTRRRVNQ AAALNNSSAG ETLAHDNASP RTPGGGGGGG GDDSANQLLS KTYMSPIEKL LIKNGASSPN STGFEAGSED LGIRPIVRKH VKRKMKRVPK AKVTLELDEK NQQEVDEKSV KTEPIDEEVD RTDEAPTQEA QTTAISIKSE TEAEHKAAVD VHIKQEDTIR LDIVNNPVES TSIVITEEPK DLEKSTEELA FALPLASSTE VDLKSPPDLS STALATSIKS PSSVSIDSAK GLSIVTDPGW PTYQVGDLFW GKVFSYCFWP CMVCPDPLGQ IVGNMPSHPQ RSSLDNANVP IQVHVRFFAD NGRRNWIKPE NLLTFAGLKA FDDMREELRI KHGPKSAKYR QMVPKRTKVV IWRQAIEEAQ AMTQIPYSDR LEKFYQTYEN VVTLNRQKRK RTKYMMQDTS DVGSSLYDST DNLHNKQGTQ LLAVKRERSE SPFSPAFSPV KSKNEKRAKR RKLSNGTEAD TGSNSMAVTP SQTETTVDSS AYENPEFRQL LSAVMEYVMM NRSDEKVEKV LLSVVSNIWS LKQIQLRELE RDLASGEIEE PLGSSVVGRG SGVGTIKRLS NRLMTMMVRR SMTPVVTPST TPAPSEPDRR LSEPPKTKKP VNRPIEEVIE DILQLDSKYL FRGLSREPIC KYCYQAGSDL VRCSRTCSSW LHADCLERKV TGAPMPKIGS RKALVIPPTS KSPSPDEDHV TADAKEVVAV GTSLVCHECN VGEPEGCVIC HQVESPAVPS TPRKEDSSSH TPIEDKLLTC SQPMCGKRFH TSCCKYWPQA SSSKHSARCP RHVCHTCVSD DPSGKFQQLG SSKLAKCVRC PATYHQLSKC IPAGTQMLNT TNIICPRHNI AKADAHVNVL WCYICVKGGE LVCCETCPIA VHAHCRNIPI KTNESYICEE CESGRLPLYG EIVWAKFNNF RWWPAIILPP TEVPSNILKK AHGENDFVVR FFGTHDHGWI SRRRVYLYIE GDTGDGHKTK SQLFRNYTTG VEEASRFLPI IKARRQEQDM ERQSGNKLHP PPYVKIKTNK AVPPLRFSQN LEDLSTCNCL PVDEHPCGPE AGCLNRMLFN ECNPEYCKAG SLCENRMFEQ RKSPRLEVVY MNERGFGLVN REPIAVGDFV IEYVGEVINH AEFQRRMEQK QRDRDENYYF LGVEKDFIID AGPKGNLARF MNHSCEPNCE TQKWTVNCIH RVGIFAIKDI PVNSELTFNY LWDDLMNNSK KACFCGAKRC SGEIGGKLKD DAVKAHAKLK QMRRAKASAV RIHVKPKKTP KVKHISADDE PMDAKDE // ID METK_DROME STANDARD; PRT; 408 AA. AC P40320; Q9VPJ2; Q9VPJ3; Q9VPJ4; Q9VPJ5; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE S-adenosylmethionine synthetase (EC 2.5.1.6) (Methionine DE adenosyltransferase) (AdoMet synthetase). GN M(2)21AB OR SAMS OR CG2674. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Canton-S; RX MEDLINE=94200395; PubMed=8150093; RA Larsson J., Rasmuson-Lestander A.; RT "Molecular cloning of the S-adenosylmethionine synthetase gene in RT Drosophila melanogaster."; RL FEBS Lett. 342:329-333(1994). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2; 3 AND 4). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.P., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CATALYZES THE FORMATION OF S-ADENOSYLMETHIONINE FROM CC METHIONINE AND ATP. CC -!- CATALYTIC ACTIVITY: ATP + L-METHIONINE + H(2)O = PHOSPHATE + CC DIPHOSPHATE + S-ADENOSYL-L-METHIONINE. CC -!- COFACTOR: BINDS 2 DIVALENT IONS, SUCH AS MAGNESIUM OR COBALT, AND CC 1 POTASSIUM ION PER SUBUNIT (BY SIMILARITY). CC -!- PATHWAY: ACTIVATED METHYL CYCLE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=2; Synonyms=A, D; CC IsoId=P40320-1; Sequence=Displayed; CC Name=1; Synonyms=B; CC IsoId=P40320-2; Sequence=VSP_005963, VSP_005964, VSP_005965; CC Name=3; Synonyms=B, C; CC IsoId=P40320-3; Sequence=VSP_005963; CC Name=4; Synonyms=G; CC IsoId=P40320-4; Sequence=VSP_005961, VSP_005962, VSP_005963; CC -!- SIMILARITY: BELONGS TO THE ADOMET SYNTHETASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X77392; CAA54567.1; -. DR EMBL; AE003590; AAF51554.1; -. DR EMBL; AE003590; AAF51556.1; -. DR EMBL; AE003590; AAF51557.1; -. DR EMBL; AE003590; AAF51558.1; -. DR EMBL; AY051918; AAK93342.1; -. DR PIR; S43258; S41917. DR HSSP; P04384; 1MXB. DR FlyBase; FBgn0005278; M(2)21AB. DR InterPro; IPR002133; S-AdoMet_synt. DR Pfam; PF00438; S-AdoMet_synt; 1. DR Pfam; PF02772; S-AdoMet_syntD2; 1. DR Pfam; PF02773; S-AdoMet_syntD3; 1. DR PROSITE; PS00376; ADOMET_SYNTHETASE_1; 1. DR PROSITE; PS00377; ADOMET_SYNTHETASE_2; 1. KW Transferase; One-carbon metabolism; Magnesium; Potassium; KW Metal-binding; ATP-binding; Alternative splicing. FT NP_BIND 142 147 ATP (POTENTIAL). FT METAL 42 42 MAGNESIUM (BY SIMILARITY). FT METAL 68 68 POTASSIUM (BY SIMILARITY). FT METAL 294 294 POTASSIUM (BY SIMILARITY). FT METAL 302 302 MAGNESIUM (BY SIMILARITY). FT BINDING 170 170 ATP (POTENTIAL). FT VARSPLIC 1 27 Missing (in isoform 4). FT /FTId=VSP_005961. FT VARSPLIC 28 41 TFLFTSESVGEGHP -> MISAECHSEEYTPN (in FT isoform 4). FT /FTId=VSP_005962. FT VARSPLIC 112 141 FKTCNVLLALDQQSPEIAAGVHVNRAEEEI -> WKTLNLL FT VAIEQQSPNIANGVHINREEEDV (in isoform 1, FT isoform 3 and isoform 4). FT /FTId=VSP_005963. FT VARSPLIC 147 200 GIMFGYATDETEECMPLTVVLAHKLNEKIAELRRSDVFWWA FT RPDSKTQVTCEYL -> VSISKRAMCCWHWTNNRLRSLREC FT MSTVPRKRSVPEIRVSCLDMPPTKPRNVCP (in FT isoform 1). FT /FTId=VSP_005964. FT VARSPLIC 201 408 Missing (in isoform 1). FT /FTId=VSP_005965. FT CONFLICT 34 34 E -> V (IN REF. 1). FT CONFLICT 94 94 V -> I (IN REF. 1). FT CONFLICT 290 290 G -> A (IN REF. 1). FT CONFLICT 400 408 EAKPLEIDN -> SQASGD (IN REF. 1). SQ SEQUENCE 408 AA; 44697 MW; CA0F97C1EA6623DF CRC64; MPQKTNGHSA NGCNGSNGNS YDMEDGATFL FTSESVGEGH PDKMCDQISD AILDAHLKQD PNAKVACETV AKTGMILLCG EITSKAVVDY QKVVRETVQH IGYDDSSKGF DFKTCNVLLA LDQQSPEIAA GVHVNRAEEE IGAGDQGIMF GYATDETEEC MPLTVVLAHK LNEKIAELRR SDVFWWARPD SKTQVTCEYL FNQGSAVPKR VHTIVVSMQH SEKISLETLR SEVMEKVVKV VIPAKYIDAN TIVHINPCGL FVIGGPMGDA GLTGRKIIVD TYGGWGAHGG GAFSGKDFTK VDRSAAYAAR WVAKSLVKAG LCKRCLVQVS YAIGLAEPLS ITVFDYGTSH KSQKELLDII RRNFDLRPGK IVKDLNLRQP IYQRTSTYGH FGRAGFSWEE AKPLEIDN // ID METL_DROME STANDARD; PRT; 325 AA. AC Q86BS6; Q960S9; Q9W0C0; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Methyltransferase-like protein (EC 2.1.1.-). GN METL OR CG13929. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 3). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND RP INTERACTION WITH PSN. RX MEDLINE=21601112; PubMed=11738826; RA Zhang S.X., Guo Y., Boulianne G.L.; RT "Identification of a novel family of putative methyltransferases that RT interact with human and Drosophila presenilins."; RL Gene 280:135-144(2001). CC -!- FUNCTION: PROBABLE METHYLTRANSFERASE. CC -!- SUBUNIT: INTERACTS WITH PSN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q86BS6-1; Sequence=Displayed; CC Name=2; Synonyms=Metl-a; CC IsoId=Q86BS6-2; Sequence=VSP_008484; CC Name=3; CC IsoId=Q86BS6-3; Sequence=VSP_008483; CC Note=Derived from EST datas. No experimental confirmation CC available; CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED. EXPRESSED IN OVARIES, HEAD, CC THORAX AND ABDOMEN OF ADULT FLIES, AND IN THE CNS OF THIRD INSTAR CC LARVAE. ISOFORM 2 IS PREDOMINANTLY EXPRESSED IN LARVAE AND IN CC ADULT TISSUES THAT HAVE BEEN TESTED. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYOGENESIS, AS WELL CC AS IN LARVAE AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE METHYLTRANSFERASE SUPERFAMILY. METL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003472; AAF47531.1; -. DR EMBL; AE003472; AAF47532.2; -. DR EMBL; AY051875; AAK93299.1; -. DR EMBL; BI231115; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0035247; metl. DR InterPro; IPR001601; Methyltransf. DR InterPro; IPR000051; SAM_bind. KW Transferase; Methyltransferase; Alternative splicing. FT VARSPLIC 1 52 MLTTSSSTMLGKYGWQILRRLASKSWEHTRQRKKPSGAGSR FT VLTDAREVFEF -> MSDNPAAENEKRPQFGTRLLTDADDV FT FKH (in isoform 3). FT /FTId=VSP_008483. FT VARSPLIC 1 79 Missing (in isoform 2). FT /FTId=VSP_008484. SQ SEQUENCE 325 AA; 38131 MW; 3EFBB4FDC1C7311D CRC64; MLTTSSSTML GKYGWQILRR LASKSWEHTR QRKKPSGAGS RVLTDAREVF EFNAWDHVQW DEEQELAAKA AVAKNSTSKM EAEQKERFQT DAPKFWDSFY GIHDNRFFKD RHWLFTEFPE LAPLAADSAV LQPRSIFELG CGVGNTILPL LQYSSEPQLK VFGCDFSARA IEILRSQRQF DEKRCEVFVM DATLDHWQVP FEENSQDIIV MIFVLSAIEP KKMQRVLDNC YRYLRPGGLL LFRDYGRYDL AQLRFKSGKC MEDNFYVRGD GTMVYFFTEE ELRGMMTQAG LQEEQLIVDR RLQVNRCRGL KMYRVWIQTK FRKPL // ID MEX1_DROME STANDARD; PRT; 83 AA. AC P23487; Q9VUP7; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Midgut expression 1 protein. GN MEX1 OR CG7936. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91085652; PubMed=1985021; RA Schulz R.A., Xie X., Andres A.J., Galewsky S.; RT "Endoderm-specific expression of the Drosophila mex1 gene."; RL Dev. Biol. 143:206-211(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN DROSOPHILA MORPHOGENESIS AND DEVELOPMENT. CC -!- TISSUE SPECIFICITY: DIFFERENTIATING MIDGUT. CC -!- DEVELOPMENTAL STAGE: EMBRYOGENESIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58286; CAA41224.2; -. DR EMBL; M63626; AAA28685.1; -. DR EMBL; AE003530; AAF49628.1; -. DR PIR; A49763; A49763. DR FlyBase; FBgn0004228; mex1. KW Developmental protein; Embryo. FT DOMAIN 1 24 CYS-RICH. SQ SEQUENCE 83 AA; 9424 MW; 3C5EFBFF8BA8E2A0 CRC64; MCNALCECLK CPGKVVCCCC SCACKMLLSI VFSALLMVVV IGLIVYFTVF YHKDKNTDEV QKQVAQLTPI VKRSIRDYFN KEY // ID MGN_DROME STANDARD; PRT; 147 AA. AC P49028; Q9W2L3; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mago nashi protein. GN MAGO OR MGN OR CG9401. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94298529; PubMed=8026338; RA Newmark P.A., Boswell R.E.; RT "The mago nashi locus encodes an essential product required for germ RT plasm assembly in Drosophila."; RL Development 120:1303-1313(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=97417587; PubMed=9272960; RA Newmark P.A., Mohr S.E., Gong L., Boswell R.E.; RT "Mago nashi mediates the posterior follicle cell-to-oocyte signal to RT organize axis formation in Drosophila."; RL Development 124:3197-3207(1997). RN [4] RP FUNCTION. RX MEDLINE=97362356; PubMed=9210377; RA Micklem D.R., Dasgupta R., Elliott H., Gergely F., Davidson C., RA Brand A., Gonzalez-Reyes A., St Johnston D.; RT "The mago nashi gene is required for the polarisation of the oocyte RT and the formation of perpendicular axes in Drosophila."; RL Curr. Biol. 7:468-478(1997). CC -!- FUNCTION: PARTICIPATES IN THE BIDIRECTIONAL INTERCELLULAR CC SIGNALING BETWEEN THE POSTERIOR FOLLICLE CELLS AND OOCYTE TO CC ESTABLISH SPATIAL COORDINATES THAT INDUCES AXIS FORMATION. CC REQUIRED FOR THE POLARIZATION OF THE OOCYTE MICROTUBULE CC CYTOSKELETON. MUTATIONS IN MGN DISRUPT THE OOCYTE POSTERIOR CC LOCALIZATION OF THE OSKAR MRNA AND THE STAUFEN PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR; WITHIN THE POSTERIOR POLE PLASM. CC -!- MISCELLANEOUS: 'MAGO NASHI' MEANS 'WITHOUT GRANDCHILDREN' IN CC JAPANESE. CC -!- SIMILARITY: BELONGS TO THE MAGO NASHI FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03559; AAC13746.1; -. DR EMBL; AE003453; AAF46677.1; -. DR FlyBase; FBgn0002736; mago. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP. DR GO; GO:0008104; P:protein localization; IMP. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localiz...; IMP. DR InterPro; IPR004023; Mago_nashi. DR Pfam; PF02792; Mago_nashi; 1. DR ProDom; PD009481; Mago_nashi; 1. KW Developmental protein; Nuclear protein. FT VARIANT 19 19 G -> R (IN ALLELE MAGO-1). FT VARIANT 91 91 I -> T (IN ALLELE MAGO-WE7). SQ SEQUENCE 147 AA; 17311 MW; B9A2CBFCC5EBEFED CRC64; MSTEDFYLRY YVGHKGKFGH EFLEFEFRPD GKLRYANNSN YKNDTMIRKE AFVHQSVMEE LKRIIIDSEI MQEDDLPWPP PDRVGRQELE IVIGDEHISF TTSKTGSLVD VNRSKDPEGL RCFYYLVQDL KCLVFSLIGL HFKIKPI // ID MGR_DROME STANDARD; PRT; 976 AA. AC P91685; Q9V485; DT 15-JUL-1998 (Rel. 36, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Metabotropic glutamate receptor precursor. GN GLU-RA OR GLURA OR CG11144. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96421661; PubMed=8824309; RA Parmentier M.L., Pin J.P., Bockaert J., Grau Y.; RT "Cloning and functional expression of a Drosophila metabotropic RT glutamate receptor expressed in the embryonic CNS."; RL J. Neurosci. 16:6687-6694(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RECEPTOR FOR GLUTAMATE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE CNS OF THE LATE EMBRYO. CC -!- SIMILARITY: BELONGS TO FAMILY 3 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99675; CAA67993.1; -. DR EMBL; AE003846; AAF59402.1; -. DR FlyBase; FBgn0019985; Glu-RA. DR InterPro; IPR001828; ANF_receptor. DR InterPro; IPR000337; GPCR_Mgr. DR Pfam; PF00003; 7tm_3; 1. DR Pfam; PF01094; ANF_receptor; 1. DR PRINTS; PR00248; GPCRMGR. DR PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1. DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1. DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1. DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 25 POTENTIAL. FT CHAIN 26 976 METABOTROPIC GLUTAMATE RECEPTOR. FT DOMAIN 26 626 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 627 649 I (POTENTIAL). FT DOMAIN 650 663 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 664 684 II (POTENTIAL). FT DOMAIN 685 695 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 696 714 III (POTENTIAL). FT DOMAIN 715 738 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 739 759 IV (POTENTIAL). FT DOMAIN 760 782 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 783 804 V (POTENTIAL). FT DOMAIN 805 817 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 818 840 VI (POTENTIAL). FT DOMAIN 841 850 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 851 876 VII (POTENTIAL). FT DOMAIN 877 976 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 112 112 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 143 143 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 216 216 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 299 299 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 386 386 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 491 491 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 524 524 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 834 834 V -> A (IN REF. 1). SQ SEQUENCE 976 AA; 108485 MW; 43A0E1F918EDACC4 CRC64; MKQKNNNGTI LVVVMVLSWS RVVDLKSPSN THTQDSVSVS LPGDIILGGL FPVHEKGEGA PCGPKVYNRG VQRLEAMLYA IDRVNNDPNI LPGITIGVHI LDTCSRDTYA LNQSLQFVRA SLNNLDTSGY ECADGSSPQL RKNASSGPVF GVIGGSYSSV SLQVANLLRL FHIPQVSPAS TAKTLSDKTR FDLFARTVPP DTFQSVALVD ILKNFNWSYV STIHSEGSYG EYGIEALHKE ATERNVCIAV AEKVPSAADD KVFDSIISKL QKKPNARGVV LFTRAEDARR ILQAAKRANL SQPFHWIASD GWGKQQKLLE GLEDIAEGAI TVELQSEIIA DFDRYMMQLT PETNQRNPWF AEYWEDTFNC VLTSLSVKPD TSNSANSTDN KIGVKAKTEC DDSYRLSEKV GYEQESKTQF VVDAVYAFAY ALHNLHNDRC NTQSDQTTET RKHLQSESVW YRKISTDTKS QACPDMANYD GKEFYNNYLL NVSFIDLAGS EVKFDRQGDG LARYDILNYQ RQENSSGYQY KVIGKWFNGL QLNSETVVWN KETEQPTSAC SLPCEVGMIK KQQGDTCCWI CDSCESFEYV YDEFTCKDCG PGLWPYADKL SCYALDIQYM KWNSLFALIP MAIAIFGIAL TSIVIVLFAK NHDTPLVRAS GRELSYTLLF GILVCYCNTF ALIAKPTIGS CVLQRFGIGV GFSIIYSALL TKTNRISRIF HSASKSAQRL KYISPQSQVV ITTSLIAIQV LITMIWMVVE PPGTRFYYPD RREVILKCKI QDMSFLFSQL YNMILITICT IYAIKTRKIP ENFNESKFIG FTMYTTCIIW LAFVPIYFGT GNSYEVQTTT LCISISLSAS VALVCLYSPK VYILVFHPDK NVRKLTMNST VYRRSAAAVA QGAPTSSGYS RTHAPGTSAL TGGAVGTNAS SSTLPTQNSP HLDEASAQTN VAHKTNGEFL PEVGERVEPI CHIVNK // ID MIP_DROME STANDARD; PRT; 211 AA. AC Q9VVF7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Allatostatins MIP precursor (Myoinhibitory-like protein) (B-type DE Allostatin preprohormone) [Contains: Drostatin B1; Drostatin B2; DE Drostatin B3; Drostatin B4; Drostatin B5]. GN MIP OR CG6456. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=21092858; PubMed=11181081; RA Williamson M., Lenz C., Winther M.E., Naessel D.R., RA Grimmelikhuijzen C.J.P.; RT "Molecular cloning, genomic organization, and expression of a B-type RT (cricket-type) allatostatin preprohormone from Drosophila RT melanogaster."; RL Biochem. Biophys. Res. Commun. 281:544-550(2001). RN [2] RP SEQUENCE FROM N.A. RA Claeys I., Torfs H., Janssen T., Vanden Broeck J.; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 151-159 AND 193-202, AND AMIDATION. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- FUNCTION: MAY HAVE A REGULATORY ROLE IN GUT MOTILITY. CC -!- TISSUE SPECIFICITY: IN LARVAE, EXPRESSED IN BRAIN NEURONS, CC ABDOMINAL GANGLIA AND ENDOCRINE CELLS IN THE GUT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, WEAKLY IN CC EMBRYOS AND STRONGLY IN LARVAE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF312379; AAK29381.1; -. DR EMBL; AJ291725; CAC17604.1; -. DR EMBL; AE003524; AAF49354.1; -. DR EMBL; AY118306; AAM48335.1; -. DR PIR; JC7617; JC7617. DR FlyBase; FBgn0036713; MIP. DR GO; GO:0005184; F:neuropeptide hormone activity; NAS. DR GO; GO:0005102; F:receptor binding; IDA. DR GO; GO:0045968; P:negative regulation of juvenile hormone bio...; NAS. DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA. KW Neuropeptide; Signal; Cleavage on pair of basic residues; Amidation. FT SIGNAL 1 24 POTENTIAL. FT PROPEP 25 63 FT PEPTIDE 66 74 DROSTATIN B1 (POTENTIAL). FT PROPEP 78 148 FT PEPTIDE 151 159 DROSTATIN B2. FT PEPTIDE 163 175 DROSTATIN B3 (POTENTIAL). FT PEPTIDE 179 189 DROSTATIN B4 (POTENTIAL). FT PEPTIDE 193 202 DROSTATIN B5. FT PROPEP 206 211 FT MOD_RES 74 74 AMIDATION (G-75 PROVIDE AMIDE GROUP) FT (POTENTIAL). FT MOD_RES 159 159 AMIDATION (G-160 PROVIDE AMIDE GROUP). FT MOD_RES 175 175 AMIDATION (G-176 PROVIDE AMIDE GROUP) FT (POTENTIAL). FT MOD_RES 189 189 AMIDATION (G-190 PROVIDE AMIDE GROUP) FT (POTENTIAL). FT MOD_RES 202 202 AMIDATION (G-203 PROVIDE AMIDE GROUP). SQ SEQUENCE 211 AA; 23412 MW; 616C8BDEA4D4DADB CRC64; MAHTKTRRTY GFLMVLLILG SACGNLVASG SAGSPPSNEP GGGGLSEQVV LDQLSESDLY GNNKRAWQSL QSSWGKRSSS GDVSDPDIYM TGHFVPLVIT DGTNTIDWDT FERLASGQSA QQQQQQPLQQ QSQSGEDFDD LAGEPDVEKR AWKSMNVAWG KRRQAQGWNK FRGAWGKREP TWNNLKGMWG KRDQWQKLHG GWGKRSQLPS N // ID MKK2_DROME STANDARD; PRT; 359 AA. AC P49071; Q9W480; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE MAP kinase-activated protein kinase 2 (EC 2.7.1.-) (MAPK-activated DE protein kinase 2) (MAPKAP kinase 2) (MAPKAPK-2). GN MAPK-AK2 OR CG3086. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BIC-D(R26); TISSUE=Ovary; RX MEDLINE=96011635; PubMed=7590268; RA Larochelle S., Suter B.; RT "The Drosophila melanogaster homolog of the mammalian MAPK-activated RT protein kinase-2 (MAPKAPK-2) lacks a proline-rich N-terminus."; RL Gene 163:209-214(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ITS PHYSIOGICAL SUBSTRATE SEEMS TO BE THE SMALL HEAT CC SHOCK PROTEIN (HSP27/HSP25) (BY SIMILARITY). CC -!- PTM: PHOSPHORYLATED AND ACTIVATED BY MAP KINASE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U20757; AAA86885.1; -. DR EMBL; AE003435; AAG22408.1; -. DR PIR; JC4297; JC4297. DR HSSP; Q63450; 1A06. DR FlyBase; FBgn0013987; MAPk-Ak2. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Phosphorylation. FT DOMAIN 20 281 PROTEIN KINASE. FT NP_BIND 26 34 ATP (BY SIMILARITY). FT BINDING 49 49 ATP (BY SIMILARITY). FT ACT_SITE 142 142 BY SIMILARITY. SQ SEQUENCE 359 AA; 41401 MW; 69C5F9A94D1511EC CRC64; MLSLQNQRQP KTTPLTDDYV TSNTVLGYGI NGKVVQCTHR RTQQNYALKV LLDSERARRE VDLHWRVSGC RYIVNIIDVY ENTFKDRKCL LVVMECMEGG ELFQRIQDKA DGAFTEREAA QIMHEICAAV DYLHSRDIAH RDLKPENLLY TTTQPNATLK LTDFGFAKET FTSYTLQTPC YTPYYVAPEV LGPEKYDKSC DIWSLGVVMY IIMCGFPPFY SNHGLAISPG MKNRIRTGQY DFPDPEWTNV SQAAKDLIKG MLNVDPSKRL RIQDVISNKW IAQYNAVPQT PLCTGRMLKE AEETWPEVQE EMTRSLATMR VDYDQMQIKA LDKSNNPLLT KRRKKIEEME LYMANATRN // ID MLC1_DROME STANDARD; PRT; 155 AA. AC P06742; P06743; P92155; P92156; P92157; P92183; P92187; P92196; AC Q24380; Q24381; Q24382; Q24383; Q27304; Q27315; Q27381; Q27414; AC Q94988; Q9VB12; DT 01-JAN-1988 (Rel. 06, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myosin light chain alkali (Catalytic). GN MLC1 OR MLC-ALK OR CG5596. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo, Larva, and Pupae; RX MEDLINE=85113215; PubMed=2982157; RA Falkenthal S., Parker V.P., Davidson N.; RT "Developmental variations in the splicing pattern of transcripts from RT the Drosophila gene encoding myosin alkali light chain result in RT different carboxyl-terminal amino acid sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 82:449-453(1985). RN [2] RP SEQUENCE FROM N.A. (ISOFORM LARVAL-ADULT), DEVELOPMENTAL STAGE, RP AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Embryo, Flight muscle, and Pupae; RX MEDLINE=84219416; PubMed=6328279; RA Falkenthal S., Parker V.P., Mattox W.W., Davidson N.; RT "Drosophila melanogaster has only one myosin alkali light-chain gene RT which encodes a protein with considerable amino acid sequence RT homology to chicken myosin alkali light chains."; RL Mol. Cell. Biol. 4:956-965(1984). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM LARVAL-ADULT). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE OF 62-155 FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=M86, M171, M174, M179, M180, M192, M219, M223, M234, M237, RC M240, M241N, M242, M245, M247, and M249; RX MEDLINE=95220668; PubMed=7535717; RA Leicht B.G., Muse S.V., Hanczyc M., Clark A.G.; RT "Constraints on intron evolution in the gene encoding the myosin RT alkali light chain in Drosophila."; RL Genetics 139:299-308(1995). RN [7] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RC TISSUE=Abdomen, Flight muscle, Head, Muscle, and Pupae; RX MEDLINE=87191414; PubMed=3106119; RA Falkenthal S., Graham M., Wilkinson J.; RT "The indirect flight muscle of Drosophila accumulates a unique myosin RT alkali light chain isoform."; RL Dev. Biol. 121:263-272(1987). CC -!- SUBUNIT: MYOSIN IS AN HEXAMER OF 2 HEAVY CHAINS AND 4 LIGHT CC CHAINS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Larval-adult; Synonyms=Larval-non-IFM; CC IsoId=P06742-1; Sequence=Displayed; CC Name=Indirect flight muscle; Synonyms=Pupa, Adult flight muscle; CC IsoId=P06742-2; Sequence=VSP_003367; CC -!- TISSUE SPECIFICITY: INDIRECT FLIGHT MUSCLE ISOFORM IS FOUND ONLY CC IN THE INDIRECT FLIGHT MUSCLES. THE LARVAL AND ADULT ISOFORM IS CC PRESENT IN THE LARVAL AND ADULT MUSCULATURE. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING LATE EMBRYOGENESIS, LARVAL CC INSTARS, LATE STAGES OF PUPARIATION AND ADULT. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS, BUT THIS CC PROTEIN DOES NOT BIND CALCIUM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M10125; AAA28711.1; -. DR EMBL; M10125; AAA28712.1; -. DR EMBL; K01567; AAA28710.1; -. DR EMBL; AE003761; AAF56733.2; -. DR EMBL; AE003761; AAN14121.1; -. DR EMBL; AY070972; AAL48594.1; -. DR EMBL; L37312; AAA53441.1; -. DR EMBL; L37312; AAA53442.1; -. DR EMBL; L37313; AAA53443.1; -. DR EMBL; L37313; AAA53444.1; -. DR EMBL; L37314; AAA53445.1; -. DR EMBL; L37314; AAA53446.1; -. DR EMBL; L37315; AAA53447.1; ALT_SEQ. DR EMBL; L37315; AAA53448.1; ALT_SEQ. DR EMBL; L37316; AAA56798.1; -. DR EMBL; L37316; AAA56799.1; ALT_SEQ. DR EMBL; L37317; AAA53449.1; -. DR EMBL; L37317; AAA53450.1; -. DR EMBL; L37318; AAA53451.1; -. DR EMBL; L37318; AAA53452.1; -. DR EMBL; L37319; AAA53453.1; -. DR EMBL; L37319; AAA53454.1; -. DR EMBL; L37320; AAA53455.1; -. DR EMBL; L37320; AAA53456.1; -. DR EMBL; L37321; AAA53457.1; -. DR EMBL; L37321; AAA53458.1; -. DR EMBL; L37322; AAA53459.1; -. DR EMBL; L37322; AAA53460.1; -. DR EMBL; L37323; AAA53461.1; -. DR EMBL; L37323; AAA53462.1; -. DR EMBL; L37324; AAA53463.1; -. DR EMBL; L37324; AAA53464.1; -. DR EMBL; L37325; AAA53465.1; -. DR EMBL; L37325; AAA53466.1; -. DR EMBL; L37326; AAA53467.1; -. DR EMBL; L37326; AAA53468.1; -. DR EMBL; L37327; AAA53469.1; -. DR EMBL; L37327; AAA53470.1; -. DR FlyBase; FBgn0002772; Mlc1. DR GO; GO:0005859; C:muscle myosin; IDA. DR GO; GO:0003776; F:muscle motor activity; NAS. DR GO; GO:0006936; P:muscle contraction; NAS. DR InterPro; IPR002048; EF-hand. KW Myosin; Muscle protein; Alternative splicing. FT VARSPLIC 142 155 QFVQRLMSDPVVFD -> PFLARMCDRPDQLK (in FT isoform Indirect flight muscle). FT /FTId=VSP_003367. FT CONFLICT 2 2 A -> V (IN REF. 1). FT CONFLICT 67 67 L -> M (IN REF. 6; AAA53454/AAA53458/ FT AAA53460/AAA53466/AAA53468). FT CONFLICT 150 150 D -> H (IN REF. 1). SQ SEQUENCE 155 AA; 17524 MW; 65C92CD17995ECF5 CRC64; MADVPKREVE NVEFVFEVMG SPGEGIDAVD LGDALRALNL NPTLALIEKL GGTKKRNEKK IKLDEFLPIY SQVKKEKEQG CYEDFIECLK LYDKEENGTM LLAELQHALL ALGESLDDEQ VETLFADCMD PEDDEGFIPY SQFVQRLMSD PVVFD // ID MLC2_DROME STANDARD; PRT; 147 AA. AC P54357; Q9W4A8; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myosin II essential light chain (Nonmuscle myosin essential light DE chain). GN MLC-C OR CG3201. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96129611; PubMed=8567936; RA Edwards K.A., Chang X., Kiehart D.P.; RT "Essential light chain of Drosophila nonmuscle myosin II."; RL J. Muscle Res. Cell Motil. 16:491-498(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBUNIT: MYOSIN IS AN HEXAMER OF 2 HEAVY CHAINS AND 4 LIGHT CC CHAINS (BY SIMILARITY). CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U25057; AAA84897.1; -. DR EMBL; AE003434; AAF46048.1; -. DR HSSP; P02593; 1CDM. DR FlyBase; FBgn0004687; Mlc-c. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 3. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 3. DR PROSITE; PS00018; EF_HAND; 1. KW Myosin. FT CA_BIND 93 104 EF-HAND (POTENTIAL). SQ SEQUENCE 147 AA; 16613 MW; A37FA3C9DE942B90 CRC64; MAAYTEDQLA EFQEAFNLFD NRGDGKIQLS QVGECLRALG QNPTESDVKK CTHQLKPDER ISFEVFLPIY QAISKARSGD TADDFIEGLR HFDKDASGYI SSAELRHLLT TLGEKLTDEE VEQLLANMED QQGNINYEEF VRMVMSG // ID MLE_DROME STANDARD; PRT; 1293 AA. AC P24785; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Dosage compensation regulator (Male-less protein) (No action potential DE protein). GN MLE OR NAP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND ALTERNATIVE RP SPLICING. RC TISSUE=Imaginal disks; RX MEDLINE=91364175; PubMed=1653648; RA Kuroda M.I., Kernan M.J., Kreber R., Ganetzky B., Baker B.S.; RT "The maleless protein associates with the X chromosome to regulate RT dosage compensation in Drosophila."; RL Cell 66:935-947(1991). CC -!- FUNCTION: REQUIRED IN MALES FOR DOSAGE COMPENSATION OF X CC CHROMOSOME LINKED GENES. MLE, MSL-1 AND MSL-3 ARE CO-LOCALIZED ON CC X CHROMOSOME. EACH OF THE MSL PROTEINS REQUIRES ALL THE OTHER MSLS CC FOR WILD-TYPE X-CHROMOSOME BINDING. PROBABLY UNWINDS DOUBLE- CC STRANDED DNA AND RNA IN A 3' TO 5' DIRECTION. CC -!- SUBCELLULAR LOCATION: NUCLEAR; MLE IS ASSOCIATED WITH HUNDREDS OF CC DISCRETE SITES ALONG THE LENGTH OF THE X CHROMOSOME IN MALES AND CC NOT IN FEMALES, AND IS ASSOCIATED WITH 30-40 AUTOSOMAL SITES IN CC BOTH SEXES. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=25; CC IsoId=P24785-1; Sequence=Displayed; CC Name=12; CC IsoId=P24785-2; Sequence=VSP_005775, VSP_005776; CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT; HIGHEST IN CC EMBRYOS AND AT EQUAL LEVELS IN MALES AND FEMALES. CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. DEAH CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 DRBM (DOUBLE-STRANDED RNA-BINDING) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74121; AAC41573.1; -. DR PIR; B40025; B40025. DR FlyBase; FBgn0002774; mle. DR GO; GO:0005717; C:chromatin; IDA. DR GO; GO:0016456; C:dosage compensation complex (sensu Drosophila); NAS. DR GO; GO:0003682; F:chromatin binding; IDA. DR GO; GO:0009047; P:dosage compensation, by hyperactivation of ...; NAS. DR InterPro; IPR001410; DEAD. DR InterPro; IPR002464; DEAH_box. DR InterPro; IPR001159; DS_RBD. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR007502; Helicase_dom. DR Pfam; PF00035; dsrm; 2. DR Pfam; PF04408; HA2; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00358; DSRM; 2. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS50137; DS_RBD; 2. KW Helicase; ATP-binding; Nuclear protein; Alternative splicing; KW Repeat. FT DOMAIN 2 70 DRBM 1. FT DOMAIN 169 241 DRBM 2. FT NP_BIND 407 414 ATP (BY SIMILARITY). FT SITE 507 510 DEAH BOX. FT DOMAIN 1202 1263 9 X 7 AA TANDEM REPEATS OF G-G-G-Y-G-N-N. FT REPEAT 1202 1208 1. FT REPEAT 1209 1215 2. FT REPEAT 1216 1222 3. FT REPEAT 1223 1229 4. FT REPEAT 1230 1236 5. FT REPEAT 1237 1243 6. FT REPEAT 1244 1250 7. FT REPEAT 1251 1257 8. FT REPEAT 1258 1263 9. FT VARSPLIC 199 226 SFLAELSIYVPALNRTVTARESGSNKKS -> YVLPFQLSS FT ACISDLTRYGLRPNLKCSP (in isoform 12). FT /FTId=VSP_005775. FT VARSPLIC 227 1293 Missing (in isoform 12). FT /FTId=VSP_005776. FT VARIANT 1276 1276 G -> V. SQ SEQUENCE 1293 AA; 143587 MW; 4D890E7F2705F259 CRC64; MDIKSFLYQF CAKSQIEPKF DIRQTGPKNR QRFLCEVRVE PNTYIGVGNS TNKKDAEKNA CRDFVNYLVR VGKLNTNDVP ADAGASGGGP RTGLEGAGMA GGSGQQKRVF DGQSGPQDLG EAYRPLNHDG GDGGNRYSVI DRIQEQRDMN EAEAFDVNAA IHGNWTIENA KERLNIYKQT NNIRDDYKYT PVGPEHARSF LAELSIYVPA LNRTVTARES GSNKKSASKS CALSLVRQLF HLNVIEPFSG TLKKKKDEQL KPYPVKLSPN LINKIDEVIK GLDLPVVNPR NIKIELDGPP IPLIVNLSRI DSSQQDGEKR QESSVIPWAP PQANWNTWHA CNIDEGELAT TSIDDLSMDY ERSLRDRRQN DNEYRQFLEF REKLPIAAMR SEILTAINDN PVVIIRGNTG CGKTTQIAQY ILDDYICSGQ GGYANIYVTQ PRRISAISVA ERVARERCEQ LGDTVGYSVR FESVFPRPYG AILFCTVGVL LRKLEAGLRG VSHIIVDEIH ERDVNSDFLL VILRDMVDTY PDLHVILMSA TIDTTKFSKY FGICPVLEVP GRAFPVQQFF LEDIIQMTDF VPSAESRRKP KEVEDEEQLL SEDKDEAEIN YNKVCEDKYS QKTRNAMAML SESDVSFELL EALLMHIKSK NIPGAILVFL PGWNLIFALM KFLQNTNIFG DTSQYQILPC HSQIPRDEQR KVFEPVPEGV TKIILSTNIA ETSITIDDIV FVIDICKARM KLFTSHNNLT SYATVWASKT NLEQRKGRAG RVRPGFCFTL CSRARFQALE DNLTPEMFRT PLHEMALTIK LLRLGSIHHF LSKALEPPPV DAVIEAEVLL REMRCLDAND ELTPLGRLLA RLPIEPRLGK MMVLGAVFGC ADLMAIMASY SSTFSEVFSL DIGQRRLANH QKALSGTKCS DHVAMIVASQ MWRREKQRGE HMEARFCDWK GLQMSTMNVI WDAKQQLLDL LQQAGFPEEC MISHEVDERI DGDDPVLDVS LALLCLGLYP NICVHKEKRK VLTTESKAAL LHKTSVNCSN LAVTFPYPFF VFGEKIRTRA VSCKQLSMVS PLQVILFGSR KIDLAANNIV RVDNWLNFDI EPELAAKIGA LKPALEDLIT VACDNPSDIL RLEEPYAQLV KVVKDLCVKS AGDFGLQRES GILPHQSRQF SDGGGPPKRG RFETGRFTNS SFGRRGNGRT FGGGYGNNGG GYGNNGGGYG NIGGGYGNNA GGYGNNGGYG NNGGGYRNNG GGYGNNGGGY GNNRGGFGDS FESNRGSGGG FRNGDQGGRW GNF // ID MLF_DROME STANDARD; PRT; 309 AA. AC Q9NKV0; Q9V7G3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myeloid leukemia factor (Myelodysplasia-myeloid leukemia factor) DE (dMLF). GN MLF OR CG8295. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=20578896; PubMed=11137299; RA Ohno K., Takahashi Y., Hirose F., Inoue Y.H., Taguchi O., Nishida Y., RA Matsukage A., Yamaguchi M.; RT "Characterization of a Drosophila homologue of the human RT myelodysplasia/myeloid leukemia factor (MLF)."; RL Gene 260:133-143(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. INTERACTS WITH DRE-BINDING CC FACTOR (DREF). CC -!- TISSUE SPECIFICITY: EXPRESSED AT HIGH LEVELS IN UNFERTILIZED EGGS, CC EARLY EMBRYOS, PUPAE AND ADULT MALES WHILE A LOW LEVEL EXPRESSION CC IS FOUND IN ADULT FEMALES AND LARVAE. CC -!- DEVELOPMENTAL STAGE: HIGH LEVELS ARE SEEN IN UNFERTILIZED EGGS AND CC EXPRESSION INCREASES SLIGHTLY DURING EARLY EMBRYO STAGES (2-3 CC HRS). LEVELS ARE HIGH IN EMBRYOS UNTIL 4 HRS AFTER FERTILIZATION CC AND THEN DECREASE GRADUALLY THROUGH EMBRYONIC AND LARVAL STAGES. CC -!- SIMILARITY: BELONGS TO THE MLF FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB043986; BAA96391.1; -. DR EMBL; AE003809; AAF58093.2; -. DR FlyBase; FBgn0034051; Mlf. FT DOMAIN 96 202 INTERACTION WITH DREF. FT DOMAIN 236 243 POLY-ASP. SQ SEQUENCE 309 AA; 34413 MW; 4C50951D548FD9AD CRC64; MSLFGALMGD FDDDLGLMNN HMNHTMNAMN MQMRSMNRLM NSFMPDPFMQ VSPFDQGFQQ NALMERPQMP AMPAMGLFGM PMMPNFNRLL NADIGGNSGA SFCQSTVMTM SSGPDGRPQI YQASTSTKTG PGGVRETRRT VQDSRTGVKK MAIGHHIGER AHIIEKEQDM RSGQLEERQE FINLEEGEAE QFDREFTSRA SRGAVQSRHH AGGMQAIMPA RPAAHTSTLT IEPVEDDDDD DDDCVIQEQQ PVRSSAGRHY SSAPTAPQNS IHPHPYAANP RRQQRAVKHF HTEDEAASSY KAVKRGKKK // ID MLP1_DROME STANDARD; PRT; 92 AA. AC P53777; Q9W1B4; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Muscle LIM protein 1. GN MLP60A OR LIM2 OR MLP1 OR CG3220. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95042720; PubMed=7954791; RA Arber S., Halder G., Caroni P.; RT "Muscle LIM protein, a novel essential regulator of myogenesis, RT promotes myogenic differentiation."; RL Cell 79:221-231(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96387325; PubMed=8794860; RA Stronach B.E., Siegrist S.E., Beckerle M.C.; RT "Two muscle-specific LIM proteins in Drosophila."; RL J. Cell Biol. 134:1179-1195(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: POSITIVE REGULATOR OF MYOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: IN THE EMBRYO, EXPRESSION IS RESTRICTED TO THE CC SOMATIC, VICERAL, AND PHARYNGEAL MUSCLES. WITHIN THE SOMATIC CC MUSCULATURE, MLP60 IS DISTRIBUTED THROUGHOUT THE MUSCLE FIBERS. CC THERE IS NO EXPRESSION IN CARDIAC MESODERM OR IN FAT BODY. CC -!- DEVELOPMENTAL STAGE: EXPRESSION IS BIPHASIC, PEAKING LATE IN CC EMBRYOGENESIS (16-24 H EMBRYOS) AND DURING THE LARVAL TO PUPAL CC TRANSITION, WHEN THE MUSCULATURE IS DIFFERENTIATING. FOUND IN CC DEVELOPING MUSCLES OF THE VISCERAL AND SOMATIC MESODERM SUBSEQUENT CC TO THE FORMATION OF THE MUSCLE PRECURSOR CELLS. DECREASED LEVELS CC ARE STILL DETECTABLE IN ADULTS. CC -!- SIMILARITY: TO THE VERTEBRATE CYSTEINE-RICH PROTEINS. CC -!- SIMILARITY: CONTAINS 1 LIM ZINC-BINDING DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X81192; CAA57064.1; -. DR EMBL; X91244; CAA62626.1; -. DR EMBL; AE003462; AAF47158.2; -. DR HSSP; Q05158; 1A7I. DR FlyBase; FBgn0011643; Mlp60A. DR InterPro; IPR001781; LIM. DR Pfam; PF00412; LIM; 1. DR ProDom; PD000094; LIM; 1. DR SMART; SM00132; LIM; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 1. DR PROSITE; PS50023; LIM_DOMAIN_2; 1. KW Nuclear protein; Repeat; LIM domain; Metal-binding; Zinc; Myogenesis; KW Developmental protein; Differentiation. FT DOMAIN 11 62 LIM. FT DOMAIN 64 79 GLY-RICH. FT DOMAIN 65 70 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). SQ SEQUENCE 92 AA; 9958 MW; FDDBDDA1A90065A8 CRC64; MPFVPVETPK CPACGKSVYA AEERVAGGYK FHKTCFKCSM CNKALDSTNC TEHEKELFCK NCHGRKYGPK GYGFGGGAGC LSTDTGAHLN RE // ID MLP2_DROME STANDARD; PRT; 495 AA. AC Q24400; Q9VI62; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Muscle LIM protein MLP84B. GN LIM3 OR MLP84B OR CG10699. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96387325; PubMed=8794860; RA Stronach B.E., Siegrist S.E., Beckerle M.C.; RT "Two muscle-specific LIM proteins in Drosophila."; RL J. Cell Biol. 134:1179-1195(1996). RN [2] RP SEQUENCE FROM N.A. RA Stronach B.E., Renfranz P.J., Lilly B., Beckerle M.C.; RT "Muscle LIM proteins associate with muscle sarcomeres and require RT dMEF2 for their expression during Drosophila myogenesis."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PLAYS A ROLE IN CELL DIFFERENTIATION LATE IN MYOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: IN THE EMBRYO, EXPRESSION IS RESTRICTED TO THE CC SOMATIC, VICERAL, AND PHARYNGEAL MUSCLES. WITHIN THE SOMATIC CC MUSCULATURE, MLP48B IS LOCALIZED AT THE ENDS OF MUSCLES FIBERS AT CC THE POINT OF ATTACHMENT TO THE EPIDERMIS. THERE IS NO EXPRESSION CC IN CARDIAC MESODERM OR IN FAT BODY. CC -!- DEVELOPMENTAL STAGE: EXPRESSION IS BIPHASIC, PEAKING LATE IN CC EMBRYOGENESIS (16-24 H EMBRYOS) AND DURING THE LARVAL TO PUPAL CC TRANSITION, WHEN THE MUSCULATURE IS DIFFERENTIATING. FOUND IN CC DEVELOPING MUSCLES OF THE VISCERAL AND SOMATIC MESODERM SUBSEQUENT CC TO THE FORMATION OF THE MUSCLE PRECURSOR CELLS. DECREASED LEVELS CC ARE STILL DETECTABLE IN ADULTS. CC -!- SIMILARITY: TO THE VERTEBRATE CYSTEINE-RICH PROTEINS. CC -!- SIMILARITY: CONTAINS 5 LIM ZINC-BINDING DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X91245; CAA62627.1; -. DR EMBL; AF090832; AAC61591.1; -. DR EMBL; AE003672; AAF54063.1; -. DR HSSP; P32965; 1CTL. DR FlyBase; FBgn0014863; Mlp84B. DR InterPro; IPR001781; LIM. DR Pfam; PF00412; LIM; 5. DR ProDom; PD000094; LIM; 5. DR SMART; SM00132; LIM; 5. DR PROSITE; PS00478; LIM_DOMAIN_1; 5. DR PROSITE; PS50023; LIM_DOMAIN_2; 5. KW Nuclear protein; Repeat; LIM domain; Metal-binding; Zinc; Myogenesis; KW Developmental protein; Differentiation. FT DOMAIN 12 63 LIM 1. FT DOMAIN 65 80 GLY-RICH. FT DOMAIN 66 71 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 120 172 LIM 2. FT DOMAIN 175 180 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 178 189 GLY-RICH. FT DOMAIN 222 274 LIM 3. FT DOMAIN 276 291 GLY-RICH. FT DOMAIN 325 377 LIM 4. FT DOMAIN 379 390 GLY-RICH. FT DOMAIN 421 473 LIM 5. FT DOMAIN 475 490 GLY-RICH. SQ SEQUENCE 495 AA; 53525 MW; 2E559B9178E54C0E CRC64; MPSFQPIEAP KCPRCGKSVY AAEERLAGGY VFHKNCFKCG MCNKSLDSTN CTEHERELYC KTCHGRKFGP KGYGFGTGAG TLSMDNGSQF LRENGDVPSV RNGARLEPRA IARAPEGEGC PRCGGYVYAA EQMLARGRSW HKECFKCGTC KKGLDSILCC EAPDKNIYCK GCYAKKFGPK GYGYGQGGGA LQSDCYAHDD GAPQIRAAID VDKIQARPGE GCPRCGGVVY AAEQKLSKGR EWHKKCFNCK DCHKTLDSIN ASDGPDRDVY CRTCYGKKWG PHGYGFACGS GFLQTDGLTE DQISANRPFY NPDTTSIKAR DGEGCPRCGG AVFAAEQQLS KGKVWHKKCY NCADCHRPLD SVLACDGPDG DIHCRACYGK LFGPKGFGYG HAPTLVSTSG ESTIQFPDGR PLAGPKTSGG CPRCGFAVFA AEQMISKTRI WHKRCFYCSD CRKSLDSTNL NDGPDGDIYC RACYGRNFGP KGVGYGLGAG ALTTF // ID MLRN_DROME STANDARD; PRT; 174 AA. AC P40423; Q9W428; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myosin regulatory light chain, nonmuscle (MRLC-C) (Spaghetti-squash DE protein). GN SQH OR CG3595. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91292521; PubMed=1905980; RA Karess R.E., Chang X.J., Edwards K.A., Kulkarni S., Aguilera I., RA Kiehart D.P.; RT "The regulatory light chain of nonmuscle myosin is encoded by RT spaghetti-squash, a gene required for cytokinesis in Drosophila."; RL Cell 65:1177-1189(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR CYTOKINESIS, COULD REGULATE CONTRACTILE CC RING FUNCTION. CC -!- SUBUNIT: MYOSIN IS AN HEXAMER OF 2 HEAVY CHAINS AND 4 LIGHT CC CHAINS. CC -!- MISCELLANEOUS: THIS CHAIN BINDS CALCIUM (BY SIMILARITY). CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M67494; AAC13367.1; -. DR EMBL; AE003436; AAF46132.1; -. DR PIR; A39932; A39932. DR HSSP; P13543; 1SCM. DR FlyBase; FBgn0003514; sqh. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 2. DR ProDom; PD000012; EF-hand; 2. DR PROSITE; PS00018; EF_HAND; 1. KW Myosin; Calcium-binding. FT CA_BIND 44 55 EF-HAND (POTENTIAL). SQ SEQUENCE 174 AA; 19954 MW; 2D95C9F0460B8766 CRC64; MSSRKTAGRR ATTKKRAQRA TSNVFAMFDQ AQIAEFKEAF NMIDQNRDGF VEKEDLHDML ASLGKNPTDD YLDGMMNEAP GPINFTMFLT LFGERLQGTD PEDVIKNAFG CFDEENMGVL PEDRLRELLT TMGDRFTDED VDEMYREAPI KNGLFDYLEF TRILKHGAKD KDEQ // ID MLR_DROME STANDARD; PRT; 221 AA. AC P18432; Q9VA98; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myosin regulatory light chain 2 (MLC-2). GN MLC2 OR CG2184. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=87083550; PubMed=3025224; RA Toffenetti J., Mischke D., Pardue M.L.; RT "Isolation and characterization of the gene for myosin light chain RT two of Drosophila melanogaster."; RL J. Cell Biol. 104:19-28(1987). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Pupae; RX MEDLINE=86310773; PubMed=3018498; RA Parker V.P., Falkenthal S., Davidson N.; RT "Characterization of the myosin light-chain-2 gene of Drosophila RT melanogaster."; RL Mol. Cell. Biol. 5:3058-3068(1985). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: MYOSIN IS AN HEXAMER OF 2 HEAVY CHAINS AND 4 LIGHT CC CHAINS. CC -!- MISCELLANEOUS: THIS CHAIN BINDS CALCIUM. CC -!- MISCELLANEOUS: MLC2 HAS AT LEAST TWO ISOFORMS IN EACH TYPE OF CC MUSCLE AND THE ISOFORMS OF TUBULAR MUSCLE DIFFER SLIGHTLY FROM CC THOSE OF FIBRILLAR MUSCLE. THESE ISOFORMS MAY ARISE THROUGH CC POSTTRANSLATIONAL MODIFICATIONS. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28643; AAA28576.1; -. DR EMBL; M11947; AAA51466.1; -. DR EMBL; AE003772; AAF57016.1; -. DR EMBL; AY060369; AAL25408.1; -. DR PIR; A27270; A27270. DR HSSP; P02593; 1CDM. DR FlyBase; FBgn0002773; Mlc2. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 2. DR ProDom; PD000012; EF-hand; 1. DR PROSITE; PS00018; EF_HAND; 1. KW Myosin; Calcium-binding; Muscle protein; Acetylation. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT CA_BIND 87 98 EF-HAND (BY SIMILARITY). SQ SEQUENCE 221 AA; 23583 MW; B9D84B048F769539 CRC64; ADEKKKVKKK KTKEEGGTSE TASEAASEAA TPAPAATPAP AASATGSKRA SGGSRGSRKS KRAGSSVFSV FSQKQIAEFK EAFQLMDADK DGIIGKNDLR AAFDSVGKIA NDKELDAMLG EASGPINFTQ LLTLFANRMA TSGANDEDEV VIAAFKTFDN DGLIDGDKFR EMLMNFGDKF TMKEVDDAYD QMVIDDKNQI DTAALIEMLT GKGEEEEEEA A // ID MNB_DROME STANDARD; PRT; 843 AA. AC P49657; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Serine/threonine protein kinase minibrain (EC 2.7.1.-). GN MNB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS A; B AND C). RC STRAIN=Berlin; RX MEDLINE=95161060; PubMed=7857639; RA Tejedor F., Zhu X.R., Kaltenbach E., Ackermann A., Baumann A., RA Canal I., Heisenberg M., Fischbach K.F., Pongs O.; RT "Minibrain: a new protein kinase family involved in postembryonic RT neurogenesis in Drosophila."; RL Neuron 14:287-301(1995). CC -!- FUNCTION: ROLE IN THE SPECIFIC CONTROL OF PROPER PROLIFERATION OF CC OPTIC LOBE NEURONAL PROGENY. MUTANTS ARE CHARACTERIZED BY A CC SPECIFIC AND MARKED SIZE REDUCTION OF THE OPTIC LOBES AND CENTRAL CC BRAIN HEMISPHERES BUT NO MAJOR ALTERATION IN NEURONAL ARCHITECTURE CC CAN BE FOUND. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=P49657-1; Sequence=Displayed; CC Name=B; CC IsoId=P49657-2; Sequence=VSP_004913, VSP_004914; CC Name=C; CC IsoId=P49657-3; Sequence=VSP_004915, VSP_004916; CC -!- TISSUE SPECIFICITY: IN VENTRAL NERVE CORD AND SUPRAOESOPHAGEAL CC GANGLION OF EMBRYOS. IS MOST PROMINENT IN THE MUSHROOM BODY CC NEUROPIL AND THE OUTER PROLIFERATION CENTER OF THE OPTIC LOBES IN CC THIRD INSTAR LARVAE. CC -!- DEVELOPMENTAL STAGE: THE FORMS A AND C ARE PRESENT MAINLY IN CC EMBRYOS AND PUPAE. BY CONTRAST, FORM B APPEARS TO BE EXPRESSED CC MOST MARKEDLY IN THIRD INSTAR LARVAE AND PUPAE. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC MNB/DYRK SUBFAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-16 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X70794; CAA50065.1; -. DR EMBL; X70798; CAA50068.1; -. DR EMBL; X70799; CAA50069.1; -. DR HSSP; P24941; 1BUH. DR FlyBase; FBgn0002777; mnb. DR GO; GO:0007623; P:circadian rhythm; IGI. DR GO; GO:0007611; P:learning and/or memory; NAS. DR GO; GO:0007399; P:neurogenesis; IMP. DR GO; GO:0008355; P:olfactory learning; IMP. DR GO; GO:0007632; P:visual behavior; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Nuclear protein; Alternative splicing; Developmental protein; KW Neurogenesis. FT DOMAIN 5 11 POLY-SER. FT DOMAIN 56 74 BIPARTITE NUCLEAR LOCALIZATION SIGNAL. FT DOMAIN 99 419 PROTEIN KINASE. FT NP_BIND 105 113 ATP (BY SIMILARITY). FT BINDING 128 128 ATP (BY SIMILARITY). FT ACT_SITE 227 227 BY SIMILARITY. FT DOMAIN 426 843 GLY/ALA/SER-RICH. FT DOMAIN 471 474 POLY-SER. FT DOMAIN 505 508 POLY-GLN. FT DOMAIN 642 646 POLY-PRO. FT DOMAIN 677 680 POLY-SER. FT DOMAIN 682 692 POLY-ALA. FT DOMAIN 767 776 POLY-SER. FT DOMAIN 825 828 POLY-SER. FT VARSPLIC 536 539 GLLM -> DDRR (in isoform B). FT /FTId=VSP_004913. FT VARSPLIC 540 843 Missing (in isoform B). FT /FTId=VSP_004914. FT VARSPLIC 536 542 GLLMHSV -> VRRIVRI (in isoform C). FT /FTId=VSP_004915. FT VARSPLIC 543 843 Missing (in isoform C). FT /FTId=VSP_004916. FT VARIANT 126 126 A -> T (IN MNB1; REDUCED BRAIN VOLUME). SQ SEQUENCE 843 AA; 89093 MW; 4AD4EB02CD4ED70E CRC64; MHHHSSPSSS SEVRAMQARI PNHFREPASG PLRKLSVDLI KTYKHINEVY YAKKKRRAQQ TQGDDDSSNK KERKLYNDGY DDDNHDYIIK NGEKFLDRYE IDSLIGKGSF GQVVKAYDHE EQCHVAIKII KNKKPFLNQA QIEVKLLEMM NRADAENKYY IVKLKRHFMW RNHLCLVFEL LSYNLYDLLR NTNFRGVSLN LTRKFAQQLC TALLFLSTPE LNIIHCDLKP ENILLCNPKR SAIKIVDFGS SCQLGQRIYH YIQSRFYRSP EVLLGIQYDL AIDMWSLGCI LVEMHTGEPL FSGCNEVDQM NKIVEVLGMP PKYLLDQAHK TRKFFDKIVA DGSYVLKKNQ NGRKYKPPGS RKLHDILGVE TGGPGGRRLD EPGHSVSDYL KFKDLILRML DFDPKTRVTP YYALQHNFFK RTADEATNTS GAGATANAGA GGSGSSGAGG SSGGGVGGGL GASNSSSGAV SSSSAAAPTA ATAAATAAGS SGSGSSVGGG SSAAQQQQAM PLPLPLPLPL PPLAGPGGAS DGQCHGLLMH SVAANAMNNF SALSLQSNAH PPPSLANSHH STNSLGSLNH ISPGSTGCHN NNSNSSNNNT RHSRLYGSNM VNMVGHHNSG SSNNHNSISY PHAMECDPPQ MPPPPPNGHG RMRVPAIMQL QPNSYAPNSV PYYGNMSSSS VAAAAAAAAA AASHLMMTDS SVISASAAGG GQGGGNPGQN PVTPSAAAFL FPSQPAGTLY GTALGSLSDL PLPMPLPMSV PLQLPPSSSS SVSSGSASVG SGGVGVGVVG QRRHITGPAA QVGISQSVGS GSSGSATGAS SSDASSSSPM VGVCVQQNPV VIH // ID MO25_DROME STANDARD; PRT; 339 AA. AC P91891; Q9VV85; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE MO25 protein (dMo25). GN MO25 OR CG4083. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96268479; PubMed=8672247; RA Nozaki M., Onishi Y., Togashi S., Miyamoto H.; RT "Molecular characterization of the Drosophila Mo25 gene, which is RT conserved among Drosophila, mouse, and yeast."; RL DNA Cell Biol. 15:505-509(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE MO25 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB000402; BAA19098.1; -. DR EMBL; AE003526; AAF49432.1; -. DR FlyBase; FBgn0017572; Mo25. DR InterPro; IPR008938; ARM. DR InterPro; IPR004892; Mo25. DR Pfam; PF03204; Mo25; 1. FT CONFLICT 51 51 Y -> H (IN REF. 1). FT CONFLICT 102 102 V -> L (IN REF. 1). SQ SEQUENCE 339 AA; 39385 MW; 5790BD91754C1C74 CRC64; MPLFGKSQKS PVELVKSLKE AINALEAGDR KVEKAQEDVS KNLVSIKNML YGSSDAEPPA DYVVAQLSQE LYNSNLLLLL IQNLHRIDFE GKKHVALIFN NVLRRQIGTR SPTVEYICTK PEILFTLMAG YEDAHPEIAL NSGTMLRECA RYEALAKIML HSDEFFKFFR YVEVSTFDIA SDAFSTFKEL LTRHKLLCAE FLDANYDKFF SQHYQRLLNS ENYVTRRQSL KLLGELLLDR HNFTVMTRYI SEPENLKLMM NMLKEKSRNI QFEAFHVFKV FVANPNKPKP ILDILLRNQT KLVDFLTNFH TDRSEDEQFN DEKAYLIKQI KELKPLPEA // ID MODU_DROME STANDARD; PRT; 542 AA. AC P13469; Q9V9S2; DT 01-JAN-1990 (Rel. 13, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-binding protein modulo. GN MOD OR CG2050. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90045936; PubMed=2510126; RA Krejci E., Garzino V., Mary C., Bennani N., Pradel J.; RT "Modulo, a new maternally expressed Drosophila gene encodes a DNA- RT binding protein with distinct acidic and basic regions."; RL Nucleic Acids Res. 17:8101-8116(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP POSSIBLE FUNCTION. RX MEDLINE=95113187; PubMed=7813788; RA Graba Y., Laurenti P., Perrin L., Aragnol D., Pradel J.; RT "The modifier of variegation modulo gene acts downstream of RT dorsoventral and HOM-C genes and is required for morphogenesis in RT Drosophila."; RL Dev. Biol. 166:704-715(1994). CC -!- FUNCTION: ITS CAPACITY TO BIND DNA AND PROTEIN(S), AND ITS CC DIFFERENTIAL EXPRESSION DURING DEVELOPMENT SUGGEST A ROLE IN THE CC REGULATION OF GENE EXPRESSION DURING DROSOPHILA DEVELOPMENT. IT CC COULD, IN INTERACTION WITH OTHER FACTORS, BE REQUIRED FOR THE CC TRANSLATION OF INSTRUCTIONS PROVIDED BY PATTERN FORMING GENES AND CC CONTROLS, VIA CHROMATIN CHANGES, THE ACTIVITY OF GENES CRITICAL CC FOR THE PROCESS OF MORPHOGENESIS OF SEVERAL EMBRYONIC CC TERRITORIES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: PHOSPHORYLATED. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -!- SIMILARITY: CONTAINS 4 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15702; CAA33732.1; -. DR EMBL; AE003780; AAF57213.1; -. DR EMBL; AY058519; AAL13748.1; -. DR PIR; S06602; S06602. DR HSSP; P09012; 1URN. DR FlyBase; FBgn0002780; mod. DR GO; GO:0003677; F:DNA binding; IDA. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 4. DR SMART; SM00360; RRM; 4. DR PROSITE; PS50102; RRM; 4. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW DNA-binding; RNA-binding; Nuclear protein; Phosphorylation; Repeat. FT DOMAIN 175 251 RNA-BINDING (RRM) 1. FT DOMAIN 258 331 RNA-BINDING (RRM) 2. FT DOMAIN 340 429 RNA-BINDING (RRM) 3. FT DOMAIN 420 489 RNA-BINDING (RRM) 4. FT DOMAIN 60 134 ASP/GLU-RICH (ACIDIC). FT MOD_RES 330 330 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT CONFLICT 74 74 P -> A (IN REF. 1). FT CONFLICT 329 329 I -> V (IN REF. 1). FT CONFLICT 505 542 RAPRKFQKDTKPNFGKKPFNKRPAQENGGKSFVKRARF -> FT APRGSSKRTLSQTLVKNHLTSARHKRMVVNRLLKGQDFRT FT (IN REF. 1). SQ SEQUENCE 542 AA; 60309 MW; E5E383B2A0595E2E CRC64; MAQKKAVTVK GKKATNGEEK PLAKRVTKST KVQEEETVVP QSPSKKSRKQ PVKEVPQFSE EDESDVEEQN DEQPGDDSDF ETEEAAGLID DEAEEDEEYN SDDEEDDDDD ELEPGEVSKS EGADEVDESD DDEEAPVEKP VSKKSEKANS EKSEENRGIP KVKVGKIPLG TPKNQIVFVT NLPNEYLHKD LVALFAKFGR LSALQRFTNL NGNKSVLIAF DTSTGAEAVL QAKPKALTLG DNVLSVSQPR NKEENNERTV VVGLIGPNIT KDDLKTFFEK VAPVEAVTIS SNRLMPRAFV RLASVDDIPK ALKLHSTELF SRFITVRRIS QESISRTSEL TLVVENVGKH ESYSSDALEK IFKKFGDVEE IDVVCSKAVL AFVTFKQSDA ATKALAQLDG KTVNKFEWKL HRFERSTSGR AILVTNLTSD ATEADLRKVF NDSGEIESII MLGQKAVVKF KDDEGFCKSF LANESIVNNA PIFIEPNSLL KHRLLKKRLA IGQTRAPRKF QKDTKPNFGK KPFNKRPAQE NGGKSFVKRA RF // ID MOEH_DROME STANDARD; PRT; 578 AA. AC P46150; P91930; Q24053; Q24435; Q9W3B4; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Moesin/ezrin/radixin homolog 1 (Ezrin-moesin-radixin-1) (D17 protein) DE (Moesin protein) (dMoesin). GN MOE OR EMR1 OR CG10701. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=96234672; PubMed=8666669; RA McCartney B.M., Fehon R.G.; RT "Distinct cellular and subcellular patterns of expression imply RT distinct functions for the Drosophila homologues of moesin and the RT neurofibromatosis 2 tumor suppressor, merlin."; RL J. Cell Biol. 133:843-852(1996). RN [2] RP REVISIONS TO 183-184. RA Fehon R.G.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 208-296 FROM N.A. RA Winge P., Fleming J.T., Gobel V.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE OF 256-578 FROM N.A. (ISOFORM 2). RC TISSUE=Embryo; RX MEDLINE=94240181; PubMed=8183953; RA Edwards K.A., Montague R.A., Shepard S., Edgar B.A., Erikson R.L., RA Kiehart D.P.; RT "Identification of Drosophila cytoskeletal proteins by induction of RT abnormal cell shape in fission yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 91:4589-4593(1994). CC -!- FUNCTION: INVOLVED IN CONNECTIONS OF MAJOR CYTOSKELETAL STRUCTURES CC TO THE PLASMA MEMBRANE. CC -!- SUBUNIT: INTERACTS WITH MER AND ARM AT THE ADHERENS JUNCTION. CC INTERACTS WITH CYTOSKELETAL ACTIN AT APICAL BUDS OF MICROVILLI IN CC THE PRECELLULARISED EMBRYO. CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED; ADHERENS JUNCTIONS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P46150-1; Sequence=Displayed; CC Name=2; Synonyms=D; CC IsoId=P46150-2; Sequence=VSP_007499; CC -!- TISSUE SPECIFICITY: EXPRESSED IN APICAL AND BASOLATERAL ENDS OF CC FOLLICULAR EPITHELIUM DURING OOGENESIS. IN EMBRYONIC CNS, CC EXPRESSION IS SEEN IN THE NEUROPIL, DEVELOPING BRAIN AND NEURONAL CC CELL BODIES. IN EMBRYONIC PNS, EXPRESSION IS SEEN AT THE CELL CC MEMBRANE. IN THIRD INSTAR LARVAE, EYE IMAGINAL DISK EXPRESSION IS CC SEEN AT THE MEMBRANES OF DEVELOPING PHOTORECEPTORS POSTERIOR TO CC THE MORPHOGENETIC FURROW. IN PUPAL EYES, EXPRESSON IS AT THE CC MEMBRANE OF CONE CELLS, SECONDARY AND TERTIARY PIGMENT CELLS, CC BRISTLE PRECURSOR CELLS AND RHABDOMERES. CC -!- SIMILARITY: CONTAINS 1 FERM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L38909; AAB48934.1; -. DR EMBL; AE003445; AAF46415.2; -. DR EMBL; AY069855; AAL40000.1; -. DR EMBL; U23798; AAA65059.1; -. DR EMBL; U08218; AAA19857.1; -. DR FlyBase; FBgn0011661; Moe. DR GO; GO:0005912; C:adherens junction; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0045197; P:establishment and/or maintenance of epithel...; IDA. DR GO; GO:0016336; P:establishment and/or maintenance of polarit...; IMP. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR008954; Moesin. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF00769; ERM; 1. DR PRINTS; PR00935; BAND41. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Structural protein; Membrane; Cytoskeleton; Actin-binding; KW Alternative splicing. FT DOMAIN 1 296 FERM. FT VARSPLIC 451 453 Missing (in isoform 2). FT /FTId=VSP_007499. FT CONFLICT 217 219 LWL -> SLV (IN REF. 6). SQ SEQUENCE 578 AA; 68141 MW; 24FBA67A3CDF3809 CRC64; MSPKALNVRV TTMDAELEFA IQSTTTGKQL FDQVVKTIGL REVWFFGLQY TDSKGDSTWI KLYKKVMNQD VKKENPLQFR FRAKFYPEDV AEELIQDITL RLFYLQVKNA ILTDEIYCPP ETSVLLASYA VQARHGDHNK TTHTAGFLAN DRLLPQRVID QHKMSKDEWE QSIMTWWQEH RSMLREDAMM EYLKIAQDLE MYGVNYFEIR NKKGTDLWLG VDALGLNIYE QDDRLTPKIG FPWSEIRNIS FSEKKFIIKP IDKKAPDFMF FAPRVRINKR ILALCMGNHE LYMRRRKPDT IDVQQMKAQA REEKNAKQQE REKLQLALAA RERAEKKQQE YEDRLKQMQE DMERSQRDLL EAQDMIRRLE EQLKQLQAAK DELELRQKEL QAMLQRLEEA KNMEAVEKLK LEEEIMAKQM EVQRIQDEVN AKDEETKRLQ DEVEDARRKQ VIAAEAAAAL LAASTTPQHH HVAEDENENE EELTNGDAGG DVSRDLDTDE HIKDPIEDRR TLAERNERLH DQLKALKQDL AQSRDETKET ANDKIHRENV RQGRDKYKTL REIRKGNTKR RVDQFENM // ID MOF_DROME STANDARD; PRT; 827 AA. AC O02193; Q9W463; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Males-absent on the first protein (EC 2.3.1.-) (Putative acetyl DE transferase MOF). GN MOF OR CG3025. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97299882; PubMed=9155031; RA Hilfiker A., Hilfiker-Kleiner D., Pannuti A., Lucchesi J.C.; RT "mof, a putative acetyl transferase gene related to the Tip60 and MOZ RT human genes and to the SAS genes of yeast, is required for dosage RT compensation in Drosophila."; RL EMBO J. 16:2054-2060(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE HISTONE ACETYLTRANSFERASE THAT PLAYS A DIRECT CC ROLE IN THE SPECIFIC HISTONE ACETYLATION ASSOCIATED WITH DOSAGE CC COMPENSATION. DOSAGE COMPENSATION INSURES THAT MALES WITH A SINGLE CC X CHROMOSOME HAVE THE SAME AMOUNT OF MOST X-LINKED GENE PRODUCTS CC AS FEMALES WITH TWO X CHROMOSOMES. MAY BE DIRECTLY INVOLVED IN THE CC ACETYLATION OF HISTONE 4 AT LYS 16 ON THE X CHROMOSOME OF CC DROSOPHILA MALES. CC -!- SIMILARITY: BELONGS TO THE MYST (SAS/MOZ) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U71219; AAC47507.1; -. DR EMBL; AE003435; AAF46095.1; -. DR FlyBase; FBgn0014340; mof. DR GO; GO:0016456; C:dosage compensation complex (sensu Drosophila); NAS. DR GO; GO:0009047; P:dosage compensation, by hyperactivation of ...; NAS. DR InterPro; IPR000953; Chromo. DR InterPro; IPR002717; MOZ_SAS. DR Pfam; PF01853; MOZ_SAS; 1. DR SMART; SM00298; CHROMO; 1. KW Transferase; Acyltransferase; Zinc-finger. FT ZN_FING 572 594 C2HC-TYPE. FT DOMAIN 112 116 POLY-SER. FT DOMAIN 135 141 POLY-GLN. FT DOMAIN 245 252 POLY-PRO. FT DOMAIN 340 346 POLY-GLU. FT DOMAIN 466 472 POLY-ALA. FT VARIANT 691 691 G -> E (MALES FAIL TO METAMORPHOSE AND FT HATCH). SQ SEQUENCE 827 AA; 92656 MW; 8B9C5E87E3B01317 CRC64; MSEAELEQTP SAGHVQEQPI EEEHEPEQEP TDAYTIGGPP RTPVEDAAAE LSASLDVSGS DQSAEQSLDL SGVQAEAAAE SEPPAKRQHR DISPISEDST PASSTSTSST RSSSSSRYDD VSEAEEAPPE PEPEQPQQQQ QEEKKEDGQD QVKSPGPVEL EAQEPAQPQK QKEVVDQEIE TEDEPSSDTV ICVADINPYG SGSNIDDFVM DPDAPPNAII TEVVTIPAPL HLKGTQQLGL PLAAPPPPPP PPAAEQVPET PASPTDDGEE PPAVYLSPYI RSRYMQESTP GLPTRLAPRD PRQRNMPPPA VVLPIQTVLS ANVEAISDDS SETSSSDDDE EEEEDEDDAL TMEHDNTSRE TVITTGDPLM QKIDISENPD KIYFIRREDG TVHRGQVLQS RTTENAAAPD EYYVHYVGLN RRLDGWVGRH RISDNADDLG GITVLPAPPL APDQPSTSRE MLAQQAAAAA AASSERQKRA ANKDYYLSYC ENSRYDYSDR KMTRYQKRRY DEINHVQKSH AELTATQAAL EKEHESITKI KYIDKLQFGN YEIDTWYFSP FPEEYGKART LYVCEYCLKY MRFRSSYAYH LHECDRRRPP GREIYRKGNI SIYEVNGKEE SLYCQLLCLM AKLFLDHKVL YFDMDPFLFY ILCETDKEGS HIVGYFSKEK KSLENYNVAC ILVLPPHQRK GFGKLLIAFS YELSRKEGVI GSPEKPLSDL GRLSYRSYWA YTLLELMKTR CAPEQITIKE LSEMSGITHD DIIYTLQSMK MIKYWKGQNV ICVTSKTIQD HLQLPQFKQP KLTIDTDYLV WSPQTAAAVV RAPGNSG // ID MP20_DROME STANDARD; PRT; 184 AA. AC P14318; Q9V6M7; DT 01-JAN-1990 (Rel. 13, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Muscle-specific protein 20. GN MP20 OR TPN OR CG4696. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Muscle; RX MEDLINE=89139570; PubMed=2537318; RA Ayme-Southgate A., Lasko P., French C., Pardue M.L.; RT "Characterization of the gene for mp20: a Drosophila muscle protein RT that is not found in asynchronous oscillatory flight muscle."; RL J. Cell Biol. 108:521-531(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: FOUND IN SYNCHRONOUS MUSCLE; NOT FOUND IN CC ASYNCHRONOUS INDIRECT FLIGHT MUSCLE. CC -!- SIMILARITY: BELONGS TO THE CALPONIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 CALPONIN-HOMOLOGY (CH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00795; CAA68746.1; -. DR EMBL; AE003819; AAF58396.1; -. DR PIR; A30128; A30128. DR FlyBase; FBgn0002789; Mp20. DR InterPro; IPR001715; Calponin-like. DR InterPro; IPR000557; Calponin_repeat. DR InterPro; IPR003247; CH_type. DR InterPro; IPR003096; SM22_calponin. DR Pfam; PF00402; calponin; 1. DR Pfam; PF00307; CH; 1. DR PRINTS; PR00888; SM22CALPONIN. DR ProDom; PD001527; CH_type; 1. DR SMART; SM00033; CH; 1. DR PROSITE; PS01052; CALPONIN; 1. DR PROSITE; PS50021; CH; 1. KW Muscle protein. FT DOMAIN 17 122 CH. FT REPEAT 157 182 CALPONIN-LIKE 26 AA MOTIF. FT CONFLICT 13 13 S -> G (IN REF. 1). SQ SEQUENCE 184 AA; 20190 MW; B291ACA92AED3873 CRC64; MSLERAVRAK IASKRNPEMD KEAQEWIEAI IAEKFPAGQS YEDVLKDGQV LCKLINVLSP NAVPKVNSSG GQFKFMENIN NFQKALKEYG VPDIDVFQTV DLYEKKDIAN VTNTIFALGR ATYKHADFKG PFLGPKPADE CKRDFTEEQL KAGQTIVGLQ AGSNKGATQA GQNLGAGRKI LLGK // ID MPIP_DROME STANDARD; PRT; 479 AA. AC P20483; Q9VAL9; DT 01-FEB-1991 (Rel. 17, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE M-phase inducer phosphatase (EC 3.1.3.48) (String protein) (Cdc25-like DE protein). GN STG OR CDC25 OR CG1395. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89195217; PubMed=2702688; RA Edgar B.A., O'Farrell P.H.; RT "Genetic control of cell division patterns in the Drosophila embryo."; RL Cell 57:177-187(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91006056; PubMed=2120044; RA Jimenez J., Alphey L., Nurse P., Glover D.M.; RT "Complementation of fission yeast cdc2ts and cdc25ts mutants RT identifies two cell cycle genes from Drosophila: a cdc2 homologue and RT string."; RL EMBO J. 9:3565-3571(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS PROTEIN FUNCTIONS AS A DOSAGE-DEPENDENT INDUCER IN CC MITOTIC CONTROL. IT IS A TYROSINE PROTEIN PHOSPHATASE REQUIRED FOR CC PROGRESSION OF THE CELL CYCLE. IT MAY DIRECTLY DEPHOSPHORYLATE CC P34(CDC2) AND ACTIVATE THE P34(CDC2) KINASE ACTIVITY. CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- SIMILARITY: BELONGS TO THE MPI PHOSPHATASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 RHODANESE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24909; AAA28916.1; -. DR EMBL; X57495; CAA40732.1; -. DR EMBL; AE003768; AAF56885.1; -. DR PIR; A32290; A32290. DR HSSP; P30304; 1C25. DR FlyBase; FBgn0003525; stg. DR GO; GO:0005708; C:mitotic chromosome; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA. DR GO; GO:0007099; P:centriole replication; IMP. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP. DR GO; GO:0007369; P:gastrulation; NAS. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA. DR InterPro; IPR000751; MPI_Phosphatase. DR InterPro; IPR001763; Rhodanese-like. DR Pfam; PF00581; Rhodanese; 1. DR PRINTS; PR00716; MPIPHPHTASE. DR SMART; SM00450; RHOD; 1. DR PROSITE; PS50206; RHODANESE_3; 1. KW Cell division; Mitosis; Hydrolase. FT DOMAIN 316 432 RHODANESE. FT ACT_SITE 379 379 BY SIMILARITY. FT CONFLICT 228 228 A -> T (IN REF. 1). SQ SEQUENCE 479 AA; 54094 MW; 68483F3A285962CC CRC64; MLWETIVEEN NCSMDCNISN NTSSSSSINK MSGSRRARRS LELMSMDQEE LSFYDDDVVP QDQQRSASPE LMGLLSPEGS PQRFQIVRQP KILPAMGVSS DHTPARSFRI FNSLSSTCSM ESSMDDEYME LFEMESQSQQ TALGFPSGLN SLISGQIKEQ PAAKSPAGLS MRRPSVRRCL SMTESNTNST TTPPPKTPET ARDCFKRPEP PASANCSPIQ SKRHRCAAVE KENCPAPSPL SQVTISHPPP LRKCMSLNDA EIMSALARSE NRNEPELIGD FSKAYALPLM EGRHRDLKSI SSETVARLLK GEFSDKVASY RIIDCRYPYE FEGGHIEGAK NLYTTEQILD EFLTVQQTEL QQQQNAESGH KRNIIIFHCE FSSERGPKMS RFLRNLDRER NTNAYPALHY PEIYLLHNGY KEFFESHVEL CEPHAYRTML DPAYNEAYRH FRAKSKSWNG DGLGGATGRL KKSRSRLML // ID MR15_DROME STANDARD; PRT; 424 AA. AC Q9Y0I1; Q9VF99; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE MRG15 protein. GN MRG15 OR CG6363. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Bertram M.J., Pereira-Smith O.M.; RT "Conservation of the MORF4 related gene family: identification of a RT new chromo domain subfamily and novel protein motif."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE MRG FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF152245; AAD38047.1; -. DR EMBL; AE003708; AAF55161.1; -. DR EMBL; AY051679; AAK93103.1; -. DR FlyBase; FBgn0027378; MRG15. DR InterPro; IPR000953; Chromo. DR InterPro; IPR008676; MRG. DR Pfam; PF05712; MRG; 1. DR SMART; SM00298; CHROMO; 1. KW Nuclear protein. SQ SEQUENCE 424 AA; 47194 MW; B0E1F615252D8EDD CRC64; MGEVKPAKVE NYSTGTDANT LFVDGERVLC FHGPLIYEAK VLKTKPDATP VEYYIHYAGW SKNWDEWVPE NRVLKYNDDN VKRRQELARQ CGERSKKDNK KGSAKAKKME QMRNESRAST PSKDSNTSQS TASSTPTTSA GPGSKSEAGS TGTTTTNSTA NSTTSRAHRK STQSTPSTAR PGTPSDKKED PAAAETTEEE GPVAPKKKRM SEQRPSLTGS DVAEKPLPPT TTPSTPTTEP APCVESEEAY AAKVEVKIKI PDELKHYLTD DWYAVVREHK LLELPAKVTV QQISEQYLAH KKSVKSTSAS KEVAINDVLD GIVEYFNVML GSQLLYKFER TQYADVMQKH PDTPLSELYG SFHLLRLFVR LGSMLSYSAL DQQSMQNLLT HVQDFLKFLV KNSSIFFSMS NFINVDPEYV RNAQ // ID MS2A_DROME STANDARD; PRT; 264 AA. AC P10333; O76297; O76298; O76299; Q9UB48; Q9UB76; Q9VML6; DT 01-MAR-1989 (Rel. 10, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland-specific peptide 26Aa precursor (Male accessory DE gland secretory protein 355A). GN ACP26AA OR MST26AA OR MST355A OR CG8982. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89053045; PubMed=3142802; RA Monsma S.A., Wolfner M.F.; RT "Structure and expression of a Drosophila male accessory gland gene RT whose product resembles a peptide pheromone precursor."; RL Genes Dev. 2:1063-1073(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=NC1, NC2, NC3, NC4, NC5, NC6, NC7, NC8, NC9, and NC10; RX MEDLINE=93106377; PubMed=1361475; RA Aguade M., Miyashita N., Langley C.H.; RT "Polymorphism and divergence in the Mst26A male accessory gland gene RT region in Drosophila."; RL Genetics 132:755-770(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=MO52B, and MA60; RX MEDLINE=99016087; PubMed=9799260; RA Aguade M.; RT "Different forces drive the evolution of the Acp26Aa and Acp26Ab RT accessory gland genes in the Drosophila melanogaster species RT complex."; RL Genetics 150:1079-1089(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 8-264 FROM N.A. RC STRAIN=AF1/ZH3, AF2/ZH12, AF3/ZH24, AF4/ZH26, AF5/ZS2, AF6/ZS6, RC AF7/ZS10, AF8/ZS24, AF9/ZS28, AF10/ZS49, AU1, AU2, AU3, AU4, AU5, RC AU6, AU7, AU8, AU9, AU10, NY1/NY CLOSS3, NY2, NY3, NY4, NY5, NY6, RC NY7, NY8, TW1/TW 253.4, TW2/TW 253.6, TW3/TW 253.8, TW4/TW 253.9, RC TW5/TW 253.24, TW6/TW 253.27, TW7/TW 253.28, TW8/TW 253.29, RC TW9/TW 253.35, TW10/TW 253.36, TW11/TW 253.37, NC1, NC2, NC3, NC4, RC NC5, NC6, NC7, NC8, NC98, and NC10; RX MEDLINE=98384843; PubMed=9718731; RA Tsaur S.-C., Ting C.-T., Wu C.-I.; RT "Positive selection driving the evolution of a gene of male RT reproduction, Acp26Aa, of Drosophila. II. Divergence versus RT polymorphism."; RL Mol. Biol. Evol. 15:1040-1045(1998). CC -!- FUNCTION: THIS PROTEIN IS TRANSFERRED FROM MALE TO FEMALE'S CC HEMOLYMPH DURING MATING, AFFECTING EGGLAYING AND BEHAVIOR AFTER CC MATING. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: MAIN CELLS OF THE ACCESSORY GLANDS OF MALES. CC -!- PTM: IT UNDERGOES SEVERAL CLEAVAGES AS IT IS SECRETED AND IT CC IS FURTHER PROCESSED IN THE RECIPIENT FEMALE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00219; CAA68366.1; -. DR EMBL; X70888; CAA50232.1; -. DR EMBL; X70889; CAA50234.1; -. DR EMBL; X70890; CAA50236.1; -. DR EMBL; X70891; CAA50238.1; -. DR EMBL; X70892; CAA50240.1; -. DR EMBL; X70893; CAA50242.1; -. DR EMBL; X70894; CAA50244.1; -. DR EMBL; X70895; CAA50246.1; -. DR EMBL; X70896; CAA50248.1; -. DR EMBL; X70897; CAA50250.1; -. DR EMBL; AJ231357; CAB37208.1; -. DR EMBL; AJ231400; CAB37292.1; -. DR EMBL; AE003611; AAF52298.1; -. DR EMBL; AF052470; AAC27995.1; -. DR EMBL; AF052471; AAC27997.1; -. DR EMBL; AF052472; AAC27999.1; -. DR EMBL; AF052473; AAC28001.1; -. DR EMBL; AF052474; AAC28003.1; -. DR EMBL; AF052475; AAC28005.1; -. DR EMBL; AF052476; AAC28007.1; -. DR EMBL; AF052477; AAC28009.1; -. DR EMBL; AF052478; AAC28011.1; -. DR EMBL; AF052479; AAC28013.1; -. DR EMBL; AF052480; AAC28015.1; -. DR EMBL; AF052481; AAC28017.1; -. DR EMBL; AF053250; AAC28790.1; -. DR EMBL; AF053251; AAC28792.1; -. DR EMBL; AF053252; AAC28794.1; -. DR EMBL; AF053253; AAC28796.1; -. DR EMBL; AF053254; AAC28798.1; -. DR EMBL; AF053255; AAC28800.1; -. DR EMBL; AF053256; AAC28802.1; -. DR EMBL; AF053257; AAC28804.1; -. DR EMBL; AF053258; AAC28806.1; -. DR EMBL; AF053259; AAC28808.1; -. DR EMBL; AF053260; AAC28810.1; -. DR EMBL; AF053261; AAC28812.1; -. DR EMBL; AF053262; AAC28814.1; -. DR EMBL; AF053263; AAC28816.1; -. DR EMBL; AF053264; AAC28818.1; -. DR EMBL; AF053265; AAC28820.1; -. DR EMBL; AF053266; AAC28822.1; -. DR EMBL; AF053267; AAC28824.1; -. DR EMBL; AF053268; AAC28826.1; -. DR EMBL; AF053269; AAC28828.1; -. DR EMBL; AF053270; AAC28830.1; -. DR EMBL; AF053271; AAC28832.1; -. DR EMBL; AF053272; AAC28834.1; -. DR EMBL; AF053273; AAC28836.1; -. DR EMBL; AF053274; AAC28838.1; -. DR EMBL; AF053275; AAC28840.1; -. DR EMBL; AF053276; AAC28842.1; -. DR PIR; S02853; S02853. DR FlyBase; FBgn0002855; Acp26Aa. DR GO; GO:0045297; P:post-mating behavior; NAS. DR GO; GO:0046662; P:regulation of oviposition; NAS. DR GO; GO:0007321; P:sperm displacement; NAS. DR InterPro; IPR004315; Male_ac_gland_sc. DR Pfam; PF03082; MAGSP; 1. DR ProDom; PD017367; Male_ac_gland_sc; 1. KW Glycoprotein; Behavior; Signal; Polymorphism. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 264 ACCESSORY GLAND-SPECIFIC PEPTIDE 26AA. FT CARBOHYD 88 88 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 122 122 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 138 138 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 145 145 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 19 19 S -> N (IN STRAINS AF1, AF4, AF6, AF8, FT AF9, AU1, AU3, AU7, AU9, NY1, NY6, NY8, FT TW2, TW3, TW6, TW9, TW10, NC5, NC7 AND FT NC10). FT VARIANT 24 24 Q -> K (IN STRAINS NC5, NC7 AND NC10). FT VARIANT 25 25 Q -> K (IN STRAINS AU6, NY1, NY2, NY6, FT NY8, TW2, TW3, TW4, TW7, TW9 AND TW10). FT VARIANT 32 32 L -> Q (IN STRAINS AF2, AF7, AU4, MO52B, FT NC9, NY3, NY5 AND TW11). FT VARIANT 39 39 S -> G (IN STRAIN NY2). FT VARIANT 40 40 A -> S (IN STRAIN AU3). FT VARIANT 44 46 NVA -> SVT (IN STRAIN AU3). FT VARIANT 46 46 A -> P (IN STRAINS AF1, AF3, AF4, AF5, FT AF6, AF8, AF9, AF10, AU1, AU2, AU3, AU4, FT AU6, AU7, AU8, AU10, MA60, MO52B, NY1, FT NY2, NY4, NY6, NY8, TW1, TW2, TW3, TW4, FT TW5, TW6, TW7, TW8, TW9, NC1, NC4, NC5, FT NC6, NC7, NC8 AND NC10). FT VARIANT 46 46 A -> T (IN STRAINS AF2, AF7, AU5, AU9, FT NC2, NC3, NC9, NY3, NY5, NY7, TW10 AND FT TW11). FT VARIANT 56 56 I -> L (IN STRAIN AU3). FT VARIANT 65 65 D -> G (IN STRAIN AF8). FT VARIANT 76 76 D -> N (IN STRAIN NC3). FT VARIANT 79 79 D -> N (IN STRAINS AU2, AU3, AU8, NC4, FT NC6, NC8, NY4, TW1, TW5 AND TW8). FT VARIANT 101 101 N -> S (IN STRAINS AF1, AF2, AF3, AF5, FT AF6, AF7, AF8, AF9, AF10, AU3, AU4, AU6, FT AU7, MO52B, NC1, NC2, NC3, NC9, NY2, NY3, FT NY5, NY6, TW3, TW4, TW6, TW7, TW10 AND FT TW11). FT VARIANT 109 109 L -> I (IN STRAINS AF1, AF2, AF3, AF5, FT AF6, AF7, AF8, AF9, AF10, AU2, AU4, AU6, FT AU7, AU8, MO52B, NC1, NC2, NC4, NC6, NC8, FT NC9, NY2, NY3, NY4, NY5, TW1, TW3, TW4, FT TW5, TW6, TW7, TW8, TW10 AND TW11). FT VARIANT 172 172 E -> Q (IN STRAINS AU1, AU3 AND AU9). FT VARIANT 207 207 S -> I (IN STRAINS AU5, NC2 AND NY2). FT VARIANT 212 212 A -> V (IN STRAIN NY2). FT VARIANT 221 221 R -> K (IN STRAIN NY2, NC2, NC11 AND FT NC10). FT VARIANT 226 226 N -> Y (IN STRAIN TW9). FT VARIANT 253 253 E -> D (IN STRAINS AF6, AF8, AF9, AU4, FT TW1 AND TW11). FT VARIANT 262 262 P -> S (IN STRAINS AF5, AF10, AU5 AND FT TW10). SQ SEQUENCE 264 AA; 29618 MW; 97377826FAE93EB6 CRC64; MNQILLCSPI LLLLFTVASC DSEQQLDSAM HLKSDSTKSA SLKNVAPKND ETQAKIAKDD VALKDAKKGD YIMDIDISDL PLDDYPINRS KSLKSSSIDL NNIPFNKGLD DFPAKEKNQG SNQSALKALQ QRLLTEQNNS LLLRNHSIYL MKEIEARKTD IIKVRQLNLD LELELNTVNR RLLELNGQLQ NTRKSTKPCK KRSSKDSAPP AANQFQEANV RNTYRNKYLT LLKELSQKIN NEIAKVATDV PTETNPSQGN LPTL // ID MS2B_DROME STANDARD; PRT; 90 AA. AC P10334; O76300; O76302; O77456; Q9V432; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland-specific peptide 26Ab precursor (Male accessory DE gland secretory protein 355B). GN ACP26AB OR MST26AB OR MST355B OR CG9024. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89053045; PubMed=3142802; RA Monsma S.A., Wolfner M.F.; RT "Structure and expression of a Drosophila male accessory gland gene RT whose product resembles a peptide pheromone precursor."; RL Genes Dev. 2:1063-1073(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=NC1, NC2, NC3, NC4, NC5, NC6, NC7, NC8, NC9, and NC10; RX MEDLINE=93106377; PubMed=1361475; RA Aguade M., Miyashita N., Langley C.H.; RT "Polymorphism and divergence in the Mst26A male accessory gland gene RT region in Drosophila."; RL Genetics 132:755-770(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=AF1/ZH3, AF2/ZH12, AF3/ZH24, AF4/ZH26, AF5/ZS2, AF6/ZS6, RC AF7/ZS10, AF8/ZS24, AF9/ZS28, AF10/ZS49, AU1, AU2, AU3, AU4, AU5, AU6, RC AU7, AU8, AU9, AU10, NY1/NY CLOSS3, NY2, NY3, NY4, NY5, NY6, NY7, NY8, RC TW1/TW 253.4, TW2/TW 253.6, TW3/TW 253.8, TW4/TW 253.9, TW5/TW 253.24, RC TW6/TW 253.27, TW7/TW 253.28, TW8/TW 253.29, TW9/TW 253.35, RC TW10/TW 253.36, TW11/TW 253.37, NC1, NC2, NC3, NC4, NC5, NC6, NC7, RC NC8, NC98, and NC10; RX MEDLINE=98384843; PubMed=9718731; RA Tsaur S.-C., Ting C.-T., Wu C.-I.; RT "Positive selection driving the evolution of a gene of male RT reproduction, Acp26Aa, of Drosophila: II. Divergence versus RT polymorphism."; RL Mol. Biol. Evol. 15:1040-1046(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=MO36A, MO37A, MO47A, MO79B, MO80B, LA25, LA46, and LA108; RX MEDLINE=99016087; PubMed=9799260; RA Aguade M.; RT "Different forces drive the evolution of the Acp26Aa and Acp26Ab RT accessory gland genes in the Drosophila melanogaster species RT complex."; RL Genetics 150:1079-1089(1998). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS PROTEIN IS TRANSFERRED FROM MALE TO FEMALE DURING CC MATING AND MAY AFFECT EGGLAYING AND BEHAVIOR AFTER MATING. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: MAIN CELLS OF THE ACCESSORY GLANDS OF MALES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00219; CAA68367.1; -. DR EMBL; X70888; CAA50233.1; -. DR EMBL; X70889; CAA50235.1; -. DR EMBL; X70890; CAA50237.1; -. DR EMBL; X70891; CAA50239.1; -. DR EMBL; X70892; CAA50241.1; -. DR EMBL; X70893; CAA50243.1; -. DR EMBL; X70894; CAA50245.1; -. DR EMBL; X70895; CAA50247.1; -. DR EMBL; X70896; CAA50249.1; -. DR EMBL; X70897; CAA50251.1; -. DR EMBL; AF052470; AAC27996.1; -. DR EMBL; AF052471; AAC27998.1; -. DR EMBL; AF052472; AAC28000.1; -. DR EMBL; AF052473; AAC28002.1; -. DR EMBL; AF052474; AAC28004.1; -. DR EMBL; AF052475; AAC28006.1; -. DR EMBL; AF052476; AAC28008.1; -. DR EMBL; AF052477; AAC28010.1; -. DR EMBL; AF052478; AAC28012.1; -. DR EMBL; AF052479; AAC28014.1; -. DR EMBL; AF052480; AAC28016.1; -. DR EMBL; AF052481; AAC28018.1; -. DR EMBL; AF053250; AAC28791.1; -. DR EMBL; AF053251; AAC28793.1; -. DR EMBL; AF053252; AAC28795.1; -. DR EMBL; AF053253; AAC28797.1; -. DR EMBL; AF053254; AAC28799.1; -. DR EMBL; AF053255; AAC28801.1; -. DR EMBL; AF053256; AAC28803.1; -. DR EMBL; AF053257; AAC28805.1; -. DR EMBL; AF053258; AAC28807.1; -. DR EMBL; AF053259; AAC28809.1; -. DR EMBL; AF053260; AAC28811.1; -. DR EMBL; AF053261; AAC28813.1; -. DR EMBL; AF053262; AAC28815.1; -. DR EMBL; AF053263; AAC28817.1; -. DR EMBL; AF053264; AAC28819.1; -. DR EMBL; AF053265; AAC28821.1; -. DR EMBL; AF053266; AAC28823.1; -. DR EMBL; AF053267; AAC28825.1; -. DR EMBL; AF053268; AAC28827.1; -. DR EMBL; AF053269; AAC28829.1; -. DR EMBL; AF053270; AAC28831.1; -. DR EMBL; AF053271; AAC28833.1; -. DR EMBL; AF053272; AAC28835.1; -. DR EMBL; AF053273; AAC28837.1; -. DR EMBL; AF053274; AAC28839.1; -. DR EMBL; AF053275; AAC28841.1; -. DR EMBL; AF053276; AAC28843.1; -. DR EMBL; AJ231353; CAB37201.1; -. DR EMBL; AJ231354; CAB37203.1; -. DR EMBL; AJ231356; CAB37207.1; -. DR EMBL; AJ231358; CAB37211.1; -. DR EMBL; AJ231359; CAB37213.1; -. DR EMBL; AJ231365; CAB37225.1; -. DR EMBL; AJ231372; CAB37239.1; -. DR EMBL; AJ231379; CAB37251.1; -. DR EMBL; AE003611; AAF52297.1; -. DR PIR; S02854; S02854. DR FlyBase; FBgn0002856; Acp26Ab. DR InterPro; IPR008392; Acp26Ab. DR Pfam; PF05777; Acp26Ab; 1. KW Behavior; Signal; Polymorphism. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 90 ACCESSORY GLAND-SPECIFIC PEPTIDE 26AB. FT VARIANT 64 64 Q -> H (IN STRAINS AF1, AF2, AF3, AF5, FT AF6, AF7, AF8, AF9, AF10, AU4, AU7, AU8, FT NC3, NC4, NC6, NC8, NC9, NY2, NY3, NY4, FT NY5, TW1, TW2, TW5, TW6, TW7, TW8, TW10 FT AND TW11). FT VARIANT 77 77 P -> R (IN STRAIN TW9). FT VARIANT 80 80 I -> V (IN STRAINS NC2, NC3, NC4, NC6, FT NC8, NY2, NY4, TW2, TW4, TW5, TW8, TW10 FT AND TW11). FT VARIANT 89 89 M -> I (IN STRAIN AU4). FT VARIANT 90 90 A -> E (IN STRAINS TW1, TW6, AF1, AF2, FT AF3, AF5, AF6, AF7, AF8, AF9 AND AF10). SQ SEQUENCE 90 AA; 10162 MW; 1FDFDC7951F9BDFF CRC64; MNYFAVICIF SCICLWQFSD AAPFISVQSS SQSRSQKVMN GMLRTLYDYS VQDSVNDATG HLIQTHKADF NSDVMSPDEI ESVRQQLNMA // ID MSDA_DROME STANDARD; PRT; 75 AA. AC Q9VBL6; Q24390; Q8MSH9; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland-specific peptide 57Da precursor (Male accessory gland DE secretory protein 57Da). GN MST57DA OR BCDNA:GH19893 OR CG9074. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; RX MEDLINE=95227188; PubMed=7711745; RA Simmerl E., Schaefer M., Schaefer U.; RT "Structure and regulation of a gene cluster for male accessory gland RT transcripts in Drosophila melanogaster."; RL Insect Biochem. Mol. Biol. 25:127-137(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 2-75 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TRANSFERRED FROM MALE TO FEMALE DURING MATING AND MAY CC AFFECT EGGLAYING AND BEHAVIOR AFTER MATING. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: LUMEN FLUID OF MALE ACCESSORY GLANDS, BECOMES CC SEMINAL FLUID. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z33647; CAA83925.1; -. DR EMBL; AE003753; AAF56515.1; -. DR EMBL; AY118802; AAM50662.1; -. DR FlyBase; FBgn0011668; Mst57Da. KW Signal; Behavior. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 75 ACCESSORY GLAND-SPECIFIC PEPTIDE 57DA. FT DOMAIN 39 64 ALA/PRO-RICH DOMAIN. FT CONFLICT 39 46 MISSING (IN REF. 1). FT CONFLICT 64 75 MISSING (IN REF. 1). SQ SEQUENCE 75 AA; 7106 MW; BCD3D70817C98E14 CRC64; MKFLALFVTL LVVLALVSAQ KSQNTNHNVI VIGAKKPGAA PAAAAAAAPA APPAAAPAAA PAAPEAGLAD APAES // ID MSDB_DROME STANDARD; PRT; 40 AA. AC Q9VBL7; Q24391; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland-specific peptide 57Db precursor (Male accessory gland DE secretory protein 57Db). GN MST57DB OR CG5016. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; TISSUE=Male accessory gland; RX MEDLINE=95227188; PubMed=7711745; RA Simmerl E., Schaefer M., Schaefer U.; RT "Structure and regulation of a gene cluster for male accessory gland RT transcripts in Drosophila melanogaster."; RL Insect Biochem. Mol. Biol. 25:127-137(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSFERRED FROM MALE TO FEMALE DURING MATING AND MAY CC AFFECT EGGLAYING AND BEHAVIOR AFTER MATING. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: LUMEN FLUID OF MALE ACCESSORY GLANDS, BECOMES CC SEMINAL FLUID. CC -!- DEVELOPMENTAL STAGE: LAST DAY OF PUPAL DEVELOPMENT AND ADULTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z33647; CAA83926.1; -. DR EMBL; AE003753; AAF56514.1; -. DR FlyBase; FBgn0011669; Mst57Db. KW Signal; Behavior. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 40 ACCESSORY GLAND-SPECIFIC PEPTIDE 57DB. FT CONFLICT 37 37 S -> N (IN REF. 1). SQ SEQUENCE 40 AA; 4184 MW; 66F14C76C2649B50 CRC64; MKITSALVLL FAGVAFAQSA DPNTNENKNV IHINSPSAAK // ID MSDC_DROME STANDARD; PRT; 103 AA. AC Q9V3J3; Q24392; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Accessory gland-specific peptide 57Dc precursor (Male accessory gland DE secretory protein 57Dc) (45-kDa cAMP-dependent phosphoprotein) (Pp45). GN MST57DC OR CG4986. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SEQUENCE OF 52-67, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION. RC TISSUE=Male accessory gland; RX MEDLINE=99381229; PubMed=10451922; RA Cho K.S., Lim J.H., Won D.H., Gye M.C., Chung K.W., Lee C.C.; RT "A 45-kDa cAMP-dependent phosphoprotein which is related to the RT product of Mst57Dc in Drosophila melanogaster."; RL Insect Biochem. Mol. Biol. 29:701-710(1999). RN [2] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Male accessory gland; RX MEDLINE=95227188; PubMed=7711745; RA Simmerl E., Schaefer M., Schaefer U.; RT "Structure and regulation of a gene cluster for male accessory gland RT transcripts in Drosophila melanogaster."; RL Insect Biochem. Mol. Biol. 25:127-137(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSFERRED FROM MALE TO FEMALE DURING MATING AND MAY CC AFFECT EGGLAYING AND BEHAVIOR AFTER MATING. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: LUMEN FLUID OF MALE ACCESSORY GLANDS, BECOMES CC SEMINAL FLUID. CC -!- DEVELOPMENTAL STAGE: ACCUMULATES AFTER ECLOSION AND GRADUALLY CC INCREASES DURING SEXUAL MATURATION. IN MALES, LEVELS DECLINE CC IMMEDIATELY AFTER MATING AND RECOVER PROGRESSIVELY. CC -!- PTM: CAMP-DEPENDENT PHOSPHORYLATION. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 31. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF142325; AAD33884.1; -. DR EMBL; Z33647; CAA83927.1; ALT_FRAME. DR EMBL; AE003753; AAF56513.1; -. DR FlyBase; FBgn0011670; Mst57Dc. KW Signal; Behavior; Phosphorylation. FT SIGNAL 1 44 POTENTIAL. FT CHAIN 45 103 ACCESSORY GLAND-SPECIFIC PEPTIDE 57DC. FT CONFLICT 24 24 Q -> H (IN REF. 2). SQ SEQUENCE 103 AA; 11608 MW; B4BC4BA01166CD42 CRC64; MPINDFISCY LKQLQRISIV SIHQVVKMHG THFLILLLLC GVLGSNGVTP DIKNVAKAER NMHNMLRCLK KNEPIVKSRI LTLPPNCNQY VSAVVETWKP EGV // ID MSH2_DROME STANDARD; PRT; 963 AA. AC P43248; Q86BK6; Q9NKC4; Q9VJT0; DT 01-NOV-1995 (Rel. 32, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA mismatch repair protein spellchecker 1. GN SPEL1 OR BG:DS01068.9 OR CG4215. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), AND FUNCTION. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=99178998; PubMed=10077620; RA Flores C., Engels W.; RT "Microsatellite instability in Drosophila spellchecker1 (MutS homolog) RT mutants."; RL Proc. Natl. Acad. Sci. U.S.A. 96:2964-2969(1999). RN [2] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: INVOLVED IN POSTREPLICATION MISMATCH REPAIR. BINDS CC SPECIFICALLY TO DNA CONTAINING MISMATCHED NUCLEOTIDES THUS CC PROVIDING A TARGET FOR THE EXCISION REPAIR PROCESSES CC CHARACTERISTIC OF POSTREPLICATION MISMATCH REPAIR (BY SIMILARITY). CC -!- SUBUNIT: HETERODIMER OF MSH2/SPEL AND MSH6 (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=P43248-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=A; CC IsoId=P43248-2; Sequence=VSP_008036; CC -!- SIMILARITY: BELONGS TO THE DNA MISMATCH REPAIR MUTS FAMILY. CC -!- CAUTION: REF.1 AND REF.2 SEQUENCES DIFFER FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17893; AAA62406.1; ALT_SEQ. DR EMBL; AE003409; AAF44872.1; ALT_SEQ. DR EMBL; AE003643; AAF53392.2; -. DR EMBL; AE003643; AAO41195.1; -. DR FlyBase; FBgn0015546; spel1. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0006298; P:mismatch repair; IMP. DR GO; GO:0006301; P:postreplication repair; ISS. DR InterPro; IPR000432; MutS_C. DR InterPro; IPR007860; MutS_II. DR InterPro; IPR007696; MutS_III. DR InterPro; IPR007861; MutS_IV. DR InterPro; IPR007695; MutS_N. DR Pfam; PF01624; MutS_I; 1. DR Pfam; PF05188; MutS_II; 1. DR Pfam; PF05192; MutS_III; 1. DR Pfam; PF05190; MutS_IV; 1. DR Pfam; PF00488; MutS_V; 1. DR ProDom; PD001263; MutS_C; 1. DR SMART; SM00534; MUTSac; 1. DR SMART; SM00533; MUTSd; 1. DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1. KW DNA repair; ATP-binding; DNA-binding; Alternative splicing. FT NP_BIND 713 720 ATP (POTENTIAL). FT VARSPLIC 1 46 Missing (in isoform A). FT /FTId=VSP_008036. FT CONFLICT 863 863 S -> P (IN REF. 1). SQ SEQUENCE 963 AA; 109149 MW; AA104A3D28F83DE6 CRC64; MIWFLHIWYL FTRKWYIGWH RIRSHFVYAE TGAKLCDYFN HFKSGKMQAK ATDSRQEPTL NMDTNARRNF IKFHAKLGEK PATTVRFFDH TDRYTVHGSD DCELVAKIVY KSTAFIGALL PDDKKETLQF VSMSKGNFEL AVRELLLVRN YRVEVYVKNS SDWEIEYRGS PGNLLQFEDI LFSNKEVLVG NSIISLLVKL DGGGQRRVGV ASVEQNDCKF QLLEFLDDDF FTELEATVVL LGPKECLLPS IEGEYSAVKT LLDRNGVMIT MPKKSGDNDL LQDLNRLLRF AKGQQEDATG LKELQLQLAS NALKTAIKYL DLVNDAGNLG HYEIKQLDLN RFVHLDSAAV AALNIMPKPG THPSMPSYRW QSVLGVLDHC RTPQGHRLMG QWVKQPLRSR NILNDRHNIV QCLLESPDTM ETLSLDYLKR IPDILMLTKK LMRRKANLQD LFRIYQVILR TPKILKVLHE LDNSTIESVI CAPFKSFLKD LTGLKQMVEQ VVDFEAIERG EYLVKASFDS RLMELQQMMT ELYSKMEELQ FKCSQELNLD GKNQVKLESV AKLGHHFRIT VKDDSVLRKN KNYRIVDVIK GGVRFTSDKL EGYADEFASC RTRYEEQQLS IVEEIIHVAV GYAAPLTLLN NELAQLDCLV SFAIAARSAP TPYVRPKMLE EGARELVLED VRHPCLELQE HVNFIANSVD FKKEECNMFI ITGPNMGGKS TYIRSVGTAV LMAHIGAFVP CSLATISMVD SILGRVGASD NIIKGLSTFM VEMIETSGII RTATDKSLVI IDELGRGTST YEGCGIAWSI AEHLAKETKC FTLFATHFHE ITKLAETLST VKNCHMAAVA DADDFTLLYQ VRSGVMEKSF GIQVARLANF PEHVVQNAQE VYNEFEDEHV DKQKKEDKAL LEKIQVAIQQ LSTAGNNVDI NVEDLTQLVT QFTKDIEQLD SDYFKSVLAT SEA // ID MSL1_DROME STANDARD; PRT; 1039 AA. AC P50535; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Male-specific lethal-1 protein. GN MSL-1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE OF 85-1039 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93314941; PubMed=8325488; RA Palmer M.J., Mergner V.A., Richman R., Manning J.E., Kuroda M.I., RA Lucchesi J.C.; RT "The male-specific lethal-one (msl-1) gene of Drosophila melanogaster RT encodes a novel protein that associates with the X chromosome in RT males."; RL Genetics 134:545-557(1993). RN [2] RP REVISIONS, SEQUENCE FROM N.A. RX MEDLINE=95300219; PubMed=7781064; RA Kelley R.L., Solovyeva I., Lyman L.M., Richman R., Solovyev V., RA Kuroda M.I.; RT "Expression of msl-2 causes assembly of dosage compensation RT regulators on the X chromosomes and female lethality in Drosophila."; RL Cell 81:867-877(1995). CC -!- FUNCTION: THE MSL PROTEINS ARE ESSENTIAL FOR ELEVATING CC TRANSCRIPTION OF THE SINGLE X CHROMOSOME IN THE MALE (X CHROMOSOME CC DOSAGE COMPENSATION). MSL-1 IS A PIONEER PROTEIN. MLE, MSL-1 AND CC MSL-3 ARE CO-LOCALIZED ON THE X CHROMOSOME. EACH OF THE MSL CC PROTEINS REQUIRES ALL THE OTHER MSLS FOR WILD-TYPE X-CHROMOSOME CC BINDING. CC -!- SUBUNIT: MSL-1 SEEMS TO FORM A TIGHT COMPLEX WITH MSL-2. CC -!- SUBCELLULAR LOCATION: NUCLEAR; MSL-1 IS ASSOCIATED WITH HUNDREDS CC OF DISCRETE SITES ALONG THE LENGTH OF THE X CHROMOSOME IN MALES CC AND NOT IN FEMALES, AND IS ALSO ASSOCIATED WITH 10-20 AUTOSOMAL CC SITES IN MALES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L42514; AAA98918.1; -. DR PIR; S52959; S52959. DR FlyBase; FBgn0005617; msl-1. DR GO; GO:0016456; C:dosage compensation complex (sensu Drosophila); NAS. DR GO; GO:0003682; F:chromatin binding; IDA. DR GO; GO:0009047; P:dosage compensation, by hyperactivation of ...; NAS. KW Nuclear protein. FT CONFLICT 188 193 PLPPAA -> HCHLLP (IN REF. 1). FT CONFLICT 492 492 L -> S (IN REF. 1). FT CONFLICT 670 670 I -> M (IN REF. 1). SQ SEQUENCE 1039 AA; 117412 MW; 4759E9B5EF6E9F14 CRC64; MDKRFKWPPK KRANYLESPY PHIPSGGRQR NLHGHPNQTQ HLHQHPGKIY ERQQYGNGRG GHGGGNNNYR KLLHSLPAEH GGGAMAPPSS GGTVCAGADM VKLISENNNL RRMVMLNLNL MQEQTDSIAA KDKELDDQSA KMSVVKAQNE ELKQAVAQLE AANQELCKQL RRKNQRRNDN DDDDDDPPLP PAAPQQKLIR CHAETQTVFR EREQGTQTID AQPQFANALP RGINMKESPA LDHHAGAVTN QPASKRSESK GRGEFNGKKV STFILQRMNQ DFEHHIHEQT EVAEEHEMEA HKEQISQEED QLVAEEDHLH MQEVHTEEVV GGDIFHDALE SIEMEVVTEE LVDMEEHGQS VDANGHIEED DDEDDEDDEN SDKDDDSEED DYPWMHSDAD VNARTEEELW QNQNYLLELD PTEEKTCAPS AHSTPNHQQK SSTQAEIRKE GNQNRITEKL LQLKPEPMVD ALEAPILPKW VAFKKKDKEH ELVPESPEVP KQQPHQEDAI VDHNAIKNQL EVPKPDLKPK DQPKDEQRQD GQLDVRVEPQ EDVRKVQKET LKRQPEDAPK HLPKAVAPKV TKTSSRESTL PKANTADIKD APAQKVIANH QSTKTQTDPV KTQRLQVKIR QYEMHPDMRT GSSAPSDIRK QKNVDPVSTP ETKTIKSKSI LVNDKKTTSE TSQSPDQEID VETVRRKLAE HLKKELLSQS HSSQVTLKKI RERVATNLIY PPPSAPVSST TITPAPTPST TPTPGSTPQH AVTSSMDQEI SAAKSKSKAA EQIATPLTPQ SNSSVSSTTS TIRKTLNNCS PHTYSKATAR SGKLQSRFRT ATFPYSTRTW EDQEFHCDNE FFLEEADELL ADNPSLEIPK WRDVPVPPSS DKIDTELLSD ATFERRHQKY VKDEVDRKCR DARYMKEQIR LEQLRMRRNQ DEVLVALDPL RASTFYPLPE DIEAIQFVNE VTVQAFGENV VNMEARDDFG VPWVDAIEAP TSIARSKALA EPVATLASKK IPTTAAEARH QENHSSYVFP KRRKRQKNR // ID MSL2_DROME STANDARD; PRT; 773 AA. AC P50534; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Male-specific lethal-2 protein. GN MSL-2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95300219; PubMed=7781064; RA Kelley R.L., Solovyeva I., Lyman L.M., Richman R., Solovyev V., RA Kuroda M.I.; RT "Expression of msl-2 causes assembly of dosage compensation RT regulators on the X chromosomes and female lethality in Drosophila."; RL Cell 81:867-877(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95317307; PubMed=7796814; RA Zhou S., Yang Y., Scott M.J., Pannuti A., Fehr K.C., Eisen A., RA Koonin E.V., Fouts D.L., Wrightsman R., Manning J.E., Lucchesi J.C.; RT "Male-specific lethal 2, a dosage compensation gene of Drosophila, RT undergoes sex-specific regulation and encodes a protein with a RING RT finger and a metallothionein-like cysteine cluster."; RL EMBO J. 14:2884-2895(1995). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=96017637; PubMed=7588059; RA Bashaw G.J., Baker B.S.; RT "The msl-2 dosage compensation gene of Drosophila encodes a putative RT DNA-binding protein whose expression is sex specifically regulated RT by Sex-lethal."; RL Development 121:3245-3258(1995). CC -!- FUNCTION: THE MSL PROTEINS ARE ESSENTIAL FOR ELEVATING CC TRANSCRIPTION OF THE SINGLE X CHROMOSOME IN THE MALE (X CHROMOSOME CC DOSAGE COMPENSATION). MSL-2 IS REQUIRED FOR TRANSLATION AND/OR CC STABILITY OF MSL-1 IN MALES. BOTH MSL-1 AND MSL-2 BIND TO HUNDREDS CC OF SITES ALONG THE MALE X CHROMOSOME, BUT NOT THE FEMALE X OR THE CC AUTOSOMES IN EITHER SEX. CC -!- SUBUNIT: MSL-2 SEEMS TO FORM A TIGHT COMPLEX WITH MSL-1. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: THE MSL-2 PROTEIN IS ONLY PRODUCED IN MALES. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L42553; AAA75573.1; -. DR EMBL; Z48443; CAA88358.1; -. DR EMBL; X89241; CAA61529.1; -. DR PIR; S55554; S55554. DR FlyBase; FBgn0005616; msl-2. DR GO; GO:0016456; C:dosage compensation complex (sensu Drosophila); NAS. DR GO; GO:0003682; F:chromatin binding; IDA. DR GO; GO:0009047; P:dosage compensation, by hyperactivation of ...; NAS. DR InterPro; IPR001841; Znf_ring. DR SMART; SM00184; RING; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Zinc-finger; Nuclear protein; DNA-binding; Coiled coil. FT ZN_FING 41 85 RING-TYPE. FT DOMAIN 283 519 COILED COIL (POTENTIAL). FT CONFLICT 280 280 T -> N (IN REF. 2). FT CONFLICT 370 373 MISSING (IN REF. 2). FT CONFLICT 371 373 LKT -> VEE (IN REF. 3). FT CONFLICT 380 380 P -> Q (IN REF. 2). FT CONFLICT 403 403 T -> I (IN REF. 2). FT CONFLICT 405 405 T -> A (IN REF. 2). FT CONFLICT 423 423 H -> Q (IN REF. 3). FT CONFLICT 429 429 Q -> H (IN REF. 2). FT CONFLICT 431 431 A -> E (IN REF. 2 AND 3). FT CONFLICT 433 433 S -> P (IN REF. 2 AND 3). FT CONFLICT 439 439 E -> V (IN REF. 2). FT CONFLICT 443 443 A -> P (IN REF. 2). FT CONFLICT 471 471 T -> A (IN REF. 3). FT CONFLICT 591 591 M -> L (IN REF. 3). FT CONFLICT 642 642 E -> D (IN REF. 2). SQ SEQUENCE 773 AA; 84841 MW; AE38BA76A4174225 CRC64; MAQTAYLKVT RIAMRSASNL SKRRVEELNS GLGELRQLLS CVVCCQLLVD PYSPKGKRCQ HNVCRLCLRG KKHLFPSCTQ CEGCSDFKTY EENRMMAAQL LCYKTLCVHL LHSALFGELA GMRPQVAREL VPRIKLPPKT TQEFIREGSN ISDTFDIFLP QPDLPFLKDM PTSLPAETPP TSAVTTPELP YDHHLNISDI EAEAAATAEQ GHFSPLPLLP TGSRMGMLSH AGQIVIATES SESGFMDQAW TDQVDLSGTV SVSKYTNSGN NFAVSYVMPT SATTKFDPQE LQIGQVVQMA DSTQLAVLAA VEETVETSTQ LTVLSTTVEE TVETSTQLEV LTSAEEPNEI SDQLANLQVE ESDEALVEET LKTAEGTSIP SEVVAEHMEE DQHLDVHTSQ SPTQTEMEEA VEEHVATKTQ LGHVQTELQD AESLQKDFED AKAAAEEAKE KEKDLHAISA ELQKEDSDEP TLKRKRTRTL KASQAAKIEP VPSEVKTKVQ SGKGALRRIR GKDKEEKVKP PKPKCRCGIS GSSNTLTTCR NSRCPCYKSY NSCAGCHCVC CKNPHKEDYV ESDEDDDLED FEMPKDVPEP MTQSEEPVVA EPRQEENSMA PPDSSAPISL VPLNNLQQSQ HPLVLVQNEK GEYQGFNIFQ GSKPLDPVTV GFTIRVQLQH TDGFGSLPQY AYIMPTIDPP NPPAPSLSPP PPPAPDREVI EPPAKKFRTS RTRRGRANFS ALDTVDELVS GGSRSNSAAG DRSSATDNAH SLFEEIMSGS DDL // ID MSL3_DROME STANDARD; PRT; 512 AA. AC P50536; Q8IQ74; Q9VS18; DT 01-OCT-1996 (Rel. 34, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Male-specific lethal-3 protein. GN MSL-3 OR CG8631. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=95285767; PubMed=7768187; RA Gorman M., Franke A., Baker B.S.; RT "Molecular characterization of the male-specific lethal-3 gene and RT investigations of the regulation of dosage compensation in RT Drosophila."; RL Development 121:463-475(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE MSL PROTEINS ARE ESSENTIAL FOR ELEVATING CC TRANSCRIPTION OF THE SINGLE X CHROMOSOME IN THE MALE (X CHROMOSOME CC DOSAGE COMPENSATION). MLE, MSL-1 AND MSL-3 ARE CO-LOCALIZED ON THE CC X CHROMOSOME. EACH OF THE MSL PROTEINS REQUIRES ALL THE OTHER MSLS CC FOR WILD-TYPE X-CHROMOSOME BINDING. CC -!- SUBCELLULAR LOCATION: NUCLEAR; MSL-3 IS ASSOCIATED WITH HUNDREDS CC OF DISCRETE SITES ALONG THE LENGTH OF THE X CHROMOSOME IN MALES CC AND NOT IN FEMALES, AND IS ALSO ASSOCIATED WITH 10-20 AUTOSOMAL CC SITES IN MALES. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=A; CC IsoId=P50536-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=P50536-2; Sequence=VSP_007640; CC Note=No experimental confirmation available; CC -!- SIMILARITY: CONTAINS 1 CHROMO DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X81321; CAA57101.1; -. DR EMBL; AE003560; AAF50612.1; -. DR EMBL; AE003560; AAN12073.1; -. DR EMBL; AY071074; AAL48696.1; -. DR PIR; S48828; S48828. DR FlyBase; FBgn0002775; msl-3. DR GO; GO:0016456; C:dosage compensation complex (sensu Drosophila); NAS. DR GO; GO:0003682; F:chromatin binding; IDA. DR GO; GO:0009047; P:dosage compensation, by hyperactivation of ...; NAS. DR InterPro; IPR000953; Chromo. DR InterPro; IPR008676; MRG. DR Pfam; PF05712; MRG; 1. DR SMART; SM00298; CHROMO; 1. DR PROSITE; PS00598; CHROMO_1; FALSE_NEG. DR PROSITE; PS50013; CHROMO_2; FALSE_NEG. KW Chromatin regulator; Nuclear protein; Transcription regulation; KW Alternative splicing. FT DOMAIN 11 90 CHROMO. FT VARSPLIC 1 34 MTELRDETPLFHKGEIVLCYEPDKSKARVLYTSK -> MPQ FT (in isoform 2). FT /FTId=VSP_007640. FT CONFLICT 184 184 A -> T (IN REF. 1). FT CONFLICT 352 352 V -> G (IN REF. 1). SQ SEQUENCE 512 AA; 58852 MW; 3101BC92B2339991 CRC64; MTELRDETPL FHKGEIVLCY EPDKSKARVL YTSKVLNVFE RRNEHGLRFY EYKIHFQGWR PSYDRCVRAT VLLKDTEENR QLQRELAEAA KLQIRGDYSY KGTPDKPSAK KKRGGKAAHV EEPIVVPMDT GHLEAEHEMA PTPRAAGNRT RDNSGGKRKE KPPSGDGRLK GNRGRQTETF YNNAINDVSV YNHVPQEDRI MMRVSERLRE LIEYDRNMIK VLGKQHALPA RVPIVTIMEN FVKQQAVELA ISIKQDSSRA RNTQSRNARM EREYDRVMST VCMLKEVVDG LRIYFEFHVD DHLLYTEEKE YVHNYLTDDN MRNCSLILNK SYEYINPSGD TELIGLDGTP VVEGSGDTNG QIGVINIGGP EYEKQLQKCL LYIVTASGKN TAQAYERTSP YTAAYKLPVE MRGFLNETFK WRLLSAESPP EKSMVFGAPH LVRLMIKMPM FLNASPISNK KLEDLLPHLD AFINYLENHR EWFDRENFVN STALPQEDLQ RELLDSLDGI AA // ID MSRB_DROME STANDARD; PRT; 207 AA. AC Q8INK9; Q8INK8; Q8INL0; Q8STJ0; Q9VGV4; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Methionine-R-sulfoxide reductase (EC 1.8.4.-) (Selenoprotein R). GN MSRB OR SELR OR CG6584. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), ENZYME ACTIVITY, AND ZINC BINDING. RX MEDLINE=21927628; PubMed=11929995; RA Kryukov G.V., Kumar R.A., Koc A., Sun Z., Gladyshev V.N.; RT "Selenoprotein R is a zinc-containing stereo-specific methionine RT sulfoxide reductase."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4245-4250(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP ZINC BINDING, DISULFIDE BOND, MASS SPECTROMETRY, AND MUTAGENESIS OF RP CYS-92; CYS-95; CYS-110; CYS-153; CYS-156; HIS-159; HIS-162; CYS-176 RP AND SER-179. RX MEDLINE=22241889; PubMed=12145281; RA Kumar R.A., Koc A., Cerny R.L., Gladyshev V.N.; RT "Reaction mechanism, evolutionary analysis, and role of zinc in RT Drosophila methionine-R-sulfoxide reductase."; RL J. Biol. Chem. 277:37527-37535(2002). CC -!- CATALYTIC ACTIVITY: PROTEIN L-METHIONINE + OXIDIZED THIOREDOXIN = CC PROTEIN L-METHIONINE R-OXIDE + REDUCED THIOREDOXIN. CC -!- COFACTOR: BINDS 1 ZINC ION PER SUBUNIT. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=E; CC IsoId=Q8INK9-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=A; CC IsoId=Q8INK9-2; Sequence=VSP_008300, VSP_008301; CC Name=B; CC IsoId=Q8INK9-3; Sequence=VSP_008300; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q8INK9-4; Sequence=VSP_008301; CC Note=No experimental confirmation available; CC Name=D; CC IsoId=Q8INK9-5; Sequence=VSP_008300, VSP_008302; CC Note=No experimental confirmation available; CC -!- MASS SPECTROMETRY: MW=19439.6; METHOD=ELECTROSPRAY. CC -!- SIMILARITY: BELONGS TO THE MSRB MET SULFOXIDE REDUCTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF486578; AAM10931.1; -. DR EMBL; AE003688; AAF54569.1; -. DR EMBL; AE003688; AAN13490.1; -. DR EMBL; AE003688; AAN13491.1; -. DR EMBL; AE003688; AAN13492.1; -. DR EMBL; AE003688; AAN13493.1; -. DR EMBL; AY070627; AAL48098.1; -. DR FlyBase; FBgn0037847; SelR. DR InterPro; IPR002579; DUF25. DR Pfam; PF01641; SelR; 1. DR ProDom; PD004057; DUF25; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. KW Oxidoreductase; Metal-binding; Zinc; Alternative splicing. FT INIT_MET 0 0 FT METAL 92 92 ZINC. FT METAL 95 95 ZINC. FT METAL 153 153 ZINC. FT METAL 156 156 ZINC. FT DISULFID 110 176 FT VARSPLIC 1 41 Missing (in isoform A, isoform B and FT isoform D). FT /FTId=VSP_008300. FT VARSPLIC 133 143 Missing (in isoform A and isoform FT C). FT /FTId=VSP_008301. FT VARSPLIC 135 145 GNILLLIAHPE -> MVRTEVRCSRCSAHMGHVFDDGPPPK FT HRRFCINSASIDFVKK (in isoform D). FT /FTId=VSP_008302. FT MUTAGEN 92 92 C->G: LOSS OF ACTIVITY AND ZINC FT BINDING. FT MUTAGEN 95 95 C->G,S: LOSS OF ACTIVITY AND ZINC FT BINDING. FT MUTAGEN 110 110 C->S: THIOREDOXIN-DEPENDENT ACTIVITY FT REDUCED, BUT NO CHANGE IN DTT-DEPENDENT FT ACTIVITY. FT MUTAGEN 153 153 C->G,S: LOSS OF ACTIVITY AND ZINC FT BINDING. FT MUTAGEN 156 156 C->S: LOSS OF ACTIVITY AND ZINC FT BINDING. FT MUTAGEN 159 159 H->G: LOSS OF THIOREDOXIN-DEPENDENT FT ACTIVITY, 81% DTT-DEPENDENT ACTIVITY. FT MUTAGEN 162 162 H->G: LOSS OF THIOREDOXIN-DEPENDENT FT ACTIVITY, 80% DTT-DEPENDENT ACTIVITY. FT MUTAGEN 176 176 C->K,S: LOSS OF ACTIVITY. FT MUTAGEN 179 179 S->G: LOSS OF THIOREDOXIN-DEPENDENT FT ACTIVITY, 85% DTT-DEPENDENT ACTIVITY. SQ SEQUENCE 207 AA; 23168 MW; 2E3229C87010535F CRC64; FALSARHALR RTRIFAIPRF FADSRQDSDN PDKRYSGPAA TMDNKSEKVT VNKEELRKRL TPVQYQVTQE AGTERPFTGC YNKHYEKGVY QCIVCHQDLF SSETKYDSGC GWPAFNDVLD KGKVTLHRDA SIPGGNILLL IAHPERIRTE VRCARCNAHM GHVFEDGPKP TRKRYCINSA SIEFVNADPA TSSPPVATPT AAPIAQQ // ID MSTA_DROME STANDARD; PRT; 462 AA. AC O46040; O46041; Q9UB82; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Msta protein. GN MSTA OR EG:103B4.4 OR CG32800/CG18033. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=20242230; PubMed=10779958; RA Alatortsev V.E., Kovalenko T.A., Kalmykova A.I.; RT "Local duplication of genes with insertion of a complex RT microsatellite."; RL Mol. Biol. (Mosk) 34:300-303(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- SIMILARITY: CONTAINS 1 SET DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ238707; CAB42051.1; -. DR EMBL; AE003423; AAN09072.1; -. DR EMBL; AL009193; CAA15694.2; ALT_INIT. DR FlyBase; FBgn0023548; msta. DR InterPro; IPR001214; SET. DR Pfam; PF00856; SET; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS50280; SET; 1. FT DOMAIN 170 291 SET. FT CONFLICT 76 76 A -> S (IN REF. 1). SQ SEQUENCE 462 AA; 52156 MW; 04E956E80BC86416 CRC64; MSTAAQCPPP RPGGGGGDTT LAALSAHMAP CRDTTPEQLA QLIDVHLGDL RQEQPNWTIS SSTVAGRGVF ATRDIAAGEL IFQERALVTG PTARKGQLSS CICCHETLPQ TGFLCRHRCT LPVCETCSDS EEHQAECEHF RRWQPKDVDA EQEQVNPMSL RILTAVRVFH LGKEQRHLVD AMQANAERAY RREIIQAAQC FRNFPTTDRV FMDQLFRIVG VLNTNAFEAP CRSGGHETLL RGLFPLTAIM NHECTPNASH YFENGRLAVV RAARDIPKGG EITTTYTKIL WGNLTRNIFL KMTKHFACDC VRCHDNTENG TYLSALFCRE QGCRGLVIPV QTRTLQPDWR CITCENVFPH AKMAKYQDFA LNTINNRINS CSVQDMIHFI NELCPRFCPS SNYVLIEAKL NVIWRMTRFD HEEYTPEEMG HMDRYREEVL AILHKLGAGE CTLKKLITGE IQ // ID MT1_DROME STANDARD; PRT; 40 AA. AC P04357; Q9VH67; DT 20-MAR-1987 (Rel. 04, Created) DT 20-MAR-1987 (Rel. 04, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Metallothionein 1 (MT-1). GN MTNA OR CG9470. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86165787; PubMed=3007277; RA Maroni G., Otto E., Lastowski-Perry D.; RT "Molecular and cytogenetic characterization of a metallothionein gene RT of Drosophila."; RL Genetics 112:493-504(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85105016; PubMed=2578462; RA Lastowski-Perry D., Otto E., Maroni G.; RT "Nucleotide sequence and expression of a Drosophila metallothionein."; RL J. Biol. Chem. 260:1527-1530(1985). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=86219988; PubMed=3086075; RA Maroni G., Lastowski-Perry D., Otto E., Watson D.; RT "Effects of heavy metals on Drosophila larvae and a metallothionein RT cDNA."; RL Environ. Health Perspect. 65:107-116(1986). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=88029907; PubMed=2822463; RA Maroni G., Otto E., Lastowski-Perry D., Price D.H.; RT "The metallothionein gene of Drosophila."; RL Experientia Suppl. 52:385-392(1987). RN [5] RP SEQUENCE FROM N.A. RX MEDLINE=92201681; PubMed=1802803; RA Theodore L., Ho A.-S., Maroni G.; RT "Recent evolutionary history of the metallothionein gene Mtn in RT Drosophila."; RL Genet. Res. 58:203-210(1991). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [7] RP REGULATION AND EXPRESSION. RX MEDLINE=91012582; PubMed=1976815; RA Silar P., Theodore L., Mokdad R., Erraiss N.-E., Cadic A., Wegnez M.; RT "Metallothionein Mto gene of Drosophila melanogaster: structure and RT regulation."; RL J. Mol. Biol. 215:217-224(1990). CC -!- FUNCTION: THIS PROTEIN BINDS CATIONS OF SEVERAL TRANSITION CC ELEMENTS. IT IS THOUGHT TO BE INVOLVED IN DETOXIFICATION CC PROCESSES. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYOGENESIS, LARVA AND ADULT. CC -!- INDUCTION: STRONGLY INDUCED BY CADMIUM, COPPER AND MERCURY. CC -!- MISCELLANEOUS: ALL CYSTEINE RESIDUES ARE ARRANGED IN C-X-C GROUPS. CC THESE ARE THOUGHT TO BE THE METAL-BINDING SITES IN OTHER CC METALLOTHIONEINS. CC -!- SIMILARITY: BELONGS TO THE METALLOTHIONEIN SUPERFAMILY; FAMILY 5. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03758; CAA27391.1; -. DR EMBL; K02314; AAA28681.1; -. DR EMBL; M27708; AAA28684.1; -. DR EMBL; M69015; AAB41334.1; -. DR EMBL; AE003684; AAF54452.1; -. DR PIR; A25294; SMFF. DR FlyBase; FBgn0002868; MtnA. DR InterPro; IPR000966; Metallthion_5. DR Pfam; PF02067; Metallothio_5; 1. DR PRINTS; PR00872; MTDIPTERA. KW Metal-binding; Copper; Cadmium; Zinc; Mercury; Polymorphism. FT VARIANT 40 40 E -> K (IN MTNA-3). SQ SEQUENCE 40 AA; 3853 MW; 99A2A53CCCAE634A CRC64; MPCPCGSGCK CASQATKGSC NCGSDCKCGG DKKSACGCSE // ID MT2_DROME STANDARD; PRT; 43 AA. AC P11956; Q9VDM2; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Metallothionein 2 (MT-2). GN MTNB OR MTO OR CG4312. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=87204190; PubMed=3106973; RA Mokdad R., Debec A., Wegnez M.; RT "Metallothionein genes in Drosophila melanogaster constitute a dual RT system."; RL Proc. Natl. Acad. Sci. U.S.A. 84:2658-2662(1987). RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 3-27. RC STRAIN=Oregon-R; RX MEDLINE=91012582; PubMed=1976815; RA Silar P., Theodore L., Mokdad R., Erraiss N.-E., Cadic A., Wegnez M.; RT "Metallothionein Mto gene of Drosophila melanogaster: structure and RT regulation."; RL J. Mol. Biol. 215:217-224(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS PROTEIN BINDS CATIONS OF SEVERAL TRANSITION CC ELEMENTS. THOUGHT TO BE INVOLVED IN METAL ION HOMEOSTASIS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED PREDOMINANTLY IN EMBRYONIC AND CC LARVAL STAGES. CC -!- INDUCTION: STRONGLY INDUCED BY CADMIUM, COPPER AND MERCURY. CC -!- MISCELLANEOUS: ALL CYSTEINE RESIDUES ARE ARRANGED IN C-X-C GROUPS. CC THESE ARE THOUGHT TO BE THE METAL-BINDING SITES IN OTHER CC METALLOTHIONEINS. CC -!- SIMILARITY: BELONGS TO THE METALLOTHIONEIN SUPERFAMILY; FAMILY 5. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16250; AAA28683.1; -. DR EMBL; X52098; CAA36318.1; -. DR EMBL; AE003730; AAF55768.1; -. DR PIR; S14706; SMFF2. DR FlyBase; FBgn0002869; MtnB. DR GO; GO:0005507; F:copper ion binding; IDA. DR InterPro; IPR000966; Metallthion_5. DR Pfam; PF02067; Metallothio_5; 1. DR PRINTS; PR00872; MTDIPTERA. KW Metal-binding; Copper; Cadmium; Zinc. SQ SEQUENCE 43 AA; 4525 MW; 5EE0CF9171BD9A97 CRC64; MVCKGCGTNC QCSAQKCGDN CACNKDCQCV CKNGPKDQCC SNK // ID MTDC_DROME STANDARD; PRT; 357 AA. AC Q04448; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, DE mitochondrial precursor [Includes: NAD-dependent DE methylenetetrahydrofolate dehydrogenase (EC 1.5.1.15); DE Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)]. GN NMDMC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93250056; PubMed=8485162; RA Price B.D., Laughon A.; RT "The isolation and characterization of a Drosophila gene encoding a RT putative NAD-dependent methylenetetrahydrofolate dehydrogenase- RT methenyltetrahydrofolate cyclohydrolase."; RL Biochim. Biophys. Acta 1173:94-98(1993). CC -!- FUNCTION: MAY PLAY SOME ROLE IN SPERMATOGENESIS. CC -!- CATALYTIC ACTIVITY: 5,10-METHYLENETETRAHYDROFOLATE + NAD(+) = CC 5,10-METHENYLTETRAHYDROFOLATE + NADH. CC -!- CATALYTIC ACTIVITY: 5,10-METHENYLTETRAHYDROFOLATE + H(2)O = 10- CC FORMYLTETRAHYDROFOLATE. CC -!- COFACTOR: MAGNESIUM. THIS NAD-DEPENDENT BIFUNCTIONAL ENZYME HAS CC VERY DIFFERENT KINETIC PROPERTIES THAN THE LARGER NADP-DEPENDENT CC TRIFUNCTIONAL ENZYME AND IS UNIQUE IN THAT IT REQUIRES FORMATION CC OF AN ENZYME-MAGNESIUM COMPLEX TO ALLOW BINDING OF NAD. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN DEVELOPING TISSUES AND AT HIGH CC LEVELS IN ADULT TISSUES. CC -!- SIMILARITY: TO OTHER DEHYDROGENASE/CYCLOHYDROLASE ENZYMES OR CC DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L07958; AAB41352.1; -. DR PIR; S32562; S32562. DR HSSP; P11586; 1A4I. DR FlyBase; FBgn0010222; Nmdmc. DR InterPro; IPR000672; THF_Dhg_Cyh. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR ProDom; PD002300; THF_Dhg_Cyh; 1. DR PROSITE; PS00766; THF_DHG_CYH_1; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. KW Multifunctional enzyme; One-carbon metabolism; Oxidoreductase; NAD; KW Hydrolase; Mitochondrion; Transit peptide; Magnesium. FT TRANSIT 1 53 MITOCHONDRION (POTENTIAL). FT CHAIN 54 357 BIFUNCTIONAL METHYLENETETRAHYDROFOLATE FT DEHYDROGENASE/CYCLOHYDROLASE. SQ SEQUENCE 357 AA; 38759 MW; ABD8F5D1119CC198 CRC64; MATVMGPTPP GTGVMWPAIW RTSSKAIGIR QSVQFEFSTR KISQKPQKEV TISNMAQIID GKAIAQEVRT QLAHELKGME AAGYPKPHLT AVIVGEDPAS EKYVANKMVA CREVGISSET KRLPASTTQE ELLQLIADLN KDPQVTGILV QLPVPEHINE RTICNAVDVD KDVDGFNEVN IGRTALDMEA NIPATPLGVK RLLEHMKIET LGRNAVVVGR SKNVSLPMAI LLHADGKYAT KAMDATVTIC HRYTPPKELA RHCRQADIIV VAVGKPGLIT KDMVKPGACV IDVGINRIKD ESTGQFKLVG DVDFEEVRQV AGHITPVPGG VGPMTVAMLM HNTLKAARKQ FDDRKSS // ID MTH1_DROME STANDARD; PRT; 676 AA. AC Q9VXD9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 1 precursor (Methuselah- DE like 1 protein). GN MTHL1 OR CG4521. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003503; AAF48635.1; -. DR EMBL; AY118371; AAM48400.1; -. DR FlyBase; FBgn0030766; mthl1. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 37 POTENTIAL. FT CHAIN 38 676 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 1. FT DOMAIN 38 335 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 336 356 1 (POTENTIAL). FT DOMAIN 357 365 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 366 386 2 (POTENTIAL). FT DOMAIN 387 403 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 404 424 3 (POTENTIAL). FT DOMAIN 425 441 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 442 462 4 (POTENTIAL). FT DOMAIN 463 488 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 489 509 5 (POTENTIAL). FT DOMAIN 510 540 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 541 561 6 (POTENTIAL). FT DOMAIN 562 562 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 563 583 7 (POTENTIAL). FT DOMAIN 584 676 CYTOPLASMIC (POTENTIAL). FT DISULFID 198 283 BY SIMILARITY. FT DISULFID 199 212 BY SIMILARITY. FT DISULFID 246 298 BY SIMILARITY. FT CARBOHYD 136 136 N-LINKED (GLCNAC...) (BY FT SIMILARITY). FT CARBOHYD 165 165 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 276 276 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 486 486 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 676 AA; 74465 MW; 99814D3D1300ACFD CRC64; MDRSRSSRAA SSNQFIRPCG LLTTVILLQT LVSMSLAIEE MSPPPAAPPR PSPPPTVKLN KCCHSGEYLN DGTCIAGSEA LWLPMVYLVQ QQRFFEPHGA SPRFLKFLPN TRPTCRKDQT TEIFRSRGAN VMLFPNGTLY VRERALMVQP SDYCVDWEVA VVCLNDSQPI NALEDPDYAA NPLVQQEPPK ASLRLSKCCG KWGSYNTQLQ NCDLQPNHQA AVDGLLRLSP QLPEGSYQTS YGLPDCGQPG GYSIAGDWQD AKLDRNTAML QLPHKNLSAG QYCLEHTQRE GEVKIIACQH LFSSAAGAGI HDGSIGGTIE QANGQNLQKA VLTGGILVSI VFLSATLVAG FLLPAVHHAL HWRCQICYVT CLLFGKILLA IEELSSSLQP GSAACHTLAI TMQFFFLAAF FWLNTMCFNI WWTFRDFRPS SLERNQEALR RYLYSLYAWG GPLLITFVAA CVDQLPETTL LRPGFGQLYC WFDNRNLSIF AYFYGPIGLL LCANIALFVS TTHQLTCGLW KRDDVKSSSE KSALGRVCLK LVVVMGVTWI ADILSWLVGG PHGVWFFTDL INALQGVFIF IVVGCQPQVW TACRRIFCPR LRHDITNTTN GVQHSSSSQG LPSMAGGTEI TQNTTTTTTT TNTTATHMPS NPAEDEVPEK APIAPVAPIV KMETIC // ID MTH2_DROME STANDARD; PRT; 518 AA. AC Q9VRN2; Q8SWY8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 2 precursor (Methuselah- DE like 2 protein). GN MTHL2 OR CG17795. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003565; AAF50761.3; -. DR EMBL; AY094944; AAM11297.1; -. DR HSSP; Q9GT60; 1FJR. DR FlyBase; FBgn0035623; mthl2. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 518 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 2. FT DOMAIN 27 220 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 221 241 1 (POTENTIAL). FT DOMAIN 242 250 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 251 271 2 (POTENTIAL). FT DOMAIN 272 279 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 280 300 3 (POTENTIAL). FT DOMAIN 301 321 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 322 342 4 (POTENTIAL). FT DOMAIN 343 371 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 372 392 5 (POTENTIAL). FT DOMAIN 393 426 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 427 447 6 (POTENTIAL). FT DOMAIN 448 455 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 456 476 7 (POTENTIAL). FT DOMAIN 477 518 CYTOPLASMIC (POTENTIAL). FT DISULFID 31 85 BY SIMILARITY. FT DISULFID 87 92 BY SIMILARITY. FT DISULFID 96 190 BY SIMILARITY. FT DISULFID 97 108 BY SIMILARITY. FT DISULFID 152 211 BY SIMILARITY. FT CARBOHYD 47 47 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 111 111 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 125 125 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 201 201 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 85 85 C -> G (IN REF. 3). SQ SEQUENCE 518 AA; 60349 MW; 587A0E64EEE5D003 CRC64; MIASSKMLLS ASILIYFLLN LQSSSAEIAD CSFYDTVDIS EGQRLSNGSY LYEGLLIPAH LTAKYEFKLL ANGDKEQVPS HVRGCVCKLR TCVRFCCPHD HIMDMGECYA NMTTEENELL DPMLNVTLDD GSVVQRHYKK ELMVQWDLPK PCDDMFYLDN RDIMDEYTLF ENGRLLRHYD QVYLDKSEYC LQHRTFGEGN NNSIRIIPHN CLILPSRTGQ TVVMITSLIC LVLTIAVYLC VKKLMNLEGK CFICYMMCLF FGYLFLLLDL WELSLDFCKA AGFLGYFFVM AAFFWLSIIS RHYWKCLTNP CASMNIRSER AFLLYSCFAW AMPLALTGVT YLADNVVNNE EWQPRVGDEG HCWIYTKSWS AMVYFYGPMV LLILFNITMF VLTAKHIIDS KRTLRKIARN EGRIQKLNSD KQNYTQFLLL FTVMGMSWSF EIFSYLVQRE KLWVNIFLVA DYFNWSQGVI IFVLFILRRK TLVLFKKQIF PKQRAFSRSA TQSTIESISQ TKRHFNMT // ID MTH3_DROME STANDARD; PRT; 511 AA. AC Q9V818; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 3 precursor (Methuselah- DE like 3 protein). GN MTHL3 OR BEST:GM02553 OR CG6530. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003803; AAF57863.2; -. DR HSSP; Q9GT60; 1FJR. DR FlyBase; FBgn0028956; mthl3. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 511 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 3. FT DOMAIN 22 215 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 216 236 1 (POTENTIAL). FT DOMAIN 237 245 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 246 266 2 (POTENTIAL). FT DOMAIN 267 273 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 274 294 3 (POTENTIAL). FT DOMAIN 295 317 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 318 338 4 (POTENTIAL). FT DOMAIN 339 366 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 367 387 5 (POTENTIAL). FT DOMAIN 388 422 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 423 443 6 (POTENTIAL). FT DOMAIN 444 452 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 453 473 7 (POTENTIAL). FT DOMAIN 474 511 CYTOPLASMIC (POTENTIAL). FT DISULFID 26 80 BY SIMILARITY. FT DISULFID 82 87 BY SIMILARITY. FT DISULFID 92 103 BY SIMILARITY. FT CARBOHYD 42 42 N-LINKED (GLCNAC...) (Potential). FT CARBOHYD 120 120 N-LINKED (GLCNAC...) (Potential). FT CARBOHYD 168 168 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 511 AA; 58756 MW; A525811B3188A0A0 CRC64; MRIVIGSFTA FLLLLLQNSN AEIPGCDFFD TVDISKAPRF SNGSYLYEGL LIPAHLTAEY DYKLLADDSK EKVASHVRGC ACHLRPCIRF CCPQYQKMQK SKCYGDMSED ELNKHDPFVN VTLSDGSVVR RHFKEDLIVQ SDLAKPGCPR MYFLNHELPG NEFTLFENGS LLRHWDKVEL SKREYCVQHL SFKDDSIRIA PHFCPLSSEH SRTWKTVAIV ISLICIILTI SVYLYVEKLR NLHGKCFICY LASLFLGYFF LVLNVWKYSS GFCVTAGFLG YFSVIAAFFW LSVISLTLWN SFSGNSSWLN RFLPQNRFLS YNLYAWGMAL LLTAITYIAD QVVKNEKLRP RVGVGKNCWI YTGDMTVMIY FYGPMLLIIV FNITMFVLTA FRIMKVKKEA QNFTQQQKTT NRLNSDKQTY ALFLRLFIIM GLSWSLEIIS FLLSKNQAWA KAFMVADYFN WSQGTVIFLL FVLRPSTLKL LKERIKGGRD EAGASDEHIS LQNTKIDPSV F // ID MTH4_DROME STANDARD; PRT; 480 AA. AC Q9V817; DT 28-FEB-2003 (Rel. 41, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 4 precursor (Methuselah- DE like 4 protein). GN MTHL4 OR CG6536. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003803; AAF57864.4; -. DR HSSP; Q9GT60; 1FJR. DR FlyBase; FBgn0034219; mthl4. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 480 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 4. FT DOMAIN 19 212 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 213 233 1 (POTENTIAL). FT DOMAIN 234 242 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 243 263 2 (POTENTIAL). FT DOMAIN 264 272 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 273 293 3 (POTENTIAL). FT DOMAIN 294 319 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 320 340 4 (POTENTIAL). FT DOMAIN 341 363 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 364 384 5 (POTENTIAL). FT DOMAIN 385 414 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 415 435 6 (POTENTIAL). FT DOMAIN 436 456 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 457 477 7 (POTENTIAL). FT DOMAIN 478 480 CYTOPLASMIC (POTENTIAL). FT DISULFID 23 77 BY SIMILARITY. FT DISULFID 79 84 BY SIMILARITY. FT DISULFID 88 183 BY SIMILARITY. FT DISULFID 89 100 BY SIMILARITY. FT CARBOHYD 39 39 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 117 117 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 165 165 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 456 456 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 480 AA; 55286 MW; 25C481DCD1437E4F CRC64; MRILLIAVLF LLMPKSNAEI PGCDFFDTVD ISKAPRFSNG SYLYEGLLIP AHLTAEYDYK LLADDSKEKV ASHVRGCACH LRPCIRFCCP QYQKMQKSKC YGDMSEDELN KHDPFVNVTL SDGSVVRRHF KEDLIVQSDL AKPGCPRMYF LNHELPGNEF TLFENGSLLR HWDKVELSKR EYCVQHLSFK DDSIRIAPHF CPLSSEHSRT WKTVAIVISL ICIILTISVY LYVEKLRNLH GKCFICYLAS LFLGYFFLVL NVWKYSSGFC VTAGFLGYFS VMAAFFWLSV IGIHLRIKFS LASNCLHRLL PENPFRAYNL YAWGIPLIMT AITYTADQVV KNEKLRPRVG VGKNCWIYTG DMTVMIYFYG PMLLLIAFNI IMFVLSAIYI YNIKKNVKGL VHKQQTNQQI NDQQMFAIFL RLFILMGLSW SFEILSFLLT KQQAWARALM VADYFNWSQG TIIFVLFILK PSILKLIIAG // ID MTH5_DROME STANDARD; PRT; 496 AA. AC Q9VGG8; Q8MRB8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 5 (Methuselah-like 5 DE protein). GN MTHL5 OR CG6965. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003693; AAF54714.3; -. DR EMBL; AY121676; AAM52003.1; -. DR FlyBase; FBgn0037960; mthl5. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PRINTS; PR00249; GPCRSECRETIN. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family. FT DOMAIN 1 219 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 220 240 1 (POTENTIAL). FT DOMAIN 241 246 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 247 267 2 (POTENTIAL). FT DOMAIN 268 276 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 277 297 3 (POTENTIAL). FT DOMAIN 298 327 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 328 348 4 (POTENTIAL). FT DOMAIN 349 366 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 367 387 5 (POTENTIAL). FT DOMAIN 388 411 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 412 432 6 (POTENTIAL). FT DOMAIN 433 438 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 439 459 7 (POTENTIAL). FT DOMAIN 460 496 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 82 82 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 63 63 V -> F (IN REF. 3). SQ SEQUENCE 496 AA; 56350 MW; 2D6EDF1A9F864E33 CRC64; MLVKTLGAHF AAGQNAKKCS CCALLISLLC VLLLSLNPLP VTSHVTSAGS STALSSDPNL VLVNKCCEKF EIHVDHECQQ VNETDYFQPM FTSYGGEQNR PVKFKFVIGI PNCGSMQMWP IYHYAGSSDK LVLLDDGRLR HYTNAENEAE ERHGIQSDYE EDIAGSLEPL YHDYDKGLYC IDKATSSTGE ENVLFANICL ARKEIKWSDS NFLLRKILNP IFHGISLVIL LVIAIIYFIL PTLRDLVGNI VTTIAMCLMV SQAADLVRIF TELTSHVSFI VADIILCFSL LAAFFWLNSF GFYIWKTFRS RNVFLRVTDG RKYCYYSAYA WGCTATMAAL AVFAHFFLDA ESYKQEHMVG EQETIGWLGI CIFFAPIACT ILVNIFFYVT TRKLINRRTV YGRIAHKLKA NFIMFSLMLL VMSIAWLFLI MSWLQMEGLL YAHIVVNALQ TPLLLYICVL RQRHVTFLLK KTCCYNEPPS ANDWGDELHY MNGNDY // ID MTH6_DROME STANDARD; PRT; 480 AA. AC Q9VS77; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 6 precursor (Methuselah- DE like 6 protein). GN MTHL6 OR CG16992. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003558; AAO41272.1; -. DR HSSP; Q9GT60; 1FJR. DR FlyBase; FBgn0035789; mthl6. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 480 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 6. FT DOMAIN 21 202 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 203 225 1 (POTENTIAL). FT DOMAIN 226 231 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 232 254 2 (POTENTIAL). FT DOMAIN 255 263 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 264 283 3 (POTENTIAL). FT DOMAIN 284 303 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 304 326 4 (POTENTIAL). FT DOMAIN 327 356 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 357 379 5 (POTENTIAL). FT DOMAIN 380 405 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 406 428 6 (POTENTIAL). FT DOMAIN 429 437 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 438 457 7 (POTENTIAL). FT DOMAIN 458 480 CYTOPLASMIC (POTENTIAL). FT DISULFID 25 78 BY SIMILARITY. FT DISULFID 80 85 BY SIMILARITY. FT DISULFID 89 179 BY SIMILARITY. FT DISULFID 90 101 BY SIMILARITY. FT CARBOHYD 40 40 N-LINKED (GLCNAC...) (Potential). FT CARBOHYD 160 160 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 170 170 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 480 AA; 56079 MW; 6553CF7AC9F57A63 CRC64; MLLNILAIIL VFVISSQSEA VIPGCDYFDT VDISHIPKLN DSYAYEELII PAHLTGLYTF RQLADGSQEP VKSHLRACIC KLKPCIRFCC PRNKMMPNSR CSDGLTENLK RINPYLKITL EDGTIGKYYL LTDMIVLRYE FRYCEKVVSV QEDQYKLYEN GSFMIKPDVN WTLSKQWYCL HPRLEDPNSI WILEHVYIPK SMPAVPQVGT ISMVGCILTI AVYLYIKKLR NLLGKCFICY VFCKFVQYLI WAGGDLNLWN NICSLAGYTN YFFALASHFW LSVMSHQIWK NLRLINRDER SYHFLIYNIY GWGTPAIMTA ITYLVDWAWE DRPDKLNWIP GVGLYRCWIN TYDWSAMIYL YGPMLILSLF NVVTFILTVN HIMKIKSSVK SSTQQQRKCI QNNDFLLYLR LSVMMGVTGI SEVITYFVKR HKFWRQVLRV PNFFHLGSGI VVFVLFILKR STFQMIMERI SGPRRQQPAS // ID MTH7_DROME STANDARD; PRT; 491 AA. AC Q9VSE7; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 7 precursor (Methuselah- DE like 7 protein). GN MTHL7 OR CG7476. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=Q9VSE7-1; Sequence=Displayed; CC Name=A; CC IsoId=Q9VSE7-2; Sequence=VSP_007000; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -!- CAUTION: REF.1 (AAO41271) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003556; AAF50475.1; -. DR EMBL; AE003556; AAO41271.1; ALT_SEQ. DR HSSP; Q9GT60; 1FJR. DR FlyBase; FBgn0035847; mthl7. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Alternative splicing; Multigene family. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 491 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 7. FT DOMAIN 23 167 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 168 188 1 (POTENTIAL). FT DOMAIN 189 222 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 223 243 2 (POTENTIAL). FT DOMAIN 244 252 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 253 273 3 (POTENTIAL). FT DOMAIN 274 325 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 326 346 4 (POTENTIAL). FT DOMAIN 347 372 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 373 393 5 (POTENTIAL). FT DOMAIN 394 434 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 435 455 6 (POTENTIAL). FT DOMAIN 456 458 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 459 479 7 (POTENTIAL). FT DOMAIN 480 491 CYTOPLASMIC (POTENTIAL). FT DISULFID 27 80 BY SIMILARITY. FT DISULFID 82 87 BY SIMILARITY. FT DISULFID 92 103 BY SIMILARITY. FT CARBOHYD 18 18 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 42 42 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 248 248 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 427 491 Missing (in isoform A). FT /FTId=VSP_007000. SQ SEQUENCE 491 AA; 57382 MW; 4FBBC9FDC80F0F14 CRC64; MRLPWVIFCT VLLLIFTNNS NADIPGCNYY DTVDISYIER QNDSYLYDDI EIPASLTGYY EFRQFGDGSI TPIEKHLRAC VCSVRPCIRI CCPAKNFLAN GKCDDGLKEE LARFKPYIYF TYMDLQARVP LTDMAIIRDE FFDCDEMIYI SDFNYFLEEV SIQIFNKCGL IVWFQDGKFW VTVDLFMEKQ DYCLYRHNFD SDFPKSMWII RHRCTSHISP GSLEILIITM ICFVLTIAVY LYIKKLRNVT GKCIVCCIVS RFIQCLIMIL DHLNLLNGIC SPAGYSSHFF RMASNLWLSV ISYHTWKVLT SLNRVDPNYR FLRYNAFVWS TAAIMTGSIY IVNQIWENDP SKWNWLPLVG FIRCSVKDWH PSVWIYISGP SLALSTFNVA MFALTAIYIR KVKGGINKFT NEEEGRINCI NFDSQTYLQF LRLSIVMGLT WIFNVIPYSA RLHIFWEWVG IISEYFHSAF GIVLFVLLVL KRSTWTLMMD S // ID MTH8_DROME STANDARD; PRT; 492 AA. AC Q9W0V7; Q9W0V8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 8 precursor (Methuselah- DE like 8 protein). GN MTHL8 OR CG32475/CG11869/CG13406. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003467; AAF47322.2; -. DR EMBL; AY069723; AAL39868.1; -. DR FlyBase; FBgn0052475; mthl8. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 492 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 8. FT DOMAIN 22 218 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 219 239 1 (POTENTIAL). FT DOMAIN 240 245 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 246 266 2 (POTENTIAL). FT DOMAIN 267 282 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 283 303 3 (POTENTIAL). FT DOMAIN 304 317 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 318 338 4 (POTENTIAL). FT DOMAIN 339 362 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 363 383 5 (POTENTIAL). FT DOMAIN 384 411 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 412 432 6 (POTENTIAL). FT DOMAIN 433 441 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 442 462 7 (POTENTIAL). FT DOMAIN 463 492 CYTOPLASMIC (POTENTIAL). FT DISULFID 30 82 BY SIMILARITY. FT DISULFID 84 89 BY SIMILARITY. FT DISULFID 93 184 BY SIMILARITY. FT DISULFID 94 107 BY SIMILARITY. FT DISULFID 149 202 BY SIMILARITY. FT CARBOHYD 37 37 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 51 51 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 129 129 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 169 169 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 192 192 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 275 275 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 360 360 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 438 438 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 492 AA; 56329 MW; 931F166A9C6AD1DE CRC64; MAQFCILGVL LILSGTHCSW GFHEETHYPC AFIDTANITG SYGLDGPFVH NWTVIPRHFV AVYDFVIENG IRIPASRHLR ACVCKTKPCV RICCLRGEIY DLEKRQCLVP VAGVSSLPSH SHMEVELGNG SLRLVKLQPR FSIHVETPCE HMKAVTKGSE YVHWTLHENG TISHRGHIFS KHYCFTPLLH GNSTWEWQPL ACAPEKLYFV LGVREWTYAI CLLIAILSMF IVLMVYLMCS EMRNSFYGVA IKAYAICMIL GYALLAYLTL HNPANLSNAA CRILPSLALM NLVLSFYILS FIAFKLYLSF YGVVFTKLMF WLIFTPIVLV AVGWSFFVGF SYYGSRLIFG GDTCWFDPRN WSVMIYFYAP VFVACAISGF FYVLSQIYIR DQPDIETEKS FESIEKNRFK SFWKYFGYTA VVWVVCICSF AFNYYWENRS HLNYAVSFCM AFHGFAALYA LIGKNQQIQN FLRRIDNGED TCENSVPLSS FG // ID MTH9_DROME STANDARD; PRT; 513 AA. AC Q9W0R6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 9 precursor (Methuselah- DE like 9 protein). GN MTHL9 OR CG17084. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003468; AAF47377.1; -. DR EMBL; AY070598; AAL48069.1; -. DR EMBL; AY113401; AAM29406.1; -. DR HSSP; Q9GT60; 1FJR. DR FlyBase; FBgn0035131; mthl9. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 513 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 9. FT DOMAIN 20 207 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 208 228 1 (POTENTIAL). FT DOMAIN 229 242 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 243 263 2 (POTENTIAL). FT DOMAIN 264 276 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 277 297 3 (POTENTIAL). FT DOMAIN 298 314 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 315 335 4 (POTENTIAL). FT DOMAIN 336 360 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 361 381 5 (POTENTIAL). FT DOMAIN 382 403 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 404 424 6 (POTENTIAL). FT DOMAIN 425 438 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 439 459 7 (POTENTIAL). FT DOMAIN 460 513 CYTOPLASMIC (POTENTIAL). FT DISULFID 29 82 BY SIMILARITY. FT DISULFID 84 89 BY SIMILARITY. FT DISULFID 93 181 BY SIMILARITY. FT DISULFID 94 107 BY SIMILARITY. FT DISULFID 145 199 BY SIMILARITY. FT CARBOHYD 36 36 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 106 106 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 125 125 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 165 165 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 513 AA; 59038 MW; 9F0B25A5098A314C CRC64; MVSPLIILLI IWLSVGAKSV EIASINHPCA YAHTVNITDG LRMKDGSYSY AGVVVPPHLM AEYSFKVIDG VEYRAKKHLR GCVCLLKPCI SFCCPENLVF DAKHWNCTMP HQVRESTHVE LTYANRTVDQ VRIRDRFVVR TELGCRNKFV DKKHDNFWQW DLFENGTLRR DNRLWSTDEY CFSPLEHNPE QWELTPLNCE RFQTGYRVWI YAICSIIAII INIFILSLLG SVRDARKSHY GQLIIYYLLS MIVGYSLLVY LALKNPMKLS HVACRNIGFL AYFCIMLSFV FLAICSLDFL LKFKQKAVRS SVRRLSLALA VLAVIGLRFL VSLAQDSKLP KHFKPGMGED YCWFDVRTWG ILIYYYGPIA LLLIFSIVCC LKAYFSIYEL PPDTQYILGT QLKIVKTHFY AFSAYIVGVF AVWIREIVVY IMARVREHFF IIDFWSGICI LGLAIAGFIL LLGKNLHVKS WWAINVESSQ TDLSIINARV YKFDEKGDLK SSDSPYKPTV TSL // ID MTHA_DROME STANDARD; PRT; 575 AA. AC Q9W0R5; Q86BK3; Q95NU7; Q95YN4; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 10 precursor (Methuselah- DE like 10 protein). GN MTHL10 OR MTH2 OR CG17061. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE OF 40-575 FROM N.A. RC STRAIN=CT97_1, CT97_3, CT97_4, HFL97_8, HFL97_15, HFL97_16, JFL97_1, RC JFL97_5, JFL97_9, MA97_6, MA97_4, MA97_1, MFL97_1, VT97_1, ZIM(H)23, RC ZIM(H)26, ZIM(H)39, ZIM(H)44, ZIM(S)15, ZIM(S)24, ZIM(S)35, RC ZIM(S)37, and ZIM(S)49; RX MEDLINE=22582089; PubMed=12694290; RA Duvernell D.D., Schmidt P.S., Eanes W.F.; RT "Clines and adaptive evolution in the methuselah gene region in RT Drosophila melanogaster."; RL Mol. Ecol. 12:1277-1285(2003). RN [4] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003468; AAO41210.1; -. DR EMBL; AF300364; AAK97869.1; -. DR EMBL; AF300363; AAK97869.1; JOINED. DR EMBL; AF300366; AAK97870.1; -. DR EMBL; AF300365; AAK97870.1; JOINED. DR EMBL; AF300368; AAK97871.1; -. DR EMBL; AF300367; AAK97871.1; JOINED. DR EMBL; AF300370; AAK97872.1; -. DR EMBL; AF300369; AAK97872.1; JOINED. DR EMBL; AF300372; AAK97873.1; -. DR EMBL; AF300371; AAK97873.1; JOINED. DR EMBL; AF300374; AAK97874.1; -. DR EMBL; AF300373; AAK97874.1; JOINED. DR EMBL; AF300376; AAK97875.1; -. DR EMBL; AF300375; AAK97875.1; JOINED. DR EMBL; AF300378; AAK97876.1; -. DR EMBL; AF300377; AAK97876.1; JOINED. DR EMBL; AF300380; AAK97877.1; -. DR EMBL; AF300379; AAK97877.1; JOINED. DR EMBL; AF300382; AAK97878.1; -. DR EMBL; AF300381; AAK97878.1; JOINED. DR EMBL; AF300384; AAK97879.1; -. DR EMBL; AF300383; AAK97879.1; JOINED. DR EMBL; AF300386; AAK97880.1; -. DR EMBL; AF300385; AAK97880.1; JOINED. DR EMBL; AF300388; AAK97881.1; -. DR EMBL; AF300387; AAK97881.1; JOINED. DR EMBL; AF300390; AAK97882.1; -. DR EMBL; AF300389; AAK97882.1; JOINED. DR EMBL; AF300392; AAK97883.1; -. DR EMBL; AF300391; AAK97883.1; JOINED. DR EMBL; AF300394; AAK97884.1; -. DR EMBL; AF300393; AAK97884.1; JOINED. DR EMBL; AF300396; AAK97885.1; -. DR EMBL; AF300395; AAK97885.1; JOINED. DR EMBL; AF300398; AAK97886.1; -. DR EMBL; AF300397; AAK97886.1; JOINED. DR EMBL; AF300400; AAK97887.1; -. DR EMBL; AF300399; AAK97887.1; JOINED. DR EMBL; AF300402; AAK97888.1; -. DR EMBL; AF300401; AAK97888.1; JOINED. DR EMBL; AF300404; AAK97889.1; -. DR EMBL; AF300403; AAK97889.1; JOINED. DR EMBL; AF300406; AAK97890.1; -. DR EMBL; AF300405; AAK97890.1; JOINED. DR EMBL; AF300408; AAK97891.1; -. DR EMBL; AF300407; AAK97891.1; JOINED. DR HSSP; Q9GT60; 1FJR. DR FlyBase; FBgn0035132; mthl10. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Polymorphism; Multigene family. FT SIGNAL 1 32 POTENTIAL. FT CHAIN 33 575 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 10. FT DOMAIN 33 250 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 251 271 1 (POTENTIAL). FT DOMAIN 272 280 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 281 301 2 (POTENTIAL). FT DOMAIN 302 312 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 313 333 3 (POTENTIAL). FT DOMAIN 334 353 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 354 374 4 (POTENTIAL). FT DOMAIN 375 404 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 405 425 5 (POTENTIAL). FT DOMAIN 426 456 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 457 477 6 (POTENTIAL). FT DOMAIN 478 488 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 489 509 7 (POTENTIAL). FT DOMAIN 510 575 CYTOPLASMIC (POTENTIAL). FT DISULFID 56 110 BY SIMILARITY. FT DISULFID 112 117 BY SIMILARITY. FT DISULFID 121 216 BY SIMILARITY. FT DISULFID 122 135 BY SIMILARITY. FT DISULFID 177 236 BY SIMILARITY. FT CARBOHYD 63 63 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 72 72 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 142 142 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 152 152 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 157 157 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 198 198 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 223 223 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 150 150 M -> V (IN STRAIN ZIM(S)24). SQ SEQUENCE 575 AA; 66005 MW; EEFF0873C8B922B6 CRC64; MPKKIHQPGG SLYCGVTLLG VLCLVVFRLI PGIPFGTYVM AERDHYHTID DPNVPCNFYD TVNLTGHRLF PNGSYDYYGT IVPAELVGTY DYIHSSLTER IEVREHVRGC VCKFKSCLNI CCPWRQVFNS EVDGCIIDHS DNRTWPDPPM LNITFRNEST ILVNMFTQFA IQSFRPCPKM FSLQPETNNW DDYLLFENGS MLRVDDKLLI RKNEFCMVPT YVNESDMFYT IHPANCDMQD DHSTVKIINS YAMMFSIPFM MLTIAVYLLI PELRNQHGKS LVCYLIGLSV GYSSLCYVQL YQVDATGVTC KVFGYTAYFF FMGAYMWLSV ISFDLWHNFR GTRGINRFQE KKRFLFYSLY SWGIALVFLA FTYCAQQLTN LPANLKPGIG DGVYCWLDMS NWAAMIYFYG PILAIVVANT IMFIMTAIKI HGVQREMARI IASENSTKNL RTEKDKFGLF LRLFLIMGIT WLTELISYFV GSDKGWSKLF YISDLANAMQ GFLIFMLFVM KKKVKHLITN RCSSVRDGSN QRQSQYSTKT TSSSVANLSL HEKPSVEKPL VISSSVDPQK TTIFR // ID MTHB_DROME STANDARD; PRT; 471 AA. AC P83118; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 11 precursor (Methuselah- DE like 11 protein) (Fragment). GN MTHL11 OR MTH-LIKE-11. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION. RX MEDLINE=21173629; PubMed=11274391; RA West A.P. Jr., Llamas L.L., Snow P.M., Benzer S., Bjorkman P.J.; RT "Crystal structure of the ectodomain of Methuselah, a Drosophila G RT protein-coupled receptor associated with extended lifespan."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3744-3749(2001). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003687; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0045443; mthl11. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 471 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 11. FT DOMAIN 21 213 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 214 234 1 (POTENTIAL). FT DOMAIN 235 240 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 241 261 2 (POTENTIAL). FT DOMAIN 262 268 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 269 289 3 (POTENTIAL). FT DOMAIN 290 309 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 310 330 4 (POTENTIAL). FT DOMAIN 331 357 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 358 378 5 (POTENTIAL). FT DOMAIN 379 409 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 410 430 6 (POTENTIAL). FT DOMAIN 431 439 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 440 460 7 (POTENTIAL). FT DOMAIN 461 471 CYTOPLASMIC (POTENTIAL). FT DISULFID 26 80 BY SIMILARITY. FT DISULFID 82 87 BY SIMILARITY. FT DISULFID 91 184 BY SIMILARITY. FT DISULFID 92 103 BY SIMILARITY. FT DISULFID 145 204 BY SIMILARITY. FT CARBOHYD 42 42 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 123 123 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 166 166 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 195 195 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). FT NON_TER 471 471 SQ SEQUENCE 471 AA; 55095 MW; 1FA8ABB109EE982B CRC64; MGMFRVEYLL LGILVIGVRS RDIPNCDFFD TVQLRESEKL CNGSYRYEDV VIPAKLTGKY DYEIDYDGDR VSVPKHIRGC VCKLKTCIRF CCHHKKLMAG NLCSQDVYEN LTYEYTLDIT QLNGSVIKKH VLNDMVVQQD LPLPCERHYS LDAETSTYDM WSLYENGSLF RHFDQRYLSK QEFCLQPNPT STGKNYSLIV AFNCIQKPSM NASIPVKFSS VFFMVITIAA YLWLPKFRSL HGKCCNLYFI CLAITFLLNV ISLFGIGYFT VMATFLWLSV ISFDVWRRFA MRKFQVFYKN KRSSFFNYNI IVWSSAGLLT CIIFLVDQFV ETNLDNPYNP AVGVFSCWIF SKLWSATFYF YAPLAILIIL NCASFFLTTR YIYVENKQNQ KVLNNSEPQK LSRNHASYRI YFRLFIIMGG SWFLEIIAFI CEMENMWKPL IILNDYINCS QGIIIFVATF CNHEMFRLIR K // ID MTHC_DROME STANDARD; PRT; 488 AA. AC P83119; Q8INH4; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 12 precursor (Methuselah- DE like 12 protein). GN MTHL12 OR MTH-LIKE-12 OR CG32853. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=21173629; PubMed=11274391; RA West A.P. Jr., Llamas L.L., Snow P.M., Benzer S., Bjorkman P.J.; RT "Crystal structure of the ectodomain of Methuselah, a Drosophila G RT protein-coupled receptor associated with extended lifespan."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3744-3749(2001). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003699; AAN13556.1; ALT_SEQ. DR FlyBase; FBgn0045442; mthl12. DR GO; GO:0004930; F:G-protein coupled receptor activity; ISS. DR GO; GO:0008340; P:determination of adult life span; ISS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; ISS. DR GO; GO:0006950; P:response to stress; ISS. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 488 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 12. FT DOMAIN 18 215 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 216 236 1 (POTENTIAL). FT DOMAIN 237 247 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 248 268 2 (POTENTIAL). FT DOMAIN 269 283 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 284 304 3 (POTENTIAL). FT DOMAIN 305 315 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 316 336 4 (POTENTIAL). FT DOMAIN 337 373 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 374 394 5 (POTENTIAL). FT DOMAIN 395 416 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 417 437 6 (POTENTIAL). FT DOMAIN 438 454 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 455 475 7 (POTENTIAL). FT DOMAIN 476 488 CYTOPLASMIC (POTENTIAL). FT DISULFID 27 81 BY SIMILARITY. FT DISULFID 83 88 BY SIMILARITY. FT DISULFID 92 189 BY SIMILARITY. FT DISULFID 93 104 BY SIMILARITY. FT DISULFID 155 209 BY SIMILARITY. FT CARBOHYD 19 19 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 34 34 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 55 55 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 141 141 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 365 365 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 488 AA; 56780 MW; 3CE6B05F8D1DC103 CRC64; MFLWLKCFCT LIIVTIAKNS SAKIPHCKYD ETINISHFKR LNDAYIYEHF EIPANLTGEF DYKELMDGSK VPTEFPNLRG CICKVRPCIR ICCARKNILS NGECSDGVKN EIKLTMLDLT MQDILLTDPT LAELNMIPQY NSTELLILRE QFQPCDEIVS LKRDEYTILK DGSILLHTSA EILSNDQYCL YPEIYSDFPE TIRIINRRCY RNVMPGIAQL SVISVVGFIL TLAVYLSVEK LRNLLGKCLI CSLFSMFMEY FIWTMDYFRL LQSICSAAGY MKYFFSMSSY LWFSVVSFHL WELFTSLNRH EPQYRFLIYN TFVWCTAAIP TVVIFSMNQM WENDPGKSEW LPLVGYFGCS VKDWNSSSWF YSHIPIVILN SFNVIMFVLT AIYIWKVKKG VKSFAQHDER NTTCLEFNVQ TYIQFVRLFL IMGASWLLDQ LTRLAEDSHL LLDTIVLNLT VYLNAAFGIL IFVLLILKGS TFKMIMER // ID MTHE_DROME STANDARD; PRT; 533 AA. AC Q8SYV9; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable G-protein-coupled receptor Mth-like 14 precursor (Methuselah- DE like 14 protein). GN MTHL14 OR BCDNA:RE31310 OR CG32476. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RC STRAIN=Berkeley; RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY071287; AAL48909.1; -. DR EMBL; AE003467; AAN11432.1; -. DR FlyBase; FBgn0052476; mthl14. DR InterPro; IPR000832; GPCR_secretin. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; FALSE_NEG. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Signal; Multigene family. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 533 PROBABLE G-PROTEIN-COUPLED RECEPTOR MTH- FT LIKE 14. FT DOMAIN 24 242 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 243 263 1 (POTENTIAL). FT DOMAIN 264 279 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 280 300 2 (POTENTIAL). FT DOMAIN 301 303 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 304 324 3 (POTENTIAL). FT DOMAIN 325 347 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 348 368 4 (POTENTIAL). FT DOMAIN 369 395 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 396 416 5 (POTENTIAL). FT DOMAIN 417 451 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 452 472 6 (POTENTIAL). FT DOMAIN 473 480 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 481 501 7 (POTENTIAL). FT DOMAIN 502 533 CYTOPLASMIC (POTENTIAL). FT DISULFID 120 216 BY SIMILARITY. FT DISULFID 121 139 BY SIMILARITY. FT DISULFID 177 230 BY SIMILARITY. FT CARBOHYD 20 20 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 29 29 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 30 30 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 36 36 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 47 47 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 133 133 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 178 178 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 206 206 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 533 AA; 60134 MW; 6D13D70ECCBEAC49 CRC64; MNLGHWNFLL ALISLQTFFN ASAQISTVNN SSKGSNNSNI FHEDTFNSTS IDVLDASIHS TLVVPQTYST EAATISGARF ATSVPVQSPV DNPLDPADCS QREKYRKQPV ATPSSRLRKC CPHGENLNIY RENQSDSMCD NGLLSFEPTI ISAVLFDNCI EDLEVETTLD YDIGNPCNSS LLYDDKDDVF FVLQDGSLLI IDKFGNESYT VKEHYCLDID KSGHLFAFTC VTQVEEQIAF AKVVFVAVLM LISMPCLLLV SYLHMTLRLL RNLHGLSLSL MSLCLASGYF VHSVVHIYGI PNQGFIGYVI QFCILSYFFW YLCICFNVLL NVWYKLPCCI QCSKSWATFN FACYAVFAFS GPATIVALTV QKGLPGMPSY FLQGLTESIR DSQRYFIPPV STILFLSFLL NIISFFGFQR ISGYAKAEKN IQERKCLFDQ QKYEDVKKDA KCVSLLGIIM VVSWLLEIIT FYSGSNSNYL ILCDMVNGLQ GVWVLLIFLV VRRRRTIILR WWYDRGSHEI EGTELQALSN SPT // ID MTH_DROME STANDARD; PRT; 514 AA. AC O97148; Q9GN21; Q9GN78; Q9GND6; Q9GNE8; Q9GT57; Q9GT58; Q9GT59; AC Q9GT60; Q9W0R4; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE G-protein-coupled receptor Mth precursor (Methuselah protein). GN MTH OR CG6936. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), AND FUNCTION. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=99011353; PubMed=9794765; RA Lin Y.-J., Seroude L., Benzer S.; RT "Extended life-span and stress resistance in the Drosophila mutant RT methuselah."; RL Science 282:943-946(1998). RN [2] RP SEQUENCE FROM N.A. (ISOFORM A), AND VARIANTS. RC STRAIN=CT97_1, CT97_3, CT97_4, DPF96_3.0, DPF96_74.2, HFL97_8, RC HFL97_12, HFL97_15, HFL97_16, JFL97_1, JFL97_5, JFL97_9, MA97_1, RC MA97_4, MA97_6, MFL97_1, MFL97_3, MFL97_6, SC96_19.4, VT97_1, VT97_39, RC VT97_41, ZIM(H)23, ZIM(H)26, ZIM(H)39, ZIM(H)44, ZIM(S)15, ZIM(S)24, RC ZIM(S)35, ZIM(S)37, and ZIM(S)49; RX MEDLINE=20461461; PubMed=10995474; RA Schmidt P.S., Duvernell D.D., Eanes W.F.; RT "Adaptive evolution of a candidate gene for aging in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 97:10861-10865(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=22255725; PubMed=12367510; RA Song W., Ranjan R., Dawson-Scully K., Bronk P., Marin L., Seroude L., RA Lin Y.J., Nie Z., Atwood H.L., Benzer S., Zinsmaier K.E.; RT "Presynaptic regulation of neurotransmission in Drosophila by the G RT protein-coupled receptor methuselah."; RL Neuron 36:105-119(2002). RN [7] RP REVIEW. RX MEDLINE=20370890; PubMed=10908591; RA Brody T., Cravchik A.; RT "Drosophila melanogaster G protein-coupled receptors."; RL J. Cell Biol. 150:F83-F88(2000). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-219. RX MEDLINE=21173629; PubMed=11274391; RA West A.P. Jr., Llamas L.L., Snow P.M., Benzer S., Bjorkman P.J.; RT "Crystal structure of the ectodomain of Methuselah, a Drosophila G RT protein-coupled receptor associated with extended lifespan."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3744-3749(2001). CC -!- FUNCTION: INVOLVED IN BIOLOGICAL AGING AND STRESS RESPONSE. CC ESSENTIAL FOR ADULT SURVIVAL. REQUIRED IN THE PRESYNAPTIC MOTOR CC NEURON TO UPREGULATE NEUROTRANSMITTER EXOCYTOSIS AT LARVAL CC GLUTAMATERGIC NEUROMUSCULAR JUNCTIONS (NMJS). REGULATES A STEP CC ASSOCIATED WITH DOCKING AND CLUSTERING OF VESICLES AT RELEASE CC SITES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN; PLASMA MEMBRANE CC OF PRESYNAPTIC TERMINALS AND INNERVATING AXONS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=O97148-1; Sequence=Displayed; CC Name=B; CC IsoId=O97148-2; Sequence=VSP_002023; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC MTH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF109308; AAD16981.1; -. DR EMBL; AF280552; AAG22708.1; ALT_SEQ. DR EMBL; AF280553; AAG22709.1; ALT_SEQ. DR EMBL; AF280554; AAG22710.1; ALT_SEQ. DR EMBL; AF280555; AAG22711.1; ALT_SEQ. DR EMBL; AF280556; AAG22712.1; ALT_SEQ. DR EMBL; AF280557; AAG22713.1; ALT_SEQ. DR EMBL; AF280558; AAG22714.1; ALT_SEQ. DR EMBL; AF280559; AAG22715.1; ALT_SEQ. DR EMBL; AF280560; AAG22716.1; ALT_SEQ. DR EMBL; AF280561; AAG22717.1; ALT_SEQ. DR EMBL; AF280562; AAG22718.1; ALT_SEQ. DR EMBL; AF280563; AAG22719.1; ALT_SEQ. DR EMBL; AF280564; AAG22720.1; ALT_SEQ. DR EMBL; AF280565; AAG22721.1; ALT_SEQ. DR EMBL; AF280566; AAG22722.1; ALT_SEQ. DR EMBL; AF280567; AAG22723.1; ALT_SEQ. DR EMBL; AF280568; AAG22724.1; ALT_SEQ. DR EMBL; AF280569; AAG22725.1; ALT_SEQ. DR EMBL; AF280570; AAG22726.1; ALT_SEQ. DR EMBL; AF280571; AAG22727.1; ALT_SEQ. DR EMBL; AF280572; AAG22728.1; ALT_SEQ. DR EMBL; AF280573; AAG22729.1; ALT_SEQ. DR EMBL; AF280574; AAG22730.1; ALT_SEQ. DR EMBL; AF280575; AAG22731.1; ALT_SEQ. DR EMBL; AF280576; AAG22732.1; ALT_SEQ. DR EMBL; AF280577; AAG22733.1; ALT_SEQ. DR EMBL; AF280578; AAG22734.1; ALT_SEQ. DR EMBL; AF280579; AAG22735.1; ALT_SEQ. DR EMBL; AF280580; AAG22736.1; ALT_SEQ. DR EMBL; AF280581; AAG22737.1; ALT_SEQ. DR EMBL; AF280582; AAG22738.1; ALT_SEQ. DR EMBL; AE003468; AAF47379.2; -. DR EMBL; AE003468; AAN11440.1; -. DR EMBL; AY052111; AAK93535.1; -. DR PDB; 1FJR; 04-APR-01. DR FlyBase; FBgn0023000; mth. DR GO; GO:0016021; C:integral to membrane; TAS. DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS. DR GO; GO:0008340; P:determination of adult life span; IMP. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS. DR GO; GO:0006950; P:response to stress; IMP. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00002; 7tm_2; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW Exocytosis; Neurotransmitter transport; Receptor; KW G-protein coupled receptor; Signal; Transmembrane; Glycoprotein; KW Alternative splicing; Polymorphism; Multigene family; 3D-structure. FT SIGNAL 1 24 FT CHAIN 25 514 G-PROTEIN-COUPLED RECEPTOR MTH. FT DOMAIN 25 218 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 219 239 1 (POTENTIAL). FT DOMAIN 240 248 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 249 269 2 (POTENTIAL). FT DOMAIN 270 278 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 279 299 3 (POTENTIAL). FT DOMAIN 300 320 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 321 341 4 (POTENTIAL). FT DOMAIN 342 370 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 371 391 5 (POTENTIAL). FT DOMAIN 392 424 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 425 445 6 (POTENTIAL). FT DOMAIN 446 454 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 455 475 7 (POTENTIAL). FT DOMAIN 476 514 CYTOPLASMIC (POTENTIAL). FT DISULFID 29 83 FT DISULFID 85 90 FT DISULFID 94 188 FT DISULFID 95 106 FT DISULFID 150 209 FT CARBOHYD 45 45 N-LINKED (GLCNAC...). FT CARBOHYD 109 109 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 123 123 N-LINKED (GLCNAC...). FT CARBOHYD 170 170 N-LINKED (GLCNAC...). FT CARBOHYD 198 198 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 449 449 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 487 514 SIRGEGEEVNNSEEEISLENTTTRNVLL -> RNHPKSTRS FT VISNRSMASRITVGTTPKNKARNSPLA (in isoform FT B). FT /FTId=VSP_002023. FT VARIANT 1 1 M -> I (IN STRAIN ZIM(S)37). FT VARIANT 54 54 L -> I (IN STRAIN MA97_6). FT VARIANT 132 132 S -> A (IN STRAINS ZIM(S)49 AND FT ZIM(H)44). FT VARIANT 151 151 D -> N (IN STRAINS CT97_3, MFL97_1 AND FT ZIM(S)37). FT VARIANT 281 281 F -> V (IN STRAINS ZIM(S)49 AND FT ZIM(H)44). FT VARIANT 357 357 H -> N (IN STRAINS DPF96_3.0, HFL97_15, FT JFL97_1, JFL97_9 AND ZIM(S)37). FT VARIANT 387 387 T -> N (IN STRAIN ZIM(S)35). FT VARIANT 407 407 A -> V (IN STRAIN ZIM(H)23). SQ SEQUENCE 514 AA; 59644 MW; F2A5370CECCD1D5C CRC64; MKTLLVLRIS TVILVVLVIQ KSYADILECD YFDTVDISAA QKLQNGSYLF EGLLVPAILT GEYDFRILPD DSKQKVARHI RGCVCKLKPC VRFCCPHDHI MDNGVCYDNM SDEELAELDP FLNVTLDDGS VSRRHFKNEL IVQWDLPMPC DGMFYLDNRE EQDKYTLFEN GTFFRHFDRV TLRKREYCLQ HLTFADGNAT SIRIAPHNCL IVPSITGQTV VMISSLICMV LTIAVYLFVK KLQNLHGKCF ICYMVCLFMG YLFLLLDLWQ ISISFCKPAG FLGYFFVMAA FFWLSVISLH LWNTFRGSSH KANRFLFEHR FLAYNTYAWG MAVVLTGITV LADNIVENQD WNPRVGHEGH CWIYTQAWSA MLYFYGPMVF LIAFNITMFI LTAKRILGVK KDIQNFAHRQ ERKQKLNSDK QTYTFFLRLF IIMGLSWSLE IGSYFSQSNQ TWANVFLVAD YLNWSQGIII FILFVLKRST WRLLQESIRG EGEEVNNSEE EISLENTTTR NVLL // ID MTK_DROME STANDARD; PRT; 52 AA. AC Q24395; Q24396; Q9V7B9; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Metchnikowin precursor. GN MTK OR CG8175. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 27-52. RC STRAIN=Oregon-R; TISSUE=Abdomen, and Thorax; RX MEDLINE=96067716; PubMed=7588819; RA Levashina E.A., Ohresser S., Bulet P., Reichhart J.-M., Hetru C., RA Hoffmann J.A.; RT "Metchnikowin, a novel immune-inducible proline-rich peptide from RT Drosophila with antibacterial and antifungal properties."; RL Eur. J. Biochem. 233:694-700(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=98263241; PubMed=9600835; RA Levashina E.A., Ohresser S., Lemaitre B., Imler J.-L.; RT "Two distinct pathways can control expression of the gene encoding RT the Drosophila antimicrobial peptide metchnikowin."; RL J. Mol. Biol. 278:515-527(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP INDUCTION, MASS SPECTROMETRY, AND TISSUE SPECIFICITY. RX MEDLINE=98409659; PubMed=9736738; RA Uttenweiler-Josepash S., Moniatte M., Lagueux M., Van Dorsselaer A., RA Hoffmann J.A., Bulet P.; RT "Differential display of peptides induced during the immune response RT of Drosophila: a matrix-assisted laser desorption ionization RT time-of-flight mass spectrometry study."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998). CC -!- FUNCTION: POTENT ANTIFUNGAL AND ANTIBACTERIAL ACTIVITY AGAINST CC GRAM-POSITIVE BACTERIA. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: HIGHEST EXPRESSION IN FAT BODY. MAYBE BLOOD CC CELLS PARTICIPATE IN THE PRODUCTION OF THE PEPTIDE. IN HEMOLYMPH 6 CC HOURS AFTER IMMUNE CHALLENGE, LEVELS OF EXPRESSION INCREASE FOR CC FIRST 24 HOURS AND PERSIST FOR THE FOLLOWING TWO WEEKS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED RAPIDLY AND STRONGLY AT ALL STAGES. CC -!- MASS SPECTROMETRY: MW=3045.4; METHOD=MALDI. CC -!- POLYMORPHISM: THERE ARE 2 ALLELIC FORMS (A1 AND A2) VARYING IN TWO CC POSITIONS. THE ISOFORM SHOWN HERE IS A1. CC -!- SIMILARITY: TO DIPTERICIN, HEMIPTERICIN, DROSOCIN, APIDAECINS AND CC TO THE C-TERMINUS OF ABAECIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X91060; CAA62511.1; -. DR EMBL; X91061; CAA62512.1; -. DR EMBL; AF030959; AAC64659.1; -. DR EMBL; AE003811; AAF58139.1; -. DR PIR; S63981; S63981. DR FlyBase; FBgn0014865; Mtk. DR GO; GO:0003799; F:antifungal peptide activity; IDA. DR GO; GO:0008224; F:Gram-positive antibacterial peptide activity; IDA. DR GO; GO:0006961; P:antibacterial humoral response (sensu Inver...; IEP. DR GO; GO:0006966; P:antifungal humoral response (sensu Inverteb...; IEP. KW Insect immunity; Antibiotic; Fungicide; Signal. FT SIGNAL 1 24 POTENTIAL. FT PROPEP 25 26 FT PEPTIDE 27 52 METCHNIKOWIN. FT VARIANT 19 19 A -> T (IN STRAIN A2). FT VARIANT 29 29 H -> R (IN STRAIN A2). SQ SEQUENCE 52 AA; 5654 MW; 0B1E2112BAE03129 CRC64; MQLNLGAIFL ALLGVMATAT SVLAEPHRHQ GPIFDTRPSP FNPNQPRPGP IY // ID MVL_DROME STANDARD; PRT; 596 AA. AC P49283; Q95TT7; Q9VDF5; DT 01-FEB-1996 (Rel. 33, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Malvolio protein. GN MVL OR CG3671. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM C). RX MEDLINE=95347327; PubMed=7621816; RA Rodrigues V., Cheah P.Y., Ray K., Chia W.; RT "Malvolio, the Drosophila homologue of mouse NRAMP-1 (Bcg), is RT expressed in macrophages and in the nervous system and is required RT for normal taste behaviour."; RL EMBO J. 14:3007-3020(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PUTATIVE TRANSPORTER REQUIRED FOR NORMAL TASTE CC BEHAVIOR. MAY BE A NITRITE/NITRATE TRANSPORTER. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=B; CC IsoId=P49283-2; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=P49283-1; Sequence=VSP_008202; CC -!- TISSUE SPECIFICITY: EXPRESSED IN MACROPHAGES AND IN THE NERVOUS CC SYSTEM. CC -!- MISCELLANEOUS: 'MALVOLIO' IS A CHARACTER IN SHAKESPEARE'S TWELFTH CC NIGHT, WHO 'TASTE(D) WITH DISTEMPERED APPETITE'. CC -!- SIMILARITY: BELONGS TO THE NRAMP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U23948; AAA82593.1; -. DR EMBL; AE003733; AAF55839.2; -. DR EMBL; AY058543; AAL13772.1; -. DR PIR; S56140; S56140. DR FlyBase; FBgn0011672; Mvl. DR InterPro; IPR001046; Nramp. DR Pfam; PF01566; Nramp; 1. DR PRINTS; PR00447; NATRESASSCMP. DR ProDom; PD001861; Nramp; 1. DR TIGRFAMs; TIGR01197; nramp; 1. KW Transport; Transmembrane; Glycoprotein; Alternative splicing. FT TRANSMEM 77 97 POTENTIAL. FT TRANSMEM 105 125 POTENTIAL. FT TRANSMEM 154 174 POTENTIAL. FT TRANSMEM 186 206 POTENTIAL. FT TRANSMEM 216 236 POTENTIAL. FT TRANSMEM 263 283 POTENTIAL. FT TRANSMEM 309 329 POTENTIAL. FT TRANSMEM 373 393 POTENTIAL. FT TRANSMEM 424 444 POTENTIAL. FT TRANSMEM 463 483 POTENTIAL. FT TRANSMEM 490 510 POTENTIAL. FT TRANSMEM 520 540 POTENTIAL. FT CARBOHYD 41 41 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 359 359 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 574 574 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 487 596 Missing (in isoform C). FT /FTId=VSP_008202. SQ SEQUENCE 596 AA; 65466 MW; 1128C4A7795C2F9E CRC64; MSSNEAYHEP GAGGDGPGGS SGASGGGSQR SNQLHHQQIL NETTYLKPAA KQAYFSDEKV LIPDDDSTNV GFSFRKLWAF TGPGFLMSIA YLDPGNIESD MQSGAAAKYK ILWVLLWATV LGLLMQRLAA RLGVVTGLHL AEMCYRQYKR LPRWILWIMI EIAIIGSDMQ EVIGTAIAIY LLSNKVVPLW GGVLITIVDT FTFLFLDKYG LRKLEFLFGT LITIMAVSFG YEYIVSAPNQ GEVLEGMFVP WCSNCNSNVL LQAVGVVGAV IMPHNLYLHS ALVKSRDIDR RQTKKVSEAN FYFFIEASVA LFVSFIINLF VVAVFAHGMY GKTNNDVVEV CKDKSMYEDA KMSFVDNVNG TAIIDADLYK GGLFLGCTFG AVAMYIWGVG ILAAGQSSTM TGTYAGQFSM EGFLNLQWPR WCRVLVTRCI AIIPTFCLAM FSKMEDLTSM NDILNAVMSL QLPFAAIPTI AFTSCAAIMG EFVNGLGNKI VSILLTIVVI GVNLYFVVVQ VENMEIKGGL LALVCIFAIL YILFNLYLVI HMAACMGNQR LMNSRWVQRF VLPSQNSFSI KNANSTYARI ATSSDQEPEG LAGEDA // ID MY1A_DROME STANDARD; PRT; 1011 AA. AC Q23978; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myosin IA (MIA) (Brush border myosin IA) (BBMIA). GN MYO31DF OR CG7438. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=94260541; PubMed=8201616; RA Morgan N.S., Skovronsky D.M., Artavanis-Tsakonas S., Mooseker M.S.; RT "The molecular cloning and characterization of Drosophila melanogaster RT myosin-IA and myosin-IB."; RL J. Mol. Biol. 239:347-356(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=96069904; PubMed=7589814; RA Morgan N.S., Heintzelman M.B., Mooseker M.S.; RT "Characterization of myosin-IA and myosin-IB, two unconventional RT myosins associated with the Drosophila brush border cytoskeleton."; RL Dev. Biol. 172:51-71(1995). CC -!- FUNCTION: INVOLVED IN DIRECTING THE MOVEMENT OF ORGANELLES ALONG CC ACTIN FILAMENTS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. PROTEIN SHIFTS FROM THE CC BASOLATERAL TO APICAL DOMAIN IN ENTEROCYTES AND FOLLICLE CC CELLS. CC -!- TISSUE SPECIFICITY: IN THE EMBRYO, EXPRESSED IN GASTRIC CAECAE, CC MIDGUT CELLS OF THE PROVENTRICULUS, AND IN THE MID AND HINDGUT. IN CC THE LARVAL GUT BRUSH BORDER, EXPRESSION IS IN THE TERMINAL WEB CC DOMAIN. IN THE ADULT GUT BRUSH BORDER, EXPRESSION REMAINS IN THE CC WEB DOMAIN AND HAS ALSO MOVED INTO THE MICROVILLI. ALSO EXPRESSED CC AT LOW LEVELS IN FOLLICLE CELLS DURING OOGENESIS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT TO ADULTHOOD WITH HIGHEST LEVELS AT THE END CC OF LARVAL DEVELOPMENT. EXPRESSION IN EMBRYOGENESIS IS CORRELATED CC WITH THE FORMATION OF A BRUSH BORDER WITHIN THE ALIMENTARY CC CANAL. CC -!- SIMILARITY: CONTAINS 1 MYOSIN-LIKE GLOBULAR HEAD DOMAIN. CC -!- SIMILARITY: CONTAINS 2 IQ DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U07595; AAA19590.1; -. DR EMBL; AE003628; AAF52966.1; -. DR HSSP; P08799; 1MND. DR FlyBase; FBgn0011673; Myo31DF. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR001609; myosin_head. DR Pfam; PF00612; IQ; 2. DR Pfam; PF00063; myosin_head; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR ProDom; PD000355; myosin_head; 1. DR SMART; SM00015; IQ; 2. DR SMART; SM00242; MYSc; 1. DR PROSITE; PS50096; IQ; 1. KW Myosin; ATP-binding; Actin-binding; Calmodulin-binding; Repeat; KW Multigene family. FT DOMAIN 1 694 MYOSIN HEAD-LIKE. FT DOMAIN 695 721 IQ 1. FT DOMAIN 716 736 IQ 2. FT NP_BIND 100 107 ATP (BY SIMILARITY). FT DOMAIN 567 589 ACTIN-BINDING (BY SIMILARITY). SQ SEQUENCE 1011 AA; 117094 MW; 31206C065B5D5DFA CRC64; MAMQREAGVQ DFVLLDQVSM EKFMDNLRKR FQNGSIYTYI GEVCVSMNPY RQMNIYGPET IRKYKGRELF ENAPHLFAIA DSAYRVLKQR QQDTCILISG ESGAGKTEAS KIIMKYIAAV TNAQGQNEIE RVKNVLIQSN AILETFGNAK TNRNDNSSRF GKYMDIEFDY KADPVGGIIT NYLLEKSRVV QQQPGERNFH SFYQLLRGAN DNELRQYELQ KETGKYHYLN QGSMDILTEK SDYKGTCNAF KTLGFSTDEV QTIWRTIAAV LHLGNVEFQT IEDELVISNK QHLKSTAKLL QVTETELSTA LTKRVIAAGG NVMQKDHNAT QAEYGKDALA KAIYDRLFTW IISRINRAIL FRGSKTQARF NSVIGVLDIY GFEIFDSNSF EQFCINYCNE KLQQLFIELV LKQEQEEYQR EGIEWTNIEY FNNKIICDLV EQPHKGIIAI MDEACLSVGK VTDDTLLGAM DKNLSKHPHY TSRQLKPTDK ELKHREDFRI THYAGDVIYN INGFIEKNKD TLYQDFKRLL HNSKDANLSE MWPEGAQDIK KTTKRPLTAG TLFQRSMADL VVTLLKKEPF YVRCIKPNDL KSSTVFDEER VEHQVRYLGL LENLRVRRAG FVHRQRYDKF LLRYKMISQY TWPNFRAGSD RDGVRVLIEE KKFAQDVKYG HTKIFIRSPR TLFALEHQRN EMIPHIVTLL QKRVRGWIVR RNFKKMKAAI TIVRAYKAYK LRSYVQELAN RLRKAKQMRD YGKSIQWPQP PLAGRKVEAK LHRMFDFWRA NMILHKYPRS EWPQLRLQII AATALAGRRP YWGQARRWVG DYLANSQENS GYEAYNGSIK NIRNHPADGE TFQQVLFSSF VKKFNHFNKQ ANRAFIVSDS TIHKLDGIKN KFKDMKRTIK IRELTSISVS PGRDQLIVFH SSKNKDLVFS LESEYTPLKE DRIGEVVGIV CKKYHDLTGT ELRVNVTTNI SCRLDGKARI ITVEAASNVE VPNFRPKEGN IIFEVPAAYC V // ID MY1B_DROME STANDARD; PRT; 1026 AA. AC Q23979; Q9W0H0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myosin IB (MIB) (Brush border myosin IB) (BBMIB). GN MYO61F OR CG9155. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RC TISSUE=Head; RX MEDLINE=94260541; PubMed=8201616; RA Morgan N.S., Skovronsky D.M., Artavanis-Tsakonas S., Mooseker M.S.; RT "The molecular cloning and characterization of Drosophila melanogaster RT myosin-IA and myosin-IB."; RL J. Mol. Biol. 239:347-356(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 338-697 FROM N.A. RX MEDLINE=94029958; PubMed=8216259; RA Cheney C.M., Kravit N.G., Verbsky J.W.; RT "A new myosin I gene in Drosophila."; RL Biochem. Biophys. Res. Commun. 195:1280-1288(1993). RN [4] RP SEQUENCE OF 630-1026 FROM N.A. RA Caggese C.; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=96069904; PubMed=7589814; RA Morgan N.S., Heintzelman M.B., Mooseker M.S.; RT "Characterization of myosin-IA and myosin-IB, two unconventional RT myosins associated with the Drosophila brush border cytoskeleton."; RL Dev. Biol. 172:51-71(1995). CC -!- FUNCTION: INVOLVED IN DIRECTING THE MOVEMENT OF ORGANELLES ALONG CC ACTIN FILAMENTS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. PROTEIN SHIFTS FROM THE CC BASOLATERAL TO APICAL DOMAIN IN ENTEROCYTES AND FOLLICLE CC CELLS. CC -!- TISSUE SPECIFICITY: IN THE EMBRYO, EXPRESSED IN GASTRIC CAECAE, CC MIDGUT CELLS OF THE PROVENTRICULUS, AND IN THE MID AND HINDGUT. IN CC THE LARVAL AND ADULT GUT BRUSH BORDER, EXPRESSED IN THE CC MICROVILLI. ALSO EXPRESSED AT HIGH LEVELS IN FOLLICLE CELLS DURING CC OOGENESIS. CC -!- DEVELOPMENTAL STAGE: EXPRESSION STARTS AT 8-12 HOURS EMBRYONIC CC DEVELOPMENT, CONTINUES TO INCREASE UNTIL THIRD LARVAL INSTAR, CC DISAPPEARS IN PUPAE AND IS PRESENT AT A LOW LEVEL IN ADULTS. CC EXPRESSION IN EMBRYOGENESIS IS CORRELATED WITH THE FORMATION OF A CC BRUSH BORDER WITHIN THE ALIMENTARY CANAL. CC -!- SIMILARITY: CONTAINS 1 MYOSIN-LIKE GLOBULAR HEAD DOMAIN. CC -!- SIMILARITY: CONTAINS 2 IQ DOMAINS. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U07596; AAA19591.1; -. DR EMBL; AE003471; AAF47477.1; ALT_SEQ. DR EMBL; L13070; -; NOT_ANNOTATED_CDS. DR EMBL; AJ000879; CAA04367.1; -. DR PIR; S45574; S45574. DR HSSP; P08799; 1MND. DR FlyBase; FBgn0010246; Myo61F. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR001609; myosin_head. DR Pfam; PF00612; IQ; 2. DR Pfam; PF00063; myosin_head; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR ProDom; PD000355; myosin_head; 1. DR SMART; SM00015; IQ; 3. DR SMART; SM00242; MYSc; 1. DR PROSITE; PS50096; IQ; 1. KW Myosin; ATP-binding; Calmodulin-binding; Actin-binding; Repeat. FT DOMAIN 1 ? MYOSIN HEAD-LIKE. FT DOMAIN ? ? IQ 1. FT DOMAIN 697 724 IQ 2. FT NP_BIND 105 112 ATP (BY SIMILARITY). FT DOMAIN 583 590 ACTIN-BINDING (BY SIMILARITY). FT CONFLICT 64 64 D -> N (IN REF. 1). FT CONFLICT 221 221 R -> G (IN REF. 1). FT CONFLICT 242 242 R -> S (IN REF. 1). FT CONFLICT 262 262 T -> G (IN REF. 1). FT CONFLICT 545 545 S -> N (IN REF. 2). FT CONFLICT 551 552 EL -> DV (IN REF. 3). FT CONFLICT 688 688 D -> AI (IN REF. 3). SQ SEQUENCE 1026 AA; 117955 MW; 60852B647FE98057 CRC64; METGLHERDR AGVQDFVLLE NYQSEEAFIG NLKKRFQEDL IYTYIGQVLI SVNPYKQLPI YTDDHVKAYR NKHFYEMPPH IFAVTDNAFR SLIEENRGQC VLISGESGSG KTEASKKVLQ FIAACSGNQT TVEGVKDKLL KSNPVLEAFG NAKTNRNDNS SRFGKYMDIQ FDFKGAPIGG NILNYLLEKS RVVAQMGGER NFHIFYQLLA GADEALLQEL RLERALDTYS YLTDGLNGTV TRINDADSFK QVQQALTVID FTKEEQREIF GIVASILHLG NVGFTEVEGN AKVNSRDLVV TAARLLGVNA SELEAALTHR TIDARGDVVT SPLNQELAIY ARDALAKAVY DRLFSWLVQR LNISLQAKET RASRNNVMGI LDIYGFEIFQ KNSFEQFCIN FCNEKLQQLF IELTLKSEQD EYRREGIEWI PVEYFDNKVI CNLIEEKHKG IISILDEECL RPGEPTDKTF LEKLTQKLAQ HHHYVCHEKA PAHIKKIMLR DEFRLVHYAG EVTYSVNGFL DKNNDLLFRD LKETLSKAGN GIVRSCFPEK ELRSLKRPET AITQFRASLN NLMDILMCKE PSYIRCIKPN DLQTANVFND ELVLHQVKYL GLMENLRVRR AGFAYRRTYE LFLERYKSLS KSTWPNYKGP GGPKAGVQQL VKDLGWDEEK YRVGETKLFI RWPRTLFDTE DAYQEKKHEI AAIIQAHWKG LMQRRKYLKL RAQVIIMQSY CRRKLAQQAA KKRREAADKI RAFIKGFITR NDAPNGFNEE FIANAKRMWL LRLAKELPTK VLDKSWPHAP GHCEEASGIL HRLHRLHLAR IYRLKLTPQQ KRQFELKVLA EKVFKGKKNN YASSVSTWFQ EDRIPKEHIQ RVNDFVASTF GSEQLKYQSF CTKFDRHGYK SRDRFILLSN KAIYVLDGKT YKQKHRLPLD KIDFTLTNHN DDLMVIRIPL DLKKDKGDLI LIIPRIIEFS TYIIDTVGTA SIVSIVDRNS LEHNVVKGKG GVIDIQTGAE PGVVRDKGHL VIIGTQ // ID MYB_DROME STANDARD; PRT; 657 AA. AC P04197; Q9VXM9; DT 20-MAR-1987 (Rel. 04, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myb protein. GN MYB OR CG9045. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=88082681; PubMed=3121304; RA Peters C.W.B., Sippel A.E., Vingron M., Klempnauer K.-H.; RT "Drosophila and vertebrate myb proteins share two conserved regions, RT one of which functions as a DNA-binding domain."; RL EMBO J. 6:3085-3090(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-441 FROM N.A. RX MEDLINE=85176969; PubMed=3921261; RA Katzen A.L., Kornberg T.B., Bishop J.M.; RT "Isolation of the proto-oncogene c-myb from D. melanogaster."; RL Cell 41:449-456(1985). CC -!- FUNCTION: DNA-BINDING PROTEIN THAT SPECIFICALLY RECOGNIZES THE CC SEQUENCE 5'-YAAC[GT]G-3'. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 3 MYB-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05939; CAA29373.1; -. DR EMBL; AE003500; AAF48529.1; -. DR EMBL; M11281; AAA70367.1; -. DR PIR; S00578; TVFFMA. DR HSSP; P01103; 1POM. DR FlyBase; FBgn0002914; Myb. DR GO; GO:0007049; P:cell cycle; IGI. DR GO; GO:0007098; P:centrosome cycle; IMP. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA. DR InterPro; IPR001005; Myb_DNA_binding. DR Pfam; PF00249; myb_DNA-binding; 3. DR SMART; SM00717; SANT; 3. DR PROSITE; PS00037; MYB_1; 3. DR PROSITE; PS00334; MYB_2; 3. DR PROSITE; PS50090; MYB_3; 3. KW Nuclear protein; DNA-binding; Repeat. FT DNA_BIND 87 130 MYB 1. FT DNA_BIND 131 182 MYB 2. FT DNA_BIND 183 233 MYB 3. FT CONFLICT 370 370 A -> V (IN REF. 1). FT CONFLICT 440 441 QL -> KY (IN REF. 3). SQ SEQUENCE 657 AA; 74045 MW; 8265B37ABB250AE4 CRC64; MASASTENGE ELMNYGSNSD SEESEYSENE DTQVCDKDSQ QNSNADSGYP LDSPELQDSK TTGQKGQNKS GKTSIGAVHP NYGFGKRWSK SEDVLLKQLV ETHGENWEII GPHFKDRLEQ QVQQRWAKVL NPELIKGPWT RDEDDMVIKL VRNFGPKKWT LIARYLNGRI GKQCRERWHN HLNPNIKKTA WTEKEDEIIY QAHLELGNQW AKIAKRLPGR TDNAIKNHWN STMRRKYDVE RRSVNASGSD LKSSRTHLIT LIKSGGISKC MNNMQHNKES GGEAVNKSEN ADGASVTAVK GGDLAQESQD DHQKGSNLAH LSMQHLIKLT MPRQTPIILK RTRKHIPETH HQAGCSSSET FNQEEAAGNA RSRPPSSPVI SPIKSLPFSP SHFLKSPCLT TFEDMDLRAS TPVTKVYNRV GMEIKKEMET SSIETPHKSQ LGPRTPTPFK KALAAIGKKR DGRRYEPSSP SSLVEDLAEI IHEEHLSNSL TANNSKMMGA ADQNSTLSTE YNAQSPPHMK RARKSLLSTW SSNHPYNAGS AKRIQPFETE TPSKFLTSPG DILKDTLCSE QDLPFDEGRK ENRPFHNRRI NKYRGGLTYD HVIDPKWARV ACGKSRDQMF MEEQAYACLK NLSCISRSLN FEKQKCLVNS FDRFGSL // ID MYOD_DROME STANDARD; PRT; 332 AA. AC P22816; Q9VCJ1; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Myogenic-determination protein (Nautilus protein) (dMyd). GN NAU OR MYD OR CG10250. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX MEDLINE=91219456; PubMed=1902570; RA Paterson B.M., Walldorf U., Eldridge J., Duebendorfer A., RA Frasch M., Gehring W.J.; RT "The Drosophila homologue of vertebrate myogenic-determination genes RT encodes a transiently expressed nuclear protein marking primary RT myogenic cells."; RL Proc. Natl. Acad. Sci. U.S.A. 88:3782-3786(1991). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=91099658; PubMed=2176634; RA Michelson A.M., Abmayr S.M., Bate M., Arias A.M., Maniatis T.; RT "Expression of a MyoD family member prefigures muscle pattern in RT Drosophila embryos."; RL Genes Dev. 4:2086-2097(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY PLAY AN IMPORTANT ROLE IN THE EARLY DEVELOPMENT OF CC MUSCLE. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: INITIALLY LOCALIZED TO SEGMENTALLY REPEATED CC CLUSTERS OF MESODERMAL CELLS, AND SUBSEQUENTLY IN AT LEAST A CC SUBSET OF GROWING MUSCLE PRECURSORS AND MATURE MUSCLE FIBERS THAT CC EXHIBIT DISTINCT SEGMENTAL DIFFERENCES. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M68897; AAA28477.1; -. DR EMBL; X56161; CAA39629.1; -. DR EMBL; AE003744; AAF56168.1; -. DR PIR; A36663; A36663. DR HSSP; P10085; 1MDY. DR TRANSFAC; T01540; -. DR FlyBase; FBgn0002922; nau. DR InterPro; IPR002546; Basic. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF01586; Basic; 1. DR Pfam; PF00010; HLH; 1. DR SMART; SM00520; BASIC; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Myogenesis; DNA-binding; Nuclear protein; Developmental protein; KW Transcription regulation; Differentiation. FT DNA_BIND 161 173 BASIC DOMAIN. FT DOMAIN 174 213 HELIX-LOOP-HELIX MOTIF. FT CONFLICT 28 29 PT -> QA (IN REF. 2). FT CONFLICT 95 97 HPA -> NPV (IN REF. 3). FT CONFLICT 131 131 L -> H (IN REF. 1). SQ SEQUENCE 332 AA; 36185 MW; 5DD23D24CAA8BEFC CRC64; MTKYNSGSSE MPAAQTIKQE YHNGYGQPTH PGYGFSAYSQ QNPIAHPGQN PHQTLQNFFS RFNAVGDASA GNGGAASISA NGSGSSCNYS HANHHPAELD KPLGMNMTPS PIYTTDYDDE NSSLSSEEHV LAPLVCSSAQ SSRPCLTWAC KACKKKSVTV DRRKAATMRE RRRLRKVNEA FEILKRRTSS NPNQRLPKVE ILRNAIEYIE SLEDLLQESS TTRDGDNLAP SLSGKSCQSD YLSSYAGAYL EDKLSFYNKH MEKYGQFTDF DGNANGSSLD CLNLIVQSIN KSTTSPIQNK ATPSASDTQS PPSSGATAPT SLHVNFKRKC ST // ID MYS9_DROME STANDARD; PRT; 1253 AA. AC Q01989; Q9VCA4; DT 01-JUN-1994 (Rel. 29, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Myosin heavy chain 95F (95F MHC) (Jaguar protein). GN JAR OR MHC95F OR CG5695. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., CHARACTERIZATION, AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; TISSUE=Embryo, and Ovary; RX MEDLINE=93054915; PubMed=1429838; RA Kellerman K.A., Miller K.G.; RT "An unconventional myosin heavy chain gene from Drosophila RT melanogaster."; RL J. Cell Biol. 119:823-834(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM EM-3). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX MEDLINE=98139549; PubMed=9472041; RA Lantz V.A., Miller K.G.; RT "A class VI unconventional myosin is associated with a homologue of a RT microtubule-binding protein, cytoplasmic linker protein-170, in RT neurons and at the posterior pole of Drosophila embryos."; RL J. Cell Biol. 140:897-910(1998). CC -!- FUNCTION: MYOSIN IS A PROTEIN THAT BINDS TO ACTIN AND HAS ATPASE CC ACTIVITY THAT IS ACTIVATED BY ACTIN. TOGETHER CLIP-190 AND JAR MAY CC COORDINATE THE INTERACTION BETWEEN THE ACTIN AND MICROTUBULE CC CYTOSKELETON. MAY LINK ENDOCYTIC VESICLES TO MICROTUBULES AND MAY CC BE INVOLVED IN TRANSPORT IN THE EARLY EMBRYO AND IN THE DYNAMIC CC PROCESS OF DORSAL CLOSURE. IT IS BELIEVED THAT ITS FUNCTION CC CHANGES DURING THE LIFE CYCLE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC; MICROTUBULE-ASSOCIATED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist; CC Name=Em-3; Synonyms=A, B; CC IsoId=Q01989-1; Sequence=Displayed; CC Name=Em-1; CC IsoId=Q01989-2; Sequence=VSP_003343; CC Name=Em-5; CC IsoId=Q01989-3; Sequence=VSP_003344, VSP_003345; CC Name=145 kDa; CC IsoId=Q01989-4; Sequence=Not described; CC -!- TISSUE SPECIFICITY: ISOFORM EM-3 IS PRESENT AT A HIGHER LEVEL IN CC THE HEAD AND GONADS THAN IN THE THORAXES. ISOFORM 145 KDA IS FOUND CC ONLY IN THE HEAD. CLIP-190 AND JAR ARE COEXPRESSED AT SEVERAL CC TIMES IN DEVELOPMENT AND IN A NUMBER OF TISSUES, INCLUDING CC EMBRYONIC AXONAL NEURON PROCESSES AND POSTERIOR POLE. CC -!- DEVELOPMENTAL STAGE: ISOFORM EM-3 IS EXPRESSED BOTH MATERNALLY AND CC ZYGOTICALLY THROUGHOUT DEVELOPMENT WITH HIGHEST LEVEL DURING MID- CC EMBRYOGENESIS AND ADULTHOOD. AT THESE ZYGOTIC STAGES ISOFORM EM-5 CC IS ALSO EXPRESSED. CC -!- SIMILARITY: CONTAINS 1 MYOSIN-LIKE GLOBULAR HEAD DOMAIN. CC -!- SIMILARITY: CONTAINS 1 IQ DOMAIN. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 1147. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67077; CAA47462.1; -. DR EMBL; AE003747; AAF56269.1; -. DR EMBL; BT004859; AAO45215.1; ALT_FRAME. DR PIR; A44400; A44400. DR HSSP; P08799; 1MND. DR FlyBase; FBgn0011225; jar. DR GO; GO:0030139; C:endocytic vesicle; IDA. DR GO; GO:0005875; C:microtubule associated complex; IDA. DR GO; GO:0016461; C:unconventional myosin; IDA. DR GO; GO:0003779; F:actin binding; IDA. DR GO; GO:0008017; F:microtubule binding; IDA. DR GO; GO:0003774; F:motor activity; NAS. DR GO; GO:0008570; F:myosin ATPase activity; NAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0007391; P:dorsal closure; IEP. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR001609; myosin_head. DR InterPro; IPR004009; Myosin_N. DR InterPro; IPR008989; Myosin_S1_N. DR Pfam; PF00612; IQ; 1. DR Pfam; PF00063; myosin_head; 1. DR Pfam; PF02736; Myosin_N; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR ProDom; PD000355; myosin_head; 1. DR PROSITE; PS50096; IQ; 1. KW Myosin; Alternative splicing; Phosphorylation; ATP-binding; KW Actin-binding; Coiled coil; Multigene family; Developmental protein; KW Calmodulin-binding. FT DOMAIN 1 807 MYOSIN HEAD-LIKE. FT DOMAIN 808 837 IQ. FT DOMAIN 901 1026 COILED COIL (POTENTIAL). FT DOMAIN 1187 1193 HYDROPHOBIC REGION. FT DOMAIN 647 666 ACTIN-BINDING. FT NP_BIND 151 158 ATP. FT VARSPLIC 1047 1047 R -> SFSQVVSNIASRYLNK (in isoform Em-1). FT /FTId=VSP_003343. FT VARSPLIC 1048 1073 SENVRAQQQALGKQKYDLSKWKYSEL -> YSTLYELPMST FT TLVNFVNLFLLSQKH (in isoform Em-5). FT /FTId=VSP_003344. FT VARSPLIC 1074 1253 Missing (in isoform Em-5). FT /FTId=VSP_003345. FT CONFLICT 220 220 V -> M (IN REF. 1). FT CONFLICT 1051 1051 V -> L (IN REF. 1). FT CONFLICT 1121 1121 R -> P (IN REF. 1). SQ SEQUENCE 1253 AA; 143297 MW; 7586E03ECE8DCC59 CRC64; MLEDTQLVWV RDAAEGYIQG RITEIGAKEF EVTPTDRKYP KRTCHFDDIH SSCDGPQDHD DNCELMLLNE ATFLDNLKTR YYKDKIYTYV ANILIAVNPY REIKELYAPD TIKKYNGRSL GELPPHVFAI ADKAIRDMRV YKLSQSIIVS GESGAGKTES TKYLLKYLCY SHDSAGPIET KILDANPVLE AFGNAKTTRN NNSSRFGKFI EVHYDAKCQV VGGYISHYLL EKSRICTQSA EERNYHVFYM LLAGAPQQLR DKLSLGKPDD YRYLSGCTQY FANAKTEQLI PGSQKSKNHQ QKGPLKDPII DDYQHFHNLD KALGRLGLSD TEKLGIYSLV AAVLHLGNIA FEEIPDDVRG GCQVSEASEQ SLTITSGLLG VDQTELRTAL VSRVMQSKGG GFKGTVIMVP LKIYEASNAR DALAKAIYSR LFDRIVGLIN QSIPFQASNF YIGVLDIAGF EYFTVNSFEQ FCINYCNEKL QKFFNDNILK NEQELYKREG LNVPEITFTD NQDIIELIEA KSNGIFTLLD EESKLPKPSY SHFTAEVHKS WANHYRLGLP RSSRLKAHRT LRDEEGFLVR HFAGAVCYNT EQFIEKNNDA LHASLEGLVQ ECDNPLLQTL FPSGSSTSVR GKLNFISVGS KFKTQLGELM EKLEQNGTNF IRCIKPNSKM IDRQFEGSLA LAQLKCSGTI SVLELMEHGY PSRVLFADLY SMYKSVLPPE LVSLPARTFC EAMFQSLNLS AKDFKFGITK VFFRPGKFVE FDRIMRSDPE NMLAIVAKVK KWLIRSRWVK SALGALCVIK LRNRIIYRNK CVLIAQRIAR GFLARKQHRP RYQGIGKINK IRTNTLKTIE IASGLKMGRE EIISGVNDIY RQIDDAIKKI KMNPRITQRE MDSMYTVVMA NMNKLTVDLN TKLKEQQQAE EQERLRKIQE ALEAERAAKE AEEQRQREEI ENKRLKAEME TRRKAAEAQR LRQEEEDRRA ALALQEQLEK EAKDDAKYRQ QLEQERRDHE LALRLANESN GQVEDSPPVI RNGVNDASPM GPNKLIRSEN VRAQQQALGK QKYDLSKWKY SELRDAINTS CDIELLEACR QEFHRRLKVY HAWKAKNRKR TTMDENERAP RSVMEAAFKQ PPLVQPIQEI VTAQHRYFRI PFMRANAPDN TKRGLWYAHF DGQWIARQME LHADKPPILL VAGTDDMQMC ELSLEETGLT RKRGAEILEH EFNREWERNG GKAYKNLGAA KPNGPAAAMQ KQQ // ID MYSA_DROME STANDARD; PRT; 1962 AA. AC P05661; DT 01-NOV-1988 (Rel. 09, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Myosin heavy chain, muscle. GN MHC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; TISSUE=Pupae; RX MEDLINE=89384556; PubMed=2506434; RA George E.L., Ober M.B., Emerson C.P. Jr.; RT "Functional domains of the Drosophila melanogaster muscle myosin RT heavy-chain gene are encoded by alternatively spliced exons."; RL Mol. Cell. Biol. 9:2957-2974(1989). RN [2] RP SEQUENCE OF 1-264 FROM N.A. RX MEDLINE=87280141; PubMed=3038896; RA Wassenberg D.R. II, Kronert W.A., O'Donnell P.T., Bernstein S.I.; RT "Analysis of the 5' end of the Drosophila muscle myosin heavy chain RT gene. Alternatively spliced transcripts initiate at a single site and RT intron locations are conserved compared to myosin genes of other RT organisms."; RL J. Biol. Chem. 262:10741-10747(1987). RN [3] RP SEQUENCE OF 333-614 FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryonic muscle; RX MEDLINE=91330870; PubMed=1907912; RA Kronert W.A., Edwards K.A., Roche E.S., Wells L., Bernstein S.I.; RT "Muscle-specific accumulation of Drosophila myosin heavy chains: a RT splicing mutation in an alternative exon results in an isoform RT substitution."; RL EMBO J. 10:2479-2488(1991). CC -!- FUNCTION: MUSCLE CONTRACTION. CC -!- SUBUNIT: MUSCLE MYOSIN IS A HEXAMERIC PROTEIN THAT CONSISTS OF 2 CC HEAVY CHAIN SUBUNITS (MHC), 2 ALKALI LIGHT CHAIN SUBUNITS (MLC) CC AND 2 REGULATORY LIGHT CHAIN SUBUNITS (MLC-2). CC -!- SUBCELLULAR LOCATION: THICK FILAMENTS OF THE MYOFIBRILS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=15; CC Comment=Additional isoforms seem to exist. Exons 3, 7, 9, 11 and CC 15 are mutually exclusive splicing exons and exon 18 is included CC or excluded. Experimental confirmation may be lacking for some CC isoforms; CC Name=AAAAA; CC IsoId=P05661-1; Sequence=Displayed; CC Name=BDBBA; CC IsoId=P05661-2; Sequence=VSP_003329, VSP_003332, VSP_003333, CC VSP_003335; CC Name=BABDB; CC IsoId=P05661-3; Sequence=VSP_003329, VSP_003333, VSP_003337, CC VSP_003339; CC Name=3b; CC IsoId=P05661-4; Sequence=VSP_003329; CC Name=7b; CC IsoId=P05661-5; Sequence=VSP_003330; CC Name=7c; CC IsoId=P05661-6; Sequence=VSP_003331; CC Name=7d; CC IsoId=P05661-7; Sequence=VSP_003332; CC Name=9b; CC IsoId=P05661-8; Sequence=VSP_003333; CC Name=9c; CC IsoId=P05661-9; Sequence=VSP_003334; CC Name=11b; CC IsoId=P05661-10; Sequence=VSP_003335; CC Name=11c; CC IsoId=P05661-11; Sequence=VSP_003336; CC Name=11d; CC IsoId=P05661-12; Sequence=VSP_003337; CC Name=11e; CC IsoId=P05661-13; Sequence=VSP_003338; CC Name=15b; CC IsoId=P05661-14; Sequence=VSP_003339; CC Name=18; CC IsoId=P05661-15; Sequence=VSP_003340, VSP_003341; CC -!- TISSUE SPECIFICITY: EXPRESSED IN LARVAL AND ADULT MUSCLES. CC ISOFORMS CONTAINING EXON 9A ARE EXPRESSED IN INDIRECT FLIGHT CC MUSCLES, EXONS 9A AND 9B ARE EXPRESSED IN JUMP MUSCLES, EXONS 9B CC AND 9C ARE EXPRESSED IN OTHER LARVAL AND ADULT MUSCLES. CC -!- DOMAIN: ALTERNATIVE SPLICING EXONS CONTRIBUTE TO THE SPECIALIZED CC CONTRACTILE ACTIVITIES OF DIFFERENT MUSCLE TYPES. EXON 3 ENCODES CC THE HYDROPHOBIC POCKET ADJACENT TO THE ATP-BINDING SITE, EXON 9 IS CC ADJACENT TO THE ACTIN-BINDING DOMAIN, EXON 11 IS INVOLVED IN CC ACTIN-BINDING, EXON 15 IN THE S2 HINGE AND EXONS 18 AND 19 THE CC NON-COILED TAIL REGION. CC -!- MISCELLANEOUS: EACH MYOSIN HEAVY CHAIN CAN BE SPLIT INTO 1 LIGHT CC MEROMYOSIN (LMM) AND 1 HEAVY MEROMYOSIN (HMM). IT CAN LATER BE CC SPLIT FURTHER INTO 2 GLOBULAR SUBFRAGMENTS (S1) AND 1 ROD-SHAPED CC SUBFRAGMENT (S2). CC -!- SIMILARITY: CONTAINS 1 MYOSIN-LIKE GLOBULAR HEAD DOMAIN. CC -!- SIMILARITY: CONTAINS 1 IQ DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M61229; AAA28686.1; -. DR EMBL; M61229; AAA28687.1; -. DR EMBL; J02788; AAA28706.1; -. DR EMBL; J02788; AAA28707.1; -. DR EMBL; X60196; CAA42752.1; -. DR EMBL; X60196; CAA42753.1; -. DR EMBL; X60196; CAA42754.1; -. DR PIR; A28492; A28492. DR PIR; A32491; A32491. DR PIR; B32491; B32491. DR PIR; S16600; S16600. DR PIR; S16601; S16601. DR PIR; S16602; S16602. DR HSSP; P08799; 1MND. DR FlyBase; FBgn0002741; Mhc. DR GO; GO:0005859; C:muscle myosin; IDA. DR GO; GO:0005863; C:striated muscle thick filament; IDA. DR GO; GO:0008307; F:structural constituent of muscle; TAS. DR GO; GO:0006941; P:striated muscle contraction; TAS. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR001609; myosin_head. DR InterPro; IPR004009; Myosin_N. DR InterPro; IPR002928; Myosin_tail. DR Pfam; PF00612; IQ; 1. DR Pfam; PF00063; myosin_head; 1. DR Pfam; PF02736; Myosin_N; 1. DR Pfam; PF01576; Myosin_tail; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR ProDom; PD000355; myosin_head; 1. DR SMART; SM00015; IQ; 1. DR SMART; SM00242; MYSc; 1. DR PROSITE; PS50096; IQ; 1. KW Myosin; Muscle protein; Coiled coil; Thick filament; Actin-binding; KW ATP-binding; Calmodulin-binding; Alternative splicing; KW Multigene family. FT DOMAIN 1 779 MYOSIN HEAD-LIKE. FT DOMAIN 780 809 IQ. FT DOMAIN 802 1927 COILED COIL (POTENTIAL). FT NP_BIND 179 186 ATP (BY SIMILARITY). FT VARSPLIC 69 116 VRDIKSEKVEKVNPPKFEKIEDMADMTVLNTPCVLHNLRQR FT YYAKLIY -> TRDLKKDLLQQVNPPKYEKAEDMSNLTYLN FT DASVLHNLRQRYYNKLIY (in isoform 3b, FT isoform BDBBA and isoform BABDB). FT /FTId=VSP_003329. FT VARSPLIC 298 332 DICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTD -> EY FT CLLSNNIYDYRIVSQGKTTIPSVNDGEEWVAVD (in FT isoform 7b). FT /FTId=VSP_003330. FT VARSPLIC 298 332 DICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTD -> EM FT VFLGQHIGDYPGICQGKTRIPGVNDGEEFELTD (in FT isoform 7c). FT /FTId=VSP_003331. FT VARSPLIC 298 332 DICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTD -> EM FT CFLSDNIYDYYNVSQGKVTVPNMDDGEEFQLAD (in FT isoform 7d and isoform BDBBA). FT /FTId=VSP_003332. FT VARSPLIC 469 525 YNGFEQLCINFTNEKLQQFFNHIMFVMEQEEYKKEGINWDF FT IDFGMDLLACIDLIEK -> YNGFEQLCINFTNEKLQQFFN FT HHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEK (in FT isoform 9b, isoform BDBBA and isoform FT BABDB). FT /FTId=VSP_003333. FT VARSPLIC 469 525 YNGFEQLCINFTNEKLQQFFNHIMFVMEQEEYKKEGINWDF FT IDFGMDLLACIDLIEK -> YNGFEQLCINFTNEKLQQFFN FT HHMFVLEQEEYQREGIEWTFIDFGMDLQLCIDLIEK (in FT isoform 9c). FT /FTId=VSP_003334. FT VARSPLIC 723 761 YQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTK FT -> YQILNPAGIVGVDDPKKCGSIILESTALDPDMYRIGHT FT K (in isoform 11b and isoform BDBBA). FT /FTId=VSP_003335. FT VARSPLIC 723 761 YQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTK FT -> YQILNPKGIKGIEDPKKCTKVLIESTELNDDQYRLGNT FT K (in isoform 11c). FT /FTId=VSP_003336. FT VARSPLIC 723 761 YQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTK FT -> YKIMCPKLLQGVEKDKKATEIIIKFIDLPEDQYRLGNT FT K (in isoform 11d and isoform BABDB). FT /FTId=VSP_003337. FT VARSPLIC 723 761 YQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTK FT -> YMILAPAIMAAEKVAKNAAGKCLEAVGLDPDMYRIGHT FT K (in isoform 11e). FT /FTId=VSP_003338. FT VARSPLIC 1216 1241 AEHDRQTCHNELNQTRTACDQLGRDK -> AEKEKNEYYGQ FT LNDLRAGVDHITNEK (in isoform 15b and FT isoform BABDB). FT /FTId=VSP_003339. FT VARSPLIC 1936 1936 P -> I (in isoform 18). FT /FTId=VSP_003340. FT VARSPLIC 1937 1962 Missing (in isoform 18). FT /FTId=VSP_003341. FT CONFLICT 43 44 EK -> RE (IN REF. 2). FT CONFLICT 68 68 E -> K (IN REF. 2). FT CONFLICT 215 215 L -> M (IN REF. 2). SQ SEQUENCE 1962 AA; 224480 MW; F5A888932E414F7F CRC64; MPKPVANQED EDPTPYLFVS LEQRRIDQSK PYDSKKSCWI PDEKEGYLLG EIKATKGDIV SVGLQGGEVR DIKSEKVEKV NPPKFEKIED MADMTVLNTP CVLHNLRQRY YAKLIYTYSG LFCVAINPYK RYPVYTNRCA KMYRGKRRNE VPPHIFAISD GAYVDMLTNH VNQSMLITGE SGAGKTENTK KVIAYFATVG ASKKTDEAAK SKGSLEDQVV QTNPVLEAFG NAKTVRNDNS SRFGKFIRIH FGPTGKLAGA DIETYLLEKA RVISQQSLER CYHIFYQIMS GSVPGVKDIC LLTDNIYDYH IVSQGKVTVA SIDDAEEFSL TDQAFDILGF TKQEKEDVYR ITAAVMHMGG MKFKQRGREE QAEQDGEEEG GRVSKLFGCD TAELYKNLLK PRIKVGNEFV TQGRNVQQVT NSIGALCKGV FDRLFKWLVK KCNETLDTQQ KRQHFIGVLD IAGFEIFEYN GFEQLCINFT NEKLQQFFNH IMFVMEQEEY KKEGINWDFI DFGMDLLACI DLIEKPMGIL SILEEESMFP KATDQTFSEK LTNTHLGKSA PFQKPKPPKP GQQAAHFAIA HYAGCVSYNI TGWLEKNKDP LNDTVVDQFK KSQNKLLIEI FADHAGQSGG GEQAKGGRGK KGGGFATVSS AYKEQLNSLM TTLRSTQPHF VRCIIPNEMK QPGVVDAHLV MHQLTCNGVL EGIRICRKGF PNRMMYPDFK MRYQILNPRG IKDLDCPKKA SKVLIESTEL NEDLYRLGHT KVFFRAGVLG QMEEFRDERL GKIMSWMQAW ARGYLSRKGF KKLQEQRVAL KVVQRNLRKY LQLRTWPWYK LWQKVKPLLN VSRIEDEIAR LEEKAKKAEE LHAAEVKVRK ELEALNAKLL AEKTALLDSL SGEKGALQDY QERNAKLTAQ KNDLENQLRD IQERLTQEED ARNQLFQQKK KADQEISGLK KDIEDLELNV QKAEQDKATK DHQIRNLNDE IAHQDELINK LNKEKKMQGE TNQKTGEELQ AAEDKINHLN KVKAKLEQTL DELEDSLERE KKVRGDVEKS KRKVEGDLKL TQEAVADLER NKKELEQTIQ RKDKELSSIT AKLEDEQVVV LKHQRQIKEL QARIEELEEE VEAERQARAK AEKQRADLAR ELEELGERLE EAGGATSAQI ELNKKREAEL SKLRRDLEEA NIQHESTLAN LRKKHNDAVA EMAEQVDQLN KLKAKAEHDR QTCHNELNQT RTACDQLGRD KAAQEKIAKQ LQHTLNEVQS KLDETNRTLN DFDASKKKLS IENSDLLRQL EEAESQVSQL SKIKISLTTQ LEDTKRLADE ESRERATLLG KFRNLEHDLD NLREQVEEEA EGKADLQRQL SKANAEAQVW RSKYESDGVA RSEELEEAKR KLQARLAEAE ETIESLNQKC IGLEKTKQRL STEVEDLQLE VDRANAIANA AEKKQKAFDK IIGEWKLKVD DLAAELDASQ KECRNYSTEL FRLKGAYEEG QEQLEAVRRE NKNLADEVKD LLDQIGEGGR NIHEIEKARK RLEAEKDELQ AALEEAEAAL EQEENKVLRA QLELSQVRQE IDRRIQEKEE EFENTRKNHQ RALDSMQASL EAEAKGKAEA LRMKKKLEAD INELEIALDH ANKANAEAQK NIKRYQQQLK DIQTALEEEQ RARDDAREQL GISERRANAL QNELEESRTL LEQADRGRRQ AEQELADAHE QLNEVSAQNA SISAAKRKLE SELQTLHSDL DELLNEAKNS EEKAKKAMVD AARLADELRA EQDHAQTQEK LRKALEQQIK ELQVRLDEAE ANALKGGKKA IQKLEQRVRE LENELDGEQR RHADAQKNLR KSERRVKELS FQSEEDRKNH ERMQDLVDKL QQKIKTYKRQ IEEAEEIAAL NLAKFRKAQQ ELEEAEERAD LAEQAISKFR AKGRAGSVGR GASPAPRATS VRPQFDGLAF PPRFDLAPEN EF // ID MYSN_DROME STANDARD; PRT; 2017 AA. AC Q99323; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Myosin heavy chain, non-muscle (Zipper protein) (Myosin II). GN ZIP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC TISSUE=Embryo; RX MEDLINE=90349606; PubMed=2117279; RA Ketchum A.S., Stewart C.T., Stewart M., Kiehart D.P.; RT "Complete sequence of the Drosophila nonmuscle myosin heavy-chain RT transcript: conserved sequences in the myosin tail and differential RT splicing in the 5' untranslated sequence."; RL Proc. Natl. Acad. Sci. U.S.A. 87:6316-6320(1990). CC -!- FUNCTION: NONMUSCLE MYOSIN APPEARS TO BE RESPONSIBLE FOR CC CELLULARIZATION. REQUIRED FOR MORPHOGENESIS AND CYTOKINESIS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q99323-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q99323-2; Sequence=VSP_003342; CC -!- SIMILARITY: CONTAINS 1 MYOSIN-LIKE GLOBULAR HEAD DOMAIN. CC -!- SIMILARITY: CONTAINS 1 IQ DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M35012; AAA28713.1; -. DR PIR; A36014; A36014. DR HSSP; P10587; 1BR2. DR FlyBase; FBgn0005634; zip. DR GO; GO:0005856; C:cytoskeleton; NAS. DR GO; GO:0005860; C:non-muscle myosin; NAS. DR GO; GO:0030018; C:Z disc; IDA. DR GO; GO:0046663; P:leading edge cell differentiation; IMP. DR GO; GO:0006936; P:muscle contraction; IMP. DR GO; GO:0045214; P:sarcomere organization; IMP. DR GO; GO:0007395; P:spreading of leading edge cells; IMP. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR001609; myosin_head. DR InterPro; IPR004009; Myosin_N. DR InterPro; IPR002928; Myosin_tail. DR Pfam; PF00612; IQ; 1. DR Pfam; PF00063; myosin_head; 1. DR Pfam; PF02736; Myosin_N; 1. DR Pfam; PF01576; Myosin_tail; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR ProDom; PD000355; myosin_head; 1. DR SMART; SM00015; IQ; 1. DR SMART; SM00242; MYSc; 1. DR PROSITE; PS50096; IQ; 1. KW Myosin; Alternative splicing; Coiled coil; Actin-binding; KW ATP-binding; Calmodulin-binding. FT DOMAIN 1 829 MYOSIN HEAD-LIKE. FT DOMAIN 830 859 IQ. FT DOMAIN 886 2017 COILED COIL (POTENTIAL). FT NP_BIND 225 232 ATP. FT DOMAIN 250 260 25 kDa/50 kDa JUNCTION. FT DOMAIN 682 694 50 kDa/20 kDa JUNCTION. FT DOMAIN 705 727 ACTIN-BINDING. FT DOMAIN 742 758 REACTIVE SULFHYDRYL/ACTIN-BINDING. FT DOMAIN 1303 2017 LIGHT MEROMYOSIN (LMM). FT DOMAIN 1303 1970 ALPHA-HELICAL TAILPIECE (LMM). FT DOMAIN 1971 2017 GLOBULAR TAILPIECE. FT VARSPLIC 1 45 Missing (in isoform Short). FT /FTId=VSP_003342. SQ SEQUENCE 2017 AA; 232016 MW; 73E3CB02BA8F2528 CRC64; MKSAWLALKS KSALHPKSEY PVSNIHYPKA ANYRQTRNYL EIAAKMSEEV DRNDPELKYL SVERNQFNPI RPRRPSGHRS VLVWVPHENQ GFVAASIKRE HGDEVEVELA ETGKRVMILR DDIQKMNPPK FDKVEDMAEL TCLNEASVLH NIKDRYYSGL IYTYSGLFCV VVNPYKKLPI YTEKIMERYK GIKRHEVPPH VFAITDSAYR NMLGDREDQS ILCTGESGAG KTENTKKVIQ FLAYVAASKP KGSGAVPHPA VLIGELEQQL LQANPILEAF GNAKTVKNDN SSRFGKFIRI NFDASGFISG ANIETYLLEK SRAIRQAKDE RTFHIFYQLL AGATPEQREK FILDDVKSYA FLSNGSLPVP GVDDYAEFQA TVKSMNIMGM TSEDFNSIFR IVSAVLLFGS MKFRQERNND QATLPDNTVA QKIAHLLGLS VTDMTRAFLT PRIKVGRDFV TKAQTKEQVE FAVEAIAKAC YERMFKWLVN RINRSLDRTK RQGASFIGIL DMAGFEIFEL NSFEQLCINY TNEKLQQLFN HTMFILEQEE YQREGIEWKF IDFGLDLQPT IDLIDKPGGI MALLDEECWF PKATDKTFVD KLVSAHSMHP KFMKTDFRGV ADFAIVHYAG RVDYSAAKWL MKNMDPLNEN IVSLLQGSQD PFVVNIWKDA EIVGMAQQAL TDTQFGARTR KGMFRTVSHL YKEQLAKLMD TLRNTNPNFV RCIIPNHEKR AGKIDAPLVL DQLRCNGVLE GIRICRQGFP NRIPFQEFRQ RYELLTPNVI PKGFMDGKKA CEKMIQALEL DSNLYRVGQS KIFFRAGVLA HLEEERDFKI SDLIVNFQAF CRGFLARRNY QKRLQQLNAI RIIQRNCAAY LKLRNWQWWR LYTKVKPLLE VTKQEEKLVQ KEDELKQVRE KLDTLAKNTQ EYERKYQQAL VEKTTLAEQL QAEIELCAEA EESRSRLMAR KQELEDMMQE LETRIEEEEE RVLALGGEKK KLELNIQDLE EQLEEEEAAR QKLQLEKVQL DAKIKKYEED LALTDDQNQK LLKEKKLLEE RANDLSQTLA EEEEKAKHLA KLKAKHEATI TELEERLHKD QQQRQESDRS KRKIETEVAD LKEQLNERRV QVDEMQAQLA KREEELTQTL LRIDEESATK ATAQKAQREL ESQLAEIQED LEAEKAARAK AEKVRRDLSE ELEALKNELL DSLDTTAAQQ ELRSKREQEL ATLKKSLEEE TVNHEGVLAD MRHKHSQELN SINDQLENLR KAKTVLEKAK GTLEAENADL ATELRSVNSS RQENDRRRKQ AESQIAELQV KLAEIERARS ELQEKCTKLQ QEAENITNQL EEAELKASAA VKSASNMESQ LTEAQQLLEE ETRQKLGLSS KLRQIESEKE ALQEQLEEDD EAKRNYERKL AEVTTQMQEI KKKAEEDADL AKELEEGKKR LNKDIEALER QVKELIAQND RLDKSKKKIQ SELEDATIEL EAQRTKVLEL EKKQKNFDKI LAEEKAISEQ IAQERDTAER EAREKETKVL SVSRELDEAF DKIEDLENKR KTLQNELDDL ANTQGTADKN VHELEKAKRA LESQLAELKA QNEELEDDLQ LTEDAKLRLE VNMQALRSQF ERDLLAKEEG AEEKRRGLVK QLRDLETELD EERKQRTAAV ASKKKLEGDL KEIETTMEMH NKVKEDALKH AKKLQAQVKD ALRDAEEAKA AKEELQALSK EADGKVKALE AEVLQLTEDL ASSERARRAA ETERDELAEE IANNANKGSL MIDEKRRLEA RIATLEEELE EEQSNSEVLL DRAAARQLQI EQLTTELANE KSNSQKNENG RALLERQNKE LKAKLAEIET AQRTKVKATI ATLEAKIAKV EEQLENEGKE RLLQQKANRK MDKKIKELTM NIEDERRHVD QHKEQMDKLN SRIKLLKRNL DETEEELQKE KTQKRKYQRE CEDMIESQEA MNREINSLKT KLRRTGGIGL SSSRLTGTPS SKRAGGGGGS DDSSVQDESL DGEDSAN // ID MYSP_DROME STANDARD; PRT; 879 AA. AC P35415; Q8T0Q3; Q9VSP6; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Paramyosin, long form. GN PRM OR CG5939. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Muscle; RX MEDLINE=92113004; PubMed=1730773; RA Becker K.D., O'Donnell P.T., Heitz J.M., Vito M., Bernstein S.I.; RT "Analysis of Drosophila paramyosin: identification of a novel isoform RT which is restricted to a subset of adult muscles."; RL J. Cell Biol. 116:669-681(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92167957; PubMed=1371577; RA Vinos J., Maroto M., Garesse R., Marco R., Cervera M.; RT "Drosophila melanogaster paramyosin: developmental pattern, mapping RT and properties deduced from its complete coding sequence."; RL Mol. Gen. Genet. 231:385-394(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 103-571 FROM N.A., AND CHARACTERIZATION. RC STRAIN=Oregon-R; RX MEDLINE=91332901; PubMed=1908014; RA Vinos J., Domingo A., Marco R., Cervera M.; RT "Identification and characterization of Drosophila melanogaster RT paramyosin."; RL J. Mol. Biol. 220:687-700(1991). CC -!- FUNCTION: PARAMYOSIN IS A MAJOR STRUCTURAL COMPONENT OF MANY THICK CC FILAMENTS ISOLATED FROM INVERTEBRATE MUSCLES. CC -!- SUBUNIT: HETERODIMER OF TWO ISOFORMS (POTENTIAL). CC -!- SUBCELLULAR LOCATION: THICK FILAMENTS OF THE MYOFIBRILS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist. Isoforms can also be CC produced by post-translational modifications; CC Name=Long; Synonyms=A, B; CC IsoId=P35415-1; Sequence=Displayed; CC Name=Short; Synonyms=C, D; CC IsoId=P35416-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN ALL LARVAL AND ADULT MUSCLE CC TISSUES. EXPRESSION IS FIVE TIMES HIGHER IN TUBULAR THAN IN CC FIBRILLAR MUSCLES. CC -!- DEVELOPMENTAL STAGE: UNDETECTABLE DURING GASTRULATION AND EARLY CC PHASES OF GERM BAND FORMATION. INCREASES DURING ORGANOGENESIS, CC AROUND 10 HOURS POSTFERTILIZATION, TO THE ADULT STAGE. CC -!- PTM: THE MORE ACIDIC AND LESS-ABUNDANT ISOFORM IS PHOSPHORYLATED CC IN VIVO. CC -!- SIMILARITY: HIGH, TO MYOSIN HEAVY CHAINS. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A STOP CC CODON IN POSITION 703. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62590; CAA44475.1; -. DR EMBL; X58722; CAA41557.1; -. DR EMBL; AE003554; AAF50370.1; -. DR EMBL; AY069132; AAL39277.1; ALT_SEQ. DR PIR; S22028; S22028. DR FlyBase; FBgn0003149; Prm. DR InterPro; IPR002928; Myosin_tail. DR Pfam; PF01576; Myosin_tail; 1. KW Coiled coil; Muscle protein; Thick filament; Myosin; Phosphorylation; KW Alternative splicing. FT DOMAIN 1 31 NONHELICAL REGION (POTENTIAL). FT DOMAIN 32 858 COILED COIL (POTENTIAL). FT DOMAIN 859 879 NONHELICAL REGION (POTENTIAL). FT DISULFID 368 368 INTERCHAIN (POTENTIAL). FT DISULFID 784 784 INTERCHAIN (POTENTIAL). FT CONFLICT 500 500 MISSING (IN REF. 2). SQ SEQUENCE 879 AA; 102338 MW; 85BB333519815A1A CRC64; MSSSQAVRSS KYSYRATSTG PGTADVNIEY IQDLSSLSRL EDKIRLLQDD LEVERELRQR IEREKADLSV QVIQMSERLE EAEGGAEHQF EANRKRDAEL LKLRKLLEDV HLESEETTLL LKKKHNEIIT DFQEQVEILT KNKARAEKDK AKFQTEVYEL LSQIESYNKE KIVSEKHISK LEVSISELNV KIEELNRTVI DISSHRSRLS QENIELTKDV QDLKVQLDTV SFSKSQVISQ LEDARRRLED EDRRRSLLES SLHQVEIELD SVRNQLEEES EARIDLERQL VKANADATSW QNKWNSEVAA RAEEVEEIRR KYQVRITELE EHIESLIVKV NNLEKMKTRL ASEVEVLIID LEKSNNSCRE LTKSVNTLEK HNVELKSRLD ETIILYETSQ RDLKNKHADL VRTVHELDKV KDNNNQLTRE NKKLGDDLHE AKGAINELNR RLHELELELR RLENERDELT AAYKEAEAGR KAEEQRGQRL AADFNQYRHD AERRLAEKDE EIEAIRKQTS IEIEQLNARV IEAETRLKTE VTRIKKKLQI QITELEMSLD VANKTNIDLQ KVIKKQSLQL TELQAHYEDV QRQLQATLDQ YAVAQRRLAG LNGELEEVRS HLDSANRAKR TVELQYEEAA SRINELTTAN VSLVSIKSKL EQELSVVASD YEEVSKELRI SDERYQKVQV ELKHVVEQVH EEQERIVKLE TIKKSLEVEV KNLSIRLEEV ELNAVAGSKR IISKLEARIR DLELELEEEK RRHAETIKIL RKKERTVKEV LVQCEEDQKN LILLQDALDK STAKINIYRR QLSEQEGVSQ QTTTRVRRFQ RELEAAEDRA DTAESSLNII RAKHRTFVTT STVPGSQVYI QETTRTITE // ID MYSQ_DROME STANDARD; PRT; 640 AA. AC P35416; Q961L6; Q9VSP5; DT 01-JUN-1994 (Rel. 29, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Paramyosin, short form (Miniparamyosin). GN PRM OR CG5939. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE OF 1-276 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 118-640 FROM N.A. RC STRAIN=Canton-S; TISSUE=Muscle; RX MEDLINE=92113004; PubMed=1730773; RA Becker K.D., O'Donnell P.T., Heitz J.M., Vito M., Bernstein S.I.; RT "Analysis of Drosophila paramyosin: identification of a novel isoform RT which is restricted to a subset of adult muscles."; RL J. Cell Biol. 116:669-681(1992). CC -!- FUNCTION: PARAMYOSIN IS A MAJOR STRUCTURAL COMPONENT OF MANY THICK CC FILAMENTS ISOLATED FROM INVERTEBRATE MUSCLES. CC -!- SUBCELLULAR LOCATION: THICK FILAMENTS OF THE MYOFIBRILS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist. Isoforms can also be CC produced by post-translational modifications; CC Name=Short; Synonyms=C, D; CC IsoId=P35416-1; Sequence=Displayed; CC Name=Long; Synonyms=A, B; CC IsoId=P35415-1; Sequence=External; CC -!- TISSUE SPECIFICITY: FOUND IN ALL ADULT MUSCLE TISSUES EXCEPT IN CC INDIRECT FLIGHT MUSCLES AND A SET OF TEMPORARY ABDOMINAL MUSCLES. CC NOT DETECTED IN LARVAL MUSCLE. CC -!- PTM: PHOSPHORYLATED. CC -!- SIMILARITY: HIGH, TO MYOSIN HEAVY CHAINS. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 128. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003554; AAF50371.2; -. DR EMBL; AY051521; AAK92945.1; ALT_SEQ. DR EMBL; X62591; CAA44476.1; ALT_FRAME. DR PIR; S22027; S22027. DR FlyBase; FBgn0003149; Prm. DR InterPro; IPR002928; Myosin_tail. DR Pfam; PF01576; Myosin_tail; 1. KW Coiled coil; Muscle protein; Thick filament; Myosin; Phosphorylation; KW Alternative splicing. FT DOMAIN 1 122 NONHELICAL REGION (POTENTIAL). FT DOMAIN 123 619 COILED COIL (POTENTIAL). FT DOMAIN 420 640 NONHELICAL REGION (POTENTIAL). FT CONFLICT 118 118 E -> Q (IN REF. 4). SQ SEQUENCE 640 AA; 74277 MW; 020966960AB68D61 CRC64; MALALKQRPS RFRPTTTTYE DNYGYTMNFY QPMLDYLDAK AKGLEVKKPH LPWVSERGLK QYRPSNAVRQ YNADEIVRLS RTCAARADEI LLNFRAQKRS PFSVQKLVDA SRVTKHLEPD TVVERSRQRR RRRQEELEDL IKRDTLKILQ RIRKIELDNE LDKMSDDFKR SIRGKSASAI AQALLSESEK NIKTAKKEEE DYIAQTLVRS SRAVSRARSR SSSPLDGQYR AHALHIELMD DRLVDKLDHR VSSSLHNVKR QLSTLNQRTV EFYADSSKQT SIEIEQLNAR VIEAETRLKT EVTRIKKKLQ IQITELEMSL DVANKTNIDL QKVIKKQSLQ LTELQAHYED VQRQLQATLD QYAVAQRRLA GLNGELEEVR SHLDSANRAK RTVELQYEEA ASRINELTTA NVSLVSIKSK LEQELSVVAS DYEEVSKELR ISDERYQKVQ VELKHVVEQV HEEQERIVKL ETIKKSLEVE VKNLSIRLEE VELNAVAGSK RIISKLEARI RDLELELEEE KRRHAETIKI LRKKERTVKE VLVQCEEDQK NLILLQDALD KSTAKINIYR RQLSEQEGVS QQTTTRVRRF QRELEAAEDR ADTAESSLNI IRAKHRTFVT TSTVPGSQVY IQETTRTITE // ID NACH_DROME STANDARD; PRT; 535 AA. AC O61365; Q86LH4; Q9V7S4; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sodium channel protein Nach (Pickpocket 4). GN NACH OR PPK4 OR CG8178. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Canton-S; RA Da Lage J.-L.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=22480307; PubMed=12571352; RA Liu L., Johnson W.A., Welsh M.J.; RT "Drosophila DEG/ENaC pickpocket genes are expressed in the tracheal RT system, where they may be involved in liquid clearance."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2128-2133(2003). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PART OF A COMPLEX THAT PLAYS A ROLE IN TRACHEAL LIQUID CC CLEARANCE. PROBABLE ROLE IN SODIUM TRANSPORT. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=O61365-1; Sequence=Displayed; CC Name=A; CC IsoId=O61365-2; Sequence=VSP_008551; CC -!- TISSUE SPECIFICITY: EMBRYONIC AND LARVAL TRACHEAL SYSTEM; DORSAL CC TRUNK (BUT NOT AT FUSION WITH TRANSVERSE CONNECTIVE), SEVERAL CC BRANCHES AND TERMINAL CELLS. ALSO EXPRESSED IN ADULT TRACHEAL CC SYSTEM; DORSAL TRUNK, BUT NOT AT THE SPIRACLES. CC -!- SIMILARITY: BELONGS TO THE AMILORIDE-SENSITIVE SODIUM CHANNEL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF022713; AAD09149.1; -. DR EMBL; AY226538; AAO47364.1; -. DR EMBL; AE003806; AAF57970.1; -. DR FlyBase; FBgn0024319; Nach. DR InterPro; IPR001873; Na+channel_ASC. DR Pfam; PF00858; ASC; 1. DR PRINTS; PR01078; AMINACHANNEL. DR PROSITE; PS01206; ASC; FALSE_NEG. KW Ion transport; Sodium transport; Ionic channel; Transmembrane; KW Glycoprotein; Alternative splicing. FT DOMAIN 1 49 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 50 70 POTENTIAL. FT DOMAIN 71 471 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 472 492 POTENTIAL. FT DOMAIN 493 535 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 165 165 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 239 239 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 367 367 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 219 237 Missing (in isoform A). FT /FTId=VSP_008551. FT CONFLICT 22 22 Y -> S (IN REF. 1). FT CONFLICT 269 269 S -> L (IN REF. 1). FT CONFLICT 289 289 S -> F (IN REF. 1). FT CONFLICT 312 313 SS -> FF (IN REF. 1). FT CONFLICT 365 365 D -> A (IN REF. 1). SQ SEQUENCE 535 AA; 62329 MW; 63C88935FAD62161 CRC64; MGHQEELKPE QVDLKVTPFV GYLRRTWSDF CATSSIHGLK YTRDEDTNKI VHLVWLLISV VMFICAVVMA RTFYMDYRSS PTRMNVESDN TPVNRLYFPP VTICPDVLFN MQKSEAFLNT LRLPKGAELR GILRKLHIFY GFMLDDERYS AEDIEQMEAL LFLNNLTIPE FVEHLRWNCD EILYRCRFNG EIMDCSKIFQ LSKTFFGHCC SFNLRQKGWV NNKLNNLESF KVFHLNSLNF TAQRAIGGLR YGLSVVVRYK DDNYDPLQSY SYGVKLLIQE ADAFPSAHSA AKFIAFNSET FAAVRPQETF CSSAVKALII EERNCVFQNE FPMRYFSDYV YPNCELNCRV TNMVKFCGCH TYFFDFNRTS DRICTFRDIP CLVDNFANII TRKKSTQCYC PLTCEHIDYD VQLTNFPLEL NMPVADKFYS GLAKNDGVLH VFINSFSYRR LRRDLLSNMV TLVSNLGSAF SLFVGMSMLS VVEIIYYFSV ILRKNYKLEC ETRSQMLHKK PKFAWPKAND THSKEQKSVF IIHKS // ID NBEA_DROME STANDARD; PRT; 3584 AA. AC Q9W4E2; O16024; Q8IRR9; Q961G8; Q9GP69; Q9GP70; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Neurobeachin protein (Rugose protein) (A-kinase anchor protein 550) DE (AKAP 550) (dAKAP550). GN RG OR AKAP550 OR CG6775. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS B AND S), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RC TISSUE=Head; RX MEDLINE=20556611; PubMed=11102458; RA Wang X., Herberg F.W., Laue M.M., Wullner C., Hu B., RA Petrasch-Parwez E., Kilimann M.W.; RT "Neurobeachin: a protein kinase A-anchoring, beige/Chediak-Higashi RT protein homolog implicated in neuronal membrane traffic."; RL J. Neurosci. 20:8551-8565(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 1-2389 FROM N.A. (ISOFORMS B AND S), FUNCTION, SUBUNIT, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=97476266; PubMed=9334242; RA Han J.-D., Baker N.E., Rubin C.S.; RT "Molecular characterization of a novel A kinase anchor protein from RT Drosophila melanogaster."; RL J. Biol. Chem. 272:26611-26619(1997). RN [5] RP SEQUENCE OF 2606-3584 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY. RX MEDLINE=22067642; PubMed=12072466; RA Shamloula H.K., Mbogho M.P., Pimentel A.C., RA Chrzanowska-Lightowlers Z.M., Hyatt V., Okano H., Venkatesh T.R.; RT "rugose (rg), a Drosophila A kinase anchor protein, is required for RT retinal pattern formation and interacts genetically with multiple RT signaling pathways."; RL Genetics 161:693-710(2002). RN [7] RP INTERACTION WITH NOTCH-MEDIATED SIGNALING PATHWAY. RX MEDLINE=22119716; PubMed=12124948; RA Schreiber S.L., Preiss A., Nagel A.C., Wech I., Maier D.; RT "Genetic screen for modifiers of the rough eye phenotype resulting RT from overexpression of the Notch antagonist hairless in Drosophila."; RL Genesis 33:141-152(2002). CC -!- FUNCTION: BINDS TO TYPE II REGULATORY SUBUNITS OF PROTEIN KINASE A CC AND ANCHORS/TARGETS THEM TO THE MEMBRANE. MAY ANCHOR THE KINASE TO CC CYTOSKELETAL AND/OR ORGANELLE-ASSOCIATED PROTEINS. REQUIRED FOR CC CORRECT RETINAL PATTERN FORMATION AND MAY FUNCTION IN CELL FATE CC DETERMINATION THROUGH ITS INTERACTIONS WITH THE EGFR AND NOTCH CC SIGNALING PATHWAYS. CC -!- SUBUNIT: INTERACTS WITH RII SUBUNIT OF PKA AND COMPONENTS OF THE CC EGFR-MEDIATED AND NOTCH-MEDIATED SIGNALING CC PATHWAYS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND MEMBRANE-ASSOCIATED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=Q9W4E2-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=B; CC IsoId=Q9W4E2-2; Sequence=VSP_050543; CC Name=S; CC IsoId=Q9W4E2-3; Sequence=VSP_050258; CC -!- TISSUE SPECIFICITY: IN EARLY EMBRYOS, UBIQUITOUS EXPRESSION WITH CC ELEVATED LEVELS IN VENTRAL FURROW AND FLANKING MESECTODERMAL CC CELLS, NEUROBLASTS AND MESODERM. LATE EMBRYOS SHOW REDUCED CC EXPRESSION IN EPIDERMIS AND SKELETAL MUSCLE AND ELEVATED IN CC NERVOUS SYSTEM, GUT ENDOTHELIUM, TRACHEAL SYSTEM AND SALIVARY CC GLAND. LARVAE SHOW EXPRESSION IN IMAGINAL DISKS AND MANY NEURAL CC CELLS. DEVELOPING EYE IMAGINAL DISK SHOWS EXPRESSION THROUGHOUT CC THE DISK AND IN THE REGION OF THE MORPHOGENETIC FURROW. UBIQUITOUS CC EXPRESSION IN ADULTS WITH HIGHER LEVELS IN HEAD REGION. CC -!- DEVELOPMENTAL STAGE: ALL STAGES OF DEVELOPMENT. CC -!- DOMAIN: RII-ALPHA BINDING SITE, PREDICTED TO FORM AN AMPHIPATHIC CC HELIX, COULD PARTICIPATE IN PROTEIN-PROTEIN INTERACTIONS WITH A CC COMPLEMENTARY SURFACE ON THE R-SUBUNIT DIMER. CC -!- SIMILARITY: BELONGS TO THE NEUROBEACHIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 BEACH DOMAIN. CC -!- SIMILARITY: CONTAINS 5 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y18278; CAC18799.1; -. DR EMBL; Y18278; CAC18800.1; -. DR EMBL; AE003433; AAF46011.2; -. DR EMBL; AE003433; AAN09135.1; -. DR EMBL; AF003622; AAB83959.1; -. DR EMBL; AY051596; AAK93020.1; ALT_INIT. DR PIR; T03094; T03094. DR FlyBase; FBgn0003244; rg. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0016021; C:integral to membrane; IDA. DR GO; GO:0005079; F:protein kinase A anchoring activity; IDA. DR GO; GO:0042462; P:eye photoreceptor cell development; IMP. DR InterPro; IPR000409; Beige_BEACH. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR001680; WD40. DR Pfam; PF02138; Beach; 1. DR Pfam; PF00400; WD40; 5. DR ProDom; PD007848; Beige_BEACH; 1. DR SMART; SM00320; WD40; 4. DR PROSITE; PS50197; BEACH; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Repeat; WD repeat; Membrane; Alternative splicing. FT DOMAIN 1350 1369 RII-BINDING. FT DOMAIN 1406 1425 RII-BINDING. FT REPEAT 1701 1743 WD 1. FT DOMAIN 2911 3200 BEACH. FT REPEAT 3359 3402 WD 2. FT REPEAT 3416 3456 WD 3. FT REPEAT 3498 3537 WD 4. FT REPEAT 3540 3579 WD 5. FT DOMAIN 284 411 ALA-RICH. FT DOMAIN 1218 1260 ASN-RICH. FT DOMAIN 1274 1550 GLU-RICH. FT DOMAIN 1963 2168 GLN/HIS/SER-RICH. FT DOMAIN 2169 2273 GLY-RICH. FT DOMAIN 2416 2430 GLN-RICH. FT VARSPLIC 1 62 Missing (in isoform B). FT /FTId=VSP_050543. FT VARSPLIC 253 459 Missing (in isoform S). FT /FTId=VSP_050258. FT CONFLICT 83 83 F -> C (IN REF. 1 AND 4). FT CONFLICT 102 102 C -> S (IN REF. 1 AND 4). FT CONFLICT 276 276 T -> A (IN REF. 1 AND 4). FT CONFLICT 280 280 T -> S (IN REF. 1 AND 4). FT CONFLICT 417 417 H -> D (IN REF. 1 AND 4). FT CONFLICT 455 455 N -> D (IN REF. 1 AND 4). FT CONFLICT 1557 1557 N -> T (IN REF. 1 AND 4). FT CONFLICT 2021 2021 H -> Q (IN REF. 1 AND 4). FT CONFLICT 2348 2357 ENEVPEVESS -> GKTKCPRWSHP (IN REF. 1 AND FT 4). FT CONFLICT 2694 2694 V -> G (IN REF. 1). SQ SEQUENCE 3584 AA; 396493 MW; D93EF0592ABA0810 CRC64; MLGVLASYSI TVKELKLLFG TMKATNGKWP RHSAKLLNVL RQMPHRNGPD VFFSFPGRKG SAMVLPPLAK WPYENGFTFT TWFRLDPINS VNIEREKPYL YCFKTSKGVG YTAHFVGNCL VLTSMKVKGK GFQHCVKYEF QPRKWYMIAI VYIYNRWTKS EIKCLVNGQL ASSTEMAWFV STNDPFDKCY IGATPELDEE RVFCGQMSAI YLFSEALTTQ QICAMHRLGP GYKSQFRFDN ECYLNLPDNH KRVSHFQLLP ATLGASALSG GSGSGTGSGT GNDASAAAAA AVAAGQQQQL QLQFQILAAE QEARAIDWSD EKLDLNAAFV KIRAVLTARN AVTLAGSSST GTTAVATAAA AAAAAGAGAG TTAAATSAAA AAAATQNEND AAVGQQQHAT HHHATAATGS ADDPLGHLPT GNASSSSSSF EQLRRMSSVS SLNSMVGSAD TEEVNQLKAV LYDGKLSNAI VFMYNPVATD GQLCLQSSPK GNVSYFVHTP HALMLQDVKA VVTHSIHCTL NSIGGIQVLF PLFSQLDMAH EGLGDIKRDP TLCSKLLGFI CELVETSQTV QQHMIQNRGF LVISFMLQRS SREHLTLEVL GSFLNLTKYL VTCLSANSDL LLKQLLDHVL FNPALWIYTP ANVQARLYSY LATEFLSDTQ IYSNVRRVST VLQTVHTLKY YYWVVNPRAK SGIIPKGLDG PRPAQKDILA IRAYILLFLK QLIMIGNGVK EDELQSILNY LTTMHEDENL HDVLQMLISL MSEHPSSMVP AFDVKHGVRS IFKLLAAESQ LIRLQALKLL GFFLSRSTHK RKYDVMSPHN LYTLLAERLL LYEESLSLPT YNVLYEIMTE HISQQILYTR HPEPESHYRL ENPMILKVVA TLIRQSKQTE SLIDVKKLFL QDMTLLCNSN RENRRTVLQM SVWQEWLIAM AYIHPKSSEE QKISDMVYSL FRMLLHHAIK HEYGGWRVWV DTLAIVHSKV SYEEFKLQFA QMYEHYERQR TDNITDPALR QARPISTISG WEREELHQQQ NGGSAAAVAT NQTAAVKGSV SIASLEDVPP VVEEEVEELE LEEVEIQEGP ITEETEQKSV IANISDVYNE QLKTDATCNG NLEDVKEEEP VQQQIGDLEK QPEPSTPLGA LRETLQLGDD MDVEELELAT AKDALNAEQH VSRVLQASEA ALNDCKMAVD DVLQESSSVL KDEEIELAVN EVVQGVLNNE KKTQSQDNKD NKEQPGEQDV NVSLLNSKNL LNNNNNNNNN SPSPTPTTAT ATAETEAETE VNANEIVSST EAPKAETETS VAPEVETPET AKPSPIVPSP VLATNQKTED AANKLNNNEK LAEISASPEP PIVVETPEAD LLQLSDSETK PNKETEAEDS VALAVRDIVE QLIDKVIDAT EAESASETKT ETNNNEIPKK EKQTSEEPED VETAETLAAA AKEIVQEVVE AALVMVQEES TQEKPEKGAN SEEEKNEIGK EEILLQLEEK PASTEVQETK IEGDLKKPED PKGHSSVEPK TPNLEEPKPQ ETEQQKSQEV AEELPQKPEE QVVAIVNQVL DTLVDDTVKA VAAEQTTQTS PAPEEQSPQI LAMESPATSV RVKPTEVDST TQTTPKNEAG SSLLVEQVQQ VLQEDDAQQS AGMTIEDEDY SNQQAAAAVE NANSSQLDAN HYGPGNPESK QQQQRSKSGS TRPMFSPGPT RPPFRIPEFK WSYIHQRLLS DVLFSLETDI QVWRSHSTKS VLDFVNSSEN AIFVVNTVHL ISQLADNLII ACGGLLPLLA SATSPNSELD VLEPTQGMPL EVAVSFLQRL VNMADVLIFA TSLNFGELEA EKNMSSGGIL RQCLRLVCTC AVRNCLECKE RTRYNVGALA RDVPGAAHLQ ALIRGAQASP KNIVESITGQ LSPVKDPEKL LQDMDVNRLR AVIYRDVEET KQAQFLSLAI VYFISVLMVS KYRDILEPPA EPQIQRQSPV LQRTAGGEAA SARPLFPQWS HHVYPQFLPE SHQNHNSNMQ HQQQQQQQQQ HQQQQHYYQQ QQQQQVVHNH SHHHMTAAYY QQQQHQQVAA GQQQHSPTPL ATHSTSSSAS STATSQPASS SSLSSLASQS QQQSHRQLHK QQQQQQQQQQ QQQPHYHPHQ PHYGLINGHQ QHPQLNGKHY AENGSTAGYH PHSHPHPHGG YMRNGDTSTL QQNGMPDYQA VGLMNGHGSG GTGNNNNSSL MNNMRNLRNG GGANSSSSPP GSHQVIQGVA TAGAVNANAA VGVGMGGAVG VGMGGVAGGL DGGVVYKTSA INNNYRYNGR NASAGTGGRQ IQDSDYEIIV VDENNPSVLA DNDSHSSGPP SIKSVDSDVG SLNMNSTENE VPEVESSSEI LIDDHKPSHS NDESWTDVNL NEDAAVQAAS AGIVVGLVDN RGNVISDKHD PSHHNQQQQQ QAGIIGQQQQ HGSLGHSERG DKPDSEISVV RVPDGYGGAG SGGGVNSGQG QGVPSNQRPR PEELPMKAPA LVAQLPLTTP SREASLTQKL EIALGPVCPL LREIMVDFAP FLSKTLVGSH GQELLMEGKG LTTFKNSHSV VELVMLLCSQ EWQNSLQKHA GLAFIELINE GRLLSHAMKD HIVRVANEAE FILNRMRADD VLKHADFESQ CAQTLLERRE EERMCDHLIT AARRRDNVIA SRLLEKVRNI MCNRHGAWGD SSSTSSGGAI VGAVQKSPYW KLDAWEDDAR RRKRMVQNPR GSSHPQATLK AALENGGPED AILQTRDEFH TQIAVSRTHP SGQHNGELLD DAELLIEDRE LDLDLTGPVN ISTKARLIAP GLVAPGTVSI TSTEMFFEVD EEHPEFQKID GEVLKYCDHL HGKWYFSEVR AIFSRRYLLQ NVALEIFLAS RTSILFAFPD QHTVKKVIKA LPRVGVGIKY GIPQTRRASM MSPRQLMRNS NMTQKWQRRE ISNFEYLMFL NTIAGRTYND LNQYPIFPWV LTNYESKDLD LSLPSNYRDL SKPIGALNPS RRAYFEERYE SWDSDTIPPF HYGTHYSTAA FTLNWLVRVE PFTTMFLALQ GGKFDYPDRL FSSVSLSWKN CQRDTSDVKE LIPEWYFLPE MFYNSSGYRL GHREDGALVD DIELPPWAKS PEEFVRINRM ALESEFVSCQ LHQWIDLIFG YKQRGPEAIR ATNVFYYLTY EGSVDLDGVL DPVMREAVEN QIRNFGQTPS QLLMEPHPPR SSAMHLSPMM FSAMPEDLCQ MLKFYQNSPV IHISANTYPQ LSLPSVVTVT AGHQFAVNRW NCNYTASVQS PSYAESPQSP GSNQPLTIDP VLAVHGTNNN SNAASRRHLG DNFSQMLKIR SNCFVTTVDS RFLIACGFWD NSFRVFATET AKIVQIVFGH FGVVTCMARS ECNITSDCYI ASGSADCTVL LWHWNARTQS IVGEGDVPTP RATLTGHEQA VTSVVISAEL GLVVSGSSNG PVLIHTTFGD LLRSLDPPAE FHSPELITMS REGFIVINYD KGNVAAYTIN GKKLRHETHN DNLQCMLLSR DGEYLMTAGD RGIVEVWRTF NLAPLYAFPA CNAGIRSLAL THDQKYLLAG LSTGSIIVFH IDFNRWHHEY QQRY // ID NCAH_DROME STANDARD; PRT; 189 AA. AC P42325; Q9VW67; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Neurocalcin homolog. GN NCA OR CG7641. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95081147; PubMed=7989365; RA Teng D.H.-F., Chen C.-K., Hurley J.B.; RT "A highly conserved homologue of bovine neurocalcin in Drosophila RT melanogaster is a Ca(2+)-binding protein expressed in neuronal RT tissues."; RL J. Biol. Chem. 269:31900-31907(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP MYRISTOYLATION, AND FUNCTION. RX MEDLINE=96215323; PubMed=8626592; RA Faurobert E., Chen C.-K., Hurley J.B., Teng D.H.-F.; RT "Drosophila neurocalcin, a fatty acylated, Ca2+-binding protein that RT associates with membranes and inhibits in vitro phosphorylation of RT bovine rhodopsin."; RL J. Biol. Chem. 271:10256-10262(1996). CC -!- FUNCTION: INHIBITS THE PHOSPHORYLATION OF RHODOPSIN IN A CALCIUM- CC DEPENDENT MANNER. PROBABLY BINDS TWO OR THREE CALCIUM IONS. CC -!- TISSUE SPECIFICITY: EXPRESSED IN NEURONAL TISSUES. HIGH LEVEL CC EXPRESSION SEEN IN THE CORTICAL REGIONS OF THE CENTRAL BRAIN AND CC LOWER LEVELS IN THE LAMINA, THE FIRST OPTIC LOBE OF THE BRAIN. IT CC IS ALSO FOUND IN THE THORACIC GANGLIA. CC -!- DEVELOPMENTAL STAGE: FOUND IN THE EMBRYOS, LARVAE AND PUPAE. CC EXPRESSION IN THE ADULT HEADS IS HIGHER THAN IN THE BODIES. CC -!- MASS SPECTROMETRY: MW=21975.51; METHOD=ELECTROSPRAY. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS, BELONGS TO CC THE RECOVERIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U15735; AAA62152.1; -. DR EMBL; AE003515; AAF49082.1; -. DR PIR; A55666; A55666. DR HSSP; P36610; 1G8I. DR FlyBase; FBgn0013303; Nca. DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; ISS. DR GO; GO:0005829; C:cytosol; ISS. DR GO; GO:0003779; F:actin binding; ISS. DR GO; GO:0005509; F:calcium ion binding; ISS. DR GO; GO:0030276; F:clathrin binding; ISS. DR GO; GO:0015631; F:tubulin binding; ISS. DR GO; GO:0016192; P:vesicle-mediated transport; ISS. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR001125; Recoverin. DR Pfam; PF00036; efhand; 3. DR PRINTS; PR00450; RECOVERIN. DR ProDom; PD000012; EF-hand; 1. DR SMART; SM00054; EFh; 3. DR PROSITE; PS00018; EF_HAND; 3. KW Calcium-binding; Repeat; Myristate; Lipoprotein. FT INIT_MET 0 0 FT LIPID 1 1 N-myristoyl glycine. FT DOMAIN 35 46 ANCESTRAL CALCIUM SITE 1. FT CA_BIND 72 83 EF-HAND 2 (POTENTIAL). FT CA_BIND 108 119 EF-HAND 3 (POTENTIAL). FT CA_BIND 156 167 EF-HAND 4 (POTENTIAL). SQ SEQUENCE 189 AA; 21762 MW; 3715201BEA2A824F CRC64; GKQNSKLKPE VLEDLKQNTE FTDAEIQEWY KGFLKDCPSG HLSVEEFKKI YGNFFPYGDA SKFAEHVFRT FDANGDGTID FREFLCALSV TSRGKLEQKL KWAFSMYDLD GNGYISRQEM LEIVTAIYKM VGSVMKMPED ESTPEKRTDK IFRQMDRNKD GKLSLEEFIE GAKSDPSIVR LLQCDPQSH // ID NCD_DROME STANDARD; PRT; 700 AA. AC P20480; Q9VAG8; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Claret segregational protein. GN NCD OR CA(ND) OR CG7831. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Canton-S; TISSUE=Ovary; RX MEDLINE=90231469; PubMed=1691829; RA Endow S.A., Henikoff S., Soler-Niedziela L.; RT "Mediation of meiotic and early mitotic chromosome segregation in RT Drosophila by a protein related to kinesin."; RL Nature 345:81-83(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 16-700 FROM N.A. RX MEDLINE=90275618; PubMed=2140958; RA McDonald H.B., Goldstein L.S.B.; RT "Identification and characterization of a gene encoding a RT kinesin-like protein in Drosophila."; RL Cell 61:991-1000(1990). RN [5] RP MOTOR DIRECTIONALITY. RX MEDLINE=91043032; PubMed=2146510; RA Walker R.A., Salmon E.D., Endow S.A.; RT "The Drosophila claret segregation protein is a minus-end directed RT motor molecule."; RL Nature 347:780-782(1990). RN [6] RP CHARACTERIZATION. RX MEDLINE=94155838; PubMed=8112290; RA Lockhart A., Cross R.A.; RT "Origins of reversed directionality in the ncd molecular motor."; RL EMBO J. 13:751-757(1994). RN [7] RP MUTANT ALLELE NCD(D). RX MEDLINE=91122049; PubMed=1825056; RA Komma D.J., Horne A.S., Endow S.A.; RT "Separation of meiotic and mitotic effects of claret RT non-disjunctional on chromosome segregation in Drosophila."; RL EMBO J. 10:419-424(1991). RN [8] RP CHARACTERIZATION OF MUTANT ALLELE NCD(D). RX MEDLINE=96283629; PubMed=8670831; RA Moore J.D., Song H., Endow S.A.; RT "A point mutation in the microtubule binding region of the Ncd motor RT protein reduces motor velocity."; RL EMBO J. 15:3306-3314(1996). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 335-700. RX MEDLINE=96195067; PubMed=8606780; RA Sablin E.P., Kull F.J., Cooke R., Vale R.D., Fletterick R.J.; RT "Crystal structure of the motor domain of the kinesin-related motor RT ncd."; RL Nature 380:555-559(1996). CC -!- FUNCTION: NCD IS REQUIRED FOR NORMAL CHROMOSOMAL SEGREGATION IN CC MEIOSIS, IN FEMALES, AND IN EARLY MITOTIC DIVISIONS OF THE EMBRYO. CC THE NCD MOTOR ACTIVITY IS DIRECTED TOWARD THE MICROTUBULE'S MINUS CC END. CC -!- MISCELLANEOUS: NCD(D) IS A MUTANT ALLELE THAT SHOWS ABNORMAL CC CHROMOSOMAL SEGREGATION. CC -!- SIMILARITY: BELONGS TO THE KINESIN-LIKE PROTEIN FAMILY. NCD CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52814; CAA36998.1; -. DR EMBL; M33932; AAA28716.1; -. DR EMBL; AE003771; AAF56942.1; -. DR EMBL; AY058596; AAL13825.1; -. DR EMBL; X57475; CAA40713.1; -. DR PIR; S09748; S09748. DR PDB; 1CZ7; 05-NOV-99. DR PDB; 2NCD; 09-JUN-99. DR FlyBase; FBgn0002924; ncd. DR GO; GO:0007100; P:centrosome separation; IGI. DR GO; GO:0000212; P:meiotic spindle assembly; NAS. DR InterPro; IPR001752; kinesin_motor. DR Pfam; PF00225; kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1. KW Motor protein; Cell division; Microtubule; ATP-binding; Coiled coil; KW Meiosis; Mitosis; 3D-structure. FT DOMAIN 196 346 COILED COIL (POTENTIAL). FT DOMAIN 347 700 KINESIN-MOTOR (BY SIMILARITY). FT NP_BIND 434 441 ATP (BY SIMILARITY). FT MUTAGEN 556 556 V->F: IN NCD(D); REDUCES MOTOR VELOCITY. FT CONFLICT 697 697 S -> N (IN REF. 1). SQ SEQUENCE 700 AA; 77473 MW; ADE043CBCE7FD561 CRC64; MESRLPKPSG LKKPQMPIKT VLPTDRIRAG LGGGAAGAGA FNVNANQTYC GNLLPPLSRD LNNLPQVLER RGGGARAASP EPMKLGHRAK LRRSRSACDI NELRGNKRTA AAPSLPSIPS KVSRLGGALT VSSQRLVRPA APSSITATAV KRPPVTRPAP RAAGGAAAKK PAGTGAAASS GAAAAAPKRI APYDFKARFH DLLEKHKVLK TKYEKQTEDM GELESMPQQL EETQNKLIET ESSLKNTQSD NECLQRQVKQ HTAKIETITS TLGRTKEELS ELQAIHEKVK TEHAALSTEV VHLRQRTEEL LRCNEQQAAE LETCKEQLFQ SNMERKELHN TVMDLRGNIR VFCRIRPPLE SEENRMCCTW TYHDESTVEL QSIDAQAKSK MGQQIFSFDQ VFHPLSSQSD IFEMVSPLIQ SALDGYNICI FAYGQTGSGK TYTMDGVPES VGVIPRTVDL LFDSIRGYRN LGWEYEIKAT FLEIYNEVLY DLLSNEQKDM EIRMAKNNKN DIYVSNITEE TVLDPNHLRH LMHTAKMNRA TASTAGNERS SRSHAVTKLE LIGRHAEKQE ISVGSINLVD LAGSESPKTS TRMTETKNIN RSLSELTNVI LALLQKQDHI PYRNSKLTHL LMPSLGGNSK TLMFINVSPF QDCFQESVKS LRFAASVNSC KMTKAKRNRY LNNSVANSST QSNNSGSFDK // ID NCKX_DROME STANDARD; PRT; 856 AA. AC Q9U6A0; Q9VL95; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sodium/potassium/calcium exchanger (Na(+)/K(+)/Ca(2+)-exchange DE protein). GN NCKX30C OR CG18660/CG4106. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=20015003; PubMed=10545508; RA Haug-Collet K., Pearson B., Webel R., Szerencsei R.T., Winkfein R.J., RA Schnetkamp P.P.M., Colley N.J.; RT "Cloning and characterization of a potassium-dependent sodium/calcium RT exchanger in Drosophila."; RL J. Cell Biol. 147:659-670(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY FUNCTION IN THE REMOVAL AND MAAINTENANCE OF CALCIUM CC HOMEOSTASIS DURING SIGNALING IN THE ADULT AND IN SIGNALING EVENTS CC DURING EMBRYOGENESIS AND PATTERNING OF IMAGINAL DISKS. TRANSPORTS CC ONE CA(2+) AND ONE K(+) IN EXCHANGE FOR FOUR NA(+). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ADULT NERVOUS SYSTEM. CC EXPRESSED IN THE PHOTORECEPTOR CELLS AS WELL AS IN THE LAMINA, CC MEDULLA, AND OPTIC LOBES OF THE BRAIN. CC -!- DEVELOPMENTAL STAGE: EXPRESED DURING VENTRAL NERVE CORD CC DEVELOPMENT IN THE EMBRYO AND IN LARVAL IMAGINAL DISKS. EXPRESSED CC IN A DORSAL-VENTRAAL PATTERN IN THE EYE-ANTENNL DISK. CC -!- SIMILARITY: BELONGS TO THE SLC24A FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF190455; AAF07938.1; -. DR EMBL; AE003626; AAF52801.1; -. DR FlyBase; FBgn0028704; Nckx30C. DR InterPro; IPR004481; K_NaCaexchng. DR InterPro; IPR004837; NaCa_Exmemb. DR Pfam; PF01699; Na_Ca_Ex; 2. DR TIGRFAMs; TIGR00367; TIGR00367; 1. KW Transport; Antiport; Symport; Calcium transport; Potassium transport; KW Sodium transport; Transmembrane; Glycoprotein; Repeat. FT DOMAIN 1 330 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 331 351 POTENTIAL. FT DOMAIN 352 375 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 376 396 POTENTIAL. FT DOMAIN 397 402 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 403 423 POTENTIAL. FT DOMAIN 424 433 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 434 454 POTENTIAL. FT DOMAIN 455 458 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 459 479 POTENTIAL. FT DOMAIN 480 668 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 669 685 POTENTIAL. FT DOMAIN 686 695 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 696 716 POTENTIAL. FT DOMAIN 717 731 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 732 752 POTENTIAL. FT DOMAIN 753 770 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 771 791 POTENTIAL. FT DOMAIN 792 797 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 798 818 POTENTIAL. FT DOMAIN 819 827 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 828 848 POTENTIAL. FT DOMAIN 849 856 CYTOPLASMIC (POTENTIAL). FT REPEAT 372 412 ALPHA-1. FT REPEAT 739 770 ALPHA-2. FT DOMAIN 10 16 POLY-GLN. FT DOMAIN 98 105 POLY-ARG. FT CARBOHYD 69 69 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 303 303 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 309 309 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 110 110 S -> F (IN REF. 1). FT CONFLICT 365 365 K -> R (IN REF. 1). FT CONFLICT 827 827 K -> R (IN REF. 1). SQ SEQUENCE 856 AA; 92148 MW; E51D71F7C34A994A CRC64; MLQPTTCSKQ QQQRQQPAIA TAAVGGAAVQ ELLRKAAAKD HGALAAATAT ATAASTTATT ATAATASRNS SNTWCHSDDM LSAGRSRSSS TTIDFNSRRR RGRLRGHAPS DLAMNKQHQA TILDECVNIF KRLVLLTLKT ISATTITKAK TRSRTAAQLP ATSAASATSS RGASAEQLLH PSSRSRCRSR RCLRLPIYSI LLLCLTTQGL GLGDAAKPRP AKQHFGGSNS NSPNQNQNHN DVLGGVGAPS QTSGEDEAEI MYPFQSGEQM FGLEEDQEQD PELNSNAVPG SDEDNAGNQR GINDTHNDNS TTTKTPLFPK DLFTKEQLEN GAVILHIIGV IYMFVALAIV CDEFFVPSLD VIIEKLGITD DVAGATFMAA GGSAPELFTS VIGVFVSFDD VGIGTIVGSA VFNILFVIGM CALFSKTVLS LTWWPLFRDC SFYSISLLVL IYFFRDNRIF WWEALILFTI YIGYVAFMKW NVQVETCVKK MITKNKVTRV RSTDQLMPAG NAANSSETSM ATQPGGSVTS RAASETRSGP PGSSNAGATG NSSGGGGTSG STQTGAKFRH GLLQLMIHTI DPLHDGKVDE KATQLHAIAS LKVLLDATKP QRGGATTSAA NHVKINLKET TLADRPNGNI DTTLDSAPEI EDEPEPLSMA WPDTARKRLT YVLVAPLLVP MWLTLPDTRT PRGKRFFPVT FIGSIVWIAA FSYLMVWWAN VAGDTARIPP EVMGLTFLAA GTSIPDLITS VIVARKGFGD MAVSSSVGSN IFDVTVGLPI PWLLYGIIYG APVEVNSVGM VCSITILFMM LVFVVMSIAC FRWRMNKGLG FTMFLLYFAF VAVSLMFEYD VITCPF // ID NCPR_DROME STANDARD; PRT; 679 AA. AC Q27597; Q9VMF2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NADPH-cytochrome P450 reductase (EC 1.6.2.4) (CPR) (P450R). GN CPR OR CG11567. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Antenna; RX MEDLINE=97311413; PubMed=9168130; RA Hovemann B.T., Sehlmeyer F., Malz J.; RT "Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: RT pronounced expression in antennae may be related to odorant RT clearance."; RL Gene 189:213-219(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THIS ENZYME IS REQUIRED FOR ELECTRON TRANSFER FROM NADP CC TO CYTOCHROME P450 IN MICROSOMES. IT CAN ALSO PROVIDE ELECTRON CC TRANSFER TO HEME OXYGENASE AND CYTOCHROME B5. MAY FUNCTION TO CC CLEAR THE OLFACTORY ORGAN (ANTENNAE) FROM ACCUMULATING CHEMICALS. CC -!- CATALYTIC ACTIVITY: NADPH + 2 FERRICYTOCHROME = NADP(+) + 2 CC FERROCYTOCHROME. CC -!- COFACTOR: FAD AND FMN. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM. ANCHORED TO THE ER CC MEMBRANE BY ITS N-TERMINAL HYDROPHOBIC REGION (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: HIGH IN ANTENNAE. CC -!- DEVELOPMENTAL STAGE: EMBRYOS AND ADULTS. CC -!- SIMILARITY: CONTAINS 1 FAD-BINDING DOMAIN. CC -!- SIMILARITY: CONTAINS 1 FLAVODOXIN-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X93090; CAA63639.1; -. DR EMBL; AE003613; AAF52367.1; -. DR EMBL; AY052000; AAK93424.1; -. DR HSSP; P16435; 1B1C. DR FlyBase; FBgn0015623; Cpr. DR InterPro; IPR003097; FAD_binding. DR InterPro; IPR008254; Flav_nitox_synth. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001709; FPN_cyt_redctse. DR InterPro; IPR001433; Oxred_FAD/NAD(P). DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; flavodoxin; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Oxidoreductase; Flavoprotein; FMN; FAD; NADP; Endoplasmic reticulum; KW Membrane. FT DOMAIN 84 228 FLAVODOXIN-LIKE. FT DOMAIN 278 497 FAD-BINDING. FT NP_BIND 176 207 FMN (PYRIMIDINE PART) (BY SIMILARITY). FT NP_BIND 320 331 FAD (ADP PART) (BY SIMILARITY). FT NP_BIND 457 467 FAD (FLAVIN PART) (BY SIMILARITY). FT NP_BIND 537 555 NADP (RIBOSE PART) (BY SIMILARITY). FT NP_BIND 632 648 NADP (ADP PART) (BY SIMILARITY). FT CONFLICT 38 39 AA -> VT (IN REF. 1). FT CONFLICT 45 45 S -> T (IN REF. 1). FT CONFLICT 132 132 I -> T (IN REF. 1). SQ SEQUENCE 679 AA; 76346 MW; C6387C111A0EDB4A CRC64; MASEQTIDGA AAIPSGGGDE PFLGLLDVAL LAVLIGGAAF YFLRSRKKEE EPTRSYSIQP TTVCTTSASD NSFIKKLKAS GRSLVVFYGS QTGTGEEFAG RLAKEGIRYR LKGMVADPEE CDMEELLQLK DIDNSLAVFC LATYGEGDPT DNAMEFYEWI TSGDVDLSGL NYAVFGLGNK TYEHYNKVAI YVDKRLEELG ANRVFELGLG DDDANIEDDF ITWKDRFWPA VCDHFGIEGG GEEVLIRQYR LLEQPDVQPD RIYTGEIARL HSIQNQRPPF DAKNPFLAPI KVNRELHKGG GRSCMHIELS IEGSKMRYDA GDHVAMFPVN DKSLVEKLGQ LCNADLDTVF SLINTDTDSS KKHPFPCPTT YRTALTHYLE ITAIPRTHIL KELAEYCTDE KEKELLRSMA SISPEGKEKY QSWIQDACRN IVHILEDIKS CRPPIDHVCE LLPRLQPRYY SISSSAKLHP TDVHVTAVLV EYKTPTGRIN KGVATTYLKN KQPQGSEEVK VPVFIRKSQF RLPTKPETPI IMVGPGTGLA PFRGFIQERQ FLRDEGKTVG ESILYFGCRK RSEDYIYESE LEEWVKKGTL NLKAAFSRDQ GKKVYVQHLL EQDADLIWNV IGENKGHFYI CGDAKNMAVD VRNILVKILS TKGNMSEADA VQYIKKMEAQ KRYSADVWS // ID NDKA_DROME STANDARD; PRT; 153 AA. AC P08879; Q9V9U5; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nucleoside diphosphate kinase (EC 2.7.4.6) (NDK) (NDP kinase) DE (Abnormal wing discs protein) (Killer-of-prune protein). GN AWD OR K-PN OR CG2210. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89079007; PubMed=2849580; RA Biggs J., Tripoulas N., Hersperger E., Dearolf C., Shearn A.; RT "Analysis of the lethal interaction between the prune and Killer of RT prune mutations of Drosophila."; RL Genes Dev. 2:1333-1343(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 90-106. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). RN [5] RP FUNCTION. RX MEDLINE=91077931; PubMed=2175255; RA Biggs J., Hersperger E., Steeg P.S., Liotta L.A., Shearn A.; RT "A Drosophila gene that is homologous to a mammalian gene associated RT with tumor metastasis codes for a nucleoside diphosphate kinase."; RL Cell 63:933-940(1990). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX MEDLINE=94363226; PubMed=8081741; RA Chiadmi M., Morera S., Lascu I., Dumas C., le Bras G., Veron M., RA Janin J.; RT "Crystal structure of the Awd nucleotide diphosphate kinase from RT Drosophila."; RL Structure 1:283-293(1993). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=95399390; PubMed=7669763; RA Morera S., Chiadmi M., Lebras G., Lascu I., Janin J.; RT "Mechanism of phosphate transfer by nucleoside diphosphate kinase: RT X-ray structures of the phosphohistidine intermediate of the enzymes RT from Drosophila and Dictyostelium."; RL Biochemistry 34:11062-11070(1995). CC -!- FUNCTION: MAJOR ROLE IN THE SYNTHESIS OF NUCLEOSIDE TRIPHOSPHATES CC OTHER THAN ATP. THIS NDK IS MICROTUBULE-ASSOCIATED. CC -!- CATALYTIC ACTIVITY: ATP + NUCLEOSIDE DIPHOSPHATE = ADP + CC NUCLEOSIDE TRIPHOSPHATE. CC -!- SUBUNIT: HOMOHEXAMER. CC -!- MISCELLANEOUS: MUTATIONS CAUSE ABNORMAL TISSUE MORPHOLOGY AND CC NECROSIS AND WIDESPREAD ABERRANT DIFFERENTIATION. CC -!- SIMILARITY: BELONGS TO THE NDK FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13107; CAA31500.1; -. DR EMBL; AE003779; AAF57188.2; -. DR PIR; S01908; S01908. DR PDB; 1NDL; 30-APR-94. DR PDB; 1NSQ; 10-JUL-95. DR FlyBase; FBgn0000150; awd. DR GO; GO:0005874; C:microtubule; IDA. DR InterPro; IPR001564; NDK. DR Pfam; PF00334; NDK; 1. DR PRINTS; PR01243; NUCDPKINASE. DR ProDom; PD001018; NDK; 1. DR SMART; SM00562; NDK; 1. DR PROSITE; PS00469; NDP_KINASES; 1. KW Transferase; Kinase; ATP-binding; 3D-structure. FT ACT_SITE 119 119 FT HELIX 3 5 FT STRAND 7 12 FT HELIX 14 18 FT TURN 19 20 FT HELIX 22 32 FT TURN 33 33 FT STRAND 35 39 FT STRAND 42 42 FT HELIX 46 52 FT TURN 53 53 FT HELIX 54 56 FT TURN 57 58 FT TURN 60 61 FT HELIX 62 69 FT TURN 70 70 FT STRAND 74 80 FT TURN 82 83 FT HELIX 84 92 FT HELIX 97 99 FT TURN 102 103 FT HELIX 105 109 FT HELIX 113 115 FT STRAND 118 120 FT HELIX 124 134 FT HELIX 137 139 FT TURN 146 147 FT HELIX 148 150 FT TURN 151 151 SQ SEQUENCE 153 AA; 17170 MW; E98765853255445E CRC64; MAANKERTFI MVKPDGVQRG LVGKIIERFE QKGFKLVALK FTWASKELLE KHYADLSARP FFPGLVNYMN SGPVVPMVWE GLNVVKTGRQ MLGATNPADS LPGTIRGDFC IQVGRNIIHG SDAVESAEKE IALWFNEKEL VTWTPAAKDW IYE // ID NDL_DROME STANDARD; PRT; 2616 AA. AC P98159; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Serine protease nudel precursor (EC 3.4.21.-). GN NDL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Ovary; RX MEDLINE=95401268; PubMed=7671306; RA Hong C.C., Hashimoto C.; RT "An unusual mosaic protein with a protease domain, encoded by the RT nudel gene, is involved in defining embryonic dorsoventral polarity RT in Drosophila."; RL Cell 82:785-794(1995). CC -!- FUNCTION: NUDEL, PIPE AND WINDBEUTEL TOGETHER TRIGGER THE PROTEASE CC CASCADE WITHIN THE EXTRAEMBRYONIC PERIVITELLINE COMPARTMENT WHICH CC INDUCES DORSOVENTRAL POLARITY OF THE DROSOPHILA EMBRYO. NUDEL IS CC DIRECTLY INVOLVED IN LOCALLY PRODUCING THE TOLL LIGAND. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR MATRIX. CC -!- TISSUE SPECIFICITY: FOLLICLE. CC -!- PTM: REQUIRES CLEAVAGE FOR ACTIVATION (PRESUMABLY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -!- SIMILARITY: CONTAINS 11 LDL-RECEPTOR CLASS A DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U29153; AAA83086.1; -. DR PIR; A57096; A57096. DR HSSP; P00763; 1DPO. DR MEROPS; S01.013; -. DR FlyBase; FBgn0002926; ndl. DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS. DR GO; GO:0007306; P:insect chorion formation; IMP. DR GO; GO:0007310; P:oocyte dorsal/ventral axis determination; NAS. DR GO; GO:0016485; P:protein processing; IGI. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR002172; LDL_receptor_A. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00057; ldl_recept_a; 6. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00261; LDLRECEPTOR. DR SMART; SM00192; LDLa; 8. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS01209; LDLRA_1; 6. DR PROSITE; PS50068; LDLRA_2; 8. DR PROSITE; PS50240; TRYPSIN_DOM; 2. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Serine protease; Glycoprotein; Signal; Developmental protein; KW Hydrolase; Repeat; Zymogen; Extracellular matrix. FT SIGNAL 1 43 POTENTIAL. FT CHAIN 44 2616 SERINE PROTEASE NUDEL. FT REPEAT 261 269 WIID 1. FT REPEAT 320 328 WIID 2. FT REPEAT 399 407 WIID 3. FT REPEAT 446 454 WIID 4. FT REPEAT 477 485 WIID 5. FT REPEAT 528 536 WIID 6. FT DOMAIN 889 929 LDL-RECEPTOR CLASS A 1. FT DOMAIN 929 956 LDL-RECEPTOR CLASS A 2 (PARTIAL). FT DOMAIN 955 1006 LDL-RECEPTOR CLASS A 3. FT DOMAIN 1145 1383 SERINE PROTEASE 1. FT DOMAIN 1394 1432 LDL-RECEPTOR CLASS A 4. FT DOMAIN 1489 1702 SER/THR-RICH. FT DOMAIN 1713 1743 LDL-RECEPTOR CLASS A 5 (PARTIAL). FT DOMAIN 1745 1775 LDL-RECEPTOR CLASS A 6 (PARTIAL). FT DOMAIN 1774 1813 LDL-RECEPTOR CLASS A 7. FT DOMAIN 2027 2301 SERINE PROTEASE 2. FT DOMAIN 2308 2346 LDL-RECEPTOR CLASS A 8. FT DOMAIN 2349 2389 LDL-RECEPTOR CLASS A 9. FT DOMAIN 2387 2419 LDL-RECEPTOR CLASS A 10 (PARTIAL). FT DOMAIN 2419 2459 LDL-RECEPTOR CLASS A 11. FT SITE 1031 1033 CELL ATTACHMENT SITE (POTENTIAL). FT ACT_SITE 1185 1185 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 1233 1233 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 1332 1332 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 891 905 BY SIMILARITY. FT DISULFID 899 918 BY SIMILARITY. FT DISULFID 912 927 BY SIMILARITY. FT DISULFID 957 982 BY SIMILARITY. FT DISULFID 964 995 BY SIMILARITY. FT DISULFID 989 1004 BY SIMILARITY. FT DISULFID 1170 1186 BY SIMILARITY. FT DISULFID 1276 1338 POTENTIAL. FT DISULFID 1305 1317 BY SIMILARITY. FT DISULFID 1328 1359 BY SIMILARITY. FT DISULFID 1396 1408 BY SIMILARITY. FT DISULFID 1401 1421 BY SIMILARITY. FT DISULFID 1415 1430 BY SIMILARITY. FT DISULFID 1776 1789 BY SIMILARITY. FT DISULFID 1783 1802 BY SIMILARITY. FT DISULFID 1796 1811 BY SIMILARITY. FT DISULFID 2310 2320 BY SIMILARITY. FT DISULFID 2315 2333 BY SIMILARITY. FT DISULFID 2327 2344 BY SIMILARITY. FT DISULFID 2351 2364 BY SIMILARITY. FT DISULFID 2358 2377 BY SIMILARITY. FT DISULFID 2371 2387 BY SIMILARITY. FT DISULFID 2421 2435 BY SIMILARITY. FT DISULFID 2428 2448 BY SIMILARITY. FT DISULFID 2442 2457 BY SIMILARITY. FT CARBOHYD 291 291 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 347 347 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 379 379 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 417 417 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 492 492 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 515 515 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 598 598 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 794 794 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 827 827 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 829 829 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 861 861 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 975 975 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1064 1064 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1445 1445 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1878 1878 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1956 1956 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2023 2023 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2144 2144 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2173 2173 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2197 2197 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2237 2237 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2269 2269 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2420 2420 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2556 2556 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2601 2601 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 2616 AA; 292371 MW; 25DCB13213DC7D13 CRC64; MNYNMDEMEA TRLLRHPRRW WSIGFGKRIV AISILVIIVL LFSLVYHGLV VEKIDQVQQI AALNARHQVL FNQPFEEDQS ALTVSPQTLH FKLLDEDMNK DMEDSKNRRR KHMRQMLVKL RLNKKHRMRR DLHGLDLLDP VRMEANMQHL YTKLRSKRAR EALSQLEHEF VRCKKHTPQD CMSAFLRMYK MAKEVTEKME KMKAIMREQQ PKLESSSMES HEQKGTFSPA DLIQVTTAEA TTVAVHATEK PARTKIKPSR ISWIIDGHDH DESPVYTDGA PKKETTKAPW NTTQLVEITT TKIDATATER TTVESTTEKI SWILDHFDKP QEILRTTEGP GQRIIRNVTT TSASSEPIVD TETTNSDHVP TTENGLVFNI TTDGPVETTK STAQRKLSFD WILDGEENVE PEVKSTNTTT TTAATTTTGA TSETIIVTTE LPKITFDWII DGREVVEPQE TTTEVTGTTE RLRKMPFDWI IDGEEVVEPQ ENVTTTTIAT TVAVSTTEIN ERIHNSTAYP TKPKPVKFDW IIDGGESSGE VSTSSTSQPK LTTREAISNP ESPRSSHPLD NPTSIENMLE SFEQHEEQKP ILRVLNANES SSETVTDGYE RQLWLKKFED QARPNQNELI DTFGTALDAK ALDKMGPKIN PLNGHTWNAA DAQILSLCER VALRMRNKVA TMSDGETKEK GETFTASPSV QFTSRAPGGF PVSGETMKAS AQFMFNPNFG MPSIPVCFYM TPANFRMPMW SNTPTFMGMQ GAHFGGSSNP GAGIFFVPQQ FGPSGNFFGG SGGSGAGGQG ANIFSKNASP QKPTNGQQQV YCSYMQNQSG RGAGQSQTSS QQQQGGQSAF SNANFKMRHA NQTSTANQQG QIIYASYAGL PQQPIQERSR CPEPDQFSCF GQQECIPAAR WCDNVVDCSD GSDESACTCA DRVDEERLCD GYEDCPMGED ELGCFGCESL AYSCYENPQD FAKRNRSTIS MCYSRLERCD GFMNCLNGRD EEQCSMLVTD VADHMSHGAS ASEGYLYHNY RGDWHPVCNN GEKWAALACQ MDENSRMDHS ASLNVSFQTL TLPGPFIEPS LHAGVHFAQA CHGRNSHDSL VDHVAYVKCP PMQCGLPSKS SMLEHSKRVR RAVSDSKEIV GDGRIVGGSH TSALQWPFVV AIYRNGKFHC GGTIYSDRWI ISAAHCVINY GKYFYEVRAG LLRRSSYSPA TQIQPVSHVV VHQAYERRSM RNDLSLLRLL NPLQFNRWVK PICLPDKGRT TVGDDWIWGP VEHTLCTVVG WGAIREKGPS SDPMRQVIVP IRKKCTDPED QASEDICAGD PDGGRDACQG DSGGPLFCRS VSNADEFYLA GVVSHGNGCA RPQEFGVYTR VTLYLDWLEM ATTPRLLPKL QPLQLCPGFI CVWGGKRCIS KRQRCDRNVD CLGGEDEVGC TYNFLPDMVG GVRQNISTTT ESDYHPVKES EEKSKMREVI PIDDEDLKAE QDEEDLLKST TSLGQTETTQ GPMDLSFAEQ ITSTTSDDLS ITDETTSTDF TVSDSATSPS TLLPTTTNPS TWLPSTNIET STFSFTTTES EASTKQETLP TTVAQTTTIP TSTEDLKKLT DLVTEFMEST TFETTMEVET TTLSLTSTDA PILVTTEGVK ETTTTEDTTT ISSIVTLTTT PLATISTTIP TTEKHVAVTT LAPTTTTESA KTTTTHSSST HSEKDQIQIP NKFVCKKMSQ IVDIMMRCDR KVDCEDGTDE LDCTCKDYLK GSLKGLICDG KADCEDLTDE QNCVECQSNE FRCPLSKTCL PLSKRCDNKV DCKFKEDEKD CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH ETGYHEHQAK TANAVCALLG FNGAHYFNSS EFVTQQEKQP ITPELKGGRN RMAAQIHSMV GDNVQFTENE VIIPELGHPS ASRPEKDRLL PRKCVGIYVE CNPYSNKTTP LKTFSAGQVV KEKPIEQVPV LSPTIETHNT PNVHFKPQIP AMVVNKKDEI LDRLDKLIKS KKNKTILVNE QLHEAIEELH WPWLADVYMN GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH EQIRRVDCFE GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSNARQ CISVLHDDAT GRIKTVAITR IHNATNCDSC YKLQEKQPPA NLMRLLNVSA EDMASISEEV ELINGVAPTE LPAITKFTTC NQFGLKNVSD AHHNPSDQGV LVCRDSHTGW FPTALFNYNN SDCQSFKQPF GIRTLELVYK SLQDIIDKPS CKMLLPAPDC STHRCPLGTC LPQAAMCNGR SDCHDGSDEE ETKCRQQKQQ CAPGEMKCRT SFKCVPKSKF CDHVPDCEDM TDEPTICSCF TYLQATDPSK ICDGKRNCWD KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN GEDERYCFGI EHPLHLQKKD FWTNSQHTQP EIAPQYGQVI EQTYGIWHTK CFPKSKPPQV DEVREICKKL GYNPYRQPSY RLIDDEENKP VHTYELADRQ GRSFSNESLM GKYRDSTKAL IISKFSPLQL NERLTLFLKS SRPIAELVRW NATDSSMCYR LEIRCA // ID NEMS_DROME STANDARD; PRT; 100 AA. AC P41494; Q9VC91; DT 01-NOV-1995 (Rel. 32, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dromyosuppressin precursor (Neomyosuppressin) (NEB-MS). GN DMS OR NEMS OR CG6440. OS Drosophila melanogaster (Fruit fly), and OS Sarcophaga bullata (Grey flesh fly) (Neobellieria bullata). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7385; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 87-96. RC SPECIES=D.melanogaster; RX MEDLINE=93002195; PubMed=1390001; RA Nichols R.; RT "Isolation and structural characterization of Drosophila RT TDVDHVFLRFamide and FMRFamide-containing neural peptides."; RL J. Mol. Neurosci. 3:213-218(1992). RN [4] RP SEQUENCE OF 87-96, AND AMIDATION. RC SPECIES=D.melanogaster; TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). RN [5] RP SEQUENCE OF 87-96. RC SPECIES=S.bullata; TISSUE=Head; RX MEDLINE=93047886; PubMed=1358537; RA Fonagy A., Schoofs L., Proost P., Van Damme J., Bueds H., De Loof A.; RT "Isolation, primary structure and synthesis of neomyosuppressin, a RT myoinhibiting neuropeptide from the grey fleshfly, Neobellieria RT bullata."; RL Comp. Biochem. Physiol. 102C:239-245(1992). CC -!- FUNCTION: MYOINHIBITING NEUROPEPTIDE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003747; AAF56283.1; -. DR EMBL; AY075325; AAL68192.1; -. DR PIR; A56633; A56633. DR FlyBase; FBgn0011581; Dms. DR GO; GO:0005184; F:neuropeptide hormone activity; NAS. KW Neuropeptide; Signal; Cleavage on pair of basic residues; Amidation. FT SIGNAL 1 24 POTENTIAL. FT PROPEP 25 84 FT PEPTIDE 87 96 DROMYOSUPPRESSIN. FT MOD_RES 96 96 AMIDATION (G-97 PROVIDE AMIDE GROUP). SQ SEQUENCE 100 AA; 11070 MW; 177CBFA528D8BE58 CRC64; MSFAQFFVAC CLAIVLLAVS NTRAAVQGPP LCQSGIVEEM PPHIRKVCQA LENSDQLTSA LKSYINNEAS ALVANSDDLL KNYNKRTDVD HVFLRFGKRR // ID NETA_DROME STANDARD; PRT; 727 AA. AC Q24567; Q94528; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Netrin-A precursor. GN NETA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=96374354; PubMed=8780645; RA Mitchell K.J., Doyle J.L., Serafini T., Kennedy T., RA Tessier-Lavigne M., Goodman C.S., Dickson B.J.; RT "Genetic analysis of Netrin genes in Drosophila: Netrins guide CNS RT commissural axons and peripheral motor axons."; RL Neuron 17:203-215(1996). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=96374355; PubMed=8780646; RA Harris R., Moore-Sabatelli L., Seeger M.; RT "Guidance cues at the Drosophila CNS midline: identification and RT characterization of two Drosophila Netrin/UNC-6 homologs."; RL Neuron 17:217-228(1996). CC -!- FUNCTION: NETRINS CONTROL GUIDANCE OF CNS COMMISSURAL AXONS AT THE CC MIDLINE AND PERIPHERAL MOTOR AXONS. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: AT THE MIDLINE OF DEVELOPING CNS AND IN CC DIFFERENT SUBSETS OF NEURONS, MUSCLES, AND EPIDERMAL PATCHES. CC -!- SIMILARITY: CONTAINS 1 LAMININ N-TERMINAL DOMAIN. CC -!- SIMILARITY: CONTAINS 3 LAMININ EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 C345C DOMAIN. CC -!- SIMILARITY: TO CAENORHABDITIS ELEGANS UNC-6 PROTEIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U60316; AAB17533.1; -. DR EMBL; U63736; AAB17547.1; -. DR HSSP; P02468; 1TLE. DR FlyBase; FBgn0015773; NetA. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR008212; Lam_N2. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR008211; LamNT. DR InterPro; IPR001134; Netrin_C. DR Pfam; PF00053; laminin_EGF; 3. DR Pfam; PF00055; laminin_Nterm; 1. DR Pfam; PF01759; NTR; 1. DR ProDom; PD002082; Lam_N2; 1. DR SMART; SM00643; C345C; 1. DR SMART; SM00180; EGF_Lam; 3. DR SMART; SM00136; LamNT; 1. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01248; LAMININ_TYPE_EGF; 3. KW Glycoprotein; Extracellular matrix; Signal; Laminin EGF-like domain; KW Repeat. FT SIGNAL 1 29 POTENTIAL. FT CHAIN 30 727 NETRIN-A. FT DOMAIN 30 311 LAMININ N-TERMINAL (DOMAIN VI). FT DOMAIN 313 368 LAMININ EGF-LIKE 1. FT DOMAIN 369 431 LAMININ EGF-LIKE 2. FT DOMAIN 432 481 LAMININ EGF-LIKE 3. FT DOMAIN 482 727 C345C (DOMAIN C). FT DISULFID 313 322 BY SIMILARITY. FT DISULFID 315 332 BY SIMILARITY. FT DISULFID 334 343 BY SIMILARITY. FT DISULFID 346 366 BY SIMILARITY. FT DISULFID 369 378 BY SIMILARITY. FT DISULFID 371 396 BY SIMILARITY. FT DISULFID 399 408 BY SIMILARITY. FT DISULFID 411 429 BY SIMILARITY. FT DISULFID 432 444 BY SIMILARITY. FT DISULFID 434 451 BY SIMILARITY. FT DISULFID 453 462 BY SIMILARITY. FT DISULFID 465 479 BY SIMILARITY. FT CARBOHYD 108 108 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 112 112 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 127 127 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 445 445 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 653 653 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 680 680 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 514 516 GAA -> APP (IN REF. 2). FT CONFLICT 637 637 T -> S (IN REF. 2). SQ SEQUENCE 727 AA; 80358 MW; 90A80868B51752D5 CRC64; MIRGILLLLL GTTRFSPIQC IFNDVYFKMF SQQAPPEDPC YNKAHEPRAC IPDFVNAAYD APVVASSTCG SSGAQRYCEY QDHERSCHTC DMTDPLRSFP ARSLTDLNNS NNVTCWRSEP VTGSGDNVTL TLSLGKKFEL TYVILQLCPH APRPDSMVIY KSTDHGLSWQ PFQFFSSQCR RLFGRPARQS TGRHNEHEAR CSDVTRPLVS RIAFSTLEGR PSSRDLDSSP VLQDWVTATD IRVVFHRLQR PDPQALLSLE AGGATDLASG KYSVPLANGP AGNNIEANLG GDVATSGSGL HYAISDFSVG GRCKCNGHAS KCSTDASGQL NCECSHNTAG RDCERCKPFH FDRPWARATA KEANECKECN CNKHARQCRF NMEIFRLSQG VSGGVCQNCR HSTTGRNCHQ CKEGFYRDAT KPLTHRKVCK ACDCHPIGSS GKICNSTSGQ CPCKDGVTGL TCNRCARGYQ QSRSHIAPCI KQPPRMINML DTQNTAPEPD APESSPGSGG DRNGAAEWPP SLSTIAPRAA GVKCGKCRVS TKRLNLNKFC KRDYAIMAKV IGRDTSSEAV SREVQRRAMD PDVADYEMDQ VQPGSARSPI TGVYEFQAAD YPNPNPNPRG SEMERFDLQI QAVFKRTRPG ESSGAGNVYG MPNTTLKRGP MTWIIPTKDL ECRCPRIRVN RSYLILGRDS EAPPGYLGIG PHSIVIEWKE DWYRRMKRFQ RRARTCA // ID NETB_DROME STANDARD; PRT; 793 AA. AC Q24568; Q9VY23; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Netrin-B precursor. GN NETB OR CG10521. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=96374354; PubMed=8780645; RA Mitchell K.J., Doyle J.L., Serafini T., Kennedy T., RA Tessier-Lavigne M., Goodman C.S., Dickson B.J.; RT "Genetic analysis of Netrin genes in Drosophila: Netrins guide CNS RT commissural axons and peripheral motor axons."; RL Neuron 17:203-215(1996). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=96374355; PubMed=8780646; RA Harris R., Moore-Sabatelli L., Seeger M.; RT "Guidance cues at the Drosophila CNS midline: identification and RT characterization of two Drosophila Netrin/UNC-6 homologs."; RL Neuron 17:217-228(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NETRINS CONTROL GUIDANCE OF CNS COMMISSURAL AXONS AT THE CC MIDLINE AND PERIPHERAL MOTOR AXONS. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: AT THE MIDLINE OF DEVELOPING CNS AND IN CC DIFFERENT SUBSETS OF NEURONS, MUSCLES, AND EPIDERMAL PATCHES. CC -!- SIMILARITY: CONTAINS 1 LAMININ N-TERMINAL DOMAIN. CC -!- SIMILARITY: CONTAINS 3 LAMININ EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 C345C DOMAIN. CC -!- SIMILARITY: TO CAENORHABDITIS ELEGANS UNC-6 PROTEIN. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-9 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U60317; AAB17534.1; -. DR EMBL; U63737; AAB17548.1; -. DR EMBL; AE003496; AAF48382.1; -. DR HSSP; P02468; 1KLO. DR FlyBase; FBgn0015774; NetB. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR008212; Lam_N2. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR008211; LamNT. DR InterPro; IPR001134; Netrin_C. DR Pfam; PF00053; laminin_EGF; 3. DR Pfam; PF00055; laminin_Nterm; 1. DR Pfam; PF01759; NTR; 1. DR PRINTS; PR00011; EGFLAMININ. DR ProDom; PD002082; Lam_N2; 1. DR SMART; SM00643; C345C; 1. DR SMART; SM00180; EGF_Lam; 3. DR SMART; SM00136; LamNT; 1. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01248; LAMININ_TYPE_EGF; 3. KW Glycoprotein; Extracellular matrix; Signal; Laminin EGF-like domain; KW Repeat. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 793 NETRIN-B. FT DOMAIN 24 403 LAMININ N-TERMINAL (DOMAIN VI). FT DOMAIN 405 497 LAMININ EGF-LIKE 1. FT DOMAIN 498 560 LAMININ EGF-LIKE 2. FT DOMAIN 561 610 LAMININ EGF-LIKE 3. FT DOMAIN 609 727 C345C (DOMAIN C). FT DISULFID 405 414 BY SIMILARITY. FT DISULFID 407 461 BY SIMILARITY. FT DISULFID 463 472 BY SIMILARITY. FT DISULFID 475 495 BY SIMILARITY. FT DISULFID 498 507 BY SIMILARITY. FT DISULFID 500 525 BY SIMILARITY. FT DISULFID 528 537 BY SIMILARITY. FT DISULFID 540 558 BY SIMILARITY. FT DISULFID 561 573 BY SIMILARITY. FT DISULFID 563 580 BY SIMILARITY. FT DISULFID 582 591 BY SIMILARITY. FT DISULFID 594 608 BY SIMILARITY. FT CARBOHYD 103 103 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 125 125 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 298 298 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 746 746 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 793 AA; 87133 MW; 7F6CEAD3B09B79F4 CRC64; MVRATGTRMG LLLPIILALA IGSSAAGISS NDPCYFEGKP RKCLPSFVNA AYGNPVQASS VCGAQQPERY CELLRDGNAG ECRSCEQQRY GPAALTDLNN PSNVTCWRSG AVNVPHDPDS APPDNVTLTL SLGKKYELTY ISLSFCPRSP RPDSLAIFKS SDFGQTWQPF QFYSSQCQKF YGRPDRAKIS KFNEQEARCI NSQHDTGGAA QRFAFNTLEG RPSANDLDSS LVLQDWVTAT DIRVVFHRLE LPPQLLKVKN ANAFSDEMGG SREEDEDDDA DLELDGEQDE YDYNLQDNDS ADAGYDEYEE PKKHLELDDD HLHLDYASDG ESVVKRQGKH KGSAYEKHYQ SKLAATTPPQ QPPKVTPPGK VTPPSTAAPS AAASAVTLPI SQHYAVSDFA VGGRCKCNGH ASECVATVSS GSGTALSDQD DGQDEDTPSA PSLANHFGRS TQMSAKLTMT CACKHNTAGP ECERCKPFYF DRPWGRATDN DANECKMCQC NGHARRCRFN LELYKLSGRV SGGVCYNCQH DTTGRYCHYC REGYYRDATK PPNHRKVCKR CDCHPVGSTG KTCNHLSGQC PCKEGVTGLT CNRCARGYQQ TRSHVAPCIK VPTNANMIQA ESAGGGGGGG TGDYKDGGGS QVEEMKKYCG KCKASPKKLN LNKFCMEDYA ILAKVIGHDR ASQDISTEKF SIERQNEIYK YEINIQTIFK RNPMSGTTSS LLGRGNMMLL VPRKSIECQC PKIKLNKSYL ILGRDSEAAP GYLAIGPSSV VLEWKDEWSL RMKRFQRRAR KCS // ID NEUR_DROME STANDARD; PRT; 754 AA. AC P29503; Q26306; Q27273; Q8INP6; Q8INP7; Q960M1; DT 01-APR-1993 (Rel. 25, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Neuralized protein. GN NEUR OR NEU OR CG11988. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Oregon-R; RX MEDLINE=92007742; PubMed=1717258; RA Boulianne G.L., de la Concha A., Campos-Ortega J.A., Jan L.Y., RA Jan Y.N.; RT "The Drosophila neurogenic gene neuralized encodes a novel protein RT and is expressed in precursors of larval and adult neurons."; RL EMBO J. 10:2975-2983(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=93285111; PubMed=8508767; RA Price B.D., Chang Z., Smith R., Bockheim S., Laughon A.; RT "The Drosophila neuralized gene encodes a C3HC4 zinc finger."; RL EMBO J. 12:2411-2418(1993). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2). RX MEDLINE=93285130; PubMed=8508781; RA Boulianne G.L., de la Concha A., Campos-Ortega J.A., Jan L.Y., RA Jan Y.N.; RT "The Drosophila neurogenic gene neuralized encodes a novel protein and RT is expressed in precursors of larval and adult neurons."; RL EMBO J. 12:2586-2586(1993). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE FROM N.A. (ISOFORMS 2 AND 3). RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN NEUROGENESIS. INTERACTS WITH OTHER CC NEUROGENIC PROTEINS IN THE SPECIFICATION OF THE NEUROBLAST CC VERSUS EPIDERMOBLAST CELL FATE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P29503-1; Sequence=Displayed; CC Name=2; CC IsoId=P29503-2; Sequence=VSP_008046; CC Name=3; CC IsoId=P29503-3; Sequence=VSP_008045; CC Name=4; CC IsoId=P29503-4; Sequence=VSP_008045, VSP_008046; CC -!- SIMILARITY: CONTAINS 2 NEUZ DOMAINS. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC FRAMESHIFTS IN POSITION 406; 518; 554 AND 709. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61617; CAA43806.1; ALT_FRAME. DR EMBL; S62583; AAB27147.1; -. DR EMBL; L12218; AAA28403.1; -. DR EMBL; S62597; AAB27151.1; -. DR EMBL; AE003681; AAF54330.1; -. DR EMBL; AE003681; AAF54326.2; -. DR EMBL; AE003681; AAN13406.1; -. DR EMBL; AE003681; AAN13407.1; -. DR EMBL; AY051987; AAK93411.1; -. DR EMBL; BT003772; AAO41451.1; -. DR PIR; S35371; S35371. DR PIR; S35503; S35503. DR FlyBase; FBgn0002932; neur. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR GO; GO:0007498; P:mesoderm development; IMP. DR GO; GO:0007423; P:sensory organ development; IMP. DR GO; GO:0016360; P:sensory organ precursor cell fate determina...; IMP. DR InterPro; IPR006573; Neu_Z. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00588; NEUZ; 2. DR SMART; SM00184; RING; 1. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW Neurogenesis; DNA-binding; Nuclear protein; Zinc-finger; Repeat; KW Alternative splicing. FT DOMAIN 104 225 NEUZ 1. FT DOMAIN 366 489 NEUZ 2. FT ZN_FING 701 742 RING-TYPE. FT DOMAIN 23 55 GLN-RICH. FT VARSPLIC 1 90 MGLSDIPANYMQGSHPHLTLHPQQQHHQNQQHLQHLQQMQQ FT LHNAMPTPAQQAAQVLAMESNELLMSTKDKLSSKKKMHLLK FT KIKKRFGL -> MGQSAGKI (in isoform 3 and FT isoform 4). FT /FTId=VSP_008045. FT VARSPLIC 672 672 Missing (in isoform 2 and isoform 4). FT /FTId=VSP_008046. FT CONFLICT 234 234 T -> S (IN REF. 1). FT CONFLICT 270 270 A -> V (IN REF. 3). FT CONFLICT 588 588 T -> N (IN REF. 3). FT CONFLICT 694 694 S -> R (IN REF. 3). SQ SEQUENCE 754 AA; 82325 MW; A2887404502D70BF CRC64; MGLSDIPANY MQGSHPHLTL HPQQQHHQNQ QHLQHLQQMQ QLHNAMPTPA QQAAQVLAME SNELLMSTKD KLSSKKKMHL LKKIKKRFGL VRRSPSSCPG PNNLPPLQFH SVHGDNIRIS RDGTLARRFE SFCRAITFSA RPVRINERIC VKFAEISNNW NGGIRFGFTS NDPVTLEGTL PKYACPDLTN RPGFWAKALH EQYCEKDNIL YYYVNGAGDV IYGINNEEKG VILTGIDTRS LLWTVIDIYG NCTGIEFLDS RIYMYQQQPA AIPMATVPAQ QQQMPQPAAN ASSALNSHHP HQQSRRSLPG HTAAIEHDLE RHVMPSLQSL HLAGNGGSVA SVEQAAIAHD LANGLPPLRY NANGRLIPVP FHNTKGRNVR LSQDRFVASR TESDFCQGYV FTARPIRIGE KLIVQVLKTE QMYVGALALG LTSCNPAMLQ PNDLPNDSDF LLDRPEYWVV SKDIAAAPQR GDEIAFFVAP NGEVSISKNN GPAVVVMHVD QSLQLWAFLD VYGSTQSLRM FRQQLPNMVA YPSQPQVNVN ASSSSACNAA STSRMLPMTE SMSSLNAGAT AKLLHHPSQL SVAQSTSTLA SAGGVNGSRM ISMPSNGDIL QIQPNGGGTV LVVNLPPASS SHDINGQLAA RPTATVTSSG VLAGACSSGT LISTTSSQYI EQPIANSTNN AANKWKDSLS DQQSTDSSAE CTICYENPID SVLYMCGHMC MCYDCAIEQW RGVGGGQCPL CRAVIRDVIR TYTT // ID NG1_DROME STANDARD; PRT; 107 AA. AC P23938; Q9V3M5; DT 01-MAR-1992 (Rel. 21, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE New-glue protein 1 precursor (NG-1) (Salivary glue protein homolog). GN NG1 OR NGP OR EG:96G10.5 OR CG10781. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Salivary gland; RX MEDLINE=91016924; PubMed=2120680; RA Furia M., Digilio F.A., Artiaco D., Giordano E., Polito L.C.; RT "A new gene nested within the dunce genetic unit of Drosophila RT melanogaster."; RL Nucleic Acids Res. 18:5837-5841(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: SALIVARY GLAND SPECIFIC. CC -!- DEVELOPMENTAL STAGE: ABUNDANT ONLY DURING THE THIRD LARVAL STAGE. CC -!- SIMILARITY: STRONG TO NG-2, ALSO TO SGS-3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52118; CAA36363.1; -. DR EMBL; AE003427; AAF45856.1; -. DR EMBL; AL024484; CAA19667.1; -. DR PIR; S12607; S12607. DR FlyBase; FBgn0002933; ng1. KW Repeat; Signal. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 107 NEW-GLUE PROTEIN 1. FT DOMAIN 26 63 THR-RICH. FT DOMAIN 31 62 4 X 8 AA TANDEM REPEATS OF T-S-A-S-A-T- FT T-T. FT REPEAT 31 38 1. FT REPEAT 39 46 2. FT REPEAT 47 54 3. FT REPEAT 55 62 4. FT CONFLICT 24 24 A -> G (IN REF. 1). SQ SEQUENCE 107 AA; 11371 MW; 9EFC129DDA17FD59 CRC64; MKITVVLVLL ATFLGCVMIH ESEASTTTTS TSASATTTTS ASATTTTSAS ATTTTSASAT TTTASPSSSS KKKTVTHYKR KVKRPKKVRK ITRRRGLRSR NGRRSDE // ID NG2_DROME STANDARD; PRT; 112 AA. AC P40139; O76916; Q9V3M0; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE New-glue protein 2 precursor (NG-2). GN NG2 OR EG:96G10.4 OR CG14266. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Salivary gland; RX MEDLINE=93287124; PubMed=8510164; RA Furia M., D'Avino P.P., Crispi S., Artiaco D., Polito L.C.; RT "Dense cluster of genes is located at the ecdysone-regulated 3C puff RT of Drosophila melanogaster."; RL J. Mol. Biol. 231:531-538(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: SALIVARY GLAND SPECIFIC. CC -!- DEVELOPMENTAL STAGE: ABUNDANT ONLY DURING THE THIRD LARVAL STAGE. CC -!- SIMILARITY: STRONG TO NG-1, ALSO TO SGS-3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61945; CAA43951.1; -. DR EMBL; AE003426; AAF45854.1; -. DR EMBL; AL024484; CAA19671.1; -. DR PIR; S33822; S33822. DR FlyBase; FBgn0010294; ng2. KW Repeat; Signal. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 112 NEW-GLUE PROTEIN 2. FT DOMAIN 26 63 THR-RICH. FT DOMAIN 31 62 4 X 8 AA TANDEM REPEATS OF T-S-A-S-A-T- FT T-T. FT REPEAT 31 38 1. FT REPEAT 39 46 2. FT REPEAT 47 54 3. FT REPEAT 55 62 4. FT CONFLICT 14 14 L -> F (IN REF. 1). FT CONFLICT 21 21 E -> Q (IN REF. 3; CAA19671). SQ SEQUENCE 112 AA; 11985 MW; A30FFA279FC1B2B2 CRC64; MKITVVLVLL ATFLGCVMIH ESEASTTTTS TSASATTTTS ASATTTTSAS ATTTTSASAT TTTASPSSSS KKKTVTHYKR KVKRPKKVRK ITRRRGLRSR NGRSSRNRRS EE // ID NG3_DROME STANDARD; PRT; 165 AA. AC P40140; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE New-glue protein 3 precursor (NG-3). GN NG3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Salivary gland; RX MEDLINE=93287124; PubMed=8510164; RA Furia M., D'Avino P.P., Crispi S., Artiaco D., Polito L.C.; RT "Dense cluster of genes is located at the ecdysone-regulated 3C puff RT of Drosophila melanogaster."; RL J. Mol. Biol. 231:531-538(1993). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: SALIVARY GLAND SPECIFIC. CC -!- DEVELOPMENTAL STAGE: ABUNDANT DURING THE THIRD LARVAL STAGE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61945; CAA43952.1; -. DR PIR; S33823; S33823. DR FlyBase; FBgn0010295; ng3. KW Signal. FT SIGNAL 1 19 OR 26 (POTENTIAL). FT CHAIN 20 165 NEW-GLUE PROTEIN 3. SQ SEQUENCE 165 AA; 17482 MW; 0ED75C20669AC0E5 CRC64; MRYSCVLLLL ATVACLLIPQ TGGSTATQPQ LLLRLPPPLP PRPRQPLRRI QLLPQRLPQP LRPPPQRVKR RRGRITIHVM CIGQSGYDIS IGTRPTTTKA LPIAPAHAAV VVAAAVAAVA AVAAPVAAVV TVASAAGEPE VPDACLSDHI SYNKPTDLIV TPLKM // ID NG4_DROME STANDARD; PRT; 57 AA. AC P40141; Q9W4T5; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE New-glue protein 4 precursor (NG-4). GN NG4 OR EG:96G10.2 OR CG10789. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93287124; PubMed=8510164; RA Furia M., D'Avino P.P., Crispi S., Artiaco D., Polito L.C.; RT "Dense cluster of genes is located at the ecdysone-regulated 3C puff RT of Drosophila melanogaster."; RL J. Mol. Biol. 231:531-538(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67501; CAA47835.1; -. DR EMBL; AL024484; CAA19672.1; -. DR EMBL; AE003427; AAF45857.1; -. DR PIR; S33824; S33824. DR FlyBase; FBgn0010296; ng4. KW Signal. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 57 NEW-GLUE PROTEIN 4. SQ SEQUENCE 57 AA; 7100 MW; 9D774610E1DBBFD5 CRC64; MEWKLLLIVL PWLLVCKIFY KVEDFTEPDV AYQSIDYHPE DYIDSFTDFQ KHDYFQY // ID NHPX_DROME STANDARD; PRT; 127 AA. AC Q9U3Z7; Q9VL98; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NHP2-like protein (Hoi-polloi protein). GN HOIP OR CG3949. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Prokopenko S.N., He Y., Lu Y., Bellen H.J.; RT "Mutations affecting the development of the peripheral nervous system RT in Drosophila: A molecular screen for novel genes."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE L7AE FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF208396; AAF20209.1; -. DR EMBL; AE003625; AAF52798.2; -. DR HSSP; P55769; 1E7K. DR FlyBase; FBgn0015393; hoip. DR GO; GO:0007399; P:neurogenesis; IMP. DR InterPro; IPR004038; Ribosomal_L7A. DR InterPro; IPR004037; Ribosomal_L7Ae. DR Pfam; PF01248; Ribosomal_L7Ae; 1. DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1. KW Nuclear protein. SQ SEQUENCE 127 AA; 13883 MW; E3CA6F5389A1F0A4 CRC64; MTEEVNPKAF PLADAQLTAK IMNLLQQALN YNQLRKGANE ATKTLNRGLA DIVVLAGDAE PIEILLHLPL LCEDKNVPYV FVRSKQALGR ACGVSRPIVA CSVTTNEGSQ LKSQITSIQQ EIERLLV // ID NICA_DROME STANDARD; PRT; 695 AA. AC Q9VC27; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nicastrin homolog precursor. GN NCT OR NCSTN OR CG7012. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20445163; PubMed=10993067; RA Yu G., Nishimura M., Arawaka S., Levitan D., Zhang L., Tandon A., RA Song Y.-Q., Rogaeva E., Chen F., Kawarai T., Supala A., Levesque L., RA Yu H., Yang D.S., Holmes E., Milman P., Liang Y., Zhang D.M., Xu D.H., RA Sato C., Rogaev E., Smith M., Janus C., Zhang Y., Aebersold R., RA Farrer L.S., Sorbi S., Bruni A., Fraser P.E., St George-Hyslop P.H.; RT "Nicastrin modulates presenilin-mediated notch/glp-1 signal RT transduction and betaAPP processing."; RL Nature 407:48-54(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION IN NOTCH SIGNALING. RX MEDLINE=21640648; PubMed=11781576; RA Chung H.-M., Struhl G.; RT "Nicastrin is required for Presenilin-mediated transmembrane cleavage RT in Drosophila."; RL Nat. Cell Biol. 3:1129-1132(2001). RN [6] RP FUNCTION IN THE GAMMA-SECRETASE COMPLEX. RX MEDLINE=21642113; PubMed=11782315; RA Hu Y., Ye Y., Fortini M.E.; RT "Nicastrin is required for gamma-secretase cleavage of the Drosophila RT Notch receptor."; RL Dev. Cell 2:69-78(2002). RN [7] RP FUNCTION IN NOTCH SIGNALING. RX MEDLINE=21642114; PubMed=11782316; RA Lopez-Schier H., St Johnston D.; RT "Drosophila nicastrin is essential for the intramembranous cleavage RT of notch."; RL Dev. Cell 2:79-89(2002). RN [8] RP FUNCTION IN THE GAMMA-SECRETASE COMPLEX, AND INTERACTION WITH PSN; RP PEN-2 AND APH-1. RX MEDLINE=22547312; PubMed=12660785; RA Takasugi N., Tomita T., Hayashi I., Tsuruoka M., Niimura M., RA Takahashi Y., Thinakaran G., Iwatsubo T.; RT "The role of presenilin cofactors in the gamma-secretase complex."; RL Nature 422:438-441(2003). CC -!- FUNCTION: ESSENTIAL SUBUNIT OF THE GAMMA-SECRETASE COMPLEX, AN CC ENDOPROTEASE COMPLEX THAT CATALYZES THE INTRAMEMBRANE CLEAVAGE OF CC INTEGRAL MEMBRANE PROTEINS SUCH AS NOTCH. IT PROBABLY REPRESENTS A CC STABILIZING COFACTOR REQUIRED FOR THE ASSEMBLY OF THE GAMMA- CC SECRETASE COMPLEX. CC -!- SUBUNIT: COMPONENT OF THE GAMMA-SECRETASE COMPLEX, A COMPLEX CC COMPOSED OF A PRESENILIN (PSN) HOMODIMER, NICASTRIN (NCT), APH-1 CC AND PEN-2. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE NICASTRIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF240470; AAG11414.1; -. DR EMBL; AE003749; AAF56349.2; -. DR EMBL; BT003245; AAO25002.1; ALT_INIT. DR FlyBase; FBgn0039234; nct. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; IMP. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP. DR GO; GO:0007220; P:N receptor processing; IGI. DR InterPro; IPR008710; Nicastrin. DR Pfam; PF05450; Nicastrin; 1. KW Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 695 NICASTRIN HOMOLOG. FT DOMAIN 23 654 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 655 675 POTENTIAL. FT DOMAIN 676 695 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 45 45 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 108 108 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 116 116 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 138 138 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 381 381 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 461 461 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 489 489 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 585 585 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 609 609 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 244 257 YATLYPRKPAIENN -> SPPCTPESQQSETT (IN REF. FT 1). FT CONFLICT 448 448 I -> T (IN REF. 1). SQ SEQUENCE 695 AA; 77993 MW; C9D9D0C05CDC772B CRC64; MEMRLNAASI WLLILSYGAT IAQGERTRDK MYEPIGGASC FRRLNGTHQT GCSSTYSGSV GVLHLINVEA DLEFLLSSPP SPPYAPMIPP HLFTRNNLMR LKEAGPKNIS VVLLINRTNQ MKQFSHELNC PNQYSGLNST SETCDASNPA KNWNPWGTGL LHEDFPFPIY YIADLDQVTK LEKCFQDFNN HNYETHALRS LCAVEVKSFM SAAVNTEVCM RRTNFINNLG GSKYCDPLEG RNVYATLYPR KPAIENNLET VHTNEKFILV TCRLDTTTMF DGVGLGAMDS LMGFAVFTHV AYLLKQLLPP QSKDLHNVLF VTFNGESYDY IGSQRFVYDM EKLQFPTEST GTPPIAFDNI DFMLDIGTLD DISNIKLHAL NGTTLAQQIL ERLNNYAKSP RYGFNLNIQS EMSAHLPPTS AQSFLRRDPN FNALILNARP TNKYYHSIYD DADNVDFTYA NTSKDFTQLT EVNDFKSLNP DSLQMKVRNV SSIVAMALYQ TITGKEYTGT KVANPLMADE FLYCFLQSAD CPLFKAASYP GSQLTNLPPM RYISVLGGSQ ESSGYTYRLL GYLLSQLQPD IHRDNCTDLP LHYFAGFNNI GECRLTTQNY SHALSPAFLI DGYDWSSGMY STWTESTWSQ FSARIFLRPS NVHQVTTLSV GIVVLIISFC LVYIISSRSE VLFEDLPASN AALFG // ID NINC_DROME STANDARD; PRT; 1501 AA. AC P10676; P10677; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Neither inactivation nor afterpotential protein C (EC 2.7.1.37). GN NINAC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND ALTERNATIVE SPLICING. RX MEDLINE=88151067; PubMed=2449973; RA Montell C., Rubin G.M.; RT "The Drosophila ninaC locus encodes two photoreceptor cell specific RT proteins with domains homologous to protein kinases and the myosin RT heavy chain head."; RL Cell 52:757-772(1988). CC -!- FUNCTION: REQUIRED FOR PHOTORECEPTOR CELL FUNCTION. THE NINAC CC PROTEINS JOIN PUTATIVE SERINE/THREONINE-PROTEIN KINASE AND MYOSIN CC ACTIVITIES. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- SUBCELLULAR LOCATION: CYTOSKELETON. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P10676-1; Sequence=Displayed; CC Name=Short; CC IsoId=P10676-2; Sequence=VSP_004940, VSP_004941; CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE SER/THR CC FAMILY OF PROTEIN KINASES. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE MYOSIN CC SUPERFAMILY. CC -!- SIMILARITY: CONTAINS 1 IQ DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03131; AAA28718.1; -. DR EMBL; J03131; AAA28719.1; -. DR EMBL; M20230; AAA28721.1; -. DR EMBL; M20231; AAA28720.1; -. DR PIR; A29813; A29813. DR PIR; B29813; B29813. DR HSSP; P08799; 1MND. DR FlyBase; FBgn0002938; ninaC. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0042385; C:myosin III; NAS. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0005516; F:calmodulin binding; IMP. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA. DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IMP. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; IMP. DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP. DR GO; GO:0007603; P:phototransduction, visible light; IMP. DR GO; GO:0008104; P:protein localization; IMP. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR001609; myosin_head. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00612; IQ; 2. DR Pfam; PF00063; myosin_head; 1. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR ProDom; PD000355; myosin_head; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00015; IQ; 2. DR SMART; SM00242; MYSc; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS50096; IQ; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Cytoskeleton; Actin-binding; ATP-binding; Myosin; Transferase; Vision; KW Serine/threonine-protein kinase; Alternative splicing. FT DOMAIN 16 282 PROTEIN KINASE. FT DOMAIN 335 1035 MYOSIN. FT DOMAIN 1036 1065 IQ. FT DOMAIN 1066 1501 NON ALPHA-HELICAL, C-TERMINAL DOMAIN. FT NP_BIND 22 30 ATP (BY SIMILARITY). FT BINDING 45 45 ATP (BY SIMILARITY). FT ACT_SITE 145 145 BY SIMILARITY. FT DOMAIN 913 934 ACTIN-BINDING (BY SIMILARITY). FT VARSPLIC 1082 1135 AFRGFRDPVRLPPLVNEKSGQLNENTADFIRPFAKKWREKS FT IFQVLLHYRAARF -> GKKTQVDRLREYDEEHIDISETPS FT EAEEMFLEARMDEALAAVRIAKIEQASAEE (in FT isoform Short). FT /FTId=VSP_004940. FT VARSPLIC 1136 1501 Missing (in isoform Short). FT /FTId=VSP_004941. FT CONFLICT 253 253 K -> Q (IN REF. 1; AAA28720/AAA28721). FT CONFLICT 1089 1089 P -> R (IN REF. 1; AAA28721). SQ SEQUENCE 1501 AA; 174269 MW; D167EABC82A3933A CRC64; MMYLPYAQLP DPTDKFEIYE EIAQGVNAKV FRAKELDNDR IVALKIQHYD EEHQVSIEEE YRTLRDYCDH PNLPEFYGVY KLSKPNGPDE IWFVMEYCAG GTAVDMVNKL LKLDRRMREE HIAYIIRETC RAAIELNRNH VLHRDIRGDN ILLTKNGRVK LCDFGLSRQV DSTLGKRGTC IGSPCWMAPE VVSAMESREP DITVRADVWA LGITTIELAD GKPPFADMHP TRAMFQIIRN PPPTLMRPTN WSKQINDFIS ESLEKNAENR PMMVEMVEHP FLTELIENED EMRSDIAEML ELSRDVKTLY KEPELFVDRG YVKRFDEKPE KMYPEDLAAL ENPVDENIIE SLRHRILMGE SYSFIGDILL SLNSNEIKQE FPQEFHAKYR FKSRSENQPH IFSVADIAYQ DMLHHKEPQH IVLSGESYSG KSTNARLLIK HLCYLGDGNR GATGRVESSI KAILMLVNAG TPVNNDSTRC VLQYCLTFGK TGKMSGAVFN MYMLEKLRVA TTDGTQHNFH IFYYFYDFIN QQNQLKEYNL KADRNYRYLR VPPEVPPSKL KYRRDDPEGN VERYREFENI LRDIDFNHKQ LETVRKVLAA ILNIGNIRFR QNGKYAEVEN TDIVSRIAEL LRVDEKKFMW SLTNFIMVKG GIAERRQYTT EEARDARDAV ASTLYSRLVD FIINRINMNM SFPRAVFGDT NAIIIHDMFG FECFNRNGLE QLMINTLNEQ MQYHYNQRIF ISEMLEMEAE DIDTINLNFY DNKTALDNLL TKPDGLFYII DDASRSCQDQ NLIMDRVSEK HSQFVKKHTA TEISVAHYTG RIIYDTRAFT DINRDFVPPE MIETFRSSLD ESIMLMFTNQ LTKAGNLTMP FEAVQHKDES ERKSYALNTL SAGCISQVNN LRTLAANFRF TCLTLLKMLS QNANLGVHFV RCIRADLEYK PRSFHSDVVQ QQMKALGVLD TVIARQKGFS SRLPFDEFLR RYQFLAFDFD EPVEMTKDNC RLLFLRLKME GWALGKTKVF LRYYNDEFLA RLYELQVKKV IKVQSMMRAL LARKRVKGGK VFKLGKKGPE HHDVAASKIQ KAFRGFRDPV RLPPLVNEKS GQLNENTADF IRPFAKKWRE KSIFQVLLHY RAARFQDFVN LSQQVHIYNQ RMVAGLNKCT RAVPFERINM REVNSSQLGP LPVPIKKMPF RLDQIPFYDT QYMVDPANSI SRQAFPNQLL TQHMEDDEPW DSPLQRNPSM TSCALTYNAY KKEQACQTNW DRMGESDNIY NQGYFRDPQQ LRRNQMQMNM NAYNNAYNSY NSNYNNQNWG EHRSGSRRNS LKGYAAPPPP PPPMPSSNYY RNNPNQQQRN YQQRSSYPPS DPVRELQNMA RNEGDNSEDP PFNFKAMLRK TNYPRGSETN TYDFNNRRGS DSGDQHTFQP PKLRSTGRRY QDDEGYNSSS GNYGVSRKFG QQQRAPTLRQ SPASVGRSFE DSNARSFEEA GSYVEEEIAP GITLSGYAVD I // ID NLFB_DROME STANDARD; PRT; 594 AA. AC Q9Y113; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Negative elongation factor B homolog. GN CG12152/CG32721. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RA Rubin G.M., Wan K.H., Harvey D., Lewis S.E., Brokstein P., Tsang G., RA Agbayani A., Arcaina T.T., Baxter E., Blazej R.G., Butenhoff C., RA Champe M., Chavez C., Chew M., Doyle C.M., Farfan D.E., Frise E., RA Galle R., George R.A., Harris N.L., Hoskins R.A., Evans-Holm M., RA Houston K.A., Hummasti S.R., Kim E., Li P., Moshrefi M., Pacleb J.M., RA Park S., Sequeira A., Sethi H., Snir E., Svirskas R.R., Weinburg T., RA Celniker S.E.; RT "Full length Drosophila melanogaster cDNA sequence."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: POTENTIAL COMPONENT OF THE NELF COMPLEX, A COMPLEX THAT CC NEGATIVELY REGULATES THE ELONGATION OF TRANSCRIPTION BY RNA CC POLYMERASE II (BY SIMILARITY). CC -!- SUBUNIT: MAY BELONG TO THE NELF COMPLEX (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE NELF-B FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003441; AAF46268.1; -. DR EMBL; AF145659; AAD38634.1; -. DR FlyBase; FBgn0027553; BcDNA:GH10333. KW Transcription regulation; Repressor; Nuclear protein. SQ SEQUENCE 594 AA; 67934 MW; D5A87283888A97F4 CRC64; MIMSTPAKNN NGTGLEDVNI PGQAYLREAL TSCTDPLKAI ESFQLENGVL LPSLRPMLPL LDLHGVRRLD FHTSLMEELR DKLIAHINEM GQKEPRERDK KLKELLVKSF PVVRVKSLRP VVMAILRNTQ HIDDKYLKIL VRDRELYADT DTEVKRQIWR DNQSLFGDEV SPLLSQYIRE KEHILFDHTN LNNLFFHPTP KVRRQGEVVQ KLANMIGTSV KLYDMVLQFL RTLFLRTRNV HYCTLRAELL MALHDLEVQE IISIDPCHKF TWCLDACIRE KNVDIKRSRE LQGFLDNIKR GQEQVLGDLS MTLCDPYAIN FLATSAIKIL HHLINNEGMP RDNQILILLL RMLALGLSAW VMIDSQDFKE PKLDCQVVTK FLPALMSLMV DDQCRSLHAK LPPDERESAL TTIEHSGPAP DAVEAYIQES SVASILAMYY TLHTARLKDR VGVLRVLAIL SACKDDRAYE DPFLHSLIAL LIPMSEEFAT EDFCTTLFDE FIFAGLTREN VTSRHMLKLL WYVHNKLPAG RLATLMKAMQ PTTAHNEHIH KLYEILQERI GTGAAETPVI EAPPMEFDSP LKSVPTPGPH YNVQ // ID NLFD_DROME STANDARD; PRT; 578 AA. AC Q24134; Q24553; Q9V418; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Negative elongation factor D. GN TH1 OR NELF-D OR CG9984. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20483332; PubMed=11030415; RA Bonthron D.T., Hayward B.E., Moran V., Strain L.; RT "Characterization of TH1 and CTSZ, two non-imprinted genes downstream RT of GNAS1 in chromosome 20q13."; RL Hum. Genet. 107:165-175(2000). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RA Oliveri D.R., Banga S.S., Boyd J.B.; RT "Characterization of a prominent transcript in Drosophila embryos."; RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 1-393 FROM N.A. RX MEDLINE=95401271; PubMed=7671309; RA Hari K.L., Santerre A., Sekelsky J.J., McKim K.S., Boyd J.B., RA Hawley R.S.; RT "The mei-41 gene of D. melanogaster is a structural and functional RT homolog of the human ataxia telangiectasia gene."; RL Cell 82:815-821(1995). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NELF-E. RX MEDLINE=22666610; PubMed=12782658; RA Wu C.-H., Yamaguchi Y., Benjamin L.R., Horvat-Gordon M., Washinsky J., RA Enerly E., Larsson J., Lambertsson A., Handa H., Gilmour D.; RT "NELF and DSIF cause promoter proximal pausing on the hsp70 promoter RT in Drosophila."; RL Genes Dev. 17:1402-1414(2003). CC -!- FUNCTION: ESSENTIAL COMPONENT OF THE NELF COMPLEX, A COMPLEX THAT CC NEGATIVELY REGULATES THE ELONGATION OF TRANSCRIPTION BY RNA CC POLYMERASE II BY RNA POLYMERASE II. THE NELF COMPLEX, WHICH ACTS CC VIA AN ASSOCIATION WITH THE DSIF COMPLEX, CAUSES TRANSCRIPTIONAL CC PAUSING. CC -!- SUBUNIT: COMPONENT OF THE NELF COMPLEX, WHICH IS AT LEAST COMPOSED CC OF TH1/NELF-D AND NELF-E (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR; ASSOCIATES WITH POLYTENE CC CHROMOSOMES. ASSOCIATES WITH THE HSP70 PROMOTER WHEN IT IS CC INACTIVE, BUT NOT WHEN IT IS ACTIVATED. THE NELF COMPLEX POSSIBLY CC DISSOCIATES FROM CHROMATIN FOLLOWING PHOSPHORYLATION OF RNA CC POLYMERASE II. CC -!- SIMILARITY: BELONGS TO THE NELF-D FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO MULTIPLE CC FRAMESHIFTS. CC -!- CAUTION: REF.5 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ238377; CAB64258.1; -. DR EMBL; AJ238378; CAB64259.1; -. DR EMBL; L01790; AAA28932.1; ALT_FRAME. DR EMBL; AE003502; AAF48603.1; -. DR EMBL; AY051957; AAK93381.1; -. DR EMBL; U34925; AAC46880.1; ALT_SEQ. DR PIR; T13287; T13287. DR FlyBase; FBgn0010416; TH1. DR InterPro; IPR006942; TH1. DR Pfam; PF04858; TH1; 1. KW Transcription regulation; Repressor; Nuclear protein. SQ SEQUENCE 578 AA; 65780 MW; 2949EE378AEC19BE CRC64; MEVEYDDSGW QGRAKGQTNP EETLEDNPQK TIQECLEKFL TPDYIMEPGI FTQLKRYFQS GGSPEEVISM LSENYKAVAQ MANLLAEWLI LAGVKVTEVQ AMVENHLKEM ILKSFDPKKA DTIFTEEGET PDWLTEMIDH YTWRSLIYRL AEEYPDCLML NFTIKLISDA GFQSEITSIS TAAQQIEVFS RVLKTSIVKF LNNPDDVHGA IQECARMVCH GQHTYVYSQV LIQVLSQEQK GGFNMKRLSQ EIIKYALQNN QNVTPITMAL NGSAVYPQAC QALTSMLTRN TLNPADITVL FRNYSGSDPP PIDLIRNPQF LELLVDALFR SGVKINPEHK PKYMFLLAYA SAVIDQPAKK RPMTERMLNK EELKSTIQAI EKAHTICNVD QGSTELIAEL QTLYNCIKYP VVGVGVIRWI ENVVMEPSYF KLSTDSCPTH LAVLDEVAAV HPTLQQQILF LLIRLFESKQ DELEILVQLE MKKMILDRMV NLLTRGCVVP VLRYIKQCCA IEDTDISLIR YFVTEVLETI THPYSPEFVQ LFLPMVENEE ITGTMRGEGD NDPVSEFIVH CKAHYTTV // ID NLFE_DROME STANDARD; PRT; 280 AA. AC P92204; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Negative elongation factor E. GN NELF-E OR ANON-66DA OR CG5994. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97379971; PubMed=9236770; RA Saeboe-Larssen S., Urbanczyk Mohebi B., Lambertsson A.; RT "The Drosophila ribosomal protein L14-encoding gene, identified by a RT novel Minute mutation in a dense cluster of previously undescribed RT genes in cytogenetic region 66D."; RL Mol. Gen. Genet. 255:141-151(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NELF-E. RX MEDLINE=22666610; PubMed=12782658; RA Wu C.-H., Yamaguchi Y., Benjamin L.R., Horvat-Gordon M., Washinsky J., RA Enerly E., Larsson J., Lambertsson A., Handa H., Gilmour D.; RT "NELF and DSIF cause promoter proximal pausing on the hsp70 promoter RT in Drosophila."; RL Genes Dev. 17:1402-1414(2003). CC -!- FUNCTION: ESSENTIAL COMPONENT OF THE NELF COMPLEX, A COMPLEX THAT CC NEGATIVELY REGULATES THE ELONGATION OF TRANSCRIPTION BY RNA CC POLYMERASE II BY RNA POLYMERASE II. THE NELF COMPLEX, WHICH ACTS CC VIA AN ASSOCIATION WITH THE DSIF COMPLEX, CAUSES TRANSCRIPTIONAL CC PAUSING. CC -!- SUBUNIT: COMPONENT OF THE NELF COMPLEX, WHICH IS AT LEAST COMPOSED CC OF TH1/NELF-D AND NELF-E (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR; ASSOCIATES WITH POLYTENE CC CHROMOSOMES. ASSOCIATES WITH THE HSP70 PROMOTER WHEN IT IS CC INACTIVE, BUT NOT WHEN IT IS ACTIVATED. THE NELF COMPLEX POSSIBLY CC DISSOCIATES FROM CHROMATIN FOLLOWING PHOSPHORYLATION OF RNA CC POLYMERASE II. CC -!- SIMILARITY: BELONGS TO THE NELF-E FAMILY. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y10015; CAA71120.1; -. DR EMBL; Y10016; CAA71123.1; -. DR EMBL; AE003555; AAF50394.1; -. DR EMBL; AY071061; AAL48683.1; -. DR FlyBase; FBgn0017430; Nelf-E. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Transcription regulation; Repressor; Nuclear protein; RNA-binding. FT DOMAIN 166 236 RNA-BINDING (RRM). SQ SEQUENCE 280 AA; 31811 MW; 9F1F351727D53C47 CRC64; MVYIHFPNNL TEEEQMLQAK YQKLKKKKKA LQAHKAPKPE PESSLTLKRP TDARDAREVA RKLIKSGAIP AIQKQTKQDQ TSFKRPKGQE RAKRSTSETT VASYQPFSST QNDVAQETII SEIIKEEPRR QNLYQHFATE RDREERGMPE KVPMDTAQPE KPRAGNTIFV SGNKVTEDFL KKTFNDYGTI VNVSMEIEKS RGFVSFAKPE SADRAIAEIH GKNVNGINLQ VQLARRQPQI EPINDASSSA VWSSIAASKS QKGSHKDHRE MVQYDEDFLL // ID NLP_DROME STANDARD; PRT; 152 AA. AC Q27415; Q24565; Q9VAC3; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nucleoplasmin-like protein (dNLP) (Chromatin decondensation protein DE 1). GN NLP OR CRP1 OR CG7917. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1), AND SEQUENCE OF 116-148. RX MEDLINE=97242931; PubMed=9087911; RA Crevel G.L., Huikeshoven H., Cotterill S., Simon M., Wall J., RA Philpott A., Laskey R.A., McConnell M., Fisher P.A., Berrios M.; RT "Molecular and cellular characterization of CRP1, a Drosophila RT chromatin decondensation protein."; RL J. Struct. Biol. 118:9-22(1997). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), AND PARTIAL SEQUENCE. RX MEDLINE=96394681; PubMed=8798787; RA Ito T., Tyler J.K., Bulger M., Kobayashi R., Kadonaga J.T.; RT "ATP-facilitated chromatin assembly with a nucleoplasmin-like protein RT from Drosophila melanogaster."; RL J. Biol. Chem. 271:25041-25048(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS TO CORE HISTONES AND FUNCTIONS IN THE ATP- CC FACILITATED ASSEMBLY OF APPROXIMATELY REGULARLY SPACED NUCLEOSOMAL CC ARRAYS. MAY PARTICIPATE IN PARALLEL WITH OTHER HISTONE-BINDING CC PROTEINS SUCH AS NAP-1. CC -!- FUNCTION: ISOFORM 2 IS INACTIVE FOR CHROMATIN ASSEMBLY. IN VITRO CC IT APPEARS TO FORM A HIGH MOLECULAR MASS AGGREGATE WITH THE CORE CC HISTONES. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long, DNLP; CC IsoId=Q27415-1; Sequence=Displayed; CC Name=2; Synonyms=Short, DNLP-S; CC IsoId=Q27415-2; Sequence=VSP_003618; CC -!- DEVELOPMENTAL STAGE: PRESENT THROUGHOUT DEVELOPMENT. HIGHEST CC LEVELS ARE FOUND DURING OOGENESIS AND IN EARLY EMBRYOS. CC -!- SIMILARITY: BELONGS TO THE NUCLEOPLASMIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99293; CAA67679.1; -. DR EMBL; U59498; AAC47295.1; -. DR EMBL; U59497; AAC47294.1; -. DR EMBL; AE003772; AAF56988.1; -. DR PDB; 1NLQ; 01-MAR-03. DR FlyBase; FBgn0016685; Nlp. DR InterPro; IPR004301; Nucleoplasmin. DR Pfam; PF03066; Nucleoplasmin; 1. KW Nuclear protein; Alternative splicing; 3D-structure. FT DOMAIN 106 129 ASP/GLU-RICH (ACIDIC). FT VARSPLIC 1 32 MAEESFYGVTLTAESDSVTWDVDEDYARGQKL -> M (in FT isoform 2). FT /FTId=VSP_003618. SQ SEQUENCE 152 AA; 16996 MW; 324CF99C17AF3CDE CRC64; MAEESFYGVT LTAESDSVTW DVDEDYARGQ KLVIKQILLG AEAKENEFNV VEVNTPKDSV QIPIAVLKAG ETRAVNPDVE FYESKVTFKL IKGSGPVYIH GHNIKDDVEV VDMEEDDEED DVAEDEEDEH PKKRAKIENA ADGKNAKNNK KK // ID NMT_DROME STANDARD; PRT; 387 AA. AC O61613; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (Peptide N- DE myristoyltransferase) (Myristoyl-CoA:protein N-myristoyltransferase) DE (NMT) (dNMT). GN NMT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97196956; PubMed=9044045; RA Ntwasa M., Egerton M., Gay N.J.; RT "Sequence and expression of Drosophila myristoyl-CoA: protein N- RT myristoyl transferase: evidence for proteolytic processing and RT membrane localisation."; RL J. Cell Sci. 110:149-156(1997). CC -!- FUNCTION: ADDS A MYRISTOYL GROUP TO THE N-TERMINAL GLYCINE RESIDUE CC OF CERTAIN CELLULAR PROTEINS. CC -!- CATALYTIC ACTIVITY: TETRADECANOYL-COA + GLYCYL-PEPTIDE = COA + N- CC TETRADECANOYLGLYCYL-PEPTIDE. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- SIMILARITY: BELONGS TO THE NMT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF053725; AAC08578.1; -. DR HSSP; P30418; 1NMT. DR FlyBase; FBgn0020392; Nmt. DR InterPro; IPR000903; Nmt. DR Pfam; PF01233; NMT; 1. DR Pfam; PF02799; NMT_C; 1. DR PROSITE; PS00975; NMT_1; 1. DR PROSITE; PS00976; NMT_2; 1. KW Transferase; Acyltransferase; Membrane. SQ SEQUENCE 387 AA; 45121 MW; 0BF518F24CECEC0C CRC64; MASTRQMAKK FAFWSTQPVT KLDEQVTTNE CIEPNKEISE IRALPYTLPG FKWVTLDLND ANDLKELYTL LNENYVEDDD AMFRFDYQPE FLKWSLQPPG WKRDWHVGVR VEKSGKLVGF ISAIPSKLKS YDKVLKVVDI NFLCVHKKLR SKRVAPVLIR EISRRVNLTG IFQAAYTAGV VLPTPVATCR YWHRSLNPKK LVDVRFSHLA RNMTMQRTMK LYKLPDQPKT KGYRRITAKD MDKAHKLLED YLKRFQLSPV FSKEEFRHWF TPKEGIIDCF VVADEKGNIT DLTSYYCLPS SVMHHPVHKT VRAAYSFYNV STKTPWLDLM GDALISARNV QMDVYNALDL MENKKYFAPL KFGAGDGNLQ YYLYNWRCPS MQPERLL // ID NNOS_DROME STANDARD; PRT; 401 AA. AC P25724; Q9VDZ6; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nanos protein. GN NOS OR CG5637. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91347366; PubMed=1908748; RA Wang C.I., Lehmann R.; RT "Nanos is the localized posterior determinant in Drosophila."; RL Cell 66:637-647(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MATERNAL FACTOR LOCALIZED TO THE POSTERIOR POLE OF THE CC EGG CELL INVOLVED IN SEGMENTAL PATTERN. NANOS PROTEIN ACTS AT A CC DISTANCE TO DIRECT ABDOMEN DEVELOPMENT. NANOS IS THE RESCUING CC FACTOR FOR THE ABDOMINAL DEFECT OF POSTERIOR GROUP MUTANTS. THE CC OTHER POSTERIOR GROUP GENES ARE NOT REQUIRED FOR NANOS FUNCTION CC BUT RATHER PLAY A ROLE IN LOCALIZATION OR DISTRIBUTION OF NANOS CC PROTEIN. NANOS MAY REGULATE THE TRANSLATION OF HB AND BCD RNAS. CC -!- TISSUE SPECIFICITY: POLE PLASM AND POLE CELLS. CC -!- DEVELOPMENTAL STAGE: DURING OOGENESIS AND EARLY STAGES OF CC EMBRYOGENESIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M72421; AAA28715.1; -. DR EMBL; AE003725; AAF55641.1; -. DR PIR; A40042; A40042. DR FlyBase; FBgn0002962; nos. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR GO; GO:0007314; P:oocyte anterior/posterior axis determination; NAS. DR InterPro; IPR008705; Nanos. DR InterPro; IPR001878; Znf_CCHC. DR Pfam; PF05741; Nanos; 1. DR SMART; SM00343; ZnF_C2HC; 1. KW Developmental protein. FT DOMAIN 111 115 POLY-GLN. FT DOMAIN 198 205 POLY-GLN. FT DOMAIN 296 302 POLY-ASN. SQ SEQUENCE 401 AA; 43428 MW; FA4ACFC2FFC01A75 CRC64; MFRSNLEGSG AAAVGVANPP SLAQSGKIFQ LQDNFSAFHA RGGLNILGLQ DMYLDTSGAN SSATLSPPIT PVTPDPSTSA QSTHFPFLAD SAATANSLLM QRQYHYHLLL QQQQQLAMAQ HQLALAASAA AASASHQQTD EIARSLKIFA QVTTGAAENA AGSMQDVMQE FATNGYASDD LGRMSYGSAP PQVQMPPQQQ HQQQQGLHLP LGRNPAQLQT NGGNLMPIPL ATHWLNNYRE HLNNVWRNMS YIPAAPNTMG LQAQTAATVS TNLGVGMGLG LPVQGEQLRG ASNSSNNNNN NNKVYKRYNS KAKEISRHCV FCENNNEPEA VINSHSVRDN FNRVLCPKLR TYVCPICGAS GDSAHTIKYC PKKPIITMED AIKAESFRLA KSSYYKQQMK V // ID NNP1_DROME STANDARD; PRT; 687 AA. AC Q9VJZ7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NNP-1 protein homolog. GN NNP-1 OR CG12396. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PLAYS A CRITICAL ROLE IN THE GENERATION OF 28S RRNA (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE NNP-1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003639; AAF53287.1; -. DR FlyBase; FBgn0022069; Nnp-1. DR InterPro; IPR008938; ARM. KW Nuclear protein. SQ SEQUENCE 687 AA; 78996 MW; 8055B70217B78604 CRC64; MVTRKKPVKR NAEAAEIQVE QEEDASQPKV AKELMVVAQE VKIIRALACN DVVERNRQIR ILRKWFKARA GSSFPFNEDD FMRIWKGLYY TMWMSDKPLV QEELAEKLAQ MVDSFGGNTA CSLAYFSAFM RTMCQEYFGI DQWRMDKFLM LTRRMVRYLL RFLKQNNWNA DLIAAFNSSM QLSVMSEQPK SRGMTMHYLD VFFEELAKAA NGEITAAQVN MFLRPFVTYI ATQRDAKLVA QCRTRVLYHL MYQSDLGRQY SEKYNAWKQM GFPTASIDDI EKLDSGFDEE DDEVNAEEEQ PRATSLDPRA GNVDVHMPEL PLNADCVLDE LQTQLRTNDF NSKRRKGLRK LIQIFETYQR GEFPLGVRTM PKVEGQTLSE MVEQKVAALD KMEDEVFATG RKLKKLNKSK RKRLLQSINF EEVDEHNYDE VISKALPPEL QKKVNYNAKV RSSINNAWVV EEVKEAEPKS KKAKKEEPPQ QNKDDQTKVK KKSQLKPKND QSKPKIEDQP TLKAEKEEPA KRKKLDHSKT KEEQSKPKTD EQPKPTPKVE GQSKAKPTPK TKAAGVDDDA PTNGWDAPLE DGEQDIFVPS RKLQVKQANS KLPQSTPKQP ARAEFATPQT GSGKHVRIVT KSNCIYPKSD YYRQLKLSPQ VPYDANRLPG KSALKPHWIP GPIHPSYKAK RLFNDTL // ID NO60_DROME STANDARD; PRT; 508 AA. AC O44081; Q9V3Z5; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nucleolar protein AT band 60B (Minifly protein). GN NOP60B OR MFL OR CG3333. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99045289; PubMed=9829824; RA Phillips B., Billin A.N., Cadwell C., Buchholz R., Erickson C., RA Merriam J.R., Carbon J., Poole S.J.; RT "The Nop60B gene of Drosophila encodes an essential nucleolar protein RT that functions in yeast."; RL Mol. Gen. Genet. 260:20-29(1998). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=99189256; PubMed=10087258; RA Giordano E., Peluso I., Senger S., Furia M.; RT "minifly, a Drosophila gene required for ribosome biogenesis."; RL J. Cell Biol. 144:1123-1133(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PLAYS A CENTRAL ROLE IN RIBOSOMAL RNA PROCESSING. CC -!- SUBCELLULAR LOCATION: NUCLEAR; NUCLEOLAR. CC -!- SIMILARITY: BELONGS TO THE PSEUDOURIDINE SYNTHASE TRUB FAMILY. CC -!- SIMILARITY: CONTAINS 1 PUA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF017230; AAC97117.1; -. DR EMBL; AF089837; AAD16092.1; -. DR EMBL; AE003463; AAF47178.1; -. DR FlyBase; FBgn0023184; Nop60B. DR InterPro; IPR004802; Cbf5. DR InterPro; IPR002478; PUA. DR InterPro; IPR002501; TruB__synth_N. DR Pfam; PF01472; PUA; 1. DR Pfam; PF01509; TruB_N; 1. DR SMART; SM00359; PUA; 1. DR TIGRFAMs; TIGR00425; CBF5; 1. DR PROSITE; PS50890; PUA; 1. KW Nuclear protein; tRNA processing. FT DOMAIN 294 369 PUA. FT DOMAIN 8 16 POLY-LYS. FT DOMAIN 450 453 POLY-ALA. FT DOMAIN 461 471 POLY-LYS. FT DOMAIN 489 499 POLY-LYS. SQ SEQUENCE 508 AA; 56830 MW; 3CAE3F91C84E0A94 CRC64; MADVEVRKEK KKKKIKEEPL DGDDIGTLQK QGNFQIKPSS KIAELDTSQW PLLLKNFDKL NIRSNHYTPL AHGSSPLNRD IKEYMKTGFI NLDKPSNPSS HEVVAWIKKI LKVEKTGHSG TLDPKVTGCL IVCIDRATRL VKSQQSAGKE YVAIFKLHGA VESVAKVRQG LEKLRGALFQ RPPLISAVKR QLRVRTVYDS KLLDYDETRN MGVFWVSCEA GSYIRTMCVH LGLVLGVGGQ MLELRRVRSG IQSERDGMVT MHDVLDAMWL YENHKDESML RRVIKPLEGL LVNHKRIIMK DSSVNAVCYG AKITLPGVLR YEDGIEIDQE IVICTTKGEA ICLAIALMTT ATMASCDHGV VAKIKRVIME RDTYPRKWGL GPKASAKKAL IAAGKLDKFG RPNENTPKEW LTGYVDYNAK KPAAQEVSPT NGSSEPSKRK LSTSSVEETA AAAVSEETPS KDKKKKKKKH KGDEEAPEAA EEEAEPVEKE KKKKKKKDKD RDRDEAQE // ID NOD_DROME STANDARD; PRT; 666 AA. AC P18105; Q9VYW9; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Kinesin-like protein NOD. GN NOD OR NODA OR CG1763. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90381763; PubMed=2144792; RA Zhang P., Knowles B.A., Goldstein L.S.B., Hawley R.S.; RT "A kinesin-like protein required for distributive chromosome RT segregation in Drosophila."; RL Cell 62:1053-1062(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NOD(DTW) ALLELE. RX MEDLINE=92077391; PubMed=1743485; RA Rasooly R.S., New C.M., Zhang P., Hawley R.S., Baker B.S.; RT "The lethal(1)TW-6cs mutation of Drosophila melanogaster is a RT dominant antimorphic allele of nod and is associated with a single RT base change in the putative ATP-binding domain."; RL Genetics 129:409-422(1991). CC -!- FUNCTION: REQUIRED FOR THE DISTRIBUTIVE CHROMOSOME SEGREGATION CC OF NONEXCHANGE CHROMOSOMES DURING MEIOSIS. IT MAY BE A CC MICROTUBULE MOTOR REQUIRED TO HOLD DISTRIBUTIVELY "PAIRED" CC CHROMOSOMES AT THE METAPHASE PLATE UNTIL ANAPHASE. CC -!- TISSUE SPECIFICITY: IN ADULT FEMALE IT IS ONLY FOUND IN CC MEIOTICALLY ACTIVE OVARIES. CC -!- DEVELOPMENTAL STAGE: EMBRYONIC, LARVAL, AND PUPAL STAGES. IN CC ADULTS IT IS ONLY PRESENT IN FEMALES. CC -!- MISCELLANEOUS: THE NOD(DTW) MUTATION IS A COLD-SENSITIVE RECESSIVE CC LETHAL MUTATION. CC -!- SIMILARITY: BELONGS TO THE KINESIN-LIKE PROTEIN FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M36195; AAA28653.1; -. DR EMBL; M94188; AAC14452.1; -. DR EMBL; AE003486; AAF48064.1; ALT_SEQ. DR EMBL; AY050238; AAK84937.1; -. DR PIR; A36026; A36026. DR HSSP; P33176; 1BG2. DR FlyBase; FBgn0002948; nod. DR GO; GO:0005871; C:kinesin complex; IDA. DR GO; GO:0016326; F:kinesin motor activity; IMP. DR GO; GO:0045132; P:meiotic chromosome segregation; IMP. DR GO; GO:0000212; P:meiotic spindle assembly; NAS. DR InterPro; IPR000445; HhH. DR InterPro; IPR003583; HHH_1. DR InterPro; IPR001752; kinesin_motor. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00225; kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00278; HhH1; 1. DR SMART; SM00129; KISc; 1. DR PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1. KW Motor protein; Microtubule; ATP-binding; Coiled coil. FT DOMAIN 1 318 KINESIN-MOTOR (POTENTIAL). FT DOMAIN 639 666 COILED COIL (POTENTIAL). FT NP_BIND 87 94 ATP (BY SIMILARITY). FT VARIANT 94 94 S -> N (IN ALLELE NOD(DTW)). SQ SEQUENCE 666 AA; 73907 MW; E3DEF72C08973FC2 CRC64; MEGAKLSAVR IAVREAPYRQ FLGRREPSVV QFPPWSDGKS LIVDQNEFHF DHAFPATISQ DEMYQALILP LVDKLLEGFQ CTALAYGQTG TGKSYSMGMT PPGEILPEHL GILPRALGDI FERVTARQEN NKDAIQVYAS FIEIYNEKPF DLLGSTPHMP MVAARCQRCT CLPLHSQADL HHILELGTRN RRVRPTNMNS NSSRSHAIVT IHVKSKTHHS RMNIVDLAGS EGVRRTGHEG VARQEGVNIN LGLLSINKVV MSMAAGHTVI PYRDSVLTTV LQASLTAQSY LTFLACISPH QCDLSETLST LRFGTSAKKL RLNPMQVARQ KQSLAARTTH VFRQALCTST AIKSNAANHN SIVVPKSKYS TTKPLSAVLH RTRSELGMTP KAKKRARELL ELEETTLELS SIHIQDSSLS LLGFHSDSDK DRHLMPPPTG QEPRQASSQN STLMGIVEET EPKESSKVQQ SMVAPTVPTT VRCQLFNTTI SPISLRASSS QRELSGIQPM EETVVASPQQ PCLRRSVRLA SSMRSQNYGA IPKVMNLRRS TRLAGIREHA TSVVVKNETD AIPHLRSTVQ KKRTRNVKPA PKAWMANNTK CFLDLLNNGN VKQLQEIPGI GPKSAFSLAL HRSRLGCFEN LFQVKSLPIW SGNKWERFCQ INCLDT // ID NOF1_DROME STANDARD; PRT; 633 AA. AC P15296; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 71 kDa protein in NOF-FB transposable element. GN NOF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=89356666; PubMed=2548860; RA Templeton N.S., Potter S.S.; RT "Complete foldback transposable elements encode a novel protein found RT in Drosophila melanogaster."; RL EMBO J. 8:1887-1894(1989). CC -!- FUNCTION: NOT KNOWN. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: TO N-TERMINAL OF NOF-FB ELEMENT PROTEIN IN CC STRAIN TE146(Z). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15469; CAA33496.1; -. DR PIR; S07824; S07824. DR FlyBase; FBgn0044029; NOF\ORF. KW Nuclear protein; Transposable element. SQ SEQUENCE 633 AA; 71919 MW; 8C1368057F846CBC CRC64; MPAKPQVDGH TLVDAFCCAN IFTETGALKP RSDKVWMDIS NQLKGAISAK TLNFYARINR NNMITVVKER CGIQQLDTSA NLTLNSTFPD DDPEFQITEA SKNGPLPILY FNLELDLELW RSIAPKKDQK TEKLQPNWTD TMAKLIYKKV PLPCAFNFRK AKLSDKVDNI WLRIEGYCND CSSILKGHCL VKPDEQCGIM ISVSVPDTRG IPHNKKRRCT GSRRLEIGNE LILKKAALWR KEATDNMNDD DPEPSYIPNL PTLRKLREEA TNRHLGITKD RDPVSSLYLK KYEGELAGCI LDIGLDEFFC IYCTGTQVKT YASRIKTIRK ISIDATGSVV LPIQKPNGDS SYVFLYQIVM EGDDSIFPVF QMLSAKHDTA SIQFWLSRFI SKSGHFPLEV VSDFSLALLN GISLSFNECR IATYIKKCFH SLLMEERTDL PPCYIRLDIA HLIKMICRKN VFKSKLPNLK DFYTRCIGLA TTCETKDSFA ELIKSVLIVA LSQSSGEDEK GDILSSYRNE KYLLARIATF TAPDHKETIE DNCIPEDQEE IDEDVTDFIS NIKIAAEEEA LNCNSVNCRP NPYFLPELMP PLIKLCKYFV LWTNVMKEKL CSKYDVGSSA LVEAYFKDLN FWT // ID NOF2_DROME STANDARD; PRT; 403 AA. AC P15297; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 46 kDa protein in NOF-FB transposable element. GN NOF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=89356666; PubMed=2548860; RA Templeton N.S., Potter S.S.; RT "Complete foldback transposable elements encode a novel protein found RT in Drosophila melanogaster."; RL EMBO J. 8:1887-1894(1989). CC -!- FUNCTION: NOT KNOWN. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: TO C-TERMINAL OF NOF-FB ELEMENT PROTEIN IN CC STRAIN TE146(Z). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15469; CAA33497.1; -. DR PIR; S07825; S07825. DR FlyBase; FBgn0044029; NOF\ORF. KW Nuclear protein; Transposable element. SQ SEQUENCE 403 AA; 46519 MW; 52606117EF64A164 CRC64; MKRKTVKTPS FIKENAPKKM CSKETKGFLE EILEESEVEY LLQEENWKVK NKTIKPTEGN DAEDNDTDDE NKEMDLSEQP KEKPRGKYLK KCPNVELLYN RPHRRKQDEI LHNGGSMGPV WIGKQLLQFK NTCPFDSLVE ILSTAYIDNF YYKSLLDDFY TDNLTIELVK KYAVEGVSSS LYCDRGLVLK SFFDEKHQII KCDANIGSFI EKALNGVPSA SSHRTHIKNN HDCRNQKYIH HRLEVIDVEK VGHLDVQEVV IPFIDEFFAR TDGECKICGG QQILERQPGP HVILDIEFAM DAFHQIHHNG LPGTTTLLQV PGGNFNTGKE IYFKWCHRIC SCDGRGNWTL HCILPQSHWI LGSAQRYVQA MEKVLSSKYQ NDTPHFDIHP EKLMFIFKPC LKV // ID NOF_DROME STANDARD; PRT; 984 AA. AC P16320; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 112 kDa protein in NOF-FB transposable element. GN NOF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=TE146(Z); RX MEDLINE=91060072; PubMed=2174013; RA Harden N., Ashburner M.; RT "Characterization of the FB-NOF transposable element of Drosophila RT melanogaster."; RL Genetics 126:387-400(1990). RN [2] RP SEQUENCE FROM N.A. RA Harden N.; RL Thesis (1989), University of Cambridge, U.K. CC -!- FUNCTION: MAY BE INVOLVED IN THE TRANSPOSITION OF NOF-FB AND OTHER CC FB ELEMENTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: TO 71 KDA AND 46 KDA PROTEINS OF NOF-FB ELEMENT IN CC STRAIN OREGON-R. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51937; CAA36201.1; -. DR PIR; S14382; S14382. DR FlyBase; FBgn0044029; NOF\ORF. KW Nuclear protein; Transposable element. SQ SEQUENCE 984 AA; 112748 MW; D235CCFE1378B6C2 CRC64; IQQLDTSANL TLNSTFPDDD PEFQITEASK NGPLPILYFN LELDLELWRS IAPKKDQKTE KLQPNWTDTM AKLIYKKVPL PCAFNFRKAK LSDKVDNIWL RIEGYCNDCS SILKGHCLVK PDEQCGIMIS VSVPDTRGIP HNKKRRCTGS RRLEIGNELI LKKAALWRKE ATDNMNDDDP EPSYIPNLPT LRKLREEATN RHLGITKDRD PVSSLYLKKY EGELAGCILD IGLDEFFCIY CTGTQVKTYA SRIKTIRKIS IDATGSVVLP IQKPNGDSSY VFLYQIVMEG DDSIFPVFQM LSAKHDTASI QFWLSRFISK SGHFPLEVVS DFSLALLNGI SLSFNECRIA TYIKKCFHSL LMEERTDLPP CYIRLDIAHL IKMICRKNVF KSKLPNLKDF YTRCIGLATT CETKDSFAEL IKSVLIVALS QSSGEDEKGD ILSSYRNEKY LLARIATFTA PDHKETIEDN CIPEDQEEID EDVTDFISNI KIAAEEEALN CNSVNCRPNP YFLPELMPPL IKLCKYFVLW TNVMKEKFCS KYDVGSSALV EAYFKDLKNT DMSIFHRPVR ADKFVVQHIR CIEAVCKLER AAMKRKTVKT PSFIKENAPK KMCSKETKGF LEEILEESEV EYLLQEENWK VKNKTIKPTE GNDAEDNDTD DENKEMDLSE QPKEKPRGKY LKKCPNVELL YNRPHRRKQD EILHNGGSMG PVWIGKQLLQ FKNTCPFDSL VEILSTAYID NFYYKSLLDD FYTDNLTIEL VKKYAVEGVS SSLYCDRGLV LKSFFDEKHQ IIKCDANIGS FIEKALNGVP SASSHRTHIK NNHDCRNQKY IHHRLEVIDV EKVGHLDVQE VVIPFIDEFF ARTDGECKIC GGQQILERQP GPHVILDIEF AMDAFHQIHH NGLPGTTTLL QVPEEILIQE KKYILSGAIE YVPAMGGEIG HYIAYCRRVI GSWEVHNDMC RQWKKFSALN TKMTLHILIY TRKN // ID NOI_DROME STANDARD; PRT; 503 AA. AC O46106; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Splicing factor 3A subunit 3 (Noisette protein). GN NOI OR CG2925. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Embryo, and Ovary; RX MEDLINE=98187604; PubMed=9528755; RA Meyer V., Oliver B., Pauli D.; RT "Multiple developmental requirements of noisette, the Drosophila RT homolog of the U2 snRNP-associated polypeptide SP3a60."; RL Mol. Cell. Biol. 18:1835-1843(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PROBABLE SUBUNIT OF A SPLICING FACTOR COMPLEX REQUIRED CC FOR 'A' COMPLEX ASSEMBLY FORMED BY THE STABLE BINDING OF U2 SNRNP CC TO THE BRANCHPOINT SEQUENCE (BPS) IN PRE-MRNA (BY SIMILARITY). CC INVOLVED IN MALE FERTILITY. CC -!- SUBUNIT: PROBABLE COMPONENT OF A THE U2 SMALL NUCLEAR CC RIBONUCLEOPROTEINS COMPLEX (U2 SNRNP) (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR; EXCLUDED FROM THE NUCLEOLI. CC -!- TISSUE SPECIFICITY: UBIQUITOUS. IN OVARIES AND TESTES, IT IS CC EXPRESSED IN ALL GERM AND SOMATIC CELLS. HIGHLY EXPRESSED IN CC SPERMATOGONIAS AND SPERMATOCYTES. HIGHLY EXPRESSED IN THE GERM CC CELLS OF LARVAL TESTES, WHILE IT IS WEAKLY EXPRESSED IN FAT BODY CC CELLS, IN POLYPLOID NUCLEI OF SALIVARY GLANDS, AND IN LARVAL CC BRAIN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYOGENESIS FROM CC SYNCYTIAL BLASTODERM STAGE. CC -!- MISCELLANEOUS: 'NOISETTE' MEANS 'HAZEL NUT' IN FRENCH, AND IS DUE CC TO THE SMALL SIZE OF TESTES IN MUTANTS. CC -!- SIMILARITY: BELONGS TO THE SF3A3 FAMILY. CC -!- SIMILARITY: CONTAINS 1 MATRIN-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ223042; CAA11045.1; -. DR EMBL; AE003602; AAF51999.1; -. DR EMBL; AY051676; AAK93100.1; -. DR FlyBase; FBgn0014366; noi. DR GO; GO:0005681; C:spliceosome complex; ISS. DR GO; GO:0008248; F:pre-mRNA splicing factor activity; ISS. DR GO; GO:0009566; P:fertilization; IMP. DR GO; GO:0008380; P:RNA splicing; ISS. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR000690; Znf_matrin. DR SMART; SM00355; ZnF_C2H2; 1. DR PROSITE; PS50171; ZF_MATRIN; 1. KW Spliceosome; mRNA processing; mRNA splicing; Nuclear protein; KW Metal-binding; Zinc-finger; Zinc. FT ZN_FING 408 439 MATRIN-TYPE. SQ SEQUENCE 503 AA; 58421 MW; 20F3C259C41DE406 CRC64; METLLEQQRR LHEERERLVK LMVDEHATKK PGEKERIHSE HRLKYLMELH HNSTSQLRDL YEDKDNERKA EIAALSGPNE FNEFYARLKQ IKQFYKSHPA EVSVPLSVEF DEMIRVYNNP DDMSALVEFT DEEGGGRYLD LNECYELYLN LRSVEKLDYI TYLMSFDHVF DIPRERKNRE YRIYIETLND YLHHFILRIQ PLLDLEGELL KVELDFQRQW LMGTFPGFSI KETESALANT GAHLDLSAFS SWEELASLGL DRLKSALVAL GLKCGGTLEE RAQRLFSTKG KSTLDPALMA KKPSAKTASA QSREHERHKE IAQLEALLYK YADLLSEQRA ATKENVQRKQ ARTGGERDDS DVEASESDNE DDPDADDVPY NPKNLPLGWD GKPIPYWLYK LHGLNISYNC EICGNFTYKG PKAFQRHFAE WRHAHGMRCL GIPNTAHFAN VTQIEDAITL WEKLKSQKQS ERWVADQEEE FEDSLGNVVN RKTFEDLKRQ GLL // ID NONA_DROME STANDARD; PRT; 700 AA. AC Q04047; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE No-on-transient A protein. GN NONA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS I AND II). RX MEDLINE=90262721; PubMed=2344408; RA Jones K.R., Rubin G.M.; RT "Molecular analysis of no-on-transient A, a gene required for normal RT vision in Drosophila."; RL Neuron 4:711-723(1990). CC -!- FUNCTION: REQUIRED FOR NORMAL VISION IN DROSOPHILA. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=I; CC IsoId=Q04047-1; Sequence=Displayed; CC Name=II; CC IsoId=Q04047-2; Sequence=VSP_005801; CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33496; AAA03214.1; -. DR EMBL; M33496; AAA03215.1; -. DR PIR; JH0162; JH0162. DR PIR; JH0163; JH0163. DR HSSP; P11940; 1CVJ. DR FlyBase; FBgn0004227; nonA. DR GO; GO:0045433; P:male courtship behavior (sensu Insecta), so...; NAS. DR GO; GO:0042331; P:phototaxis; NAS. DR GO; GO:0007632; P:visual behavior; NAS. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW RNA-binding; Repeat; Vision; Alternative splicing. FT DOMAIN 302 374 RNA-BINDING (RRM) 1. FT DOMAIN 376 457 RNA-BINDING (RRM) 2. FT DOMAIN 73 76 POLY-GLY. FT DOMAIN 254 264 POLY-GLY. FT DOMAIN 619 626 POLY-GLY. FT DOMAIN 648 652 POLY-ASN. FT VARSPLIC 666 700 DSFAFEFGVNNMNQGGNQRGNNGGGNNVPWGRRRF -> VC FT PHPKYYPTKYSVTNRSVELQELLSMIPFMKL (in FT isoform II). FT /FTId=VSP_005801. SQ SEQUENCE 700 AA; 76967 MW; 732DB77FC5DF6D47 CRC64; MESAGKQDNN ATQQLPQRQQ RGNQQANKNL GKHNAQKQND SADGGPAEKK QRFGGPNAQN QNQNQNQNGG VTGGGGAVGG PNQNKNFGNN KGGFVGNRNR NNNRAGNQNR TFPGNNNSNQ KPNNETSKAD GPNALAKNNE PATAAAGQNQ ANQNANKGQN QRQGQNQNQN QVHGQGNQGG PGNQGGAGNQ GGQGNQGGAG NQGNGQGFRG RNAGNNQGGG FSGGPQNQQR DNRNRSGPRP GGGAGGAMNS TNMGGGGGGG GGGGPRGGED FFITQRLRSI SGPTFELEPV EVPTETKFSG RNRLYVGNLT NDITDDELRE MFKPYGEISE IFSNLDKNFT FLKVDYHPNA EKAKRALDGS MRKGRQLRVR FAPNATILRV SNLTPFVSNE LLYKSFEIFG PIERASITVD DRGKHMGEGI VEFAKKSSAS ACLRMCNEKC FFLTASLRPC LVDPMEVNDD TDGLPEKAFN KKMPDFNQER SIGPRFADPN SFEHEYGSRW KQLHNLFKTK QDALKRELKM EEDKLEAQME YARYEQETEL LRQELRKREV DNERKKLEWE MREKQAEEMR KREEETMRRH QTEMQSHMNR QEEDMLRRQQ ETLFMKAQQL NSLLDQQEGF GGGGGGNNST FDNFAGNSNS PFEVFRGNNN NNSTMIGNNA APNTQDSFAF EFGVNNMNQG GNQRGNNGGG NNVPWGRRRF // ID NOS_DROME STANDARD; PRT; 1349 AA. AC Q27571; Q9U096; Q9VKP8; DT 30-MAY-2000 (Rel. 39, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nitric-oxide synthase (EC 1.14.13.39) (dNOS). GN NOS OR CG6713. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC TISSUE=Head; RX MEDLINE=96016111; PubMed=7568075; RA Regulski M., Tully T.; RT "Molecular and biochemical characterization of dNOS: a Drosophila RT Ca2+/calmodulin-dependent nitric oxide synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 92:9072-9076(1995). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND ALTERNATIVE SPLICING. RC TISSUE=Embryo, and Larva; RX MEDLINE=21551173; PubMed=11526108; RA Stasiv Y., Regulski M., Kuzin B., Tully T., Enikolopov G.; RT "The Drosophila nitric-oxide synthase gene (dNOS) encodes a family of RT proteins that can modulate NOS activity by acting as dominant RT negative regulators."; RL J. Biol. Chem. 276:42241-42251(2001). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PRODUCES NITRIC OXIDE (NO) WHICH IS A MESSENGER MOLECULE CC WITH DIVERSE FUNCTIONS THROUGHOUT THE BODY. TRUNCATED ISOFORMS (3, CC 4, 5 AND 6) ARE ABLE TO FORM INTRACELLULAR COMPLEXES WITH THE FULL CC LENGTH PROTEIN AND SERVE AS DOMINANT NEGATIVE INHIBITORS OF THE CC ENZYME ACTIVITY. CC -!- CATALYTIC ACTIVITY: L-ARGININE + N NADPH + M O(2) = CITRULLINE + CC NITRIC OXIDE + N NADP(+). CC -!- COFACTOR: HEME. BINDS ONE MOLE EACH OF FAD AND FMN (BY CC SIMILARITY). CC -!- ENZYME REGULATION: STIMULATED BY CALCIUM/CALMODULIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=dNOS-1; CC IsoId=Q27571-1; Sequence=Displayed; CC Name=2; Synonyms=dNOS-2; CC IsoId=Q27571-2; Sequence=VSP_003587; CC Name=3; Synonyms=dNOS-3; CC IsoId=Q27571-3; Sequence=VSP_003585, VSP_003586; CC Name=4; Synonyms=dNOS-4; CC IsoId=Q27571-4; Sequence=VSP_003592, VSP_003593; CC Name=5; Synonyms=dNOS-5; CC IsoId=Q27571-5; Sequence=VSP_003588, VSP_003589; CC Name=6; Synonyms=dNOS-6; CC IsoId=Q27571-6; Sequence=VSP_003590, VSP_003591; CC Name=10; Synonyms=dNOS-10; CC IsoId=Q27571-7; Sequence=VSP_003594; CC -!- DEVELOPMENTAL STAGE: ISOFORM 3 IS EXPRESSED IN LARVAE ONLY. CC ISOFORMS 4, 5, 6 AND 10 ARE EXPRESSED THROUGHOUT DEVELOPMENT FROM CC EMBRYOS TO ADULTS. CC -!- SIMILARITY: BELONGS TO THE NOS FAMILY. CC -!- SIMILARITY: CONTAINS 1 FLAVODOXIN-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U25117; AAC46882.1; -. DR EMBL; AF215700; AAF25682.1; -. DR EMBL; AF215691; AAF25682.1; JOINED. DR EMBL; AF215692; AAF25682.1; JOINED. DR EMBL; AF215693; AAF25682.1; JOINED. DR EMBL; AF215694; AAF25682.1; JOINED. DR EMBL; AF215695; AAF25682.1; JOINED. DR EMBL; AF215696; AAF25682.1; JOINED. DR EMBL; AF215697; AAF25682.1; JOINED. DR EMBL; AF215698; AAF25682.1; JOINED. DR EMBL; AF215699; AAF25682.1; JOINED. DR EMBL; AE003630; AAF53014.1; -. DR PIR; T13254; T13254. DR HSSP; P29477; 1DD7. DR FlyBase; FBgn0011676; Nos. DR GO; GO:0005516; F:calmodulin binding; NAS. DR GO; GO:0020037; F:heme binding; NAS. DR GO; GO:0004517; F:nitric-oxide synthase activity; TAS. DR GO; GO:0006809; P:nitric oxide biosynthesis; TAS. DR InterPro; IPR003097; FAD_binding. DR InterPro; IPR008254; Flav_nitox_synth. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001709; FPN_cyt_redctse. DR InterPro; IPR004030; NO_synthase. DR InterPro; IPR001433; Oxred_FAD/NAD(P). DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; flavodoxin; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF02898; NO_synthase; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PROSITE; PS60001; NOS; 1. KW Oxidoreductase; NADP; FAD; FMN; Calmodulin-binding; Heme; KW Alternative splicing. FT DOMAIN 671 868 FLAVODOXIN-LIKE. FT DOMAIN 24 51 GLN-RICH. FT DOMAIN 76 79 POLY-GLY. FT DOMAIN 145 156 POLY-GLY. FT METAL 328 328 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT DOMAIN 641 661 CALMODULIN-BINDING (POTENTIAL). FT NP_BIND 814 845 FMN (PYRIMIDINE PART) (BY SIMILARITY). FT NP_BIND 957 968 FAD (ADP PART) (BY SIMILARITY). FT NP_BIND 1100 1110 FAD (FLAVIN PART) (BY SIMILARITY). FT NP_BIND 1175 1193 NADP (RIBOSE PART) (BY SIMILARITY). FT NP_BIND 1273 1287 NADP (ADP PART) (BY SIMILARITY). FT VARSPLIC 201 214 FMHLDDEGRSLLMR -> RFFPARRPPVRAAL (in FT isoform 3). FT /FTId=VSP_003585. FT VARSPLIC 215 1349 Missing (in isoform 3). FT /FTId=VSP_003586. FT VARSPLIC 417 521 Missing (in isoform 2). FT /FTId=VSP_003587. FT VARSPLIC 701 704 IYCM -> VSLT (in isoform 5). FT /FTId=VSP_003588. FT VARSPLIC 705 1349 Missing (in isoform 5). FT /FTId=VSP_003589. FT VARSPLIC 701 746 IYCMSDYDISSIEHEALLIVVASTFGNGDPPENGELFSQEL FT YAMRV -> CPVGSVSSDPQDPVQLGLVVVLVSSTCVCKKH FT LPAAWQNKISCKHL (in isoform 6). FT /FTId=VSP_003590. FT VARSPLIC 747 1349 Missing (in isoform 6). FT /FTId=VSP_003591. FT VARSPLIC 737 757 FSQELYAMRVQESSEHGLQDS -> VSTPPRKDHTELINGL FT GPAAF (in isoform 4). FT /FTId=VSP_003592. FT VARSPLIC 758 1349 Missing (in isoform 4). FT /FTId=VSP_003593. FT VARSPLIC 760 1293 Missing (in isoform 10). FT /FTId=VSP_003594. FT CONFLICT 20 20 S -> A (IN REF. 1). FT CONFLICT 24 24 Q -> QQ (IN REF. 1). FT CONFLICT 105 105 S -> L (IN REF. 1). FT CONFLICT 287 287 S -> C (IN REF. 1). FT CONFLICT 373 373 T -> S (IN REF. 2). FT CONFLICT 1197 1197 R -> S (IN REF. 3). SQ SEQUENCE 1349 AA; 151783 MW; FB96861AFEAF77EC CRC64; MSQHFTSIFE NLRFVTIKRS TNAQQQQQQQ QQQLQQQQQQ LQQQKAQTQQ QNSRKIKTQA TPTLNGNGLL SGNPNGGGGD SSPSHEVDHP GGAQGAQAAG GLPSSSGTPL RHHKRASIST ASPPIRERRG TNTSIVVELD GSGSGSGSGG GGVGVGQGAG CPPSGSCTAS GKSSRELSPS PKNQQQPRKM SQDYRSRAGS FMHLDDEGRS LLMRKPMRLK NIEGRPEVYD TLHCKGREIL SCSKATCTSS IMNIGNAAVE ARKSDLILEH AKDFLEQYFT SIKRTSSTAH ETRWKQVRQS IETTGHYQLT ETELIYGAKL AWRNSSRCIG RIQWSKLQVF DCRYVTTTSG MFEAICNHIK YATNKGNLRS AITIFPQRTD AKHDYRIWNN QLISYAGYKQ ADGKIIGDPM NVEFTEVCTK LGWKSKGSEW DILPLVVSAN GHDPDYFDYP PELILEVPLT HPKFEWFSDL GLRWYALPAV SSMLFDVGGI QFTATTFSGW YMSTEIGSRN LCDTNRRNML ETVALKMQLD TRTPTSLWKD KAVVEMNIAV LHSYQSRNVT IVDHHTASES FMKHFENESK LRNGCPADWI WIVPPLSGSI TPVFHQEMAL YYLKPSFEYQ DPAWRTHVWK KGRGESKGKK PRRKFNFKQI ARAVKFTSKL FGRALSKRIK ATVLYATETG KSEQYAKQLC ELLGHAFNAQ IYCMSDYDIS SIEHEALLIV VASTFGNGDP PENGELFSQE LYAMRVQESS EHGLQDSSIG SSKSFMKASS RQEFMKLPLQ QVKRIDRWDS LRGSTSDTFT EETFGPLSNV RFAVFALGSS AYPNFCAFGQ YVDNILGELG GERLLRVAYG DEMCGQEQSF RKWAPEVFKL ACETFCLDPE ESLSDASLAL QNDSLTVNTV RLVPSANKGS LDSSLSKYHN KKVHCCKAKA KPHNLTRLSE GAKTTMLLEI CAPGLEYEPG DHVGIFPANR TELVDGLLNR LVGVDNPDEV LQLQLLKEKQ TSNGIFKCWE PHDKIPPDTL RNLLARFFDL TTPPSRQLLT LLAGFCEDTA DKERLELLVN DSSAYEDWRH WRLPHLLDVL EEFPSCRPPA PLLLAQLTPL QPRFYSISSS PRRVSDEIHL TVAIVKYRCE DGQGDERYGV CSNYLSGLRA DDELFMFVRS ALGFHLPSDR SRPIILIGPG TGIAPFRSFW QEFQVLRDLD PTAKLPKMWL FFGCRNRDVD LYAEEKAELQ KDQILDRVFL ALSREQAIPK TYVQDLIEQE FDSLYQLIVQ ERGHIYVCGD VTMAEHVYQT IRKCIAGKEQ KSEAEVETFL LTLRDESRYH EDIFGITLRT AEIHTKSRAT ARIRMASQP // ID NOTC_DROME STANDARD; PRT; 2703 AA. AC P07207; O97458; P04154; Q9W4T8; DT 01-NOV-1986 (Rel. 03, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Neurogenic locus Notch protein precursor. GN N OR EG:140G11.1 OR EG:163A10.2 OR CG3936. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=86079539; PubMed=3935325; RA Wharton K.A., Johansen K.M., Xu T., Artavanis-Tsakonas S.; RT "Nucleotide sequence from the neurogenic locus notch implies a gene RT product that shares homology with proteins containing EGF-like RT repeats."; RL Cell 43:567-581(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo; RX MEDLINE=87064624; PubMed=3097517; RA Kidd S., Kelley M.R., Young M.W.; RT "Sequence of the notch locus of Drosophila melanogaster: relationship RT of the encoded protein to mammalian clotting and growth factors."; RL Mol. Cell. Biol. 6:3094-3108(1986). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP SEQUENCE OF 2505-2611 FROM N.A. RX MEDLINE=85099329; PubMed=2981631; RA Wharton K.A., Yedvobnick B., Finnerty V.G., Artavanis-Tsakonas S.; RT "opa: a novel family of transcribed repeats shared by the Notch locus RT and other developmentally regulated loci in D. melanogaster."; RL Cell 40:55-62(1985). RN [6] RP SEQUENCE OF 1-8 FROM N.A. RX MEDLINE=87257846; PubMed=3037327; RA Kelley M.R., Kidd S., Berg R.L., Young M.W.; RT "Restriction of P-element insertions at the Notch locus of Drosophila RT melanogaster."; RL Mol. Cell. Biol. 7:1545-1548(1987). RN [7] RP INTERACTION WITH DX, AND MUTANT SU42C. RX MEDLINE=94215489; PubMed=8162848; RA Diederich R.J., Matsuno K., Hing H., Artavanis-Tsakonas S.; RT "Cytosolic interaction between deltex and Notch ankyrin repeats RT implicates deltex in the Notch signaling pathway."; RL Development 120:473-481(1994). RN [8] RP INTERACTION WITH DX. RX MEDLINE=95401878; PubMed=7671825; RA Matsuno K., Diederich R.J., Go M.J., Blaumueller C.M., RA Artavanis-Tsakonas S.; RT "Deltex acts as a positive regulator of Notch signaling through RT interactions with the Notch ankyrin repeats."; RL Development 121:2633-2644(1995). RN [9] RP S3 CLEAVAGE BY PSN. RX MEDLINE=99221487; PubMed=10206646; RA Struhl G., Greenwald I.; RT "Presenilin is required for activity and nuclear access of Notch in RT Drosophila."; RL Nature 398:522-525(1999). RN [10] RP S3 CLEAVAGE BY PSN. RX MEDLINE=99221488; PubMed=10206647; RA Ye Y., Lukinova N., Fortini M.E.; RT "Neurogenic phenotypes and altered Notch processing in Drosophila RT Presenilin mutants."; RL Nature 398:525-529(1999). RN [11] RP S2 CLEAVAGE BY KUZ. RX MEDLINE=21657146; PubMed=11799064; RA Lieber T., Kidd S., Young M.W.; RT "kuzbanian-mediated cleavage of Drosophila Notch."; RL Genes Dev. 16:209-221(2002). RN [12] RP MUTANT MCD5. RX MEDLINE=21575956; PubMed=11719214; RA Ramain P., Khechumian K., Seugnet L., Arbogast N., Ackermann C., RA Heitzler P.; RT "Novel Notch alleles reveal a Deltex-dependent pathway repressing RT neural fate."; RL Curr. Biol. 11:1729-1738(2001). RN [13] RP REVIEW. RX MEDLINE=22256570; PubMed=12369105; RA Portin P.; RT "General outlines of the molecular genetics of the Notch signalling RT pathway in Drosophila melanogaster: a review."; RL Hereditas 136:89-96(2002). CC -!- FUNCTION: SIGNALING PROTEIN, WHICH REGULATES, WITH BOTH POSITIVE CC AND NEGATIVE SIGNALS, THE DIFFERENTIATION OF AT LEAST CENTRAL AND CC PERIPHERAL NERVOUS SYSTEM AND EYE, WING DISK, OOGENESIS, SEGMENTAL CC APPENDAGES SUCH AS ANTENNAE AND LEGS, AND MUSCLES, THROUGH LATERAL CC INHIBITION OR INDUCTION. FUNCTIONS AS A RECEPTOR FOR MEMBRANE- CC BOUND LIGANDS DELTA AND SERRATE TO REGULATE CELL-FATE CC DETERMINATION. UPON LIGAND ACTIVATION, AND RELEASING FROM THE CELL CC MEMBRANE, THE NOTCH INTRACELLULAR DOMAIN (NICD) FORMS A CC TRANSCRIPTIONAL ACTIVATOR COMPLEX WITH SU(H) (SUPPRESSOR OF CC HAIRLESS) AND ACTIVATES GENES OF THE E(SPL) COMPLEX. ESSENTIAL FOR CC PROPER DIFFERENTIATION OF ECTODERM. CC -!- SUBUNIT: INTERACTS WITH SU(H) WHEN ACTIVATED. INTERACTS WITH DX CC VIA ITS ANK REPEATS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. UPON ACTIVATION AND CC S3 CLEAVAGE, IT IS RELEASED FROM THE CELL MEMBRANE AND ENTERS INTO CC THE NUCLEUS IN CONJUNCTION WITH SU(H). CC -!- PTM: UPON BINDING ITS LIGANDS SUCH AS DELTA OR SERRATE, IT IS CC CLEAVED (S2 CLEAVAGE) IN ITS EXTRACELLULAR DOMAIN, CLOSE TO THE CC TRANSMEMBRANE DOMAIN. S2 CLEAVAGE IS PROBABLY MEDIATED BY KUZ. IT CC IS THEN CLEAVED (S3 CLEAVAGE) DOWNSTREAM OF ITS TRANSMEMBRANE CC DOMAIN, RELEASING IT FROM THE CELL MEMBRANE. S3 CLEAVAGE REQUIRES CC PSN. CC -!- SIMILARITY: BELONGS TO THE NOTCH FAMILY. CC -!- SIMILARITY: CONTAINS 36 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 3 LIN/NOTCH REPEATS. CC -!- SIMILARITY: CONTAINS 6 ANK REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16152; AAB59220.1; -. DR EMBL; M16153; AAB59220.1; JOINED. DR EMBL; M16149; AAB59220.1; JOINED. DR EMBL; M16150; AAB59220.1; JOINED. DR EMBL; M16151; AAB59220.1; JOINED. DR EMBL; K03508; AAA28725.1; -. DR EMBL; M13689; AAA28725.1; JOINED. DR EMBL; K03507; AAA28725.1; JOINED. DR EMBL; AE003426; AAF45848.2; -. DR EMBL; AL035436; CAB37610.1; -. DR EMBL; AL035395; CAB37610.1; JOINED. DR EMBL; M12175; AAA74496.1; -. DR EMBL; M16025; AAA28726.1; -. DR PIR; A24420; A24420. DR HSSP; P00740; 1EDM. DR FlyBase; FBgn0004647; N. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0004888; F:transmembrane receptor activity; NAS. DR GO; GO:0007293; P:egg chamber formation (sensu Insecta); IMP. DR GO; GO:0042067; P:establishment of ommatidial polarity (sensu...; NAS. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); NAS. DR GO; GO:0007403; P:glial cell fate determination; IMP. DR GO; GO:0046331; P:lateral inhibition; NAS. DR GO; GO:0007498; P:mesoderm development; IMP. DR GO; GO:0007519; P:myogenesis; IMP. DR GO; GO:0046329; P:negative regulation of JNK cascade; NAS. DR GO; GO:0045465; P:R8 differentiation; NAS. DR GO; GO:0045468; P:regulation of R8 spacing; NAS. DR GO; GO:0007423; P:sensory organ development; IMP. DR GO; GO:0007424; P:tracheal system development (sensu Insecta); NAS. DR GO; GO:0007476; P:wing morphogenesis; NAS. DR InterPro; IPR002110; ANK. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR001438; EGF_II. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR008297; Notch. DR InterPro; IPR000800; Notch_dom. DR Pfam; PF00023; ank; 7. DR Pfam; PF00008; EGF; 36. DR Pfam; PF00066; notch; 3. DR PIRSF; PIRSF002279; Notch; 1. DR PRINTS; PR00010; EGFBLOOD. DR PRINTS; PR00011; EGFLAMININ. DR PRINTS; PR01452; NOTCH. DR SMART; SM00248; ANK; 7. DR SMART; SM00179; EGF_CA; 24. DR SMART; SM00004; NL; 3. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 5. DR PROSITE; PS00010; ASX_HYDROXYL; 22. DR PROSITE; PS00022; EGF_1; 34. DR PROSITE; PS01186; EGF_2; 28. DR PROSITE; PS50026; EGF_3; 36. DR PROSITE; PS01187; EGF_CA; 21. KW Receptor; Transcription regulation; Activator; Differentiation; KW Developmental protein; Neurogenesis; Nuclear protein; Repeat; KW ANK repeat; EGF-like domain; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 52 POTENTIAL. FT CHAIN 53 2703 NEUROGENIC LOCUS NOTCH PROTEIN. FT DOMAIN 53 1745 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1746 1766 POTENTIAL. FT DOMAIN 1767 2703 CYTOPLASMIC (POTENTIAL). FT DOMAIN 58 95 EGF-LIKE 1. FT DOMAIN 96 136 EGF-LIKE 2. FT DOMAIN 139 176 EGF-LIKE 3. FT DOMAIN 177 215 EGF-LIKE 4. FT DOMAIN 217 253 EGF-LIKE 5, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 255 291 EGF-LIKE 6. FT DOMAIN 293 329 EGF-LIKE 7, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 331 370 EGF-LIKE 8, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 372 408 EGF-LIKE 9, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 409 447 EGF-LIKE 10. FT DOMAIN 449 486 EGF-LIKE 11, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 488 524 EGF-LIKE 12, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 526 562 EGF-LIKE 13, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 564 600 EGF-LIKE 14, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 602 637 EGF-LIKE 15, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 639 675 EGF-LIKE 16, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 677 713 EGF-LIKE 17, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 715 751 EGF-LIKE 18, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 753 789 EGF-LIKE 19, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 791 827 EGF-LIKE 20, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 829 865 EGF-LIKE 21, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 867 905 EGF-LIKE 22. FT DOMAIN 907 944 EGF-LIKE 23, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 946 982 EGF-LIKE 24, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 984 1020 EGF-LIKE 25. FT DOMAIN 1022 1058 EGF-LIKE 26, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1060 1096 EGF-LIKE 27. FT DOMAIN 1098 1134 EGF-LIKE 28. FT DOMAIN 1136 1181 EGF-LIKE 29. FT DOMAIN 1183 1219 EGF-LIKE 30, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1221 1257 EGF-LIKE 31, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1259 1295 EGF-LIKE 32, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1297 1335 EGF-LIKE 33. FT DOMAIN 1337 1373 EGF-LIKE 34. FT DOMAIN 1375 1412 EGF-LIKE 35. FT DOMAIN 1415 1451 EGF-LIKE 36. FT REPEAT 1475 1513 LIN/NOTCH 1. FT REPEAT 1514 1553 LIN/NOTCH 2. FT REPEAT 1554 1593 LIN/NOTCH 3. FT REPEAT 1901 1945 ANK 1. FT REPEAT 1950 1979 ANK 2. FT REPEAT 1983 2013 ANK 3. FT REPEAT 2017 2046 ANK 4. FT REPEAT 2050 2079 ANK 5. FT REPEAT 2083 2112 ANK 6. FT DOMAIN 2486 2498 POLY-GLY. FT DOMAIN 2538 2568 POLY-GLN (OPA-REPEAT). FT DOMAIN 2664 2667 POLY-SER. FT DISULFID 62 73 BY SIMILARITY. FT DISULFID 67 83 BY SIMILARITY. FT DISULFID 85 94 BY SIMILARITY. FT DISULFID 100 111 BY SIMILARITY. FT DISULFID 105 124 BY SIMILARITY. FT DISULFID 126 135 BY SIMILARITY. FT DISULFID 143 154 BY SIMILARITY. FT DISULFID 148 164 BY SIMILARITY. FT DISULFID 166 175 BY SIMILARITY. FT DISULFID 181 192 BY SIMILARITY. FT DISULFID 186 203 BY SIMILARITY. FT DISULFID 205 214 BY SIMILARITY. FT DISULFID 221 232 BY SIMILARITY. FT DISULFID 226 241 BY SIMILARITY. FT DISULFID 243 252 BY SIMILARITY. FT DISULFID 259 270 BY SIMILARITY. FT DISULFID 264 279 BY SIMILARITY. FT DISULFID 281 290 BY SIMILARITY. FT DISULFID 297 308 BY SIMILARITY. FT DISULFID 302 317 BY SIMILARITY. FT DISULFID 319 328 BY SIMILARITY. FT DISULFID 335 349 BY SIMILARITY. FT DISULFID 343 358 BY SIMILARITY. FT DISULFID 360 369 BY SIMILARITY. FT DISULFID 376 387 BY SIMILARITY. FT DISULFID 381 396 BY SIMILARITY. FT DISULFID 398 407 BY SIMILARITY. FT DISULFID 413 424 BY SIMILARITY. FT DISULFID 418 435 BY SIMILARITY. FT DISULFID 437 446 BY SIMILARITY. FT DISULFID 453 465 BY SIMILARITY. FT DISULFID 459 474 BY SIMILARITY. FT DISULFID 476 485 BY SIMILARITY. FT DISULFID 492 503 BY SIMILARITY. FT DISULFID 497 512 BY SIMILARITY. FT DISULFID 514 523 BY SIMILARITY. FT DISULFID 530 541 BY SIMILARITY. FT DISULFID 535 550 BY SIMILARITY. FT DISULFID 552 561 BY SIMILARITY. FT DISULFID 568 579 BY SIMILARITY. FT DISULFID 573 588 BY SIMILARITY. FT DISULFID 590 599 BY SIMILARITY. FT DISULFID 606 616 BY SIMILARITY. FT DISULFID 611 625 BY SIMILARITY. FT DISULFID 627 636 BY SIMILARITY. FT DISULFID 643 654 BY SIMILARITY. FT DISULFID 648 663 BY SIMILARITY. FT DISULFID 665 674 BY SIMILARITY. FT DISULFID 681 692 BY SIMILARITY. FT DISULFID 686 701 BY SIMILARITY. FT DISULFID 703 712 BY SIMILARITY. FT DISULFID 719 730 BY SIMILARITY. FT DISULFID 724 739 BY SIMILARITY. FT DISULFID 741 750 BY SIMILARITY. FT DISULFID 757 768 BY SIMILARITY. FT DISULFID 762 777 BY SIMILARITY. FT DISULFID 779 788 BY SIMILARITY. FT DISULFID 795 806 BY SIMILARITY. FT DISULFID 800 815 BY SIMILARITY. FT DISULFID 817 826 BY SIMILARITY. FT DISULFID 833 844 BY SIMILARITY. FT DISULFID 838 853 BY SIMILARITY. FT DISULFID 855 864 BY SIMILARITY. FT DISULFID 871 882 BY SIMILARITY. FT DISULFID 876 893 BY SIMILARITY. FT DISULFID 895 904 BY SIMILARITY. FT DISULFID 911 923 BY SIMILARITY. FT DISULFID 917 932 BY SIMILARITY. FT DISULFID 934 943 BY SIMILARITY. FT DISULFID 950 961 BY SIMILARITY. FT DISULFID 955 970 BY SIMILARITY. FT DISULFID 972 981 BY SIMILARITY. FT DISULFID 988 999 BY SIMILARITY. FT DISULFID 993 1008 BY SIMILARITY. FT DISULFID 1010 1019 BY SIMILARITY. FT DISULFID 1026 1037 BY SIMILARITY. FT DISULFID 1031 1046 BY SIMILARITY. FT DISULFID 1048 1057 BY SIMILARITY. FT DISULFID 1064 1075 BY SIMILARITY. FT DISULFID 1069 1084 BY SIMILARITY. FT DISULFID 1086 1095 BY SIMILARITY. FT DISULFID 1102 1113 BY SIMILARITY. FT DISULFID 1107 1122 BY SIMILARITY. FT DISULFID 1124 1133 BY SIMILARITY. FT DISULFID 1140 1160 BY SIMILARITY. FT DISULFID 1155 1169 BY SIMILARITY. FT DISULFID 1171 1180 BY SIMILARITY. FT DISULFID 1187 1198 BY SIMILARITY. FT DISULFID 1192 1207 BY SIMILARITY. FT DISULFID 1209 1218 BY SIMILARITY. FT DISULFID 1225 1236 BY SIMILARITY. FT DISULFID 1230 1245 BY SIMILARITY. FT DISULFID 1247 1256 BY SIMILARITY. FT DISULFID 1263 1274 BY SIMILARITY. FT DISULFID 1268 1283 BY SIMILARITY. FT DISULFID 1285 1294 BY SIMILARITY. FT DISULFID 1301 1314 BY SIMILARITY. FT DISULFID 1306 1323 BY SIMILARITY. FT DISULFID 1325 1334 BY SIMILARITY. FT DISULFID 1341 1352 BY SIMILARITY. FT DISULFID 1346 1361 BY SIMILARITY. FT DISULFID 1363 1372 BY SIMILARITY. FT DISULFID 1379 1389 BY SIMILARITY. FT DISULFID 1384 1400 BY SIMILARITY. FT DISULFID 1402 1411 BY SIMILARITY. FT DISULFID 1419 1430 BY SIMILARITY. FT DISULFID 1424 1439 BY SIMILARITY. FT DISULFID 1441 1450 BY SIMILARITY. FT CARBOHYD 322 322 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 371 371 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 430 430 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 475 475 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1045 1045 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1157 1157 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1242 1242 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1271 1271 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1521 1521 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1594 1594 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1627 1627 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 578 578 I -> T. FT VARIANT 2044 2044 I -> R. FT VARIANT 2265 2265 A -> V. FT VARIANT 2407 2407 H -> R. FT VARIANT 2445 2445 R -> L. FT MUTAGEN 739 739 C->Y: IN MCD5; INDUCES LOSS OF FT MICROCHAETAE SENSORY PRECURSORS. FT MUTAGEN 2060 2060 A->V: IN SU42C; DELTEX-LIKE MUTATION THAT FT INDUCES OUTSTRECHED WINGS AND FT VARIABILITY-FUSED OCELLI. FT CONFLICT 9 9 R -> G (IN REF. 4). FT CONFLICT 84 84 A -> G (IN REF. 4). FT CONFLICT 103 103 M -> I (IN REF. 1). FT CONFLICT 119 119 R -> H (IN REF. 2). FT CONFLICT 231 231 T -> I (IN REF. 1). FT CONFLICT 240 240 Q -> R (IN REF. 4). FT CONFLICT 267 267 G -> A (IN REF. 1). FT CONFLICT 1561 1561 S -> T (IN REF. 1 AND 2). FT CONFLICT 2257 2257 G -> S (IN REF. 2). FT CONFLICT 2568 2568 Q -> QQ (IN REF. 4). FT CONFLICT 2577 2577 A -> E (IN REF. 5). SQ SEQUENCE 2703 AA; 288851 MW; 0EAE23F426FECD7B CRC64; MQSQRSRRRS RAPNTWICFW INKMHAVASL PASLPLLLLT LAFANLPNTV RGTDTALVAA SCTSVGCQNG GTCVTQLNGK TYCACDSHYV GDYCEHRNPC NSMRCQNGGT CQVTFRNGRP GISCKCPLGF DESLCEIAVP NACDHVTCLN GGTCQLKTLE EYTCACANGY TGERCETKNL CASSPCRNGA TCTALAGSSS FTCSCPPGFT GDTCSYDIEE CQSNPCKYGG TCVNTHGSYQ CMCPTGYTGK DCDTKYKPCS PSPCQNGGIC RSNGLSYECK CPKGFEGKNC EQNYDDCLGH LCQNGGTCID GISDYTCRCP PNFTGRFCQD DVDECAQRDH PVCQNGATCT NTHGSYSCIC VNGWAGLDCS NNTDDCKQAA CFYGATCIDG VGSFYCQCTK GKTGLLCHLD DACTSNPCHA DAICDTSPIN GSYACSCATG YKGVDCSEDI DECDQGSPCE HNGICVNTPG SYRCNCSQGF TGPRCETNIN ECESHPCQNE GSCLDDPGTF RCVCMPGFTG TQCEIDIDEC QSNPCLNDGT CHDKINGFKC SCALGFTGAR CQINIDDCQS QPCRNRGICH DSIAGYSCEC PPGYTGTSCE ININDCDSNP CHRGKCIDDV NSFKCLCDPG YTGYICQKQI NECESNPCQF DGHCQDRVGS YYCQCQAGTS GKNCEVNVNE CHSNPCNNGA TCIDGINSYK CQCVPGFTGQ HCEKNVDECI SSPCANNGVC IDQVNGYKCE CPRGFYDAHC LSDVDECASN PCVNEGRCED GINEFICHCP PGYTGKRCEL DIDECSSNPC QHGGTCYDKL NAFSCQCMPG YTGQKCETNI DDCVTNPCGN GGTCIDKVNG YKCVCKVPFT GRDCESKMDP CASNRCKNEA KCTPSSNFLD FSCTCKLGYT GRYCDEDIDE CSLSSPCRNG ASCLNVPGSY RCLCTKGYEG RDCAINTDDC ASFPCQNGGT CLDGIGDYSC LCVDGFDGKH CETDINECLS QPCQNGATCS QYVNSYTCTC PLGFSGINCQ TNDEDCTESS CLNGGSCIDG INGYNCSCLA GYSGANCQYK LNKCDSNPCL NGATCHEQNN EYTCHCPSGF TGKQCSEYVD WCGQSPCENG ATCSQMKHQF SCKCSAGWTG KLCDVQTISC QDAADRKGLS LRQLCNNGTC KDYGNSHVCY CSQGYAGSYC QKEIDECQSQ PCQNGGTCRD LIGAYECQCR QGFQGQNCEL NIDDCAPNPC QNGGTCHDRV MNFSCSCPPG TMGIICEINK DDCKPGACHN NGSCIDRVGG FECVCQPGFV GARCEGDINE CLSNPCSNAG TLDCVQLVNN YHCNCRPGHM GRHCEHKVDF CAQSPCQNGG NCNIRQSGHH CICNNGFYGK NCELSGQDCD SNPCRVGNCV VADEGFGYRC ECPRGTLGEH CEIDTLDECS PNPCAQGAAC EDLLGDYECL CPSKWKGKRC DIYDANYPGW NGGSGSGNDR YAADLEQQRA MCDKRGCTEK QGNGICDSDC NTYACNFDGN DCSLGINPWA NCTANECWNK FKNGKCNEEC NNAACHYDGH DCERKLKSCD SLFDAYCQKH YGDGFCDYGC NNAECSWDGL DCENKTQSPV LAEGAMSVVM LMNVEAFREI QAQFLRNMSH MLRTTVRLKK DALGHDIIIN WKDNVRVPEI EDTDFARKNK ILYTQQVHQT GIQIYLEIDN RKCTECFTHA VEAAEFLAAT AAKHQLRNDF QIHSVRGIKN PGDEDNGEPP ANVKYVITGI ILVIIALAFF GMVLSTQRKR AHGVTWFPEG FRAPAAVMSR RRRDPHGQEM RNLNKQVAMQ SQGVGQPGAH WSDDESDMPL PKRQRSDPVS GVGLGNNGGY ASDHTMVSEY EEADQRVWSQ AHLDVVDVRA IMTPPAHQDG GKHDVDARGP CGLTPLMIAA VRGGGLDTGE DIENNEDSTA QVISDLLAQG AELNATMDKT GETSLHLAAR FARADAAKRL LDAGADANCQ DNTGRTPLHA AVAADAMGVF QILLRNRATN LNARMHDGTT PLILAARLAI EGMVEDLITA DADINAADNS GKTALHWAAA VNNTEAVNIL LMHHANRDAQ DDKDETPLFL AAREGSYEAC KALLDNFANR EITDHMDRLP RDVASERLHH DIVRLLDEHV PRSPQMLSMT PQAMIGSPPP GQQQPQLITQ PTVISAGNGG NNGNGNASGK QSNQTAKQKA AKKAKLIEGS PDNGLDATGS LRRKASSKKT SAASKKAANL NGLNPGQLTG GVSGVPGVPP TNSAAQAAAA AAAAVAAMSH ELEGSPVGVG MGGNLPSPYD TSSMYSNAMA APLANGNPNT GAKQPPSYED CIKNAQSMQS LQGNGLDMIK LDNYAYSMGS PFQQELLNGQ GLGMNGNGQR NGVGPGVLPG GLCGMGGLSG AGNGNSHEQG LSPPYSNQSP PHSVQSSLAL SPHAYLGSPS PAKSRPSLPT SPTHIQAMRH ATQQKQFGGS NLNSLLGGAN GGGVVGGGGG GGGGVGQGPQ NSPVSLGIIS PTGSDMGIML APPQSSKNSA IMQTISPQQQ QQQQQQQQQQ HQQQQQQQQQ QQQQQQQQLG GLEFGSAGLD LNGFCGSPDS FHSGQMNPPS IQSSMSGSSP STNMLSPSSQ HNQQAFYQYL TPSSQHSGGH TPQHLVQTLD SYPTPSPESP GHWSSSSPRS NSDWSEGVQS PAANNLYISG GHQANKGSEA IYI // ID NPSN_DROME STANDARD; PRT; 273 AA. AC Q9VXK0; Q9U5W0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NipSnap protein. GN NIPSNAP OR CG9212. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 1-193 FROM N.A. RA Kedra D., Dumanski J.P.; RT "Cloning of NIPSNAP gene orthologues in Danio rerio and Drosophila RT melanogaster."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE NIPSNAP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003501; AAF48562.2; -. DR EMBL; AY061048; AAL28596.1; -. DR EMBL; AJ249798; CAB56699.1; -. DR FlyBase; FBgn0030724; Nipsnap. FT CONFLICT 191 193 NNW -> KQT (IN REF. 4). SQ SEQUENCE 273 AA; 31965 MW; 3F7DEBB24670636D CRC64; MLKLRNLLAV GKSNNNAVRS LSTTPSRNDS ESWFSKLLVR KIEPTKESHS RMLSDKEIIY ALHTHNVRPD SMGSYLNNYK TTVALINEKK ANLSCELVAS WTVQVGDMDQ CLHLWKYTGG FEKIDQAKED LWNDPEYLSL MQERSKFLRS RHLQYLLAFS YWPQIASRTG KNIYEMRSYR LTPGTMIEWG NNWARAINYR KHNNEAFAGF FSQIGRLYNV HHIWCYKSLQ DRKETREAAW RSPGWDECVA YTVPLIREMH CRVLAPTEFS PSQ // ID NRG_DROME STANDARD; PRT; 1302 AA. AC P20241; O61541; O61542; Q24414; Q24415; Q95U64; Q9V3X0; DT 01-FEB-1991 (Rel. 17, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Neuroglian precursor. GN NRG OR CG1634. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM SHORT), AND SEQUENCE OF 24-41 AND 737-751. RX MEDLINE=90030418; PubMed=2805067; RA Bieber A.J., Snow P.M., Hortsch M., Patel N.H., Jacobs J.R., RA Traquina Z.R., Schilling J., Goodman C.S.; RT "Drosophila neuroglian: a member of the immunoglobulin superfamily RT with extensive homology to the vertebrate neural adhesion molecule RT L1."; RL Cell 59:447-460(1989). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=98332718; PubMed=9666073; RA Zhao G., Hortsch M.; RT "The analysis of genomic structures in the L1 family of cell adhesion RT proteins provides no evidence for exon shuffling events after the RT separation of arthropod and chordate lineages."; RL Gene 215:47-55(1998). RN [3] RP REVISIONS. RA Hortsch M.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE OF 1182-1302 FROM N.A., FUNCTION, ALTERNATIVE SPLICING, AND RP TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=90262720; PubMed=1693086; RA Hortsch M., Bieber A.J., Patel N.H., Goodman C.S.; RT "Differential splicing generates a nervous system-specific form of RT Drosophila neuroglian."; RL Neuron 4:697-709(1990). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 610-814. RX MEDLINE=94213741; PubMed=7512815; RA Huber A.H., Wang Y.-M.E., Bieber A.J., Bjorkman P.J.; RT "Crystal structure of tandem type III fibronectin domains from RT Drosophila neuroglian at 2.0 A."; RL Neuron 12:717-731(1994). CC -!- FUNCTION: THE LONG ISOFORM MAY PLAY A ROLE IN NEURAL AND GLIAL CC CELL ADHESION IN THE DEVELOPING EMBRYO. THE SHORT ISOFORM MAY BE A CC MORE GENERAL CELL ADHESION MOLECULE INVOLVED IN OTHER TISSUES AND CC IMAGINAL DISK MORPHOGENESIS. VITAL FOR EMBRYONIC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P20241-1; Sequence=Displayed; CC Name=Short; CC IsoId=P20241-2; Sequence=VSP_002601, VSP_002602; CC -!- TISSUE SPECIFICITY: LONG ISOFORM IS RESTRICTED TO SURFACE OF CC NEURONS AND GLIA IN THE DEVELOPING NERVOUS SYSTEM AND THE SHORT CC ISOFORM TO OTHER NONNEURONAL TISSUES. CC -!- SIMILARITY: CONTAINS 6 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -!- SIMILARITY: CONTAINS 5 FIBRONECTIN TYPE III DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28231; AAA28728.2; -. DR EMBL; AF050085; AAC28613.2; -. DR EMBL; AF050084; AAC28613.2; JOINED. DR EMBL; AF050085; AAC28614.2; -. DR EMBL; AF050084; AAC28614.2; JOINED. DR EMBL; AE003444; AAF46387.1; -. DR EMBL; AY058284; AAL13513.1; -. DR EMBL; X76243; CAA53822.1; -. DR EMBL; X76244; CAA53823.1; -. DR PIR; A32579; A32579. DR PDB; 1CFB; 30-NOV-94. DR FlyBase; FBgn0002968; Nrg. DR GO; GO:0005886; C:plasma membrane; IEP. DR GO; GO:0005194; F:cell adhesion molecule activity; IMP. DR GO; GO:0007560; P:imaginal disc morphogenesis; IMP. DR GO; GO:0007158; P:neuronal cell adhesion; IMP. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003961; FN_III. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR Pfam; PF00041; fn3; 5. DR Pfam; PF00047; ig; 6. DR SMART; SM00060; FN3; 5. DR SMART; SM00408; IGc2; 4. DR PROSITE; PS50835; IG_LIKE; 6. KW Cell adhesion; Glycoprotein; Transmembrane; Repeat; 3D-structure; KW Immunoglobulin domain; Signal; Developmental protein; KW Alternative splicing. FT SIGNAL 1 23 FT CHAIN 24 1302 NEUROGLIAN. FT DOMAIN 24 1138 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1139 1154 POTENTIAL. FT DOMAIN 1155 1302 CYTOPLASMIC (POTENTIAL). FT DOMAIN 29 133 IG-LIKE C2-TYPE 1. FT DOMAIN 134 225 IG-LIKE C2-TYPE 2. FT DOMAIN 245 330 IG-LIKE C2-TYPE 3. FT DOMAIN 339 426 IG-LIKE C2-TYPE 4. FT DOMAIN 432 524 IG-LIKE C2-TYPE 5. FT DOMAIN 521 610 IG-LIKE C2-TYPE 6. FT DOMAIN 629 690 FIBRONECTIN TYPE-III 1. FT DOMAIN 729 792 FIBRONECTIN TYPE-III 2. FT DOMAIN 832 896 FIBRONECTIN TYPE-III 3. FT DOMAIN 932 997 FIBRONECTIN TYPE-III 4. FT DOMAIN 1024 1098 FIBRONECTIN TYPE-III 5. FT DISULFID 59 111 POTENTIAL. FT DISULFID 625 706 FT CARBOHYD 182 182 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 198 198 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 411 411 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 448 448 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 652 652 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 683 683 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 821 821 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1125 1125 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1224 1239 QFTEDGSFIGQYVPGK -> MNEDGSFIGQYGRKGL (in FT isoform Short). FT /FTId=VSP_002601. FT VARSPLIC 1240 1302 Missing (in isoform Short). FT /FTId=VSP_002602. FT CONFLICT 85 86 NR -> KP (IN REF. 2). FT CONFLICT 1282 1282 MISSING (IN REF. 6). FT STRAND 619 625 FT STRAND 629 635 FT TURN 640 641 FT STRAND 646 653 FT TURN 657 658 FT STRAND 661 668 FT TURN 669 670 FT STRAND 673 677 FT STRAND 682 692 FT TURN 693 694 FT STRAND 695 696 FT STRAND 706 708 FT STRAND 721 723 FT TURN 727 728 FT STRAND 730 733 FT HELIX 739 741 FT TURN 742 742 FT STRAND 748 755 FT TURN 758 759 FT STRAND 763 767 FT TURN 770 771 FT STRAND 774 777 FT STRAND 785 794 FT TURN 795 796 FT STRAND 797 798 FT STRAND 806 809 SQ SEQUENCE 1302 AA; 143617 MW; 59BD9DF286756F1A CRC64; MWRQSTILAA LLVALLCAGS AESKGNRPPR ITKQPAPGEL LFKVAQQNKE SDNPFIIECE ADGQPEPEYS WIKNGKKFDW QAYDNRMLRQ PGRGTLVITI PKDEDRGHYQ CFASNEFGTA TSNSVYVRKA ELNAFKDEAA KTLEAVEGEP FMLKCAAPDG FPSPTVNWMI QESIDGSIKS INNSRMTLDP EGNLWFSNVT REDASSDFYY ACSATSVFRS EYKIGNKVLL DVKQMGVSAS QNKHPPVRQY VSRRQSLALR GKRMELFCIY GGTPLPQTVW SKDGQRIQWS DRITQGHYGK SLVIRQTNFD DAGTYTCDVS NGVGNAQSFS IILNVNSVPY FTKEPEIATA AEDEEVVFEC RAAGVPEPKI SWIHNGKPIE QSTPNPRRTV TDNTIRIINL VKGDTGNYGC NATNSLGYVY KDVYLNVQAE PPTISEAPAA VSTVDGRNVT IKCRVNGSPK PLVKWLRASN WLTGGRYNVQ ANGDLEIQDV TFSDAGKYTC YAQNKFGEIQ ADGSLVVKEH TRITQEPQNY EVAAGQSATF RCNEAHDDTL EIEIDWWKDG QSIDFEAQPR FVKTNDNSLT IAKTMELDSG EYTCVARTRL DEATARANLI VQDVPNAPKL TGITCQADKA EIHWEQQGDN RSPILHYTIQ FNTSFTPASW DAAYEKVPNT DSSFVVQMSP WANYTFRVIA FNKIGASPPS AHSDSCTTQP DVPFKNPDNV VGQGTEPNNL VISWTPMPEI EHNAPNFHYY VSWKRDIPAA AWENNNIFDW RQNNIVIADQ PTFVKYLIKV VAINDRGESN VAAEEVVGYS GEDRPLDAPT NFTMRQITSS TSGYMAWTPV SEESVRGHFK GYKIQTWTEN EGEEGLREIH VKGDTHNALV TQFKPDSKNY ARILAYNGRF NGPPSAVIDF DTPEGVPSPV QGLDAYPLGS SAFMLHWKKP LYPNGKLTGY KIYYEEVKES YVGERREYDP HITDPRVTRM KMAGLKPNSK YRISITATTK MGEGSEHYIE KTTLKDAVNV APATPSFSWE QLPSDNGLAK FRINWLPSTE GHPGTHFFTM HRIKGETQWI RENEEKNSDY QEVGGLDPET AYEFRVVSVD GHFNTESATQ EIDTNTVEGP IMVANETVAN AGWFIGMMLA LAFIIILFII ICIIRRNRGG KYDVHDRELA NGRRDYPEEG GFHEYSQPLD NKSAGRQSVS SANKPGVESD TDSMAEYGDG DTGQFTEDGS FIGQYVPGKL QPPVSPQPLN NSAAAHQAAP TAGGSGAAGS AAAAGASGGA SSAGGAAASN GGAAAGAVAT YV // ID NRT_DROME STANDARD; PRT; 846 AA. AC P23654; DT 01-NOV-1991 (Rel. 20, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Neurotactin. GN NRT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91301057; PubMed=2100266; RA Hortsch M., Patel N.P., Bieber A.J., Traquina Z.R., Goodman C.S.; RT "Drosophila neurotactin, a surface glycoprotein with homology to RT serine esterases, is dynamically expressed during embryogenesis."; RL Development 110:1327-1340(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=91006059; PubMed=2120047; RA de la Escalera S., Bockamp E.O., Moya F., Piovant M., Jimenez F.; RT "Characterization and gene cloning of neurotactin, a Drosophila RT transmembrane protein related to cholinesterases."; RL EMBO J. 9:3593-3601(1990). RN [3] RP FUNCTION. RX MEDLINE=91006060; PubMed=2120048; RA Barthalay Y., Hipeau-Jacquotte R., de la Escalera S., Jimenez F., RA Piovant M.; RT "Drosophila neurotactin mediates heterophilic cell adhesion."; RL EMBO J. 9:3603-3609(1990). CC -!- FUNCTION: MAY MEDIATE OR MODULATE CELL ADHESION BETWEEN EMBRYONIC CC CELLS DURING DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN MEMBRANES DURING EMBRYOGENESIS CC AND THEN ACCUMULATES IN CNS AND PNS. CC -!- PTM: PHOSPHORYLATED. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE TYPE-B CC CARBOXYLESTERASE/LIPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53837; CAA37831.1; -. DR EMBL; X54999; CAA38746.1; -. DR PIR; S12005; S12005. DR PIR; S13795; S13795. DR HSSP; P37967; 1QE3. DR FlyBase; FBgn0004108; Nrt. DR GO; GO:0016323; C:basolateral plasma membrane; NAS. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00135; COesterase; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. KW Cell adhesion; Glycoprotein; Transmembrane; Phosphorylation; KW Signal-anchor. FT DOMAIN 1 324 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 325 346 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 347 846 EXTRACELLULAR (POTENTIAL). FT MOD_RES 28 28 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 75 75 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 103 103 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 169 169 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 186 186 PHOSPHORYLATION (POTENTIAL). FT DISULFID 422 437 BY SIMILARITY. FT DISULFID 600 605 BY SIMILARITY. FT DISULFID 738 830 BY SIMILARITY. FT CARBOHYD 410 410 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 417 417 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 428 428 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 636 636 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 691 691 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 720 720 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 250 250 G -> S (IN REF. 2). FT CONFLICT 555 555 S -> T (IN REF. 2). FT CONFLICT 567 567 F -> Y (IN REF. 2). SQ SEQUENCE 846 AA; 92745 MW; F5EC54904D1D0657 CRC64; MGELEEKETP PTETTAAQQE ALEEPKETDK MLDKKEDAKE KTPSPQTSKP ASPNAGKKSS PVAEKKIDDA ELAKSKSGNG EEIIDIPAEN GTKPDSADDK KISKEEREVK PKKIPIGGLK LPGFFMKNKP KADGDGAEGE LLEKEKEEDK DKEANGDAAT GSGKDEQKSR PGLGERLRSF FARKPSAEKE KKQLVNGDAD AKSEATAEAT PAEDASDAPP KRGLLNAIKL PIANMIPKKK SNDDVELGLG KAGLASMETL DDSLKDQDTV DRAPVKTNGT EELKGELKDE KLAAEEKLAA EEEEQNRPVS LLTRLRGYKC SVDDALIVFG ILLFVLLLGV IGYVLTHETL TSPPLREGRY IMAVTGCGPV EGVKEDGAFA FRGIPYAKPP VDRLRWKPAE LIDDINMCWN DTLQTHNSSV VCTQRLGNGT TVGDEDCLYL DVVTPHVRYN NPLPVVVLIG AESLAGPSPG ILRPSARYSR SHDVIFVRPN FRLGVFGFLA LDALTKEAHP PTSGNYALTD IIAVLNWIKL NIVHFGGDPQ SVTLLGHRAG ATLVSLLVNS QKVKGLFTRA WASSGSAILP GKPLSESGKQ NEQLMATLEC ADIQCLREAS SERLWAATPD TWLHFPVDLP QPQEANASGS RHEWLVLDGD VVFEHPSDTW KREQANDKPV LVMGATAHEA HTEKLRELHA NWTREEVRAY LENSQIGALG LTDEVIEKYN ASSYASLVSI ISDIRSVCPL LTNARQQPSV PFYVVTQGEG PDQLATVDAD VQAILGRYEP HTVEQRRFVS AMQQLFYYYV SHGTVQSFVQ NRRVINVGQD AQPEEDYLPC NYWISKDIVP RYARVD // ID NRX4_DROME STANDARD; PRT; 1284 AA. AC Q94887; Q9VTU5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Neurexin IV precursor. GN NRX OR CG6827. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97133213; PubMed=8978610; RA Baumgartner S.W., Littleton J.T., Broadie K., Bhat M.A., Harbecke R., RA Lengyel J.A., Chiquet-Ehrismann R., Prokop A., Bellen H.J.; RT "A Drosophila neurexin is required for septate junction and blood- RT nerve barrier formation and function."; RL Cell 87:1059-1068(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP INTERACTION WITH CORACLE. RX MEDLINE=98177173; PubMed=9508778; RA Ward R.E. IV, Lamb R.S., Fehon R.G.; RT "A conserved functional domain of Drosophila coracle is required for RT localization at the septate junction and has membrane-organizing RT activity."; RL J. Cell Biol. 140:1463-1473(1998). RN [4] RP INTERACTION WITH DISCS LOST. RX MEDLINE=99200394; PubMed=10102271; RA Bhat M.A., Izaddoost S., Lu Y., Cho K.O., Choi K.W., Bellen H.J.; RT "Discs Lost, a novel multi-PDZ domain protein, establishes and RT maintains epithelial polarity."; RL Cell 96:833-845(1999). CC -!- FUNCTION: SEEMS TO PLAY A ROLE IN THE FORMATION AND FUNCTION OF CC SEPTATE JUNCTIONS. IS REQUIRED FOR THE BLOOD-BRAIN BARRIER CC FORMATION. CC -!- SUBUNIT: THE C-TERMINAL REGION INTERACTS WITH CORACLE. INTERACTS CC WITH DISCS LOST IN CIS FORM. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: FOUND IN SEPTATE JUNCTIONS OF EPITHELIAL AND CC GLIAL CELLS. CC -!- SIMILARITY: CONTAINS 2 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 F5/8 TYPE C DOMAIN. CC -!- SIMILARITY: CONTAINS 4 LAMININ G-LIKE DOMAINS. CC -!- SIMILARITY: BELONGS TO THE NEUREXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86685; CAA60383.1; -. DR EMBL; AE003542; AAF49951.1; -. DR PIR; T13799; T13799. DR HSSP; P00740; 1EDM. DR FlyBase; FBgn0013997; Nrx. DR GO; GO:0005887; C:integral to plasma membrane; NAS. DR GO; GO:0005918; C:septate junction; NAS. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0016081; P:synaptic vesicle docking; NAS. DR GO; GO:0016080; P:synaptic vesicle targeting; NAS. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR000421; FA58_C. DR InterPro; IPR008979; Gal_bind_like. DR InterPro; IPR006210; IEGF. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR003585; Neurexin-like. DR Pfam; PF00008; EGF; 2. DR Pfam; PF00754; F5_F8_type_C; 1. DR Pfam; PF00054; laminin_G; 2. DR SMART; SM00294; 4.1m; 1. DR SMART; SM00181; EGF; 2. DR SMART; SM00231; FA58C; 1. DR SMART; SM00282; LamG; 4. DR PROSITE; PS00022; EGF_1; FALSE_NEG. DR PROSITE; PS01186; EGF_2; FALSE_NEG. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS01285; FA58C_1; 1. DR PROSITE; PS01286; FA58C_2; 1. DR PROSITE; PS50022; FA58C_3; 1. DR PROSITE; PS50025; LAM_G_DOMAIN; 4. KW EGF-like domain; Glycoprotein; Cell adhesion; Signal; Transmembrane; KW Repeat. FT SIGNAL 1 35 POTENTIAL. FT CHAIN 36 1284 NEUREXIN IV. FT DOMAIN 36 1217 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1218 1238 POTENTIAL. FT DOMAIN 1239 1284 CYTOPLASMIC (POTENTIAL). FT DOMAIN 47 185 F5/8 TYPE C. FT DOMAIN 220 369 LAMININ G-LIKE 1. FT DOMAIN 403 540 LAMININ G-LIKE 2. FT DOMAIN 542 579 EGF-LIKE 1. FT DOMAIN 824 962 LAMININ G-LIKE 3. FT DOMAIN 962 999 EGF-LIKE 2. FT DOMAIN 1032 1183 LAMININ G-LIKE 4. FT CONFLICT 1 4 MRPP -> MSA (IN REF. 1). FT CONFLICT 926 926 E -> D (IN REF. 1). SQ SEQUENCE 1284 AA; 145467 MW; 9372C71AC70E3D56 CRC64; MRPPRSNTKA AFSSLQFGLL CLLLLVNNGI KSVQADAFTD YFSDYDCNQP LMERAVLTAT SSLTERGPDK ARLNGNAAWT PVENTYNHFL TLDLGDPRMV RKIATMGRMH TDEFVTEYIV QYSDDGEFWR SYVNPTSEPQ MFKGNSDGNS IHYNVFEVPI IAQWVRINPT RWHDRISMRV ELYGCDYISE NLYFNGTGLV RYDLRREPIT STKESIRFRF KTAFANGVMM YSRGTQGDYY ALQLKDNKMV LNLDLGSRVM TSLSVGSLLD DNVWHDVVIS RNQRDIIFSV DRVIVRGRIQ GEFTRLNLNR ELYLGGVPNV QEGLIVQQNF SGCLENIYFN STNFIRVMKD STELGEGYLF TRVNTIYACP SPPIYPVTFT TRSSFVRLKG YENSQRLNVS FYFRTYEETG VMLHHDFYSG GYLKVFLEFG KVKIDLKVKD KARIILDNYD DQFNDGKWHS FVISIEKNRL ILNIDQRPMT TTKSMQVATG AQYYIAGGKD KNGFVGCMRL ISVDGNYKLP QDWVKGEEVC CGDDVVVDAC QMIDRCNPNP CQHKGLCHQN SREFFCDCGH TGYAGAVCHT SNNPLSCLAL KNVQHVQQRV NLNLDVDGSG PLEPFPVTCE FYSDGRVITT LSHSQEHTTT VDGFQEPGSF EQSIMYDANQ LQIEALLNRS HSCWQRLSYS CRSSRLFNSP SEAGNFRPFS WWISRHNQPM DYWAGALPGS RKCECGILGK CHDPTKWCNC DSNSLEWMED GGDIREKEYL PVRAVKFGDT GTPLDEKMGR YTLGPLRCEG DDLFSNVVTF RIADASINLP PFDMGHSGDI YLEFRTTQEN SVIFHATGPT DYIKLSLNGG NKLQFQYQAG SGPLGVNVGT SYHLNDNNWH TVSVERNRKE ARLVVDGSIK AEVREPPGPV RALHLTSDLV IGATTEYRDG YVGCIRALLL NGKMVDLKEY SKRGLYGIST GCVGRCESNP CLNNGTCIER YDGYSCDCRW SAFKGPICAD EIGVNLRSSS IIRYEFEGSF RSTIAENIRV GFTTTIPKGF LLGFSSNLTG EYLTIQISNS GHLRCVFDFG FERQEIIFPK KHFGLGQYHD MHFMRKNGGS TVVLKVDNYE PVEYNFDIKA SADAQFNNIQ YMYIGKNESM TDGFVGCVSR VQFDDIYPLK LMFQQNPPKN VKSLGTQLTE DFCGVEPVTH PPIEIETRPP PLVDEEKLRK AYNEVDSVLL ACLLVILFLL LILMFFLIGR YLHRHKGDYL THEDQGADGA DDPDDAVLHS TTGHQVRKRT EIFI // ID NSF1_DROME STANDARD; PRT; 745 AA. AC P46461; Q9VYF4; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Vesicular-fusion protein Nsf1 (N-ethylmaleimide-sensitive fusion DE protein 1) (NEM-sensitive fusion protein 1) (dNsf-1) (Comatose DE protein). GN COMT OR NSF1 OR NSF-1 OR NSF OR CG1618. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=94261657; PubMed=8202553; RA Ordway R.W., Pallanck L., Ganetzky B.; RT "Neurally expressed Drosophila genes encoding homologs of the NSF and RT SNAP secretory proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5715-5719(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR VESICLE-MEDIATED TRANSPORT. CATALYZES THE CC FUSION OF TRANSPORT VESICLES WITHIN THE GOLGI CISTERNAE. IS ALSO CC REQUIRED FOR TRANSPORT FROM THE ENDOPLASMIC RETICLUM TO THE GOLGI CC STACK. SEEM TO FUNCTION AS A FUSION PROTEIN REQUIRED FOR THE CC DELIVERY OF CARGO PROTEINS TO ALL COMPARTMENTS OF THE GOLGI STACK CC INDEPENDENT OF VESICLE ORIGIN. CC -!- COFACTOR: BINDS 1 MAGNESIUM PER SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: HOMOHEXAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: NERVOUS SYSTEM. CC -!- SIMILARITY: BELONGS TO THE AAA ATPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U09373; AAA83413.1; -. DR EMBL; AE003492; AAF48244.2; -. DR EMBL; BT010259; AAQ23577.1; -. DR HSSP; P18708; 1NSF. DR FlyBase; FBgn0000346; comt. DR GO; GO:0005737; C:cytoplasm; NAS. DR GO; GO:0007030; P:Golgi organization and biogenesis; IMP. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016082; P:synaptic vesicle priming; NAS. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR InterPro; IPR009010; Asp_decarb_fold. DR InterPro; IPR003338; ATPaseVAT_N. DR InterPro; IPR004201; Cdc48_2. DR Pfam; PF00004; AAA; 2. DR Pfam; PF02933; cdc48_2; 1. DR Pfam; PF02359; cdc48_N; 1. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00674; AAA; 1. KW Transport; Protein transport; Endoplasmic reticulum; Golgi stack; KW ATP-binding; Metal-binding; Magnesium; Repeat; Multigene family. FT NP_BIND 260 267 ATP (POTENTIAL). FT NP_BIND 543 550 ATP (POTENTIAL). FT METAL 550 550 MAGNESIUM. SQ SEQUENCE 745 AA; 82555 MW; A34E7B037E91769F CRC64; MAYILKATKC PTDELSLTNR AIVNVGDFPE EIKYADISPA PGQHFIFALE KTVEVPSGYV GFSLVQRKWA MVSINQELEV RPYRFDASSD VITCVSFETD FLQKKTVSQE PYDSDQMAKE FIMQFAGMAL TVGQSLVFNF KDKKLLGLAV KSLEAIDPKS LGEGKDTAMR NVRFGRILGN TVVQFEKAEN SSLNLQGKSK GKVVRQSIIN PDWDFGKMGI GGLDKEFNSI FRRAFASRVF PPELVEQLGC KHVKGILLYG PPGTGKTLMA RQIGTMLNAR EPKIVNGPQI LDKYVGESEA NVRRLFAEAE EEEKRLGPNS GLHIIIFDEI DAICKQRGSV AGNSGVHDTV VNQLLTKIDG VDQLNNILVI GMTNRRDMID EALLRPGRLE VQMEISLPNE QGRVQILNIH TKRMREFNKI NDDVDNKEIA ALTKNFSGAE LEGLVRAAQS SAMNRLIKAD AKVTVDPEAM EKLKVNRDDF LHSLEHDIKP AFGTAQEILD NMLARGVINW GAPVSNLLED GMLYVQQAKA PESSGLVSVL VAGAPNSGKT ALAAQLAKMS DFPFVKVCSP EDMVGYTESA KCLHIRKIFD DAYRSMLSCI VVDNVERLLD YGSIGPRYSN MTLQALLVLL KKQPPKGRKL LILCTSSRRE VLEEMEMLTA FTSVLHVPNL SKPDHVLAVL ENTDIFSKGE IQAIGKKMAG KRVFIGIKKL LGLIDMARQT EQSQRAIKFL SKMEEEGGLD MVARQ // ID NSF2_DROME STANDARD; PRT; 752 AA. AC P54351; Q9VFQ5; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vesicular-fusion protein Nsf2 (N-ethylmaleimide-sensitive fusion DE protein 2) (NEM-sensitive fusion protein 2) (dNsf-2). GN NSF2 OR NSF-2 OR CG33101/CG9931. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95370175; PubMed=7642522; RA Pallanck L., Ordway R.W., Ramaswami M., Chi W.Y., Krishnan K.S., RA Ganetzky B.; RT "Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) RT suggested by the identification of a second Drosophila NSF homolog."; RL J. Biol. Chem. 270:18742-18744(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 9-752 FROM N.A. RC TISSUE=Head; RX MEDLINE=95350218; PubMed=7624376; RA Boulianne G.L., Trimble W.S.; RT "Identification of a second homolog of N-ethylmaleimide-sensitive RT fusion protein that is expressed in the nervous system and secretory RT tissues of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7095-7099(1995). CC -!- FUNCTION: REQUIRED FOR VESICLE-MEDIATED TRANSPORT. CATALYZES THE CC FUSION OF TRANSPORT VESICLES WITHIN THE GOLGI CISTERNAE. IS ALSO CC REQUIRED FOR TRANSPORT FROM THE ENDOPLASMIC RETICLUM TO THE GOLGI CC STACK. SEEM TO FUNCTION AS A FUSION PROTEIN REQUIRED FOR THE CC DELIVERY OF CARGO PROTEINS TO ALL COMPARTMENTS OF THE GOLGI STACK CC INDEPENDENT OF VESICLE ORIGIN (BY SIMILARITY). CC -!- SUBUNIT: HOMOHEXAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: NERVOUS SYSTEM AND SECRETORY TISSUES. CC -!- DEVELOPMENTAL STAGE: THE HIGHEST LEVELS ARE DETECTED IN EMBRYOS CC BEFORE AND DURING CELLULARIZATION. AFTER ONSET OF GASTRULATION THE CC HIGHEST LEVELS OF EXPRESSION APPEAR IN EMBRYONIC REGIONS THAT GIVE CC RISE TO ENDODERMAL AND ECTODERMAL TISSUES INCLUDING THE MIDGUT AND CC HINDGUT. CC -!- SIMILARITY: BELONGS TO THE AAA ATPASE FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-9 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U30502; AAA75044.1; -. DR EMBL; AE003702; AAF54995.2; -. DR EMBL; U28836; AAC46844.1; -. DR HSSP; P18708; 1NSF. DR FlyBase; FBgn0013998; Nsf2. DR GO; GO:0005737; C:cytoplasm; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016082; P:synaptic vesicle priming; NAS. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR InterPro; IPR003338; ATPaseVAT_N. DR InterPro; IPR004201; Cdc48_2. DR Pfam; PF00004; AAA; 2. DR Pfam; PF02933; cdc48_2; 1. DR Pfam; PF02359; cdc48_N; 1. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00674; AAA; 1. KW Transport; Protein transport; Endoplasmic reticulum; Golgi stack; KW ATP-binding; Repeat; Multigene family. FT NP_BIND 265 272 ATP (POTENTIAL). FT NP_BIND 548 555 ATP (POTENTIAL). FT CONFLICT 680 680 H -> N (IN REF. 2). SQ SEQUENCE 752 AA; 83457 MW; 0D76008F65A318AF CRC64; MSIEKAHRMR AIKCPTDELS LTNKAIVNVS DFTEEVKYVD ISPGPGLHYI FALEKISGPE LPLGHVGFSL VQRKWATLSI NQEIDVRPYR FDASADIITL VSFETDFLQK KTTTQEPYDS DEMAKEFLMQ FAGMPLTVGQ TLVFQFKDKK FLGLAVKTLE AVDPRTVGDS LPKTRNVRFG RILGNTVVQF EKAENSVLNL QGRSKGKIVR QSIINPDWDF GKMGIGGLDK EFNAIFRRAF ASRVFPPELV EQLGIKHVKG ILLYGPPGTG KTLMARQIGT MLNAREPKIV NGPQILDKYV GESEANIRRL FAEAEEEEKR LGPNSGLHII IFDEIDAICK ARGSVAGNSG VHDTVVNQLL AKIDGVEQLN NILVIGMTNR RDMIDEALLR PGRLEVQMEI SLPNEQGRVQ ILNIHTKRMR DFNKIASDVD NNEIAAKTKN FSGAELEGLV RAAQSTAMNR LIKADSKVHV DPEAMEKLRV TRADFLHALD NDIKPAFGAA QEMLENLLAR GIINWGPPVT ELLEDGMLSV QQAKATESSG LVSVLIEGAP NSGKSALAAN LAQLSDFPFV KVCSPEDMVG FTESAKCLHI RKIFDDAYRS TLSCIVVDNV ERLLDYGPIG PRYSNLTLQA LLVLLKKQPP KGRKLLILCT SSRRDVLEEM EMLSAFTSVL HVSNLSTPEH VLAVLDDSDL FSPEELQSIA RKMAGKRLCI GIKKLLALID MIRQSEPHQR VIKFLSKMEE EGGLEMDRVQ GH // ID NT53_DROME STANDARD; PRT; 484 AA. AC P82149; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Lethal(2)neighbour of tid protein 2 (NOT53). GN L(2)NOT2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=apxo; RX MEDLINE=98038975; PubMed=9373138; RA Kurzik-Dumke U., Kaymer M., Gundacker D., Debes A., Labitzke K.; RT "Gene within gene configuration and expression of the Drosophila RT melanogaster genes lethal(2) neighbour of tid [l(2)not] and lethal(2) RT relative of tid."; RL Gene 200:45-58(1997). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: EXPRESSED ONLY IN EMBRYOS. CC -!- MISCELLANEOUS: IN STRAINS HARVICH AND APXO, THERE ARE 2 GENES CC WHICH CODE FOR L(2)NOT PROTEIN. THEY DIFFER IN THEIR C-TERMINUS. CC -!- SIMILARITY: BELONGS TO THE ALG3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y10074; CAA71168.1; -. DR EMBL; X95244; CAA64533.1; -. DR FlyBase; FBgn0011297; l(2)not. DR InterPro; IPR007873; ALG3. DR Pfam; PF05208; ALG3; 1. KW Transmembrane; Endoplasmic reticulum; Developmental protein; KW Multigene family. FT TRANSMEM 44 64 POTENTIAL. FT TRANSMEM 98 118 POTENTIAL. FT TRANSMEM 126 146 POTENTIAL. FT TRANSMEM 172 192 POTENTIAL. FT TRANSMEM 212 232 POTENTIAL. FT TRANSMEM 234 254 POTENTIAL. FT TRANSMEM 295 315 POTENTIAL. FT TRANSMEM 404 424 POTENTIAL. SQ SEQUENCE 484 AA; 55458 MW; 0E1142BED20EA9D2 CRC64; MAPPKAASHR PAVRRKKSGT LVDSILDKYL NVRFFKYLLL EPAALPIVGL FVLLAELVIN VVVIQRVPYT EIDWVAYMQE CEGFLNGTTN YSLLRGDTGP LVYPAAFVYI YSALYYVTSH GTNVRLAQYI FAGIYLLQLA LVLRLYSKSR KVPPYVLVLS AFTSYRIHSI YVLRLFNDPV AVLLLYAALN LFLDRRWTLG STFFSLAVGV KMNILLFAPA LLLFYLANLG LLRTILQLAV CGVIQLLLGA PFLLTHPVEY LRGSFDLGRI FEHKWTVNYR FLSRDVFENR TFHVSLLGLH LLLLLAFAKP TWTFFQSYVR LRRIEDQLQP QIAQQNLELK AQKRPKKVEK DKDKDQKKFT TEQQSFLKAF EKSLQKASGG KATPAPAQAE PERYGIHFDR CTQLALLPFF LCNLVGVACS RSLHYQFYVW YFHSLPYLAW STPYSLGVRC LILGLIEYCW NTYPSTNFSS AALHFTHIIP PYQL // ID NT56_DROME STANDARD; PRT; 510 AA. AC Q27333; O02532; O02533; Q24419; Q24420; Q24421; Q24607; Q95R76; AC Q9W1K8; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lethal(2)neighbour of tid protein (NOT56) (NOT45). GN L(2)NOT OR CG4084. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Oregon-R, Harvich, bIf, and apxo; TISSUE=Embryo; RX MEDLINE=98038975; PubMed=9373138; RA Kurzik-Dumke U., Kaymer M., Gundacker D., Debes A., Labitzke K.; RT "Gene within gene configuration and expression of the Drosophila RT melanogaster genes lethal(2) neighbour of tid [l(2)not] and lethal(2) RT relative of tid."; RL Gene 200:45-58(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-2; RA Gundacker S., Neubhuer M., Kurzik-Dumke U.; RT "Sequence of a 10291 nt genomic region of Drosophila melanogaster RT harbouring the genes l(2)tid, l(2)not, l(2)rot, and l(2)dtl."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 179-510 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: EXPRESSED ONLY IN EMBRYOS. CC -!- MISCELLANEOUS: IN STRAINS HARVICH AND APXO, THERE ARE 2 GENES CC WHICH CODE FOR L(2)NOT PROTEIN. THEY DIFFER IN THEIR C-TERMINUS. CC -!- SIMILARITY: BELONGS TO THE ALG3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95241; CAA64529.1; -. DR EMBL; X77820; CAA54835.1; -. DR EMBL; X95248; CAA64537.1; -. DR EMBL; X95252; CAA64541.1; -. DR EMBL; X95243; CAA64532.1; -. DR EMBL; Y10074; CAA71167.1; -. DR EMBL; X98094; CAA66721.1; -. DR EMBL; AE003461; AAF47050.1; -. DR EMBL; AY061582; AAL29130.1; ALT_INIT. DR FlyBase; FBgn0011297; l(2)not. DR InterPro; IPR007873; ALG3. DR Pfam; PF05208; ALG3; 1. KW Transmembrane; Endoplasmic reticulum; Developmental protein; KW Multigene family; Polymorphism. FT TRANSMEM 44 64 POTENTIAL. FT TRANSMEM 98 118 POTENTIAL. FT TRANSMEM 126 146 POTENTIAL. FT TRANSMEM 172 192 POTENTIAL. FT TRANSMEM 212 232 POTENTIAL. FT TRANSMEM 234 254 POTENTIAL. FT TRANSMEM 295 315 POTENTIAL. FT TRANSMEM 404 424 POTENTIAL. FT TRANSMEM 427 447 POTENTIAL. FT TRANSMEM 465 485 POTENTIAL. FT VARIANT 286 286 V -> L (IN STRAINS BERKELEY AND BIF). FT VARIANT 311 311 I -> T (IN STRAINS BERKELEY, BIF AND FT APXO). FT VARIANT 333 333 T -> A (IN STRAINS BERKELEY, BIF AND FT APXO). FT VARIANT 338 338 Q -> E (IN STRAINS BERKELEY, BIF AND FT APXO). FT VARIANT 340 340 K -> N (IN STRAINS BERKELEY AND BIF). FT VARIANT 489 489 I -> V (IN STRAINS BERKELEY, BIF AND FT APXO). FT MUTAGEN 433 433 H->R: IN TID4 MUTANT. SQ SEQUENCE 510 AA; 58460 MW; E2F7415940465F25 CRC64; MAPPKAASHR PAVRRKKSGT LVDSILDKYL NVRFFKYLLL EPAALPIVGL FVLLAELVIN VVVIQRVPYT EIDWVAYMQE CEGFLNGTTN YSLLRGDTGP LVYPAAFVYI YSALYYVTSH GTNVRLAQYI FAGIYLLQLA LVLRLYSKSR KVPPYVLVLS AFTSYRIHSI YVLRLFNDPV AVLLLYAALN LFLDRRWTLG STFFSLAVGV KMNILLFAPA LLLFYLANLG LLRTILQLAV CGVIQLLLGA PFLLTHPVEY LRGSFDLGRI FEHKWTVNYR FLSRDVFENR TFHVSLLGLH LLLLLAFAKP IWTFFQSYVR LRRIEDQLQP QITQQNLQLK AQKRPKKVEK DKDKDQKKFT TEQQSFLKAF EKSLQKASGG KATPAPAQAE PERYGIHFDR CTQLALLPFF LCNLVGVACS RSLHYQFYVW YFHSLPYLAW STPYSLGVRC LILGLIEYCW NTYPSTNFSS AALHFTHIIL LAGVAKQLIQ TMRINNAAKR EQQEQQKKLQ // ID NU1M_DROME STANDARD; PRT; 312 AA. AC P18929; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE NADH-ubiquinone oxidoreductase chain 1 (EC 1.6.5.3). GN MT:ND1 OR ND1. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Bretagne; RX MEDLINE=88212147; PubMed=3130291; RA Garesse R.; RT "Drosophila melanogaster mitochondrial DNA: gene organization and RT evolutionary considerations."; RL Genetics 118:649-663(1988). CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -!- SIMILARITY: BELONGS TO THE COMPLEX I SUBUNIT 1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37275; AAA69715.1; -. DR EMBL; U37541; AAC47823.1; -. DR FlyBase; FBgn0013679; mt:ND1. DR InterPro; IPR001694; Resp_NADH_dh1. DR Pfam; PF00146; NADHdh; 1. DR PROSITE; PS00667; COMPLEX1_ND1_1; 1. DR PROSITE; PS00668; COMPLEX1_ND1_2; 1. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion; Transmembrane. SQ SEQUENCE 312 AA; 35910 MW; B2B01BE6213CE722 CRC64; MEFILSLIGS LLLIICVLVS VAFLTLLERK VLGYIQIRKG PNKVGLMGIP QPFCDAIKLF TKEQTYPLLS NYLSYYISPI FSLFLSLFVW MCMPFFVKLY SFNLGGLFFL CCTSLGVYTV MVAGWSSNSN YALLGGLRAV AQTISYEVSL ALILLSFIFL IGSYNMIYFF FYQVYMWFLI ILFPMALVWV SISLAETNRN PFDFAEGESE LVSGFNVEYS SGGLALIFMA EYASILFMSM LFCVIFLPCD VFNLLIYMKL TFISFVFIWV RGTLPRFRYD KLMYLAWKCF LSFSLNYLLF FIGFKILLFS LL // ID NU2M_DROME STANDARD; PRT; 341 AA. AC P03896; DT 21-JUL-1986 (Rel. 01, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE NADH-ubiquinone oxidoreductase chain 2 (EC 1.6.5.3). GN ND2. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96423163; PubMed=8825764; RA Lewis D.L., Farr C.L., Kaguni L.S.; RT "Drosophila melanogaster mitochondrial DNA: completion of the RT nucleotide sequence and evolutionary comparisons."; RL Insect Mol. Biol. 4:263-278(1995). RN [2] RP SEQUENCE OF 56-341 FROM N.A. RX MEDLINE=83245048; PubMed=6408489; RA de Bruijn M.H.L.; RT "Drosophila melanogaster mitochondrial DNA, a novel organization and RT genetic code."; RL Nature 304:234-241(1983). CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE COMPLEX I SUBUNIT 2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37541; AAC47811.1; -. DR EMBL; J01404; AAB59238.1; -. DR PIR; A00419; QXFF2M. DR FlyBase; FBgn0013680; mt:ND2. DR InterPro; IPR003917; NADHub_oxred2. DR InterPro; IPR001750; Oxidored_q1. DR Pfam; PF00361; oxidored_q1; 1. DR PRINTS; PR01436; NADHDHGNASE2. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion; Transmembrane. SQ SEQUENCE 341 AA; 39773 MW; 2B8E9528C28007D8 CRC64; MFNNSSKILF ITIMIIGTLI TVTSNSWLGA WMGLEINLLS FIPLLSDNNN LMSTEASLKY FLTQVLASTV LLFSSILLML KNNMNNEINE SFTSMIIMSA LLLKSGAAPF HFWFPNMMEG LTWMNALMLM TWQKIAPLML ISYLNIKYLL LISVILSVII GAIGGLNQTS LRKLMAFSSI NHLGWMLSSL MISESIWLIL FFFYSFLSFV LTFMFNIFKL FHLNQLFSWF VNSKILKFTL FMNFLSLGGL PPFLGFLPKW LVIQQLTLCN QYFMLTIMMM STLITLFFYL RICYSAFMMN YFENNWIMKM NMNSINYNMY MIMTFFSIFG LFLISLFYFM F // ID NU3M_DROME STANDARD; PRT; 117 AA. AC P18930; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NADH-ubiquinone oxidoreductase chain 3 (EC 1.6.5.3). GN MT:ND3 OR ND3. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Bretagne; RX MEDLINE=88212147; PubMed=3130291; RA Garesse R.; RT "Drosophila melanogaster mitochondrial DNA: gene organization and RT evolutionary considerations."; RL Genetics 118:649-663(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Zimbabwe 53; RX MEDLINE=20363871; PubMed=10903372; RA Ballard J.W.O.; RT "Comparative genomics of mitochondrial DNA in members of the RT Drosophila melanogaster subgroup."; RL J. Mol. Evol. 51:48-63(2000). RN [3] RP SEQUENCE OF 1-29 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=83220794; PubMed=6304652; RA Clary D.O., Wahleithner J.A., Wolstenholme D.R.; RT "Transfer RNA genes in Drosophila mitochondrial DNA: related 5' RT flanking sequences and comparisons to mammalian mitochondrial tRNA RT genes."; RL Nucleic Acids Res. 11:2411-2425(1983). CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -!- SIMILARITY: BELONGS TO THE COMPLEX I SUBUNIT 3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37275; AAA69709.1; -. DR EMBL; U37541; AAC47817.1; -. DR EMBL; AF200828; AAF77232.1; -. DR EMBL; AF200829; AAF77244.1; -. DR EMBL; J01404; AAB59244.1; -. DR PIR; S01185; S01185. DR FlyBase; FBgn0013681; mt:ND3. DR InterPro; IPR000440; Oxidored_q4. DR Pfam; PF00507; oxidored_q4; 1. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion. SQ SEQUENCE 117 AA; 13563 MW; 6DB7AFDA72924892 CRC64; MFSIIFIALL ILLITTIVMF LASILSKKAL IDREKSSPFE CGFDPKSSSR LPFSLRFFLI TIIFLIFDVE IALILPMIII MKYSNIMIWT ITSIIFILIL LIGLYHEWNQ GMLNWSN // ID NU4M_DROME STANDARD; PRT; 446 AA. AC P18931; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE NADH-ubiquinone oxidoreductase chain 4 (EC 1.6.5.3). GN MT:ND4 OR ND4. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Bretagne; RX MEDLINE=88212147; PubMed=3130291; RA Garesse R.; RT "Drosophila melanogaster mitochondrial DNA: gene organization and RT evolutionary considerations."; RL Genetics 118:649-663(1988). CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37275; AAA69711.1; ALT_TERM. DR EMBL; U37541; AAC47819.1; -. DR FlyBase; FBgn0013682; mt:ND4. DR InterPro; IPR003918; NADHub_oxred4. DR InterPro; IPR001750; Oxidored_q1. DR InterPro; IPR000260; Oxidored_q5_N. DR Pfam; PF00361; oxidored_q1; 1. DR Pfam; PF01059; oxidored_q5_N; 1. DR PRINTS; PR01437; NUOXDRDTASE4. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion. FT CONFLICT 161 161 S -> V (IN REF. 1; AAC47819). SQ SEQUENCE 446 AA; 51371 MW; 8AB4A98563238BB2 CRC64; MLKIIFFLLF LIPFCFINNM YWMVQIMMFF ISFIFLLMNN FMNYWSEISY FLGCDMLSYG LILLSLWICS LMLLASEMIN KHNNYKNLFL LNIIILLLLL ILTFSSMSLF MFYLFFESSL IPTLFLILGW GYQPERLQAG LYLLFYTLLV SLPMLIGIFY SMNKIGSMNF YLMNNFMFNY DLLYFCLLCA FLVKMPMFLV YLWLPKAHVE APVSGSMILA GIMLKLGGYG MLRVISFLQL MNLKYSFVWI SISLVGGVLV SLVCLRQTDL KALIAYSSVA HMGIVLSGLL TMTYWGLCGS YTLMIAHGLC SSGLFCLANV SYERLGSRSM LINKGLLNFM PSMTLWWFLL SSANMAAPPT LNLLGEISLL NSIVSWSWIS MILLSFLSFF SAAYTLYLYS FSQHGKLFSG VYSFSSGKIR EYLLMLLHWL PLNLLILKSE SFMLWL // ID NU5M_DROME STANDARD; PRT; 572 AA. AC P18932; Q36735; Q9MGN9; DT 01-NOV-1990 (Rel. 16, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NADH-ubiquinone oxidoreductase chain 5 (EC 1.6.5.3). GN MT:ND5. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Bretagne; RX MEDLINE=88212147; PubMed=3130291; RA Garesse R.; RT "Drosophila melanogaster mitochondrial DNA: gene organization and RT evolutionary considerations."; RL Genetics 118:649-663(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Zimbabwe 53; RX MEDLINE=20363871; PubMed=10903372; RA Ballard J.W.O.; RT "Comparative genomics of mitochondrial DNA in members of the RT Drosophila melanogaster subgroup."; RL J. Mol. Evol. 51:48-63(2000). RN [3] RP SEQUENCE OF 6-510 FROM N.A. RX MEDLINE=95154701; PubMed=7851771; RA Rand D.M., Dorfsman M., Kann L.M.; RT "Neutral and non-neutral evolution of Drosophila mitochondrial DNA."; RL Genetics 138:741-756(1994). CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37275; AAA69710.1; ALT_TERM. DR EMBL; U37541; AAC47818.1; -. DR EMBL; AF200828; AAF77233.1; -. DR EMBL; AF200829; AAF77251.1; -. DR EMBL; S76764; AAB33356.1; -. DR PIR; S01186; S01186. DR FlyBase; FBgn0013684; mt:ND5. DR InterPro; IPR003916; NADHub_oxred5. DR InterPro; IPR001750; Oxidored_q1. DR InterPro; IPR001516; Oxidored_q1_N. DR Pfam; PF00361; oxidored_q1; 1. DR Pfam; PF00662; oxidored_q1_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion. FT CONFLICT 331 331 I -> IGI (IN REF. 1). SQ SEQUENCE 572 AA; 65144 MW; 8BFEEF4CE24B5575 CRC64; MCSISFVNLI SMSLSCFLLS LYFLLNDMIY FIEWELVSLN SMSIVMTFLF DWMSLLFMSF VLMISSLVIF YSKEYMMNDN HINRFIMLVL MFVLSMMLLI ISPNLISILL GWDGLGLVSY CLVIYFQNIK SYNAGMLTAL SNRIGDVALL LSIAWMLNYG SWNYIFYLEI MQNEFEMLMI GSLVMLAAMT KSAQIPFSSW LPAAMAAPTP VSALVHSSTL VTAGVYLLIR FNIILSTSWL GQLMLLLSGL TMFMAGLGAN FEFDLKKIIA LSTLSQLGLM MSILSMGFLK LAMFHLLTHA LFKALLFMCA GAIIHNMNNS QDIRLMGGLS IHMPLTSACF NVSNLALCGM PFLAGFYSKD MILEIVSISN VNMFSFFLYY FSTGLTVSYS FRLVYYSMTG DLNCGSLNML NDESWIMLRG MMGLLIMSII GGSMLNWLIF PFPYMICLPI YMKLLTLFVC IVGGLFGYLI SLSNLFFLNK SLFMYNLSTF LGSMWFMPYI STYGMIFYPL NYGQLVVKSF DQGWSEYFGG QHLYQKLSMY SKTLFLMHNN SLKIYLLLFV FWILILLILL FL // ID NU6M_DROME STANDARD; PRT; 174 AA. AC P18933; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NADH-ubiquinone oxidoreductase chain 6 (EC 1.6.5.3). GN MT:ND6 OR ND6. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Bretagne; RX MEDLINE=88212147; PubMed=3130291; RA Garesse R.; RT "Drosophila melanogaster mitochondrial DNA: gene organization and RT evolutionary considerations."; RL Genetics 118:649-663(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Zimbabwe 53; RX MEDLINE=20363871; PubMed=10903372; RA Ballard J.W.O.; RT "Comparative genomics of mitochondrial DNA in members of the RT Drosophila melanogaster subgroup."; RL J. Mol. Evol. 51:48-63(2000). CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37275; AAA69713.1; -. DR EMBL; U37541; AAC47821.1; -. DR EMBL; AF200828; AAF77236.1; -. DR EMBL; AF200829; AAF77248.1; -. DR PIR; S01189; S01189. DR FlyBase; FBgn0013685; mt:ND6. DR InterPro; IPR001457; Oxidored_q3. DR Pfam; PF00499; oxidored_q3; 1. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion. SQ SEQUENCE 174 AA; 20074 MW; 6390850F8B5CE011 CRC64; MIQLMLYSLI ITTSIIFLNM IHPLALGLTL LIQTIFVCLL TGLMTKSFWY SYILFLIFLG GMLVLFIYVT SLASNEMFNL SMKLTLFSSL ILIFMLILSF IMDKTSSSLF LMNNDMQSII NMNSYFMENS LSLNKLYNFP TNFITILLMN YLLITLIVIV KITKLFKGPI RMMS // ID NUAM_DROME STANDARD; PRT; 731 AA. AC Q94511; Q9W3H1; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial precursor DE (EC 1.6.5.3) (EC 1.6.99.3) (Complex I-75Kd) (CI-75Kd). GN ND75 OR CG2286. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-653 FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). CC -!- FUNCTION: THIS IS THE LARGEST SUBUNIT OF COMPLEX I AND IT IS A CC COMPONENT OF THE IRON-SULFUR (IP) FRAGMENT OF THE ENZYME. IT MAY CC FORM PART OF THE ACTIVE SITE CREVICE WHERE NADH IS OXIDIZED (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -!- CATALYTIC ACTIVITY: NADH + ACCEPTOR = NAD(+) + REDUCED ACCEPTOR. CC -!- COFACTOR: BINDS 3 4FE-4S CLUSTERS PER SUBUNIT (POTENTIAL). CC -!- SUBUNIT: COMPLEX I IS COMPOSED OF ABOUT 45 DIFFERENT SUBUNITS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: MATRIX AND CYTOPLASMIC SIDE OF THE CC MITOCHONDRIAL INNER MEMBRANE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE COMPLEX I 75 KDA SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003443; AAF46356.1; -. DR EMBL; Y09063; CAA70284.1; -. DR FlyBase; FBgn0017566; ND75. DR InterPro; IPR000283; Complex1_75K. DR InterPro; IPR001041; Ferredoxin. DR InterPro; IPR006656; Molybdopterin. DR Pfam; PF00111; fer2; 1. DR Pfam; PF00384; molybdopterin; 1. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion; Transit peptide; KW Metal-binding; Iron; Iron-sulfur; 2Fe-2S; 4Fe-4S. FT TRANSIT 1 27 MITOCHONDRION (BY SIMILARITY). FT CHAIN 28 731 NADH-UBIQUINONE OXIDOREDUCTASE 75 kDa FT SUBUNIT. FT METAL 74 74 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 85 85 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 88 88 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 102 102 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 138 138 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 141 141 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 147 147 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 190 190 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 193 193 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 196 196 IRON-SULFUR (4FE-4S) (POTENTIAL). FT METAL 240 240 IRON-SULFUR (4FE-4S) (POTENTIAL). FT CONFLICT 65 65 Q -> L (IN REF. 2). FT CONFLICT 94 94 K -> N (IN REF. 2). FT CONFLICT 111 111 R -> P (IN REF. 2). FT CONFLICT 120 120 R -> P (IN REF. 2). FT CONFLICT 470 470 A -> S (IN REF. 2). FT CONFLICT 611 611 Q -> H (IN REF. 2). SQ SEQUENCE 731 AA; 78630 MW; B3CA26B56AFACBFD CRC64; MIRAPLVKAL GALGSPTHQM ASRAVRTSAM VAQTPAKAPE KIEVFVDDIP VQVVPGTTVL QAAAQIGVEI PRFCYHERLA VAGNCRMCLV EVEKSPKPVA ACAMPVMKGW RIKTNSDLTR KAREGVMEFL LMNHPLDCPI CDQGGECDLQ DQAMAFGSDR SRFTDINYTG KRAVEDKDIG PLVKTIMTRC IHCTRCVRFA SEIAGVDDLG TTGRGNDMQI GTYVEKLFLT ELSGNVIDLC PVGALTNKPY SFVARPWEIR KVSSIDVLDA VGSNIVVSTR TNEVLRILPR ENEDVNEEWL ADKSRFACDG LKRQRLVAPM VRMPNGELQA VEWEGALIAV AKAIKAAGGQ IAGISGQLAD LEAQVALKDL LNRLGSEVVA TEQGFIAGGT DNRANYLLNS TIAGLEEADA VLLVGTNPRY EAPLVNTRLR KAYVHNELQI ASIGPKIDLS YDHENLGADA ALVKDVCSGA HAFSKVLEGA KKPAIIIGAD LLERADGAAI HATVAEYCKK LKKPNWNPFN VLQTNAAQVG ALDVGYKAGA QTAVKAQPKV LFLLNADAGK VTREQLPKDC FVVYIGSHGD NGASIADAVL PGAAYTEKQG IYVNTEGRPQ QTLPGVSPPG MAREDWKILR ALSEVVGKPL PYDNLDELRN RLEDVAPHLT RLGQLEPAGD AGAAGTISKS IGGGAIDIKL KELRDYFMTD AISRASPTMA KCISAVNKQQ RENEAKQSVA I // ID NUDM_DROME STANDARD; PRT; 407 AA. AC P91929; Q9VD54; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NADH-ubiquinone oxidoreductase 42 kDa subunit, mitochondrial precursor DE (EC 1.6.5.3) (EC 1.6.99.3) (Complex I-42KD) (CI-42KD). GN ND42 OR CG6343. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 45-205 FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). CC -!- FUNCTION: TRANSFER OF ELECTRONS FROM NADH TO THE RESPIRATORY CC CHAIN. THE IMMEDIATE ELECTRON ACCEPTOR FOR THE ENZYME IS BELIEVED CC TO BE UBIQUINONE. CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -!- CATALYTIC ACTIVITY: NADH + ACCEPTOR = NAD(+) + REDUCED ACCEPTOR. CC -!- COFACTOR: BINDS 1 FAD PER SUBUNIT. CC -!- SUBUNIT: MAMMALIAN COMPLEX I IS COMPOSED OF 45 DIFFERENT SUBUNITS. CC THIS A COMPONENT OF THE HYDROPHOBIC PROTEIN FRACTION (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003737; AAF55947.1; -. DR EMBL; AY051764; AAK93188.1; -. DR EMBL; Y10911; CAA71852.1; -. DR FlyBase; FBgn0019957; ND42. DR InterPro; IPR002624; dNK. DR Pfam; PF01712; dNK; 1. KW Oxidoreductase; NAD; Ubiquinone; Flavoprotein; FAD; Mitochondrion; KW Transit peptide. FT TRANSIT 1 60 MITOCHONDRION (POTENTIAL). FT CHAIN 61 407 NADH-UBIQUINONE OXIDOREDUCTASE 42 kDa FT SUBUNIT. FT CONFLICT 177 177 H -> R (IN REF. 3). FT CONFLICT 198 198 M -> L (IN REF. 3). SQ SEQUENCE 407 AA; 46897 MW; 4B5F4EC7DED9B8D4 CRC64; MTAVFRVGLV RLVSRATQSP NLLQAQTNAL PAAFQQRCSI SGKTMRGGPR VPKAAPYPYK TKKYSVFNAI FDKTSKRFDE NSKVICVEGP IAAGKSKFAK ELAEELDMEY YPAVDLDLIY INSYGYDMRK LDPQLPPSCR SYDVRNFCLD PSHDLAAQFQ IRMYMLRYSQ YIDALQHVLS TGQGVVLERS PYSDFVFMEA MFRQGYLSRG ARSVYNELRQ NTIGELLKPH LVIYLDLPVD AVKKQIKARN VDYEVQSKVF SDAYLSDLEQ LYKQQYLKDI STHAELLIYD WTAGGETEVV VEDIERIDFN QFEADIHNKK MLDWRFPLEA EWCEARIKYC HEKPDLMNYF NVPRFDVPEL VRSADDGKVW RDVWFNAPGM KYRPGYNADM GDEGLLTKTK IGINQGI // ID NULL_DROME STANDARD; PRT; 213 AA. AC P32845; Q9W3S9; DT 01-OCT-1993 (Rel. 27, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nullo protein. GN NULLO OR CG14426. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92331931; PubMed=1378418; RA Rose L.S., Wieschaus E.; RT "The Drosophila cellularization gene nullo produces a blastoderm- RT specific transcript whose levels respond to the nucleocytoplasmic RT ratio."; RL Genes Dev. 6:1255-1268(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTIN-MYOSIN NETWORK STABILITY DURING CELLULARIZATION. CC MIGHT BE INVOLVED IN INCREASING ACTIN-ACTIN INTERACTIONS OR CC MEMBRANE-TO-CYTOSKELETON ATTACHMENTS. NULLO TOGETHER WITH SRY-A CC AND BNK MAY PROVIDE AUXILIARY FUNCTIONS, BY ACTING BOTH TO CC STABILIZE A LARGE AND DYNAMIC MICROFILAMENT STRUCTURE AND REGULATE CC ITS FUNCTIONS. CC -!- SUBCELLULAR LOCATION: COLOCALIZES WITH THE STRUCTURAL TRANSITIONS CC IN THE MICROFILAMENT NETWORK DURING CELLULARIZATION. CC -!- TISSUE SPECIFICITY: BLASTODERM. THROUGHOUT THE ENTIRE CORTEX OF CC THE EMBRYO ALTHOUGH THE DISTRIBUTION IS NOT UNIFORM. CC -!- DEVELOPMENTAL STAGE: APPEARS FIRST AT NUCLEAR CELL CYCLE 11 AND CC DISAPPEARS RAPIDLY AS CELLULARIZATION BEGINS. DURING CYCLE 14, CC NULLO PROTEIN LEVELS ARE COUPLED TO THE NUCLEOCYTOPLASMIC RATIO. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65444; CAA46446.1; -. DR EMBL; AE003439; AAF46238.1; -. DR PIR; A46237; A46237. DR FlyBase; FBgn0004143; nullo. DR GO; GO:0007043; P:intercellular junction assembly; IMP. DR GO; GO:0008104; P:protein localization; NAS. KW Developmental protein. FT VARIANT 138 138 V -> A. FT CONFLICT 35 35 N -> K (IN REF. 1). SQ SEQUENCE 213 AA; 24192 MW; D48BEAA4DF95B2FE CRC64; MGSTHSAEKV KSVEDSTSPA NPGIFCTPLP GFISNIQRLV LRKLSISARK QKRLNKRSKH LLRPMPRCSS FGSCGTLLTP TKKSASNIAD RRYAQWKCSF EHLAQKQPRL HDISEAMTGQ TTPRGFPSHT DPKRCLMVMD SSSPESPLYD MVGGQKVRRR LSLRSHALVR RPSARQKAEQ AKLDAQFQRD LRDLEDYYGG FHFAQRRERL VKV // ID NULM_DROME STANDARD; PRT; 96 AA. AC P18934; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NADH-ubiquinone oxidoreductase chain 4L (EC 1.6.5.3). GN MT:ND4L OR ND4L. OS Drosophila melanogaster (Fruit fly). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Bretagne; RX MEDLINE=88212147; PubMed=3130291; RA Garesse R.; RT "Drosophila melanogaster mitochondrial DNA: gene organization and RT evolutionary considerations."; RL Genetics 118:649-663(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Zimbabwe 53; RX MEDLINE=20363871; PubMed=10903372; RA Ballard J.W.O.; RT "Comparative genomics of mitochondrial DNA in members of the RT Drosophila melanogaster subgroup."; RL J. Mol. Evol. 51:48-63(2000). CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37275; AAA69712.1; -. DR EMBL; U37541; AAC47820.1; -. DR EMBL; AF200828; AAF77235.1; -. DR EMBL; AF200829; AAF77247.1; -. DR PIR; S01188; S01188. DR FlyBase; FBgn0013683; mt:ND4L. DR InterPro; IPR001133; Oxidored_4L. DR InterPro; IPR003214; Oxidred4L. DR Pfam; PF00420; oxidored_q2; 1. DR ProDom; PD000359; Oxidred4L; 1. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion. SQ SEQUENCE 96 AA; 11359 MW; D383557D738A175B CRC64; MIMILYWSLP MILFILGLFC FVSNRKHLLS MLLSLEFIVL MLFFMLFIYL NMLNYESYFS MMFLTFSVCE GALGLSILVS MIRTHGNDYF QSFSIM // ID NUMB_DROME STANDARD; PRT; 556 AA. AC P16554; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Numb protein. GN NUMB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89324081; PubMed=2752427; RA Uemura T., Shepherd S., Ackerman L., Jan L.Y., Jan Y.N.; RT "Numb, a gene required in determination of cell fate during sensory RT organ formation in Drosophila embryos."; RL Cell 58:349-360(1989). RN [2] RP STRUCTURE BY NMR OF 64-210. RX MEDLINE=99061335; PubMed=9846878; RA Li S.-C., Zwahlen C., Vincent S.J., McGlade C.J., Kay L.E., Pawson T., RA Forman-Kay J.D.; RT "Structure of a Numb PTB domain-peptide complex suggests a basis for RT diverse binding specificity."; RL Nat. Struct. Biol. 5:1075-1083(1998). CC -!- FUNCTION: NUMB IS REQUIRED IN DETERMINATION OF CELL FATE DURING CC SENSORY ORGAN FORMATION IN DROSOPHILA EMBRYOS. IT FUNCTIONS IN CC NUCLEI AND SEEMS TO INTERACT WITH NUCLEIC ACIDS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; CC Comment=2 isoforms, Long/Zygotic (shown here) and CC Short/Maternal, may be produced by alternative initiation; CC -!- SIMILARITY: CONTAINS 1 PID DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27815; AAA28730.1; -. DR PIR; A32466; A32466. DR PDB; 2NMB; 04-NOV-98. DR PDB; 1DDM; 12-APR-00. DR FlyBase; FBgn0002973; numb. DR GO; GO:0045180; C:basal cortex; NAS. DR InterPro; IPR006020; PTB_PID. DR Pfam; PF00640; PID; 1. DR SMART; SM00462; PTB; 1. DR PROSITE; PS01179; PID; 1. KW Developmental protein; Nuclear protein; ATP-binding; KW Alternative initiation; 3D-structure. FT CHAIN 1 556 NUMB PROTEIN, ISOFORM LONG. FT CHAIN 42 556 NUMB PROTEIN, ISOFORM SHORT. FT INIT_MET 42 42 FOR ISOFORM SHORT. FT NP_BIND 22 29 ATP (POTENTIAL). FT DOMAIN 25 57 ARG/LYS-RICH (BASIC). FT DOMAIN 81 208 PID. FT TURN 66 68 FT HELIX 69 78 FT STRAND 83 92 FT HELIX 100 111 FT TURN 112 113 FT STRAND 119 122 FT STRAND 129 132 FT STRAND 138 138 FT TURN 144 146 FT STRAND 163 165 FT TURN 167 168 FT STRAND 172 179 FT HELIX 188 194 FT TURN 195 198 FT TURN 200 201 SQ SEQUENCE 556 AA; 60628 MW; 4FECAAE9C98FEE71 CRC64; MGNSSSHTHE PLERGFTRGK FGDVKNGKSA SFRFSKKSPK KMDRLRRSFR DSFRRRKDRV PESSKPHQWQ ADEEAVRSAT CSFSVKYLGC VEVFESRGMQ VCEEALKVLR QSRRRPVRGL LHVSGDGLRV VDDETKGLIV DQTIEKVSFC APDRNHERGF SYICRDGTTR RWMCHGFLAC KDSGERLSHA VGCAFAVCLE RKQRRDKECG VTMTFDTKNS TFTRTGSFRQ QTLTERLAMA TVGTNERSVD GPGSAMPGPP AATVKPFNPF AIERPHATPN MLERQSSFRL STIGSQSPFK RQMSLRINDL PSNADRQRAF LAAAADNPLQ TPLRSVSPIA EVSPAKSAGA DPSSAAAVAA DSVSQLCQEL SQGLSLLTQT DALLATGEDL NFNNNRSINQ NIIAAEKQVQ HVHSYAPPTA QVTPRVASTT PTYQTLHSQS PSRSEQSIET STELPNAEQW LGHVVRSTSP AAPKRPTYLA NVGRAQTLAS GTGAAVGGGG PDDPFDAEWV ANVAAAKQLS PDLPIPSTAR SPLARHSTNP FISPPKAPAQ SFQVQL // ID NUP1_DROME STANDARD; PRT; 546 AA. AC Q9VDV3; Q8SYM7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable nucleoporin Nup58. GN NUP58 OR CG7360. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLE COMPONENT OF SOME NUCLEAR PORE COMPLEX, A CC COMPLEX REQUIRED FOR THE TRAFFICKING ACROSS THE NUCLEAR MEMBRANE CC (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: LOCALIZES TO THE NUCLEAR PORE COMPLEX REGION CC (BY SIMILARITY). CC -!- DOMAIN: CONTAINS F-G REPEATS. CC -!- SIMILARITY: BELONGS TO THE NUPL1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003727; AAF55687.1; -. DR EMBL; AY071440; AAL49062.1; -. DR FlyBase; FBgn0038722; Nup58. DR InterPro; IPR004325; Nucleoporin_FG. DR Pfam; PF03093; Nucleoporin_FG; 13. KW Transport; Nuclear protein; Repeat. FT DOMAIN 22 200 17 X 2 AA REPEATS OF F-G. FT REPEAT 22 23 1. FT REPEAT 36 37 2. FT REPEAT 45 46 3. FT REPEAT 64 65 4. FT REPEAT 73 74 5. FT REPEAT 82 83 6. FT REPEAT 92 93 7. FT REPEAT 101 102 8. FT REPEAT 110 111 9. FT REPEAT 119 120 10. FT REPEAT 128 129 11. FT REPEAT 137 138 12. FT REPEAT 146 147 13. FT REPEAT 155 156 14. FT REPEAT 166 167 15. FT REPEAT 197 198 16. FT REPEAT 199 200 17. FT CONFLICT 267 267 MISSING (IN REF. 2). SQ SEQUENCE 546 AA; 55528 MW; EBA7C812DDBEEACE CRC64; MFTPTTNNAI GGATAATGAF AFGARPATTT APPPSFGAAT STPTFGAAPA TTSLFAAPAA TPAFGAPAAT PAFGAPASTP GFGATSTAAP AFGTAAATPA FGIPAATSAF GAPAATPAFG AAAATPAFGA PAATPAFGAP AATSAFGAPA ATTAFGAPAS TQASAFGAPA PAVGTVAPTF SFATPATSAP TTAPPAFGFG TTATTAAAAM PASLSSGIGS FSFPKPQATT AASLNFNTTT TTATAQPFNT GLKLGTTNAT TTLGGGGIFS KPAGQAAAPA ASTFVGLGGI DVTATQPKLG DNKQDGIKIK ETQVPDEIIK TVDGLKAYIK QQKTISSDIG RTSTSKFTNV SHEITNLKWA LQNMATLVEG SNQQIRLMRQ ETVKAIQSLE MAQRTQDTPA GLQFENNAPF QYFQCLVAKY EQDLIAFRQQ IALTERHMHA ISNPQSISPD DLKRGFRQLN ESFISLAGRL HEVHQRVEEH KEHYLNLRRY RLRDTTNVFE RIDNPPLPTV EPQRISSGPT PFSNISALMN KSYAAAASSA SNATGN // ID NXF1_DROME STANDARD; PRT; 672 AA. AC Q9U1H9; Q9NFQ2; Q9NFQ3; Q9VZ65; Q9VZ68; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nuclear RNA export factor 1 (Tip associating protein) (Small DE bristles protein). GN NXF1 OR SBR OR CG1664. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21638996; PubMed=11780634; RA Wilkie G.S., Zimyanin V., Kirby R., Korey C., Francis-Lang H., RA Van Vactor D., Davis I.; RT "Small bristles, the Drosophila ortholog of NXF-1, is essential for RT mRNA export throughout development."; RL RNA 7:1781-1792(2001). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=21638995; PubMed=11780633; RA Herold A., Klymenko T., Izaurralde E.; RT "NXF1/p15 heterodimers are essential for mRNA nuclear export in RT Drosophila."; RL RNA 7:1768-1780(2001). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 281-672 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MEDIATES THE EXPORT OF THE MAJORITY OF MRNAS FROM THE CC NUCLEUS TO THE CYTOPLASM. CC -!- SUBUNIT: ASSOCIATES WITH NXT1. CC -!- SUBCELLULAR LOCATION: NUCLEAR; LOCALIZED IN THE NUCLEOPLASM AND AT CC BOTH THE NUCLEOPLASMIC AND CYTOPLASMIC FACES OF THE NUCLEAR PORE CC COMPLEX. SHUTTLES BETWEEN THE NUCLEUS AND THE CYTOPLASM. CC -!- TISSUE SPECIFICITY: EXPRESSED UBIQUITOUSLY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYONIC DEVELOPMENT. CC -!- DOMAIN: THE LEUCINE-RICH REPEATS AND THE NTF2-DOMAIN ARE ESSENTIAL CC FOR THE EXPORT OF MRNA FROM THE NUCLEUS. CC -!- DOMAIN: THE C-TERMINAL FRAGMENT, CONTAINING THE UBA-LIKE DOMAIN CC AND PART OF THE NTF2-LIKE DOMAIN, NAMED THE NPC-BINDING DOMAIN, CC MEDIATES DIRECT INTERACTIONS WITH NUCLEOPORIN-FG-REPEATS AND IS CC NECESSARY AND SUFFICIENT FOR LOCALIZATION OF NXF1 TO THE NUCLEAR CC RIM. CC -!- MISCELLANEOUS: THE RNA-BINDING DOMAIN IS A NON-CANONICAL RNP-TYPE CC DOMAIN. CC -!- SIMILARITY: BELONGS TO THE NXF FAMILY. CC -!- SIMILARITY: CONTAINS 4 LEUCINE-RICH (LRR) REPEATS. CC -!- SIMILARITY: CONTAINS 1 NTF2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 UBA-LIKE DOMAIN. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ251947; CAB64382.2; -. DR EMBL; AJ272389; CAB75848.1; ALT_INIT. DR EMBL; AJ272390; CAB75849.1; ALT_SEQ. DR EMBL; AJ318090; CAC41645.1; -. DR EMBL; AE003484; AAF47959.2; ALT_SEQ. DR EMBL; AE003484; AAF47962.1; ALT_SEQ. DR EMBL; AY069415; AAL39560.1; ALT_INIT. DR FlyBase; FBgn0003321; sbr. DR GO; GO:0016973; P:poly(A)+ mRNA-nucleus export; IMP. DR InterPro; IPR001611; LRR. DR InterPro; IPR002075; NTF2. DR InterPro; IPR005637; TAP_C. DR Pfam; PF00560; LRR; 2. DR Pfam; PF03943; TAP_C; 1. DR PROSITE; PS50177; NTF2_DOMAIN; 1. KW Transport; mRNA transport; Nuclear protein; RNA-binding; Repeat; KW Leucine-rich repeat; Multigene family. FT DOMAIN 113 193 RNA-BINDING (RRM) (BY SIMILARITY). FT REPEAT 255 280 LRR 1. FT REPEAT 281 304 LRR 2. FT REPEAT 305 332 LRR 3. FT REPEAT 333 360 LRR 4. FT DOMAIN 375 529 NTF2. FT DOMAIN 619 661 UBA-LIKE. FT CONFLICT 292 292 I -> V (IN REF. 1; CAB75848). FT CONFLICT 328 340 SEVRRKFPKLVKL -> RYTM (IN REF. 3; FT AAF47959). FT CONFLICT 640 640 K -> KR (IN REF. 1; CAB75849). SQ SEQUENCE 672 AA; 76248 MW; FADEF8B6DA7B7F5F CRC64; MPKRGGGSSQ RYNNNVGNGG GRYNAPEDFD DFDVEDRQRR KDRNKRRVSF KPSQCLHNKK DIKLRPEDLR RWDEDDDMSD MTTAVKDRPT SRRRGSPIPR GKFGKLMPNS FGWYQVTLQN AQIYEKETLL SALLAAMSPH VFIPQYWRVE RNCVIFFTDD YEAAERIQHL GKNGHLPDGY RLMPRVRSGI PLVAIDDAFK EKMKVTMAKR YNIQTKALDL SRFHADPDLK QVFCPLFRQN VMGAAIDIMC DNIPDLEALN LNDNSISSME AFKGVEKRLP NLKILYLGDN KIPSLAHLVV LRNLSILELV LKNNPCRSRY KDSQQFISEV RRKFPKLVKL DGETLEPQIT FDLSEQGRLL ETKASYLCDV AGAEVVRQFL DQYFRIFDSG NRQALLDAYH EKAMLSISMP SASQAGRLNS FWKFNRNLRR LLNGEENRTR NLKYGRLACV STLDEWPKTQ HDRRTFTVDL TIYNTSMMVF TVTGLFKELN DETNNPASME LYDVRHFART YVVVPQNNGF CIRNETIFIT NATHEQVREF KRSQHQPAPG AMPSTSSAVT SPQAGAAAGL QGRLNALGVA TGPVAILSGD PLAATAPVNS GSAAISTTAV APGAQDESTK MQMIEAMSAQ SQMNVIWSRK CLEETNWDFN HAAFVFEKLF KENKIPPEAF MK // ID NXF2_DROME STANDARD; PRT; 841 AA. AC Q9VV73; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Nuclear RNA export factor 2. GN NXF2 OR CG4118. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21638995; PubMed=11780633; RA Herold A., Klymenko T., Izaurralde E.; RT "NXF1/p15 heterodimers are essential for mRNA nuclear export in RT Drosophila."; RL RNA 7:1768-1780(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE INVOLVED IN THE EXPORT OF MRNA FROM THE NUCLEUS CC TO THE CYTOPLASM. CC -!- SUBUNIT: INTERACTS WITH NXT1. CC -!- SUBCELLULAR LOCATION: LOCALIZED IN BOTH THE NUCLEOPLASM AND THE CC CYTOPLASM. NOT DETECTED AT THE NUCLEAR RIM. CC -!- TISSUE SPECIFICITY: EXPRESSED UBIQUITOUSLY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYONIC DEVELOPMENT. CC -!- MISCELLANEOUS: THE RNA-BINDING DOMAIN IS A NON-CANONICAL RNP-TYPE CC DOMAIN. CC -!- SIMILARITY: BELONGS TO THE NXF FAMILY. CC -!- SIMILARITY: CONTAINS 4 LEUCINE-RICH (LRR) REPEATS. CC -!- SIMILARITY: CONTAINS 1 NTF2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 UBA-LIKE DOMAIN. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ312282; CAC41644.1; -. DR EMBL; AE003527; AAF49447.2; ALT_SEQ. DR EMBL; AY075582; AAL68387.1; -. DR FlyBase; FBgn0036640; nxf2. DR InterPro; IPR001611; LRR. DR InterPro; IPR003603; LRRcap. DR InterPro; IPR002075; NTF2. DR InterPro; IPR005637; TAP_C. DR Pfam; PF00560; LRR; 1. DR Pfam; PF03943; TAP_C; 1. DR SMART; SM00446; LRRcap; 1. DR PROSITE; PS50177; NTF2_DOMAIN; 1. KW Transport; mRNA transport; Nuclear protein; RNA-binding; Repeat; KW Leucine-rich repeat; Multigene family. FT DOMAIN 325 408 RNA-BINDING (RRM) (BY SIMILARITY). FT REPEAT 473 496 LRR 1. FT REPEAT 498 522 LRR 2. FT REPEAT 524 548 LRR 3. FT REPEAT 556 579 LRR 4. FT DOMAIN 585 758 NTF2. FT DOMAIN 788 831 UBA-LIKE (BY SIMILARITY). SQ SEQUENCE 841 AA; 96634 MW; 581CE6B0C57FF098 CRC64; MPNQMRVLDF GDGSVPIQLD YPDSKIFSKC SSYGDRVPGT HWNEITVHHK GRLEYSPNPE QIILDALYQA IDGADFFPVF YQRGKNMDTM LVRNCKAAID KLFKQRLSIN LKGGASIPIS IQLGVAQYQR HQITPTFHIA RVVTRLMKQL IQRDGVDGLL NLDNFGSHPE FKNLVVSLGN PSILMNVCQV IHNDDNERFR LNGFILSNNR IRDIRPLTLL ANVDYALLDL RGNKIKSAER LCRALEQFRA RELLLENNPI VKISNFPANI KSLESNFELV DGKPFNMLHK IFSPLDVEID LEVDGARIDT NNMWKLPEFE NSQHWHAFMI PDPSHEFNQE VFFDFFFIRL DPTLSNFYPC YYKYINTEHV FLVRNCFDQI AHLVNNCNLE MTIPTGDRIF RYYLRMNVST VKQHHVDPEE CIQKAVSQCY VAQNRMLNLE RFHSRECLKD VMVSLSSPKI LTYVLSVASR KFMTTCSEIR LCHNKVLVLD GAHVLGMMGC LRAVDLSHNW VQDLSSIHSL GNLPLKSLVL HGNKLCRNYR LPSEYVRAVK EVFPQLTTLD GVDLQTNPGQ SLQKNFLCDT GAYELVGAFL ENYLREFEND EFRHNLYKYY SENSIFTLTC NYNVVQNHQT PKILQRLSKY NRHARNLRNK DYSKASDGVF FGCTYIVEIL LQLPRVTHDF HSLQTDVMHY NGKGAVIYVA GLLRDEPPST RNGHGSKTDI GGVLLGFSRQ FVVTFDEANL GLGKRARRLK IANERLHITN PSKTAIRNAF SVNFPDPSER QAEEDSLDVK DHKLLLFQEV TGLISTWVTS IVEEADWDFE RALKLFIQKN ADHEIPDLAF A // ID NXT1_DROME STANDARD; PRT; 133 AA. AC Q9V3H8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NTF2-related export protein (p15). GN NXT1 OR CG12752. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20036817; PubMed=10567585; RA Black B.E., Levesque L., Holaska J.M., Wood T.C., Paschal B.M.; RT "Identification of an NTF2-related factor that binds Ran-GTP and RT regulates nuclear protein export."; RL Mol. Cell. Biol. 19:8616-8624(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: STIMULATOR OF PROTEIN EXPORT FOR NES-CONTAINING CC PROTEINS. ALSO PLAYS A ROLE IN THE NUCLEAR EXPORT OF. U1 SNRNA, CC TRNA, AND MRNA (BY SIMILARITY). CC -!- SUBUNIT: PREFERENTIALLY BINDS RAN-GTP (BY SIMILARITY). ASSOCIATES CC WITH NXF1. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 1 NTF2 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF156959; AAD54944.1; -. DR EMBL; AE003462; AAF47066.1; -. DR FlyBase; FBgn0028411; Nxt1. DR GO; GO:0016973; P:poly(A)+ mRNA-nucleus export; IMP. DR InterPro; IPR002075; NTF2. DR Pfam; PF02136; NTF2; 1. DR PROSITE; PS50177; NTF2_DOMAIN; 1. KW Transport; Protein transport; mRNA transport; Nuclear protein. FT DOMAIN 15 130 NTF2. SQ SEQUENCE 133 AA; 15181 MW; C6E664950AA370AA CRC64; MDSDLKAKVE SCARTADTFT RLYYASVDNR RQQIGRLYLD NATLSWNGNG AIGRQMIESY FQELPSSNHQ LNTLDAQPIV DQAVSNQLAY LIMASGSVKF ADQQLRKFQQ TFIVTAENDK WKVVSDCYRM QEV // ID NYR_DROME STANDARD; PRT; 449 AA. AC P25931; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 01-AUG-1992 (Rel. 23, Last annotation update) DE Neuropeptide Y receptor (NPY-R) (PR4 receptor). GN NEPYR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92112730; PubMed=1370455; RA Li X.-J., Wu Y.-N., North R.A., Forte M.; RT "Cloning, functional expression, and developmental regulation of a RT neuropeptide Y receptor from Drosophila melanogaster."; RL J. Biol. Chem. 267:9-12(1992). CC -!- FUNCTION: RECEPTOR FOR NEUROPEPTIDE Y AND PEPTIDE YY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- DEVELOPMENTAL STAGE: AT LOW LEVELS DURING EARLY EMBRYONIC STAGES, CC ITS EXPRESSION INCREASES LATER AND REACHES THE HIGHEST LEVEL CC DURING LATE STAGES OF EMBRYOGENESIS. SUBSEQUENTLY, PR4 LEVELS ARE CC REDUCED DURING LARVAL STAGES AND INCREASE DURING PUPAL STAGES. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC HIGHEST TO TACHYKININS RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81490; AAA28727.1; -. DR PIR; A41738; A41738. DR FlyBase; FBgn0004842; NepYr. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein. FT DOMAIN 1 85 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 86 111 1 (POTENTIAL). FT DOMAIN 112 120 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 121 145 2 (POTENTIAL). FT DOMAIN 146 165 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 166 187 3 (POTENTIAL). FT DOMAIN 188 203 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 204 232 4 (POTENTIAL). FT DOMAIN 233 256 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 257 282 5 (POTENTIAL). FT DOMAIN 283 309 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 310 330 6 (POTENTIAL). FT DOMAIN 331 347 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 348 372 7 (POTENTIAL). FT DOMAIN 373 449 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 34 34 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 64 64 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 70 70 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 449 AA; 51885 MW; 1ADB32EFD50146C3 CRC64; MYYIAHQQPM LRNEDDNYQE GYFIRPDPAS LIYNTTALPA DDEGSNYGYG STTTLSGLQF ETYNITVMMN FSCDDYDLLS EDMWSSAYFK IIVYMLYIPI FIFALIGNGT VCYIVYSTPR MRTVTNYFIA SLAIGDILMS FFCEPSSFIS LFILNYWPFG LALCHFVNYS QAVSVLVSAY TLVAISIDRY IAIMWPLKPR ITKRYATFII AGVWFIALAT ALPIPIVSGL DIPMSPWHTK CEKYICREMW PSRSQEYYYT LSLFALQFVV PLGVLIFTYA RITIRVWAKR PPGEAETNRD QRMARSKRKM VKMMLTVVIV FTCCWLPFNI LQLLLNDEEF AHWDPLPYVW FAFHWLAMSH CCYNPIIYCY MNARFRSGFV QLMHRMPGLR RWCCLRSVGD RMNATSGTGP ALPLNRMNTS TTYISARRKP RATSLRANPL SCGETSPLR // ID O10A_DROME STANDARD; PRT; 406 AA. AC Q9VYZ1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 10a. GN OR10A OR CG17867. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003486; AAF48042.1; -. DR FlyBase; FBgn0030298; Or10a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 45 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 46 66 1 (POTENTIAL). FT DOMAIN 67 74 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 75 95 2 (POTENTIAL). FT DOMAIN 96 143 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 144 164 3 (POTENTIAL). FT DOMAIN 165 189 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 190 210 4 (POTENTIAL). FT DOMAIN 211 281 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 282 302 5 (POTENTIAL). FT DOMAIN 303 308 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 309 329 6 (POTENTIAL). FT DOMAIN 330 372 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 373 393 7 (POTENTIAL). FT DOMAIN 394 406 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 406 AA; 46765 MW; 118A61F2E90EC7EA CRC64; MSEWLRFLKR DQQLDVYFFA VPRLSLDIMG YWPGKTGDTW PWRSLIHFAI LAIGVATELH AGMCFLDRQQ ITLALETLCP AGTSAVTLLK MFLMLRFRQD LSIMWNRLRG LLFDPNWERP EQRDIRLKHS AMAARINFWP LSAGFFTCTT YNLKPILIAM ILYLQNRYED FVWFTPFNMT MPKVLLNYPF FPLTYIFIAY TGYVTIFMFG GCDGFYFEFC AHLSALFEVL QAEIESMFRP YTDHLELSPV QLYILEQKMR SVIIRHNAII DLTRFFRDRY TIITLAHFVS AAMVIGFSMV NLLTLGNNGL GAMLYVAYTV AALSQLLVYC YGGTLVAESS TGLCRAMFSC PWQLFKPKQR RLVQLLILRS QRPVSMAVPF FSPSLATFAA ILQTSGSIIA LVKSFQ // ID O22A_DROME STANDARD; PRT; 397 AA. AC P81909; Q9U6X7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 22a. GN OR22A OR OR22A.1 OR DOR22A.1 OR DOR53 OR AN11 OR CG12193. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Berkeley; RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 5-397 FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RC TISSUE=Antenna; RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN 17-20 SENSORY NEURONS ON THE CC MEDIAL-PROXIMAL EDGE OF THE ANTENNA. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003586; AAF51364.1; -. DR EMBL; AF127923; AAD26358.2; -. DR FlyBase; FBgn0026398; Or22a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; KW Multigene family. FT DOMAIN 1 49 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 50 70 1 (POTENTIAL). FT DOMAIN 71 86 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 87 107 2 (POTENTIAL). FT DOMAIN 108 136 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 137 157 3 (POTENTIAL). FT DOMAIN 158 182 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 183 203 4 (POTENTIAL). FT DOMAIN 204 263 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 264 280 5 (POTENTIAL). FT DOMAIN 281 286 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 287 304 6 (POTENTIAL). FT DOMAIN 305 356 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 357 377 7 (POTENTIAL). FT DOMAIN 378 397 CYTOPLASMIC (POTENTIAL). FT CONFLICT 256 256 D -> SIPFLFINGLFLFLS (IN REF. 1). FT CONFLICT 376 397 MVKLAFSVVTVIKQFNLAERFQ -> VGVNILDISLILHLF FT (IN REF. 1). SQ SEQUENCE 397 AA; 46753 MW; E9D20EF06E69E883 CRC64; MLSKFFPHIK EKPLSERVKS RDAFIYLDRV MWSFGWTEPE NKRWILPYKL WLAFVNIVML ILLPISISIE YLHRFKTFSA GEFLSSLEIG VNMYGSSFKC AFTLIGFKKR QEAKVLLDQL DKRCLSDKER STVHRYVAMG NFFDILYHIF YSTFVVMNFP YFLLERRHAW RMYFPYIDSD EQFYISSIAE CFLMTEAIYM DLCTDVCPLI SMLMARCHIS LLKQRLRNLR SKPGRTEDEY LEELTECIRD HRLLLDYVDA LRPVFSGTIF VQFLLIGTVL GLSMINLMFF STFWTGVATC LFMFDVSMET FPFCYLCNMI IDDCQEMSNC LFQSDWTSAD RRYKSTLVYF LHNLQQPITL TAGGVFPISM QTNLAMVKLA FSVVTVIKQF NLAERFQ // ID O22B_DROME STANDARD; PRT; 397 AA. AC P81910; Q9U6X6; Q9VQ19; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 22b. GN OR22B OR OR22A.2 OR DOR22A.2 OR DOR67 OR AN12 OR CG4231. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). RN [2] RP REVISION TO 58. RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RC TISSUE=Antenna; RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN 20-22 SENSORY NEURONS ON THE CC MEDIAL-PROXIMAL EDGE OF THE ANTENNA. THIS EXPRESSION PATTERN CC MATCHES THE DISTRIBUTION OF THE LARGE SENSILLA BASICONICA. CC EXPRESSION IS FIRST SEEN AT 60 HOURS APF IN A SUBSET OF CELLS CC RESTRICTED TO A SUBREGION OF THE DEVELOPING ANTENNA. EXPRESSION CC CONTINUES THROUGHOUT ANTENNAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF127924; AAD26359.2; -. DR EMBL; AE003586; AAF51363.1; -. DR FlyBase; FBgn0026397; Or22b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; KW Multigene family. FT DOMAIN 1 49 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 50 70 1 (POTENTIAL). FT DOMAIN 71 85 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 86 105 2 (POTENTIAL). FT DOMAIN 106 143 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 144 164 3 (POTENTIAL). FT DOMAIN 165 194 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 195 215 4 (POTENTIAL). FT DOMAIN 216 268 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 269 289 5 (POTENTIAL). FT DOMAIN 290 295 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 296 316 6 (POTENTIAL). FT DOMAIN 317 347 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 348 368 7 (POTENTIAL). FT DOMAIN 369 397 CYTOPLASMIC (POTENTIAL). FT CONFLICT 58 58 V -> L (IN REF. 3, 4 AND 5). FT CONFLICT 256 256 D -> TICFDKFFYLPYFFS (IN REF. 3). FT CONFLICT 376 397 MVKLAFTVVTIVKQFNLAEKFQ -> VSINQYEL (IN FT REF. 3). SQ SEQUENCE 397 AA; 46387 MW; EB7816E9D0A13E50 CRC64; MLSQFFPHIK EKPLSERVKS RDAFVYLDRV MWSFGWTVPE NKRWDLHYKL WSTFVTLVIF ILLPISVSVE YIQRFKTFSA GEFLSSIQIG VNMYGSSFKS YLTMMGYKKR QEAKMSLDEL DKRCVCDEER TIVHRHVALG NFCYIFYHIA YTSFLISNFL SFIMKRIHAW RMYFPYVDPE KQFYISSIAE VILRGWAVFM DLCTDVCPLI SMVIARCHIT LLKQRLRNLR SEPGRTEDEY LKELADCVRD HRLILDYVDA LRSVFSGTIF VQFLLIGIVL GLSMINIMFF STLSTGVAVV LFMSCVSMQT FPFCYLCNMI MDDCQEMADS LFQSDWTSAD RRYKSTLVYF LHNLQQPIIL TAGGVFPISM QTNLNMVKLA FTVVTIVKQF NLAEKFQ // ID O22C_DROME STANDARD; PRT; 402 AA. AC P81911; Q9VQ70; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 22c. GN OR22C OR OR22C.1 OR DOR22C.1 OR CG15377. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP IDENTIFICATION. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: NOT EXPRESSED IN EITHER THE ANTENNA OR CC MAXILLARY PALP. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003584; AAF51309.2; -. DR FlyBase; FBgn0026396; Or22c. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 42 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 43 63 1 (POTENTIAL). FT DOMAIN 64 73 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 74 94 2 (POTENTIAL). FT DOMAIN 95 134 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 135 155 3 (POTENTIAL). FT DOMAIN 156 173 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 174 194 4 (POTENTIAL). FT DOMAIN 195 201 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 202 222 5 (POTENTIAL). FT DOMAIN 223 276 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 277 297 6 (POTENTIAL). FT DOMAIN 298 307 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 308 328 7 (POTENTIAL). FT DOMAIN 329 379 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 402 AA; 44873 MW; 0E11A6CF16D29B2E CRC64; MTDSGQPAIA DHFYRIPRIS GLIVGLWPQR IRGGGGRPWH AHLLFVFAFA MVVVGAVGEV SYGCVHLDNL VVALEAFCPG TTKAVCVLKL WVFFRSNRRW AELVQRLRAI LWESRRQEAQ RMLVGLATTA NRLSLLLLSS GTATNAAFTL QPLIMGLYRW IVQLPGQTEL PFNIILPSFA VQPGVFPLTY VLLTASGACT VFAFSFVDGF FICSCLYICG AFRLVQQDIR RIFADLHGDS VDVFTEEMNA EVRHRLAQVV ERHNAIIDFC TDLTRQFTVI VLMHFLSAAF VLCSTILDIM LNTSSLSGLT YICYIIAALT QLFLYCFGGN HVSESSAAVA DVLYDMEWYK CDARTRKVIL MILRRSQRAK TIAVPFFTPS LPALRSILST AGSYITLLKT FL // ID O23A_DROME STANDARD; PRT; 379 AA. AC P81912; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 23a. GN OR23A OR OR23A.1 OR DOR23A.1 OR DOR64 OR AN5 OR CG9880. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). RN [2] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN 10-40 SENSORY CELLS IN THE THIRD CC ANTENNA SEGMENT AND IN THE MAXILLARY PALP. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF127925; AAD26360.1; -. DR EMBL; AE003582; AAF51230.3; -. DR FlyBase; FBgn0026395; Or23a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; KW Multigene family. FT DOMAIN 1 36 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 37 57 1 (POTENTIAL). FT DOMAIN 58 64 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 65 85 2 (POTENTIAL). FT DOMAIN 86 125 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 126 146 3 (POTENTIAL). FT DOMAIN 147 162 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 163 183 4 (POTENTIAL). FT DOMAIN 184 253 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 254 274 5 (POTENTIAL). FT DOMAIN 275 280 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 281 301 6 (POTENTIAL). FT DOMAIN 302 340 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 341 361 7 (POTENTIAL). FT DOMAIN 362 379 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 379 AA; 43793 MW; 4DC3E1D9F4C8BBCF CRC64; MKLSETLKID YFRVQLNAWR ICGALDLSEG RYWSWSMLLC ILVYLPTPML LRGVYSFEDP VENNFSLSLT VTSLSNLMKF CMYVAQLTKM VEVQSLIGQL DARVSGESQS ERHRNMTEHL LRMSKLFQIT YAVVFIIAAV PFVFETELSL PMPMWFPFDW KNSMVAYIGA LVFQEIGYVF QIMQCFAADS FPPLVLYLIS EQCQLLILRI SEIGYGYKTL EENEQDLVNC IRDQNALYRL LDVTKSLVSY PMMVQFMVIG INIAITLFVL IFYVETLYDR IYYLCFLLGI TVQTYPLCYY GTMVQESFAE LHYAVFCSNW VDQSASYRGH MLILAERTKR MQLLLAGNLV PIHLSTYVAC WKGAYSFFTL MADRDGLGS // ID O24A_DROME STANDARD; PRT; 369 AA. AC P81913; Q9VQX1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 24a. GN OR24A OR OR24D.1 OR DOR24D.1 OR CG11767. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP IDENTIFICATION. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: NOT EXPRESSED IN EITHER THE ANTENNA OR CC MAXILLARY PALP. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003577; AAF51040.1; -. DR FlyBase; FBgn0026394; Or24a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 35 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 36 56 1 (POTENTIAL). FT DOMAIN 57 63 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 64 84 2 (POTENTIAL). FT DOMAIN 85 95 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 96 116 3 (POTENTIAL). FT DOMAIN 117 170 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 171 191 4 (POTENTIAL). FT DOMAIN 192 240 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 241 261 5 (POTENTIAL). FT DOMAIN 262 266 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 267 287 6 (POTENTIAL). FT DOMAIN 288 338 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 339 359 7 (POTENTIAL). FT DOMAIN 360 369 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 369 AA; 42181 MW; 309BC89B592DA9B5 CRC64; MERHYFMVPK FALSLIGFYP EQKRTVLVKL WSFFNFFILT YGCYAEAYYG IHYIPINIAT ALDALCPVAS SILSLVKMVA IWWYQDELRS LIERRFYTLA TQLTFLLLCC GFCTSTSYSV RHLIDNILRR THGKDWIYET PFKMMFPDLL LRLPLYPITY ILVHWHGYIT VVCFVGADGF FLGFCLYFTV LLLCLQDDVC DLLEVENIEK SPSEAEEARI VREMEKLVDR HNEVAELTER LSGVMVEITL AHFVTSSLII GTSVVDILLF SGLGIIVYVV YTCAVGVEIF LYCLGGSHIM EACSNLARST FSSHWYGHSV RVQKMTLLMV ARAQRVLTIK IPFFSPSLET LTSILRFTGS LIALAKSVI // ID O30A_DROME STANDARD; PRT; 378 AA. AC Q9VLE5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 30a. GN OR30A OR CG13106. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003623; AAF52748.2; ALT_SEQ. DR FlyBase; FBgn0032096; Or30a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 34 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 35 55 1 (POTENTIAL). FT DOMAIN 56 65 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 66 86 2 (POTENTIAL). FT DOMAIN 87 127 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 128 148 3 (POTENTIAL). FT DOMAIN 149 172 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 173 193 4 (POTENTIAL). FT DOMAIN 194 254 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 255 275 5 (POTENTIAL). FT DOMAIN 276 280 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 281 301 6 (POTENTIAL). FT DOMAIN 302 344 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 345 365 7 (POTENTIAL). FT DOMAIN 366 378 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 378 AA; 43997 MW; 5D70161A2582D993 CRC64; MELKSMDPVE MPIFGSTLKL MKFWSYLFVH NWRRYVAMTP YIIINCTQYV DIYLSTESLD FIIRNVYLAV LFTNTVVRGV LLCVQRFSYE RFINILKSFY IELLQSDDPI INILVKETTR LSVLISRINL LMGCCTCIGF VTYPIFGSER VLPYGMYLPT IDEYKYASPY YEIFFVIQAI MAPMGCCMYI PYTNMVVTFT LFAILMCRVL QHKLRSLEKL KNEQVRGEII WCIKYQLKLS GFVDSMNALN THLHLVEFLC FGAMLCVLLF SLIIAQTIAQ TVIVIAYMVM IFANSVVLYY VANELYFQSF DIAIAAYESN WMDFDVDTQK TLKFLIMRSQ KPLAILVGGT YPMNLKMLQS LLNAIYSFFT LLRRVYGZ // ID O33A_DROME STANDARD; PRT; 378 AA. AC P81914; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 33a. GN OR33A OR OR33B.1 OR DOR33B.1 OR DOR73 OR AN3 OR CG16960. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003634; AAF53131.1; -. DR FlyBase; FBgn0026392; Or33a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 33 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 34 54 1 (POTENTIAL). FT DOMAIN 55 62 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 63 83 2 (POTENTIAL). FT DOMAIN 84 127 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 128 148 3 (POTENTIAL). FT DOMAIN 149 163 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 164 184 4 (POTENTIAL). FT DOMAIN 185 254 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 255 275 5 (POTENTIAL). FT DOMAIN 276 285 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 286 306 6 (POTENTIAL). FT DOMAIN 307 355 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 356 376 7 (POTENTIAL). FT DOMAIN 377 378 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 189 189 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 330 330 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 378 AA; 43891 MW; D5BE000865EBCA21 CRC64; MDSRRKVRSE NLYKTYWLYW RLLGVEGDYP FRRLVDFTIT SFITILFPVH LILGMYKKPQ IQVFRSLHFT SECLFCSYKF FCFRWKLKEI KTIEGLLQDL DSRVESEEER NYFNQNPSRV ARMLSKSYLV AAISAIITAT VAGLFSTGRN LMYLGWFPYD FQATAAIYWI SFSYQAIGSS LLILENLAND SYPPITFCVV SGHVRLLIMR LSRIGHDVKL SSSENTRKLI EGIQDHRKLM KIIRLLRSTL HLSQLGQFLS SGINISITLI NILFFAENNF AMLYYAVFFA AMLIELFPSC YYGILMTMEF DKLPYAIFSS NWLKMDKRYN RSLIILMQLT LVPVNIKAGG IVGIDMSAFF ATVRMAYSFY TLALSFRV // ID O33B_DROME STANDARD; PRT; 379 AA. AC P81915; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 33b. GN OR33B OR OR33B.2 OR DOR33B.2 OR DOR72 OR AN1 OR CG16961. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003634; AAF53132.1; -. DR FlyBase; FBgn0026391; Or33b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 37 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 38 58 1 (POTENTIAL). FT DOMAIN 59 64 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 65 85 2 (POTENTIAL). FT DOMAIN 86 129 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 130 150 3 (POTENTIAL). FT DOMAIN 151 165 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 166 186 4 (POTENTIAL). FT DOMAIN 187 256 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 257 277 5 (POTENTIAL). FT DOMAIN 278 281 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 282 302 6 (POTENTIAL). FT DOMAIN 303 355 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 356 376 7 (POTENTIAL). FT DOMAIN 377 379 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 191 191 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 253 253 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 328 328 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 379 AA; 43633 MW; 4A50047EC1113C0E CRC64; MDLKPRVIRS EDIYRTYWLY WHLLGLESNF FLNRLLDLVI TIFVTIWYPI HLILGLFMER SLGDVCKGLP ITAACFFASF KFICFRFKLS EIKEIEILFK ELDQRALSRE ECEFFNQNTR REANFIWKSF IVAYGLSNIS AIASVLFGGG HKLLYPAWFP YDVQATELIF WLSVTYQIAG VSLAILQNLA NDSYPPMTFC VVAGHVRLLA MRLSRIGQGP EETIYLTGKQ LIESIEDHRK LMKIVELLRS TMNISQLGQF ISSGVNISIT LVNILFFADN NFAITYYGVY FLSMVLELFP CCYYGTLISV EMNQLTYAIY SSNWMSMNRS YSRILLIFMQ LTLAEVQIKA GGMIGIGMNA FFATVRLAYS FFTLAMSLR // ID O33C_DROME STANDARD; PRT; 384 AA. AC P81916; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 33c. GN OR33C OR OR33B.3 OR DOR33B.3 OR DOR71 OR AN2 OR CG5006. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ANTENNA AND IN A SUBSET OF 18 CC OLFACTORY RECEPTOR NEURONS IN THE MAXILLARY PALP. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003634; AAF53133.1; -. DR FlyBase; FBgn0026390; Or33c. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 35 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 36 56 1 (POTENTIAL). FT DOMAIN 57 63 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 64 84 2 (POTENTIAL). FT DOMAIN 85 128 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 129 149 3 (POTENTIAL). FT DOMAIN 150 169 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 170 190 4 (POTENTIAL). FT DOMAIN 191 251 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 252 272 5 (POTENTIAL). FT DOMAIN 273 274 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 275 295 6 (POTENTIAL). FT DOMAIN 296 358 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 359 379 7 (POTENTIAL). FT DOMAIN 380 384 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 193 193 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 384 AA; 44374 MW; 9F71EEC446BDAAE6 CRC64; MVIIDSLSFY RPFWICMRLL VPTFFKDSSR PVQLYVVLLH ILVTLWFPLH LLLHLLLLPS TAEFFKNLTM SLTCVACSLK HVAHLYHLPQ IVEIESLIEQ LDTFIASEQE HRYYRDHVHC HARRFTRCLY ISFGMIYALF LFGVFVQVIS GNWELLYPAY FPFDLESNRF LGAVALGYQV FSMLVEGFQG LGNDTYTPLT LCLLAGHVHL WSIRMGQLGY FDDETVVNHQ RLLDYIEQHK LLVRFHNLVS RTISEVQLVQ LGGCGATLCI IVSYMLFFVG DTISLVYYLV FFGVVCVQLF PSCYFASEVA EELERLPYAI FSSRWYDQSR DHRFDLLIFT QLTLGNRGWI IKAGGLIELN LNAFFATLKM AYSLFAVVVR AKGI // ID O35A_DROME STANDARD; PRT; 416 AA. AC Q9V3Q2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 35a. GN OR35A OR BG:BACR44L22.5 OR CG17868. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -!- CAUTION: REF.1 AND REF.2 SEQUENCES DIFFER FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003413; AAF44954.1; ALT_SEQ. DR EMBL; AE003648; AAF53473.1; ALT_SEQ. DR FlyBase; FBgn0028946; Or35a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 35 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 36 56 1 (POTENTIAL). FT DOMAIN 57 64 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 65 85 2 (POTENTIAL). FT DOMAIN 86 139 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 140 160 3 (POTENTIAL). FT DOMAIN 161 177 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 178 198 4 (POTENTIAL). FT DOMAIN 199 273 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 274 294 5 (POTENTIAL). FT DOMAIN 295 302 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 303 323 6 (POTENTIAL). FT DOMAIN 324 379 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 380 400 7 (POTENTIAL). FT DOMAIN 401 416 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 416 AA; 48164 MW; 78D5E447F782F8FB CRC64; MVRYVPRFAD GQKVKLAWPL AVFRLNHIFW PLDPSTGKWG RYLDKVLAVA MSLVFMQHND AELRYLRFEA SNRNLDAFLT GMPTYLILVE AQFRSLHILL HFEKLQKFLE IFYANIYIDP RKEPEMFRKV DGKMIINRLV SAMYGAVISL YLIAPVFSII NQSKDFLYSM IFPFDSDPLY IFVPLLLTNV WVGIVIDTMM FGETNLLCEL IVHLNGSYML LKRDLQLAIE KILVARDRPH MAKQLKVLIT KTLRKNVALN QFGQQLEAQY TVRVFIMFAF AAGLLCALSF KAYTNPMANY IYAIWFGAKT VELLSLGQIG SDLAFTTDSL STMYYLTHWE QILQYSTNPS ENLRLLKLIN LAIEMNSKPF YVTGLKYFRV SLQAGLKILQ ASFSYFTFLT SMQRRQMSNY GVKTVE // ID O42A_DROME STANDARD; PRT; 406 AA. AC Q9V9I2; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 42a. GN OR42A OR CG17250. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003785; AAF57307.2; -. DR FlyBase; FBgn0033041; Or42a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 44 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 45 65 1 (POTENTIAL). FT DOMAIN 66 86 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 87 107 2 (POTENTIAL). FT DOMAIN 108 142 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 143 163 3 (POTENTIAL). FT DOMAIN 164 181 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 182 202 4 (POTENTIAL). FT DOMAIN 203 271 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 272 292 5 (POTENTIAL). FT DOMAIN 293 298 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 299 319 6 (POTENTIAL). FT DOMAIN 320 359 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 360 380 7 (POTENTIAL). FT DOMAIN 381 406 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 406 AA; 46916 MW; D7B7FE8C5493D6C6 CRC64; MDLRRWFPTL YTQSKDSPVR SRDATLYLLR CVFLMGVRKP PAKFFVAYVL WSFALNFCST FYQPIGFLTG YISHLSEFSP GEFLTSLQVA FNAWSCSTKV LIVWALVKRF DEANNLLDEM DRRITDPGER LQIHRAVSLS NRIFFFFMAV YMVYATNTFL SAIFIGRPPY QNYYPFLDWR SSTLHLALQA GLEYFAMAGA CFQDVCVDCY PVNFVLVLRA HMSIFAERLR RLGTYPYESQ EQKYERLVQC IQDHKVILRF VDCLRPVISG TIFVQFLVVG LVLGFTLINI VLFANLGSAI AALSFMAAVL LETTPFCILC NYLTEDCYKL ADALFQSNWI DEEKRYQKTL MYFLQKLQQP ITFMAMNVFP ISVGTNISVT KFSFSVFTLV KQMNISEKLA KSEMEE // ID O42B_DROME STANDARD; PRT; 399 AA. AC Q9V9I4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 42b. GN OR42B OR CG12754. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003785; AAF57305.2; -. DR FlyBase; FBgn0033043; Or42b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 45 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 46 66 1 (POTENTIAL). FT DOMAIN 67 83 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 84 104 2 (POTENTIAL). FT DOMAIN 105 140 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 141 161 3 (POTENTIAL). FT DOMAIN 162 178 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 179 199 4 (POTENTIAL). FT DOMAIN 200 268 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 269 289 5 (POTENTIAL). FT DOMAIN 290 292 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 293 313 6 (POTENTIAL). FT DOMAIN 314 356 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 357 377 7 (POTENTIAL). FT DOMAIN 378 399 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 234 234 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 399 AA; 46074 MW; 0435E598EDB6E2ED CRC64; MVFELIRPAP LTEQKRSRDG CIYLYRAMKF IGWLPPKQGV LRYVYLTWTL MTFVWCTTYL PLGFLGSYMT QIKSFSPGEF LTSLQVCINA YGSSVKVAIT YSMLWRLIKA KNILDQLDLR CTAMEEREKI HLVVARSNHA FLIFTFVYCG YAGSTYLSSV LSGRPPWQLY NPFIDWHDGT LKLWVASTLE YMVMSGAVLQ DQLSDSYPLI YTLILRAHLD MLRERIRRLR SDENLSEAES YEELVKCVMD HKLILRYCAI IKPVIQGTIF TQFLLIGLVL GFTLINVFFF SDIWTGIASF MFVITILLQT FPFCYTCNLI MEDCESLTHA IFQSNWVDAS RRYKTTLLYF LQNVQQPIVF IAGGIFQISM SSNISVAKFA FSVITITKQM NIADKFKTD // ID O43A_DROME STANDARD; PRT; 376 AA. AC P81917; Q9U6X4; Q9V4J0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 43a. GN OR43A OR OR43B.1 OR DOR43B.1 OR DOR87 OR AN14 OR CG1854. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-342 FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN 20 SENSORY NEURONS ON THE DISTAL CC EDGE OF THE ANTENNA. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF127926; AAD26361.1; -. DR EMBL; AE003842; AAF59280.1; -. DR FlyBase; FBgn0026389; Or43a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; KW Multigene family. FT DOMAIN 1 32 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 33 53 1 (POTENTIAL). FT DOMAIN 54 58 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 59 79 2 (POTENTIAL). FT DOMAIN 80 123 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 124 144 3 (POTENTIAL). FT DOMAIN 145 178 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 179 199 4 (POTENTIAL). FT DOMAIN 200 247 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 248 268 5 (POTENTIAL). FT DOMAIN 269 276 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 277 297 6 (POTENTIAL). FT DOMAIN 298 342 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 343 363 7 (POTENTIAL). FT DOMAIN 364 376 CYTOPLASMIC (POTENTIAL). FT CONFLICT 154 154 L -> V (IN REF. 1). FT CONFLICT 237 272 MISSING (IN REF. 3). SQ SEQUENCE 376 AA; 43090 MW; 1B3638FE7EA49606 CRC64; MTIEDIGLVG INVRMWRHLA VLYPTPGSSW RKFAFVLPVT AMNLMQFVYL LRMWGDLPAF ILNMFFFSAI FNALMRTWLV IIKRRQFEEF LGQLATLFHS ILDSTDEWGR GILRRAEREA RNLAILNLSA SFLDIVGALV SPLFREERAH PFGLALPGVS MTSSPVYEVI YLAQLPTPLL LSMMYMPFVS LFAGLAIFGK AMLQILVHRL GQIGGEEQSE EERFQRLASC IAYHTQVMRY VWQLNKLVAN IVAVEAIIFG SIICSLLFCL NIITSPTQVI SIVMYILTML YVLFTYYNRA NEICLENNRV AEAVYNVPWY EAGTRFRKTL LIFLMQTQHP MEIRVGNVYP MTLAMFQSLL NASYSYFTML RGVTGK // ID O43B_DROME STANDARD; PRT; 403 AA. AC P81918; Q9U6Y0; Q9V332; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 43b. GN OR43B OR OR44A.1 OR DOR25A.1 OR AN7 OR CG17853. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN 16 OLFACTORY RECEPTOR NEURONS IN CC A BROAD AREA ACROSS THE ANTENNA, INCLUDING BOTH ANTERIOR AND CC POSTERIOR FACES AND IN THE MAXILLARY PALP. THIS EXPRESSION PATTERN CC MATCHES THE DISTRIBUTRION OF THE SMALL SENSILLA BASICONICA. CC EXPRESSION IN THE ANTENNA IS OBSERVED LATE IN ANTENNAL DEVELOPMENT CC AT 93 HOURS APF. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003839; AAF59173.2; -. DR FlyBase; FBgn0026393; Or43b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 49 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 50 70 1 (POTENTIAL). FT DOMAIN 71 83 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 84 104 2 (POTENTIAL). FT DOMAIN 105 139 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 140 160 3 (POTENTIAL). FT DOMAIN 161 193 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 194 214 4 (POTENTIAL). FT DOMAIN 215 271 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 272 292 5 (POTENTIAL). FT DOMAIN 293 299 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 300 320 6 (POTENTIAL). FT DOMAIN 321 372 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 373 393 7 (POTENTIAL). FT DOMAIN 394 403 CYTOPLASMIC (POTENTIAL). FT CONFLICT 259 259 N -> KCS (IN REF. 1). SQ SEQUENCE 403 AA; 46625 MW; 90C55CCBB5C5B94F CRC64; MFGHFKLVYP APISEPIQSR DSNAYMMETL RNSGLNLKND FGIGRKIWRV FSFTYNMVIL PVSFPINYVI HLAEFPPELL LQSLQLCLNT WCFALKFFTL IVYTHRLELA NKHFDELDKY CVKPAEKRKV RDMVATITRL YLTFVVVYVL YATSTLLDGL LHHRVPYNTY YPFINWRVDR TQMYIQSFLE YFTVGYAIYV ATATDSYPVI YVAALRTHIL LLKDRIIYLG DPSNEGSSDP SYMFKSLVDC IKAHRTMLNF CDAIQPIISG TIFAQFIICG SILGIIMINM VLFADQSTRF GIVIYVMAVL LQTFPLCFYC NAIVDDCKEL AHALFHSAWW VQDKRYQRTV IQFLQKLQQP MTFTAMNIFN INLATNINVA KFAFTVYAIA SGMNLDQKLS IKE // ID O45A_DROME STANDARD; PRT; 378 AA. AC Q9V568; DT 16-OCT-2001 (Rel. 40, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Putative odorant receptor 45a. GN OR45A OR CG1978. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003833; AAF58951.3; -. DR FlyBase; FBgn0033404; Or45a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 30 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 31 51 1 (POTENTIAL). FT DOMAIN 52 129 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 130 150 2 (POTENTIAL). FT DOMAIN 151 173 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 174 194 3 (POTENTIAL). FT DOMAIN 195 197 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 198 218 4 (POTENTIAL). FT DOMAIN 219 249 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 250 270 5 (POTENTIAL). FT DOMAIN 271 285 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 286 306 6 (POTENTIAL). FT DOMAIN 307 342 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 343 363 7 (POTENTIAL). FT DOMAIN 364 378 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 378 AA; 43338 MW; BC0BEF021AA26973 CRC64; MDASYFAVQR RALEIVGFDP STPQLSLKHP IWAGILILSL ISHNWPMVVY ALQDLSDLTR LTDNFAVFMQ GSQSTFKFLV MMAKRRRIGS LIHRLHKLNQ AASATPNHLE KIERENQLDR YVARSFRNAA YGVICASAIA PMLLGLWGYV ETGVFTPTTP MEFNFWLDER KPHFYWPIYV WGVLGVAAAA WLAIATDTLF SWLTHNVVIQ FQLLELVLEE KDLNGGDSRL TGFVSRHRIA LDLAKELSSI FGEIVFVKYM LSYLQLCMLA FRFSRSGWSA QVPFRATFLV AIIIQLSSYC YGGEYIKQQS LAIAQAVYGQ INWPEMTPKK RRLWQMVIMR AQRPAKIFGF MFVVDLPLLL WVIRTAGSFL AMLRTFER // ID O45B_DROME STANDARD; PRT; 396 AA. AC Q9V589; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 45b. GN OR45B OR CG12931. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003833; AAF58928.1; -. DR FlyBase; FBgn0033422; Or45b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 60 1 (POTENTIAL). FT DOMAIN 61 73 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 74 94 2 (POTENTIAL). FT DOMAIN 95 135 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 136 156 3 (POTENTIAL). FT DOMAIN 157 200 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 201 221 4 (POTENTIAL). FT DOMAIN 222 276 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 277 297 5 (POTENTIAL). FT DOMAIN 298 301 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 302 322 6 (POTENTIAL). FT DOMAIN 323 369 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 370 390 7 (POTENTIAL). FT DOMAIN 391 396 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 396 AA; 46324 MW; 91A87F38F0572A84 CRC64; MYPRFLSRNY PLAKHLFFVT RYSFGLLGLR FGKEQSWLHL LWLVFNFVNL AHCCQAEFVF GWSHLRTSPV DAMDAFCPLA CSFTTLFKLG WMWWRRQEVA DLMDRIRLLI GEQEKREDSR RKVAQRSYYL MVTRCGMLVF TLGSITTGAF VLRSLWEMWV RRHQEFKFDM PFRMLFHDFA HRMPWFPVFY LYSTWSGQVT VYAFAGTDGF FFGFTLYMAF LLQALRYDIQ DALKPIRDPS LRESKICCQR LADIVDRHNE IEKIVKEFSG IMAAPTFVHF VSASLVIATS VIDILLYSGY NIIRYVVYTF TVSSAIFLYC YGGTEMSTES LSLGEAAYSS AWYTWDRETR RRVFLIILRA QRPITVRVPF FAPSLPVFTS VIKFTGSIVA LAKTIL // ID O46A_DROME STANDARD; PRT; 385 AA. AC P81919; Q9U6X9; Q9V5H3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 46a. GN OR46A OR OR46F.1 OR DOR46F.1 OR AN9 OR CG17849. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN A SUBSET OF 17 OLFACTORY RECEPTOR CC NEURONS IN THE MAXILLARY PALP. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003830; AAF58834.2; -. DR FlyBase; FBgn0026388; Or46a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 37 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 38 58 1 (POTENTIAL). FT DOMAIN 59 65 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 66 86 2 (POTENTIAL). FT DOMAIN 87 127 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 128 148 3 (POTENTIAL). FT DOMAIN 149 170 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 171 191 4 (POTENTIAL). FT DOMAIN 192 255 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 256 276 5 (POTENTIAL). FT DOMAIN 277 287 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 288 308 6 (POTENTIAL). FT DOMAIN 309 354 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 355 375 7 (POTENTIAL). FT DOMAIN 376 385 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 385 AA; 44483 MW; BB062862B7A59310 CRC64; MSKGVEIFYK GQKAFLNILS LWPQIERRWR IIHQVNYVHV IVFWVLLFDL LLVLHVMANL SYMSEVVKAI FILATSAGHT TKLLSIKANN VQMEELFRRL DNEEFRPRGA NEELIFAAAC ERSRKLRDFY GALSFAALSM ILIPQFALDW SHLPLKTYNP LGENTGSPAY WLLYCYQCLA LSVSCITNIG FDSLCSSLFI FLKCQLDILA VRLDKIGRLI TTSGGTVEQQ LKENIRYHMT IVELSKTVER LLCKPISVQI FCSVLVLTAN FYAIAVLSDE RLELFKYVTY QACMLIQIFI LCYYAGEVTQ RSLDLPHELY KTSWVDWDYR SRRIALLFMQ RLHSTLRIRT LNPSLGFDLM LFSSVSSFRV LTFLCTVANF HNEAH // ID O46B_DROME STANDARD; PRT; 384 AA. AC Q9V3N2; P81920; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 46b. GN OR46B OR OR46F.2 OR OR46F OR DOR46F OR DOR19 OR AN8 OR CG17848. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). RN [4] RP IDENTIFICATION. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). RN [5] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ANTENNA. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS AT SEVERAL POSITIONS FROM THAT CC SHOWN DUE TO DIFFERENCES IN THE PREDICTION OF SPLICE SITES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003830; AAF58833.1; ALT_SEQ. DR FlyBase; FBgn0026387; Or46b. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; KW Multigene family. FT DOMAIN 1 35 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 36 56 1 (POTENTIAL). FT DOMAIN 57 65 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 66 86 2 (POTENTIAL). FT DOMAIN 87 127 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 128 148 3 (POTENTIAL). FT DOMAIN 149 169 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 170 190 4 (POTENTIAL). FT DOMAIN 191 255 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 256 276 5 (POTENTIAL). FT DOMAIN 277 290 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 291 311 6 (POTENTIAL). FT DOMAIN 312 357 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 358 378 7 (POTENTIAL). FT DOMAIN 379 384 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 384 AA; 44450 MW; B86E9D7F6CC665C4 CRC64; MVTEDFYKYQ VWYFQILGVW QLPTWAADHQ RRFQSMRFGF ILVILFIMLL LFSFEMLNNI SQVREILKVF FMFATEISCM AKLLHLKLKS RKLAGLVDAM LSPEFGVKSE QEMQMLELDR VAVVRMRNSY GIMSLGAASL ILIVPCFDNF GELPLAMLEV CSIEGWICYW SQYLFHSICL LPTCVLNITY DSVAYSLLCF LKVQLQMLVL RLEKLGPVIE PQDNEKIAME LRECAAYYNR IVRFKDLVEL FIKGPGSVQL MCSVLVLVSN LYDMSTMSIA NGDAIFMLKT CIYQLVMLWQ IFIICYASNE VTVQSSRLCH SIYSSQWTGW NRANRRIVLL MMQRFNSPML LSTFNPTFAF SLEAFGSIVN CSYSYFALLK RVNS // ID O47A_DROME STANDARD; PRT; 385 AA. AC P81921; Q9U6X8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 47a. GN OR47A OR OR47E.1 OR DOR47E.1 OR DOR24 OR AN10 OR CG13225. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN 40 OLFACTORY RECEPTOR NEURONS IN CC A BROAD AREA ACROSS THE ANTENNA, INCLUDING BOTH ANTERIOR AND CC POSTERIOR FACES. THIS EXPRESSION PATTERN MATCHES THE DISTRIBUTION CC OF THE SMALL SENSILLA BASICONICA. EXPRESSION IN THE ANTENNA IS CC OBSERVED LATE IN ANTENNAL DEVELOPMENT AT 93 HOURS APF. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF156880; AAD39006.1; -. DR EMBL; AE003826; AAF58695.1; -. DR FlyBase; FBgn0026386; Or47a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; KW Multigene family. FT DOMAIN 1 33 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 34 54 1 (POTENTIAL). FT DOMAIN 55 62 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 63 83 2 (POTENTIAL). FT DOMAIN 84 129 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 130 150 3 (POTENTIAL). FT DOMAIN 151 175 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 176 196 4 (POTENTIAL). FT DOMAIN 197 255 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 256 276 5 (POTENTIAL). FT DOMAIN 277 284 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 285 305 6 (POTENTIAL). FT DOMAIN 306 357 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 358 378 7 (POTENTIAL). FT DOMAIN 379 385 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 385 AA; 43965 MW; 498DA16E50A86038 CRC64; MDSFLQVQKS TIALLGFDLF SENREMWKRP YRAMNVFSIA AIFPFILAAV LHNWKNVLLL ADAMVALLIT ILGLFKFSMI LYLRRDFKRL IDKFRLLMSN EAEQGEEYAE ILNAANKQDQ RMCTLFRTCF LLAWALNSVL PLVRMGLSYW LAGHAEPELP FPCLFPWNIH IIRNYVLSFI WSAFASTGVV LPAVSLDTIF CSFTSNLCAF FKIAQYKVVR FKGGSLKESQ ATLNKVFALY QTSLDMCNDL NQCYQPIICA QFFISSLQLC MLGYLFSITF AQTEGVYYAS FIATIIIQAY IYCYCGENLK TESASFEWAI YDSPWHESLG AGGASTSICR SLLISMMRAH RGFRITGYFF EANMEAFSSI VRTAMSYITM LRSFS // ID O47B_DROME STANDARD; PRT; 400 AA. AC P81922; Q9V5X4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 47b. GN OR47B OR OR47E.2 OR DOR47E.2 OR CG13206. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE ANTENNA. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003826; AAF58667.2; -. DR FlyBase; FBgn0026385; Or47b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 62 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 63 83 1 (POTENTIAL). FT DOMAIN 84 91 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 92 112 2 (POTENTIAL). FT DOMAIN 113 157 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 158 178 3 (POTENTIAL). FT DOMAIN 179 217 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 218 238 4 (POTENTIAL). FT DOMAIN 239 290 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 291 311 5 (POTENTIAL). FT DOMAIN 312 318 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 319 339 6 (POTENTIAL). FT DOMAIN 340 377 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 378 398 7 (POTENTIAL). FT DOMAIN 399 400 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 2 2 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 9 9 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 400 AA; 46553 MW; AE430763043ADAE1 CRC64; MNDSGYQSNL SLLRVFLDEF RSVLRQESPG LIPRLAFYYV RAFLSLPLYR WINLFIMCNV MTIFWTMFVA LPESKNVIEM GDDLVWISGM ALVFTKIFYM HLRCDEIDEL ISDFEYYNRE LRPHNIDEEV LGWQRLCYVI ESGLYINCFC LVNFFSAAIF LQPLLGEGKL PFHSVYPFQW HRLDLHPYTF WFLYIWQSLT SQHNLMSILM VDMVGISTFL QTALNLKLLC IEIRKLGDME VSDKRFHEEF CRVVRFHQHI IKLVGKANRA FNGAFNAQLM ASFSLISIST FETMAAAAVD PKMAAKFVLL MLVAFIQLSL WCVSGTLVYT QSVEVAQAAF DINDWHTKSP GIQRDISFVI LRAQKPLMYV AEPFLPFTLG TYMLVLKNCY RLLALMQESM // ID O49A_DROME STANDARD; PRT; 396 AA. AC Q9V6A9; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 49a. GN OR49A OR CG13158. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003822; AAF58519.3; -. DR FlyBase; FBgn0033727; Or49a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 6 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 7 27 1 (POTENTIAL). FT DOMAIN 28 34 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 35 55 2 (POTENTIAL). FT DOMAIN 56 70 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 71 91 3 (POTENTIAL). FT DOMAIN 92 141 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 142 162 4 (POTENTIAL). FT DOMAIN 163 209 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 210 230 5 (POTENTIAL). FT DOMAIN 231 266 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 267 287 6 (POTENTIAL). FT DOMAIN 288 296 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 297 317 7 (POTENTIAL). FT DOMAIN 318 396 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 203 203 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 396 AA; 46462 MW; DA02277581D46C76 CRC64; MEKLRSYEDF IFMANMMFKT LGYDLFHTPK PWWRYLLVRG YFVLCTISNF YEASMVTTRI IEWESLAGSP SKIMRQGLHF FYMLSSQLKF ITFMINRKRL LQLSHRLKEL YPHKEQNQRK YEVNKYYLSC STRNVLYVYY FVMVVMALEP LVQSCIMYLI GFGKADFTYK RIFPTRLTFD SEKPLGYVLA YVIDFTYSQF IVNVSLGTDL WMMCVSSQIS MHLGYLANML ASIRPSPETE QQDCDFLASI IKRHQLMIRL QKDVNYVFGL LLASNLFTTS CLLCCMAYYT VVEGFNWEGI SYMMLFASVA AQFYVVSSHG QMLIDLSTNL AKAAFESKWY EGSLRYKKEI LILMAQAQRP LEISARGVII ISLDTFKILM TITYRFFAVI RQTVEK // ID O49B_DROME STANDARD; PRT; 375 AA. AC Q9V6H2; Q9U6X5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 49b. GN OR49B OR AN13 OR CG17584. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-342 FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003820; AAF58452.1; -. DR FlyBase; FBgn0028963; Or49b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 28 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 29 49 1 (POTENTIAL). FT DOMAIN 50 60 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 61 77 2 (POTENTIAL). FT DOMAIN 78 121 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 122 142 3 (POTENTIAL). FT DOMAIN 143 176 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 177 197 4 (POTENTIAL). FT DOMAIN 198 251 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 252 272 5 (POTENTIAL). FT DOMAIN 273 278 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 279 299 6 (POTENTIAL). FT DOMAIN 300 342 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 343 363 7 (POTENTIAL). FT DOMAIN 364 375 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 101 101 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 145 146 VL -> GE (IN REF. 2). FT CONFLICT 274 274 S -> SRYVC (IN REF. 2). SQ SEQUENCE 375 AA; 43899 MW; DDC8728734B8B849 CRC64; MFEDIQLIYM NIKILRFWAL LYDKNLRRYV CIGLASFHIF TQIVYMMSTN EGLTGIIRNS YMLVLWINTV LRAYLLLADH DRYLALIQKL TEAYYDLLNL NDSYISEILD QVNKVGKLMA RGNLFFGMLT SMGFGLYPLS SSERVLPFGS KIPGLNEYES PYYEMWYIFQ MLITPMGCCM YIPYTSLIVG LIMFGIVRCK ALQHRLRQVA LKHPYGDRDP RELREEIIAC IRYQQSIIEY MDHINELTTM MFLFELMAFS ALLCALLFML IIVSGTSQLI IVCMYINMIL AQILALYWYA NELREQNLAV ATAAYETEWF TFDVPLRKNI LFMMMRAQRP AAILLGNIRP ITLELFQNLL NTTYTFFTVL KRVYG // ID O56A_DROME STANDARD; PRT; 419 AA. AC Q9V8Y7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 56a. GN OR56A OR CG12501. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003794; AAF57517.2; -. DR FlyBase; FBgn0034473; Or56a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 41 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 42 62 1 (POTENTIAL). FT DOMAIN 63 76 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 77 97 2 (POTENTIAL). FT DOMAIN 98 137 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 138 158 3 (POTENTIAL). FT DOMAIN 159 196 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 197 217 4 (POTENTIAL). FT DOMAIN 218 292 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 293 313 5 (POTENTIAL). FT DOMAIN 314 323 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 324 344 6 (POTENTIAL). FT DOMAIN 345 389 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 390 410 7 (POTENTIAL). FT DOMAIN 411 419 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 419 AA; 48920 MW; F5F82545D2560040 CRC64; MFKVKDLLLS PTTFEDPIFG THLRYFQWYG YVASKDQNRP LLSLIRCTIL TASIWLSCAL MLARVFRGYE NLNDGATSYA TAVQYFAVSI AMFNAYVQRD KVISLLRVAH SDIQNLMHEA DNREMELLVA TQAYTRTITL LIWIPSVIAG LMAYSDCIYR SLFLPKSVFN VPAVRRGEEH PILLFQLFPF GELCDNFVVG YLGPWYALGL GITAIPLWHT FITCLMKYVN LKLQILNKRV EEMDITRLNS KLVIGRLTAS ELTFWQMQLF KEFVKEQLRI RKFVQELQYL ICVPVMADFI IFSVLICFLF FALTVGVPSK MDYFFMFIYL FVMAGILWIY HWHATLIVEC HDELSLAYFS CGWYNFEMPL QKMLVFMMMH AQRPMKMRAL LVDLNLRTFI DIGRGAYSYF NLLRSSHLY // ID O59A_DROME STANDARD; PRT; 397 AA. AC P81923; Q9U6Y1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 59a. GN OR59A OR OR59D.1 OR DOR59D.1 OR DOR46 OR AN6 OR CG9820. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). RN [4] RP IDENTIFICATION. RC STRAIN=Oregon-R; TISSUE=Maxillary palps; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN NEURONS OF THE THIRD ANTENNAL CC SEGMENT. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003460; AAF47004.1; ALT_SEQ. DR FlyBase; FBgn0026384; Or59a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 36 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 37 57 1 (POTENTIAL). FT DOMAIN 58 68 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 69 92 2 (POTENTIAL). FT DOMAIN 93 128 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 129 149 3 (POTENTIAL). FT DOMAIN 150 179 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 180 200 4 (POTENTIAL). FT DOMAIN 201 274 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 275 295 5 (POTENTIAL). FT DOMAIN 296 301 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 302 322 6 (POTENTIAL). FT DOMAIN 323 372 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 373 393 7 (POTENTIAL). FT DOMAIN 394 397 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 345 345 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 397 AA; 46451 MW; 322E25A73288AC92 CRC64; MAEVRVDSLE FFKSHWTAWR YLGVAHFRVE NWKNLYVFYS IVSNLLVTLC YPVHLGISLF RNRTITEDIL NLTTFATCTA CSVKCLLYAY NIKDVLEMER LLRLLDERVV GPEQRSIYGQ VRVQLRNVLY VFIGIYMPCA LFAELSFLFK EERGLMYPAW FPFDWLHSTR NYYIANAYQI VGISFQLLQN YVSDCFPAVV LCLISSHIKM LYNRFEEVGL DPARDAEKDL EACITDHKHI LEWAGGSLVR VLFTFQLFSR LFRRIEAFIS LPMLIQFTVT ALNVCIGLAA LVFFVSEPMA RMYFIFYSLA MPLQIFPSCF FGTDNEYWFG RLHYAAFSCN WHTQNRSFKR KMMLFVEQSL KKSTAVAGGM MRIHLDTFFS TLKGAYSLFT IIIRMRK // ID O59B_DROME STANDARD; PRT; 398 AA. AC Q9W1P8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 59b. GN OR59B OR CG3569. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003460; AAF47008.1; -. DR FlyBase; FBgn0034865; Or59b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 46 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 47 67 1 (POTENTIAL). FT DOMAIN 68 84 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 85 105 2 (POTENTIAL). FT DOMAIN 106 141 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 142 162 3 (POTENTIAL). FT DOMAIN 163 179 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 180 200 4 (POTENTIAL). FT DOMAIN 201 269 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 270 290 5 (POTENTIAL). FT DOMAIN 291 293 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 294 314 6 (POTENTIAL). FT DOMAIN 315 348 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 349 369 7 (POTENTIAL). FT DOMAIN 370 398 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 124 124 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 398 AA; 46164 MW; DF631070C9BAC002 CRC64; MAVFKLIKPA PLTEKVQSRQ GNIYLYRAMW LIGWIPPKEG VLRYVYLFWT CVPFAFGVFY LPVGFIISYV QEFKNFTPGE FLTSLQVCIN VYGASVKSTI TYLFLWRLRK TEILLDSLDK RLANDSDRER IHNMVARCNY AFLIYSFIYC GYAGSTFLSY ALSGRPPWSV YNPFIDWRDG MGSLWIQAIF EYITMSFAVL QDQLSDTYPL MFTIMFRAHM EVLKDHVRSL RMDPERSEAD NYQDLVNCVL DHKTILKCCD MIRPMISRTI FVQFALIGSV LGLTLVNVFF FSNFWKGVAS LLFVITILLQ TFPFCYTCNM LIDDAQDLSN EIFQSNWVDA EPRYKATLVL FMHHVQQPII FIAGGIFPIS MNSNITVAKF AFSIITIVRQ MNLAEQFQ // ID O59C_DROME STANDARD; PRT; 411 AA. AC Q9W1P7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 59c. GN OR59C OR CG17226. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003460; AAF47009.1; -. DR FlyBase; FBgn0034866; Or59c. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 46 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 47 67 1 (POTENTIAL). FT DOMAIN 68 86 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 87 107 2 (POTENTIAL). FT DOMAIN 108 139 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 140 160 3 (POTENTIAL). FT DOMAIN 161 185 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 186 206 4 (POTENTIAL). FT DOMAIN 207 271 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 272 292 5 (POTENTIAL). FT DOMAIN 293 296 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 297 317 6 (POTENTIAL). FT DOMAIN 318 369 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 370 390 7 (POTENTIAL). FT DOMAIN 391 411 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 411 AA; 47473 MW; 08A3495C3555382E CRC64; MTKFFFKRLQ TAPLDQEVSS LDASDYYYRI AFFLGWTPPK GALLRWIYSL WTLTTMWLGI VYLPLGLSLT YVKHFDRFTP TEFLTSLQVD INCIGNVIKS CVTYSQMWRF RRMNELISSL DKRCVTTTQR RIFHKMVARV NLIVILFLST YLGFCFLTLF TSVFAGKAPW QLYNPLVDWR KGHWQLWIAS ILEYCVVSIG TMQELMSDTY AIVFISLFRC HLAILRDRIA NLRQDPKLSE MEHYEQMVAC IQDHRTIIQC SQIIRPILSI TIFAQFMLVG IDLGLAAISI LFFPNTIWTI MANVSFIVAI CTESFPCCML CEHLIEDSVH VSNALFHSNW ITADRSYKSA VLYFLHRAQQ PIQFTAGSIF PISVQSNIAV AKFAFTIITI VNQMNLGEKF FSDRSNGDIN P // ID O63A_DROME STANDARD; PRT; 420 AA. AC Q9VZW8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 63a. GN OR63A OR CG9969. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003476; AAF47697.2; -. DR FlyBase; FBgn0035382; Or63a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 43 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 44 64 1 (POTENTIAL). FT DOMAIN 65 76 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 77 97 2 (POTENTIAL). FT DOMAIN 98 150 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 151 171 3 (POTENTIAL). FT DOMAIN 172 217 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 218 238 4 (POTENTIAL). FT DOMAIN 239 296 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 297 317 5 (POTENTIAL). FT DOMAIN 318 320 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 321 341 6 (POTENTIAL). FT DOMAIN 342 387 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 388 408 7 (POTENTIAL). FT DOMAIN 409 420 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 420 AA; 49611 MW; 310A925CDE0F72A4 CRC64; MYSPEEAAEL KRRNYRSIRE MIRLSYTVGF NLLDPSRCGQ VLRIWTIVLS VSSLASLYGH WQMLARYIHD IPRIGETAGT ALQFLTSIAK MWYFLFAHRQ IYELLRKARC HELLQKCELF ERMSDLPVIK EIRQQVESTM NRYWASTRRQ ILIYLYSCIC ITTNYFINSF VINLYRYFTK PKGSYDIMLP LPSLYPAWEH KGLEFPYYHI QMYLETCSLY ICGMCAVSFD GVFIVLCLHS VGLMRSLNQM VEQATSELVP PDRRVEYLRC CIYQYQRVAN FATEVNNCFR HITFTQFLLS LFNWGLALFQ MSVGLGNNSS ITMIRMTMYL VAAGYQIVVY CYNGQRFATA SEEIANAFYQ VRWYGESREF RHLIRMMLMR TNRGFRLDVS WFMQMSLPTL MAMVRTSGQY FLLLQNVNQK // ID O65A_DROME STANDARD; PRT; 417 AA. AC P82982; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 65a. GN OR65A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003563; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041625; Or65a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 62 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 63 83 1 (POTENTIAL). FT DOMAIN 84 98 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 99 119 2 (POTENTIAL). FT DOMAIN 120 152 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 153 173 3 (POTENTIAL). FT DOMAIN 174 206 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 207 227 4 (POTENTIAL). FT DOMAIN 228 290 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 291 311 5 (POTENTIAL). FT DOMAIN 312 316 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 317 337 6 (POTENTIAL). FT DOMAIN 338 393 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 394 414 7 (POTENTIAL). FT DOMAIN 415 417 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 417 AA; 48730 MW; 2112BE9E1E356059 CRC64; MTELRSERKN GNWDRLFGPF FESWAVFKAP QAKSRHIIAY WTRDQLKALG FYMNSEQRRL PRIVAWQYFV SIQLATALAS LFYGISESIG DIVNLGRDLV FIITIIFICF RLVFFAQYAG ELDVIIDALE DIYHWSIKGP ATKEVQETKR LHFLLFMALI ITWFSFLILF MLIKISTPFW IESQTLPFHV SWPFQLHDPS KHPIAYIIIF VSQSTTMLYF LIWLGVVENM GVSLFFELTS ALRVLCIELR NLQELCLGDE DMLYRELCRM TKFHQQIILL TDRCNHIFNG AFIMQMLINF LLVSLSLFEV LAAKKNPQVA VEYMIIMLMT LGHLSFWSKF GDMFSKESEQ VALAVYEAYD PNVGSKSIHR QFCFFIQRAQ KPLIMKASPF PPFNLENYMF ILKQCYSILT ILANTLE // ID O65B_DROME STANDARD; PRT; 385 AA. AC P82983; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 65b. GN OR65B. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003563; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041624; Or65b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 34 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 35 55 1 (POTENTIAL). FT DOMAIN 56 67 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 68 88 2 (POTENTIAL). FT DOMAIN 89 123 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 124 144 3 (POTENTIAL). FT DOMAIN 145 197 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 198 218 4 (POTENTIAL). FT DOMAIN 219 254 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 255 275 5 (POTENTIAL). FT DOMAIN 276 286 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 287 307 6 (POTENTIAL). FT DOMAIN 308 360 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 361 381 7 (POTENTIAL). FT DOMAIN 382 385 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 385 AA; 44793 MW; BA7C49282F9AFE7C CRC64; MEASHSSIYY WREQMKAMAL FTTTEERLLP YRSKWHTLVY IQMVIFFASM SFGLTESMGD HVQMGRDLAF ILGAFFIIFK TYYFCWYGDE LDQVISDLDA LHPWAQKGPN PVEYQTGKRW YFVMAFFLAT SWSFFLCILL LLLITSPMWV HQQNLPFHAA FPFQWHEKSL HPISHAIIYL FQSYFAVYCL TWLLCIEGLS ICIYAEITFG IEVLCLELRQ IHRHNYGLQE LRMETNRLVK LHQKIVEILD RTNDVFHGTL IMQMGVNFSL VSLSVLEAVE ARKDPKVVAQ FAVLMLLALG HLSMWSYCGD QLSQKSLQIS EAAYEAYDPT KGSKDVYRDL CVIIRRGQDP LIMRASPFPS FNLINYSAIL NQCYGILTFL LKTLD // ID O65C_DROME STANDARD; PRT; 385 AA. AC P82984; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 65c. GN OR65C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003563; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041623; Or65c. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 34 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 35 55 1 (POTENTIAL). FT DOMAIN 56 67 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 68 88 2 (POTENTIAL). FT DOMAIN 89 123 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 124 144 3 (POTENTIAL). FT DOMAIN 145 197 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 198 218 4 (POTENTIAL). FT DOMAIN 219 254 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 255 275 5 (POTENTIAL). FT DOMAIN 276 287 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 288 308 6 (POTENTIAL). FT DOMAIN 309 360 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 361 381 7 (POTENTIAL). FT DOMAIN 382 385 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 385 AA; 45119 MW; 01C71C023D4D9431 CRC64; MESSYSAVYY WREQMKAMFL YTTSKERQMP YRSSWHTLVI IQATVCFLTM CYGVTESLGD KVQMGRDIAF IIGFFYIAFK IYYFQWYGDE LDEVVEALET FHPWAQKGPG AVDYRTAKRW YFTLAFFLAS SWLVFLCIFI LLLITSPLWV HQQILPLHAA FPFQWHEKSI HPISHAFIYL FQTWNVMYFL TWLVCIEGLS VSIYVEITFA IEVLCLELRH LHQRCHGYEQ LRLETNRLVQ FHQKIVHILD HTNKVFHGTL IMQMGVNFFL VSLSVLEAME ARKDPKVVAQ FAVLMLLALG HLSMWSYFGD LLSQKSLTIS EAAYEAYDPI KGSKDVYRDL CLIIRRGQEP LIMRASPFPS FNFINYSAIL NQCYGILTFL LKTLD // ID O67A_DROME STANDARD; PRT; 407 AA. AC Q9VT08; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 67a. GN OR67A OR CG12526. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003551; AAF50248.2; -. DR FlyBase; FBgn0036009; Or67a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 40 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 41 61 1 (POTENTIAL). FT DOMAIN 62 79 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 80 100 2 (POTENTIAL). FT DOMAIN 101 144 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 145 165 3 (POTENTIAL). FT DOMAIN 166 208 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 209 229 4 (POTENTIAL). FT DOMAIN 230 278 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 279 300 5 (POTENTIAL). FT DOMAIN 301 314 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 315 331 6 (POTENTIAL). FT DOMAIN 332 378 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 379 401 7 (POTENTIAL). FT DOMAIN 402 407 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 407 AA; 47045 MW; 8B5E96FF32FF1226 CRC64; MDNVAEMPEE KYVEVDDFLR LAVKFYNTLG IDPYETGRKR TIWFQIYFAL NMFNMVFSFY AEVATLVDRL RDNENFLESC ILLSYVSFVV MGLSKIGAVM KKKPKMTALV RQLETCFPSP SAKVQEEYAV KSWLKRCHIY TKGFGGLFMI MYFAHALIPL FIYFIQRVLL HYPDAKQIMP FYQLEPWEFR DSWLFYPSYF HQSSAGYTAT CGSIAGDLMI FAVVLQVIMH YERLAKVLRE FKIQAHNAPN GAKEDIRKLQ SLVANHIDIL RLTDLMNEVF GIPLLLNFIA SALLVCLVGV QLTIALSPEY FCKQMLFLIS VLLEVYLLCS FSQRLIDASE NVGHAAYDMD WLGSDKRFKK ILIFISMRSQ KPVCLKATVV LDLSMPTMSI FLGMSYKFFC AVRTMYQ // ID O67B_DROME STANDARD; PRT; 421 AA. AC Q9VT20; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 67b. GN OR67B OR CG14176. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003551; AAF50236.2; -. DR FlyBase; FBgn0036019; Or67b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 48 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 49 69 1 (POTENTIAL). FT DOMAIN 70 71 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 72 92 2 (POTENTIAL). FT DOMAIN 93 151 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 152 172 3 (POTENTIAL). FT DOMAIN 173 217 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 218 238 4 (POTENTIAL). FT DOMAIN 239 289 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 290 310 5 (POTENTIAL). FT DOMAIN 311 315 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 316 336 6 (POTENTIAL). FT DOMAIN 337 384 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 385 405 7 (POTENTIAL). FT DOMAIN 406 421 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 254 254 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 342 342 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 361 361 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 366 366 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 421 AA; 49515 MW; A75FDD307F35F6C6 CRC64; MQDQLDHELE RIDKLPKLGL LWVEYSAYAL GVNIAPRKRS SKYCRLTRIL VLIVNLSIIY SLVAFIMENY MISFETYVEA VLLTFQLSVG VVKMFHFQNK VESCSQLVFS TETGEVLKSL GLFQLDLPRK KELLSSVSLI LLNNWMIIDR QVMFFFKIVC MPVLYYCVRP YFQYIFDCYI KDKDTCEMTL TYPAIVPYLQ LGNYEFPSYV IRFFLLQSGP LWCFFAVFGF NSLFVVLTRY ESGLIKVLRF LVQNSTSDIL VPKDQRVKYL QCCVRLFARI SSHHNQIENL FKYIILVQCS VSSILICMLL YKISTVLEVG WVWMGMIMVY FVTIALEITL YNVSAQKVES QSELLFHDWY NCSWYNESRE FKFMIKMMLL FSRRTFVLSV GGFTSLSHKF LVQVFRLSAN FFLLLRNMNN K // ID O67C_DROME STANDARD; PRT; 404 AA. AC Q9VT90; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 67c. GN OR67C OR CG14156. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003549; AAF50163.2; -. DR FlyBase; FBgn0036078; Or67c. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 45 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 46 66 1 (POTENTIAL). FT DOMAIN 67 79 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 80 100 2 (POTENTIAL). FT DOMAIN 101 139 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 140 160 3 (POTENTIAL). FT DOMAIN 161 204 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 205 225 4 (POTENTIAL). FT DOMAIN 226 277 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 278 298 5 (POTENTIAL). FT DOMAIN 299 304 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 305 326 6 (POTENTIAL). FT DOMAIN 327 373 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 374 394 7 (POTENTIAL). FT DOMAIN 395 404 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 404 AA; 46951 MW; C48BD28C4A03EAC8 CRC64; METAKDNTAR TFMELMRVPV QFYRTIGEDI YAHRSTNPLK SLLFKIYLYA GFINFNLLVI GELVFFYNSI QDFETIRLAI AVAPCIGFSL VADFKQAAMI RGKKTLIMLL DDLENMHPKT LAKQMEYKLP DFEKTMKRVI NIFTFLCLAY TTTFSFYPAI KASVKFNFLG YDTFDRNFGF LIWFPFDATR NNLIYWIMYW DIAHGAYLAG IAFLCADLLL VVVITQICMH FNYISMRLED HPCNSNEDKE NIEFLIGIIR YHDKCLKLCE HVNDLYSFSL LLNFLMASMQ ICFIAFQVTE STVEVIIIYC IFLMTSMVQV FMVCYYGDTL IAASLKVGDA AYNQKWFQCS KSYCTMLKLL IMRSQKPASI RPPTFPPISL VTYMKVISMS YQFFALLRTT YSNN // ID O69A_DROME STANDARD; PRT; 393 AA. AC P82985; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 69a. GN OR69A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003539; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041622; Or69a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 60 1 (POTENTIAL). FT DOMAIN 61 69 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 70 90 2 (POTENTIAL). FT DOMAIN 91 138 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 139 159 3 (POTENTIAL). FT DOMAIN 160 208 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 209 229 4 (POTENTIAL). FT DOMAIN 230 269 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 270 290 5 (POTENTIAL). FT DOMAIN 291 305 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 306 326 6 (POTENTIAL). FT DOMAIN 327 365 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 366 386 7 (POTENTIAL). FT DOMAIN 387 393 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 265 265 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 269 269 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 393 AA; 46096 MW; EC1EFBB19115362C CRC64; MQLEDFMRYP DLVCQAAQLP RYTWNGRRSL EVKRNLAKRI IFWLGAVNLV YHNIGCVMYG YFGDGRTKDP IAYLAELASV ASMLGFTIVG TLNLWKMLSL KTHFENLLNE FEELFQLIKH RAYRIHHYQE KYTRHIRNTF IFHTSAVVYY NSLPILLMIR EHFSNSQQLG YRIQSNTWYP WQVQGSIPGF FAAVACQIFS CQTNMCVNMF IQFLINFFGI QLEIHFDGLA RQLETIDARN PHAKDQLKYL IVYHTKLLNL ADRVNRSFNF TFLISLSVSM ISNCFLAFSM TMFDFGTSLK HLLGLLLFIT YNFSMCRSGT HLILTSGKVL PAAFYNNWYE GDLVYRRMLL ILMMRATKPY MWKTYKLAPV SITTYMATLK FSYQMFTCVR SLK // ID O69B_DROME STANDARD; PRT; 393 AA. AC Q9VU27; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 69b. GN OR69B OR CG17902. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003539; AAF49864.1; -. DR FlyBase; FBgn0036326; Or69b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 24 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 25 45 1 (POTENTIAL). FT DOMAIN 46 61 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 62 82 2 (POTENTIAL). FT DOMAIN 83 124 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 125 145 3 (POTENTIAL). FT DOMAIN 146 174 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 175 195 4 (POTENTIAL). FT DOMAIN 196 254 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 255 275 5 (POTENTIAL). FT DOMAIN 276 290 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 291 311 6 (POTENTIAL). FT DOMAIN 312 333 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 334 350 7 (POTENTIAL). FT DOMAIN 351 393 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 393 AA; 45547 MW; 7522661FBD43F8A7 CRC64; MACIPRYQWK GRPTERQFYA SEQRIVFLLG TICQIFQITG VLIYWYCNGR LATETGTFVA QLSEMCSSFC LTFVGFCNVY AISTNRNQIE TLLEELHQIY PRYRKNHYRC QHYFDMAMTI MRIEFLFYMI LYVYYNSAPL WVLLWEHLHE EYDLSFKTQT NTWFPWKVHG SALGFGMAVL SITVGSFVGV GFSIVTQNLI CLLTFQLKLH YDGISSQLVS LDCRRPGAHK ELSILIAHHS RILQLGDQVN DIMNFVFGSS LVGATIAICM SSVSIMLLDL ASAFKYASGL VAFVLYNFVI CYMGTEVTLA VKIGSYMDGR RWIPKDSLLR SQRLQVLVAV GFFNICVLSN RRPKIEILLR YYYHIMFYSF KLYFSLRKGS LWKILSSFTL LRI // ID O71A_DROME STANDARD; PRT; 379 AA. AC Q9VUK5; Q8IQM2; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 71a. GN OR71A OR CG17871. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=Q9VUK5-3; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=B; CC IsoId=Q9VUK5-2; Sequence=VSP_008035; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q9VUK5-1; Sequence=VSP_008032, VSP_008033, VSP_008034; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003532; AAF49671.2; -. DR EMBL; AE003532; AAN11784.1; -. DR EMBL; AE003532; AAN11785.1; -. DR FlyBase; FBgn0036474; Or71a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family; Alternative splicing. FT DOMAIN 1 37 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 38 58 1 (POTENTIAL). FT DOMAIN 59 66 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 67 87 2 (POTENTIAL). FT DOMAIN 88 127 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 128 148 3 (POTENTIAL). FT DOMAIN 149 166 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 167 187 4 (POTENTIAL). FT DOMAIN 188 255 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 256 276 5 (POTENTIAL). FT DOMAIN 277 280 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 281 301 6 (POTENTIAL). FT DOMAIN 302 343 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 344 364 7 (POTENTIAL). FT DOMAIN 365 379 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 188 188 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 115 Missing (in isoform C). FT /FTId=VSP_008032. FT VARSPLIC 273 276 SPVL -> VRVT (in isoform C). FT /FTId=VSP_008033. FT VARSPLIC 277 379 Missing (in isoform C). FT /FTId=VSP_008034. FT VARSPLIC 362 379 VVFSTLENPCISYLYFRP -> TMNQAYSLLALLLNMNQ FT (in isoform B). FT /FTId=VSP_008035. SQ SEQUENCE 379 AA; 44804 MW; BA8C03FECAE3E5A7 CRC64; MDYDRIRPVR FLTGVLKWWR LWPRKESVST PDWTNWQAYA LHVPFTFLFV LLLWLEAIKS RDIQHTADVL LICLTTTALG GKVINIWKYA HVAQGILSEW STWDLFELRS KQEVDMWRFE HRRFNRVFMF YCLCSAGVIP FIVIQPLFDI PNRLPFWMWT PFDWQQPVLF WYAFIYQATT IPIACACNVT MDAVNWYLML HLSLCLRMLG QRLSKLQHDD KDLREKFLEL IHLHQRLKQQ ALSIEIFISK STFTQILVSS LIICFTIYSM QMSPVLQDLP GFAAMMQYLV AMIMQVMLPT IYGNAVIDSA NMLTDSMYNS DWPDMNCRMR RLVLMFMVYL NRPVTLKAGG FFHIGLPLFT KVVFSTLENP CISYLYFRP // ID O74A_DROME STANDARD; PRT; 404 AA. AC Q9VVF3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 74a. GN OR74A OR CG13726. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003524; AAF49358.1; -. DR FlyBase; FBgn0036709; Or74a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 38 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 39 59 1 (POTENTIAL). FT DOMAIN 60 67 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 68 88 2 (POTENTIAL). FT DOMAIN 89 141 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 142 162 3 (POTENTIAL). FT DOMAIN 163 181 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 182 202 4 (POTENTIAL). FT DOMAIN 203 274 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 275 295 5 (POTENTIAL). FT DOMAIN 296 303 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 304 324 6 (POTENTIAL). FT DOMAIN 325 380 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 381 401 7 (POTENTIAL). FT DOMAIN 402 404 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 141 141 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 249 249 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 404 AA; 47415 MW; C61127EB0D422206 CRC64; MSFHRYRPRL PGGELAPMPW PVSLYRVLNH VAWPLEAESG RWTVFLDRLM IFLGFLVFCE HNEVDFHYLI ANRQDMDNML TGLPTYLILV EMQIRCFQLA WHKDRFRALL QRFYAEIYVS EEMEPHLFAS IQRQMLATRV NSTVYLLALL NFFLVPVTNV IYHRREMLYK QVYPFDNTQL HFFIPLLVLN FWVGFIITSM LFGELNVMGE LMMHLNARYI QLGQDLRRSA QMLLKKSSSL NVAIAYRLNL THILRRNAAL RDFGQRVEKE FTLRIFVMFA FSAGLLCALF FKAFTNPWGN VAYIVWFLAK FMELLALGML GSILLKTTDE LGMMYYTADW EQVIHQSDNV GENVKLMKLV TLAIQLNSRP FFITGLNYFR VSLTAVLKII QGAFSYFTFL NSMR // ID O82A_DROME STANDARD; PRT; 385 AA. AC P82986; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 82a. GN OR82A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003607; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0041621; Or82a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 32 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 33 53 1 (POTENTIAL). FT DOMAIN 54 62 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 63 83 2 (POTENTIAL). FT DOMAIN 84 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 152 3 (POTENTIAL). FT DOMAIN 153 186 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 187 207 4 (POTENTIAL). FT DOMAIN 208 257 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 258 278 5 (POTENTIAL). FT DOMAIN 279 290 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 291 311 6 (POTENTIAL). FT DOMAIN 312 357 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 358 378 7 (POTENTIAL). FT DOMAIN 379 385 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 385 AA; 43635 MW; 5E8F81219BD3F56D CRC64; MGRLFQLQEY CLRAMGHKDD MDSTDSTALS LKHISSLIFV ISAQYPLISY VAYNRNDMEK VTACLSVVFT NMLTVIKIST FLANRKDFWE MIHRFRKMHE QSASHIPRYR EGLDYVAEAN KLASFLGRAY CVSCGLTGLY FMLGPIVKIG VCRWHGTTCD KELPMPMKFP FNDLESPGYE VCFLYTVLVT VVVVAYASAV DGLFISFAIN LRAHFQTLQR QIENWEFPSS EPDTQIRLKS IVEYHVLLLS LSRKLRSIYT PTVMGQFVIT SLQVGVIIYQ LVTNMDSVMD LLLYASFFGS IMLQLFIYCY GGEIIKAESL QVDTAVRLSN WHLASPKTRT SLSLIILQSQ KEVLIRAGFF VASLANFVGI CRTALSLITL IKSIE // ID O83A_DROME STANDARD; PRT; 453 AA. AC Q9VNB3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 83a. GN OR83A OR CG10612. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003603; AAF52033.2; -. DR FlyBase; FBgn0037322; Or83a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 28 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 29 49 1 (POTENTIAL). FT DOMAIN 50 85 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 86 106 2 (POTENTIAL). FT DOMAIN 107 148 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 149 169 3 (POTENTIAL). FT DOMAIN 170 203 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 204 224 4 (POTENTIAL). FT DOMAIN 225 322 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 323 343 5 (POTENTIAL). FT DOMAIN 344 359 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 360 380 6 (POTENTIAL). FT DOMAIN 381 408 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 409 429 7 (POTENTIAL). FT DOMAIN 430 453 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 249 249 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 453 AA; 52272 MW; 4B660B3380901192 CRC64; MKSTFKEERI KDDSKRRDLF VFVRQTMCIA AMYPFGYYVN GSGVLAVLVR FCDLTYELFN YFVSVHIAGL YICTIYINYG QGDLDFFVNC LIQTIIYLWT IAMKLYFRRF RPGLLNTILS NINDEYETRS AVGFSFVTMA GSYRMSKLWI KTYVYCCYIG TIFWLALPIA YRDRSLPLAC WYPFDYTQPG VYEVVFLLQA MGQIQVAASF ASSSGLHMVL CVLISGQYDV LFCSLKNVLA SSYVLMGANM TELNQLQAEQ SAADVEPGQY AYSVEEETPL QELLKVGSSM DFSSAFRLSF VRCIQHHRYI VAALKKIESF YSPIWFVKIG EVTFLMCLVA FVSTKSTAAN SFMRMVSLGQ YLLLVLYELF IICYFADIVF QNSQRCGEAL WRSPWQRHLK DVRSDYMFFM LNSRRQFQLT AGKISNLNVD RFRGTITTAF SFLTLLQKMD ARE // ID O83B_DROME STANDARD; PRT; 486 AA. AC Q9VNB5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 83b. GN OR83B OR CG10609. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003603; AAF52031.2; -. DR FlyBase; FBgn0037324; Or83b. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 47 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 48 68 1 (POTENTIAL). FT DOMAIN 69 75 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 76 96 2 (POTENTIAL). FT DOMAIN 97 135 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 136 156 3 (POTENTIAL). FT DOMAIN 157 191 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 192 212 4 (POTENTIAL). FT DOMAIN 213 351 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 352 372 5 (POTENTIAL). FT DOMAIN 373 390 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 391 411 6 (POTENTIAL). FT DOMAIN 412 462 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 463 483 7 (POTENTIAL). FT DOMAIN 484 486 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 33 33 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 486 AA; 54413 MW; 8DD0ACDC3091B5D6 CRC64; MTTSMQPSKY TGLVADLMPN IRAMKYSGLF MHNFTGGSAF MKKVYSSVHL VFLLMQFTFI LVNMALNAEE VNELSGNTIT TLFFTHCITK FIYLAVNQKN FYRTLNIWNQ VNTHPLFAES DARYHSIALA KMRKLFFLVM LTTVASATAW TTITFFGDSV KMVVDHETNS SIPVEIPRLP IKSFYPWNAS HGMFYMISFA FQIYYVLFSM IHSNLCDVMF CSWLIFACEQ LQHLKGIMKP LMELSASLDT YRPNSAALFR SLSANSKSEL IHNEEKDPGT DMDMSGIYSS KADWGAQFRA PSTLQSFGGN GGGGNGLVNG ANPNGLTKKQ EMMVRSAIKY WVERHKHVVR LVAAIGDTYG AALLLHMLTS TIKLTLLAYQ ATKINGVNVY AFTVVGYLGY ALAQVFHFCI FGNRLIEESS SVMEAAYSCH WYDGSEEAKT FVQIVCQQCQ KAMSISGAKF FTVSLDLFAS VLGAVVTYFM VLVQLK // ID O83C_DROME STANDARD; PRT; 397 AA. AC Q9VNK9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 83c. GN OR83C OR CG15581. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003600; AAF51921.2; -. DR FlyBase; FBgn0037399; Or83c. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 60 1 (POTENTIAL). FT DOMAIN 61 70 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 71 90 2 (POTENTIAL). FT DOMAIN 91 136 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 137 157 3 (POTENTIAL). FT DOMAIN 158 186 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 187 207 4 (POTENTIAL). FT DOMAIN 208 282 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 283 299 5 (POTENTIAL). FT DOMAIN 300 305 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 306 326 6 (POTENTIAL). FT DOMAIN 327 365 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 366 386 7 (POTENTIAL). FT DOMAIN 387 397 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 339 339 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 397 AA; 45487 MW; 59CA3EF415BB711A CRC64; MSTSESPSSR FRELSKYINS LTNLLGVDFL SPKLKFNYRT WTTIFAIANY TGFTVFTILN NGGDWRVGLK ASLMTGGLFH GLGKFLTCLL KHQDMRRLVL YSQSIYDEYE TRGDSYHRTL NSNIDRLLGI MKIIRNGYVF AFCLMELLPL AMLMYDGTRV TAMQYLIPGL PLENNYCYVV TYMIQTVTML VQGVGFYSGD LFVFLGLTQI LTFADMLQVK VKELNDALEQ KAEYRALVRV GASIDGAENR QRLLLDVIRW HQLFTDYCRA INALYYELIA TQVLSMALAM MLSFCINLSS FHMPSAIFFV VSAYSMSIYC ILGTILEFAY DQVYESICNV TWYELSGEQR KLFGFLLRES QYPHNIQILG VMSLSVRTAL QIVKLIYSVS MMMMNRA // ID O85A_DROME STANDARD; PRT; 397 AA. AC Q9VHS4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 85a. GN OR85A OR CG7454. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003678; AAF54225.1; -. DR FlyBase; FBgn0037576; Or85a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 46 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 47 67 1 (POTENTIAL). FT DOMAIN 68 83 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 84 104 2 (POTENTIAL). FT DOMAIN 105 142 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 143 163 3 (POTENTIAL). FT DOMAIN 164 192 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 193 213 4 (POTENTIAL). FT DOMAIN 214 262 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 263 283 5 (POTENTIAL). FT DOMAIN 284 294 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 295 315 6 (POTENTIAL). FT DOMAIN 316 347 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 348 368 7 (POTENTIAL). FT DOMAIN 369 397 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 25 25 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 397 AA; 45820 MW; 4ED07645226497C2 CRC64; MIFKYIQEPV LGSLFRSRDS LIYLNRSIDQ MGWRLPPRTK PYWWLYYIWT LVVIVLVFIF IPYGLIMTGI KEFKNFTTTD LFTYVQVPVN TNASIMKGII VLFMRRRFSR AQKMMDAMDI RCTKMEEKVQ VHRAAALCNR VVVIYHCIYF GYLSMALTGA LVIGKTPFCL YNPLVNPDDH FYLATAIESV TMAGIILANL ILDVYPIIYV VVLRIHMELL SERIKTLRTD VEKGDDQHYA ELVECVKDHK LIVEYGNTLR PMISATMFIQ LLSVGLLLGL AAVSMQFYNT VMERVVSGVY TIAILSQTFP FCYVCEQLSS DCESLTNTLF HSKWIGAERR YRTTMLYFIH NVQQSILFTA GGIFPICLNT NIKMAKFAFS VVTIVNEMDL AEKLRRE // ID O85B_DROME STANDARD; PRT; 390 AA. AC Q9VHQ7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 85b. GN OR85B OR CG11735. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003679; AAF54244.2; -. DR FlyBase; FBgn0037590; Or85b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 30 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 31 51 1 (POTENTIAL). FT DOMAIN 52 66 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 67 87 2 (POTENTIAL). FT DOMAIN 88 126 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 127 147 3 (POTENTIAL). FT DOMAIN 148 200 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 201 221 4 (POTENTIAL). FT DOMAIN 222 260 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 261 281 5 (POTENTIAL). FT DOMAIN 282 291 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 292 312 6 (POTENTIAL). FT DOMAIN 313 360 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 361 381 7 (POTENTIAL). FT DOMAIN 382 390 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 390 AA; 45664 MW; A0E338F8838AC3F3 CRC64; MEKLMKYASF FYTAVGIRPY TNGEESKMNK LIFHIVFWSN VINLSFVGLF ESIYVYSAFM DNKFLEAVTA LSYIGFVTVG MSKMFFIRWK KTAITELINE LKEIYPNGLI REERYNLPMY LGTCSRISLI YSLLYSVLIW TFNLFCVMEY WVYDKWLNIR VVGKQLPYLM YIPWKWQDNW SYYPLLFSQN FAGYTSAAGQ ISTDVLLCAV ATQLVMHFDF LSNSMERHEL SGDWKKDSRF LVDIVRYHER ILRLSDAVND IFGIPLLLNF MVSSFVICFV GFQMTVGVPP DIVVKLFLFL VSSMSQVYLI CHYGQLVADA SYGFSVATYN QKWYKADVRY KRALVIIIAR SQKVTFLKAT IFLDITRSTM TDLLQISYKF FALLRTMYTQ // ID O85C_DROME STANDARD; PRT; 389 AA. AC Q9VHQ6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 85c. GN OR85C OR CG17911. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003679; AAF54245.2; -. DR FlyBase; FBgn0037591; Or85c. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 33 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 34 54 1 (POTENTIAL). FT DOMAIN 55 66 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 67 87 2 (POTENTIAL). FT DOMAIN 88 130 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 131 151 3 (POTENTIAL). FT DOMAIN 152 199 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 200 220 4 (POTENTIAL). FT DOMAIN 221 259 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 260 280 5 (POTENTIAL). FT DOMAIN 281 290 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 291 311 6 (POTENTIAL). FT DOMAIN 312 359 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 360 380 7 (POTENTIAL). FT DOMAIN 381 389 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 389 AA; 45605 MW; 6EB362BCA17264EA CRC64; MKFMKYAVFF YTSVGIEPYT IDSRSKKASL WSHLLFWANV INLSVIVFGE ILYLGVAYSD GKFIDAVTVL SYIGFVIVGM SKMFFIWWKK TDLSDLVKEL EHIYPNGKAE EEMYRLDRYL RSCSRISITY ALLYSVLIWT FNLFSIMQFL VYEKLLKIRV VGQTLPYLMY FPWNWHENWT YYVLLFCQNF AGHTSASGQI STDLLLCAVA TQVVMHFDYL ARVVEKQVLD RDWSENSRFL AKTVQYHQRI LRLMDVLNDI FGIPLLLNFM VSTFVICFVG FQMTVGVPPD IMIKLFLFLF SSLSQVYLIC HYGQLIADAS SSLSISAYKQ NWQNADIRYR RALVFFIARP QRTTYLKATI FMNITRATMT DLLQVSYKFF ALLRTMYIK // ID O85D_DROME STANDARD; PRT; 412 AA. AC Q9VHQ2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 85d. GN OR85D OR CG11742. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003679; AAF54249.1; -. DR FlyBase; FBgn0037594; Or85d. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 56 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 57 77 1 (POTENTIAL). FT DOMAIN 78 84 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 85 105 2 (POTENTIAL). FT DOMAIN 106 152 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 153 173 3 (POTENTIAL). FT DOMAIN 174 219 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 220 240 4 (POTENTIAL). FT DOMAIN 241 282 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 283 303 5 (POTENTIAL). FT DOMAIN 304 314 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 315 335 6 (POTENTIAL). FT DOMAIN 336 382 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 383 403 7 (POTENTIAL). FT DOMAIN 404 412 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 412 AA; 47987 MW; 0E4E8EA5FC14A9EC CRC64; MLTKKDTQSA KEQEKLKAIP LHSFLKYANV FYLSIGMMAY DHKYSQKWKE VLLHWTFIAQ MVNLNTVLIS ELIYVFLAIG KGSNFLEATM NLSFIGFVIV GDFKIWNISR QRKRLTQVVS RLEELHPQGL AQQEPYNIGH HLSGYSRYSK FYFGMHMVLI WTYNLYWAVY YLVCDFWLGM RQFERMLPYY CWVPWDWSTG YSYYFMYISQ NIGGQACLSG QLAADMLMCA LVTLVVMHFI RLSAHIESHV AGIGSFQHDL EFLQATVAYH QSLIHLCQDI NEIFGVSLLS NFVSSSFIIC FVGFQMTIGS KIDNLVMLVL FLFCAMVQVF MIATHAQRLV DASEQIGQAV YNHDWFRADL RYRKMLILII KRAQQPSRLK ATMFLNISLV TVSDLLQLSY KFFALLRTMY VN // ID O85E_DROME STANDARD; PRT; 417 AA. AC P81924; Q9VHP5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 85e. GN OR85E OR OR104 OR DOR104 OR CG9700. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Maxillary palps; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN 15% OF THE 120 SENSORY NEURONS CC WITHIN THE MAXILLARY PALP. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF127922; AAD26357.1; -. DR EMBL; AE003679; AAF54256.1; -. DR FlyBase; FBgn0026399; Or85e. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; Glycoprotein; KW Multigene family. FT DOMAIN 1 60 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 61 81 1 (POTENTIAL). FT DOMAIN 82 98 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 99 119 2 (POTENTIAL). FT DOMAIN 120 159 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 160 180 3 (POTENTIAL). FT DOMAIN 181 212 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 213 233 4 (POTENTIAL). FT DOMAIN 234 286 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 287 307 5 (POTENTIAL). FT DOMAIN 308 334 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 335 355 6 (POTENTIAL). FT DOMAIN 356 367 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 368 388 7 (POTENTIAL). FT DOMAIN 389 417 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 39 39 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 157 157 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 410 417 NVVCSTPK -> FIRQDILIFLVNSRRAVHVTAGKFYVMDV FT NRLRSVITQAFSFLTLLQKLAAKKTESEL (IN REF. FT 1). SQ SEQUENCE 417 AA; 47212 MW; A27C0A9A76040C70 CRC64; MASLQFHGNV DADIRYDISL DPARESNLFR LLMGLQLANG TKPSPRLPKW WPKRLEMIGK VLPKAYCSMV IFTSLHLGVL FTKTTLDVLP TGELQAITDA LTMTIIYFFT GYGTIYWCLR SRRLLAYMEH MNREYRHHSL AGVTFVSSHA AFRMSRNFTV VWIMSCLLGV ISWGVSPLML GIRMLPLQCW YPFDALGPGT YTAVYATQLF GQIMVGMTFG FGGSLFVTLS LLLLGQFDVL YCSLKNLDAH TKLLGGESVN GLSSLQEELL LGDSKRELNQ YVLLQEHPTD LLRLSAGRKC PDQGNAFHNA LVECIRLHRF ILHCSQELEN LFSPYCLVKS LQITFQLCLL VFVGVSGTRE VLRIVNQLQY LGLTIFELLM FTYCGELLSR HSIRSGDAFW RGAWWKHAHN VVCSTPK // ID O85F_DROME STANDARD; PRT; 392 AA. AC Q9VHE6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 85f. GN OR85F OR CG16755. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003682; AAF54368.1; -. DR FlyBase; FBgn0037685; Or85f. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 36 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 37 57 1 (POTENTIAL). FT DOMAIN 58 69 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 70 90 2 (POTENTIAL). FT DOMAIN 91 130 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 131 151 3 (POTENTIAL). FT DOMAIN 152 179 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 180 200 4 (POTENTIAL). FT DOMAIN 201 268 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 269 289 5 (POTENTIAL). FT DOMAIN 290 295 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 296 316 6 (POTENTIAL). FT DOMAIN 317 363 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 364 384 7 (POTENTIAL). FT DOMAIN 385 392 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 392 AA; 45343 MW; 393C7E2811D3E404 CRC64; MEPVQYSYED FARLPTTVFW IMGYDMLGVP KTRSRRILYW IYRFLCLASH GVCVGVMVFR MVEAKTIDNV SLIMRYATLV TYIINSDTKF ATVLQRSAIQ SLNSKLAELY PKTTLDRIYH RVNDHYWTKS FVYLVIIYIG SSIMVVIGPI ITSIIAYFTH NVFTYMHCYP YFLYDPEKDP VWIYISIYAL EWLHSTQMVI SNIGADIWLL YFQVQINLHF RGIIRSLADH KPSVKHDQED RKFIAKIVDK QVHLVSLQND LNGIFGKSLL LSLLTTAAVI CTVAVYTLIQ GPTLEGFTYV IFIGTSVMQV YLVCYYGQQV LDLSGEVAHA VYNHDFHDAS IAYKRYLLII IIRAQQPVEL NAMGYLSISL DTFKQLMSVS YRVITMLMQM IQ // ID O88A_DROME STANDARD; PRT; 401 AA. AC Q9VFN2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 88a. GN OR88A OR CG14360. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003703; AAF55018.2; -. DR FlyBase; FBgn0038203; Or88a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 26 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 27 47 1 (POTENTIAL). FT DOMAIN 48 52 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 53 73 2 (POTENTIAL). FT DOMAIN 74 142 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 143 163 3 (POTENTIAL). FT DOMAIN 164 191 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 192 212 4 (POTENTIAL). FT DOMAIN 213 277 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 278 298 5 (POTENTIAL). FT DOMAIN 299 303 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 304 324 6 (POTENTIAL). FT DOMAIN 325 370 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 371 391 7 (POTENTIAL). FT DOMAIN 392 401 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 401 AA; 47088 MW; 8E55679940963623 CRC64; MKPTEIKKPY RMEEFLRPQM FQEVAQMVHF QWRRNPVDNS MVNASMVPFC LSAFLNVLFF GCNGWDIIGH FWLGHPANQN PPVLSITIYF SIRGLMLYLK RKEIVEFVND LDRECPRDLV SQLDMQMDET YRNFWQRYRF IRIYSHLGGP MFCVVPLALF LLTHEGKDTP VAQHEQLLGG WLPCGVRKDP NFYLLVWSFD LMCTTCGVSF FVTFDNLFNV MQGHLVMHLG HLARQFSAID PRQSLTDEKR FFVDLRLLVQ RQQLLNGLCR KYNDIFKVAF LVSNFVGAGS LCFYLFMLSE TSDVLIIAQY ILPTLVLVGF TFEICLRGTQ LEKASEGLES SLRSQEWYLG SRRYRKFYLL WTQYCQRTQQ LGAFGLIQVN MVHFTEIMQL AYRLFTFLKS H // ID O92A_DROME STANDARD; PRT; 408 AA. AC Q9VDM1; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 92a. GN OR92A OR CG17916. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003730; AAF55769.2; -. DR FlyBase; FBgn0038798; Or92a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 52 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 53 73 1 (POTENTIAL). FT DOMAIN 74 74 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 75 95 2 (POTENTIAL). FT DOMAIN 96 144 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 145 165 3 (POTENTIAL). FT DOMAIN 166 209 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 210 230 4 (POTENTIAL). FT DOMAIN 231 276 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 277 301 5 (POTENTIAL). FT DOMAIN 302 310 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 311 331 6 (POTENTIAL). FT DOMAIN 332 378 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 379 399 7 (POTENTIAL). FT DOMAIN 400 408 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 408 AA; 47552 MW; 9F30D9C61CD4EC38 CRC64; MLFRKRKPKS DDEVITFDEL TRFPMTFYKT IGEDLYSDRD PNVIRRYLLR FYLVLGFLNF NAYVVGEIAY FIVHIMSTTT LLEATAVAPC IGFSFMADFK QFGLTVNRKR LVRLLDDLKE IFPLDLEAQR KYNVSFYRKH MNRVMTLFTI LCMTYTSSFS FYPAIKSTIK YYLMGSEIFE RNYGFHILFP YDAETDLTVY WFSYWGLAHC AYVAGVSYVC VDLLLIATIT QLTMHFNFIA NDLEAYEGGD HTDEENIKYL HNLVVYHARA LDLSEEVNNI FSFLILWNFI AASLVICFAG FQITASNVED IVLYFIFFSA SLVQVFVVCY YGDEMISSSS RIGHSAFNQN WLPCSTKYKR ILQFIIARSQ KPASIRPPTF PPISFNTFMK VISMSYQFFA LLRTTYYG // ID O94A_DROME STANDARD; PRT; 387 AA. AC Q9VCS9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 94a. GN OR94A OR CG17241. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003741; AAF56076.1; -. DR FlyBase; FBgn0039033; Or94a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 45 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 46 66 1 (POTENTIAL). FT DOMAIN 67 75 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 76 96 2 (POTENTIAL). FT DOMAIN 97 133 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 134 154 3 (POTENTIAL). FT DOMAIN 155 191 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 192 212 4 (POTENTIAL). FT DOMAIN 213 255 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 256 276 5 (POTENTIAL). FT DOMAIN 277 290 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 291 311 6 (POTENTIAL). FT DOMAIN 312 362 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 363 383 7 (POTENTIAL). FT DOMAIN 384 387 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 228 228 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 387 AA; 46052 MW; C10A042A038263B6 CRC64; MDKHKDRIES MRLILQVMQL FGLWPWSLKS EEEWTFTGFV KRNYRFLLHL PITFTFIGLM WLEAFISSNL EQAGQVLYMS ITEMALVVKI LSIWHYRTEA WRLMYELQHA PDYQLHNQEE VDFWRREQRF FKWFFYIYIL ISLGVVYSGC TGVLFLEGYE LPFAYYVPFE WQNERRYWFA YGYDMAGMTL TCISNITLDT LGCYFLFHIS LLYRLLGLRL RETKNMKNDT IFGQQLRAIF IMHQRIRSLT LTCQRIVSPY ILSQIILSAL IICFSGYRLQ HVGIRDNPGQ FISMLQFVSV MILQIYLPCY YGNEITVYAN QLTNEVYHTN WLECRPPIRK LLNAYMEHLK KPVTIRAGNF FAVGLPIFVK TINNAYSFLA LLLNVSN // ID O94B_DROME STANDARD; PRT; 383 AA. AC Q9VCS8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 94b. GN OR94B OR CG6679. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003741; AAF56077.1; -. DR FlyBase; FBgn0039034; Or94b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 41 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 42 62 1 (POTENTIAL). FT DOMAIN 63 70 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 71 91 2 (POTENTIAL). FT DOMAIN 92 130 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 131 151 3 (POTENTIAL). FT DOMAIN 152 174 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 175 195 4 (POTENTIAL). FT DOMAIN 196 250 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 251 271 5 (POTENTIAL). FT DOMAIN 272 284 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 285 305 6 (POTENTIAL). FT DOMAIN 306 358 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 359 379 7 (POTENTIAL). FT DOMAIN 380 383 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 383 AA; 45262 MW; 6475485085672892 CRC64; MESTNRLSAI QTLLVIQRWI GLLKWENEGE DGVLTWLKRI YPFVLHLPLT FTYIALMWYE AITSSDFEEA GQVLYMSITE LALVTKLLNI WYRRHEAASL IHELQHDPAF NLRNSEEIKF WQQNQRNFKR IFYWYIWGSL FVAVMGYISV FFQEDYELPF GYYVPFEWRT RERYFYAWGY NVVAMTLCCL SNILLDTLGC YFMFHIASLF RLLGMRLEAL KNAAEEKARP ELRRIFQLHT KVRRLTRECE VLVSPYVLSQ VVFSAFIICF SAYRLVHMGF KQRPGLFVTT VQFVAVMIVQ IFLPCYYGNE LTFHANALTN SVFGTNWLEY SVGTRKLLNC YMEFLKRPVK VRAGVFFEIG LPIFVKTINN AYSFFALLLK ISK // ID O98A_DROME STANDARD; PRT; 397 AA. AC Q9VAZ3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 98a. GN OR98A OR CG5540. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003762; AAF56753.2; -. DR FlyBase; FBgn0039551; Or98a. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 43 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 44 64 1 (POTENTIAL). FT DOMAIN 65 77 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 78 98 2 (POTENTIAL). FT DOMAIN 99 138 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 139 159 3 (POTENTIAL). FT DOMAIN 160 192 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 193 213 4 (POTENTIAL). FT DOMAIN 214 266 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 267 287 5 (POTENTIAL). FT DOMAIN 288 293 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 294 314 6 (POTENTIAL). FT DOMAIN 315 354 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 355 375 7 (POTENTIAL). FT DOMAIN 376 397 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 336 336 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 397 AA; 45436 MW; F02F6CB7122DA45E CRC64; MLFNYLRKPN PTNLLTSPDS FRYFEYGMFC MGWHTPATHK IIYYITSCLI FAWCAVYLPI GIIISFKTDI NTFTPNELLT VMQLFFNSVG MPFKVLFFNL YISGFYKAKK LLSEMDKRCT TLKERVEVHQ GVVRCNKAYL IYQFIYTAYT ISTFLSAALS GKLPWRIYNP FVDFRESRSS FWKAALNETA LMLFAVTQTL MSDIYPLLYG LILRVHLKLL RLRVESLCTD SGKSDAENEQ DLIKCIKDHN LIIDYAAAIR PAVTRTIFVQ FLLIGICLGL SMINLLFFAD IWTGLATVAY INGLMVQTFP FCFVCDLLKK DCELLVSAIF HSNWINSSRS YKSSLRYFLK NAQKSIAFTA GSIFPISTGS NIKVAKLAFS VVTFVNQLNI ADRLTKN // ID O98B_DROME STANDARD; PRT; 382 AA. AC Q9VAW0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 98b. GN OR98B OR CG1867. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003765; AAF56788.2; -. DR FlyBase; FBgn0039582; Or98b. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 34 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 35 55 1 (POTENTIAL). FT DOMAIN 56 66 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 67 87 2 (POTENTIAL). FT DOMAIN 88 128 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 129 149 3 (POTENTIAL). FT DOMAIN 150 176 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 177 197 4 (POTENTIAL). FT DOMAIN 198 257 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 258 278 5 (POTENTIAL). FT DOMAIN 279 283 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 284 304 6 (POTENTIAL). FT DOMAIN 305 328 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 329 349 7 (POTENTIAL). FT DOMAIN 350 382 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 382 AA; 43514 MW; D42A3C682843BA9B CRC64; MLTDKFLRLQ SALFRLLGLE LLHEQDVGHR YPWRSICCIL SVASFMPLTI AFGLQNVQNV EQLTDSLCSV LVDLLALCKI GLFLWLYKDF KFLIGQFYCV LQTETHTAVA EMIVTRESRR DQFISAMYAY CFITAGLSAC LMSPLSMLIS YHEQVNCSRN FHFPVYPWDN MKLSNYIISY FWNVCAALGV ALPTVCVDTL FCSLSHNLCA LFQIARHKMM HFEGRNTKET HENLKHVFQL YALCLNLGHF LNEYFRPLIC QFVAASLHLC VLCYQLSANI LQPALLFYAA FTAAVVGQVS IYCFCGSSIH SECQLFGQAI YESSWPHLLQ ENLQLVSSLK IAMMRSSLGC PIDGYFFEAN RETLITIVRT AISYVTLLRS LA // ID OAF_DROME STANDARD; PRT; 487 AA. AC Q9NLA6; Q24556; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Out at first protein [Contains: Out at first short protein]. GN OAF OR CG9884. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=95286060; PubMed=7768442; RA Bergstrom D.E., Merli C.A., Cygan J.A., Shelby R., Blackman R.K.; RT "Regulatory autonomy and molecular characterization of the Drosophila RT out at first gene."; RL Genetics 139:1331-1346(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-89 FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; RX MEDLINE=96217926; PubMed=8675012; RA Merli C., Bergstrom D.E., Cygan J.A., Blackman R.K.; RT "Promoter specificity mediates the independent regulation of RT neighboring genes."; RL Genes Dev. 10:1260-1270(1996). CC -!- FUNCTION: VITAL FOR PROPER NEURONAL DEVELOPMENT AND HATCHING. CC -!- TISSUE SPECIFICITY: EMBRYONIC EXPRESSION IS IN SMALL CLUSTERS OF CC CELLS ALONG POSTERIOR MARGIN OF MOST SEGMENTS, BRAIN AND CC SEGMENTALLY REPEATING PATTERN ALONG MIDLINE OF NERVE CORD. CC EXPRESSED IN EMBRYONIC, LARVAL AND ADULT GONADS OF BOTH SEXES, AND CC LARVAL IMAGINAL DISKS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT WITH HIGHEST LEVELS IN PUPAE AND ADULTS. CC -!- MISCELLANEOUS: READTHROUGH OF THE TERMINATOR UGA MAY OCCUR BETWEEN CC THE CODONS FOR 332-GLU AND 334-ARG. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L31349; AAC37219.2; -. DR EMBL; AE003583; AAF51246.1; ALT_TERM. DR EMBL; U63852; AAC47551.1; -. DR FlyBase; FBgn0011818; oaf. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. KW Developmental protein. FT CHAIN 1 487 OUT AT FIRST PROTEIN. FT CHAIN 1 332 OUT AT FIRST SHORT PROTEIN. FT DOMAIN 450 480 PRO/SER/THR-RICH. FT DOMAIN 392 396 POLY-THR. FT DOMAIN 402 405 POLY-LEU. FT DOMAIN 456 459 POLY-SER. FT DOMAIN 472 480 POLY-SER. FT CONFLICT 391 391 A -> G (IN REF. 1). FT CONFLICT 400 400 R -> H (IN REF. 1). FT CONFLICT 413 413 A -> T (IN REF. 1). SQ SEQUENCE 487 AA; 53728 MW; F0D7A117BE358B3F CRC64; MILKEEHPHQ SIETAANAAR QAQVRWRMAH LKALSRTRTP AHGNCCGRVV SKNHFFKHSR AFLWFLLCNL VMNADAFAHS QLLINVQNQG GEVIQESITS NIGEDLITLE FQKTDGTLIT QVIDFRNEVQ ILKALVLGEE ERGQSQYQVM CFATKFNKGD FISSAAMAKL RQKNPHTIRT PEEDKGRETF TMSSWVQLNR SLPITRHLQG LCAEAMDATY VRDVDLKAWA ELPGSSISSL EAATEKFPDT LSTRCNEVSS LWAPCLCNLE TCIGWYPCGL KYCKGKGVAG ADSSGAQQQA QPTNYRCGIK TCRKCTQFTY YVRQKQQCLW DEXRRGELQL MQMRCARRRN GSEFGDDASA TCPGGETRAA TTTATITGGG AGGSGKDTTA ATTTTTNKLR QLLLLVQQQM PFALWSFPVH HISQSHHQSQ SQHKPSRQQK QHQHHSQVAP TSHHQSSSST PPTPSTSSSP PSSSSSSSSS AMAAIVA // ID OAR_DROME STANDARD; PRT; 601 AA. AC P22270; Q9VNW3; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyramine/octopamine receptor precursor (Tyr/Oct-Dro). GN TYRR OR OCR OR TYR OR OCTYR99AB OR CG7485. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90198291; PubMed=2156539; RA Arakawa S., Gocayne J.D., McCombie W.R., Urquhart D.A., Hall L.M., RA Fraser C.M., Venter J.C.; RT "Cloning, localization, and permanent expression of a Drosophila RT octopamine receptor."; RL Neuron 4:343-354(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=91006061; PubMed=2170118; RA Saudou F., Amlaiky N., Plassat J.-L., Borelli E., Hen R.; RT "Cloning and characterization of a Drosophila tyramine receptor."; RL EMBO J. 9:3611-3617(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RECEPTOR FOR BOTH OCTOPAMINE AND TYRAMINE, INVERTEBRATE CC NEUROTRANSMITTERS, AND NEUROMODULATORS. THE ACTIVITY OF THIS CC RECEPTOR IS MEDIATED BY G PROTEINS WHICH ACTIVATE ADENYLYL CC CYCLASE. THE RANK ORDER OF POTENCY FOR AGONISTS IS TYRAMINE > CC OCTOPAMINE > DOPAMINE > EPINEPHRINE > NOREPINEPHRINE > SEROTONIN > CC HISTAMINE. FOR ANTAGONISTS, THE RANK ORDER IS YOHIMBINE > CC CHLORPROMAZINE > PHENTOLAMINE > MIANSERINE > CYPROHEPTADINE > CC DIHYDROERGOTAMINE > CLONIDINE > SYNEPHRINE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: PREFERENTIALLY EXPRESSED IN DROSOPHILA HEADS. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60789; AAA28731.1; -. DR EMBL; X54794; CAA38565.1; -. DR EMBL; AE003596; AAF51802.1; -. DR PIR; S12004; S12004. DR HSSP; P29274; 1MMH. DR FlyBase; FBgn0004514; TyrR. DR GO; GO:0007608; P:olfaction; IMP. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 601 TYRAMINE/OCTOPAMINE RECEPTOR. FT DOMAIN 27 112 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 113 135 1 (POTENTIAL). FT DOMAIN 136 145 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 146 167 2 (POTENTIAL). FT DOMAIN 168 184 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 185 205 3 (POTENTIAL). FT DOMAIN 206 225 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 226 248 4 (POTENTIAL). FT DOMAIN 249 273 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 274 295 5 (POTENTIAL). FT DOMAIN 296 530 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 531 552 6 (POTENTIAL). FT DOMAIN 553 566 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 567 588 7 (POTENTIAL). FT DOMAIN 589 601 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 11 11 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 57 57 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 182 261 BY SIMILARITY. FT CONFLICT 34 34 S -> N (IN REF. 1). SQ SEQUENCE 601 AA; 64674 MW; 7E7581A11674B4C9 CRC64; MPSADQILFV NVTTTVAAAA LTAAAAVSTT KSGSGNAARG YTDSDDDAGM GTEAVANISG SLVEGLTTVT AALSTAQADK DSAGECEGAV EELHASILGL QLAVPEWEAL LTALVLSVII VLTIIGNILV ILSVFTYKPL RIVQNFFIVS LAVADLTVAL LVLPFNVAYS ILGRWEFGIH LCKLWLTCDV LCCTSSILNL CAIALDRYWA ITDPINYAQK RTVGRVLLLI SGVWLLSLLI SSPPLIGWND WPDEFTSATP CELTSQRGYV IYSSLGSFFI PLAIMTIVYI EIFVATRRRL RERARANKLN TIALKSTELE PMANSSPVAA SNSGSKSRLL ASWLCCGRDR AQFATPMIQN DQESISSETH QPQDSSKAGP HGNSDPQQQH VVVLVKKSRR AKTKDSIKHG KTRGGRKSQS SSTCEPHGEQ QLLPAGGDGG SCQPGGGHSG GGKSDAEIST ESGSDPKGCI QVCVTQADEQ TSLKLTPPQS STGVAAVSVT PLQKKTSGVN QFIEEKQKIS LSKERRAART LGIIMGVFVI CWLPFFLMYV ILPFCQTCCP TNKFKNFITW LGYINSGLNP VIYTIFNLDY RRAFKRLLGL N // ID OAT_DROME STANDARD; PRT; 431 AA. AC Q9VW26; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Ornithine aminotransferase, mitochondrial precursor (EC 2.6.1.13) DE (Ornithine--oxo-acid aminotransferase). GN OAT OR CG8782. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: L-ORNITHINE + A 2-OXO ACID = L-GLUTAMATE 5- CC SEMIALDEHYDE + AN L-AMINO ACID. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE (BY SIMILARITY). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003516; AAF49127.1; -. DR EMBL; AY047517; AAK77249.1; -. DR HSSP; P04181; 2OAT. DR FlyBase; FBgn0022774; Oat. DR GO; GO:0005759; C:mitochondrial matrix; NAS. DR GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; NAS. DR GO; GO:0006591; P:ornithine metabolism; NAS. DR InterPro; IPR005814; Aminotrans_3. DR Pfam; PF00202; aminotran_3; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. KW Transferase; Aminotransferase; Pyridoxal phosphate; Mitochondrion; KW Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 431 ORNITHINE AMINOTRANSFERASE. FT BINDING 286 286 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 431 AA; 47311 MW; 6E6B709C15C408E5 CRC64; MFAKLSARGI ATRMSFLAQK TASQETTAAA GSRSELVYAR ENKYGAHNYH PLPVALTKGE GVFVWDVEGK RYFDYLSAYS AVNQGHCHPK IVAALTAQAS KLALTSRAFY SDVLGEYEEY VTKLFGFDKV LPMNTGVEGG ETACKLARKW GYLEKKIPAN QAKIIFARNN FWGRTLSAVS ASNDPSSYEG FGPFMPGFEL IEYDNVSALE ESLKDPNVCA FMVEPIQGEA GVVVPSDGYL KKVRELCTKY NVLWIADEVQ TGLARTGKLL AVDYEQVQPD ILILGKALSG GMYPVSAVLC NDQVMLCIKP GEHGSTYGGN PLGCRVAMAA LEVLQEEKLA ENAFKMGDLL RNELSTLPKD VVSVVRGKGL LNAIVINQKF DAWEVCLRLK ENGLLAKPTH GDIIRFAPPL VINETQMRES IDIIRKTILS M // ID OAZ_DROME STANDARD; PRT; 254 AA. AC P54361; O44436; DT 01-OCT-1996 (Rel. 34, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ornithine decarboxylase antizyme (ODC-Az) (Gutfeeling protein). GN ODA OR GUF OR CG16747. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97032936; PubMed=8878684; RA Salzberg A., Golden K., Bodmer R., Bellen H.J.; RT "Gutfeeling, a Drosophila gene encoding an antizyme-like protein, is RT required for late differentiation of neurons and muscles."; RL Genetics 144:183-196(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=98147796; PubMed=9488472; RA Ivanov I.P., Simin K., Letsou A., Atkins J.F., Gesteland R.F.; RT "The Drosophila gene for antizyme requires ribosomal frameshifting for RT expression and contains an intronic gene for snRNP Sm D3 on the RT opposite strand."; RL Mol. Cell. Biol. 18:1553-1561(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: BINDS TO, AND DESTABILIZES, ORNITHINE DECARBOXYLASE. CC REQUIRED FOR CELLULAR DIFFERENTIATION IN NEURONAL AND MYOGENIC CC LINEAGES DURING EMBRYONIC DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN ALL STAGES OF EMBRYONIC AND CC LARVAL DEVELOPMENT AS WELL AS IN PUPAE AND ADULTS. CC -!- MISCELLANEOUS: A RIBOSOMAL FRAMESHIFT OCCURS BETWEEN THE CODONS CC FOR SER-61 AND ASP-62. AN AUTOREGULATORY MECHANISM ENABLES CC MODULATION OF FRAMESHIFTING ACCORDING TO THE CELLULAR CC CONCENTRATION OF POLYAMINES. CC -!- SIMILARITY: BELONGS TO THE ODC ANTIZYME FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U29529; AAB49330.1; ALT_SEQ. DR EMBL; AF038597; AAC97538.1; -. DR EMBL; AE003823; AAF58569.2; -. DR FlyBase; FBgn0014184; Oda. DR GO; GO:0007422; P:peripheral nervous system development; NAS. DR InterPro; IPR002993; ODC_AZ. DR Pfam; PF02100; ODC_AZ; 1. DR ProDom; PD007483; ODC_AZ; 1. DR PROSITE; PS01337; ODC_AZ; 1. KW Developmental protein; Ribosomal frameshift. SQ SEQUENCE 254 AA; 28282 MW; 22A73822A2C50D59 CRC64; MPSNMNNKLD PVFSSGFVRR EFNDSGIADG KLRTISTSSC ATTMSSESYR ISLGVGPLWW SDVPVHHRTD HDRASLLTGY SRKSSVDSAG GSLYEASSRA SSLSSSQSDC SDLESQPDIH SLCSDDDCQE VLRQILQHDQ PVQITIKLHV TEDQYTNWNT ILNPVNNLLY VALPKDLPPA GSKQTFISLL EFAEEKLEVD GIVMVMPKDQ PDRARLIEAF LFMGFEPLSR KAPQAPPAAI NDNENYYFLY SIEE // ID OB10_DROME STANDARD; PRT; 155 AA. AC Q27377; Q9VVD1; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant-binding protein A10 precursor (Antennal protein 10) DE (OS-D protein). GN A10 OR OS-D OR CG6642. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Antenna; RX MEDLINE=94121915; PubMed=7545907; RA Pikielny C.W., Hasan G., Rouyer F., Rosbash M.; RT "Members of a family of Drosophila putative odorant-binding proteins RT are expressed in different subsets of olfactory hairs."; RL Neuron 12:35-49(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CS-5; TISSUE=Antenna; RX MEDLINE=94266829; PubMed=8206941; RA McKenna M.P., Hekmat-Scafe D.S., Gaines P., Carlson J.R.; RT "Putative Drosophila pheromone-binding proteins expressed in a RT subregion of the olfactory system."; RL J. Biol. Chem. 269:16340-16347(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: ANTENNA. IN THE THIRD ANTENNAL SEGMENT. CC EXPRESSED IN SENCILLA COELOCONICA. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN ADULT BUT NOT IN LARVAL CC OLFACTORY ORGANS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05244; AAC46473.1; -. DR EMBL; U02546; AAA21358.1; -. DR EMBL; AE003525; AAF49381.1; -. DR FlyBase; FBgn0011293; a10. DR InterPro; IPR005055; A10_OS-D. DR Pfam; PF03392; OS-D; 1. KW Signal. FT SIGNAL 1 29 POTENTIAL. FT CHAIN 30 155 PUTATIVE ODORANT-BINDING PROTEIN A10. FT CONFLICT 13 13 F -> V (IN REF. 3). SQ SEQUENCE 155 AA; 17828 MW; BCB4457701848B86 CRC64; MGQPGFRRAI GHFSLVVALM CTTCFQVEGL PHPPATSPSP MMERMVEQAY DDKFDNVDLD EILNQERLLI NYIKCLEGTG PCTPDAKMLK EILPDAIQTD CTKCTEKQRY GAEKVTRHLI DNRPTDWERL EKIYDPEGTY RIKYQEMKSK ANEEP // ID OBA5_DROME STANDARD; PRT; 210 AA. AC P54185; Q9VPZ9; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant-binding protein A5 precursor (Antennal protein 5). GN A5 OR CG5430. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Antenna; RX MEDLINE=94121915; PubMed=7545907; RA Pikielny C.W., Hasan G., Rouyer F., Rosbash M.; RT "Members of a family of Drosophila putative odorant-binding proteins RT are expressed in different subsets of olfactory hairs."; RL Neuron 12:35-49(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED IN THE LUMEN OF THE SENSILLA CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: CELLS AT THE BASES OF A FEW SCATTERED SENSILLA CC ON THE POSTERIOR SURFACE OF THE ANTENNA. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATIDYLETHANOLAMINE-BINDING CC PROTEIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05243; AAC46472.1; -. DR EMBL; AE003586; AAF51385.1; -. DR HSSP; P13696; 1A44. DR FlyBase; FBgn0011294; a5. DR InterPro; IPR001858; PBP. DR InterPro; IPR008914; PEBP. DR Pfam; PF01161; PBP; 1. DR ProDom; PD004330; PBP; 1. DR PROSITE; PS01220; PBP; 1. KW Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 210 PUTATIVE ODORANT-BINDING PROTEIN A5. FT CONFLICT 13 13 F -> W (IN REF. 1). FT CONFLICT 105 105 W -> R (IN REF. 1). SQ SEQUENCE 210 AA; 24573 MW; 1DB9C0AFAD286719 CRC64; MKLPALHLLF LGFICLARSQ DNDENVRRIM KEMEVIPEIL DEPPRELLRI KYDNTIDIEE GKTYTPTELK FQPRLDWNAD PESFYTVLMI CPDAPNRENP MYRSWLHWLV VNVPGLDIMK GQPISEYFGP LPPKDSGIQR YLILVYQQSD KLDFDEKKME LSNADGHSNF DVMKFTQKYE MGSPVAGNIF QSRWDEYVPE LMKTLYGVSE // ID ODD_DROME STANDARD; PRT; 392 AA. AC P23803; DT 01-NOV-1991 (Rel. 20, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odd-skipped protein. GN ODD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91006082; PubMed=2120051; RA Coulter D.E., Swaykus E.A., Beran-Koehn M.A., Goldberg D., RA Wieschaus E., Schedl P.; RT "Molecular analysis of odd-skipped, a zinc finger encoding RT segmentation gene with a novel pair-rule expression pattern."; RL EMBO J. 9:3795-3804(1990). CC -!- FUNCTION: PAIR-RULE PROTEIN THAT ESTABLISH PORTION OF ALTERNATING CC SEGMENTS DURING EMBRYOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: CONTAINS 4 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57480; CAA40718.1; -. DR HSSP; P07248; 2ADR. DR TRANSFAC; T00667; -. DR FlyBase; FBgn0002985; odd. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 4. DR ProDom; PD000003; Znf_C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. KW Developmental protein; Pair-rule protein; Zinc-finger; Metal-binding; KW DNA-binding; Repeat; Nuclear protein. FT DOMAIN 82 93 POLY-GLN. FT DOMAIN 101 106 POLY-GLN. FT DOMAIN 142 149 POLY-GLN. FT DOMAIN 150 181 HIS/PRO-RICH. FT ZN_FING 220 242 C2H2-TYPE 1. FT ZN_FING 248 270 C2H2-TYPE 2. FT ZN_FING 276 298 C2H2-TYPE 3. FT ZN_FING 304 326 C2H2-TYPE 4. FT DOMAIN 369 375 POLY-SER. SQ SEQUENCE 392 AA; 44654 MW; 7272DD5C367F20B0 CRC64; MSSTSASPIS NITVDDELNL SREQDFAEDD FIVIKEERET SLSPMLTPPH TPTEEPLRRV HPAISEEAVA TQLHMRHMAH YQQQQQQQQQ QQQHRLWLQM QQQQQQHQAP QQYPVYPTAS ADPVAVHQQL MNHWIRNAAI YQQQQQQQQH PHHHHHHGHP HHPHPHPHHV RPYPAGLHSL HAAVVGRHFG AMPTLKLGGA GGASGVPSCA TGSSRPKKQF ICKYCNRQFT KSYNLLIHER THTDERPYSC DICGKAFRRQ DHLRDHRYIH SKDKPFKCSD CGKGFCQSRT LAVHKVTHLE EGPHKCPICQ RSFNQRANLK SHLQSHSEQS TKEVVVTTSP ATSHSVPNQA LSSPQPENLV QHLPVLDLSS SSSSSEKPKR MLGFTIDEIM SR // ID OFU1_DROME STANDARD; PRT; 402 AA. AC Q9V6X7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative GDP-fucose protein O-fucosyltransferase 1 precursor DE (EC 2.4.1.221) (Peptide O-fucosyltransferase) (O-FucT-1). GN O-FUT1 OR CG12366. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP HOMOLOGY. RX MEDLINE=21523965; PubMed=11524432; RA Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., RA Haltiwanger R.S.; RT "Modification of epidermal growth factor-like repeats with O-fucose: RT molecular cloning and expression of a novel GDP-fucose protein RT O-fucosyltransferase."; RL J. Biol. Chem. 276:40338-40345(2001). RN [3] RP HOMOLOGY. RX MEDLINE=21671316; PubMed=11698403; RA Roos C., Kolmer M., Mattila P., Renkonen R.; RT "Composition of Drosophila melanogaster proteome involved in RT fucosylated glycan metabolism."; RL J. Biol. Chem. 277:3168-3175(2002). CC -!- FUNCTION: CATALYZES THE REACTION THAT ATTACHES FUCOSE THROUGH AN CC O-GLYCOSIDIC LINKAGE TO A CONSERVED SERINE OR THREONINE RESIDUE IN CC EGF DOMAINS (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: TRANSFERS AN ALPHA-L-FUCOSYL RESIDUE FROM GDP- CC BETA-L-FUCOSE TO THE SERINE HYDROXY GROUP OF A PROTEIN ACCEPTOR. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE O-FUC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003815; AAF58290.1; -. DR FlyBase; FBgn0033901; O-fut1. DR GO; GO:0030173; C:integral to Golgi membrane; ISS. DR GO; GO:0008417; F:fucosyltransferase activity; ISS. DR GO; GO:0006493; P:O-linked glycosylation; ISS. KW Hypothetical protein; Transferase; Glycosyltransferase; KW Fucose metabolism; Signal; Glycoprotein. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 402 PUTATIVE GDP-FUCOSE PROTEIN O- FT FUCOSYLTRANSFERASE 1. FT CARBOHYD 60 60 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 402 AA; 46834 MW; E52FF4F86509C2E6 CRC64; MQWLKMKLRF VNLILLLISS TCAQLGGDPN GYLTYCPCMG RFGNQADHFL GSLAFAKALN RTLILPPWVE YRRGELRSRQ VPFNTYFEVE PLKEYHRVIT MADFMWHLAD DIWPESERVS FCYKERYSLQ QEKNDPDKPN CHAKDGNPFG PFWDTFHIDF VRSEFYAPLH FDVHHSNEAA KWQTKYPAES YPVLAFTGAP ASFPVQLENC KLQRYLQWSQ RYREASKDFI REQLPRGAFL GIHLRNGIDW VRACEHVKDS QHLFASPQCL GYKNERGALY PELCMPSKEA IIRQLKRTIK NVRQTQPDNE IKSVFVASDS NHMIGELNTA LSRMGISVHK LPEDDPYLDL AILGQSNHFI GNCISSYSAF EKRERDVHGF PSYFWGFPKE KDRKHTNVHE EL // ID OGG1_DROME STANDARD; PRT; 343 AA. AC Q9V3I8; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE N-glycosylase/DNA lyase (dOgg1) [Includes: 8-oxoguanine DNA DE glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase DE (EC 4.2.99.18) (AP lyase)]. GN OGG1 OR BCDNA:LD19945 OR CG1795. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=20547843; PubMed=11095666; RA Dherin C., Dizdaroglu M., Doerflinger H., Boiteux S., Radicella J.P.; RT "Repair of oxidative DNA damage in Drosophila melanogaster: RT identification and characterization of dOgg1, a second DNA RT glycosylase activity for 8-hydroxyguanine and formamidopyrimidines."; RL Nucleic Acids Res. 28:4583-4592(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: DNA REPAIR ENZYME THAT INCISES DNA AT 8-OXOG RESIDUES. CC EXCISES 7,8-DIHYDRO-8-OXOGUANINE AND 2,6-DIAMINO-4-HYDROXY-5-N- CC METHYLFORMAMIDOPYRIMIDINE (FAPY) FROM DAMAGED DNA. HAS A BETA- CC LYASE ACTIVITY THAT NICKS DNA 3' TO THE LESION. EFFICIENTLY CC INCISES DNA DUPLEXES CONTAINING 8-HYDROXYGUANINE (8-OH-GUA), 8- CC HYDROXYADENINE (8-OH-ADE) AND ABASIC (AP) SITES PLACED OPPOSITE TO CC A CYTOSINE. CC -!- CATALYTIC ACTIVITY: ENDONUCLEOLYTIC CLEAVAGE NEAR APURINIC OR CC APYRIMIDINIC SITES TO PRODUCTS WITH 5'-PHOSPHATE. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC IN NURSE CELLS AND CC OOCYTE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE CYTOPLASM OF THE NURSE CELLS CC FROM OOGENESIS STAGE 3 AND IN THE OOCYTE CYTOPLASM FROM STAGE CC 10B ONWARDS. EXPRESSED UNIFORMLY IN THIRD LARVAL INSTAR WING CC IMAGINAL DISK. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MATERNALLY AND ZYGOTICALLY IN THE CC LARVAE. CC -!- SIMILARITY: BELONGS TO THE OGG1 FAMILY 1. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 15. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003444; AAF46404.2; -. DR EMBL; AF160942; AAD46882.1; ALT_FRAME. DR FlyBase; FBgn0027864; Ogg1. DR InterPro; IPR003265; Endo_3c. DR InterPro; IPR000445; HhH. DR Pfam; PF00730; HhH-GPD; 1. DR Pfam; PF00633; HHH; 1. DR SMART; SM00478; ENDO3c; 1. KW Hydrolase; Nuclease; Endonuclease; Lyase; DNA repair; Glycosidase; KW Multifunctional enzyme; Nuclear protein. FT ACT_SITE 250 250 BY SIMILARITY. SQ SEQUENCE 343 AA; 39406 MW; 85E1D946A6915516 CRC64; MLAHNLGFHK KRLFSNMKAV LQDRGVIGLS LEECDLERTL LGGQSFRWRS ICDGNRTKYG GVVFNTYWVL QQEESFITYE AYGTSSPLAT KDYSSLISDY LRVDFDLKVN QKDWLSKDDN FVKFLSKPVR LLSQEPFENI FSFLCSQNNN IKRISSMIEW FCATFGTKIG HFNGADAYTF PTINRFHDIP CEDLNAQLRA AKFGYRAKFI AQTLQEIQKK GGQNWFISLK SMPFEKAREE LTLLPGIGYK VADCICLMSM GHLESVPVDI HIYRIAQNYY LPHLTGQKNV TKKIYEEVSK HFQKLHGKYA GWAQAILFSA DLSQFQNTST VACKKKSNKK PKK // ID OM40_DROME STANDARD; PRT; 344 AA. AC Q9U4L6; Q9W3P9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial import receptor subunit TOM40 homolog DE (Translocase of outer membrane 40 kDa subunit homolog) (Male sterile DE protein 15). GN TOM40 OR MS(1)15 OR MIT OR CG12157. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head, Ovary, and Testis; RA Xu E.Y., Wu C.-I.; RT "A mutation in Drosophila mitochondrial membrane import protein RT disrupts early germ cell differentiation."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ESSENTIAL FOR THE IMPORT OF PROTEIN PRECURSORS INTO THE CC MITOCHONDRIA (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC OUTER MEMBRANE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TOM40 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF165113; AAF20172.1; -. DR EMBL; AE003441; AAF46272.1; -. DR FlyBase; FBgn0016041; Tom40. DR InterPro; IPR001925; Porin_Euk. DR Pfam; PF01459; Euk_porin; 1. KW Transport; Protein transport; Outer membrane; Mitochondrion; KW Transmembrane. FT CONFLICT 2 2 G -> A (IN REF. 1). FT CONFLICT 13 13 G -> D (IN REF. 1). SQ SEQUENCE 344 AA; 36336 MW; 1EE945CBD18EDEFB CRC64; MGNVLAASSG APGSGASNLG LGLQEPAPLP SNSGSLTESS SSAEGLDSLA AAKDAALENP GTVEELHKKC KDIQAITFEG AKIMLNKGLS NHFQVSHTIN MSNVVPSGYR FGATYVGTKE FSPTEAFPVL LGDIDPAGNL NANVIHQFSA RLRCKFASQI QESKVVASQL TTDYRGSDYT LSLTVANPSI FTNSGVVVGQ YLQSVTPALA LGSELAYQFG PNVPGRQIAI MSVVGRYTAG SSVWSGTLGQ SGLHVCYYQK ASDQLQIGAE VETSLRMQES VATLAYQIDL PKANLVFRGG IDSNWQIFGV LEKRLAPLPF TLALSGRMNH VKNNFRLGCG LMIG // ID OMB_DROME STANDARD; PRT; 972 AA. AC Q24432; Q27917; Q9W4K5; DT 01-NOV-1997 (Rel. 35, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Optomotor-blind protein (Lethal(1)optomotor-blind) (L(1)omb) (Bifid DE protein). GN BI OR OMB OR CG3578. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=92159016; PubMed=1741374; RA Pflugfelder G.O., Roth H., Poeck B., Kerscher S., Schwarz H., RA Jonschker B., Heisenberg M.; RT "The lethal(1)optomotor-blind gene of Drosophila melanogaster is a RT major organizer of optic lobe development: isolation and RT characterization of the gene."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1199-1203(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 1-447 FROM N.A., AND MUTATIONAL ANALYSIS. RC TISSUE=Larva; RX MEDLINE=93261414; PubMed=8492800; RA Poeck B., Balles J., Pflugfelder G.O.; RT "Transcript identification in the optomotor-blind locus of Drosophila RT melanogaster by intragenic recombination mapping and PCR-aided RT sequence analysis of lethal point mutations."; RL Mol. Gen. Genet. 238:325-332(1993). CC -!- FUNCTION: ESSENTIAL PROTEIN THAT MAY FUNCTION AS A TRANSCRIPTION CC REGULATOR. VITAL FOR PUPAL DEVELOPMENT. REQUIRED FOR PROPER CC DEVELOPMENT OF THE OPTIC LOBES AND WINGS, AND ABDOMINAL CC PIGMENTATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: IN THIRD-INSTAR LARVAE, EXPRESSED IN THE BRAIN CC REGION THAT WILL DEVELOP INTO OPTIC LOBES AND MORE WEAKLY IN THE CC THORACIC PART OF THE VENTRAL GANGLION. CC -!- DEVELOPMENTAL STAGE: THE PEAK PERIODS OF EXPRESSION ARE: MID- CC EMBRYOGENESIS, THE SECOND DAY OF PUPAL DEVELOPMENT AND IN THE CC ADULT. CC -!- SIMILARITY: CONTAINS 1 T-BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81796; AAA28736.1; -. DR EMBL; AE003431; AAF45946.2; -. DR EMBL; S61732; AAB26697.1; -. DR EMBL; S61727; AAB26697.1; JOINED. DR EMBL; S61729; AAB26697.1; JOINED. DR EMBL; S61744; AAB26699.1; -. DR EMBL; S61743; AAB26699.1; JOINED. DR EMBL; S61955; AAB26699.1; JOINED. DR PIR; A40213; A40213. DR HSSP; P24781; 1XBR. DR FlyBase; FBgn0000179; bi. DR InterPro; IPR008967; P53-like. DR InterPro; IPR000342; Regl_Gprotein. DR InterPro; IPR001699; TF_T-box. DR Pfam; PF00907; T-box; 1. DR PRINTS; PR00937; TBOX. DR SMART; SM00425; TBOX; 1. DR PROSITE; PS01283; TBOX_1; 1. DR PROSITE; PS01264; TBOX_2; 1. DR PROSITE; PS50252; TBOX_3; 1. KW DNA-binding; Nuclear protein; Transcription regulation. FT DOMAIN 51 140 ASN-RICH. FT DOMAIN 104 107 POLY-THR. FT DOMAIN 155 282 PRO-RICH. FT DOMAIN 179 184 POLY-SER. FT DOMAIN 229 236 POLY-GLN. FT DNA_BIND 332 513 T-BOX. FT DOMAIN 571 574 POLY-ASP. FT DOMAIN 604 689 ALA-RICH. FT DOMAIN 820 829 POLY-GLY. FT DOMAIN 907 913 POLY-ALA. FT DOMAIN 922 963 GLN/HIS-RICH. FT CONFLICT 10 10 L -> F (IN REF. 2). FT CONFLICT 216 216 P -> A (IN REF. 2). FT CONFLICT 511 511 F -> L (IN REF. 1). FT CONFLICT 522 522 K -> NCYR (IN REF. 1). FT CONFLICT 820 820 MISSING (IN REF. 1). SQ SEQUENCE 972 AA; 102556 MW; 61D2B3576DC6B853 CRC64; MRYDVQELLL HQSAEDPFAR FANGMAYHPF LQLTQRPTDF SVSSLLTAGS NNNNSGNTNS GNNNSNSNNN TNSNTNNTNN LVAVSPTGGG AQLSPQSNHS SSNTTTTSNT NNSSSNNNNN NSTHNNNNNH TNNNNNNNNN TSQKQGHHLS TTEEPPSPAG TPPPTIVGLP PIPPPNNNSS SSSSNNSASA AAHPSHHPTA AHHSPSTGAA APPAGPTGLP PPTPPHHLQQ QQQQQQHPAP PPPPYFPAAA LAALAGSPAG PHPGLYPGGG LRFPPHHPGA HPHAHHLGSA YTTAEDVVLA SAVAHQLHPA MRPLRALQPE DDGVVDDPKV TLEGKDLWEK FHKLGTEMVI TKSGRQMFPQ MKFRVSGLDA KAKYILLLDI VAADDYRYKF HNSRWMVAGK ADPEMPKRMY IHPDSPTTGE QWMQKVVSFH KLKLTNNISD KHGFVSTTIL NSMHKYQPRF HLVRANDILK LPYSTFRTYV FKETEFIAVT AYQNEKITQL KIDNNPFAKG FRDTGAGKRE KKQALMSNRG SDSDKLNPTH VSSSRAPLHL GHAGRPPHLH PHAALLDNQQ DDDDKLLDVV GPPQSPLLPL SHSLQQMHAH QHSAALAAWF NHLAGAGAGA SEHAAAAAAN ASAEDALRRR LQADADVERD GSDSSCSESV GGSTGGAFRP TSTGSPKEAV GAAAAAAAAG LNPGGGSYPS PNISVGPPIH PSPHLLPYLY PHGLYPPPHL GLLHNPAAAA AMSPAGLNPG LLFNAQLALA AQHPALFGHA YAAAGHTPVS PLQGLKSHRF SPYSLPGSLG SAFDAVTPGS NANRSGDPPG GGGGGLGGGV VENGPRSLSS SPRPRPASHS PPTRPISMSP TTPPSLMKQP RGGGAGAGVA QSQHSPSELK SMEKMVNGLE VQHNGSAAAA AAALQLAEEA AQHHHHTQAH HQQQQHQSHH QQQHHQQPAQ PHPHHQTHLH SHHGATTGGT DQ // ID ONEC_DROME STANDARD; PRT; 1081 AA. AC Q9NJB5; Q9V4E4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein onecut. GN ONECUT OR CG1922. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Nguyen D.N.T., Lai Z.C.; RT "The Drosophila onecut is a neural-specific transcriptional RT regulator."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTIONAL REGULATOR. BINDS AND RECOGNIZE ATTG CC SITES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: NEURAL-SPECIFIC. CC -!- SIMILARITY: BELONGS TO THE CUT HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 CUT DOMAIN. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF169227; AAF25796.1; -. DR EMBL; AE003843; AAF59330.2; -. DR FlyBase; FBgn0028996; onecut. DR InterPro; IPR007108; Cut_homeo. DR InterPro; IPR003350; Hmoeo_CUT. DR InterPro; IPR001356; Homeobox. DR Pfam; PF02376; CUT; 1. DR Pfam; PF00046; homeobox; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Transcription regulation; Homeobox; DNA-binding; Nuclear protein. FT DNA_BIND 918 977 HOMEOBOX. FT DNA_BIND 751 837 CUT. FT CONFLICT 104 104 R -> T (IN REF. 1). FT CONFLICT 132 132 D -> H (IN REF. 1). FT CONFLICT 305 305 R -> A (IN REF. 1). FT CONFLICT 497 497 R -> K (IN REF. 1). FT CONFLICT 847 847 S -> R (IN REF. 1). SQ SEQUENCE 1081 AA; 117697 MW; 2913672792F194DA CRC64; MDSLNDIIDH QTFSQELVED ASEFITVGHH SERPSQSSQQ PNSGQDLTMS MQDIISCPVK HRTCSASGSG SASGSDSVVM VIDALGQGNR QSAYQIVPQQ LQQRNMPLPF GLLERDRQHM QHGREVNTSP VDFVSSDINL DGLTVDADVS QTDHSQETAV KQEQKLLIVQ SKSQDQSHRR IRMLVDVSSV NSGLGVHVDD MDEISSDGVG CDDEGVTLSH QHLLEQEEQF GLTSHHPHLQ PHTQIIHGLH QRSTHSEMGL DNGHGEVLSV IVHSQDSDKE DCEENDDGDA EGDLENEDDD ERDSRSREQL LSHSSYQTLT SVNDRLSSPG FSQTSYATLT PIQPLPPIST MSEKFAYSGH ISGGDSGDTD VNGDGAGGGV VEVGEVTNQS SEATGTVSIS SGNATSSVCS NNDCSSFSAL SMPIGSGHLG LGVLSGVQSP FSSYEKLSSM ISPPPNNYLV SCDLHSSVSG RVINSSHLQL SHNGNKKESG THEHTHRPAD VNGGKFSYTG HISRGDSVDN DVNGEKFSFS DHISGGDSGD EDANREKFIY SDHISEGENG PDVNSGTNWL QMHSEREVRL HMPVPAELEA RFHISSERRT RLNVPPARGS LSRHLAPNAP ICPADWKADD WKHSNAGVVS LTADMPVVVS LTPTPPPLRD DSVSGIKQNE RSSPGHREQY FLDKSQEPSS VVADQCSPGI NGTPQSVCVI HQQSPSALGN GFQSSSQQAK VSSCASPKGT VSSGGAVSNR IANSSDMEEI NTKDLAQRIS AELKRYSIPQ AIFAQRVLCR SQGTLSDLLR NPKPWSKLKS GRETFRRMYK WLQEPEFQRM SALRMAAAQI PQRAPLSSGM SLGSATGPSG STGTIPTDLD PHGGPTMIQN PLTNESDSSP ASTPVTSVLV GSVVSCRRKE EPQIEQMPQP KKPRLVFTDL QRRTLQAIFK ETKRPSKEMQ VTIARQLGLE PTTVGNFFMN ARRRSMDKWR DDDSKSTMHV AHSRQQQDEQ QKDNAHTHSQ SQIQDQNHSQ NQAIHNSMSQ DPYSNLHTTA MSPLGAFDED ADMDLELESH DFDLVDPDEH GDTNDPNGDM L // ID OPAP_DROME STANDARD; PRT; 69 AA. AC P23488; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE DROMSOPA protein. GN MSOPA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91355218; PubMed=1883837; RA Grabowski D.T., Carney J.P., Kelley M.R.; RT "An adult male specific gene in Drosophila containing the repetitive RT element opa."; RL Biochim. Biophys. Acta 1090:115-118(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91227172; PubMed=1674131; RA Grabowski D.T., Carney J.P., Kelley M.R.; RT "A Drosophila gene containing the opa repetitive element is RT exclusively expressed in adult male abdomens."; RL Nucleic Acids Res. 19:1709-1709(1991). CC -!- TISSUE SPECIFICITY: ADULT MALE ABDOMEN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56491; CAA39846.1; -. DR FlyBase; FBgn0004414; msopa. SQ SEQUENCE 69 AA; 8105 MW; 5B228ACA067CDFFA CRC64; MNFIQIAVAV RPGRSGLGQT TGRSGNLPAP EQQQHHQQQQ QHQQQQQQHH QHHQHHQLQH LKRSSGWFR // ID OPA_DROME STANDARD; PRT; 609 AA. AC P39768; Q9VN66; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pair-rule protein odd-paired. GN OPA OR CG1133. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94116854; PubMed=8288124; RA Benedyk M.J., Mullen J.R., Dinardo S.; RT "Odd-paired: a zinc finger pair-rule protein required for the timely RT activation of engrailed and wingless in Drosophila embryos."; RL Genes Dev. 8:105-117(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95301100; PubMed=7781900; RA Cimbora D.M., Sakonju S.; RT "Drosophila midgut morphogenesis requires the function of the RT segmentation gene odd-paired."; RL Dev. Biol. 169:580-595(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTION FACTOR ESSENTIAL FOR PARASEGMENTAL CC SUBDIVISION OF THE DROSOPHILA EMBRYO. IT IS INVOLVED IN THE CC ACTIVATION OF WINGLESS (WG) IN ODD PARASEGMENTS. IT IS ALSO CC REQUIRED FOR THE TIMELY ACTIVATION OF WG IN THE REMAINING CC PARASEGMENTS AND FOR THE TIMELY ACTIVATION OF ENGRAILED (EN) IN CC ALL PARASEGMENTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: THE PEAK EXPRESSION IS SEEN BETWEEN 2 AND 12 CC HR OF EMBRYOGENESIS. EXPRESSION CONTINUES THROUGH THE LARVAL CC INSTARS AND DURING PUPATION ALTHOUGH AT LOWER LEVELS COMPARED WITH CC EMBRYOGENESIS. CC -!- SIMILARITY: TO THE GLI-RELATED GROUP OF C2H2-TYPE ZINC-FINGERS CC PROTEINS. CC -!- SIMILARITY: CONTAINS 5 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04435; AAA18958.1; -. DR EMBL; S78339; AAB34592.1; -. DR EMBL; AE003604; AAF52084.1; -. DR PIR; A49839; A49839. DR HSSP; P08047; 1SP2. DR TRANSFAC; T04672; -. DR FlyBase; FBgn0003002; opa. DR GO; GO:0007494; P:midgut development; IEP. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 4. DR ProDom; PD000003; Znf_C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. KW Developmental protein; Pair-rule protein; Zinc-finger; Metal-binding; KW DNA-binding; Repeat; Nuclear protein; Transcription regulation; KW Activator. FT ZN_FING 210 249 C2H2-TYPE 1 (ATYPICAL). FT ZN_FING 258 285 C2H2-TYPE 2. FT ZN_FING 291 315 C2H2-TYPE 3. FT ZN_FING 321 345 C2H2-TYPE 4. FT ZN_FING 351 375 C2H2-TYPE 5. FT DOMAIN 33 61 GLN-RICH. FT DOMAIN 94 122 ALA-RICH. FT DOMAIN 136 140 POLY-HIS. FT DOMAIN 394 398 POLY-SER. FT DOMAIN 414 434 SER-RICH. FT DOMAIN 453 466 SER-RICH. FT DOMAIN 470 494 GLN-RICH. FT DOMAIN 529 567 ALA/HIS-RICH. FT DOMAIN 593 599 POLY-HIS. FT CONFLICT 606 606 R -> A (IN REF. 3). SQ SEQUENCE 609 AA; 66323 MW; 434CF5AEF12FD6CD CRC64; MMMNAFIEPA QHHLASYGLR MSPNTTASNS NAQQQQQQQL EMTQQQQQQQ QQQQQQQQQD QESAAATAAA YQNSGYGHFN SYASRDFLLG RREAEYGVAG SAGQASAAAD SMLFSGFPAQ AAELGSGFGQ HPFHSHHHHH QMRMGMADAY AAGHPYNHHG NFPTAAVHHP VVHHPSHHAM SAMHPAGAGA FLRYMRHQPA SSASSVKQEM QCLWIDPDQP GLVPPGGRKT CNKVFHSMHE IVTHLTVEHV GGPECTTHAC FWVGCSRNGR PFKAKYKLVN HIRVHTGEKP FACPHPGCGK VFARSENLKI HKRTHTGEKP FKCEHEGCDR RFANSSDRKK HSHVHTSDKP YNCRINGCDK SYTHPSSLRK HMKVHGNVDE KSPSHGYDSE GEESSSSSII TGGAQTPPST RLDGSAGSSS GVSSLSGGSG IKSSPHSIKS EPNPMHSVHL GASSSGSSST ASSSASHLLQ HQQHQHQQQQ QQQQHQQQAQ QQQQLTAHPS DPKSSPALQL MAASASAYLP PPLGPPPSHH HHPHHHQAAP SPGAAAASAS MLHHNHHLLY HPAAQHHPPS DWYHTTAPSG SAEAMNPLNH FGHHHHHHHL MHPGARTAY // ID OPS1_DROME STANDARD; PRT; 373 AA. AC P06002; Q9TX56; Q9VDS8; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Opsin Rh1 (Outer R1-R6 photoreceptor cells opsin) (Neither DE inactivation nor afterpotential E protein). GN NINAE OR RH1 OR CG4550. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85176937; PubMed=2985266; RA O'Tousa J.E., Baehr W., Martin R.L., Hirsh J., Pak W.L., RA Applebury M.L.; RT "The Drosophila ninaE gene encodes an opsin."; RL Cell 40:839-850(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85176938; PubMed=2580638; RA Zuker C.S., Cowman A.F., Rubin G.M.; RT "Isolation and structure of a rhodopsin gene from D. melanogaster."; RL Cell 40:851-858(1985). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 26-346 FROM N.A. RX MEDLINE=94275868; PubMed=8006992; RA Carulli J.P., Chen D.M., Stark W.S., Hartl D.L.; RT "Phylogeny and physiology of Drosophila opsins."; RL J. Mol. Evol. 38:250-262(1994). CC -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT CC MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY CC LINKED TO CIS-RETINAL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY CC BE PHOSPHORYLATED. CC -!- MISCELLANEOUS: EACH DROSOPHILA EYE IS COMPOSED OF 800 FACETS OR CC OMMATIDIA. EACH OMMATIDIUM CONTAINS 8 PHOTORECEPTOR CELLS (R1-R8), CC THE R1 TO R6 CELLS ARE OUTER CELLS, WHILE R7 AND R8 ARE INNER CC CELLS. CC -!- MISCELLANEOUS: OPSIN RH1 HAS AN ABSORPTION MAXIMUM AT 480 NM. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC OPSIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K02315; AAA28733.1; -. DR EMBL; K02320; AAA28735.1; ALT_SEQ. DR EMBL; K02316; AAA28735.1; JOINED. DR EMBL; K02317; AAA28735.1; JOINED. DR EMBL; K02318; AAA28735.1; JOINED. DR EMBL; K02319; AAA28735.1; JOINED. DR EMBL; AE003728; AAF55712.1; -. DR EMBL; BT010221; AAQ23539.1; -. DR PIR; A90864; OOFF. DR HSSP; P02699; 1EDV. DR FlyBase; FBgn0002940; ninaE. DR GO; GO:0016023; C:cytoplasmic vesicle; IDA. DR GO; GO:0016027; C:inaD signaling complex; IPI. DR GO; GO:0005771; C:multivesicular body; IDA. DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA. DR GO; GO:0005767; C:secondary lysosome; IDA. DR GO; GO:0016029; C:subrhabdomeral cisterna; IDA. DR GO; GO:0015059; F:blue-sensitive opsin; NAS. DR GO; GO:0008594; P:photoreceptor cell morphogenesis (sensu Dro...; IMP. DR GO; GO:0007602; P:phototransduction; NAS. DR GO; GO:0042052; P:rhabdomere development; IMP. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Photoreceptor; Retinal protein; Transmembrane; Phosphorylation; KW Glycoprotein; G-protein coupled receptor; Vision. FT DOMAIN 1 49 EXTRACELLULAR. FT TRANSMEM 50 74 1 (POTENTIAL). FT DOMAIN 75 86 CYTOPLASMIC. FT TRANSMEM 87 112 2 (POTENTIAL). FT DOMAIN 113 126 EXTRACELLULAR. FT TRANSMEM 127 146 3 (POTENTIAL). FT DOMAIN 147 165 CYTOPLASMIC. FT TRANSMEM 166 189 4 (POTENTIAL). FT DOMAIN 190 213 EXTRACELLULAR. FT TRANSMEM 214 241 5 (POTENTIAL). FT DOMAIN 242 276 CYTOPLASMIC. FT TRANSMEM 277 300 6 (POTENTIAL). FT DOMAIN 301 307 EXTRACELLULAR. FT TRANSMEM 308 332 7 (POTENTIAL). FT DOMAIN 333 373 CYTOPLASMIC. FT CARBOHYD 20 20 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 123 200 POTENTIAL. FT BINDING 319 319 RETINAL CHROMOPHORE. SQ SEQUENCE 373 AA; 41494 MW; FFF36C90DDD68294 CRC64; MESFAVAAAQ LGPHFAPLSN GSVVDKVTPD MAHLISPYWN QFPAMDPIWA KILTAYMIMI GMISWCGNGV VIYIFATTKS LRTPANLLVI NLAISDFGIM ITNTPMMGIN LYFETWVLGP MMCDIYAGLG SAFGCSSIWS MCMISLDRYQ VIVKGMAGRP MTIPLALGKI AYIWFMSSIW CLAPAFGWSR YVPEGNLTSC GIDYLERDWN PRSYLIFYSI FVYYIPLFLI CYSYWFIIAA VSAHEKAMRE QAKKMNVKSL RSSEDAEKSA EGKLAKVALV TITLWFMAWT PYLVINCMGL FKFEGLTPLN TIWGACFAKS AACYNPIVYG ISHPKYRLAL KEKCPCCVFG KVDDGKSSDA QSQATASEAE SKA // ID OPS2_DROME STANDARD; PRT; 381 AA. AC P08099; Q9VE29; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Opsin Rh2 (Ocellar opsin). GN RH2 OR CG16740. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86133563; PubMed=2936466; RA Cowman A.F., Zuker C.S., Rubin G.M.; RT "An opsin gene expressed in only one photoreceptor cell type of the RT Drosophila eye."; RL Cell 44:705-710(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP LOCALIZATION OF OPSIN RH2, AND ABSORPTION MAXIMUM. RX MEDLINE=88261498; PubMed=2455230; RA Feiler R., Harris W.A., Kirschfeld K., Wehrhahn C., Zuker C.S.; RT "Targeted misexpression of a Drosophila opsin gene leads to altered RT visual function."; RL Nature 333:737-741(1988). RN [4] RP LOCALIZATION OF OPSIN RH2. RX MEDLINE=88261503; PubMed=2968518; RA Pollock J.A., Benzer S.; RT "Transcript localization of four opsin genes in the three visual RT organs of Drosophila; RH2 is ocellus specific."; RL Nature 333:779-782(1988). CC -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT CC MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY CC LINKED TO CIS-RETINAL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY CC BE PHOSPHORYLATED. CC -!- MISCELLANEOUS: OPSIN RH2 IS THE PREDOMINANT OPSIN EXPRESSED IN THE CC DORSAL OCELLI. CC -!- MISCELLANEOUS: OPSIN RH2 HAS AN ABSORPTION MAXIMUM AT 420 NM. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC OPSIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12896; AAA28734.1; -. DR EMBL; AE003724; AAF55601.1; -. DR PIR; A24058; OOFF2. DR HSSP; P02699; 1BOJ. DR FlyBase; FBgn0003248; Rh2. DR GO; GO:0015053; F:opsin; IDA. DR GO; GO:0007602; P:phototransduction; IGI. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Photoreceptor; Retinal protein; Transmembrane; Phosphorylation; KW Glycoprotein; G-protein coupled receptor; Vision. FT DOMAIN 1 56 EXTRACELLULAR. FT TRANSMEM 57 81 1 (POTENTIAL). FT DOMAIN 82 93 CYTOPLASMIC. FT TRANSMEM 94 119 2 (POTENTIAL). FT DOMAIN 120 133 EXTRACELLULAR. FT TRANSMEM 134 153 3 (POTENTIAL). FT DOMAIN 154 172 CYTOPLASMIC. FT TRANSMEM 173 196 4 (POTENTIAL). FT DOMAIN 197 220 EXTRACELLULAR. FT TRANSMEM 221 248 5 (POTENTIAL). FT DOMAIN 249 283 CYTOPLASMIC. FT TRANSMEM 284 307 6 (POTENTIAL). FT DOMAIN 308 314 EXTRACELLULAR. FT TRANSMEM 315 339 7 (POTENTIAL). FT DOMAIN 340 381 CYTOPLASMIC. FT CARBOHYD 27 27 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 130 207 POTENTIAL. FT BINDING 326 326 RETINAL CHROMOPHORE. SQ SEQUENCE 381 AA; 42722 MW; 628322D228396F9D CRC64; MERSHLPETP FDLAHSGPRF QAQSSGNGSV LDNVLPDMAH LVNPYWSRFA PMDPMMSKIL GLFTLAIMII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY ETWVLGPLWC DIYAGCGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKILFI WMMAVFWTVM PLIGWSAYVP EGNLTACSID YMTRMWNPRS YLITYSLFVY YTPLFLICYS YWFIIAAVAA HEKAMREQAK KMNVKSLRSS EDCDKSAEGK LAKVALTTIS LWFMAWTPYL VICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRIVLKEK CPMCVFGNTD EPKPDAPASD TETTSEADSK A // ID OPS3_DROME STANDARD; PRT; 383 AA. AC P04950; Q9TX53; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Opsin Rh3 (Inner R7 photoreceptor cells opsin). GN RH3 OR RH92CD OR CG10888. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=87218500; PubMed=2953598; RA Fryxell K.J., Meyerowitz E.M.; RT "An opsin gene that is expressed only in the R7 photoreceptor cell of RT Drosophila."; RL EMBO J. 6:443-451(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87197540; PubMed=2437266; RA Zuker C.S., Montell C., Jones K., Laverty T., Rubin G.M.; RT "A rhodopsin gene expressed in photoreceptor cell R7 of the RT Drosophila eye: homologies with other signal-transducing molecules."; RL J. Neurosci. 7:1550-1557(1987). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [5] RP SEQUENCE OF 34-355 FROM N.A. RX MEDLINE=94275868; PubMed=8006992; RA Carulli J.P., Chen D.M., Stark W.S., Hartl D.L.; RT "Phylogeny and physiology of Drosophila opsins."; RL J. Mol. Evol. 38:250-262(1994). CC -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT CC MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY CC LINKED TO CIS-RETINAL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY CC BE PHOSPHORYLATED. CC -!- MISCELLANEOUS: EACH DROSOPHILA EYE IS COMPOSED OF 800 FACETS OR CC OMMATIDIA. EACH OMMATIDIUM CONTAINS 8 PHOTORECEPTOR CELLS (R1-R8), CC THE R1 TO R6 CELLS ARE OUTER CELLS, WHILE R7 AND R8 ARE INNER CC CELLS. CC -!- MISCELLANEOUS: OPSIN RH3 IS SENSITIVE TO UV LIGHT. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC OPSIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00043; CAA68259.1; -. DR EMBL; M17718; AAA28854.1; -. DR EMBL; AE003729; AAG22157.1; -. DR EMBL; AF184224; AAD55735.1; -. DR PIR; A26768; A26768. DR HSSP; P02699; 1F88. DR FlyBase; FBgn0003249; Rh3. DR GO; GO:0015064; F:UV-sensitive opsin; IDA. DR GO; GO:0007602; P:phototransduction; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Photoreceptor; Retinal protein; Transmembrane; Phosphorylation; KW Glycoprotein; G-protein coupled receptor; Vision. FT DOMAIN 1 57 EXTRACELLULAR. FT TRANSMEM 58 82 1 (POTENTIAL). FT DOMAIN 83 94 CYTOPLASMIC. FT TRANSMEM 95 119 2 (POTENTIAL). FT DOMAIN 120 133 EXTRACELLULAR. FT TRANSMEM 134 153 3 (POTENTIAL). FT DOMAIN 154 171 CYTOPLASMIC. FT TRANSMEM 172 196 4 (POTENTIAL). FT DOMAIN 197 220 EXTRACELLULAR. FT TRANSMEM 221 248 5 (POTENTIAL). FT DOMAIN 249 284 CYTOPLASMIC. FT TRANSMEM 285 308 6 (POTENTIAL). FT DOMAIN 309 316 EXTRACELLULAR. FT TRANSMEM 317 341 7 (POTENTIAL). FT DOMAIN 342 383 CYTOPLASMIC. FT CARBOHYD 13 13 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 130 207 POTENTIAL. FT BINDING 328 328 RETINAL CHROMOPHORE. SQ SEQUENCE 383 AA; 42940 MW; BF9D009A25CA6343 CRC64; MESGNVSSSL FGNVSTALRP EARLSAETRL LGWNVPPEEL RHIPEHWLTY PEPPESMNYL LGTLYIFFTL MSMLGNGLVI WVFSAAKSLR TPSNILVINL AFCDFMMMVK TPIFIYNSFH QGYALGHLGC QIFGIIGSYT GIAAGATNAF IAYDRFNVIT RPMEGKMTHG KAIAMIIFIY MYATPWVVAC YTETWGRFVP EGYLTSCTFD YLTDNFDTRL FVACIFFFSF VCPTTMITYY YSQIVGHVFS HEKALRDQAK KMNVESLRSN VDKNKETAEI RIAKAAITIC FLFFCSWTPY GVMSLIGAFG DKTLLTPGAT MIPACACKMV ACIDPFVYAI SHPRYRMELQ KRCPWLALNE KAPESSAVAS TSTTQEPQQT TAA // ID OPS4_DROME STANDARD; PRT; 378 AA. AC P08255; Q9VVB3; DT 01-AUG-1988 (Rel. 08, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Opsin Rh4 (Inner R7 photoreceptor cells opsin). GN RH4 OR CG9668. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87197541; PubMed=2952772; RA Montell C., Jones K., Zuker C.S., Rubin G.M.; RT "A second opsin gene expressed in the ultraviolet-sensitive R7 RT photoreceptor cells of Drosophila melanogaster."; RL J. Neurosci. 7:1558-1566(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT CC MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY CC LINKED TO CIS-RETINAL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY CC BE PHOSPHORYLATED. CC -!- MISCELLANEOUS: EACH DROSOPHILA EYE IS COMPOSED OF 800 FACETS OR CC OMMATIDIA. EACH OMMATIDIUM CONTAINS 8 PHOTORECEPTOR CELLS (R1-R8), CC THE R1 TO R6 CELLS ARE OUTER CELLS, WHILE R7 AND R8 ARE INNER CC CELLS. CC -!- MISCELLANEOUS: OPSIN RH4 IS SENSITIVE TO UV LIGHT. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC OPSIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17730; AAA28856.1; -. DR EMBL; M17719; AAA28856.1; JOINED. DR EMBL; AE003526; AAF49400.1; -. DR PIR; S28789; S28789. DR FlyBase; FBgn0003250; Rh4. DR GO; GO:0015064; F:UV-sensitive opsin; IDA. DR GO; GO:0007602; P:phototransduction; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Photoreceptor; Retinal protein; Transmembrane; Phosphorylation; KW Glycoprotein; G-protein coupled receptor; Vision. FT DOMAIN 1 53 EXTRACELLULAR. FT TRANSMEM 54 78 1 (POTENTIAL). FT DOMAIN 79 90 CYTOPLASMIC. FT TRANSMEM 91 111 2 (POTENTIAL). FT DOMAIN 112 127 EXTRACELLULAR. FT TRANSMEM 128 148 3 (POTENTIAL). FT DOMAIN 149 167 CYTOPLASMIC. FT TRANSMEM 168 192 4 (POTENTIAL). FT DOMAIN 193 216 EXTRACELLULAR. FT TRANSMEM 217 244 5 (POTENTIAL). FT DOMAIN 245 280 CYTOPLASMIC. FT TRANSMEM 281 304 6 (POTENTIAL). FT DOMAIN 305 312 EXTRACELLULAR. FT TRANSMEM 313 337 7 (POTENTIAL). FT DOMAIN 338 378 CYTOPLASMIC. FT CARBOHYD 6 6 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 126 203 POTENTIAL. FT BINDING 324 324 RETINAL CHROMOPHORE. FT CONFLICT 111 112 MISSING (IN REF. 1). FT CONFLICT 120 120 A -> AIY (IN REF. 1). FT CONFLICT 313 313 P -> Q (IN REF. 1). SQ SEQUENCE 378 AA; 42657 MW; 9A33C1E6F7BD11AD CRC64; MEPLCNASEP PLRPEARSSG NGDLQFLGWN VPPDQIQYIP EHWLTQLEPP ASMHYMLGVF YIFLFCASTV GNGMVIWIFS TSKSLRTPSN MFVLNLAVFD LIMCLKAPIF IYNSFHRGFA LGNTWCQIFA SIGSYSGIGA GMTNAAIGYD RYNVITKPMN RNMTFTKAVI MNIIIWLYCT PWVVLPLTQF WDRFVPEGYL TSCSFDYLSD NFDTRLFVGT IFFFSFVCPT LMILYYYSQI VGHVFSHEKA LREQAKKMNV ESLRSNVDKS KETAEIRIAK AAITICFLFF VSWTPYGVMS LIGAFGDKSL LTPGATMIPA CTCKLVACID PFVYAISHPR YRLELQKRCP WLGVNEKSGE ISSAQSTTTQ EQQQTTAA // ID OPS5_DROME STANDARD; PRT; 382 AA. AC P91657; P91671; Q9VKD1; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Opsin Rh5. GN RH5 OR CG5279. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Retina; RX MEDLINE=97136782; PubMed=8982159; RA Chou W.-H., Hall K.J., Wilson D.B., Wideman C.L., Townson S.M., RA Chadwell L.V., Britt S.G.; RT "Identification of a novel Drosophila opsin reveals specific RT patterning of the R7 and R8 photoreceptor cells."; RL Neuron 17:1101-1115(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=97307773; PubMed=9165115; RA Papatsenko D., Sheng G., Desplan C.; RT "A new rhodopsin in R8 photoreceptors of Drosophila: evidence for RT coordinate expression with Rh3 in R7 cells."; RL Development 124:1665-1673(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT CC MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY CC LINKED TO CIS-RETINAL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED SPECIFICALLY IN THE RETINA. EACH CC DROSOPHILA EYE IS COMPOSED OF 800 FACETS OR OMMATIDIA. EACH CC OMMATIDIUM CONTAINS 8 PHOTORECEPTOR CELLS (R1- R8), THE R1 TO R6 CC CELLS ARE OUTER CELLS, WHILE R7 AND R8 ARE INNER CELLS. RH5 IS CC EXPRESSED ONLY IN THE R8 CELLS OF OMMATIDIA IN WHICH RH3 IS CC EXPRESSED IN THE OVERLYING R7 CELLS. CC -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY CC BE PHOSPHORYLATED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC OPSIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U67905; AAC47426.1; -. DR EMBL; U80667; AAB38966.1; -. DR EMBL; AE003634; AAF53145.1; -. DR EMBL; AY069237; AAL39382.1; -. DR HSSP; P02699; 1F88. DR FlyBase; FBgn0014019; Rh5. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0016016; F:short-wave-sensitive opsin; IGI. DR GO; GO:0007602; P:phototransduction; IGI. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Photoreceptor; Retinal protein; Transmembrane; Phosphorylation; KW Glycoprotein; G-protein coupled receptor; Vision. FT DOMAIN 1 49 EXTRACELLULAR. FT TRANSMEM 50 76 1 (POTENTIAL). FT DOMAIN 77 88 CYTOPLASMIC. FT TRANSMEM 89 112 2 (POTENTIAL). FT DOMAIN 113 127 EXTRACELLULAR. FT TRANSMEM 128 147 3 (POTENTIAL). FT DOMAIN 148 165 CYTOPLASMIC. FT TRANSMEM 166 190 4 (POTENTIAL). FT DOMAIN 191 214 EXTRACELLULAR. FT TRANSMEM 215 242 5 (POTENTIAL). FT DOMAIN 243 278 CYTOPLASMIC. FT TRANSMEM 279 302 6 (POTENTIAL). FT DOMAIN 303 310 EXTRACELLULAR. FT TRANSMEM 311 335 7 (POTENTIAL). FT DOMAIN 336 382 CYTOPLASMIC. FT DISULFID 124 201 POTENTIAL. FT BINDING 322 322 RETINAL CHROMOPHORE (BY SIMILARITY). FT CARBOHYD 14 14 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 21 22 SV -> RL (IN REF. 2). FT CONFLICT 56 56 Y -> N (IN REF. 2). FT CONFLICT 147 147 F -> S (IN REF. 2). FT CONFLICT 180 180 F -> W (IN REF. 2). FT CONFLICT 190 190 G -> D (IN REF. 2). FT CONFLICT 263 263 A -> P (IN REF. 2). SQ SEQUENCE 382 AA; 42704 MW; 722B4B40015345FE CRC64; MHINGPSGPQ AYVNDSLGDG SVFPMGHGYP AEYQHMVHAH WRGFREAPIY YHAGFYIAFI VLMLSSIFGN GLVIWIFSTS KSLRTPSNLL ILNLAIFDLF MCTNMPHYLI NATVGYIVGG DLGCDIYALN GGISGMGASI TNAFIAFDRY KTISNPIDGR LSYGQIVLLI LFTWLWATPF SVLPLFQIWG RYQPEGFLTT CSFDYLTNTD ENRLFVRTIF VWSYVIPMTM ILVSYYKLFT HVRVHEKMLA EQAKKMNVKS LSANANADNM SVELRIAKAA LIIYMLFILA WTPYSVVALI GCFGEQQLIT PFVSMLPCLA CKSVSCLDPW VYATSHPKYR LELERRLPWL GIREKHATSG TSGGQESVAS VSGDTLALSV QN // ID OPS6_DROME STANDARD; PRT; 369 AA. AC O01668; Q9VF58; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Opsin Rh6 (Rhodopsin Rh6, long-wavelength). GN RH6 OR CG5192. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Retina; RX MEDLINE=97263460; PubMed=9109375; RA Huber A., Schulz S., Bentrop J., Groell C., Wolfrum U., Paulsen R.; RT "Molecular cloning of Drosophila Rh6 rhodopsin: the visual pigment of RT a subset of R8 photoreceptor cells."; RL FEBS Lett. 406:6-10(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT CC MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY CC LINKED TO CIS-RETINAL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EACH DROSOPHILA EYE IS COMPOSED OF 800 FACETS CC OR OMMATIDIA. EACH OMMATIDIUM CONTAINS 8 PHOTORECEPTOR CELLS (R1- CC R8), THE R1 TO R6 CELLS ARE OUTER CELLS, WHILE R7 AND R8 ARE INNER CC CELLS. RH6 IS EXPRESSED IN A SUBSET OF R8 CELLS, MOST LIKELY CC EXPRESSED IN THE SUBSET OF R8 CELLS PAIRED WITH RH4-EXPRESSING R7 CC CELLS (R7Y). CC -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY CC BE PHOSPHORYLATED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC OPSIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z86118; CAB06821.1; -. DR EMBL; AE003709; -; NOT_ANNOTATED_CDS. DR HSSP; P02699; 1EDV. DR FlyBase; FBgn0019940; Rh6. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0015063; F:long-wave-sensitive opsin; IGI. DR GO; GO:0007602; P:phototransduction; IGI. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Photoreceptor; Retinal protein; Transmembrane; Phosphorylation; KW Glycoprotein; G-protein coupled receptor; Vision. FT DOMAIN 1 46 EXTRACELLULAR. FT TRANSMEM 47 71 1 (POTENTIAL). FT DOMAIN 72 83 CYTOPLASMIC. FT TRANSMEM 84 109 2 (POTENTIAL). FT DOMAIN 110 123 EXTRACELLULAR. FT TRANSMEM 124 143 3 (POTENTIAL). FT DOMAIN 144 162 CYTOPLASMIC. FT TRANSMEM 163 186 4 (POTENTIAL). FT DOMAIN 187 210 EXTRACELLULAR. FT TRANSMEM 211 238 5 (POTENTIAL). FT DOMAIN 239 274 CYTOPLASMIC. FT TRANSMEM 275 298 6 (POTENTIAL). FT DOMAIN 299 305 EXTRACELLULAR. FT TRANSMEM 306 330 7 (POTENTIAL). FT DOMAIN 331 369 CYTOPLASMIC. FT DISULFID 120 197 POTENTIAL. FT BINDING 317 317 RETINAL CHROMOPHORE (BY SIMILARITY). FT CARBOHYD 17 17 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 193 193 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 208 208 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 219 236 MISSING (IN REF. 2). SQ SEQUENCE 369 AA; 41691 MW; 5670A7435AD5F244 CRC64; MASLHPPSFA YMRDGRNLSL AESVPAEIMH MVDPYWYQWP PLEPMWFGII GFVIAILGTM SLAGNFIVMY IFTSSKGLRT PSNMFVVNLA FSDFMMMFTM FPPVVLNGFY GTWIMGPFLC ELYGMFGSLF GCVSIWSMTL IAYDRYCVIV KGMARKPLTA TAAVLRLMVV WTICGAWALM PLFGWNRYVP EGNMTACGTD YFAKDWWNRS YIIVYSLWVY LTPLLTIIFS YWHIMKAVAA HEKAMREQAK KMNVASLRNS EADKSKAIEI KLAKVALTTI SLWFFAWTPY TIINYAGIFE SMHLSPLSTI CGSVFAKANA VCNPIVYGLS HPKYKQVLRE KMPCLACGKD DLTSDSRTQA TAEISESQA // ID OPT1_DROME STANDARD; PRT; 737 AA. AC P91679; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Oligopeptide transporter 1 (YIN protein). GN YIN OR OPT1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97190182; PubMed=9038337; RA Amrein H., Axel R.; RT "Genes expressed in neurons of adult male Drosophila."; RL Cell 88:459-469(1997). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN NEURONS OF ADULT MALE DROSOPHILA. CC -!- SIMILARITY: BELONGS TO THE PTR2 FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85982; AAC47465.1; -. DR FlyBase; FBgn0015565; yin. DR GO; GO:0005887; C:integral to plasma membrane; IDA. DR GO; GO:0005427; F:proton-dependent oligopeptide transporter a...; IDA. DR InterPro; IPR004768; Pep_H_symport. DR InterPro; IPR000109; PTR2. DR Pfam; PF00854; PTR2; 2. DR TIGRFAMs; TIGR00926; 2A1704; 1. DR PROSITE; PS01022; PTR2_1; 1. DR PROSITE; PS01023; PTR2_2; 1. KW Transport; Transmembrane. FT TRANSMEM 68 88 POTENTIAL. FT TRANSMEM 98 118 POTENTIAL. FT TRANSMEM 126 146 POTENTIAL. FT TRANSMEM 167 187 POTENTIAL. FT TRANSMEM 201 221 POTENTIAL. FT TRANSMEM 328 348 POTENTIAL. FT TRANSMEM 358 378 POTENTIAL. FT TRANSMEM 576 596 POTENTIAL. FT TRANSMEM 623 643 POTENTIAL. FT TRANSMEM 653 673 POTENTIAL. SQ SEQUENCE 737 AA; 81632 MW; 84FF60C354C31356 CRC64; MAFVSNAIVG PENCKSVTVS LPPIPYPKSV AFIISNEFCE RFNYYGMRTI LVLYLTNKLG YNEETATVLF HTFTMLVYIF PLIGALIADG WLGKYKTILY LSLVYSLGAM VVSFGAVPLS GMPTKAVTVV GLLLIAIGNG GINPCVSPFG GEQFSLPAQS FQLAKFFSLF YFAINAGSLI STTFTPILRA DVHCFGDQDC FSLAFGVPAI LMIFSVIIFM AGKRLYRCQP PAGNMIFGVS RCIADAFKGW QKRRHSEPME SFLDYAKPTV GSRMVQETKC LGRILRLFLP FPVFWALFDQ QGSRWTFQAT RMDGNVLGFQ IKPDQMQVVN PLLILGFLPL FDYIIYPALA RCGIRRPLQK LTLGFLLAAL GFFLSAGLEM KMEQAAYRAT PIEPDMTHLR IYNGMPCRYE ISSAVVQTPR VIEPLNVWED LSLQMTESKE YTFNAQPVSG ECPSIIDKLR LQPGKSVSYF LAQDKLVEFA DGLQMAATDT GRTSVRALLN TPDGEGPVLL STESATSQEP PLTLDKGNVP QLHRITPGFA RVDINGKKVA SFEAKEGRLY SILVTGSARD GYQHNVIEVV APSTVSILWQ LPQIVVMTAA EVMFSVTGLE FSYSQSPPSM KSVLQACWLL SVAIGNMLVV VIAEFKFTSS QSGEFTLFAS LMLVDMMIFL WLARSYQYKD QREDFEDDDD ATIDSVMQSK PKATTVDTTA RKTNGIEAEP GYGAYRNHAY DNDFSEA // ID OPT_DROME STANDARD; PRT; 487 AA. AC Q95RW8; O76291; Q8MKN3; Q9UA64; Q9V355; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Optix protein (Homeobox protein SIX3). GN OPTIX OR SIX3 OR OPT OR CG18455. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B), AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Larva; RX MEDLINE=99310670; PubMed=10381573; RA Seo H.-C., Curtiss J., Mlodzik M., Fjose A.; RT "Six class homeobox genes in Drosophila belong to three distinct RT families and are involved in head development."; RL Mech. Dev. 83:127-139(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 155-214 FROM N.A., AND DEVELOPMENTAL STAGE. RX MEDLINE=98393698; PubMed=9724757; RA Toy J., Yang J.-M., Leppert G.S., Sundin O.H.; RT "The optx2 homeobox gene is expressed in early precursors of the eye RT and activates retina-specific genes."; RL Proc. Natl. Acad. Sci. U.S.A. 95:10643-10648(1998). CC -!- FUNCTION: MAY BE INVOLVED IN HEAD OR EYE DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=A; CC IsoId=Q95RW8-1; Sequence=Displayed; CC Name=B; CC IsoId=Q95RW8-2; Sequence=VSP_002258; CC Name=C; CC IsoId=Q95RW8-3; Sequence=VSP_002259; CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING EARLY DEVELOPMENT OF THE CC HEAD. FIRST EXPRESSION IN A BAND AROUND THE HEAD END OF THE STAGE CC 5 BLASTODERM EMBRYO, AT 93% TO 85% EGG LENGTH. BY THE GASTRULA CC STAGE, THE SITE OF EXPRESSION SHIFTS TO THE DORSAL-ANTERIOR CC REGION. AT STAGE 12, EXPRESSION IS FOUND IN THE CLYPEOLABRUM, THE CC STOMODAEUM, AND IN ECTODERM DORSAL TO THE FUTURE SUPRAESOPHAGEAL CC GANGLION. CC -!- SIMILARITY: BELONGS TO THE SIX/SINE OCULIS HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF099184; AAD39863.1; -. DR EMBL; AE003839; AAF59147.3; -. DR EMBL; AE003839; AAM68882.1; -. DR EMBL; AY061077; AAL28625.1; -. DR EMBL; AF050132; AAC33852.1; -. DR FlyBase; FBgn0025360; Optix. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0003677; F:DNA binding; ISS. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IEP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR007105; SIX. DR InterPro; IPR007106; SIX_SINE_homeo. DR Pfam; PF00046; homeobox; 1. DR ProDom; PD000010; Homeobox; 1. DR PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Developmental protein; DNA-binding; Homeobox; Nuclear protein; KW Alternative splicing. FT DNA_BIND 154 214 HOMEOBOX. FT VARSPLIC 221 382 Missing (in isoform B). FT /FTId=VSP_002258. FT VARSPLIC 1 228 Missing (in isoform C). FT /FTId=VSP_002259. FT CONFLICT 446 446 G -> R (IN REF. 1). FT CONFLICT 455 487 MISSING (IN REF. 1). SQ SEQUENCE 487 AA; 52419 MW; ECA9FD59F171E599 CRC64; MAVGPTEGKQ PPSESFSPTH HQIIAPSPIL AVPTLAFSAA QVEIVCKTLE DSGDIERLAR FLWSLPVALP NMHEILNCEA VLRARAVVAY HVGNFRELYA IIENHKFTKA SYGKLQAMWL EAHYIEAEKL RGRSLGPVDK YRVRKKFPLP PTIWDGEQKT HCFKERTRSL LREWYLQDPY PNPTKKRELA KATGLNPTQV GNWFKNRRQR DRAAAAKNRI QHSQNSSGMG CRSRRADGAA SPTPSDSSDS DISLGTHSPV PSSLQLQHSP GSTSNGANDR EESLSVDDDK PRDLSGSLPL PLSLPLPLAS PTHTPPQLPP GYGGGAGAGP GGPLTGPGCL PPFKLDAATS LFSAGCYLQS FSNLKEMSQQ FPIQPIVLRP HPQLPQSLAL NGASGGPPLH HPAYAAAYSV ECVPGGHGPP HPPPKLRINS PEKLNSTAVA AAASVGGGGG NQHHEPTTTG YHHSGQLMLH RPFSTSPELK HSAPEIT // ID OR13_DROME STANDARD; PRT; 418 AA. AC Q9VXL0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 13a. GN OR13A OR CG12697. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Robertson H.M.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003500; AAF48549.1; ALT_SEQ. DR FlyBase; FBgn0030715; Or13a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 38 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 39 59 1 (POTENTIAL). FT DOMAIN 60 70 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 71 91 2 (POTENTIAL). FT DOMAIN 92 140 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 141 161 3 (POTENTIAL). FT DOMAIN 162 195 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 196 216 4 (POTENTIAL). FT DOMAIN 217 273 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 274 294 5 (POTENTIAL). FT DOMAIN 295 299 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 300 320 6 (POTENTIAL). FT DOMAIN 321 385 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 386 406 7 (POTENTIAL). FT DOMAIN 407 418 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 22 22 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 109 109 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 118 118 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 418 AA; 48263 MW; 6E8EC466CF246F0E CRC64; MFYSYPYKAL SFPIQCVWLK LNGSWPLTES SRPWRSQSLL ATAYIVWAWY VIASVGITIS YQTAFLLNNL SDIIITTENC CTTFMGVLNF VRLIHLRLNQ RKFRQLIENF SYEIWIPNSS KNNVAAECRR RMVTFSIMTS LLACLIIMYC VLPLVEIFFG PAFDAQNKPF PYKMIFPYDA QSSWIRYVMT YIFTSYAGIC VVTTLFAEDT ILGFFITYTC GQFHLLHQRI AGLFAGSNAE LAESIQLERL KRIVEKHNNI ISFAKRLEDF FNPILLANLM ISSVLICMVG FQIVTGKNMF IGDYVKFIIY ISSALSQLYV LCENGDALIK QSTLTAQILY ECQWEGSDRI EIQSFTPTTK RIRNQIWFMI LCSQQPVRIT AFKFSTLSLQ SFTAILSTSI SYFTLLRSVY FDDEKKLD // ID OR19_DROME STANDARD; PRT; 387 AA. AC Q9I816; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 19a. GN OR19A OR CG18859. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE002611; AAG22450.2; -. DR FlyBase; FBgn0041626; Or19a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 40 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 41 61 1 (POTENTIAL). FT DOMAIN 62 71 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 72 92 2 (POTENTIAL). FT DOMAIN 93 127 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 128 148 3 (POTENTIAL). FT DOMAIN 149 171 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 172 192 4 (POTENTIAL). FT DOMAIN 193 254 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 255 275 5 (POTENTIAL). FT DOMAIN 276 285 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 286 306 6 (POTENTIAL). FT DOMAIN 307 336 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 337 357 7 (POTENTIAL). FT DOMAIN 358 387 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 193 193 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 387 AA; 44227 MW; 132D2FCACB345017 CRC64; MDISKVDSTR ALVNHWRIFR IMGIHPPGKR TFWGRHYTAY SMVWNVTFHI CIWVSFSVNL LQSNSLETFC ESLCVTMPHT LYMLKLINVR RMRGQMISSH WLLRLLDKRL GCDDERQIIM AGIERAEFIF RTIFRGLACT VVLGIIYISA SSEPTLMYPT WIPWNWRDST SAYLATAMLH TTALMANATL VLNLSSYPGT YLILVSVHTK ALALRVSKLG YGAPLPAVRM QAILVGYIHD HQIILRLFKS LERSLSMTCF LQFFSTACAQ CTICYFLLFG NVGIMRFMNM LFLLVILTTE TLLLCYTAEL PCKEGESLLT AVYSCNWLSQ SVNFRRLLLL MLARCQIPMI LVSGVIVPIS MKTFTVMIKG AYTMLTLLNE IRKTSLE // ID OR1A_DROME STANDARD; PRT; 392 AA. AC Q9W5G6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 1a. GN OR1A OR CG17885. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003417; AAF45495.2; -. DR FlyBase; FBgn0029521; Or1a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 60 1 (POTENTIAL). FT DOMAIN 61 75 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 76 92 2 (POTENTIAL). FT DOMAIN 93 125 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 126 146 3 (POTENTIAL). FT DOMAIN 147 177 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 178 198 4 (POTENTIAL). FT DOMAIN 199 256 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 257 277 5 (POTENTIAL). FT DOMAIN 278 287 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 288 308 6 (POTENTIAL). FT DOMAIN 309 359 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 360 380 7 (POTENTIAL). FT DOMAIN 381 392 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 392 AA; 44960 MW; 98DADF7B62E0E7DC CRC64; MSKLIEVFLG NLWTQRFTFA RMGLDLQPDK KGNVLRSPLL YCIMCLTTSF ELCTVCAFMV QNRNQIVLCS EALMHGLQMV SSLLKMAIFL AKSHDLVDLI QQIQSPFTEE DLVGTEWRSQ NQRGQLMAAI YFMMCAGTSV SFLLMPVALT MLKYHSTGEF APVSSFRVLL PYDVTQPHVY AMDCCLMVFV LSFFCCSTTG VDTLYGWCAL GVSLQYRRLG QQLKRIPSCF NPSRSDFGLS GIFVEHARLL KIVQHFNYSF MEIAFVEVVI ICGLYCSVIC QYIMPHTNQN FAFLGFFSLV VTTQLCIYLF GAEQVRLEAE RFSRLLYEVI PWQNLPPKHR KLFLFPIERA QRETVLGAYF FELGRPLLVW IFRTAGSFTT LMNALYAKYE TH // ID OR2A_DROME STANDARD; PRT; 397 AA. AC O46077; Q9W504; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Odorant receptor 2a. GN OR2A OR OR2F.1 OR DOR2F.1 OR DOR62 OR AN4 OR EG:30B8.7 OR EG:62D9.Q GN OR CG3206. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99389723; PubMed=10458908; RA Gao Q., Chess A.; RT "Identification of candidate Drosophila olfactory receptors from RT genomic DNA sequence."; RL Genomics 60:31-39(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE OF 245-397 FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Antenna; RX MEDLINE=99189757; PubMed=10089887; RA Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.; RT "A spatial map of olfactory receptor expression in the Drosophila RT antenna."; RL Cell 96:725-736(1999). RN [5] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=99166868; PubMed=10069338; RA Clyne P.J., Warr C.G., Freeman M.R., Lessing D., Kim J., Carlson J.R.; RT "A novel family of divergent seven-transmembrane proteins: candidate RT odorant receptors in Drosophila."; RL Neuron 22:327-338(1999). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN 20 SENSORY NEURONS ON THE DISTAL CC EDGE OF THE ANTENNA. CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003423; AAF45759.1; -. DR EMBL; AL009195; CAA15703.1; -. DR EMBL; AF127921; AAD26356.1; -. DR PIR; T13426; T13426. DR FlyBase; FBgn0023523; Or2a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Transmembrane; G-protein coupled receptor; Olfaction; KW Multigene family. FT DOMAIN 1 38 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 39 59 1 (POTENTIAL). FT DOMAIN 60 72 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 73 92 2 (POTENTIAL). FT DOMAIN 93 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 150 3 (POTENTIAL). FT DOMAIN 151 176 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 177 197 4 (POTENTIAL). FT DOMAIN 198 272 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 273 293 5 (POTENTIAL). FT DOMAIN 294 301 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 302 322 6 (POTENTIAL). FT DOMAIN 323 363 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 364 383 7 (POTENTIAL). FT DOMAIN 384 397 CYTOPLASMIC (POTENTIAL). FT CONFLICT 382 397 VMRFTYSVFTLLLRAK -> ARHNYIFKCPLI (IN REF. FT 1 AND 3). SQ SEQUENCE 397 AA; 45934 MW; 624C9783627FF2A3 CRC64; MEKQEDFKLN THSAVYYHWR VWELTGLMRP PGVSSLLYVV YSITVNLVVT VLFPLSLLAR LLFTTNMAGL CENLTITITD IVANLKFANV YMVRKQLHEI RSLLRLMDAR ARLVGDPEEI SALRKEVNIA QGTFRTFASI FVFGTTLSCV RVVVRPDREL LYPAWFGVDW MHSTRNYVLI NIYQLFGLIV QAIQNCASDS YPPAFLCLLT GHMRALELRV RRIGCRTEKS NKGQTYEAWR EEVYQELIEC IRDLARVHRL REIIQRVLSV PCMAQFVCSA AVQCTVAMHF LYVADDHDHT AMIISIVFFS AVTLEVFVIC YFGDRMRTQS EALCDAFYDC NWIEQLPKFK RELLFTLART QRPSLIYAGN YIALSLETFE QVMRFTYSVF TLLLRAK // ID OR7A_DROME STANDARD; PRT; 413 AA. AC Q9W3I5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 7a. GN OR7A OR CG10759. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003443; AAF46342.1; -. DR FlyBase; FBgn0030016; Or7a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Olfaction; Multigene family. FT DOMAIN 1 50 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 51 71 1 (POTENTIAL). FT DOMAIN 72 89 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 90 110 2 (POTENTIAL). FT DOMAIN 111 144 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 145 165 3 (POTENTIAL). FT DOMAIN 166 186 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 187 207 4 (POTENTIAL). FT DOMAIN 208 281 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 282 302 5 (POTENTIAL). FT DOMAIN 303 309 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 310 330 6 (POTENTIAL). FT DOMAIN 331 369 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 370 390 7 (POTENTIAL). FT DOMAIN 391 413 CYTOPLASMIC (POTENTIAL). SQ SEQUENCE 413 AA; 47649 MW; 79B33EF50291F7A2 CRC64; MAVSTRVATK QEVPESRRAF RNLFNCFYAL GMQAPDGSRP TTSSTWQRIY ACFSVVMYVW QLLLVPTFFV ISYRYMGGME ITQVLTSAQV AIDAVILPAK IVALAWNLPL LRRAEHHLAA LDARCREQEE FQLILDAVRF CNYLVWFYQI CYAIYSSSTF VCAFLLGQPP YALYLPGLDW QRSQMQFCIQ AWIEFLIMNW TCLHQASDDV YAVIYLYVVR IQVQLLARRV EKLGTDDSGQ VEIYPDERRQ EEHCAELQRC IVDHQTMLQL LDCISPVISR TIFVQFLITA AIMGTTMINI FIFANTNTKI ASIIYLLAVT LQTAPCCYQA TSLMLDNERL ALAIFQCQWL GQSARFRKML LYYLHRAQQP ITLTAMKLFP INLATYFSIA KFSFSLYTLI KGMNLGERFN RTN // ID OR9A_DROME STANDARD; PRT; 392 AA. AC Q9W2U9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative odorant receptor 9a. GN OR9A OR CG15302. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE ROLE IN THE ODORANT RESPONSE, BEING AN ODORANT CC RECEPTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY DR-OR OF G-PROTEIN COUPLED CC RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003450; AAF46589.1; -. DR FlyBase; FBgn0030204; Or9a. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004984; F:olfactory receptor activity; NAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; NAS. DR GO; GO:0007608; P:olfaction; NAS. DR InterPro; IPR004117; 7tm_6. DR Pfam; PF02949; 7tm_6; 1. KW Hypothetical protein; Transmembrane; G-protein coupled receptor; KW Glycoprotein; Olfaction; Multigene family. FT DOMAIN 1 41 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 42 62 1 (POTENTIAL). FT DOMAIN 63 74 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 75 95 2 (POTENTIAL). FT DOMAIN 96 141 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 142 162 3 (POTENTIAL). FT DOMAIN 163 202 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 203 223 4 (POTENTIAL). FT DOMAIN 224 268 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 269 289 5 (POTENTIAL). FT DOMAIN 290 297 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 298 318 6 (POTENTIAL). FT DOMAIN 319 362 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 363 383 7 (POTENTIAL). FT DOMAIN 384 392 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 128 128 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 336 336 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 392 AA; 44622 MW; C96ADBF0A87CC977 CRC64; MSDKVKGKKQ EEKDQSLRVQ ILVYRCMGID LWSPTMANDR PWLTFVTMGP LFLFMVPMFL AAHEYITQVS LLSDTLGSTF ASMLTLVKFL LFCYHRKEFV GLIYHIRAIL AKEIEVWPDA REIIEVENQS DQMLSLTYTR CFGLAGIFAA LKPFVGIILS SIRGDEIHLE LPHNGVYPYD LQVVMFYVPT YLWNVMASYS AVTMALCVDS LLFFFTYNVC AIFKIAKHRM IHLPAVGGKE ELEGLVQVLL LHQKGLQIAD HIADKYRPLI FLQFFLSALQ ICFIGFQVAD LFPNPQSLYF IAFVGSLLIA LFIYSKCGEN IKSASLDFGN GLYETNWTDF SPPTKRALLI AAMRAQRPCQ MKGYFFEASM ATFSTIVRSA VSYIMMLRSF NA // ID ORC1_DROME STANDARD; PRT; 924 AA. AC O16810; Q9V4N1; DT 15-JUL-1999 (Rel. 38, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Origin recognition complex subunit 1 (DmORC1). GN ORC1 OR CG10667. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98028570; PubMed=9363940; RA Pak D.T.S., Pflumm M., Chesnokov I., Huang D.W., Kellum R., Marr J., RA Romanowski P., Botchan M.R.; RT "Association of the origin recognition complex with heterochromatin RT and HP1 in higher eukaryotes."; RL Cell 91:311-323(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE ORIGIN RECOGNITION COMPLEX (ORC) THAT CC BINDS ORIGINS OF REPLICATION. IT HAS A ROLE IN BOTH CHROMOSOMAL CC REPLICATION AND MATING TYPE TRANSCRIPTIONAL SILENCING. BINDS TO CC THE ARS CONSENSUS SEQUENCE (ACS) OF ORIGINS OF REPLICATION IN AN CC ATP-DEPENDENT MANNER. CC -!- SUBUNIT: ORC IS COMPOSED OF SIX SUBUNITS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ORC1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF017647; AAC47802.1; -. DR EMBL; AE003840; AAF59236.1; -. DR FlyBase; FBgn0022772; Orc1. DR GO; GO:0005664; C:nuclear origin of replication recognition c...; IDA. DR GO; GO:0006270; P:DNA replication initiation; IDA. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR001025; BAH. DR Pfam; PF00004; AAA; 1. DR Pfam; PF01426; BAH; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00439; BAH; 1. KW DNA replication; Nuclear protein; DNA-binding; ATP-binding. FT NP_BIND 598 605 ATP (POTENTIAL). FT CONFLICT 159 159 A -> S (IN REF. 1). SQ SEQUENCE 924 AA; 103280 MW; AACD002DEB10A136 CRC64; MVNKENARSV GQQVKWIGSQ DELPPVKNLE HKNVYFYQKC IYGPLTLSVG DFILVSNADA AEPDTVSGCD VARILHMYEL RELTDREPCR AIVQWYSWPK AIPHNKYDDD EVAIDFSLEV IEEHRPYDND VALGAIYRKC IVLEGTSKTS AEEILKRHAN KLKSTACPMF VSRYRFVKVK RSYRLIPLEI HLEQPEDNAR PTRSSRKSLT AHRESKRSIS ARHDDTAGNK GSSVEKRRRA SMAASSSVEF IDVNSFICEN KVSPIKIVGG RSVVRLSEKK NAPEINANYL PASPLTEKNA KVETPKSRAS AARRNLNLSL DRGADTTADS DCLNYSIVQQ TPDPKTPSND MKIKLRLSER RRSVRLASMD VDPLSLEEAV QEPNAQGRKR LGVANGDIYH TPTKKSKEPL ESAAATEQTP STRRKSILKS ATSRLAEGTP RRSIHLSNIV EQRVFEDDEI ISTPKRGRSK KTVQDNDEDY SPKKSVQKTP TRTRRSSTTT KTATTPSKGI TTATATPMTP SQKMKKIRAG ELSPSMQQRT DLPAKDSSKS ELQLAREQLH VSVVPKSLPC REREFENIYA FLEGKIQDQC GGCMYVSGVP GTGKTATVTG VIRTLQRMAK QNELPAFEYL EINGMRLTEP RQAYVQIYKQ LTGKTVSWEQ AHALLEKRFT TPAPRRVTTV LLVDELDILC NRRQDVVYNL LDWPTKSAAK LVVVTIANTM DLPERLLMGK VTSRLGLTRL TFQPYSHKQL QEIVTARLGG SETFKGEAVQ LVARKVAAVS GDARRALDIC RRATEIADTA AVKCVTMLHV QQALAEMIAS AKVQAIRNCS RMEQIFLQAI AAEVTRTGVE ETTFMGVYQQ VETIAAFMGV TFPPPGRALR LCSKLGAERL IISEHSRNDL FQKILLNVSA DDIHYALRVE EMVN // ID ORC2_DROME STANDARD; PRT; 618 AA. AC Q24168; Q9VFP4; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Origin recognition complex subunit 2 (DmORC2). GN ORC2 OR CG3041. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96099403; PubMed=7502079; RA Gossen M., Pak D.T.S., Hansen S.K., Acharya J.K., Botchan M.R.; RT "A Drosophila homolog of the yeast origin recognition complex."; RL Science 270:1674-1677(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: COMPONENT OF THE ORIGIN RECOGNITION COMPLEX (ORC) THAT CC BINDS ORIGINS OF REPLICATION. IT HAS A ROLE IN BOTH CHROMOSOMAL CC REPLICATION AND MATING TYPE TRANSCRIPTIONAL SILENCING. BINDS TO CC THE ARS CONSENSUS SEQUENCE (ACS) OF ORIGINS OF REPLICATION IN AN CC ATP-DEPENDENT MANNER. CC -!- SUBUNIT: ORC IS COMPOSED OF SIX SUBUNITS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ORC2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U43504; AAC46955.1; -. DR EMBL; AE003702; AAF55006.1; -. DR EMBL; AY051471; AAK92895.1; -. DR FlyBase; FBgn0015270; Orc2. DR GO; GO:0005664; C:nuclear origin of replication recognition c...; IDA. DR GO; GO:0006260; P:DNA replication; IMP. DR GO; GO:0006270; P:DNA replication initiation; IDA. DR GO; GO:0007076; P:mitotic chromosome condensation; IMP. DR GO; GO:0007052; P:mitotic spindle assembly; IMP. DR InterPro; IPR007220; ORC2. DR Pfam; PF04084; ORC2; 1. KW DNA replication; Nuclear protein. FT CONFLICT 113 113 A -> T (IN REF. 1). FT CONFLICT 246 246 A -> G (IN REF. 1). FT CONFLICT 274 274 N -> I (IN REF. 1). SQ SEQUENCE 618 AA; 68995 MW; 39378D065F04BD88 CRC64; MSASNKGGYK TPRKENLMSI ENLTNSEEES EDLNTAMVGN AVESQPKVTS RRSTRRPSPT KKYQAYQKES NGKGQEERIV VNYVEMSDER SSDAEDQEEE ESIEESENAA RPAAKDLHLI QSEYNVAGTS MFGFNTPKKR DAMALAALNA TPCTPKTPKT PRLGVKTPDT KRKKSMDQPK TPAHVRTRVK KQIAKIVADS DEDFSGDESD FRPSDEESSS SSSSSDAGNS SDNDAADDEP KTPSRARRAI VVPVLPKTPS AARLRQSARA KKSNEFVPES DGYFHSHASS KILTSDHTLD RLKNPRLAAD RVFSLLSEIK TSAEHEGSIN AIMEEYRSYF PKWMCILNEG FNILLYGLGS KHQLLQSFHR EVLHKQTVLV VNGFFPSLTI KDMLDSITSD ILDAGISPAN PHEAVDMIEE EFALIPETHL FLIVHNLDGA MLRNVKAQAI LSRLARIPNI HLLASIDHIN TPLLWDQGKL CSFNFSWWDC TTMLPYTNET AFENSLLVQN SGELALSSMR SVFSSLTTNS RGIYMLIVKY QLKNKGNATY QGMPFRDLYS SCREAFLVSS DLALRAQLTE FLDHKLVKSK RSVDGSEQLT IPIDGALLQQ FLEEQEKK // ID ORC5_DROME STANDARD; PRT; 460 AA. AC Q24169; Q9V398; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Origin recognition complex subunit 5. GN ORC5 OR CG7833. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96099403; PubMed=7502079; RA Gossen M., Pak D.T.S., Hansen S.K., Acharya J.K., Botchan M.R.; RT "A Drosophila homolog of the yeast origin recognition complex."; RL Science 270:1674-1677(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE ORIGIN RECOGNITION COMPLEX (ORC) THAT CC BINDS ORIGINS OF REPLICATION. IT HAS A ROLE IN BOTH CHROMOSOMAL CC REPLICATION AND MATING TYPE TRANSCRIPTIONAL SILENCING. BINDS TO CC THE ARS CONSENSUS SEQUENCE (ACS) OF ORIGINS OF REPLICATION IN AN CC ATP-DEPENDENT MANNER. CC -!- SUBUNIT: ORC IS COMPOSED OF SIX SUBUNITS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ORC5 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U43505; AAC46956.1; -. DR EMBL; AE003408; AAF44824.1; -. DR EMBL; AE003641; AAF53340.1; -. DR FlyBase; FBgn0015271; Orc5. DR GO; GO:0005664; C:nuclear origin of replication recognition c...; IDA. DR GO; GO:0006270; P:DNA replication initiation; IDA. DR GO; GO:0006260; P:DNA replication; IMP. DR GO; GO:0007076; P:mitotic chromosome condensation; IMP. DR GO; GO:0007052; P:mitotic spindle assembly; IMP. DR InterPro; IPR003593; AAA_ATPase. DR SMART; SM00382; AAA; 1. KW DNA replication; Nuclear protein; ATP-binding. FT NP_BIND 41 48 ATP (POTENTIAL). SQ SEQUENCE 460 AA; 52115 MW; FDCE3969E1CBF7D2 CRC64; MEAICSSLEP LFPCREAAIE TLGELIGDSS ETYPSAIYLF GHSGTGKTAL TRAFLKECGK RQNVRTAHLN AIECYTTKIM LEILLDSLAP DQGDALKVDN MLDFVEQLRR QAATRVEDQG FLIAVDNAER LRDMDANVLP VLLRLQELTN LNLCVILLSQ LPFEKFYNKT GLSEIVCLHL AQYNKAETQR ILGSDFQQVR NQLLEQFAQD KKRLEICQEA VTEDFYNNYL NLFLSVFYKA CRDVPELQLT ARKCLSTYLE PVLDGTVDAT DISRLWRHIA GPLRSALTQI YMRIEKPAEE VEDFTAIEDQ SVRKLAQSLE LPYYAKFLLI AAFLASHNAA KQDKRLFVKH HGKQRKRMQT VNARAKTTEK MSTTLGPKSF SIDRLLAIFY AILEEKVGLT CNLLSQISTL VHLNLLSFVS GEQNIMEGSA RLQCTIGLEF VLQIGKVVGF NVRQYLCDFM // ID ORC6_DROME STANDARD; PRT; 257 AA. AC Q9Y1B2; Q9V5C5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Origin recognition complex subunit 6. GN ORC6 OR CG1584. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99276559; PubMed=10346817; RA Chesnokov I., Gossen M., Remus D., Botchan M.; RT "Assembly of functionally active Drosophila origin recognition complex RT from recombinant proteins."; RL Genes Dev. 13:1289-1296(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE ORIGIN RECOGNITION COMPLEX (ORC) THAT CC BINDS ORIGINS OF REPLICATION. IT HAS A ROLE IN BOTH CHROMOSOMAL CC REPLICATION AND MATING TYPE TRANSCRIPTIONAL SILENCING. BINDS TO CC THE ARS CONSENSUS SEQUENCE (ACS) OF ORIGINS OF REPLICATION IN AN CC ATP-DEPENDENT MANNER (BY SIMILARITY). CC -!- SUBUNIT: ORC IS COMPOSED OF SIX SUBUNITS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ORC6 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF139064; AAD39474.1; -. DR EMBL; AE003832; AAF58890.1; -. DR FlyBase; FBgn0023180; Orc6. DR GO; GO:0005664; C:nuclear origin of replication recognition c...; IDA. DR GO; GO:0006270; P:DNA replication initiation; IDA. DR InterPro; IPR008721; ORC6. DR Pfam; PF05460; ORC6; 1. KW DNA replication; Nuclear protein; DNA-binding. FT CONFLICT 73 73 G -> A (IN REF. 1). FT CONFLICT 213 213 E -> D (IN REF. 1). SQ SEQUENCE 257 AA; 29239 MW; 19537834E47AFDDF CRC64; MTTLIEQLIT KMGLREEPNV LEKTTELVRL LELRSTNVPL QINEYGKIVL CADLASCMIG IAFDKEQALK LSGLRKSQYL NNKRMFEKLL DLNKLASVND ICVQLGLNEV ARKAEELMTL FKGVAATEDM GTDTSHPQYA TMAVFQACRL LKKKVSKSKL MPFSNLRPSQ FQLLEQQWER MIAKHHKESK VPSSTDMEGK LKENQNENIK GHEAKKAHKP PPEDYEIWKA RMLAKAQAKL KELEASQSHM DSQLLEA // ID ORD_DROME STANDARD; PRT; 479 AA. AC Q24434; Q9W1S8; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ORD protein (Orientation disrupter protein). GN ORD OR CG3134. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=96205883; PubMed=8635478; RA Bickel S.E., Wyman D.W., Miyazaki W.Y., Moore D.P., Orr-Weaver T.L.; RT "Identification of ORD, a Drosophila protein essential for sister RT chromatid cohesion."; RL EMBO J. 15:1451-1459(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP CHARACTERIZATION. RX MEDLINE=22057565; PubMed=12062057; RA Bickel S.E., Orr-Weaver T.L., Balicky E.M.; RT "The sister-chromatid cohesion protein ORD is required for chiasma RT maintenance in Drosophila oocytes."; RL Curr. Biol. 12:925-929(2002). RN [4] RP CHARACTERIZATION. RX MEDLINE=22317261; PubMed=12429833; RA Balicky E.M., Endres M.W., Lai C., Bickel S.E.; RT "Meiotic cohesion requires accumulation of ORD on chromosomes before RT condensation."; RL Mol. Biol. Cell 13:3890-3900(2002). CC -!- FUNCTION: ESSENTIAL FOR PROPER MAINTENANCE OF SISTER-CHROMATID CC COHESION IN BOTH MALE AND FEMALE MEIOSIS. MUTATIONS IN ORD CAUSE CC PREMATURE SEPARATION OF THE SISTER CHROMATIDS IN MEIOSIS I AND CC RANDOM SEGREGATION IN BOTH MEIOTIC DIVISIONS. REQUIRED FOR CHIASMA CC MAINTENANCE IN FEMALE MEIOSIS. MUTATIONS IN ORD REDUCE CC RECOMBINATION IN FEMALE MEIOSIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. IN MALE MEIOSIS IT ASSEMBLES ONTO CC CHROMOSOMES IN LATE G2 OF THE MEIOTIC CELL CYCLE. IT REMAINS AT CC THE CENTROMERES AFTER CHROMOSOME CONDENSATION, THROUGH THE MEIOSIS CC I DIVISION UNTIL THE SEPARATION OF SISTER CHROMATIDS AT ANAPHASE CC II. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X92840; CAA63426.1; -. DR EMBL; AE003460; AAF46975.1; -. DR PIR; S66578; S66578. DR GermOnline; 210255; -. DR FlyBase; FBgn0003009; ord. DR GO; GO:0007059; P:chromosome segregation; IMP. DR GO; GO:0007066; P:female meiosis sister chromatid cohesion; IMP. DR GO; GO:0007276; P:gametogenesis; IMP. DR GO; GO:0007126; P:meiosis; IMP. DR GO; GO:0007067; P:mitosis; IMP. KW Meiosis; Nuclear protein. FT CONFLICT 444 444 D -> E (IN REF. 1). SQ SEQUENCE 479 AA; 55166 MW; D2149D0325E2497D CRC64; MYGETTLNKN HVIKFIKLKI NNCLGCDEVE INFSKADNVH IIIYSLVTDM AKDLPAVTPV AQAILLLCSL TYPDSDSLET IPQLKIGKGS VSMSFKVYPV NKEEETEPES ESDLDEGPST SKQALERMVQ RAERKAKEAS TRNVHSKGIY VNVERRFDMY FALDTVSYYI NGGKRQSCPL PEFHAKFFVR PQHSINLLRQ LHEKCSGNWL KVIQSDGDGD AFKKFKDPDS PFETFVKLFE SNPIKPNDMM GKLAKTCLHV NEAVRLTERE FILEVFNQVR HIFEYITAQE YTVWFLVPCL GDKDQLRSKT LEDFDLTKVR TSIRRAGDTS NIWWDHTDHN IKDILLVAFQ LDLATHVNQS VLVISHLETL AEFSTMQYVT AFFMNDFYAK KNTEPKWICH RYLERIIDVA LFLGVIVIIE YPSAFTLLQE GRHLIKCFQK ENADSSRTSQ WEIFEDVVKE NESDLEFLKE AVGKVQQNV // ID ORK1_DROME STANDARD; PRT; 1001 AA. AC Q94526; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Open rectifier potassium channel protein 1 (Two pore domain potassium DE channel Ork1). GN ORK1 OR CG1615. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Larva; RX MEDLINE=97075152; PubMed=8917578; RA Goldstein S.A.N., Price L.A., Rosenthal D.N., Pausch M.H.; RT "ORK1, a potassium-selective leak channel with two pore domains RT cloned from Drosophila melanogaster by expression in Saccharomyces RT cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13256-13261(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BACKGROUND POTASSIUM CHANNEL. RECTIFICATION IS DEPENDENT CC ON EXTERNAL POTASSIUM CONCENTRATION. ACTS AS AN OUTWARDLY CC RECTIFYING CHANNEL BUT AS EXTERNAL POTASSIUM LEVELS INCREASE, THIS CC IS REVERSED. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: WIDESPREAD EXPRESSION IN ADULT, STRONGEST CC EXPRESSION IN MUSCLE, BRAIN AND OVARY. ALSO PRESENT AT LOW LEVELS CC IN LARVA AND EMBRYO. CC -!- MISCELLANEOUS: INHIBITED BY BARIUM. CC -!- SIMILARITY: BELONGS TO THE TWO PORE DOMAIN POTASSIUM CHANNEL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U55321; AAC69250.1; -. DR EMBL; AE003484; AAF47972.1; -. DR PIR; T13807; T13807. DR FlyBase; FBgn0017561; Ork1. DR InterPro; IPR003280; K+channel_2pore. DR InterPro; IPR001622; K+channel_pore. DR PRINTS; PR01333; 2POREKCHANEL. KW Ionic channel; Transmembrane; Ion transport; Potassium transport; KW Glycoprotein. FT DOMAIN 1 6 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 7 27 POTENTIAL. FT DOMAIN 95 111 PORE-FORMING 1 (POTENTIAL). FT TRANSMEM 120 140 POTENTIAL. FT DOMAIN 141 170 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 171 191 POTENTIAL. FT DOMAIN 208 224 PORE-FORMING 2 (POTENTIAL). FT TRANSMEM 244 264 POTENTIAL. FT DOMAIN 265 1001 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 58 58 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1001 AA; 109289 MW; 09AE1A3669072E07 CRC64; MSPNRWILLL IFYISYLMFG AAIYYHIEHG EEKISRAEQR KAQIAINEYL LEELGDKNTT TQDEILQRIS DYCDKPVTLP PTYDDTPYTW TFYHAFFFAF TVCSTVGYGN ISPTTFAGRM IMIAYSVIGI PVNGILFAGL GEYFGRTFEA IYRRYKKYKM STDMHYVPPQ LGLITTVVIA LIPGIALFLL LPSWVFTYFE NWPYSISLYY SYVTTTTIGF GDYVPTFGAN QPKEFGGWFV VYQIFVIVWF IFSLGYLVMI MTFITRGLQS KKLAYLEQQL SSNLKATQNR IWSGVTKDVG YLRRMLNELY ILKVKPVYTD VDIAYTLPRS NSCPDLSMYR VEPAPIPSRK RAFSVCADMV AAQREAGMVH ANSDTELSKL DREKTFETAE AYRQTTDLLA KVVNALATVK PPPAEQEDAA LYGGYHGFSD SQILASEWSF STVNEFTSPR RPRARACSDF NLEAPRWQSE RPLRSSHNEW TWSGDNQQIQ EAFNQRYKGQ QRANGAANST MVHLEPDALE EQLKKQSPGA GRVKKFSMPD GLRRLFPFQK KRPSQDLERK LSVVSVPEGV ISQQARSPLD YYSNTVTAAS SQSYLRNGRG PPPPFESNGS LASGGGGLTN MGFQMEDGAT PPSALGGGAY QRKAAAGKRR RESIYTQNQA PSARRGSMYP PTAHALAQMQ MRRGSLATSG SGSAAMAAVA ARRGSLFPAT ASASSLTSAP RRSSIFSVTS EKDMNVLEQT TIADLIRALE VVHTHAVLDE QQQAAAAGGA AGGGGISRGS RKQRKMGNAG LEPPQLPPIL SLFAGDQTRT LQAAAANRLY ARRSTIVGIS PTGGAATAPA ARSLLEPPPS YTERAANQSQ ITAGPSNAPT VQSKFRRRFS VRPTALQIPP GQAPPPGASL MEQSSQTALQ RRLSLRPSPL ARELSPTSPP GGSGSALPAG AIDESGGTSA QRLLPLPAGT RPSTSSTHSP LSRIVQISQA QRKSSMPSAA ATGSSGAPAE K // ID OSA_DROME STANDARD; PRT; 2716 AA. AC Q8IN94; O61603; Q9VEG7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trithorax group protein OSA (Eyelid protein). GN OSA OR ELD OR CG7467. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=97415319; PubMed=9271118; RA Treisman J.E., Luk A., Rubin G.M., Heberlein U.; RT "eyelid antagonizes wingless signaling during Drosophila development RT and has homology to the Bright family of DNA-binding proteins."; RL Genes Dev. 11:1949-1962(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX MEDLINE=99112962; PubMed=9895321; RA Vazquez M., Moore L., Kennison J.A.; RT "The trithorax group gene osa encodes an ARID-domain protein that RT genetically interacts with the brahma chromatin-remodeling factor to RT regulate transcription."; RL Development 126:733-742(1999). RN [4] RP DNA-BINDING, AND IDENTIFICATION IN A BRAHMA COMPLEX WITH BRM AND SNR1. RX MEDLINE=20069333; PubMed=10601025; RA Collins R.T., Furukawa T., Tanese N., Treisman J.E.; RT "Osa associates with the Brahma chromatin remodeling complex and RT promotes the activation of some target genes."; RL EMBO J. 18:7029-7040(1999). RN [5] RP FUNCTION. RX MEDLINE=99403006; PubMed=10471712; RA Staehling-Hampton K., Ciampa P.J., Brook A., Dyson N.; RT "A genetic screen for modifiers of E2F in Drosophila melanogaster."; RL Genetics 153:275-287(1999). RN [6] RP IDENTIFICATION IN A BRAHMA COMPLEX WITH BRM; OSA; MOR; SNR1; DALAO; RP BAP55; BAP60 AND BAP47, AND FUNCTION AS COACTIVATOR. RX MEDLINE=20270023; PubMed=10809665; RA Kal A.J., Mahmoudi T., Zak N.B., Verrijzer C.P.; RT "The Drosophila brahma complex is an essential coactivator for the RT trithorax group protein zeste."; RL Genes Dev. 14:1058-1071(2000). RN [7] RP FUNCTION AS A COREPRESSOR. RX MEDLINE=20573925; PubMed=11124806; RA Collins R.T., Treisman J.E.; RT "Osa-containing Brahma chromatin remodeling complexes are required RT for the repression of wingless target genes."; RL Genes Dev. 14:3140-3152(2000). RN [8] RP FUNCTION AS A COREPRESSOR, AND INTERACTION WITH PNR AND CHI. RX MEDLINE=22515897; PubMed=12629041; RA Heitzler P., Vanolst L., Biryukova I., Ramain P.; RT "Enhancer-promoter communication mediated by Chip during RT Pannier-driven proneural patterning is regulated by Osa."; RL Genes Dev. 17:591-596(2003). CC -!- FUNCTION: TRITHORAX GROUP (TRXG) PROTEIN REQUIRED FOR EMBRYONIC CC SEGMENTATION, DEVELOPMENT OF THE NOTUM AND WING MARGIN, AND CC PHOTORECEPTOR DIFFERENTIATION. REQUIRED FOR THE ACTIVATION OF CC GENES SUCH AS ANTP, UBX AND EVE. BINDS TO DNA WITHOUT SPECIFIC CC AFFINITY, SUGGESTING THAT IT IS RECRUITED TO PROMOTERS BY CC PROMOTER-SPECIFIC PROTEINS. ESSENTIAL COMPONENT OF THE BRAHMA CC COMPLEX, A MULTIPROTEIN COMPLEX WHICH IS THE EQUIVALENT OF THE CC YEAST SWI/SNF COMPLEX AND ACTS BY REMODELLING THE CHROMATIN BY CC CATALYZING AN ATP-DEPENDENT ALTERATION IN THE STRUCTURE OF CC NUCLEOSOMAL DNA. THIS COMPLEX CAN BOTH SERVE AS A TRANSCRIPTIONAL CC COACTIVATOR OR COREPRESSOR, DEPENDING ON THE CONTEXT. ACTS AS AN CC ESSENTIAL COACTIVATOR FOR ZESTE, WHICH RECRUITS THE WHOLE COMPLEX CC TO SPECIFIC GENES. IN CONTRAST, IT ACTS AS A COREPRESSOR FOR WG CC TARGET GENES, POSSIBLY VIA AN INTERACTION WITH PAN AND GRO. IT CC ALSO ACTS AS A NEGATIVE REGULATOR FOR PRONEURAL ACHAETE-SCUTE, CC WHEN IT IS DIRECTLY RECRUITED BY PAN AND CHI. ALSO REPRESSES E2F CC ACTIVATION. CC -!- SUBUNIT: COMPONENT OF THE BRAHMA COMPLEX, WHICH IS COMPOSED OF CC BRM, OSA, MOR, SNR1/BAP45, BAP111/DALAO, BAP55, BAP60 AND BAP47. CC INTERACTS WITH PNR AND CHI VIA ITS EHD DOMAIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED IN EARLY EMBRYO. IN CC THIRD INSTAR LARVAE, IT IS UBIQUITOUSLY EXPRESSED IN WING AND EYE- CC ANTENNA IMAGINAL DISKS, WITH A STRONGER EXPRESSION IN A BAND JUST CC ANTERIOR TO THE MORPHOGENETIC FURROW. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- DOMAIN: THE ARID DOMAINS MEDIATES THE BINDING TO DNA. CC -!- SIMILARITY: CONTAINS 1 ARID DOMAIN. CC -!- SIMILARITY: CONTAINS 1 EHD (EYELID HOMOLOGY) DOMAIN. CC -!- CAUTION: REF.2 (AAF55457) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF053091; AAC06254.1; -. DR EMBL; AE003718; AAF55457.1; ALT_SEQ. DR EMBL; AE003718; AAN13750.1; -. DR PIR; T13049; T13049. DR FlyBase; FBgn0003013; osa. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP. DR GO; GO:0045449; P:regulation of transcription; IDA. DR GO; GO:0007379; P:segment specification; IMP. DR GO; GO:0008587; P:wing margin morphogenesis; IMP. DR GO; GO:0016055; P:Wnt receptor signaling pathway; IMP. DR InterPro; IPR001606; ARID. DR InterPro; IPR008938; ARM. DR InterPro; IPR006031; XYPPX. DR Pfam; PF01388; ARID; 1. DR Pfam; PF02162; XYPPX; 8. DR SMART; SM00501; BRIGHT; 1. KW Transcription regulation; DNA-binding; Activator; Repressor; KW Chromatin regulator; Nuclear protein; Developmental protein. FT DOMAIN 997 1111 ARID. FT DOMAIN 1769 2517 EHD. FT DOMAIN 19 1763 PRO-RICH. FT DOMAIN 174 380 GLN-RICH. FT DOMAIN 619 873 GLY-RICH. FT DOMAIN 1222 1453 GLY-RICH. FT DOMAIN 1271 1751 GLN-RICH. FT DOMAIN 1730 1745 HIS-RICH. FT DOMAIN 2589 2624 SER-RICH. FT DOMAIN 2625 2716 ALA-RICH. FT CONFLICT 61 61 MISSING (IN REF. 1). FT CONFLICT 1169 1169 V -> G (IN REF. 1). FT CONFLICT 1795 1795 M -> T (IN REF. 1). FT CONFLICT 2637 2637 G -> E (IN REF. 1). SQ SEQUENCE 2716 AA; 284063 MW; EFAE76CB51C7C675 CRC64; MNEKIKSPQT QQQQQGGAPA PAATPPSAGA APGAATPPTS GPPTPNNNSN NGSDPSIQQQ QQNVAPHPYG APPPPGSGPG GPPGPDPAAV MHYHHLHQQQ QQHPPPPHMQ QQQHHGGPAP PPPGGAPEHA PGVKEEYTHL PPPHPHPAYG RYHADPNMDP YRYGQPLPGG KPPQQQQPHP QQQPPQQPGP GGSPNRPPQQ RYIPGQPPQG PTPTLNSLLQ SSNPPPPPQH RYANTYDPQQ AAASAAAAAA AQQQQAGGPP PPGHGPPPPQ HQPSPYGGQQ GGWAPPPRPY SPQLGPSQQY RTPPPTNTSR GQSPYPPAHG QNSGSYPSSP QQQQQQQQQQ QQQAGQQPGG PVPGGPPPGT GQQPPQQNTP PTSQYSPYPQ RYPTPPGLPA GGSNHRTAYS THQYPEPNRP WPGGSSPSPG SGHPLPPASP HHVPPLQQQP PPPPHVSAGG PPPSSSPGHA PSPSPQPSQA SPSPHQELIG QNSNDSSSGG AHSGMGSGPP GTPNPQQVMR PTPSPTGSSG SRSMSPAVAQ NHPISRPASN QSSSGGPMQQ PPVGAGGPPP MPPHPGMPGG PPQQQQSQQQ QASNSASSAS NSPQQTPPPA PPPNQGMNNM ATPPPPPQGA AGGGYPMPPH MHGGYKMGGP GQSPGAQGYP PQQPQQYPPG NYPPRPQYPP GAYATGPPPP PTSQAGAGGA NSMPSGAQAG GYPGRGMPNH TGQYPPYQWV PPSPQQTVPG GAPGGAMVGN HVQGKGTPPP PVVGGPPPPQ GSGSPRPLNY LKQHLQHKGG YGGSPTPPQG PQGYGNGPTG MHPGMPMGPP HHMGPPHGPT NMGPPTSTPP QSQMLQGGQP QGQGASGGPE SGGPEHISQD NGISSSGPTG AAGMHAVTSV VTTGPDGTSM DEVSQQSTLS NASAASGEDP QCTTPKSRKN DPYSQSHLAP PSTSPHPVVM HPGGGPGEEY DMSSPPNWPR PAGSPQVFNH VPVPQEPFRS TITTTKKSDS LCKLYEMDDN PDRRGWLDKL RAFMEERRTP ITACPTISKQ PLDLYRLYIY VKERGGFVEV TKSKTWKDIA GLLGIGASSS AAYTLRKHYT KNLLTFECHF DRGDIDPLPI IQQVEAGSKK KTAKAASVPS PGGGHLDAGT TNSTGSSNSQ DSFPAPPGSA PNAAIDGYPG YPGGSPYPVA SGPQPDYATA GQMQRPPSQN NPQTPHPGAA AAVAAGDNIS VSNPFEDPIA AGGGPGSGTG PGPGQGPGPG AASGGAGAVG AVGGGPQPHP PPPHSPHTAA QQAAGQHQQQ HPQHQHPGLP GPPPPQQQQG QQGQQPPPSV GGGPPPAPQQ HGPGQVPPSP QQHVRPAAGA PYPPGGSGYP TPVSRTPGSP YPSQPGAYGQ YGSSDQYNAT GPPGQPFGQG PGQYPPQNRN MYPPYGPEGE APPTGANQYG PYGSRPYSQP PPGGPQPPTQ TVAGGPPAGG APGAPPSSAY PTGRPSQQDY YQPPPDQSPQ PRRHPDFIKD SQPYPGYNAR PQIYGAWQSG TQQYRPQYPS SPAPQNWGGA PPRGAAPPPG APHGPPIQQP AGVAQWDQHR YPPQQGPPPP PQQQQQPQQQ QQQPPYQQVA GPPGQQPPQA PPQWAQMNPG QTAQSGIAPP GSPLRPPSGP GQQNRMPGMP AQQQQSQQQG GVPQPPPQQA SHGGVPSPGL PQVGPGGMVK PPYAMPPPPS QGVGQQVGQG PPGGMMSQKP PPMPGQAMQQ QPLQQQPPSH QHPHPHQHPQ HQHPHQMPPN QTAPGGYGPP GMPGGGAQLV KKELIFPHDS VESTTPVLYR RKRLMKADVC PVDPWRIFMA MRSGLLTECT WALDVLNVLL FDDSTVQFFG ISNLPGLLTL LLEHFQKNLA EMFDERENEE QSALLAEDAD DDADSGTVMC EKLRTSGRQP RCVRSISSYN RRRHYENMDR SGKDGAGNGS DSEDADEGID LGQVRVQPNP EERSLLLSFT PNYTMVTRKG VPVRIQPAEN DIFVDERQKA WDIDTNRLYE QLEPVGSDAW TYGFTEPDPL DGIIDVFKSE IVNIPFARYI RSDKKGRKRT ELASSSRKPE IKTEENSTEE QTFNKKRRLV SGGSSSSGAH AEGKKSKLTS EEFAQPNAEV KKEPGTADSD CRPVDMDIEA PQQRLTNGVA PCSSTPAIFD PRTTAKDEAR VLQRRRDSSF EDECYTRDEA SLHLVSESQD SLARRCIALS NIFRNLTFVP GNETVLAKST RFLAVLGRLL LLNHEHLRRT PKTRNYDREE DTDFSDSCSS LQGEREWWWD YLITIRENML VAMANIAGHL ELSRYDELIA RPLIDGLLHW AVCPSAHGQD PFPSCGPNSV LSPQRLALEA LCKLCVTDAN VDLVIATPPF SRLEKLCAVL TRHLCRNEDQ VLREFSVNLL HYLAAADSAM ARTVALQSPC ISYLVAFIEQ AEQTALGVAN QHGINYLREN PDSMGTSLDM LRRAAGTLLH LAKHPDNRSL FMQQEQRLLG LVMSHILDQQ VALIISRVLY QVSRGTGPIH SVEFRLLQQR QQQQLRPGPA GKQAASAGGS ATVKAETAST ETSSTEAKPA PAATTAVVND ENSNSSQQLP PAATFNDVSN SSTNSNSCGT ASSNQTNNST TNSSHSSSAI SSQSAITVAA PSAAATGAGS ATAAAIASDQ QQVSKVAAAA AAAAALSNAS AAAAAAAAAA AASVGPPTSS SVSAGAAVAQ PAAPPPTNAG TTTAVA // ID OSC_DROME STANDARD; PRT; 118 AA. AC Q23971; Q9VHX8; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Antennal-specific protein OS-C. GN OS-C OR CG3250. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CS-5; TISSUE=Antenna; RX MEDLINE=94266829; PubMed=8206941; RA McKenna M.P., Hekmat-Scafe D.S., Gaines P., Carlson J.R.; RT "Putative Drosophila pheromone-binding proteins expressed in a RT subregion of the olfactory system."; RL J. Biol. Chem. 269:16340-16347(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: ANTENNA. IN THE THIRD ANTENNAL SEGMENT. CC EXPRESSED IN SENCILLA COELOCONICA. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN ADULT BUT NOT IN LARVAL CC OLFACTORY ORGANS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U02545; AAA21357.1; -. DR EMBL; AE003677; AAF54171.1; -. DR FlyBase; FBgn0010401; Os-C. FT DOMAIN 30 51 ASP/GLU-RICH (ACIDIC). SQ SEQUENCE 118 AA; 13015 MW; 5D0CF57C19FC72AC CRC64; MLQMVTQTQA RPQDVITVAG EETEVVIKRE GDDDGDDDDS SSEETVEDSE ESRRRRREVN TDNTPSARAV IPGEQVVPIL LEAILPSVDA AGDRFARSVQ FLKNLTPGSE LFAVEKNE // ID OSKA_DROME STANDARD; PRT; 606 AA. AC P25158; Q9V3P1; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Maternal effect protein oskar. GN OSK OR CG10901. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91300549; PubMed=2070416; RA Kim-Ha J., Smith J.L., Macdonald P.M.; RT "Oskar mRNA is localized to the posterior pole of the Drosophila RT oocyte."; RL Cell 66:23-35(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91300550; PubMed=2070417; RA Ephrussi A., Dickinson L.K., Lehmann R.; RT "Oskar organizes the germ plasm and directs localization of the RT posterior determinant nanos."; RL Cell 66:37-50(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP FUNCTION. RX MEDLINE=92350278; PubMed=1641021; RA Ephrussi A., Lehmann R.; RT "Induction of germ cell formation by oskar."; RL Nature 358:387-392(1992). CC -!- FUNCTION: ORGANIZES THE GERM PLASM AND DIRECTS LOCALIZATION CC OF THE POSTERIOR DETERMINANT NANOS. OSKAR PROTEIN IS REQUIRED TO CC KEEP OSKAR RNA AND STAUFEN PROTEIN AT THE POSTERIOR POLE. CC -!- TISSUE SPECIFICITY: POSTERIOR POLE OF THE OOCYTE. CC -!- MISCELLANEOUS: CAPU, SPIR, AND STAU ARE REQUIRED FOR THE INITIAL CC LOCALIZATION OF OSK TO THE POSTERIOR POLE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63492; AAA28739.1; -. DR EMBL; M65178; AAA28738.1; -. DR EMBL; AE003681; AAF54307.1; -. DR PIR; A40313; A40313. DR FlyBase; FBgn0003015; osk. DR GO; GO:0018994; C:polar granule; IDA. DR GO; GO:0007314; P:oocyte anterior/posterior axis determination; NAS. KW Developmental protein. FT DOMAIN 54 57 POLY-SER. FT DOMAIN 425 439 LEUCINE-ZIPPER (POTENTIAL). SQ SEQUENCE 606 AA; 69284 MW; 9381287153E2D549 CRC64; MAAVTSEFPS KPISYTSTNT SAKTYYLKSV KKRVTTCFQQ LRDKLQSSGS FRKSSSSCLN QIFVRSDFSA CGERFRKIFK SARKTELPEL WKVPLVAHEL TSRQSSQQLQ VVARLFSSTQ ISTKEITYNS NSNTSENNMT IIESNYISVR EEYPDIDSEV RAILLSHAQN GITISSIKSE YRKLTGNPFP LHDNVTDFLL TIPNVTAECS ESGKRIFNLK ASLKNGHLLD MVLNQKERTS DYSSGAPSLE NIPRAPPRYW KNPFKRRALS QLNTSPRTVP KITDEKTKDI ATRPVSLHQM ANEAAESNWC YQDNWKHLNN FYQQASVNAP KMPVPINIYS PDAPEEPINL APPGHQPSCR TQSQKTEPTE NRHLGIFVHP FNGMNIMKRR HEMTPTPTIL TSGTYNDSLL TINSDYDAYL LDFPLMGDDF MLYLARMELK CRFRRHERVL QSGLCVSGLT INGARNRLKR VQLPEGTQII VNIGSVDIMR GKPLVQIEHD FRLLIKEMHN MRLVPILTNL APLGNYCHDK VLCDKIYRFN KFIRSECCHL KVIDIHSCLI NERGVVRFDC FQASPRQVTG SKEPYLFWNK IGRQRVLQVI ETSLEY // ID OSP_DROME STANDARD; PRT; 1553 AA. AC Q27421; Q24231; Q8MSX4; Q9VJS4; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outspread protein. GN OSP OR BG:DS01486.5 OR BG:DS01486.7 OR BG:DS07721.2 OR CG3479. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R., Davis T., RA Doyle C., Galle R., George R., Harris N., Hartzell G., Harvey D., RA Hong L., Houston K., Hoskins R., Johnson G., Martin C., Moshrefi A., RA Palazzolo M., Reese M.G., Spradling A., Tsang G., Wan K., Whitelaw K., RA Celniker S., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 117-271 FROM N.A. RX MEDLINE=83271489; PubMed=6410283; RA Kreitman M.; RT "Nucleotide polymorphism at the alcohol dehydrogenase locus of RT Drosophila melanogaster."; RL Nature 304:412-417(1983). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q27421-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q27421-2; Sequence=VSP_004063, VSP_004064, VSP_004065; CC -!- SIMILARITY: CONTAINS 2 PH DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003410; AAF44880.1; -. DR EMBL; AE003410; AAF44881.1; -. DR EMBL; AE003644; AAF53402.3; -. DR EMBL; AY118512; AAM49881.1; -. DR EMBL; M17837; AAA70211.1; ALT_INIT. DR EMBL; M19547; AAA70209.1; ALT_INIT. DR EMBL; Z00030; CAA77329.1; ALT_INIT. DR FlyBase; FBgn0003016; osp. DR InterPro; IPR001849; PH. DR Pfam; PF00169; PH; 2. DR SMART; SM00233; PH; 2. DR PROSITE; PS50003; PH_DOMAIN; 2. KW Repeat; Alternative splicing. FT DOMAIN 71 177 PH 1. FT DOMAIN 493 592 PH 2. FT VARSPLIC 1 462 Missing (in isoform Short). FT /FTId=VSP_004063. FT VARSPLIC 1373 1373 P -> V (in isoform Short). FT /FTId=VSP_004064. FT VARSPLIC 1374 1553 Missing (in isoform Short). FT /FTId=VSP_004065. SQ SEQUENCE 1553 AA; 174107 MW; 861104687ECB1DE1 CRC64; MSTTTITTTV PAAPSKSAPP TPTTTGAAGA TTNARTADCR KFTPNIFNKS KCSHCFRQRE EHSAAALECN RVSKCGYLFV APDWDFSNPL YRTKRWQRRW FVLYDDGELT YSVDDYPETI PQACVDMTKV LEVTSAVEVT GHPNSIAITA PERVTFVKGT SSEESQWWLN ILAAFPKSKG RHKRSATLPG GQVVGSLRPT SNGDLTLSTK LGNRHSSYHK DTLTSSQSAG NLLSSLDLGP SSTKTAGSPL TTTQSALADD EEDDGVETGE DVDEDEEDET SVPRKSKTVS MGGQDENNRN AGNEITNRVS QPTTCLLIED IRRDEKTIKD IANTITNLSQ QQNKRWSTAV NNALNNQHHF GHHSQYQVTS RDETDFQMSS NSSSTKSQNP ASERPKSLPL ASNSTPAIVS AIVKKIPTVM EQGDKTKPTA RLQLHLKSPK HYQHERGDPD GGCNLDELCV NYMAKTDELR SVGKANSKSS SGQGKPPVKE ESLNAKKGWL MKQDNRTCEW SKHWFTLSGA ALFYYRDPLC EERGVLDGVL DVNSLTSVIP EPAASKQHAF QLTTWDKQRL VLASLSPSSR NSWLAVLRSA AGLPQLDTPP KQTDIEQDFI KAQLQQPSSS PVTPGTPAGP HFSSDEEYRT ASEGGRRDSL DWGSPLSPSP PVLRSCLRNR SLASLHKRSR SSPPSSRRST VDSVASDELP LLVVPEEMQP TESRELKQQC ETLRAEASLR EARMSELLAT LQRTEQQLTA RLQEQQQQLN SELTQAKQSA SDLMHNLGMQ LTESQCQIKQ LEDRLAQGIE ENEGLYKRLR ELQAQDHSGG AALSNLQRHK IKRMDSLSDL TTISDIDPYC LQRDSLAEEY NELRSRFEKA VNEIRAMKRE LKQSQNQYDA LELAQAALQQ KLERRQHEDG AQLQLMAARI QDLTLKYSSS ERQVRALKQK LAKSERRRSL SLKGKEQLEL KLSELQRETV ERKEGTPPES SSSESSSQSP LNAHLLQRLH SLEHVLLGSK ERLEQSLTQL QQIRAGQRTR RSVSPMNDRK DGLRQLERAL AETCVMVSEQ MELTCLQDSC HKCCDLRQRV EKLSALQQQT ETDLQRSEQL LEQRETDLAQ ALEKCASQEQ EQELLLQQRQ ELSEELGRQQ ERCRRLEKRL ELLEREHGKQ LECLREVYHT EHANAADEQS FRKRYQTEIE QLRTLCEKGL SAMETSHKRL TMDLEQKHKM EIERLLAEKE TALAEETQAT LAALDAMRKA HQSEVQREVA RFKQEFLRQV QRGEQMRGDG AKLKEEDLGE LRMEILAFSE KYSIKCVENA ALEEKLHMAN SKLRHFQQMQ QLELRNKQFR AHLASDDPSN DVHFVQGLTS DAREDADCED SEPAPQILGA TATRTTATTT TTATATTTSA APSETESNPD SDRETADSSR APPEKMEQSL FVIPSHMLNS SLVPAANASD QSQRSQLYRD LDGPEDGYEP CYRPFDIFAI YQNRLSYQGL KGSSTFGKSL RKSAAQTSPA SSEITTTTTA PTTDPKKPSH KQMFKTAAVI NIQQQVAQEE KAQ // ID OST4_DROME STANDARD; PRT; 449 AA. AC Q24319; Q24355; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa DE subunit precursor (EC 2.4.1.119) (Oligosaccharyl transferase 48 kDa DE subunit) (DDOST 48 kDa subunit) (OST5OP). GN OST48 OR OST50. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95331618; PubMed=7607543; RA Stagljar I., Te Heesen S., Aebi M.; RT "PCR-mediated cloning and sequencing of the DmOST50 gene, a RT WBP1/AvOST50/OST48 homologue, from Drosophila melanogaster."; RL Gene 158:209-212(1995). RN [2] RP SEQUENCE OF 119-449 FROM N.A. RX MEDLINE=96023949; PubMed=7557364; RA Akhmanova A.S., Bindels P.S.T., Xu J., Miedema K., Kremer H., RA Hennig W.; RT "Structure and expression of histone H3.3 genes in Drosophila RT melanogaster and Drosophila hydei."; RL Genome 38:586-600(1995). CC -!- FUNCTION: ESSENTIAL SUBUNIT OF N-OLIGOSACCHARYL TRANSFERASE ENZYME CC WHICH CATALYZES THE TRANSFER OF A HIGH MANNOSE OLIGOSACCHARIDE TO CC AN ASPARAGINE RESIDUE WITHIN AN ASN-X-SER/THR CONSENSUS MOTIF IN CC NASCENT POLYPEPTIDE CHAINS. CC -!- CATALYTIC ACTIVITY: DOLICHYL DIPHOSPHOOLIGOSACCHARIDE + PROTEIN L- CC ASPARAGINE = DOLICHYL DIPHOSPHATE + A GLYCOPROTEIN WITH THE CC OLIGOSACCHARIDE CHAIN ATTACHED BY GLYCOSYLAMINE LINKAGE TO PROTEIN CC L-ASPARAGINE. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE DDOST 48 KDA SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X81999; CAA57525.1; -. DR EMBL; X81207; CAA57079.1; -. DR PIR; JC4132; JC4132. DR FlyBase; FBgn0014868; Ost48. DR InterPro; IPR005013; DDOST_48kDa. DR Pfam; PF03345; DDOST_48kD; 1. KW Transferase; Endoplasmic reticulum; Transmembrane; Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 449 DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE-- FT PROTEIN GLYCOSYLTRANSFERASE 48 kDa FT SUBUNIT. FT DOMAIN 19 411 LUMENAL (POTENTIAL). FT TRANSMEM 412 431 POTENTIAL. FT DOMAIN 432 449 CYTOPLASMIC (POTENTIAL). FT CONFLICT 148 149 EH -> DD (IN REF. 2). FT CONFLICT 175 176 AA -> R (IN REF. 2). FT CONFLICT 225 226 LL -> VV (IN REF. 2). FT CONFLICT 287 289 RLV -> QVG (IN REF. 2). FT CONFLICT 304 304 P -> T (IN REF. 2). FT CONFLICT 329 330 AR -> RA (IN REF. 2). FT CONFLICT 335 335 D -> A (IN REF. 2). SQ SEQUENCE 449 AA; 49838 MW; 99A465C725D2AFB9 CRC64; MMWKALLIAV LAIAHCQAVL ETDANTLVLL DNLAIRETHS IFFKSLQDRG FKLTYKLADD SSLLLSKYGE YLYKNVIIFA PSVEEFGGDV SVEALAQFVD DGGNVLVAGS EKSGDALREF ASECGFELDE ENAAVIDHLH YDVSDAGEHT TILTSAKNLI QADTIVGKAN RQADAAPLLY RGTGLIADKE NPLVLKLLTA ESTAYSYNPE ASVSDYPHAV GRGTLLIAAL QARNNARVVF SGSLLFFSDE SFTTAVQYAQ SGVFHKLAGN RDVAESISKW VFGETGRLVV ASVQHHKEGE LLPPDQAYTI TDPVVYTIGI EELVQGEWAR FKASDIQLEF VRIDPFVRTY LKQTNTGAYQ AKFKIPDVYG VYQFKVDYNR VGYTHLYSTT QVSVRPLEHT QYERFIPSAF PYYTSAFSMM IGVFVFSFVF LHFKDEPVGR AAKEDKKSQ // ID OTE_DROME STANDARD; PRT; 406 AA. AC P20240; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 01-MAY-1991 (Rel. 18, Last annotation update) DE Otefin. GN OTE. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90243644; PubMed=2186029; RA Padan R., Nainudel-Epszteyn S., Goitein R., Fainsod A., Gruenbaum Y.; RT "Isolation and characterization of the Drosophila nuclear envelope RT otefin cDNA."; RL J. Biol. Chem. 265:7808-7813(1990). CC -!- FUNCTION: NUCLEAR ENVELOPE PROTEIN. CC -!- SUBCELLULAR LOCATION: INNER NUCLEAR MEMBRANE-ASSOCIATED. IT IS CC A COMPONENT OF THE SPINDLE ENVELOPE DURING EARLY MITOTIC CYCLES. CC -!- DEVELOPMENTAL STAGE: THROUGHOUT THE DEVELOPMENTAL STAGES OF THE CC FRUIT FLY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17495; CAA35530.1; -. DR PIR; A35360; A35360. DR FlyBase; FBgn0003022; Ote. DR InterPro; IPR003887; LEM. KW Nuclear protein; Transmembrane. FT DOMAIN 74 81 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 133 137 SER/THR-RICH. FT DOMAIN 210 215 SER/THR-RICH. FT DOMAIN 250 254 SER/THR-RICH. FT DOMAIN 289 293 SER/THR-RICH. FT TRANSMEM 389 406 POTENTIAL. SQ SEQUENCE 406 AA; 44658 MW; 581BC0BFF6B956B1 CRC64; MLAQGLPNIP VTDSSRKVLV KRLRASIGGQ ASPAASPKKT NRRETLAPAP GAPSAPAAAS TPVDKLDGNK VAPATKARRT ITAAEAKEPV RRLPEEAVRR RPEEADRLRP EEPVAARKPT TASAAQPVQT RRSSTSSGSE RKVVEPLRKP ETIVEQPASS KRADREEKYL KVNSLIVLES DEEEDEQLVQ AADLVEQEHA ARQKTTKLAS SGTTTYEYKS KVVEPPRRQV YEATASPVLP PSVPSARAQT TSSTRSYDYA SNPAPGRYSS FVRHAAQGYV TAEAPPVASY SSSYKRTYAN ELSDDTDSKE DQYESTFARN LARLRSERIG DRISPYSRRT LASGNAGSGS LGYEPRARRS LRPNDNSVSE AFNRWLNSLE QKYHIKSKLF IVLVVLLLIG VYYIFY // ID OTP_DROME STANDARD; PRT; 264 AA. AC P56672; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeobox protein orthopedia. GN OTP OR CG10036. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94318283; PubMed=7913821; RA Simeone A., D'Apice M.R., Nigro V., Casanova J., Graziani F., RA Acampora D., Avantaggiato V.; RT "Orthopedia, a novel homeobox-containing gene expressed in the RT developing CNS of both mouse and Drosophila."; RL Neuron 13:83-101(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: APPEARS TO BE INVOLVED IN THE DEVELOPMENT OF THE CENTRAL CC NERVOUS SYSTEM SPECIFYING REGIONAL IDENTITIES IN THE DEVELOPMENT CC OF THE FOREBRAIN AND SPINAL CORD. CAN RECOGNIZE, BIND AND CC TRANSACTIVATE THE NP TARGET SEQUENCE PRESENT IN THE ENGRAILED GENE CC REGULATORY REGION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: FIRST APPEARS AT GASTRULATION IN THE CC ECTODERMAL PROCTODEUM AND LATER IN THE HINDGUT, ANAL PLATE, AND CC ALONG THE CNS. CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. BICOID CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- CAUTION: IT IS UNCERTAIN IF MET-1 IS THE INITIATOR OR IF THE CC SEQUENCE STARTS FURTHER UPSTREAM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003452; AAF46636.3; -. DR HSSP; P06601; 1FJL. DR FlyBase; FBgn0015524; otp. DR GO; GO:0003677; F:DNA binding; IDA. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DNA_BIND 6 65 HOMEOBOX. FT DOMAIN 179 184 POLY-GLN. FT DOMAIN 187 192 POLY-GLN. FT DOMAIN 206 210 POLY-GLN. SQ SEQUENCE 264 AA; 29449 MW; E839FE5A5FF8BA86 CRC64; MQQQDQKRHR TRFTPAQLNE LERCFSKTHY PDIFMREEIA MRIGLTESRV QVWFQNRRAK WKKRKKTTNV FRTPGALLPS HGLPPFGANI TNIAMGDGLC GTGMFGGDRW SVGVNPMTAG DSMMYQHSVG GVSCGPSGSP SATTPPNMNS CSSVTPPPLS AQPNSSQNEL NGEPMPLHQQ QQQQTHQHQQ QQTHQHHPMA PPTPTQQQQQ LPQSMQSPSD GANDTLHSIA ALRRRASELN AIPSYLQMAP HNYEHYNSNS NSVY // ID OTU_DROME STANDARD; PRT; 853 AA. AC P10383; Q8SYF4; Q9GYD8; Q9TWA9; Q9W3E4; DT 01-MAR-1989 (Rel. 10, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ovarian tumor locus protein. GN OTU OR CG12743. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Canton-S; TISSUE=Ovary; RX MEDLINE=89263747; PubMed=2498839; RA Champe M.A., Laird C.D.; RT "Nucleotide sequence of a cDNA from the putative ovarian tumor locus RT of Drosophila melanogaster."; RL Nucleic Acids Res. 17:3304-3304(1989). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Canton-S; RX MEDLINE=90066528; PubMed=2511440; RA Steinhauer W.R., Walsh R.C., Kalfayan L.J.; RT "Sequence and structure of the Drosophila melanogaster ovarian tumor RT gene and generation of an antibody specific for the ovarian tumor RT protein."; RL Mol. Cell. Biol. 9:5726-5732(1989). RN [3] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND ALTERNATIVE RP SPLICING. RC STRAIN=Canton-S; RX MEDLINE=92146958; PubMed=1737618; RA Steinhauer W.R., Kalfayan L.J.; RT "A specific ovarian tumor protein isoform is required for efficient RT differentiation of germ cells in Drosophila oogenesis."; RL Genes Dev. 6:233-243(1992). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP ACTIVATION BY STIL. RX MEDLINE=99203441; PubMed=10101125; RA Sahut-Barnola I., Pauli D.; RT "The Drosophila gene stand still encodes a germline chromatin- RT associated protein that controls the transcription of the ovarian RT tumor gene."; RL Development 126:1917-1926(1999). CC -!- FUNCTION: ESSENTIAL FOR FEMALE FERTILITY; GERM CELL DIVISION AND CC DIFFERENTIATION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long; CC IsoId=P10383-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; Synonyms=Short; CC IsoId=P10383-2; Sequence=VSP_004354; CC -!- TISSUE SPECIFICITY: EXPRESSED IN BOTH OOCYTE AND NURSE CELLS OF CC THE GERMARIUM. CC -!- INDUCTION: EXPRESSION IS COOPERATIVELY ACTIVATED BY OVO AND STIL. CC -!- SIMILARITY: CONTAINS 1 OTU DOMAIN. CC -!- SIMILARITY: CONTAINS 1 TUDOR DOMAIN. CC -!- CAUTION: REF.6 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 308. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13693; CAA31983.1; -. DR EMBL; M30825; AAA28740.1; -. DR EMBL; M30825; AAF97987.1; -. DR EMBL; AE003444; AAF46384.1; -. DR EMBL; AY071588; AAL49210.1; ALT_FRAME. DR PIR; S04085; S04085. DR FlyBase; FBgn0003023; otu. DR InterPro; IPR003323; OTU. DR InterPro; IPR002999; Tudor. DR Pfam; PF02338; OTU; 1. DR SMART; SM00333; TUDOR; 1. DR PROSITE; PS50802; OTU; 1. DR PROSITE; PS50304; TUDOR; 1. KW Alternative splicing. FT DOMAIN 29 150 OTU. FT DOMAIN 336 396 TUDOR. FT VARSPLIC 340 381 Missing (in isoform 2). FT /FTId=VSP_004354. FT CONFLICT 300 300 K -> Q (IN REF. 1). FT CONFLICT 831 831 T -> P (IN REF. 3). SQ SEQUENCE 853 AA; 97452 MW; D7C1F9453377B075 CRC64; MDMQVQRPIT SGSRQAPDPY DQYLESRGLY RKHTARDASS LFRVIAEQMY DTQMLHYEIR LECVRFMTLK RRIFEKEIPG DFDSYMQDMS KPKTYGTMTE LRAMSCLYRR NVILYEPYNM GTSVVFNRRY AENFRVFFNN ENHFDSVYDV EYIERAAICQ SIAFKLLYQK LFKLPDVSFA VEIMLHPHTF NWDRFNVEFD DKGYMVRIHC TDGRVFKLDL PGDTNCILEN YKLCNFHSTN GNQSINARKG GRLEIKNQEE RKASGSSGHE PNDLLPMCPN RLESCVRQLL DDGISPFPYK VAKSMDPYMY RNIEFDCWND MRKEAKLYNV YINDYNFKVG AKCKVELPNE TEMYTCHVQN ISKDKNYCHV FVERIGKEIV VPYESLHPLP PDEYRPWSLP FRYHRQMPRL PLPKYAGKAN KSSKWKKNKL FEMDQYFEHS KCDLMPYMPV DNCYQGVHIQ DDEQRDHNDP EQNDQNPTTE QRDREEPQAQ KQHQRTKASR VQPQNSSSSQ NQEVSGSAAP PPTQYMNYVP MIPSRPGHLP PPWPASPMAI AEEFPFPISG TPHPPPTEGC VYMPFGGYGP PPPGAVALSG PHPFMPLPSP PLNVTGIGEP RRSLHPNGED LPVDMVTLRY FYNMGVDLHW RMSHHTPPDE LGMFGYHQQN NTDQQAGRTV VIGATEDNLT AVESTPPPSP EVANATEQSP LEKSAYAKRN LNSVKVRGKR PEQLQDIKDS LGPAAFLPTP TPSPSSNGSQ FSFYTTPSPH HHLITPPRLL QPPPPPPIFY HKAGPPQLGG AAQGQTPYAW GMPAPVVSPY EVINNYNMDP SAQPQQQQPA TLQPAPLSVQ SQPAAVYAAT RHH // ID OVO_DROME STANDARD; PRT; 1028 AA. AC P51521; Q9XZU4; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ovo protein (Shaven baby protein). GN OVO OR SVB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=95021209; PubMed=7935398; RA Garfinkel M.D., Wang J., Liang Y., Mahowald A.P.; RT "Multiple products from the shavenbaby-ovo gene region of Drosophila RT melanogaster: relationship to genetic complexity."; RL Mol. Cell. Biol. 14:6809-6818(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91293102; PubMed=1712294; RA Mevel-Ninio M.T.M., Terracol R., Kafatos F.C.; RT "The ovo gene of Drosophila encodes a zinc finger protein required RT for female germ line development."; RL EMBO J. 10:2259-2266(1991). CC -!- FUNCTION: REQUIRED FOR SURVIVAL AND DIFFERENTIATION OF FEMALE GERM CC LINE CELLS. PLAYS A ROLE IN GERM LINE SEX DETERMINATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: FIRST APPEARS IN THE GERMARIUM AND CC ACCUMULATES IN NURSE CELLS DURING OOGENESIS. STORED IN THE EGG, CC BUT IS RAPIDLY LOST IN THE EMBRYOS EXCEPT FOR ITS CONTINUED CC PRESENCE IN THE GERM LINE PRECURSOR POLE CELLS. CC -!- SIMILARITY: CONTAINS 4 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11383; AAB60216.1; -. DR EMBL; X59772; CAB36921.1; ALT_SEQ. DR PIR; A56038; A56038. DR HSSP; P07248; 2ADR. DR TRANSFAC; T00669; -. DR FlyBase; FBgn0003028; ovo. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 3. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. KW Zinc-finger; Metal-binding; DNA-binding; Repeat; Nuclear protein; KW Transcription regulation. FT DOMAIN 62 66 POLY-ALA. FT DOMAIN 72 77 POLY-GLY. FT DOMAIN 80 85 POLY-GLY. FT DOMAIN 98 108 POLY-GLY. FT DOMAIN 144 152 POLY-HIS. FT DOMAIN 153 159 POLY-ASN. FT DOMAIN 336 339 POLY-GLN. FT DOMAIN 347 353 POLY-GLN. FT DOMAIN 357 361 POLY-GLN. FT DOMAIN 410 414 POLY-GLN. FT DOMAIN 418 422 POLY-GLN. FT DOMAIN 426 432 POLY-GLN. FT DOMAIN 445 453 POLY-GLN. FT DOMAIN 456 459 POLY-GLN. FT DOMAIN 466 474 POLY-GLN. FT DOMAIN 497 517 POLY-ALA. FT DOMAIN 524 529 POLY-SER. FT DOMAIN 549 558 POLY-ALA. FT DOMAIN 639 651 POLY-ALA. FT DOMAIN 717 725 POLY-ALA. FT DOMAIN 797 802 POLY-GLN. FT DOMAIN 820 823 POLY-GLN. FT DOMAIN 826 832 POLY-GLN. FT ZN_FING 874 896 C2H2-TYPE 1. FT ZN_FING 902 924 C2H2-TYPE 2. FT ZN_FING 930 953 C2H2-TYPE 3. FT ZN_FING 969 992 C2H2-TYPE 4. FT CONFLICT 647 647 A -> R (IN REF. 2). SQ SEQUENCE 1028 AA; 110620 MW; D7068BB2BC0F6F77 CRC64; MGGGRDGRGN YGPNSPPTGA LPPFYESLKS GQQSTASNNT GQSPGANHSH FNANPANFLQ NAAAAAYIMS AGSGGGGCTG NGGGGASGPG GGPSANSGGG GGGGGGNGYI NCGGVGGPNN SLDGNNLLNF ASVSNYNESN SKFHNHHHHH QHNNNNNNNG GQTSMMGHPF YGGNPSAYGI ILKDEPDIEY DEAKIDIGTF AQNIIQATMG SSGQFNASAY EDAIMSDLAS SGQCPNGAVD PLQFTATLML SSQTDHLLEQ LSDAVDLSSF LQRSCVDDEE STSPRQDFEL VSTPSLTPDS VTPVEQHNTN TTQLDVLHEN LLTQLTHNIV RGGSNQQQQH HQQHGVQQQQ QQQHSVQQQQ QHNVQQQHGV QQQHVQQQPP PSYQHATRGL MMQQQPQHGG YQQQAAIMSQ QQQQLLSQQQ QQSHHQQQQQ QQHAAAYQQH NIYAQQQQQQ QQQHHQQQQH HHFHHQQQQQ PQPQSHHSHH HGHGHDNSNM SLPSPTAAAA AAAAAAAAAA AAAAAAAHLQ RPMSSSSSSG GTNSSNSSGG SSNSPLLDAN AAARAAAALL DTKPLIQSVS NPIGQPLNTQ SQQQKQGQQI TLMKTTRYTE FVEMVSMDVT VKPELFSELK PEMTEITAEE LTLEAETTAA AAAAAAAAAA ATTTSATEGT QVLAAAPAPL SSGRKLRGRA KAVAYGSTMI TLISTLKSSP EVPATKTVHR TTLRSLATAA AATAAGLLAP SPTVSVLNES KVLQRRLGLP PDLQLEFVNG GHGIKNPLAV ENAHGGHHRI RNIDCIDDLS KHGHHSQHQQ QQGSPQQQNM QQSVQQQSVQ QQQSLQQQQQ QQHHQHHSNS SASSNASSHG SAEALCMGSS GGANEDSSSG NNKFVCRVCM KTFSLQRLLN RHMKCHSDIK RYLCTFCGKG FNDTFDLKRH TRTHTGVRPY KCNLCEKSFT QRCSLESHCQ KVHSVQHQYA YKERRAKMYV CEECGHTTCE PEVHYLHLKN NHPFSPALLK FYDKRHFKFT NSQFANNLLG QLPMPVHN // ID P2A_DROME STANDARD; PRT; 309 AA. AC P23696; Q9VLW4; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase PP2A (EC 3.1.3.16) (Microtubule DE star protein). GN MTS OR PP2A OR PP2A-28D OR CG7109. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91085575; PubMed=2175718; RA Orgad S., Brewis N.D., Alphey L., Axton J.M., Dudai Y., Cohen P.T.W.; RT "The structure of protein phosphatase 2A is as highly conserved as RT that of protein phosphatase 1."; RL FEBS Lett. 275:44-48(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON ION AND 1 MANGANESE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-2A CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55199; CAA38984.1; -. DR EMBL; X78577; CAA55315.1; -. DR EMBL; AE003619; AAF52567.2; -. DR EMBL; AY058571; AAL13800.1; -. DR PIR; S12961; S12961. DR HSSP; P08129; 1FJM. DR FlyBase; FBgn0004177; mts. DR GO; GO:0008600; F:protein phosphatase type 2A, intrinsic cata...; IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0008546; P:microtubule/chromatin interaction; IMP. DR GO; GO:0007067; P:mitosis; IMP. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IMP. DR GO; GO:0007465; P:R7 cell fate commitment; IGI. DR GO; GO:0007051; P:spindle assembly; IMP. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Metal-binding; Iron; Manganese. FT METAL 57 57 IRON (BY SIMILARITY). FT METAL 59 59 IRON (BY SIMILARITY). FT METAL 85 85 IRON AND MANGANESE (BY SIMILARITY). FT METAL 117 117 MANGANESE (BY SIMILARITY). FT ACT_SITE 118 118 GENERAL ACID (BY SIMILARITY). FT METAL 167 167 MANGANESE (BY SIMILARITY). FT METAL 241 241 MANGANESE (BY SIMILARITY). SQ SEQUENCE 309 AA; 35469 MW; 6F1E2486A514FBAF CRC64; MEDKATTKDL DQWIEQLNEC NQLTETQVRT LCDKAKEILS KESNVQEVKC PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDSLDHI RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNN TNGLTLVSRA HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAALMELDD SLKFSFLQFD PAPRRGEPHV TRRTPDYFL // ID P2B1_DROME STANDARD; PRT; 577 AA. AC P48456; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase 2B catalytic subunit 1 DE (EC 3.1.3.16) (Calmodulin-dependent calcineurin A1 subunit). GN CANA1 OR CNA1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93054551; PubMed=1331060; RA Guerini D., Montell C., Klee C.B.; RT "Molecular cloning and characterization of the genes encoding the two RT subunits of Drosophila melanogaster calcineurin."; RL J. Biol. Chem. 267:22542-22549(1992). CC -!- FUNCTION: CALCIUM-DEPENDENT, CALMODULIN-STIMULATED PROTEIN CC PHOSPHATASE. THIS SUBUNIT MAY HAVE A ROLE IN THE CALMODULIN CC ACTIVATION OF CALCINEURIN. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON(III) ION AND 1 ZINC ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SUBUNIT: COMPOSED OF TWO COMPONENTS (A AND B), THE A COMPONENT IS CC THE CATALYTIC SUBUNIT AND THE B COMPONENT CONFERS CALCIUM CC SENSITIVITY. CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-2B CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97012; AAA28410.1; -. DR PIR; B44307; B44307. DR HSSP; P48452; 1TCO. DR FlyBase; FBgn0010015; CanA1. DR GO; GO:0008021; C:synaptic vesicle; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016083; P:synaptic vesicle fusion; NAS. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Calmodulin-binding; Metal-binding; Iron; Zinc; KW Multigene family. FT METAL 85 85 IRON (BY SIMILARITY). FT METAL 87 87 IRON (BY SIMILARITY). FT METAL 113 113 IRON AND ZINC (BY SIMILARITY). FT METAL 145 145 ZINC (BY SIMILARITY). FT ACT_SITE 146 146 GENERAL ACID (BY SIMILARITY). FT METAL 194 194 ZINC (BY SIMILARITY). FT METAL 276 276 ZINC (BY SIMILARITY). SQ SEQUENCE 577 AA; 64587 MW; EC24E81265C6BD1B CRC64; MQYTKTRERM VDDVPLPPTH KLTMSEVYDD PKTGKPNFDA LRQHFLLEGR IEEAVALRII TEGAALLREE KNMIDVEAPI TVCGDIHGQF FDLVKLFEVG GPPATTRYLF LGDYVDRGYF SIECVLYLWS LKITYPTTLS LLRGNHECRH LTEYFTFKQE CIIKYSESIY DACMEAFDCL PLAALLNQQF LCIHGGLSPE IFTLDDIKTL NRFREPPAYG PMCDLLWSDP LEDFGNEKTN EFFSHNSVRG CSYFFSYSAC CEFLQKNNLL SIVRAHEAQD AGYRMYRKNQ VTGFPSLITI FSAPNYLDVY NNKAAVLKYE NNVMNIRQFN CSPHPYWLPN FMDVFTWSLP FVGEKVTEML VNILNICSDD ELVAGPDDEL EEELRKKIVL VPANASNNNN NNNTPSKPAS MSAVRKEIIR NKIRAIGKMS RVFSILREES ESVLQLKGLT PTGALPVGAL SGGRDSLKEA LQGLTASSHI HSFAEAKGLD AVNERMPPRR PLLMSASSSS ITTVTRSSSS SSNNNNNNSN TSSTTTTKDI SNTSSNDTAT VTKTSRTTVK SATTSNVRAG FTAKKFS // ID P2B2_DROME STANDARD; PRT; 560 AA. AC Q27889; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase 2B catalytic subunit 2, DE (EC 3.1.3.16) (Calmodulin-dependent calcineurin A2 subunit). GN PP2B-14D. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Eye imaginal disk; RX MEDLINE=94148068; PubMed=8313960; RA Brown L., Chen M.X., Cohen P.T.W.; RT "Identification of a cDNA encoding a Drosophila calcium/calmodulin RT regulated protein phosphatase, which has its most abundant expression RT in the early embryo."; RL FEBS Lett. 339:124-128(1994). CC -!- FUNCTION: CALCIUM-DEPENDENT, CALMODULIN-STIMULATED PROTEIN CC PHOSPHATASE. THIS SUBUNIT MAY HAVE A ROLE IN THE CALMODULIN CC ACTIVATION OF CALCINEURIN. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON(III) ION AND 1 ZINC ION PER SUBUNIT (BY CC SIMILARITY). CC -!- TISSUE SPECIFICITY: ABUNDANTLY EXPRESSED IN EARLY EMBRYOS AND CC ADULT FEMALES. CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-2B CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X77768; CAA54807.1; -. DR EMBL; S68806; AAB29893.1; -. DR PIR; S41743; S41743. DR HSSP; Q08209; 1AUI. DR FlyBase; FBgn0011826; Pp2B-14D. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Calmodulin-binding; Metal-binding; Iron; Zinc; KW Multigene family. FT DOMAIN 36 40 POLY-ASN. FT METAL 156 156 IRON (BY SIMILARITY). FT METAL 158 158 IRON (BY SIMILARITY). FT METAL 184 184 IRON AND ZINC (BY SIMILARITY). FT METAL 216 216 ZINC (BY SIMILARITY). FT ACT_SITE 217 217 GENERAL ACID (BY SIMILARITY). FT METAL 265 265 ZINC (BY SIMILARITY). FT METAL 338 338 ZINC (BY SIMILARITY). SQ SEQUENCE 560 AA; 61986 MW; 45F81D43ABD289CA CRC64; MSSNNQSSSV AQAATSARTV SAGSAEATDA NSTASNNNNN SSSTAAAGNN SDNSSPTTGT GTGASTGKLH GGHTAVNTKE RVVDSVPFPP SHKLTLAEVF DQRTGKPNHE LLKQHFILEG RIEEAPALKI IQEGAALLRQ EKTMIDIEAP VTVCGDIHGQ FYDLMKLFEV GGSPQSTKYL FLGDYVDRGY FSIECVLYLW SLKITYPQTL FLLRGNHECR HLTEYFTFKQ ECKIKYSERV YDACMDAFDC LPLAALMNQQ FLCVHGGLSP EIHELEDIRR LDRFKEPPAF GPMCDLLWSD PLEDFGNEKN SDFYTHNSVR GCCYFLQNNN LLSIIRAHEA QDAGYRMYRK SQTTGFPSLI TIFSAPNYLD VYNNKAAVLK YENNVMNIRQ FNCSPHPIWL PNFMDVFTWS LPFVGEKVTE MLVNVLNICS DDELMTEESE EPLSDDEAAV RKEVIRNKIR AIGKMARVFS VLREESESVL QKGLTPTGAL PLGALSGGKQ SLKNAMQGFS PNHKITSFAE AKGLDAVNER MPPRRDQPPT PSEDPNQHSQ QGGKNGAGHG // ID PABP_DROME STANDARD; PRT; 632 AA. AC P21187; DT 01-MAY-1991 (Rel. 18, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Polyadenylate-binding protein (Poly(A)-binding protein) (PABP). GN PABP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91099679; PubMed=2125288; RA Lefrere V., Vincent A., Amalric F.; RT "Drosophila melanogaster poly(A)-binding protein: cDNA cloning RT reveals an unusually long 3'-untranslated region of the mRNA, also RT present in other eukaryotic species."; RL Gene 96:219-225(1990). RN [2] RP REVISIONS. RX MEDLINE=93246264; PubMed=8482550; RA Lefrere V., Vincent A., Amalric F.; RT "Drosophila melanogaster poly(A)-binding protein: cDNA cloning RT reveals an unusually long 3'-untranslated region of the mRNA, also RT present in other eukaryotic species."; RL Gene 126:295-296(1993). CC -!- FUNCTION: BINDS THE POLY(A) TAIL OF MRNA. CC -!- SIMILARITY: CONTAINS 4 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L05109; AAA70421.1; -. DR PIR; S30887; S30887. DR HSSP; P11940; 1CVJ. DR FlyBase; FBgn0003031; pAbp. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0008143; F:poly(A) binding; NAS. DR InterPro; IPR002004; PABP/HECT. DR InterPro; IPR006515; PARP_1234. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00658; PABP; 1. DR Pfam; PF00076; rrm; 4. DR SMART; SM00517; PolyA; 1. DR SMART; SM00360; RRM; 4. DR TIGRFAMs; TIGR01628; PABP-1234; 1. DR PROSITE; PS50102; RRM; 4. DR PROSITE; PS00030; RRM_RNP_1; 3. KW RNA-binding; Nuclear protein; Repeat. FT DOMAIN 2 80 RNA-BINDING (RRM) 1. FT DOMAIN 90 167 RNA-BINDING (RRM) 2. FT DOMAIN 181 259 RNA-BINDING (RRM) 3. FT DOMAIN 285 362 RNA-BINDING (RRM) 4. SQ SEQUENCE 632 AA; 69702 MW; 8D90AEC8A75127FD CRC64; MASLYVGDLP QDVNESGLFD KFSSAGPVLS IRVCRDVITR RSLGYAYVNF QQPADAERAL DTMNFDLVRN KPIRIMWSQR DPSLRRSGVG NVFIKNLDRA IDNKAIYDTF SAFGNILSCK VATDEKGNSK GYGFVHFETE EAANTSIDKV NGMLLNGKKV YVGKFIPRKE QELGEKAKLF TNVYVKNFTE DFDDEKLKEF FEPYGKITSY KVMSKEDGKS KGFGFVAFET TEAAEAAVQA LNGKDMGEGK SLYVARAQKK AERQQELKRK FEELKQKRHE SVFGVNLYVK NLDDTIDDDR LRIAFSPYGN ITSAKVMTDE EGRSKGFGFV CFNPESEATC AVTELNGRVV GSKPLYVALA QRKEERKADL ASQYMRHMTG MRMQQLGQIY QPNAASGFFV PTLPSNQRFF GSQVATQMRN TPRWVPQVRP PAAIQGVQAG AAAAGGFQGT AGAVPTQFRS AAAGARGAQP QVQGTHAAAA AANNMRNTGA RAITGQQTAA PNMQIPGAQI AGGAQQRTSN YKYTSNMRNP PVPQLHQTQP IPQQLQGKNS EKLIASLLAN AKPQEQKQIL GERLYPMIEH MHANLAGKIT GMLLEIENSE LLHMIEDQEA LKAKVEEAVA VLQVHRVTEP AN // ID PANG_DROME STANDARD; PRT; 751 AA. AC P91943; O02548; Q9V4B0; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein pangolin. GN PAN OR DTCF OR CG17964. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97192098; PubMed=9039917; RA Brunner E., Peter O., Schweizer L., Basler K.; RT "Pangolin encodes a Lef-1 homologue that acts downstream of Armadillo RT to transduce the Wingless signal in Drosophila."; RL Nature 385:829-833(1997). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=97236499; PubMed=9118222; RA van de Wetering M., Cavallo R.A., Dooijes D., van Beest M., van Es J., RA Loureiro J., Ypma A., Hursh D., Jones T., Bejsovec A., Peifer M., RA Mortin M., Clevers H.; RT "Armadillo coactivates transcription driven by the product of the RT Drosophila segment polarity gene dTCF."; RL Cell 88:789-799(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP CHARACTERIZATION. RX MEDLINE=98454907; PubMed=9783586; RA Cavallo R.A., Cox R.T., Moline M.M., Roose J., Polevoy G.A., RA Clevers H., Peifer M., Bejsovec A.; RT "Drosophila Tcf and Groucho interact to repress Wingless signalling RT activity."; RL Nature 395:604-608(1998). CC -!- FUNCTION: SEGMENT POLARITY PROTEIN, FUNCTIONS TOGETHER WITH ARM TO CC TRANSDUCE THE WINGLESS (WG) SIGNAL. ACTS AS A TRANSCRIPTIONAL CC ACTIVATOR, BUT IN THE ABSENCE OF ARM, IT BINDS TO GRO AND ACTS AS CC A TRANSCRIPTIONAL REPRESSOR OF WG-RESPONSIVE GENES. CC -!- SUBUNIT: BINDS TO THE BETA-CATENIN HOMOLOG ARM OR TO GRO. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE TCF/LEF FAMILY. CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U88538; AAC47464.1; -. DR EMBL; Y09125; CAA70343.1; -. DR EMBL; AE003845; AAN06544.2; -. DR HSSP; P27782; 2LEF. DR TRANSFAC; T02922; -. DR FlyBase; FBgn0019664; pan. DR GO; GO:0045810; P:negative regulation of frizzled signaling p...; NAS. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW Transcription regulation; Activator; Repressor; Developmental protein; KW Segmentation polarity protein; Trans-acting factor; Nuclear protein; KW DNA-binding; Wnt signaling pathway. FT DOMAIN 1 53 BETA-CATENIN BINDING (BY SIMILARITY). FT DNA_BIND 273 341 HMG BOX. FT DOMAIN 351 357 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 351 357 POLY-LYS. SQ SEQUENCE 751 AA; 81892 MW; 1C6E5A0B36017143 CRC64; MPHTHSRHGS SGDDLCSTDE VKIFKDEGDR EDEKISSENL LVEEKSSLID LTESEEKGHK ISRPDHSPVF NKLDTHAPSF NMGYLVSPYS YANGSPSGLP VTMANKIGLP PFFCHNADPL STPPPAHCGI PPYQLDPKMG LTRPALYPFA GGQYPYPMLS SDMSQVASWH TPSVYSASSF RTPYPSSLPI NTTLASDFPF RFSPSLLPSV HATSHHVINA HSAIVGVSSK QECGVQDPTT NNRYPRNLEA KHTSNAQSNE SKETTNDKKK PHIKKPLNAF MLYMKEMRAK VVAECTLKES AAINQILGRR WHELSREEQS KYYEKARQER QLHMELYPGW SARDNYGYVS KKKKRKKDRS TTDSGGNNMK KCRARFGLDQ QSQWCKPCRR KKKCIRYMEA LNGNGPAEDG SCFDEHGSQL SDDDEDDYDD DKLGGSCGSA DETNKIEDED SESLNQSMPS PGCLSGLSSL QSPSTTMSLA SPLNMNANSA TNVIFPASSN ALLIVGADQP TAQQRPTLVS TSGSSSGSTS SISTTPNTSS TVSPVTCMTG PCLGSSQERA MMLGNRFSHL GMGLSPPVVS TSTSKSEPFF KPHPTVCNNP IFALPSIGNC SLNISSMPNT SRNPIGANPR DINNPLSINQ LTKRREYKNV ELIEASESKT IVAHAATSII QHVAVNGYHA NHSLLNSNLG HLHHQLNNRT ENPNRSEQTM LSVSNHSVNS SECHKESDSQ AIVSSNPPNA GSSDNGVISV S // ID PATC_DROME STANDARD; PRT; 1286 AA. AC P18502; Q9V4W3; DT 01-NOV-1990 (Rel. 16, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Patched protein (Hedgehog receptor). GN PTC OR CG2411. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90058658; PubMed=2582494; RA Hooper J.E., Scott M.P.; RT "The Drosophila patched gene encodes a putative membrane protein RT required for segmental patterning."; RL Cell 59:751-765(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90015164; PubMed=2797178; RA Nakano Y., Guerrero I., Hidalgo A., Taylor A., Whittle J.R.S., RA Ingham P.W.; RT "A protein with several possible membrane-spanning domains encoded by RT the Drosophila segment polarity gene patched."; RL Nature 341:508-513(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: SEGMENTATION POLARITY PROTEIN. ACTS AS A RECEPTOR FOR CC THE HEDGEHOG PROTEIN (HH). ASSOCIATES WITH THE SMOOTHENED PROTEIN CC (SMO) TO TRANSDUCE THE HEDGEHOG SIGNAL LEADING TO THE ACTIVATION CC OF WINGLESS, DECAPENTAPLEGIC AND PATCHED ITSELF. PARTICIPATES IN CC CELL INTERACTIONS THAT ESTABLISH PATTERN WITHIN THE SEGMENT AND CC THE IMAGINAL DISKS DURING DEVELOPMENT. IN THE ABSENCE OF HH, CC REPRESSES THE CONSTITUTIVE SIGNALING ACTIVITY OF SMO THROUGH FUSED CC (FU). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE PATCHED FAMILY. CC -!- SIMILARITY: CONTAINS 1 STEROL-SENSING (SSD) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28999; AAA28696.1; -. DR EMBL; M28418; AAA28696.1; JOINED. DR EMBL; X17558; CAA35591.1; -. DR EMBL; AE003836; AAF59062.1; -. DR PIR; S06119; S06119. DR FlyBase; FBgn0003892; ptc. DR GO; GO:0007455; P:eye-antennal disc metamorphosis; IMP. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP. DR InterPro; IPR003392; Patched. DR InterPro; IPR004766; Patched_rec. DR InterPro; IPR000731; SSD_5TM. DR Pfam; PF02460; Patched; 1. DR TIGRFAMs; TIGR00918; 2A060602; 1. DR PROSITE; PS50156; SSD; 1. KW Transmembrane; Developmental protein; Segmentation polarity protein; KW Glycoprotein; Receptor. FT DOMAIN 1 76 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 77 92 POTENTIAL. FT DOMAIN 93 427 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 428 448 POTENTIAL. FT DOMAIN 449 465 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 466 486 POTENTIAL. FT DOMAIN 487 492 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 493 511 POTENTIAL. FT DOMAIN 512 532 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 533 553 POTENTIAL. FT DOMAIN 554 562 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 563 583 POTENTIAL. FT DOMAIN 584 677 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 678 699 POTENTIAL. FT DOMAIN 700 931 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 932 952 POTENTIAL. FT DOMAIN 953 955 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 956 976 POTENTIAL. FT DOMAIN 977 1007 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1008 1028 POTENTIAL. FT DOMAIN 1029 1056 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1057 1077 POTENTIAL. FT DOMAIN 1078 1082 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1083 1103 POTENTIAL. FT DOMAIN 1104 1286 CYTOPLASMIC (POTENTIAL). FT DOMAIN 428 583 SSD. FT DOMAIN 1227 1232 POLY-PRO. FT CARBOHYD 142 142 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 298 298 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 335 335 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 388 388 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 807 807 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 111 111 R -> G (IN REF. 2). FT CONFLICT 274 274 G -> A (IN REF. 2). FT CONFLICT 332 332 A -> R (IN REF. 1). FT CONFLICT 636 636 P -> A (IN REF. 2). FT CONFLICT 862 864 DVF -> ASSPTELLRANCIRNR (IN REF. 2). FT CONFLICT 866 866 Y -> N (IN REF. 2). SQ SEQUENCE 1286 AA; 142830 MW; 5F22A956F8BE0EC6 CRC64; MDRDSLPRVP DTHGDVVDEK LFSDLYIRTS WVDAQVALDQ IDKGKARGSR TAIYLRSVFQ SHLETLGSSV QKHAGKVLFV AILVLSTFCV GLKSAQIHSK VHQLWIQEGG RLEAELAYTQ KTIGEDESAT HQLLIQTTHD PNASVLHPQA LLAHLEVLVK ATAVKVHLYD TEWGLRDMCN MPSTPSFEGI YYIEQILRHL IPCSIITPLD CFWEGSQLLG PESAVVIPGL NQRLLWTTLN PASVMQYMKQ KMSEEKISFD FETVEQYMKR AAIGSGYMEK PCLNPLNPNC PDTAPNKNST QPPDVGAILS GGCYGYAAKH MHWPEELIVG GAKRNRSGHL RKAQALQSVV QLMTEKEMYD QWQDNYKVHH LGWTQEKAAE VLNAWQRNFS REVEQLLRKQ SRIATNYDIY VFSSAALDDI LAKFSHPSAL SIVIGVAVTV LYAFCTLLRW RDPVRGQSSV GVAGVLLMCF STAAGLGLSA LLGIVFNAAS TQVVPFLALG LGVDHIFMLT AAYAESNRRE QTKLILKKVG PSILFSACST AGSFFAAAFI PVPALKVFCL QAAIVMCSNL AAALLVFPAM ISLDLRRRTA GRADIFCCCF PVWKEQPKVA PPVLPLNNNN GRGARHPKSC NNNRVPLPAQ NPLLEQRADI PGSSHSLASF SLATFAFQHY TPFLMRSWVK FLTVMGFLAA LISSLYASTR LQDGLDIIDL VPKDSNEHKF LDAQTRLFGF YSMYAVTQGN FEYPTQQQLL RDYHDSFVRV PHVIKNDNGG LPDFWLLLFS EWLGNLQKIF DEEYRDGRLT KECWFPNASS DAILAYKLIV QTGHVDNPVD KELVLTNRLV NSDGIINQRA FYNYLSAWAT NDVFAYGASQ GKLYPEPRQY FHQPNEYDLK IPKSLPLVYA QMPFYLHGLT DTSQIKTLIG HIRDLSVKYE GFGLPNYPSG IPFIFWEQYM TLRSSLAMIL ACVLLAALVL VSLLLLSVWA AVLVILSVLA SLAQIFGAMT LLGIKLSAIP AVILILSVGM MLCFNVLISL GFMTSVGNRQ RRVQLSMQMS LGPLVHGMLT SGVAVFMLST SPFEFVIRHF CWLLLVVLCV GACNSLLVFP ILLSMVGPEA ELVPLEHPDR ISTPSPLPVR SSKRSGKSYV VQGSRSSRGS CQKSHHHHHK DLNDPSLTTI TEEPQSWKSS NSSIQMPNDW TYQPREQRPA SYAAPPPAYH KAAAQQHHQH QGPPTTPPPP FPTAYPPELQ SIVVQPEVTV ETTHSDSNTT KVTATANIKV ELAMPGRAVR SYNFTS // ID PAX6_DROME STANDARD; PRT; 857 AA. AC O18381; Q9V4F5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Paired box protein Pax-6 (Eyeless protein). GN EY OR PAX6 OR CG1464. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS EMBRYONIC AND LARVAL). RC STRAIN=Oregon-R; TISSUE=Embryo, and Imaginal disks; RX MEDLINE=94323757; PubMed=7914031; RA Quiring R., Walldorf U., Kloter U., Gehring W.J.; RT "Homology of the eyeless gene of Drosophila to the Small eye gene in RT mice and Aniridia in humans."; RL Science 265:785-789(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: INVOLVED IN EYE MORPHOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=Larval; CC IsoId=O18381-1; Sequence=Displayed; CC Name=Embryonic; CC IsoId=O18381-2; Sequence=VSP_002369; CC Name=B; CC IsoId=O18381-3; Sequence=VSP_002368; CC -!- TISSUE SPECIFICITY: EXPRESSION IS CONFINED TO THE EYE IMAGINAL CC DISKS, PARTS OF THE BRAIN, THE VENTRAL GANGLION AND THE SALIVARY CC GLANDS. CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 PAIRED BOX DOMAIN. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X79492; CAA56037.1; -. DR EMBL; X79493; CAA56038.1; -. DR EMBL; AE003843; AAF59318.1; -. DR EMBL; AE003843; AAN06513.1; -. DR HSSP; P26367; 6PAX. DR FlyBase; FBgn0005558; ey. DR GO; GO:0008347; P:glia cell migration; IMP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR001523; Paired_box. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_BOX; 1. KW Transcription regulation; Homeobox; DNA-binding; Nuclear protein; KW Developmental protein; Paired box; Alternative splicing. FT DOMAIN 56 161 PAIRED BOX. FT DNA_BIND 411 470 HOMEOBOX. FT VARSPLIC 1 233 Missing (in isoform B). FT /FTId=VSP_002368. FT VARSPLIC 1 56 MRNLPCLGTAGGSGLGGIAGKPSPTMEAVEASTASHRHSTS FT SYFATTYYHLTDDEC -> MFTLQPTPTAIGTVVPPWSAGT FT LIERLPSLEDMAHKG (in isoform Embryonic). FT /FTId=VSP_002369. FT CONFLICT 249 249 S -> T (IN REF. 1). FT CONFLICT 367 367 E -> K (IN REF. 1). SQ SEQUENCE 857 AA; 89492 MW; 8EC3BA2F4C066269 CRC64; MRNLPCLGTA GGSGLGGIAG KPSPTMEAVE ASTASHRHST SSYFATTYYH LTDDECHSGV NQLGGVFVGG RPLPDSTRQK IVELAHSGAR PCDISRILQV SNGCVSKILG RYYETGSIRP RAIGGSKPRV ATAEVVSKIS QYKRECPSIF AWEIRDRLLQ ENVCTNDNIP SVSSINRVLR NLAAQKEQQS TGSGSSSTSA GNSISAKVSV SIGGNVSNVA SGSRGTLSSS TDLMQTATPL NSSESGGASN SGEGSEQEAI YEKLRLLNTQ HAAGPGPLEP ARAAPLVGQS PNHLGTRSSH PQLVHGNHQA LQQHQQQSWP PRHYSGSWYP TSLSEIPISS APNIASVTAY ASGPSLAHSL SPPNDIESLA SIGHQRNCPV ATEDIHLKKE LDGHQSDETG SGEGENSNGG ASNIGNTEDD QARLILKRKL QRNRTSFTND QIDSLEKEFE RTHYPDVFAR ERLAGKIGLP EARIQVWFSN RRAKWRREEK LRNQRRTPNS TGASATSSST SATASLTDSP NSLSACSSLL SGSAGGPSVS TINGLSSPST LSTNVNAPTL GAGIDSSESP TPIPHIRPSC TSDNDNGRQS EDCRRVCSPC PLGVGGHQNT HHIQSNGHAQ GHALVPAISP RLNFNSGSFG AMYSNMHHTA LSMSDSYGAV TPIPSFNHSA VGPLAPPSPI PQQGDLTPSS LYPCHMTLRP PPMAPAHHHI VPGDGGRPAG VGLGSGQSAN LGASCSGSGY EVLSAYALPP PPMASSSAAD SSFSAASSAS ANVTPHHTIA QESCPSPCSS ASHFGVAHSS GFSSDPISPA VSSYAHMSYN YASSANTMTP SSASGTSAHV APGKQQFFAS CFYSPWV // ID PBP1_DROME STANDARD; PRT; 148 AA. AC P54191; Q9VTX0; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pheromone-binding protein-related protein 1 precursor (PBPRP-1). GN PBPRP1 OR CG10436. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Antenna; RX MEDLINE=94121915; PubMed=7545907; RA Pikielny C.W., Hasan G., Rouyer F., Rosbash M.; RT "Members of a family of Drosophila putative odorant-binding proteins RT are expressed in different subsets of olfactory hairs."; RL Neuron 12:35-49(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED IN THE LUMEN OF OLFACTORY HAIRS CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: ANTENNA. MOSTLY ON THE ANTERIOR SURFACE OF THE CC THIRD ANTENNAL SEGMENT. CC -!- SIMILARITY: BELONGS TO THE PBP/GOBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05980; AAC46474.1; -. DR EMBL; AE003541; AAF49925.1; -. DR FlyBase; FBgn0011279; Pbprp1. DR InterPro; IPR006170; PBP_GOBP. DR InterPro; IPR006625; PhBP. DR Pfam; PF01395; PBP_GOBP; 1. DR SMART; SM00708; PhBP; 1. KW Multigene family; Signal. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 148 PHEROMONE-BINDING PROTEIN-RELATED PROTEIN FT 1. FT CONFLICT 102 102 H -> Y (IN REF. 1). SQ SEQUENCE 148 AA; 16726 MW; EB8D417130226A5E CRC64; MVARHFSFFL ALLILYDLIP SNQGVEINPT IIKQVRKLRM RCLNQTGASV DVIDKSVKNR ILPTDPEIKC FLYCMFDMFG LIDSQNIMHL EALLEVLPEE IHKTINGLVS SCGTQKGKDG CDTAYETVKC YIAVNGKFIW EEIIVLLG // ID PBP2_DROME STANDARD; PRT; 150 AA. AC P54192; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Pheromone-binding protein-related protein 2 precursor (PBPRP-2). GN PBPRP2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Antenna; RX MEDLINE=94121915; PubMed=7545907; RA Pikielny C.W., Hasan G., Rouyer F., Rosbash M.; RT "Members of a family of Drosophila putative odorant-binding proteins RT are expressed in different subsets of olfactory hairs."; RL Neuron 12:35-49(1994). CC -!- SUBCELLULAR LOCATION: SECRETED IN THE LUMEN OF OLFACTORY HAIRS CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: ANTENNA. MOSTLY ON THE ANTERIOR SURFACE OF THE CC THIRD ANTENNAL SEGMENT. ALSO DETECTED IN THE MAXILLARY PALPS AND CC IN CELLS AT THE BASES OF THE TASTE HAIRS ON THE PROBOSCIS AND CC INTERNAL TASTE ORGANS OF THE HEAD. CC -!- SIMILARITY: BELONGS TO THE PBP/GOBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05981; AAC46475.1; -. DR FlyBase; FBgn0011280; Pbprp2. DR GO; GO:0005550; F:pheromone binding; NAS. DR InterPro; IPR006170; PBP_GOBP. DR InterPro; IPR006625; PhBP. DR Pfam; PF01395; PBP_GOBP; 1. DR SMART; SM00708; PhBP; 1. KW Multigene family; Signal. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 150 PHEROMONE-BINDING PROTEIN-RELATED PROTEIN FT 2. SQ SEQUENCE 150 AA; 16894 MW; 0EFE064A1C24321F CRC64; MSHLVHLTVL LLVGILCLGA TSAKPHEEIN RDHLLELANE CKAETGATDE DVEQLMSHDL PERHEAKCLR ACVMKKLQIM DESGKLNKEH AIELVKVMSK HDAEKEDAPA EVVAKCEAIE TPEDHCDAAF AYEECIYEQM REHGLELEEH // ID PBP3_DROME STANDARD; PRT; 154 AA. AC P54193; Q9VNK2; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pheromone-binding protein-related protein 3 precursor (PBPRP-3) DE (Odorant-binding protein OS-F). GN PBPRP3 OR OS-F OR CG11421. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Antenna; RX MEDLINE=94121915; PubMed=7545907; RA Pikielny C.W., Hasan G., Rouyer F., Rosbash M.; RT "Members of a family of Drosophila putative odorant-binding proteins RT are expressed in different subsets of olfactory hairs."; RL Neuron 12:35-49(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CS-5; TISSUE=Antenna; RX MEDLINE=94266829; PubMed=8206941; RA McKenna M.P., Hekmat-Scafe D.S., Gaines P., Carlson J.R.; RT "Putative Drosophila pheromone-binding proteins expressed in a RT subregion of the olfactory system."; RL J. Biol. Chem. 269:16340-16347(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97184209; PubMed=9030621; RA Hekmat-Scafe D.S., Steinbrecht R.A., Carlson J.R.; RT "Coexpression of two odorant-binding protein homologs in Drosophila: RT implications for olfactory coding."; RL J. Neurosci. 17:1616-1624(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- SUBCELLULAR LOCATION: SECRETED IN THE LUMEN OF OLFACTORY HAIRS CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: ANTENNA. MOSTLY ON THE ANTERIOR SURFACE OF THE CC THIRD ANTENNAL SEGMENT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN ADULT BUT NOT IN LARVAL CC OLFACTORY ORGANS. CC -!- SIMILARITY: BELONGS TO THE PBP/GOBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05982; AAC46476.1; -. DR EMBL; U02542; AAA21355.1; -. DR EMBL; U81503; AAB51684.1; -. DR EMBL; AE003601; AAF51929.2; -. DR FlyBase; FBgn0011281; Pbprp3. DR InterPro; IPR000113; MealwormbtlB. DR InterPro; IPR006170; PBP_GOBP. DR InterPro; IPR006625; PhBP. DR Pfam; PF01395; PBP_GOBP; 1. DR PRINTS; PR00485; MEALWORMBTLB. DR SMART; SM00708; PhBP; 1. KW Multigene family; Signal. FT SIGNAL 1 33 POTENTIAL. FT CHAIN 34 154 PHEROMONE-BINDING PROTEIN-RELATED PROTEIN FT 3. SQ SEQUENCE 154 AA; 17326 MW; F46FFB077A069279 CRC64; MALNGFGRRV SASVLLIALS LLSGALILPP AAAQRDENYP PPGILKMAKP FHDACVEKTG VTEAAIKEFS DGEIHEDEKL KCYMNCFFHE IEVVDDNGDV HLEKLFATVP LSMRDKLMEM SKGCVHPEGD TLCHKAWWFH QCWKKADPKH YFLP // ID PBP4_DROME STANDARD; PRT; 175 AA. AC P54194; Q9VI86; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pheromone-binding protein-related protein 4 precursor (PBPRP-4). GN PBPRP4 OR CG1176. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Antenna; RX MEDLINE=94121915; PubMed=7545907; RA Pikielny C.W., Hasan G., Rouyer F., Rosbash M.; RT "Members of a family of Drosophila putative odorant-binding proteins RT are expressed in different subsets of olfactory hairs."; RL Neuron 12:35-49(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED IN THE LUMEN OF OLFACTORY HAIRS CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: PRESENT ONLY IN A SMALL NUMBER OF HAIRS CC SCATTERED OVER THE SURFACE OF THE FUNICULUS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05984; AAC46477.1; -. DR EMBL; AE003672; AAF54039.1; -. DR FlyBase; FBgn0011282; Pbprp4. DR InterPro; IPR006170; PBP_GOBP. DR InterPro; IPR006625; PhBP. DR Pfam; PF01395; PBP_GOBP; 1. DR SMART; SM00708; PhBP; 1. KW Multigene family; Signal. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 175 PHEROMONE-BINDING PROTEIN-RELATED PROTEIN FT 4. SQ SEQUENCE 175 AA; 19513 MW; 76339DADEC76C7F5 CRC64; MYSALVRACA VIAFLILSPN CARALQDHAK DNGDIFIINY DSFDGDVDDI STTTSAPREA DYVDFDEVNR NCNASFITSM TNVLQFNNTG DLPDDKDKVT SMCYFHCFFE KSGLMTDYKL NTDLVRKYVW PATGDSVEAC EAEGKDETNA CMRGYAIVKC VFTRALTDAR NKPTV // ID PBP5_DROME STANDARD; PRT; 143 AA. AC P54195; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Pheromone-binding protein-related protein 5 precursor (PBPRP-5). GN PBPRP5. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Antenna; RX MEDLINE=94121915; PubMed=7545907; RA Pikielny C.W., Hasan G., Rouyer F., Rosbash M.; RT "Members of a family of Drosophila putative odorant-binding proteins RT are expressed in different subsets of olfactory hairs."; RL Neuron 12:35-49(1994). CC -!- SUBCELLULAR LOCATION: SECRETED IN THE LUMEN OF OLFACTORY HAIRS CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: ANTENNA. MOSTLY ON THE MEDIAL AND POSTERIOR CC SURFACE OF THE THIRD ANTENNAL SEGMENT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05985; AAC46478.1; -. DR FlyBase; FBgn0011283; Pbprp5. DR InterPro; IPR006170; PBP_GOBP. DR InterPro; IPR006625; PhBP. DR Pfam; PF01395; PBP_GOBP; 1. DR SMART; SM00708; PhBP; 1. KW Multigene family; Signal. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 143 PHEROMONE-BINDING PROTEIN-RELATED PROTEIN FT 5. SQ SEQUENCE 143 AA; 15151 MW; AE52D172CCFDE0B3 CRC64; MQSTPIILVA IVLLGAALVR AFDEKEALAK LMESAESCMP EVGATDADLQ EMVKKQPAST YAGKCLRACV MKNIGILDAN GKLDTEAGHE KAKQYTGNDP AKLKIALDIG ETCAAITVPD DHCEAAEAYG TCFRGEAKKH GLL // ID PBP6_DROME STANDARD; PRT; 141 AA. AC Q23970; P91684; Q9VNK3; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pheromone-binding protein-related protein 6 precursor (PBPRP-6) DE (Odorant-binding protein OS-E). GN OS-E OR PBPRP6 OR CG11422. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CS-5; TISSUE=Antenna; RX MEDLINE=94266829; PubMed=8206941; RA McKenna M.P., Hekmat-Scafe D.S., Gaines P., Carlson J.R.; RT "Putative Drosophila pheromone-binding proteins expressed in a RT subregion of the olfactory system."; RL J. Biol. Chem. 269:16340-16347(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97184209; PubMed=9030621; RA Hekmat-Scafe D.S., Steinbrecht R.A., Carlson J.R.; RT "Coexpression of two odorant-binding protein homologs in Drosophila: RT implications for olfactory coding."; RL J. Neurosci. 17:1616-1624(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED IN THE LUMEN OF OLFACTORY HAIRS CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: ANTENNA. MOSTLY IN THE VENTRO-LATERAL REGION CC OF THE THIRD ANTENNAL SEGMENT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN ADULT BUT NOT IN LARVAL CC OLFACTORY ORGANS. CC -!- SIMILARITY: BELONGS TO THE PBP/GOBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U02543; AAA21356.1; -. DR EMBL; U81502; AAB51683.1; -. DR EMBL; AE003601; AAF51928.1; -. DR FlyBase; FBgn0010403; Os-E. DR InterPro; IPR000113; MealwormbtlB. DR InterPro; IPR006170; PBP_GOBP. DR InterPro; IPR006625; PhBP. DR Pfam; PF01395; PBP_GOBP; 1. DR PRINTS; PR00485; MEALWORMBTLB. DR SMART; SM00708; PhBP; 1. KW Multigene family; Signal; Polymorphism. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 141 PHEROMONE-BINDING PROTEIN-RELATED PROTEIN FT 6. FT VARIANT 2 2 L -> V (IN STRAIN CANTON-S). SQ SEQUENCE 141 AA; 16126 MW; AD6EB752B593F738 CRC64; MLKYPLILLL IGCAAAQEPR RDGEWPPPAI LKLGKHFHDI CAPKTGVTDE AIKEFSDGQI HEDEALKCYM NCLFHEFEVV DDNGDVHMEK VLNAIPGEKL RNIMMEASKG CIHPEGDTLC HKAWWFHQCW KKADPVHYFL V // ID PCNA_DROME STANDARD; PRT; 260 AA. AC P17917; Q9V909; DT 01-NOV-1990 (Rel. 16, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proliferating cell nuclear antigen (PCNA) (Cyclin) (Mutagen-sensitive DE 209 protein). GN MUS209 OR PCNA OR CG9193. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90158601; PubMed=1968224; RA Yamaguchi M., Nishida Y., Moriuchi T., Hirose F., Hui C.C., RA Suzuki Y., Matsukage A.; RT "Drosophila proliferating cell nuclear antigen (cyclin) gene: RT structure, expression during development, and specific binding of RT homeodomain proteins to its 5'-flanking region."; RL Mol. Cell. Biol. 10:872-879(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-22. RC STRAIN=Oregon-R; RX MEDLINE=90307726; PubMed=1973166; RA Ng L., Prelich G., Anderson C.W., Stillman B., Fisher P.A.; RT "Drosophila proliferating cell nuclear antigen. Structural and RT functional homology with its mammalian counterpart."; RL J. Biol. Chem. 265:11948-11954(1990). RN [4] RP MUTAGENESIS. RX MEDLINE=94185652; PubMed=7907981; RA Henderson D.S., Banga S.S., Grigliatto T.A., Boyd J.B.; RT "Mutagen sensitivity and suppression of position-effect variegation RT result from mutations in mus209, the Drosophila gene encoding PCNA."; RL EMBO J. 13:1450-1459(1994). CC -!- FUNCTION: THIS PROTEIN IS AN AUXILIARY PROTEIN OF DNA POLYMERASE CC DELTA AND IS INVOLVED IN THE CONTROL OF EUKARYOTIC DNA REPLICATION CC BY INCREASING THE POLYMERASE'S PROCESSIBILITY DURING ELONGATION OF CC THE LEADING STRAND. CC -!- SUBUNIT: HOMOTRIMER. FORMS A COMPLEX WITH ACTIVATOR 1 CC HETEROPENTAMER IN THE PRESENCE OF ATP (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE PCNA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33950; AAA28746.1; -. DR EMBL; AE003792; AAF57493.1; -. DR PIR; A34752; A34752. DR HSSP; P12004; 1AXC. DR FlyBase; FBgn0005655; mus209. DR GO; GO:0006260; P:DNA replication; IMP. DR GO; GO:0007052; P:mitotic spindle assembly; IMP. DR InterPro; IPR000730; Pr_cel_nuc_antig. DR Pfam; PF00705; PCNA; 1. DR Pfam; PF02747; PCNA_C; 1. DR PRINTS; PR00339; PCNACYCLIN. DR ProDom; PD002673; Pr_cel_nuc_antig; 1. DR TIGRFAMs; TIGR00590; pcna; 1. DR PROSITE; PS00293; PCNA_2; 1. DR PROSITE; PS01251; PCNA_1; 1. KW DNA-binding; Nuclear protein; DNA replication. FT DNA_BIND 61 80 POTENTIAL. SQ SEQUENCE 260 AA; 28830 MW; 9A46280EA2C61FC5 CRC64; MFEARLGQAT ILKKILDAIK DLLNEATFDC SDSGIQLQAM DNSHVSLVSL TLRSDGFDKF RCDRNLSMGM NLGSMAKILK CANNEDNVTM KAQDNADTVT IMFESANQEK VSDYEMKLMN LDQEHLGIPE TDFSCVVRMP AMEFARICRD LAQFSESVVI CCTKEGVKFS ASGDVGTANI KLAQTGSVDK EEEAVIIEMQ EPVTLTFACR YLNAFTKATP LSTQVQLSMC ADVPLVVEYA IKDLGHIRYY LAPKIEDNET // ID PCX_DROME STANDARD; PRT; 2483 AA. AC P18490; DT 01-NOV-1990 (Rel. 16, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pecanex protein. GN PCX. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE OF 1-545 FROM N.A. RC STRAIN=Oregon-R; RA Labonne S.G.; RL Submitted (XXX-1991) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 546-2483 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90033754; PubMed=2478400; RA Labonne S.G., Sunitha I., Mahowald A.P.; RT "Molecular genetics of pecanex, a maternal-effect neurogenic locus of RT Drosophila melanogaster that potentially encodes a large RT transmembrane protein."; RL Dev. Biol. 136:1-16(1989). CC -!- FUNCTION: INVOLVED IN NEUROGENESIS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE PECANEX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74329; AAA28747.1; -. DR EMBL; M25662; AAA28749.1; -. DR PIR; A37361; A37361. DR FlyBase; FBgn0003048; pcx. DR InterPro; IPR007735; Pecanex_C. DR Pfam; PF05041; Pecanex_C; 1. KW Developmental protein; Neurogenesis; Transmembrane; Glycoprotein; KW Repeat. FT TRANSMEM 750 771 POTENTIAL. FT TRANSMEM 859 883 POTENTIAL. FT TRANSMEM 1285 1307 POTENTIAL. FT DOMAIN 39 51 POLY-HIS. FT DOMAIN 1231 1240 5 X 2 AA TANDEM REPEATS OF G-T. FT CARBOHYD 105 105 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 117 117 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 221 221 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 393 393 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 598 598 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 711 711 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 902 902 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1118 1118 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1337 1337 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1350 1350 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1528 1528 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1688 1688 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1786 1786 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2315 2315 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 2483 AA; 266639 MW; D376A3AB57112AEE CRC64; MYYVAHLDPF PDGYLEDDSY TKSDLGIEQP HQPTFRTQHR HHHHHHHLHH HLGGAIIRKD PTSTMSALQL AAVTQPGTGG SVTGGGGAAG GGGSAAGMKR RRHSNATSYK HGSSQSNKSS LVGGGGSRGP SGEAGTSGGA GGTGGVRRIK SAALEVLCPQ PSVSNLSPHP NSVEAISGQQ QMRNPLPPPS KSLVRNQHLN LYPTQGYGDG TPSAGGGGPG NSSTCSSLFF GSSSACGSTT ALIEPPVYPI VEHSDEKTAH EEHGDDCLGI GQGNADDDDE VDDVPIRRRT RALGCSQTHY SVESDVGGFL ADEDGADEDV FKDFDDNLEH ILSELQQTHN QLDDVLKTHD LHHHSHLHHH KAASVEGAGP SGGSVAVGVS AGNDDEDEET EDNNTGSRSP LLNDRNRQPA TLREIQADKQ LRQELSHQSG AVIPAPNPPV PIRSEADSGC PSSDCEQVSA SSKDQLLSGI ELELQQYQIL QRCQLDEEQP CTSKMAAKSL GAIPKVVKYR EVDELRRRRR GGSPADAAEA GNEFALVKQT KQASRNSHSI SLTDSLTADI HKMLWLMHGG ADDRGRPITG TSADGTPIPA SSSLVPPNMS NAHFQFYQDA IQALQGTHPT SGSSVEHMTN IELARDKLRL DAKLMCEQLV AAAEANSGVR GNTLATQQMT QQQVGMLMRG GSSSRHPSSA PFSVQGLINV IRSERPAAAV NWTLEQLVMQ QQHWPLMPVR LPPFQLRCRR RSIEWRGRSF KRPRTGESPQ QPDQPNQSAQ SDEPTHAECD GHFAPYCDYW RPACLLSATE KPAAPKSFYK YRFKWCGQEH EFKIAMDRLE LLALFDRDLH WMHVLLASLL CTLVACLGAA ILQHDHYKDL CALLFCAVIA GAQYSLVKSV LPDARSPVHG FNKTVAYSRA IYFCLAGGML LLLKRLDTDY GERTPDPVVF FGMRYSPADV VALLLQALYI LLLCFPIIFS VGLCPQINTF LMYLLEQIDM HVFGGNAASS LLGENSLIPI LLLRLIPNTV QVPFCAVVRS VLAVMLLYGP LYGALDEQRG PSTFCSTIYC AMLVPLGYHL SRCASDFSHL WRLIKTCIVS TYRDDEDEDL SQMQHIATGT VTGSGTANST ALQLTTSTPK QHRQTDVKTE HEQIELSSLE KLTVNEEHHE KDHGADDQLE TDQDLPLQQK HSKSKTSSLG SSQQTLGKTI SSSKRAITAS SSCTSIGTGE PAVEAGALAE EAVEGEEQRR NTLAGEVGSK HELAENYDQA AKIDECEDKI SSSSATNPGD MSTLTAGAGT ATTDATPACL EADPDAEAEA PADEKQHQGI LGTGTGTGTG TTEASENGSG GGANRNTNSN GTGNDLPDPL PRKLQATVTT RLKNDLVVMT LLAVSVLGLH CSTVFTALQP DLNVVLYSFI GVLGLLLHYI VPQMRKHMPW LCFSRPLLRQ REFGQFEVLN APKIMWFEKL YIYLSVLERN VNPVTVTAAA APSTKECCPG NQRRRGGVVV GGTTVPGTGG VTGGGGDPQL SSSHSFANIS RQTSESAPGL GGYVAYMDQN VFVKLAKSST TTGAGAGAPT SRKESQEKPA LRLKLASVGK DAPLVSLCLP WPFGQAITAT ACHSALTGVE FFLHGLHALF KGDFRITSPR DEWVFADMEL LHSVVAPAVK MALKLQQDHI TNPDEFLDPH ALYDAIDNCS NELVISHEAD PVWRSAVLRG APNLLALRHV MEDGSDEYRI IRLTKRCLSF RVIKLNRECV RGLWAGQQQE LIYLRNRNPE RGSIQNAKQA LRNIINSSCD QPIGYPIYVS PLTTSYADTN AQLCEVIGGA ITLDTIRHTV LGWWHRIRER CRQGCSSGSA LEPHPGSGPV QLGACNFGSG GSVVGAASTA TGVGASTGSG LGVAAPGTAG STGGESGDLA PVFISAPLYN TLTVNSYYSV RPGNVPGGPI PGNLGGNYVS DSLAVVRGGL AVMPVKPTST TLIAGLLNRE RDETSGSGIM GAGASGPTRA TSSGGVRSRR PEVGSSRGRD HERRATLPIA SGGAGGEPGK DLTAPQTQVE HEPSPRSTKL SSSSGSLGLG MGVGLGNIIT TPGDYPRKTK GPICLTAVDT GTSSSAAEGK PAGSGTVAGT GVGGVIRKPR IEIFKKVIIV DDTGIYDCLD IIDAVVWPTE RMRNNGGRLS WKDWEPSAGN GGHVVHCWPP NHKDIRFRSH VNRYVYLVEI GDHYVPVEEL GLREYNQIMG STEEMANSRR SSIQRDFHEY NIQLKLAGLA PIIGGGESST ATTSDASKSH KAKIRAVSSS SSEDEDTSSA RSIPLPQGDD GDLTNFTRLV SMWKEIILDN NKRRLYDMGE LSPELLQKLD DAVQQQQQLE DALAEESKEK GTATVTANEG EEGVGEMEIE PEQEQKEVVY LEEQSPLEEV TVSKPGEQPA QPTIPASPVP AETSSTSSAK STSSPSLCQE EEDAVDPERP LNWPPRSHQA MRMARARREQ RSK // ID PC_DROME STANDARD; PRT; 390 AA. AC P26017; Q9VP49; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polycomb protein. GN PC OR CG7618. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91095442; PubMed=1898775; RA Paro R., Hogness D.S.; RT "The Polycomb protein shares a homologous domain with a RT heterochromatin-associated protein of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 88:263-267(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE SEGMENT-SPECIFIC REPRESSION OF HOMEOTIC CC SELECTOR GENES. PC MAY BE INVOLVED IN THE STABLE TRANSMISSION OF A CC DETERMINED STATE BY ITS EFFECTS ON CHROMATIN STRUCTURE. PROMOTES CC LOCUS-SPECIFIC CHROMATIN COMPACTION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: REQUIRED DURING THE ENTIRE LARVAL PERIOD FOR CC NORMAL ADULT DEVELOPMENT. IT IS FOUND IN ALMOST ALL CELLS AND CC TISSUES THROUGHOUT GASTRULATION AND ORGANOGENESIS THOUGH AT A MUCH CC LOWER LEVEL THAN IN EARLY SYNCYTIAL STAGES. CC -!- SIMILARITY: CONTAINS 1 CHROMO DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55702; CAA39229.1; -. DR EMBL; AE003594; AAF51707.1; -. DR PIR; A38565; A38565. DR HSSP; P23197; 1AP0. DR TRANSFAC; T00693; -. DR FlyBase; FBgn0003042; Pc. DR GO; GO:0016458; P:gene silencing; IGI. DR InterPro; IPR000953; Chromo. DR Pfam; PF00385; chromo; 1. DR PRINTS; PR00504; CHROMODOMAIN. DR SMART; SM00298; CHROMO; 1. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 1. KW Nuclear protein. FT DOMAIN 26 84 CHROMO. FT DOMAIN 134 143 POLY-HIS. FT DOMAIN 160 167 POLY-HIS. SQ SEQUENCE 390 AA; 43976 MW; 5DB24AE4B326C3B9 CRC64; MTGRGKGSKG KLGRDNATDD PVDLVYAAEK IIQKRVKKGV VEYRVKWKGW NQRYNTWEPE VNILDRRLID IYEQTNKSSG TPSKRGIKKK EKEPDPEPES EEDEYTFTEN DVDTHQATTS SATHDKESKK EKKHHHHHHH HHHIKSERNS GRRSESPLTH HHHHHHHESK RQRIDHSSSS NSSFTHNSFV PEPDSNSSSS EDQPLIGTKR KAEVLKESGK IGVTIKTSPD GPTIKPQPTQ QVTPSQQQPF QDQQQAEKIA SEAATQLKSE QQATPLATEA INTTPAESGA EEEEVANEEG NQQAPQVPSE NNNIPKPCNN LAINQKQPLT PLSPRALPPR FWLPAKCNIS NRVVITDVTV NLETVTIREC KTERGFFRER DMKGDSSPVA // ID PDI_DROME STANDARD; PRT; 496 AA. AC P54399; Q9VUL7; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein disulfide isomerase precursor (PDI) (EC 5.3.4.1). GN PDI OR CG6988. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=95307561; PubMed=7787847; RA McKay R.R., Zhu L., Shortridge R.D.; RT "A Drosophila gene that encodes a member of the protein disulfide RT isomerase/phospholipase C-alpha family."; RL Insect Biochem. Mol. Biol. 25:647-654(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PARTICIPATES IN THE FOLDING OF PROTEINS CONTAINING CC DISULFIDE BONDS (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: REARRANGEMENT OF BOTH INTRACHAIN AND CC INTERCHAIN DISULFIDE BONDS IN PROTEINS TO FORM THE NATIVE CC STRUCTURES. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN ALL HEAD AND BODY TISSUES. CC -!- DEVELOPMENTAL STAGE: UBIQUITOUSLY EXPRESSED DURING DEVELOPMENT. CC -!- SIMILARITY: CONTAINS 2 THIOREDOXIN DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18973; AAA86480.1; -. DR EMBL; AE003532; AAF49659.1; -. DR HSSP; P07237; 1MEK. DR FlyBase; FBgn0014002; Pdi. DR GO; GO:0005783; C:endoplasmic reticulum; IDA. DR InterPro; IPR005788; Disulph_isom. DR InterPro; IPR005792; Disulphide_isom. DR InterPro; IPR000886; ER_target_S. DR InterPro; IPR006662; Thiored. DR InterPro; IPR006663; Thioredox_dom2. DR Pfam; PF00085; thiored; 2. DR PRINTS; PR00421; THIOREDOXIN. DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1. DR TIGRFAMs; TIGR01126; pdi_dom; 2. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN; 2. KW Redox-active center; Isomerase; Endoplasmic reticulum; Repeat; Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 496 PROTEIN DISULFIDE ISOMERASE. FT DISULFID 56 59 REDOX-ACTIVE (BY SIMILARITY). FT DISULFID 397 400 REDOX-ACTIVE (BY SIMILARITY). FT DOMAIN 482 489 POLY-GLU. FT SITE 493 496 PREVENT SECRETION FROM ER (POTENTIAL). SQ SEQUENCE 496 AA; 55781 MW; EB6E04C4216E7A81 CRC64; MKFLICALFL AASYVAASAE AEVKVEEGVL VATVDNFKQL IADNEFVLVE FYAPWCGHCK ALAPEYAKAA QQLAEKESPI KLAKVDATVE GELAEQYAVR GYPTLKFFRS GSPVEYSGGR QAADIIAWVT KKTGPPAKDL TSVADAEQFL KDNEIAIIGF FKDLESEEAK TFTKVANALD SFVFGVSSNA DVIAKYEAKD NGVVLFKPFD DKKSVFEGEL NEENLKKFAQ VQSLPLIVDF NHESASKIFG GSIKSHLLFF VSREGGHIEK YVDPLKEIAK KYRDDILFVT ISSDEEDHTR IFEFFGMNKE EVPTIRLIKL EEDMAKYKPE SDDLSAETIE AFLKKFLDGK LKQHLLSQEL PEDWDKNPVK VLVSSNFESV ALDKSKSVLV EFYAPWCGHC KQLAPIYDQL AEKYKDNEDI VIAKMDSTAN ELESIKISSF PTIKYFRKED NKVIDFNLDR TLDDFVKFLD ANGEVADSEP VEETEEEEEA PKKDEL // ID PDK_DROME STANDARD; PRT; 413 AA. AC P91622; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE [Pyruvate dehydrogenase [lipoamide]] kinase, mitochondrial precursor DE (EC 2.7.1.99) (Pyruvate dehydrogenase kinase) (DmPDK). GN PDK. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=97238628; PubMed=9115642; RA Katsube T., Nomoto S., Togashi S., Ueda R., Kobayashi M., Takahisa M.; RT "cDNA sequence and expression of a gene encoding a pyruvate RT dehydrogenase kinase homolog of Drosophila melanogaster."; RL DNA Cell Biol. 16:335-339(1997). CC -!- FUNCTION: INHIBITS THE MITOCHONDRIAL PYRUVATE DEHYDROGENASE CC COMPLEX BY PHOSPHORYLATION OF THE E1 ALPHA SUBUNIT, THUS CC CONTRIBUTING TO THE REGULATION OF GLUCOSE METABOLISM. CC -!- CATALYTIC ACTIVITY: ATP + [PYRUVATE DEHYDROGENASE (LIPOAMIDE)] = CC ADP + [PYRUVATE DEHYDROGENASE (LIPOAMIDE)] PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO THE PDK/BCKDK PROTEIN KINASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 HISTIDINE KINASE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D88814; BAA13724.1; -. DR FlyBase; FBgn0017558; Pdk. DR InterPro; IPR003594; ATPbind_ATPase. DR InterPro; IPR005467; His_kinase. DR Pfam; PF02518; HATPase_c; 1. DR SMART; SM00387; HATPase_c; 1. DR PROSITE; PS50109; HIS_KIN; 1. KW Kinase; Transferase; Transit peptide; Mitochondrion. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 413 [PYRUVATE DEHYDROGENASE [LIPOAMIDE]] FT KINASE. FT DOMAIN 137 369 HISTIDINE KINASE. SQ SEQUENCE 413 AA; 46625 MW; 009044C45BD09B58 CRC64; MRLFPVRFSA ASLSMASLAK MLDFYSGFNP SPLSIKQFMD FGQNACEKKS YIFLRKELPV RLANIMKEIA LLPDNLLHTR SVSEVSSWYV KSFEDVLVYE KAEPTHDNLQ KFVADLDLIR NRHNDVVQTM AQGVIEMKEN EGGQVDAPTE SSIQYFLDRL YMSRISIRML INQHTLLFGG NPHAGGRHIG CLDPACDLSD VVRDAYENAR FLCDQYYLTS PALEIQQHSS EPGDNLPIRT VYVPSHLYYM LFELFKNSMR AVVEHHGHDN NDTLPPLKVA ICKGKEDICV KISDQGGGIP RSQTDQLFKY MYSTAPQPSK SDLHTVPLAG YGYGLPISRL YARYFHGDIV LLSCEGFGTD AIIYLKALSD EANELLPIFN KTSSKFYRAT VPTGDWSNQV KYAKKKKTSA VSQ // ID PDM1_DROME STANDARD; PRT; 601 AA. AC P31368; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Nubbin protein (Twain protein) (POU domain protein 1) (PDM-1) (dPOU- DE 19) (DOCT1). GN NUB OR TWN OR PDM-1 OR POU-19 OR OCT1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92001544; PubMed=1680380; RA Billin A.N., Cockerill K.A., Poole S.J.; RT "Isolation of a family of Drosophila POU domain genes expressed in RT early development."; RL Mech. Dev. 34:75-84(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92144419; PubMed=1685891; RA Lloyd A., Sakonju S.; RT "Characterization of two Drosophila POU domain genes, related to RT oct-1 and oct-2, and the regulation of their expression patterns."; RL Mech. Dev. 36:87-102(1991). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=91352045; PubMed=1881906; RA Dick T., Yang X., Yeo S., Chia W.; RT "Two closely linked Drosophila POU domain genes are expressed in RT neuroblasts and sensory elements."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7645-7649(1991). CC -!- FUNCTION: DNA-BINDING REGULATORY PROTEIN IMPLICATED IN EARLY CC DEVELOPMENT. INVOLVED IN NEURONAL CELL FATE DECISION. REPRESSED CC DIRECTLY OR INDIRECTLY BY THE BX-C HOMEOTIC PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: NEUROBLASTS AND SENSORY ELEMENTS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED PRIMARILY DURING THE FIRST HALF OF CC EMBRYOGENESIS. INITIAL EXPRESSION IN CELLULAR BLASTODERM STAGE, CC THEN IN ECTODERMAL STRIPES DURING GERMBAND EXTENSION. BROAD CC EXPRESSION IN THE NEUROECTODERM FOLLOWED BY LIMITATION TO DISCRETE CC SUBSETS OF CNS CELLS, AND EXPRESSION IN SPECIFIC PNS NEURONS AND CC SUPPORT CELLS. CC -!- SIMILARITY: BELONGS TO THE POU TRANSCRIPTION FACTOR FAMILY. CC CLASS-2 SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81957; AAA28829.1; -. DR EMBL; S80561; AAB21409.1; -. DR EMBL; M65015; AAA28480.1; -. DR PIR; B56564; B56564. DR HSSP; P14859; 1OCT. DR TRANSFAC; T01900; -. DR FlyBase; FBgn0002970; nub. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000327; POU_domain. DR InterPro; IPR007103; POU_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00157; pou; 1. DR PRINTS; PR00028; POUDOMAIN. DR ProDom; PD000010; Homeobox; 1. DR ProDom; PD000583; POU_domain; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00352; POU; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00035; POU_1; 1. DR PROSITE; PS00465; POU_2; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Transcription regulation; Nuclear protein; KW Developmental protein. FT DOMAIN 104 107 POLY-HIS. FT DOMAIN 191 201 POLY-ALA. FT DOMAIN 359 364 POLY-HIS. FT DOMAIN 407 415 POLY-ALA. FT DOMAIN 425 495 POU. FT DNA_BIND 523 582 HOMEOBOX. FT CONFLICT 420 420 P -> R (IN REF. 2). SQ SEQUENCE 601 AA; 65202 MW; 8FFCD7B3C162D2B2 CRC64; MVMSELRWHT ASPEDNKNSL KRDLLKSTPT SAREAAVHIM QNRYISRLSR SPSPLQSNAS DCDDNNSSVG TSSDRCRSPL SPALSLSHQQ AKRQLMSLQP HPAHHHHNPH HLNHLNHHQY KQEEDYDDAN GGALNLTSDN SRHSTQSPSN SVKSATASPV PVISVPSPVP PMISPVLAPS GCGSTTPNSM AAAAAAAAAV ASTMGSGISP LLALPGMSSP QAQLAAAGLG MNNPLLTGSL SPQDFAQFHQ LLQQRQVALT QQFNSYMELL RSGSLGLAQD DPALTAQVAA AQFLMQSQLQ ALSQASQQLQ ALQKQQQRQV DEPLQLNHKM TQQPRSSTPH SIRSPIAIRS PASSPQQLHH HHHHPLQITP PSSAASLKLS GMLTPSTPTS GTQMSQGTTT PQPKTVASAA AARAAGEPSP EETTDLEELE QFAKTFKQRR IKLGFTQGDV GLAMGKLYGN DFSQTTISRF EALNLSFKNM CKLKPLLQKW LDDADRTIQA TGGVFDPAAL QATVSTPEII GRRRKKRTSI ETTIRGALEK AFLANQKPTS EEITQLADRL SMEKEVVRVW FCNRRQKEKR INPSLDSPTG ADDDESSYMM H // ID PDM2_DROME STANDARD; PRT; 498 AA. AC P31369; Q24430; Q9VK70; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE POU domain protein 2 (didymous protein) (Pdm-2) (dPOU-28) (dOct2) DE (miti-mere). GN PDM2 OR PDM-2 OR DIM OR POU-28 OR OCT2 OR CG12287. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92144419; PubMed=1685891; RA Lloyd A., Sakonju S.; RT "Characterization of two Drosophila POU domain genes, related to RT oct-1 and oct-2, and the regulation of their expression patterns."; RL Mech. Dev. 36:87-102(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91352045; PubMed=1881906; RA Dick T., Yang X., Yeo S., Chia W.; RT "Two closely linked Drosophila POU domain genes are expressed in RT neuroblasts and sensory elements."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7645-7649(1991). RN [3] RP SEQUENCE OF 68-498 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92001544; PubMed=1680380; RA Billin A.N., Cockerill K.A., Poole S.J.; RT "Isolation of a family of Drosophila POU domain genes expressed in RT early development."; RL Mech. Dev. 34:75-84(1991). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=92357775; PubMed=1496003; RA Prakash K., Fang X.D., Engelberg D., Behal A., Parker C.S.; RT "dOct2, a Drosophila Oct transcription factor that functions in RT yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 89:7080-7084(1992). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: DNA-BINDING REGULATORY PROTEIN IMPLICATED IN EARLY CC DEVELOPMENT. INVOLVED IN NEURONAL CELL FATE DECISION. MAY ACT AS CC AN OCTAMER-DEPENDENT ACTIVATOR OF TRANSCRIPTION. COULD ALSO PLAY CC AN EARLY ROLE IN SPECIFIC ECTODERMAL CELLS, AND A SUBSEQUENT ROLE CC IN THE EMBRYONIC NERVOUS SYSTEM. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: NEUROBLASTS AND SENSORY ELEMENTS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED PRIMARILY DURING THE FIRST HALF OF CC EMBRYOGENESIS. INITIAL EXPRESSION IN CELLULAR BLASTODERM STAGE, CC THEN IN ECTODERMAL STRIPES DURING GERMBAND EXTENSION. BROAD CC EXPRESSION IN THE NEUROECTODERM FOLLOWED BY LIMITATION TO DISCRETE CC SUBSETS OF CNS CELLS, AND EXPRESSION IN SPECIFIC PNS NEURONS AND CC SUPPORT CELLS. CC -!- SIMILARITY: BELONGS TO THE POU TRANSCRIPTION FACTOR FAMILY. CC CLASS-2 SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S80559; AAB21408.1; -. DR EMBL; M65016; AAA28481.1; -. DR EMBL; M81958; AAA28830.2; -. DR EMBL; M93149; AAA28732.1; -. DR EMBL; AE003637; AAF53209.1; -. DR PIR; A56564; A56564. DR HSSP; P14859; 1OCT. DR TRANSFAC; T01901; -. DR FlyBase; FBgn0004394; pdm2. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000327; POU_domain. DR InterPro; IPR007103; POU_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00157; pou; 1. DR PRINTS; PR00028; POUDOMAIN. DR ProDom; PD000010; Homeobox; 1. DR ProDom; PD000583; POU_domain; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00352; POU; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00035; POU_1; 1. DR PROSITE; PS00465; POU_2; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Transcription regulation; Nuclear protein; KW Activator; Developmental protein. FT DOMAIN 5 10 POLY-GLN. FT DOMAIN 74 79 POLY-GLU. FT DOMAIN 290 360 POU. FT DNA_BIND 391 450 HOMEOBOX. FT CONFLICT 221 221 V -> GA (IN REF. 2). FT CONFLICT 223 224 RH -> AR (IN REF. 2). FT CONFLICT 248 248 M -> S (IN REF. 4). FT CONFLICT 447 447 K -> N (IN REF. 4). FT CONFLICT 472 474 PQA -> RRL (IN REF. 2). FT CONFLICT 475 498 MISSING (IN REF. 2). SQ SEQUENCE 498 AA; 55462 MW; 60F17AF776603974 CRC64; MMVLQQQQQQ RLWDATTTSN TNTQTQQSAN VESTPTKVCH QENAATHTFM RHMSNSPTPP SPLRSLSDCG KSFEEEELEL GENCEMPQNL SSKRQARELD SELENEVLDL APPPKRLAEE QEEEKVASVN PPQPVAFAPE EMHQALQLQL HSYIEMVRQL APEAFPNPNL ATQFLLQNSL QALAQFQALQ QMKQQQREDP LPSYSTPLAK SPLRSPSLSP VPRHSKSQQR TPPNSMTANS LGMSSAVMTP NTPSMQQQPQ LQQSTPKPTS GLTVASAMAK LEQSPEETTD LEELEQFAKT FKQRRIKLGF TQGDVGLAMG KLYGNDFSQT TISRFEALNL SFKNMCKLKP LLQKWLEDAD STVAKSGGGV FNINTMTSTL SSTPESILGR RRKKRTSIET TVRTTLEKAF LMNCKPTSEE ISQLSERLNM DKEVIRVWFC NRRQKEKRIN PSLDLDSPTG TPLSSHAFGY PPQALNMSHM QMEGGSGSFC GSSISSGE // ID PDX1_DROME STANDARD; PRT; 194 AA. AC Q9V3P0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Peroxiredoxin 1 (EC 1.11.1.-) (Thioredoxin peroxidase) (Cytosolic DE thioredoxin peroxidase) (DmTPx-1) (DPx-4783). GN JAFRAC1 OR TPX-1 OR CG1633. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20098524; PubMed=10632718; RA Rodriguez J., Agudo M., Van Damme J., Vandekerckhove J., RA Santaren J.F.; RT "Polypeptides differentially expressed in imaginal discs define the RT peroxiredoxin family of genes in drosophila."; RL Eur. J. Biochem. 267:487-497(2000). RN [2] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=21534478; PubMed=11677042; RA Radyuk S.N., Klichko V.I., Spinola B., Sohal R.S., Orr W.C.; RT "The peroxiredoxin gene family in Drosophila melanogaster."; RL Free Radic. Biol. Med. 31:1090-1100(2001). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX MEDLINE=22001321; PubMed=11877442; RA Bauer H., Kanzok S.M., Schirmer R.H.; RT "Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin RT peroxidase-1 from Drosophila melanogaster: isolation and RT characterization of a second thioredoxin in D. melanogaster and RT evidence for distinct biological functions of Trx-1 and Trx-2."; RL J. Biol. Chem. 277:17457-17463(2002). CC -!- FUNCTION: INVOLVED IN REDOX REGULATION OF THE CELL. REDUCES CC PEROXIDES WITH REDUCING EQUIVALENTS PROVIDED THROUGH THE CC THIOREDOXIN SYSTEM BUT NOT FROM GLUTAREDOXIN. MAY PLAY AN CC IMPORTANT ROLE IN ELIMINATING PEROXIDES GENERATED DURING CC METABOLISM. AS A REDUCING SUBSTRATE, THIOREDOXIN 2 IS PREFERRED CC OVER THIOREDOXIN 1. CC -!- SUBUNIT: HOMODIMER; DISULFIDE-LINKED, UPON OXIDATION (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- DEVELOPMENTAL STAGE: HIGHLY EXPRESSED DURING EMBRYOGENESIS, WEAKLY CC EXPRESSED DURING LARVAL STAGES. CC -!- MISCELLANEOUS: THE ACTIVE SITE IS THE REDOX-ACTIVE CYS-47 OXIDIZED CC TO CYS-SOH. CYS-SOH RAPIDLY REACTS WITH CYS-168-SH OF THE OTHER CC SUBUNIT TO FORM AN INTERMOLECULAR DISULFIDE WITH A CONCOMITANT CC HOMODIMER FORMATION. THE ENZYME MAY BE SUBSEQUENTLY REGENERATED BY CC REDUCTION OF THE DISULFIDE BY THIOREDOXIN (BY SIMILARITY). CC -!- MISCELLANEOUS: IRREVERSIBLY INACTIVED BY OVEROXIDATION OF CYS- CC 47 (TO CYS-SO3H) UPON OXIDATIVE STRESS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE AHPC/TSA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF167098; AAF42985.1; -. DR EMBL; AF321616; AAK06771.1; -. DR EMBL; AF321615; AAK06770.1; -. DR EMBL; AE003492; AAF48254.1; -. DR EMBL; AY070534; AAL48005.1; -. DR HSSP; P30041; 1PRX. DR FlyBase; FBgn0040309; Jafrac1. DR GO; GO:0005829; C:cytosol; IDA. DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA. DR GO; GO:0045454; P:cell redox homeostasis; IDA. DR InterPro; IPR000866; AhpC-TSA. DR Pfam; PF00578; AhpC-TSA; 1. KW Antioxidant; Peroxidase; Oxidoreductase; Redox-active center. FT ACT_SITE 47 47 CYSTEINE SULFENIC ACID INTERMEDIATE FT (BY SIMILARITY). FT DISULFID 47 47 INTERCHAIN (WITH C-168) (IN FT LINKED FORM) (BY SIMILARITY). FT DISULFID 168 168 INTERCHAIN (WITH C-47) (IN FT LINKED FORM) (BY SIMILARITY). SQ SEQUENCE 194 AA; 21738 MW; 93ED319BE144E8D1 CRC64; MPQLQKPAPA FAGTAVVNGV FKDIKLSDYK GKYLVLFFYP LDFTFVCPTE IIAFSESAAE FRKINCEVIG CSTDSQFTHL AWINTPRKQG GLGSMDIPLL ADKSMKVARD YGVLDEETGI PFRGLFIIDD KQNLRQITVN DLPVGRSVEE TLRLVQAFQY TDKYGEVCPA NWKPGQKTMV ADPTKSKEYF ETTS // ID PEB1_DROME STANDARD; PRT; 377 AA. AC Q9U6L5; Q9W0W1; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ejaculatory bulb specific protein I precursor (PEB-me). GN PEB OR BCDNA:GH06048 OR CG2668. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [4] RP SEQUENCE OF 77-90 AND 101-109, FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND VARIANT. RC STRAIN=Canton-S; RX MEDLINE=21167515; PubMed=11267893; RA Lung O., Wolfner M.F.; RT "Identification and characterization of the major Drosophila RT melanogaster mating plug protein."; RL Insect Biochem. Mol. Biol. 31:543-551(2001). CC -!- FUNCTION: MAJOR PROTEIN COMPONENT OF THE POSTERIOR MATING PLUG. CC ACCESSORY GLAND PROTEINS CONSTITUTE, OR ARE REQUIRED FOR FORMATION CC OF THE ANTERIOR MATING PLUG. POSTERIOR MATING PLUG FORMS BEFORE CC SPERM TRANSFER AND THE ANTERIOR MATING PLUG IS FORMED AFTER THE CC START OF MATING. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: SPECIFICALLY EXPRESSED IN THE EJACULATORY BULB CC AND SEMINAL FLUID. DETECTED IN MATED FEMALES 3 MINUTES AFTER THE CC START OF MATING, AND FOR AT LEAST 3 HOURS AFTER THE START OF CC MATING. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003466; AAF47319.2; -. DR EMBL; AF184225; AAD55736.1; -. DR FlyBase; FBgn0004181; Peb. KW Behavior; Signal; Polymorphism. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 377 EJACULATORY BULB SPECIFIC PROTEIN I. FT DOMAIN 116 256 PRO-RICH. FT DOMAIN 159 377 GLY-RICH. FT VARIANT 84 84 G -> GANILAG (IN STRAIN CANTON-S). SQ SEQUENCE 377 AA; 37819 MW; D020F027BD96B221 CRC64; MVRQLILVLS LILFCGSSHA VVSELARQSE SAIQGLADIK MAPLRYLDVL FGGNPGGLRG LDGGNSASLS TLQAAKVANI LARGDIASSG YSKISAGVGK GSDLITIIKN TRSYDPYLIP PGIPGYNYPL GWPLRYPLGP YWPNRPPWLP INSPPIRPGG LFPGGPSPGG PSPGEPSPGE PSPGGPSPGG PSPGGPSPGG PSPGGPSPGG PSPGGPFPGG SPPSPGGPLG PWQFPWILGG PRPNRPGRPF PGGILPGHLD GSVVPNSVLN VAGGIFGNGG LFGTGIFGQH GLFGTGFLSG PSLDPFGIFT PIGNFFGSLG NLFGFSSPSQ IIPIFGGKFG PLGRGLQGSI TLDVGGTVPS VKGILGQLLH PFLGFLG // ID PEB2_DROME STANDARD; PRT; 59 AA. AC Q23982; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ejaculatory bulb specific protein II precursor (PEB-meII). GN PEBII OR CG2665. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-RC; TISSUE=Ejaculatory bulb; RX MEDLINE=95344734; PubMed=7619487; RA Dyanov H.M., Dzitoeva S.G.; RT "Method for attachment of microscopic preparations on glass for in RT situ hybridization, PRINS and in situ PCR studies."; RL BioTechniques 18:822-824(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROTEIN COMPONENT OF THE POSTERIOR MATING PLUG (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: SPECIFICALLY EXPRESSED IN THE EJACULATORY BULB CC AND SEMINAL FLUID. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U08282; AAB40023.1; -. DR EMBL; AE003466; AAF47318.1; -. DR FlyBase; FBgn0011694; PebII. KW Behavior; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 59 EJACULATORY BULB SPECIFIC PROTEIN FT II. SQ SEQUENCE 59 AA; 6347 MW; 59C794E76C238F06 CRC64; MITFTLMTGS ALCSIEQLMR VFGGGSVGGG SRLDINRRVT IVPPEGELSF GYGFRPGFY // ID PEB3_DROME STANDARD; PRT; 126 AA. AC Q9W1C9; Q23981; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ejaculatory bulb specific protein III precursor (PEB-meIII). GN PEBIII OR CG11390. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 6-126 FROM N.A. RC STRAIN=Oregon-RC; TISSUE=Ejaculatory bulb; RX MEDLINE=95344734; PubMed=7619487; RA Dyanov H.M., Dzitoeva S.G.; RT "Method for attachment of microscopic preparations on glass for in RT situ hybridization, PRINS and in situ PCR studies."; RL BioTechniques 18:822-824(1995). CC -!- FUNCTION: PROTEIN COMPONENT OF THE POSTERIOR MATING PLUG (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: SPECIFICALLY EXPRESSED IN THE EJACULATORY BULB CC AND SEMINAL FLUID. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003462; AAF47140.2; -. DR EMBL; AY113640; AAM29645.1; -. DR EMBL; U08281; AAA87058.1; -. DR FlyBase; FBgn0011695; PebIII. DR InterPro; IPR005055; A10_OS-D. DR Pfam; PF03392; OS-D; 1. KW Behavior; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 126 EJACULATORY BULB SPECIFIC PROTEIN FT III. FT CONFLICT 6 6 A -> P (IN REF. 4). FT CONFLICT 95 101 PEEWKQL -> ARGVEAA (IN REF. 4). FT CONFLICT 108 108 D -> E (IN REF. 4). FT CONFLICT 117 126 ATAEASGIKV -> QPRGSDQGVRRIRFGNTWYMHCIRSTL FT YLIIKLFLTVGLDLRVWFFP (IN REF. 4). SQ SEQUENCE 126 AA; 14540 MW; 776BF77650F1B14D CRC64; MKMILALVVL GLVLVAAEDK YTTKYDNIDV DEILKSDRLF GNYFKCLVDN GKCTPEGREL KKSLPDALKT ECSKCSEKQR QNTDKVIRYI IENKPEEWKQ LQAKYDPDEI YIKRYRATAE ASGIKV // ID PELO_DROME STANDARD; PRT; 395 AA. AC P48612; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Pelota protein. GN PELO. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=96017658; PubMed=7588080; RA Eberhart C.G., Wasserman S.W.; RT "The pelota locus encodes a protein required for meiotic cell RT division: an analysis of G2/M arrest in Drosophila spermatogenesis."; RL Development 121:3477-3486(1995). CC -!- FUNCTION: REQUIRED PRIOR TO THE FIRST MEIOTIC DIVISION FOR CC SPINDLE FORMATION AND NUCLEAR ENVELOPE BREAKDOWN DURING CC SPERMATOGENESIS. IT IS ALSO REQUIRED FOR NORMAL EYE PATTERNING CC AND FOR MITOTIC DIVISIONS IN THE OVARY. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED THROUGHOUT ALL DEVELOPMENT STAGES. CC HIGHEST LEVELS IN EARLY EMBRYO (0-2H) AND ADULT STAGES. CC -!- SIMILARITY: TO YEAST DOM34, C.ELEGANS R74.6 AND M.JANNASCHII CC MJ0174. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U27197; AAC46879.1; -. DR PIR; T47122; T47122. DR FlyBase; FBgn0011207; pelo. DR InterPro; IPR005140; eRF1_1. DR InterPro; IPR005141; eRF1_2. DR InterPro; IPR005142; eRF1_3. DR InterPro; IPR004405; PelA. DR Pfam; PF03463; eRF1_1; 1. DR Pfam; PF03464; eRF1_2; 1. DR Pfam; PF03465; eRF1_3; 1. DR TIGRFAMs; TIGR00111; pelota; 1. KW Cell division; Meiosis; Mitosis; Nuclear protein. FT DOMAIN 377 383 ASP/GLU-RICH (ACIDIC). SQ SEQUENCE 395 AA; 44170 MW; 86B5A7464449EB38 CRC64; MKLLGKYVDK GMQGNVTLVP EESEDMWHAY NLIAKGDSVR STTIRKVQNE TATGSSTSSR VRTTLTIAVE SIDFDTQACV VRLKGRNIEE NQYVKMGAYH TLDLELNRKF ELRKPEWDTI ALERIEMACD PTQSADVAAV VMQEGLAHVC LITASMTLVR SKIEVSIPRK RKGSVQQHEK GLAKFYEQVM QSILRHVDFD VVKCVLIASP GFVRDQFYDY MFQQAVKMDY KLLLDNKSKF MLVHASSGFK HSLREILQDP AVLAKMSDTK AAGEVKALEQ FYMMLQCEPA KAFYGKKHVL QAAESQAIET LLISDNLFRC QDVSLRKEYV NLVESIRDAG GEVKIFSSMH ISGEQLAQLT GIAALLRFPM PELEDSDDDD DEDGAAGGAA DSDSD // ID PEN2_DROME STANDARD; PRT; 101 AA. AC Q86BE9; Q8MUT4; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gamma-secretase subunit pen-2 (Preselinin enhancer protein 2). GN PEN-2 OR CG33198. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RX MEDLINE=22105644; PubMed=12110170; RA Francis R., McGrath G., Zhang J., Ruddy D.A., Sym M., Apfeld J., RA Nicoll M., Maxwell M., Hai B., Ellis M.C., Parks A.L., Xu W., Li J., RA Gurney M., Myers R.L., Himes C.S., Hiebsch R., Ruble C., Nye J.S., RA Curtis D.; RT "aph-1 and pen-2 are required for Notch pathway signaling, RT gamma-secretase cleavage of betaAPP, and presenilin protein RT accumulation."; RL Dev. Cell 3:85-97(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION IN THE GAMMA-SECRETASE COMPLEX, AND INTERACTION WITH APH-1; RP PSN AND NCT. RX MEDLINE=22547312; PubMed=12660785; RA Takasugi N., Tomita T., Hayashi I., Tsuruoka M., Niimura M., RA Takahashi Y., Thinakaran G., Iwatsubo T.; RT "The role of presenilin cofactors in the gamma-secretase complex."; RL Nature 422:438-441(2003). CC -!- FUNCTION: ESSENTIAL SUBUNIT OF THE GAMMA-SECRETASE COMPLEX, AN CC ENDOPROTEASE COMPLEX THAT CATALYZES THE INTRAMEMBRANE CLEAVAGE OF CC INTEGRAL MEMBRANE PROTEINS SUCH AS NOTCH. IT PROBABLY REPRESENTS CC THE LAST STEP OF MATURATION OF GAMMA-SECRETASE, FACILITATING CC ENDOPROTEOLYSIS OF PRESENILIN AND CONFERING GAMMA-SECRETASE CC ACTIVITY. CC -!- SUBUNIT: COMPONENT OF THE GAMMA-SECRETASE COMPLEX, A COMPLEX CC COMPOSED OF A PRESENILIN/PSN HOMODIMER, NICASTRIN (NCT), APH-1 AND CC PEN-2. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PEN-2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF512426; AAM88323.1; -. DR EMBL; AE003800; AAO41356.1; -. DR FlyBase; FBgn0053198; pen-2. KW Transmembrane. FT DOMAIN 1 17 LUMENAL (POTENTIAL). FT TRANSMEM 18 38 POTENTIAL. FT DOMAIN 39 57 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 58 78 POTENTIAL. FT DOMAIN 79 101 LUMENAL (POTENTIAL). FT CONFLICT 2 2 N -> D (IN REF. 2). FT CONFLICT 56 56 MISSING (IN REF. 2). SQ SEQUENCE 101 AA; 11724 MW; 245A06C24877E208 CRC64; MNISKAPNPR KLELCRKYFF AGFAFLPFVW AINVCWFFTE AFHKPPFSEQ SQIKRYVIYS AVGTLFWLIV LTAWIIIFQT NRTAWGATAD YMSFIIPLGS A // ID PEN_DROME STANDARD; PRT; 737 AA. AC O61345; Q9VRH2; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Penguin protein. GN PEN OR CG1685. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98188272; PubMed=9520435; RA Maleszka R., de Couet H.G., Miklos G.L.G.; RT "Data transferability from model organisms to human beings: insights RT from the functional genomics of the flightless region of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: CONTAINS ? PUMILIO REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF017777; AAC28403.1; -. DR EMBL; AF132165; AAD34753.1; -. DR EMBL; AE003568; AAF50828.1; -. DR PIR; T08427; T08427. DR FlyBase; FBgn0015527; pen. DR InterPro; IPR008938; ARM. DR InterPro; IPR001313; Pumilio/Puf. KW Repeat; RNA-binding. SQ SEQUENCE 737 AA; 81302 MW; C7A4E212A9ED0FDD CRC64; MVSSEPKGPA NVANTASPLK AHESSGKRAN GQKFKPGGAG GARKFDKFGG GAGKSFVKPG AGGAKKFDKS GPGGFKKFDK SGATGDKRLG GNKFRGKPQT QPQAPAEGEK QDWNKFKKEK KDLKLKRKSA KDTYEISKEA NQIHEKLRCR RTENKDKLVE QIYKVLNVGD TISKVVKAHD TARVIQSMLK YASPALRAEI SEKLLPFTVE MCQSKYAQFC VQRMLKYGAP ATKAKLVDSL YGHIVRLAGH SIGSGLLDSM YQSATPNQRI YMRQEFYGDL YRKAKDSNVK TLSDTYKEAT NMKASILGSV KANLDHVANK QLVDSALVHA VMLEYLRACD EDEEKLEETV TAFAALVPHM LSTKEGSEAA VICFYKSTPK NRRAIIKNIK EHLLKIANHE HGHVFLISLL NALDDTKATK KAIYDHLHGD LKALMSSPYG RRVIQWLVAP GDTTCFHPEF IRTVEEGLAF GKKEKELRRK EILEQIEAPI AQSIAEDAAF WLSNSHIGLV TGDILNHIQG ESYEKAASAL AQVVVQPEWR ISADAAGPQP QDKKKPHNDV EAIIAQATKQ RRKLLYVESS SDDEDEDEDE DEESDDEGDE KEQKEAAADD AEPKVKKAKK EPKKPKAKEE EPAAPLVSGI EEAGMHIVLK KILKNDGKRE GTPFSQQLLQ NLSSDVLKAW LGVNRACFVL LKLVEECPAL LDDCKKAIAA ERSLSQILAD RKTPGAKLLA AKLDIGK // ID PEP_DROME STANDARD; PRT; 716 AA. AC P41073; Q9VVJ3; Q9VVJ4; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Zinc finger protein on ecdysone puffs. GN PEP OR CG6143. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91138953; PubMed=1899840; RA Amero S.A., Elgin S.C.R., Beyer A.L.; RT "A unique zinc finger protein is associated preferentially with RT active ecdysone-responsive loci in Drosophila."; RL Genes Dev. 5:188-200(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY PLAY A ROLE IN THE PROCESS OF EARLY AND LATE GENE CC ACTIVATION, OR POSSIBLY IN RNA PROCESSING, FOR A DEFINED SET OF CC DEVELOPMENTALLY REGULATED LOCI. CC -!- SUBCELLULAR LOCATION: NUCLEAR, WHERE IT IS ASSOCIATED WITH THE CC ACTIVE ECDYSONE-REGULATED LOCI ON POLYTENE CHROMOSOMES, AND ON CC SOME HEAT SHOCK-INDUCED PUFFS. ITS DISTRIBUTION PATTERN FOLLOWS CC THE CHANGES OF PUFFING PATTERNS IN THE DEVELOPMENTAL PROGRAM, OR CC FOLLOWING HEAT SHOCK. CC -!- DEVELOPMENTAL STAGE: MATERNAL PEP GENE TRANSCRIPTS ARE PROBABLY CC SUPPLIED TO THE EMBRYO AT EARLY GENE ACTIVATION OR EXPRESSION. THE CC ABUNDANCE OF TRANSCRIPTS THEN DECREASES TO A LOWER, FAIRLY CC CONSTANT LEVEL THEREAFTER. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-24 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56689; CAA40017.1; -. DR EMBL; AE003523; AAF49317.1; -. DR PIR; S26759; S26759. DR FlyBase; FBgn0004401; Pep. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. KW Zinc-finger; DNA-binding; Nuclear protein; Metal-binding. FT DOMAIN 7 166 ASN/GLY-RICH. FT ZN_FING 216 240 C2H2-TYPE. FT ZN_FING 288 310 C2H2-TYPE (ATYPICAL). FT ZN_FING 319 343 C2H2-TYPE. FT DOMAIN 379 383 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 388 466 ASP/GLU-RICH (ACIDIC). FT ZN_FING 489 513 C2H2-TYPE. FT DOMAIN 544 548 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 550 639 ASP/GLU-RICH (ACIDIC). FT DOMAIN 641 709 ALA-RICH. FT DOMAIN 111 116 POLY-GLY. FT DOMAIN 163 166 POLY-GLY. FT DOMAIN 367 370 POLY-GLU. FT DOMAIN 438 441 POLY-GLU. FT DOMAIN 535 538 POLY-ALA. FT DOMAIN 675 678 POLY-ALA. SQ SEQUENCE 716 AA; 78048 MW; 256D7D765C5F3050 CRC64; MVSVKVNGNP QNRLVNNAKV NGNMAFRGNQ NRNRNFGGGN NNYGGPMGAN RMGGMNMSPW ESQNPGGGQF GNNMRQGGGQ MNAQAINLAN NLLNNLFRNQ NPPSLLDLPR GGGGMGNRNQ RGGPMVSRGG GAGNRLNNRR GQGGGFQNRG ATGSGPKPPP KQGGGGIRKQ NAFDRAKKLL AKNANQNKKK EPTPGEKKIE SPTKESPYAS VPNDMFYCHL CKKHMWDANS FENHIKGRTH LMMREGIEES YRLKANMIRQ EAKIAEQLKS IEFDRLKRMG KSKQRQLDYC TMCDLNFHGH ISTHRKSEGH LQLKKFLHPK CIECNKEFAT RIDYDTHLLS AEHLKKAAEN NTKVGERKRQ TLPISTEEEE TRDLRLPQKR KKKPVKKEGE AADGEAKKEG AGDGEGAEGD EAEGEEAKEG EEAADETKEG DELNESQEEE EVALPVDPED CILDFNDGDE IPSEVDTRLP KYNWQRAVGP GLISKLECYE CSVCSKFFDT EVTAEIHSRT ATHHRNFLKF INEKSSDTKI AQKRAAAALE ENERKKRKVE EAEAPAAEGA AEETTEGAEG ELYDPSEATG DDEDVEMVDD NAEGEGEGEG DEEAEAEVEE DGAGQDNGEE EMEAQEEEGQ EGEQEPEPEP APVQTPAPAE PAPPAKTPAK TPTKAAAPAA VASPAAAATS ADASPSPAKK ATPARAAAGA KATPQRQRAR GRYNRY // ID PERO_DROME STANDARD; PRT; 690 AA. AC Q01603; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Peroxidase precursor (EC 1.11.1.7) (DmPO). GN PXD OR PO. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93129626; PubMed=1482687; RA Ng S.W., Wiedemann M., Kontermann R., Petersen G.; RT "Molecular characterization of a putative peroxidase gene of RT Drosophila melanogaster."; RL Biochim. Biophys. Acta 1171:224-228(1992). CC -!- CATALYTIC ACTIVITY: DONOR + H(2)O(2) = OXIDIZED DONOR + 2 H(2)O. CC -!- COFACTOR: BINDS 1 HEME B (IRON-PROTOPORPHYRIN IX) GROUP PER CC SUBUNIT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PEROXIDASE FAMILY. XPO SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X68131; CAA48238.1; -. DR PIR; S28222; S28222. DR HSSP; P05164; 1CXP. DR FlyBase; FBgn0004577; Pxd. DR InterPro; IPR002007; Anim_peroxidase. DR InterPro; IPR002016; Peroxidase. DR Pfam; PF03098; An_peroxidase; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR PROSITE; PS00435; PEROXIDASE_1; FALSE_NEG. DR PROSITE; PS00436; PEROXIDASE_2; FALSE_NEG. DR PROSITE; PS50292; PEROXIDASE_3; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Signal; Glycoprotein. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 690 PEROXIDASE. FT ACT_SITE 185 185 DISTAL HISTIDINE (POTENTIAL). FT ACT_SITE 331 331 DISTAL ARGININE (POTENTIAL). FT METAL 437 437 IRON (HEME AXIAL LIGAND) (BY SIMILARITY). FT CARBOHYD 310 310 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 690 AA; 76733 MW; 4B16CE5411EB73C0 CRC64; MIRARDLLLL ALLGFISSAL GLKVSSGYHI VHNQPQSSFP NYHGFSYLQG SAPYVIGNSL PTSPAPQNPF SSPASPPVSA YGYSFPTAGR VSCAAPPAVC EKTAYRTLDG SCNHLEQPGL GVANSKYGRL LTPKYADGIS APTRSVTGDE LPSARLVSLV AFGEQDVPDP EFTLHNMQWG QIMTHDMSMQ AGGTQSKKHP TRCCTDDGRL IGLDTAHKTC FAIIVPPHDP AYSQVGTECL NFVRTLTDRD SNCQYQGGPA EQLTVVTSYL DLSLVYGNSI QQNSDIREFQ GGRMIVEERN GAKWLPLSRN VTGDCDAVDA SEVCYRSGDV RVNQNPGLAI LQTILLREHN RIADALSALN PHYDDRTLFQ EARKINIAQY QQISYYEWLP IFLGGENMLK NRLIYKAPSG SYINDFDPNI DPSVLNEHAT AAFRYFHSQI EGRLDLLSEL RQVLGSLTLS DWFNRPGIIE VGDNFDSLTR GHATQPEELT DINFDRQIKH FLFRRNMPFG SDLRSLDIQR NRDHGLASYN DMREFCGLRR AHSWEGYGDL ISPPILEKLK SLYPSHEDVD LTVGASLEAH VAGTLAGPTF LCILTEQFYR TRVGDRFFFE NGDKLTGFTP DQLEELRKAS MARLLCDNGN HISSMQPEAF RTVSHSNPII PCSNIPQVDL TKWIDQKPYA TVDPSHYGKK // ID PER_DROME STANDARD; PRT; 1224 AA. AC P07663; O17483; O76882; O76883; O76884; O76885; Q24446; Q24447; AC Q24448; Q24449; Q9W4X0; DT 01-APR-1988 (Rel. 07, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Period circadian protein (Clock-6 protein) (CLK-6). GN PER OR EG:155E2.4 OR CG2647. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS PER-A-LONG; PER-B AND PER-C). RC STRAIN=Oregon-R; RX MEDLINE=87144607; PubMed=3102970; RA Citri Y., Colot H.V., Jacquier A.C., Yu Q., Hall J.C., Baltimore D., RA Rosbash M.; RT "A family of unusually spliced biologically active transcripts encoded RT by a Drosophila clock gene."; RL Nature 326:42-47(1987). RN [2] RP SEQUENCE FROM N.A. (ISOFORM PER-A-LONG). RC STRAIN=Canton-S; RA Baylies M.K., Weiner L., Vosshall L.B., Saez L., Young M.W.; RT "Genetic, molecular and cellular studies of the period locus and its RT products in Drosophila melanogaster."; RL (In) Young M.W. (eds.); RL Molecular genetics of biological rhythms, pp.123-153, Marcel Dekker, RL New York (1993). RN [3] RP SEQUENCE FROM N.A. (ISOFORM PER-A-SHORT). RC STRAIN=Canton-S; RX MEDLINE=86146900; PubMed=3081818; RA Jackson F.R., Bargiello T.A., Yun S.-H., Young M.W.; RT "Product of per locus of Drosophila shares homology with RT proteoglycans."; RL Nature 320:185-188(1986). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS PER-A-LONG; PER-A-SHORT; PER-D AND RP PER-E). RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP SEQUENCE FROM N.A., AND VARIANT (GLY-THR)20. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP SEQUENCE OF 499-1075 FROM N.A., AND VARIANT (GLY-THR)20. RC STRAIN=Oregon-R; RX MEDLINE=86245055; PubMed=3087625; RA Reddy P., Jacquier A.C., Abovich N., Petersen G., Rosbash M.; RT "The period clock locus of D. melanogaster codes for a proteoglycan."; RL Cell 46:53-61(1986). RN [7] RP SEQUENCE OF 63-573 FROM N.A. RX MEDLINE=93170641; PubMed=8436278; RA Kliman R.M., Hey J.; RT "DNA sequence variation at the period locus within and among species RT of the Drosophila melanogaster complex."; RL Genetics 133:375-387(1993). RN [8] RP PHOSPHORYLATION. RX MEDLINE=94181572; PubMed=8134384; RA Edery I., Zwiebel L.J., Dembinska M.E., Rosbash M.; RT "Temporal phosphorylation of the Drosophila period protein."; RL Proc. Natl. Acad. Sci. U.S.A. 91:2260-2264(1994). CC -!- FUNCTION: ESSENTIAL FOR BIOLOGICAL CLOCK FUNCTIONS. DETERMINES THE CC PERIOD LENGTH OF CIRCADIAN AND ULTRADIAN RHYTHMS; AN INCREASE IN CC PER DOSAGE LEADS TO SHORTENED CIRCADIAN RHYTHMS AND A DECREASE CC LEADS TO LENGTHENED CIRCADIAN RHYTHMS. ESSENTIAL FOR THE CIRCADIAN CC RHYTHMICITY OF LOCOMOTOR ACTIVITY, ECLOSION BEHAVIOR, AND FOR THE CC RHYTHMIC COMPONENT OF THE MALE COURTSHIP SONG THAT ORIGINATES IN CC THE THORACIC NERVOUS SYSTEM. THE BIOLOGICAL CYCLE DEPENDS ON THE CC RHYTHMIC FORMATION AND NUCLEAR LOCALIZATION OF THE TIM-PER CC COMPLEX. LIGHT INDUCES THE DEGRADATION OF TIM, WHICH PROMOTES CC ELIMINATION OF PER. NUCLEAR ACTIVITY OF THE HETERODIMER CC COORDINATIVELY REGULATES PER AND TIM TRANSCRIPTION THROUGH A CC NEGATIVE FEEDBACK LOOP. BEHAVES AS A NEGATIVE ELEMENT IN CIRCADIAN CC TRANSCRIPTIONAL LOOP. DOES NOT APPEAR TO BIND DNA, SUGGESTING CC INDIRECT TRANSCRIPTIONAL INHIBITION. CC -!- SUBUNIT: FORMS A HETERODIMER WITH TIMELESS (TIM); THE COMPLEX THEN CC TRANSLOCATES INTO THE NUCLEUS. CC -!- SUBCELLULAR LOCATION: NUCLEAR AT SPECIFIC PERIODS OF THE DAY. CC FIRST ACCUMULATES IN THE PERINUCLEAR REGION ABOUT ONE HOUR BEFORE CC TRANSLOCATION INTO THE NUCLEUS. INTERACTION WITH TIM IS REQUIRED CC FOR NUCLEAR LOCALIZATION. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Comment=Additional isoforms seem to exist; CC Name=PER-A-long; CC IsoId=P07663-1; Sequence=Displayed; CC Name=PER-A-short; CC IsoId=P07663-2; Sequence=VSP_004657; CC Name=PER-B; CC IsoId=P07663-3; Sequence=VSP_004658; CC Name=PER-C; CC IsoId=P07663-4; Sequence=VSP_004660; CC Name=PER-D; CC IsoId=P07663-5; Sequence=VSP_004659; CC Name=PER-E; CC IsoId=P07663-6; Sequence=VSP_004659, VSP_004661; CC -!- TISSUE SPECIFICITY: EXPRESSED IN NEURAL TISSUES AND IN SEVERAL CC NONNEURAL TISSUES OF THE ABDOMEN. MALPIGHIAN TUBULES CONTAIN A CC CIRCADIAN PACEMAKER THAT FUNCTIONS INDEPENDENTLY OF THE BRAIN. CC EXPRESSION OSCILLATES IN ALL TISSUES STUDIED EXCEPT FOR THE OVARY. CC PER-A ISOFORMS ARE MAINLY EXPRESSED IN ADULT'S HEAD. CC -!- INDUCTION: EXPRESSION IS SENSITIVE TO TEMPERATURE BUT NOT TO CC LIGHT. CC -!- DOMAIN: CONTAINS A REMARKABLE RUN OF ALTERNATING GLY-THR RESIDUES CC WHICH IS POLYMORPHIC IN LENGTH. AT LEAST THREE TYPES OF GLY-THR CC LENGTH EXIST IN THE NATURAL POPULATION, (GLY-THR)23 (SHOWN HERE), CC AND TWO MAJOR VARIANTS (GLY-THR)17 AND (GLY-THR)20. THIS GLY-THR CC STRETCH IS IMPLICATED IN THE MAINTENANCE OF CIRCADIAN PERIOD AT CC DIFFERENT TEMPERATURES. DELETION OF THE REPEAT LEADS TO A CC SHORTENING OF THE COURTSHIP SONG CYCLE PERIOD, AND THUS COULD BE CC IMPORTANT FOR DETERMINING FEATURES OF SPECIES-SPECIFIC MATING CC BEHAVIOR. CC -!- DOMAIN: MUTATIONS IN THE PAS DOMAIN RESULT IN LONGER CIRCADIAN CC RHYTHMS AND COURTSHIP SONG (PERL MUTATION) OR MAKES THE FLIES CC ARRHYTHMIC (PER01 MUTATION). CC -!- PTM: PHOSPHORYLATED WITH A CIRCADIAN RHYTHMICITY, PROBABLY BY THE CC DOUBLE-TIME PROTEIN (DBT). PHOSPHORYLATION COULD BE IMPLICATED IN CC THE STABILITY OF PER MONOMER AND IN THE FORMATION OF HETERODIMER CC PER-TIM. CC -!- SIMILARITY: TO OTHER G-T STRETCH CONTAINING PROTEINS. CC -!- SIMILARITY: CONTAINS 2 PAS (PER-ARNT-SIM) DIMERIZATION DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PAS-ASSOCIATED C-TERMINAL (PAC) DOMAIN. CC -!- DATABASE: NAME=Protein Spotlight; NOTE=Issue 6 of January 2001; CC WWW="http://www.expasy.org/spotlight/articles/sptlt006.html". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30114; AAA28752.1; -. DR EMBL; M30114; AAA28753.1; -. DR EMBL; M30114; AAA28754.1; -. DR EMBL; AF033029; AAB87476.1; -. DR EMBL; X03636; CAA27285.1; -. DR EMBL; AL024485; CAA19677.1; -. DR EMBL; AL024485; CAA19678.1; -. DR EMBL; AL024485; CAA19679.1; -. DR EMBL; AL024485; CAA19680.1; -. DR EMBL; AE003425; AAF45804.1; -. DR EMBL; D00009; BAA00007.1; -. DR EMBL; L07817; AAA28777.1; -. DR EMBL; L07818; AAA28776.1; -. DR EMBL; L07819; AAA28775.1; -. DR EMBL; L07821; AAA28773.1; -. DR EMBL; L07823; AAA28771.1; -. DR EMBL; L07825; AAA28769.1; -. DR FlyBase; FBgn0003068; per. DR GO; GO:0005737; C:cytoplasm; NAS. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003712; F:transcription cofactor activity; NAS. DR GO; GO:0007619; P:courtship behavior; NAS. DR GO; GO:0008062; P:eclosion rhythm; NAS. DR GO; GO:0045475; P:locomotor rhythm; NAS. DR GO; GO:0045433; P:male courtship behavior (sensu Insecta), so...; NAS. DR GO; GO:0000122; P:negative regulation of transcription from P...; NAS. DR GO; GO:0045187; P:regulation of sleep; IMP. DR GO; GO:0008341; P:response to cocaine (sensu Insecta); NAS. DR InterPro; IPR000014; PAS_domain. DR Pfam; PF00989; PAS; 2. DR PROSITE; PS50112; PAS; 2. KW Biological rhythms; Repeat; Nuclear protein; Phosphorylation; KW Polymorphism; Alternative splicing. FT DOMAIN 66 79 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 227 297 PAS 1. FT DOMAIN 377 447 PAS 2. FT DOMAIN 459 499 PAC. FT DOMAIN 694 743 G-T REPEATS. FT DOMAIN 74 79 POLY-LYS. FT DOMAIN 143 146 POLY-GLU. FT DOMAIN 223 226 POLY-ALA. FT DOMAIN 872 879 POLY-GLY. FT DOMAIN 898 905 POLY-GLY. FT DOMAIN 906 914 POLY-ALA. FT DOMAIN 1006 1013 POLY-ALA. FT DOMAIN 1035 1041 POLY-ALA. FT DOMAIN 749 868 REGULATES THE RHYTHM OF SPECIES-SPECIFIC FT COURTSHIP SONG. FT VARSPLIC 1 62 Missing (in isoform PER-A-short). FT /FTId=VSP_004657. FT VARSPLIC 868 963 Missing (in isoform PER-B). FT /FTId=VSP_004658. FT VARSPLIC 863 958 Missing (in isoform PER-D and isoform FT PER-E). FT /FTId=VSP_004659. FT VARSPLIC 1076 1224 TTPASMTKKVPGAFHSVTTPAQVQRPSSQSASVKTEPGSSA FT AVSDPCKKEVPDSSPIPSVMGDYNSDPPCSSSNPANNKKYT FT DSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDTEKDPKHR FT KLKSMSTSESKIMEHPEEDQTQHGDG -> VSQWPVVPHRT FT VLTPTPTPYSSIDHAGVHDEEGAGCIPLGHHSCPGAASLLA FT ERIRQDGAGLQCSGIRSLQEGGAGLLAHSLRDGRLQLRPAL FT QQQQSRQQQGMLYE (in isoform PER-C). FT /FTId=VSP_004660. FT VARSPLIC 1155 1224 KYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDTEKDP FT KHRKLKSMSTSESKIMEHPEEDQTQHGDG -> VCYTNEVH FT W (in isoform PER-E). FT /FTId=VSP_004661. FT VARIANT 697 702 MISSING (IN (GLY-THR)20). FT VARIANT 697 708 MISSING (IN (GLY-THR)17). FT CONFLICT 211 211 G -> V (IN REF. 7; AAA28777). FT CONFLICT 498 499 GP -> A (IN REF. 7; AAA28777). FT CONFLICT 637 637 E -> A (IN REF. 6). FT CONFLICT 762 762 T -> S (IN REF. 1, 4 AND 5). FT CONFLICT 762 764 TAA -> RR (IN REF. 3 AND 6). FT CONFLICT 1029 1029 L -> V (IN REF. 6). FT CONFLICT 1038 1038 A -> P (IN REF. 6). FT CONFLICT 1075 1075 T -> TVSQWPV (IN REF. 4; CAA19677). FT CONFLICT 1114 1114 S -> F (IN REF. 1). FT CONFLICT 1215 1215 E -> D (IN REF. 1). SQ SEQUENCE 1224 AA; 127852 MW; 71FA54ECF3E90F4A CRC64; MEGGESTEST HNTKVSDSAY SNSCSNSQSQ RSGSSKSRLS GSHSSGSSGY GGKPSTQASS SDMIIKRNKD KSRKKKKNKG AGQGAGQAQT LISASTSLEG RDEEKPRPSG TGCVEQQICR ELQDQQHGED HSEPQAIEQL QQEEEEDQSG SESEADRVEG VAKSEAAQSF PIPSPLSVTI VPPSMGGCGG VGHAAGLDSG LAKFDKTWEA GPGKLESMTG VGAAAAGTGQ RGERVKEDSF CCVISMHDGI VLYTTPSITD VLGYPRDMWL GRSFIDFVHL KDRATFASQI TTGIPIAESR GSVPKDAKST FCVMLRRYRG LKSGGFGVIG RPVSYEPFRL GLTFREAPEE ARPDNYMVSN GTNMLLVICA TPIKSSYKVP DEILSQKSPK FAIRHTATGI ISHVDSAAVS ALGYLPQDLI GRSIMDFYHH EDLSVMKETY ETVMKKGQTA GASFCSKPYR FLIQNGCYVL LETEWTSFVN PWSRKLEFVV GHHRVFQGPK QCNVFEAAPT CKLKISEEAQ SRNTRIKEDI VKRLAETVSR PSDTVKQEVS RRCQALASFM ETLMDEVSRA DLKLELPHEN ELTVSERDSV MLGEISPHHD YYDSKSSTET PPSYNQLNYN ENLLRFFNSK PVTAPAELDP PKTEPPEPRG TCVSGASGPM SPVHEGSGGS GSSGNFTTAS NIHMSSVTNT SIAGTGGTGT GTGTGTGTGT GTGTGTGTGT GTGTGTGTGT GTGTGTGTGT GTGNGTNSGT GTGTASSSKG GTAAIPPVTL TESLLNKHND EMEKFMLKKH RESRGRTGEK SKKSANDTLK MLEYSGPGHG IKRGGSHSWE GEANKPKQQL TLGTDAIKGA AGSAGGAVGT GGVGSGGAGV AGGGGSGTGV AGTPEGRATT TSGTGTPGGA GGGGGAGAAA AAGASSSVGS STPGPSSYPT CTQNINLWPP FSVGITPPVH STHTAMAQSS FSSAGLFPTF YYIPASLTPT SPTRSPRMHK HPHKGGTDMP TTSQQAAAAA AQAMPLQYMA GVMYPHPSLF YTHPAAAAAT AMMYQPMPFP GMANALQIPE RPLGSQSAYN KSVYTTTPAS MTKKVPGAFH SVTTPAQVQR PSSQSASVKT EPGSSAAVSD PCKKEVPDSS PIPSVMGDYN SDPPCSSSNP ANNKKYTDSN GNSDDMDGSS FSSFYSSFIK TTDGSESPPD TEKDPKHRKL KSMSTSESKI MEHPEEDQTQ HGDG // ID PFD2_DROME STANDARD; PRT; 143 AA. AC Q9VTE5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable prefoldin subunit 2. GN L(3)01239 OR CG6302. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS SPECIFICALLY TO CYTOSOLIC CHAPERONIN (C-CPN) AND CC TRANSFERS TARGET PROTEINS TO IT. BINDS TO NASCENT POLYPEPTIDE CC CHAIN AND PROMOTES FOLDING IN AN ENVIRONMENT IN WHICH THERE ARE CC MANY COMPETING PATHWAYS FOR NONNATIVE PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: HETEROHEXAMER OF TWO PFD-ALPHA TYPE AND FOUR PFD-BETA CC TYPE SUBUNITS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PREFOLDIN BETA SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003546; AAF50107.1; -. DR FlyBase; FBgn0010741; l(3)01239. DR InterPro; IPR002777; PrefoldnKE2. DR Pfam; PF01920; KE2; 1. KW Chaperone. SQ SEQUENCE 143 AA; 16203 MW; CC9209FB4271DDC1 CRC64; MSTESAKPAL SQEAIVAQFQ QLRNEQRNLV NSLNTLEMDL REHKTVIETL EAADPERKCF RQIGGVLCER TVKEVLPQLV ENKDFIAKTI QMVTNDLSKK GSELNKFKEE HNIKIRGEHL VAEGAKGDDA EDKAENRNVL VFN // ID PGK_DROME STANDARD; PRT; 415 AA. AC Q01604; Q9VQF6; DT 01-APR-1993 (Rel. 25, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Phosphoglycerate kinase (EC 2.7.2.3). GN PGK OR CG3127. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93101123; PubMed=1465095; RA Roselli-Rehfuss L., Ye F., Lissemore J.L., Sullivan D.T.; RT "Structure and expression of the phosphoglycerate kinase (Pgk) gene RT of Drosophila melanogaster."; RL Mol. Gen. Genet. 235:213-220(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: ATP + 3-PHOSPHO-D-GLYCERATE = ADP + 3- CC PHOSPHO-D-GLYCEROYL PHOSPHATE. CC -!- PATHWAY: SECOND PHASE OF GLYCOLYSIS; SECOND STEP. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE PHOSPHOGLYCERATE KINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z14029; CAA78404.1; -. DR EMBL; AE003582; AAF51218.1; -. DR PIR; S30111; KIFFPG. DR HSSP; P00560; 1QPG. DR FlyBase; FBgn0003075; Pgk. DR InterPro; IPR001576; PGK. DR Pfam; PF00162; PGK; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. KW Transferase; Kinase; Glycolysis. FT CONFLICT 410 410 A -> R (IN REF. 1). SQ SEQUENCE 415 AA; 43861 MW; 7D1225FCC81F8B42 CRC64; MAFNKLSIEN LDLAGKRVLM RVDFNVPIKE GKITSNQRIV AALDSIKLAL SKKAKSVVLM SHLGRPDGNK NIKYTLAPVA AELKTLLGQD VIFLSDCVGS EVEAACKDPA PGSVILLENV RFYVEEEGKG LDASGGKVKA DPAKVKEFRA SLAKLGDVYV NDAFGTAHRA HSSMMGDGFE QRAAGLLLNK ELKYFSQALD KPPNPFLAIL GGAKVADKIQ LIENLLDKVN EMIIGGGMAF TFLKVLNNMK IGGSLFDEEG SKIVEKLVEK AKKNNVQLHL PVDFVCGDKF AENAAVSEAT VEAGIPDGHM GLDVGPKTRE LFAAPIARAK LIVWNGPPGV FEFPNFANGT KSIMDGVVAA TKNGTVSIIG GGDTASCCAK WNTEALVSHV STGGGASLEL LEGKTLPGVA ALTSA // ID PH4H_DROME STANDARD; PRT; 452 AA. AC P17276; O46110; Q27599; Q27600; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Protein henna [Includes: Phenylalanine-4-hydroxylase (EC 1.14.16.1) DE (PAH) (Phe-4-monooxygenase); Tryptophan 5-monooxygenase (EC 1.14.16.4) DE (TRH) (Tryptophan 5-hydroxylase)]. GN HN OR TPH OR PAH OR CG7399. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo, and Head; RX MEDLINE=92156168; PubMed=1371286; RA Neckameyer W.S., White K.; RT "A single locus encodes both phenylalanine hydroxylase and tryptophan RT hydroxylase activities in Drosophila."; RL J. Biol. Chem. 267:4199-4206(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91033030; PubMed=2121612; RA Morales G., Requena J.M., Jimenez-Ruiz A., Lopez M.C., Ugarte M., RA Alonso C.; RT "Sequence and expression of the Drosophila phenylalanine hydroxylase RT mRNA."; RL Gene 93:213-219(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96332435; PubMed=8769124; RA Ruiz-Vazquez P., Moulard M., Silva F.J.; RT "Structure of the phenylalanine hydroxylase gene in Drosophila RT melanogaster and evidence of alternative promoter usage."; RL Biochem. Biophys. Res. Commun. 225:238-242(1996). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 5-93 AND 161-412 FROM N.A. (MUTANT HN-R3). RX MEDLINE=99266112; PubMed=10333570; RA Ruiz-Vazquez P., Silva F.J.; RT "Aberrant splicing of the Drosophila melanogaster phenylalanine RT hydroxylase pre-mRNA caused by the insertion of a B104/roo RT transposable element in the Henna locus."; RL Insect Biochem. Mol. Biol. 29:311-318(1999). CC -!- CATALYTIC ACTIVITY: L-PHENYLALANINE + TETRAHYDROBIOPTERIN + O(2) = CC L-TYROSINE + 4-ALPHA-HYDROXYTETRAHYDROBIOPTERIN. CC -!- CATALYTIC ACTIVITY: L-TRYPTOPHAN + TETRAHYDROBIOPTERIN + O(2) = 5- CC HYDROXY-L-TRYPTOPHAN + 4-ALPHA-HYDROXYTETRAHYDROBIOPTERIN. CC -!- COFACTOR: FERROUS ION. CC -!- ENZYME REGULATION: N-TERMINAL REGION OF PAH IS THOUGHT TO CONTAIN CC ALLOSTERIC BINDING SITES FOR PHENYLALANINE AND TO CONSTITUTE AN CC "INHIBITORY" DOMAIN THAT REGULATES THE ACTIVITY OF A CATALYTIC CC DOMAIN IN THE C-TERMINAL PORTION OF THE MOLECULE. CC -!- PATHWAY: CATABOLISM OF PHENYLALANINE; FIRST (RATE-LIMITING) STEP. CC -!- TISSUE SPECIFICITY: PHENYLALANINE HYDROLASE ACTIVITY IS FOUND IN CC YOLK GRANULES OF EMBRYOS, AND FEMALE ABDOMEN AND FAT BODY TISSUES. CC TRYPTOPHAN HYDROXYLASE IS EXPRESSED IN SEROTONERGIC NEURONS. CC BOTH ENZYMES ARE PRESENT IN CUTICULAR TISSUES. CC -!- MISCELLANEOUS: IN DROSOPHILA, THE 2 ENZYMES, PAH AND TRH ARE FOUND CC TO BE ENCODED BY THE SAME GENE. PREFERENCE FOR THE SUBSTRATE IS CC PROBABLY DUE TO POST-TRANSLATIONAL MODIFICATIONS SUCH AS CC PHOSPHORYLATION, OR BY CHANGES IN THE N-TERMINAL REGULATORY CC DOMAIN. CC -!- SIMILARITY: BELONGS TO THE BIOPTERIN-DEPENDENT AROMATIC AMINO ACID CC HYDROXYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81833; -; NOT_ANNOTATED_CDS. DR EMBL; M32802; AAA69513.1; -. DR EMBL; X98116; CAA66797.1; -. DR EMBL; X98116; CAA66798.1; -. DR EMBL; AE003558; AAF50517.1; -. DR EMBL; AY069306; AAL39451.1; -. DR EMBL; AJ001718; CAA04950.1; -. DR EMBL; AJ001719; CAB51601.1; -. DR EMBL; AJ001720; CAB51601.1; JOINED. DR EMBL; AJ001722; CAB51599.1; -. DR EMBL; AJ001723; CAB51597.1; -. DR PIR; A42271; A42271. DR PIR; JC4888; JC4888. DR PIR; JQ0766; JQ0766. DR HSSP; P00439; 2PAH. DR FlyBase; FBgn0001208; Hn. DR InterPro; IPR001273; Aaa_hydroxylase. DR InterPro; IPR002912; ACT. DR InterPro; IPR005961; Phenylala4OhaseM. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00351; biopterin_H; 1. DR PRINTS; PR00372; FYWHYDRXLASE. DR ProDom; PD002559; Aaa_hydroxylase; 1. DR TIGRFAMs; TIGR01268; Phe4hydrox_tetr; 1. DR PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1. KW Oxidoreductase; Monooxygenase; Allosteric enzyme; KW Phenylalanine catabolism; Iron; Serotonin biosynthesis; KW Phosphorylation. FT MOD_RES 272 272 PHOSPHORYLATION (BY CAMK2) (BY FT SIMILARITY). FT METAL 284 284 IRON (BY SIMILARITY). FT METAL 289 289 IRON (BY SIMILARITY). FT METAL 329 329 IRON (BY SIMILARITY). FT CONFLICT 28 28 E -> A (IN REF. 2). FT CONFLICT 39 47 KDSSLSSGA -> RIRRCPAEL (IN REF. 2). FT CONFLICT 55 56 FK -> LR (IN REF. 2). FT CONFLICT 63 71 VHIESRSSL -> CILSRILAPWF (IN REF. 2). FT CONFLICT 74 114 PGYEFFVEADGKSGALGKAIEDVKEQCSYFNIISRDYKDNA FT -> SSCFWRRMENRSLGKSHRGCEGAMLATLTSSCRELQGV FT MP (IN REF. 2). FT CONFLICT 154 154 R -> A (IN REF. 2). FT CONFLICT 164 164 A -> G (IN REF. 2). FT CONFLICT 171 171 E -> Q (IN REF. 2). FT CONFLICT 264 264 S -> C (IN REF. 2). FT CONFLICT 297 297 A -> S (IN REF. 2). FT CONFLICT 332 332 V -> L (IN REF. 1 AND 2). FT CONFLICT 333 335 CRQ -> LAK (IN REF. 2). FT CONFLICT 370 370 V -> S (IN REF. 2). FT CONFLICT 449 452 KLRV -> NCASE (IN REF. 1). SQ SEQUENCE 452 AA; 51660 MW; 990F554150056867 CRC64; MYQRQVSFDK PTRVEDSAYI VEGVDIKEAR NTCLLFSPKD SSLSSGALAN ILAIFKKHDI NLVHIESRSS LRVPGYEFFV EADGKSGALG KAIEDVKEQC SYFNIISRDY KDNATAVPWF PRRIRDLDRF ANQILSYGSE LDADHPGFTD PEYRKRRKYF ADIAYNYKHG EPLPHVDYTK EEIETWGIIF RNLTKLYKTH ACREYNHVFP LLVDNCGFRE DNIPQLEDVS NFLRDCTGFT LRPVAGLLSS RDFLAGLAFR VFHSTQYIRH PSKPMYTPEP DVCHELMGHV PLFADPAFAQ FSQEIGLASL GAPDDYIEKL STIFWFTVEY GVCRQEGELK AYGAGLLSSY GELEYCLTDK PQLKDFEPEV TGVTKYPITQ FQPLYYVADS FETAKEKTIK FANSIPRPFG VRYNAYTQSV EVLDSKPQIS NLMDNINSEF QILQNAVAKL RV // ID PHO_DROME STANDARD; PRT; 520 AA. AC Q8ST83; O76247; Q9V4A3; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polycomb protein PHO (Pleiohomeotic protein) (Transcription factor YY1 DE homolog). GN PHO OR CG17743. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND DNA-BINDING ACTIVITY. RC TISSUE=Embryo; RX MEDLINE=98315389; PubMed=9651589; RA Brown J.L., Mucci D., Whiteley M., Dirksen M.-L., Kassis J.A.; RT "The Drosophila Polycomb group gene pleiohomeotic encodes a DNA RT binding protein with homology to the transcription factor YY1."; RL Mol. Cell 1:1057-1064(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 48-373 FROM N.A. RC STRAIN=253.30, 253.27, Closs10, Closs19, North7.13, Rio, South1.10, RC Y10, ZH56, and ZW30; RX MEDLINE=21636764; PubMed=11778050; RA Wang W., Thornton K., Berry A., Long M.; RT "Nucleotide variation along the Drosophila melanogaster fourth RT chromosome."; RL Science 295:134-137(2002). RN [6] RP FUNCTION. RX MEDLINE=99365279; PubMed=10433918; RA Fritsch C., Brown J.L., Kassis J.A., Mueller J.; RT "The DNA-binding Polycomb group protein pleiohomeotic mediates RT silencing of a Drosophila homeotic gene."; RL Development 126:3905-3913(1999). RN [7] RP LACK OF INTERACTION WITH THE PRC1 POLYCOMB COMPLEX. RX MEDLINE=20545168; PubMed=11092813; RA Poux S., McCabe D., Pirrotta V.; RT "Recruitment of components of Polycomb group chromatin complexes in RT Drosophila."; RL Development 128:75-85(2001). RN [8] RP IDENTIFICATION IN A COMPLEX WITH RPD3, ESC AND E(Z), AND TRANSIENT RP INTERACTION WITH THE PRC1 COMPLEX. RX MEDLINE=21464651; PubMed=11581156; RA Poux S., Melfi R., Pirrotta V.; RT "Establishment of Polycomb silencing requires a transient interaction RT between PC and ESC."; RL Genes Dev. 15:2509-2514(2001). CC -!- FUNCTION: POLYCOMB GROUP (PCG) PROTEIN THAT BINDS TO THE 5'- CC CNGCCATNNNNG-3' SEQUENCE FOUND IN THE REGULATORY REGIONS OF MANY CC GENES. PCG PROTEINS ACT BY FORMING MULTIPROTEIN COMPLEXES, WHICH CC ARE REQUIRED TO MAINTAIN THE TRANSCRIPTIONALLY REPRESSIVE STATE OF CC HOMEOTIC GENES THROUGHOUT DEVELOPMENT. PCG PROTEINS ARE NOT CC REQUIRED TO INITIATE REPRESSION, BUT TO MAINTAIN IT DURING LATER CC STAGES OF DEVELOPMENT. THEY PROBABLY ACT VIA THE METHYLATION OF CC HISTONES, RENDERING CHROMATIN HERITABLY CHANGED IN ITS CC EXPRESSIBILITY. PROBABLY TARGETS THE ESC/E(Z) COMPLEX TO DNA. CC NECESSARY BUT NOT SUFFICIENT TO RECRUIT A FUNCTIONAL PCG CC REPRESSIVE COMPLEX THAT REPRESSES TARGET GENES, SUGGESTING THAT CC THE RECRUITMENT OF THE DISTINCT PRC1 COMPLEX IS ALSO REQUIRED TO CC ALLOW A SUBSEQUENT REPRESSION. CC -!- SUBUNIT: COMPONENT OF THE ESC/E(Z) COMPLEX, COMPOSED OF ESC, E(Z), CC SU(Z)12, RPD3 AND CAF1. THIS COMPLEX IS DISTINCT FROM THE PRC1 CC COMPLEX, WHICH CONTAINS MANY OTHER PCG PROTEINS LIKE PC, PH, PSC, CC SU(Z)2. THE TWO COMPLEXES HOWEVER COOPERATE AND INTERACT TOGETHER CC DURING THE FIRST 3 HOURS OF DEVELOPMENT TO ESTABLISH PCG CC SILENCING. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: MATERNALLY AND ZYGOTICALLY EXPRESSED. CC -!- SIMILARITY: CONTAINS 4 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF034212; AAC39123.1; -. DR EMBL; AE003846; AAF59378.2; -. DR EMBL; AY071143; AAL48765.1; -. DR EMBL; AF433865; AAM18016.1; -. DR EMBL; AF433866; AAM18017.1; -. DR EMBL; AF433867; AAM18018.1; -. DR EMBL; AF433868; AAM18019.1; -. DR EMBL; AF433869; AAM18020.1; -. DR EMBL; AF433870; AAM18021.1; -. DR EMBL; AF433871; AAM18022.1; -. DR EMBL; AF433872; AAM18023.1; -. DR EMBL; AF433873; AAM18024.1; -. DR EMBL; AF433874; AAM18025.1; -. DR HSSP; P25490; 1UBD. DR FlyBase; FBgn0002521; pho. DR GO; GO:0000790; C:nuclear chromatin; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0006342; P:chromatin silencing; NAS. DR GO; GO:0048096; P:chromatin-mediated maintenance of transcrip...; IDA. DR InterPro; IPR007087; Znf_C2H2. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. KW Transcription regulation; Repressor; Developmental protein; KW Nuclear protein; DNA-binding; Metal-binding; Zinc; Zinc-finger; KW Repeat. FT ZN_FING 357 381 C2H2-TYPE 1. FT ZN_FING 386 408 C2H2-TYPE 2. FT ZN_FING 414 438 C2H2-TYPE 3. FT ZN_FING 444 468 C2H2-TYPE 4. SQ SEQUENCE 520 AA; 58223 MW; 95E729571C5194E1 CRC64; MAYERFGIIL QSEQYDEDIG NTKVNQKMNE GNHYDLHRKN AFDRIIHSES KKGDNVINYN IHENDKIKAA DNIFSSKLKM NPNMSYEMNI NCFKNIGYGE NQETSKVLTN SLSNNDINTE ESGVVDKNSP FLTLGTTILN SNGKSRRWEQ KLVHIKTMEG EFSVTMWASG ISDDEYSGSD QIVGASDLLK GKEEFGIDGF TSQQNKEYQK MESKFTNAQT LEMPHPISSV QIMDHLIKER GNLSQENNIS ERILSKTTLS FEEPILLPDS SSIELVNETA AMTINNHRTL SNHTGNTGDL HALPSSVPFR IGLHEGQVND CLSTISQSTH QDNTDSTGCG EMNLSEVTVS YTNDKKIACP HKGCNKHFRD SSAMRKHLHT HGPRVHVCAE CGKAFVESSK LKRHQLVHTG EKPFQCTFEG CGKRFSLDFN LRTHVRIHTG DRPFVCPFDA CNKKFAQSTN LKSHILTHAK AKRNTSISGK SGCSNAESNS QSEDTSANYV KVELQDSVTE NHVPFVVYAD // ID PHP_DROME STANDARD; PRT; 1589 AA. AC P39769; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polyhomeotic-proximal chromatin protein. GN PH-P. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Imaginal disks; RX MEDLINE=92146957; PubMed=1346609; RA Decamillis M., Cheng N.S., Pierre D., Brock H.W.; RT "The polyhomeotic gene of Drosophila encodes a chromatin protein that RT shares polytene chromosome-binding sites with Polycomb."; RL Genes Dev. 6:223-232(1992). RN [2] RP SEQUENCE OF 199-1584 FROM N.A. RX MEDLINE=92039031; PubMed=1937015; RA Deatrick J., Daly M., Randsholt N.B., Brock H.W.; RT "The complex genetic locus polyhomeotic in Drosophila melanogaster RT potentially encodes two homologous zinc-finger proteins."; RL Gene 105:185-195(1991). CC -!- FUNCTION: BINDS TO POLYTENE CHROMOSOMES. SEEMS TO INTERACT WITH CC PC. MAY INTERACT WITH PROTEINS ALREADY BOUND TO PROMOTER CC COMPLEXES AND MAY BE A NEGATIVE REGULATOR OF HOMEOTIC AND CC SEGMENTATION GENES. PLAYS A ROLE IN REGULATING THE EXPRESSION OF CC OTHER PAIR-RULE GENES SUCH AS EVE, FTZ, AND H. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: SALIVARY GLANDS. CC -!- SIMILARITY: CONTAINS 1 STERILE ALPHA MOTIF (SAM) DOMAIN. CC -!- SIMILARITY: TO MOUSE EARLY DEVELOPMENT REGULATOR PROTEIN RAE-28. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-9 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63672; CAA45211.1; -. DR EMBL; M64750; -; NOT_ANNOTATED_CDS. DR PDB; 1KW4; 05-JUN-02. DR FlyBase; FBgn0004861; ph-p. DR GO; GO:0016458; P:gene silencing; IGI. DR InterPro; IPR001660; SAM. DR Pfam; PF00536; SAM; 1. DR SMART; SM00454; SAM; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. KW Zinc-finger; Developmental protein; DNA-binding; Nuclear protein; KW 3D-structure. FT ZN_FING 1365 1387 C4-TYPE. FT DOMAIN 1513 1577 SAM. FT DOMAIN 74 80 POLY-GLN. FT DOMAIN 411 450 GLN-RICH. FT DOMAIN 494 520 GLN-RICH. FT DOMAIN 619 650 GLN-RICH. FT DOMAIN 775 960 GLN-RICH. FT DOMAIN 1233 1290 SER/THR-RICH. FT CONFLICT 254 254 MISSING (IN REF. 2). FT CONFLICT 1415 1415 D -> A (IN REF. 2). SQ SEQUENCE 1589 AA; 167297 MW; A6DF0CF9106E1891 CRC64; MDRRALKFMQ KRADTESDTT TPVSTTASQG ISASAILAGG TLPLKDNSNI REKPLHHNYN HNNNNSSQHS HSHQQQQQQQ VGGKQLERPL KCLETLAQKA GITFDEKYDV ASPPHPGIAQ QQATSGTGPA TGSGSVTPTS HRHGTPPTGR RQTHTPSTPN RPSAPSTPNT NCNSIARHTS LTLEKAQNPG QQVAATTTVP LQISPEQLQQ FYASNPYAIQ VKQEFPTHTT SGSGTELKHA TNIMEVQQQL QLQQQLSEAN GGGAASAGAG GAASPANSQQ SQQQQHSTAI STMSPMQLAA ATGGVGGDWT QGRTVQLMQP STSFLYPQMI VSGNLLHPGG LGQQPIQVIT AGKPFQGNGP QMLTTTTQNA KQMIGGQAGF AGGNYATCIP TNHNQSPQTV LFSPMNVISP QQQQNLLQSM AAAAQQQQLT QQQQQFNQQQ QQQLTQQQQQ LTAALAKVGV DAQGKLAQKV VQKVTTTSSA VQAATGPGST GSTQTQQVQQ VQQQQQQTTQ TTQQCVQVSQ STLPVGVGGQ SVQTAQLLNA GQAQQMQIPW FLQNAAGLQP FGPNQIILRN QPDGTQGMFI QQQPATQTLQ TQQNQIIQCN VTQTPTKART QLDALAPKQQ QQQQQVGTTN QTQQQQLAVA TAQLQQQQQQ LTAAALQRPG APVMPHNGTQ VRPASSVSTQ TAQNQSLLKA KMRNKQQPVR PALATLKTEI GQVAGQNKVV GHLTTVQQQQ QATNLQQVVN AAGNKMVVMS TTGTPITLQN GQTLHAATAA GVDKQQQQLQ LFQKQQILQQ QQMLQQQIAA IQMQQQQAAV QAQQQQQQQV SQQQQVNAQQ QQAVAQQQQA VAQAQQQQRE QQQQVAQAQA QHQQALANAT QQILQVAPNQ FITSHQQQQQ QQLHNQLIQQ QLQQQAQAQV QAQVQAQAQQ QQQQREQQQN IIQQIVVQQS GATSQQTSQQ QQHHQSGQLQ LSSVPFSVSS STTPAGIATS SALQAALSAS GAIFQTAKPG TCSSSSPTSS VVTITNQSST PLVTSSTVAS IQQAQTQSAQ VHQHQQLISA TIAGGTQQQP QGPPSLTPTT NPILAMTSMM NATVGHLSTA PPVTVSVTST AVTSSPGQLV LLSTASSGGG GSIPATPTKE TPSKGPTATL VPIGSPKTPV SGKDTCTTPK SSTPATVSAS VEASSSTGEA LSNGDASDRS STLSKGATTP TSKQSNAAVQ PPSSTTPNSV SGKEEPKLAT CGSLTSATST STTTTITNGI GVARTTASTA VSTASTTTTS SGTFITSCTS TTTTTTSSIS NGSKDLPKAM IKPNVLTHVI DGFIIQEANE PFPVTRQRYA DKDVSDEPPK KKATMQEDIK LSGIASAPGS DMVACEQCGK MEHKAKLKRK RYCSPGCSRQ AKNGIGGVGS GETNGLGTGG IVGVDAMALV DRLDEAMAEE KMQTEATPKL SESFPILGAS TEVPPMSLPV QAAISAPSPL AMPLGSPLSV ALPTLAPLSV VTSGAAPKSS EVNGTDRPPI SSWSVDDVSN FIRELPGCQD YVDDFIQQEI DGQALLLLKE KHLVNAMGMK LGPALKIVAK VESIKEVPPP GEAKDPGAQ // ID PHSG_DROME STANDARD; PRT; 844 AA. AC Q9XTL9; Q9V467; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glycogen phosphorylase (EC 2.4.1.1). GN GLYP OR GLP1 OR BCDNA:LD24485 OR CG7254. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=99194550; PubMed=10092506; RA Tick G., Cserpan I., Dombradi V., Mechler B.M., Toeroek I., Kiss I.; RT "Structural and functional characterization of the Drosophila glycogen RT phosphorylase gene."; RL Biochem. Biophys. Res. Commun. 257:34-34(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: PHOSPHORYLASE IS AN IMPORTANT ALLOSTERIC ENZYME IN CC CARBOHYDRATE METABOLISM. ENZYMES FROM DIFFERENT SOURCES DIFFER IN CC THEIR REGULATORY MECHANISMS AND IN THEIR NATURAL SUBSTRATES. CC HOWEVER, ALL KNOWN PHOSPHORYLASES SHARE CATALYTIC AND STRUCTURAL CC PROPERTIES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: {(1,4)-ALPHA-D-GLUCOSYL}(N) + PHOSPHATE = CC {(1,4)-ALPHA-D-GLUCOSYL}(N-1) + ALPHA-D-GLUCOSE 1-PHOSPHATE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GLYCOGEN PHOSPHORYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF073177; AAD41649.1; -. DR EMBL; AF073178; AAD27759.1; -. DR EMBL; AF073179; AAD27760.1; -. DR EMBL; AE003584; AAF51303.1; -. DR EMBL; AF160947; AAD46887.1; -. DR HSSP; P00489; 1PYG. DR FlyBase; FBgn0004507; GlyP. DR InterPro; IPR000811; Glyco_trans_35. DR Pfam; PF00343; phosphorylase; 1. DR PROSITE; PS00102; PHOSPHORYLASE; 1. KW Transferase; Glycosyltransferase; Carbohydrate metabolism; KW Glycogen metabolism; Pyridoxal phosphate. FT BINDING 681 681 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT VARIANT 642 642 K -> N (IN STRAIN CANTON-S). SQ SEQUENCE 844 AA; 96996 MW; 0A65C5B9DCA060ED CRC64; MSKPQSDADR RKQISVRGIA EVGNVTEVKK NFNRHLHYTL VKDRNVSTLR DYYFALANTV KDNMVGRWIR TQQHYYEKDP KRVYYLSLEY YMGRSLTNTM INLGIQSECE EAMYQLGLDI ENLEEMEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFAQK IKNGEQVEEP DDWLRYGNPW EKARPEFMLP VNFYGRVIDT PEGKKWVDTQ RVFAMPYDNP IPGYNNNHVN TLRLWSAKSP IDFNLKFFND GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFM CAATLQDIIR RYKASKFGSR EAVRNTFDHF PDKVAIQLND THPSLAIPEL MRILVDEEHL TWEKAWDITV RSCAYTNHTV LPEALERWPV SLLESILPRH LQIIYHINFL HMENVKKKFP DDLDRMRRMS MVEEDGEKRI NMAHLSIVGS HAVNGVAAIH SQILKDSLFH DFYEMEPQKF QNKTNGITPR RWLLLCNPGL SDLIAEKIGD EWPVHLDQLV ALKKWAKDPN FQRNVARVKQ ENKLKLAAIL EKDYGVKINP SSMFDIQVKR IHEYKRQLLN CLHIITLYNR IKKDPTANFT PRTIMIGGKA APGYYVAKQI IKLICAVGNV VNNDPIVGDK LKVIFLENYR VTLAEKIMPA ADLSEQISTA GTEASGTGNM KFQLNGALTI GTLDGANVEM AEEMGLDNIF IFGMTVDEVE ALKKKGYNAY DYYNANPEVK QVIDQIQGGF FSPGNPNEFK NIADILLKYD HYYLLADYDA YIKAQDLVSK TYQNQAKWLE MSINNIASSG KFSSDRTIAE YAREIWGVEP TWEKLPAPED QPQN // ID PHS_DROME STANDARD; PRT; 101 AA. AC O76454; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pterin-4-alpha-carbinolamine dehydratase (EC 4.2.1.96) (PHS) (4-alpha- DE hydroxy-tetrahydropterin dehydratase) (Pterin carbinolamine DE dehydratase) (PCD). GN PCD OR CG1963. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Park D., Seong C., Yoon J., Jeong S., Oh Y., Yin J., Han K., Baek K.; RT "Molecular characterization of the Drosophila gene encoding the RT pterin-4a-carbinolamine dehydratase."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: (6R)-6-(L-ERYTHRO-1,2-DIHYDROXYPROPYL)- CC 5,6,7,8-TETRAHYDRO-4A-HYDROXYPTERIN = (6R)-6-(L-ERYTHRO-1,2- CC DIHYDROXYPROPYL)-7,8-DIHYDRO-6H-PTERIN + H(2)O. CC -!- SIMILARITY: BELONGS TO THE PTERIN-4-ALPHA-CARBINOLAMINE CC DEHYDRATASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF069297; AAC25196.1; -. DR EMBL; AE003770; AAF56923.1; -. DR HSSP; P80095; 1DCO. DR FlyBase; FBgn0024841; Pcd. DR InterPro; IPR001533; Trans_pterinDh. DR Pfam; PF01329; Pterin_4a; 1. DR ProDom; PD007262; Trans_pterinDh; 1. KW Lyase. SQ SEQUENCE 101 AA; 11503 MW; 5E8B920EE4AE5254 CRC64; MVVRLNEQER AEKLQPLLDA GWTLVEGRDA IFKQFVLKDF NQAFSFMTGV ALLAEKINHH PEWFNCYNKV DVTLSTHDVG GLSSQDIRMA THLETTANLL K // ID PHTF_DROME STANDARD; PRT; 880 AA. AC Q9V9A8; Q9TW25; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative homeodomain transcription factor. GN PHTF OR BCDNA:GH08636 OR CG3268. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=20195633; PubMed=10729229; RA Manuel A., Beaupain D., Romeo P.H., Raich N.; RT "Molecular characterization of a novel gene family (PHTF) conserved RT from Drosophila to mammals."; RL Genomics 64:216-220(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: MAY PLAY A ROLE IN TRANSCRIPTION REGULATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ242938; CAB62168.1; -. DR EMBL; AE003790; AAM70823.1; -. DR EMBL; AF181638; AAD55424.1; -. DR FlyBase; FBgn0028579; phtf. DR InterPro; IPR001092; HLH_basic. DR PROSITE; PS50888; HLH; FALSE_NEG. KW Transcription regulation; DNA-binding; Nuclear protein. FT DNA_BIND 815 833 BASIC DOMAIN. FT DOMAIN 834 867 HELIX-LOOP-HELIX MOTIF. SQ SEQUENCE 880 AA; 97634 MW; 3A39AC6A5BBB8E18 CRC64; MKLDEIVAWY QKRIGTYDKQ EWEKTVEQRI LDGFNSVNLK NTKLKTELID VDLVRGSTFP KAKPKQSLLT VIRLAILRYV LLPLYAQWWV KQTTPNAFGF ILVLYLTQLT NWAIYVLHSS RIVPLDYEKP PNGTLLQAEA DGDASDKDAD KESEEHAALL SALLIPCALS LLISLIHSQI VATNTASGVS GGSSKNKLRR ISASYLSDKA ATRENRVRRR KKIVRVRQVE ADLSQASSNI SLPNRRTATS TIEVLPRPVT PLPSPTVTCA TVPDPTTPTT PSPSVIRRST NEETYLTTTA ISPLTQPLAA IDACYDLSRK AGGAAPESPK KRNVNWHTPI QIYATYELGE EPCSSRKVAE ESAPESVGER LCSVKPDYQT RRNIGEDDGF ESLNGKSSSG EDNNHSPLPN AVAVAAPPAP VQTNQLRLRL NTTNGVTASA SPTEKKPQSR GNESSTSCAE SDECDDADIM SSPASGCNQE CTTSATDWLG VTTNSEDCSY TSDLDHSDGG LKHTAFSDED PGELDITPTT ILNPHSSLDR ISCTIWDQRD AKKAQLSVLE IASCIIERVD SMGEANDYIY IGVVFSFLLT LIPIFCRLCE VTLGSDAEKA SEISYFNMPQ LLWEKSSASL FTLLGLAFGD SQWERMVLAL GFVQRLCLTL ILFIIFAVAE RTFKQRFLYA KLFSHLTSSR RARKSNLPHF RLNKVRNIKT WLSVRSYLKK RGPQRSVDII VSAAFIVTLL LLAFLSVEWL KDSAHLHTHL TLEALIWSIT IGIFLLRFMT LGQKIQHKYR SVSVLITEQI NLYLQIEQKP KKKDELMVSN SVLKLAADLL KELETPFKLS GLSANPYLFT TIKVVILSAL SGVLSEVLGF KLKLHKIKIK // ID PICO_DROME STANDARD; PRT; 529 AA. AC Q9V7S5; O61364; Q8T077; Q9V7S6; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative inorganic phosphate cotransporter. GN PICOT OR CG8098. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 449-529 FROM N.A. RC STRAIN=Canton-S; RA Da Lage J.-L.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY BE AN INORGANIC PHOSPHATE COTRANSPORTER. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=Q9V7S5-1; Sequence=Displayed; CC Name=A; CC IsoId=Q9V7S5-2; Sequence=VSP_007009; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE SODIUM/PHOSPHATE COTRANSPORTER FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003806; AAF57968.1; -. DR EMBL; AE003806; AAF57969.1; -. DR EMBL; AY069501; AAL39646.1; -. DR EMBL; AF022713; AAD09148.1; -. DR FlyBase; FBgn0024315; Picot. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0005315; F:inorganic phosphate transporter activity; NAS. DR GO; GO:0006817; P:phosphate transport; NAS. DR InterPro; IPR007114; MFS. DR InterPro; IPR004745; Pi_cotranspt. DR InterPro; IPR005828; Sub_transporter. DR Pfam; PF00083; sugar_tr; 1. DR TIGRFAMs; TIGR00894; 2A0114euk; 1. DR PROSITE; PS50850; MFS; 1. KW Transport; Symport; Sodium transport; Transmembrane; KW Alternative splicing. FT TRANSMEM 37 57 POTENTIAL. FT TRANSMEM 110 130 POTENTIAL. FT TRANSMEM 148 168 POTENTIAL. FT TRANSMEM 202 222 POTENTIAL. FT TRANSMEM 232 252 POTENTIAL. FT TRANSMEM 338 358 POTENTIAL. FT TRANSMEM 429 449 POTENTIAL. FT TRANSMEM 466 486 POTENTIAL. FT VARSPLIC 1 35 MPFRRSSLNHRHRDGHVLVWNQRNLHESLEQQPQR -> MS FT ASKEAICGSTEKDLEKPALG (in isoform A). FT /FTId=VSP_007009. SQ SEQUENCE 529 AA; 58372 MW; 07B89A52D5081EFB CRC64; MPFRRSSLNH RHRDGHVLVW NQRNLHESLE QQPQRCFATR YFVTFMLFLG MANAYVMRTN MSVAIVAMVN HTAIKSGEAE EYDDECGDRD IPIDDSQDGE FAWSSALQGY ILSSFFYGYV ITQIPFGILA KKYGSLRFLG YGMLINSVFA FLVPVAARGG GVWGLCAVRF IQGLGEGPIV PCTHAMLAKW IPPNERSRMG AAVYAGAQFG TIISMPLSGL LAEYGFDGGW PSIFYVFGIV GTVWSIAFLI FVHEDPSSHP TIDEREKKYI NDSLWGTDVV KSPPIPFKAI IKSLPFYAIL FAHMGHNYGY ETLMTELPTY MKQVLRFSLK SNGLLSSLPY LAMWLFSMFI SVVADWMISS KRFSHTATRK LINSIGQYGP GVALIAASYT GCDRALTLAI LTIGVGLNGG IYSGFKINHL DLTPRFAGFL MSITNCSANL AGLLAPIAAG HLISDPSKPM MGQWQIVFFI AAFVYIICGT FYNIFGSGER QYWDNPEDDE QKPALQTTVT TSPARLSNGS TAPAAISSS // ID PIG1_DROME STANDARD; PRT; 168 AA. AC P26023; O76914; Q24519; Q9W4T3; DT 01-MAY-1992 (Rel. 22, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pre-intermoult gene-1 protein precursor (Gland specific protein). GN PIG1 OR PIG-1 OR GSG OR EG:96G10.1 OR CG10790. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R, Karsnas, and Samarkand; RX MEDLINE=88136816; PubMed=3125018; RA Hofmann A., Korge G.; RT "Upstream sequences of dosage-compensated and non-compensated alleles RT of the larval secretion protein gene Sgs-4 in Drosophila."; RL Chromosoma 96:1-7(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92120020; PubMed=1769273; RA Furia M., Digilio F.A., Artiaco D., D'Avino P.P., Cavaliere D., RA Polito L.C.; RT "Molecular organization of the Drosophila melanogaster Pig-1 gene."; RL Chromosoma 101:49-54(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Bolshakov V., Borkova D., Minana B., Kafatos F.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NOT KNOWN. CC -!- TISSUE SPECIFICITY: LOW AMOUNTS IN FIRST TO THIRD INSTAR LARVAE CC SALIVARY GLANDS. CC -!- DEVELOPMENTAL STAGE: THROUGHOUT THE LARVAL PERIOD. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24138; AAA28893.1; -. DR EMBL; X15760; CAA33767.1; -. DR EMBL; AL024484; CAA19669.1; -. DR EMBL; AE003427; AAF45859.1; -. DR FlyBase; FBgn0003086; Pig1. KW Signal; Repeat. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 168 PRE-INTERMOULT GENE-1 PROTEIN. FT DOMAIN 22 100 ALA/ASP/THR-RICH. FT DOMAIN 105 155 ARG/ASN/LYS-RICH. FT DOMAIN 27 44 3 X 6 AA TANDEM REPEATS OF S-S-A-D-S-D. FT REPEAT 27 32 1. FT REPEAT 33 38 2. FT REPEAT 39 44 3. FT CONFLICT 38 38 D -> DSSADSD (IN REF. 2 AND 4). FT CONFLICT 47 47 I -> R (IN REF. 1). FT CONFLICT 47 47 I -> T (IN REF. 3). FT CONFLICT 126 168 NNNKKRANSNNNRKRRASNNNNKKKASNNNSNRRRNNNSRR FT RG -> TTTRRGPTATTIAKGGRPTTTIKRRHPTTTAQAQE FT QQFQEAWLERKWLKQQLHVDYMHNKYFFCS (IN REF. FT 4). FT CONFLICT 128 128 MISSING (IN REF. 2). FT CONFLICT 149 168 KKASNNNSNRRRNNNSRRRG -> RRHPTTTTGAGTTIPGG FT VVRAKMVETTTTCGLY (IN REF. 1 AND 2). SQ SEQUENCE 168 AA; 18142 MW; 4DEB6346D6713841 CRC64; MKLTKLWLLF VCLGLFVTLV VSADTDSDAD SDSSADSDEN TTASGSIVTS TTESSATNSS GSSDDASGSS SDVDDGSDDD TDSGSDTDYD TPTTAPVVKK RANRKKANNN KKRASNNRKK ANNNNNNNKK RANSNNNRKR RASNNNNKKK ASNNNSNRRR NNNSRRRG // ID PIGE_DROME STANDARD; PRT; 915 AA. AC Q24118; Q9VIY7; DT 01-NOV-1997 (Rel. 35, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pigeon protein (Linotte protein). GN PIGEON OR LIO OR CG10739. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=96049131; PubMed=7576632; RA Bolwig G.M., del Vecchio M., Hannon G., Tully T.; RT "Molecular cloning of linotte in Drosophila: a novel gene that RT functions in adults during associative learning."; RL Neuron 15:829-842(1995). RN [2] RP ERRATUM. RA Bolwig G.M., del Vecchio M., Hannon G., Tully T.; RL Neuron 34:667-667(2003). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- DEVELOPMENTAL STAGE: DETECTED IN EMBRYOS, PUPAE, AND ADULTS BUT CC NOT LARVAE. CC -!- MISCELLANEOUS: 'LINOTTE' USED IN THE COLLOQUIAL SENTENCE 'TETE DE CC LINOTTE' LITERALLY MEANS 'SCATTERBRAIN' IN FRENCH. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U32865; AAA92001.1; -. DR EMBL; AE003662; AAF53775.1; -. DR EMBL; AY061465; AAL29013.1; -. DR FlyBase; FBgn0010309; pigeon. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kin...; NAS. FT CONFLICT 335 335 Y -> C (IN REF. 1). FT CONFLICT 451 452 LH -> FD (IN REF. 1). FT CONFLICT 518 518 H -> L (IN REF. 1). FT CONFLICT 867 867 A -> G (IN REF. 1). SQ SEQUENCE 915 AA; 102898 MW; 64768399B546368D CRC64; MLRQENLAAN FCGLLASQGY KEKANEWRIL GQEQDGSLLT SWIFEYADED QRKETCIGHF HATKKQLRLL WTLDNCREIV QATINSSVTL LSFVEKTEGK LYQAFVVEVR SSEGGTATPL NSEPSNRQMM TQFLWRVESA TRTCWQDKLL VLTHEESIKQ YSCVVKQSST TCSTGGGEGS AWRLDTSILT YETLARNFSW AQWDPECQAL YYIHLKPKAK SLSLLDEREE AGEQTTPTLS PTLSAFQFNE KQPTETVLNI PLNLPKLPNG SKEESPSYDD DAVPLRVHDS SLNLIILADT SGMFFVCHYY LYQPMQSEQR DVHFAYSVTL LHHGYVVHCV MPGVPWQKAR LLRPTFALHG QHHLLVSSAF FVHLLDVGLQ HEPNCHIVCA AHNRSPDITQ LVPLRKWGAL AYDAATLDLV SLSVPKSHLI EAFRNDSSLD NRISIIHYFL LHSNDMDVLA ELLNNILERP LSLDTVALLK EALVAGSYAA AVRGLPEDAK PLMRLLPLTT ALASRPIHAK VADISVGLSH ETLHNTSMML LSPQQRLSPY RTDIWTRLWD LLNESAKQEQ PRFSAEQVTE KLIFSLACYQ PEALSRCTTP LSPDTGTGGF GDYSSGSAFP FSNEVLPFIE LEGCTASKQE HVISVYLREL SVHLVKHTSK PNTGFRWLKE TFFERSQAPA HVHAVASQFV SAQLELSRAL CSLVCRAAGL DARMETSRGF QLIDQMAANQ QHSLFLILER YCLAVESIAF PLPEGFSSFF TYLGYRALGY DMFLQYVENH VFELQVDVMK AIVFDIEDSP LGIERKLSLL SALPKQRAQR LLKCWQHPDS LMIRGREHAA NILSGQQQEV LHQQRPTACV NQSRNNARSD LTAEALSPLD SFLDLLTAKA SLNELDYNLL IETTLSSIDQ LKLEA // ID PIMT_DROME STANDARD; PRT; 226 AA. AC Q27869; Q9VND1; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein-L-isoaspartate(D-aspartate) O-methyltransferase (EC 2.1.1.77) DE (Protein-beta-aspartate methyltransferase) (PIMT) (Protein L- DE isoaspartyl/D-aspartyl methyltransferase) (L-isoaspartyl protein DE carboxyl methyltransferase). GN PCMT OR PIAM OR CG2152. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97215581; PubMed=9061928; RA O'Connor M.B., Galus A., Hartenstine M., Magee M., Jackson F.R., RA O'Connor C.M.; RT "Structural organization and developmental expression of the protein RT isoaspartyl methyltransferase gene from Drosophila melanogaster."; RL Insect Biochem. Mol. Biol. 27:49-54(1997). RN [2] RP REVISION TO 124. RA O'Connor C.M.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYZES THE METHYL ESTERIFICATION OF L-ISOASPARTYL AND CC D-ASPARTYL RESIDUES IN PEPTIDES AND PROTEINS THAT RESULT FROM CC SPONTANEOUS DECOMPOSITION OF NORMAL L-ASPARTYL AND L-ASPARAGINYL CC RESIDUES. IT PLAYS A ROLE IN THE REPAIR AND/OR DEGRADATION OF CC DAMAGED PROTEINS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE + PROTEIN L-BETA- CC ASPARTATE = S-ADENOSYL-L-HOMOCYSTEINE + PROTEIN L-BETA-ASPARTATE CC METHYL ESTER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE L-ISOASPARTYL/D-ASPARTYL PROTEIN CC METHYLTRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U43737; AAA86272.2; -. DR EMBL; U37432; AAA80540.2; -. DR EMBL; AE003602; AAF52012.1; -. DR FlyBase; FBgn0015276; Pcmt. DR InterPro; IPR000682; Pcmt. DR InterPro; IPR000051; SAM_bind. DR Pfam; PF01135; PCMT; 1. DR TIGRFAMs; TIGR00080; pimt; 1. DR PROSITE; PS01279; PCMT; 1. KW Transferase; Methyltransferase. SQ SEQUENCE 226 AA; 24590 MW; AA56803256DBD567 CRC64; MAWRSVGANN EDLIRQLKDH GVIASDAVAQ AMKETDRKHY SPRNPYMDAP QPIGGGVTIS APHMHAFALE YLRDHLKPGA RILDVGSGSG YLTACFYRYI KAKGVDADTR IVGIEHQAEL VRRSKANLNT DDRSMLDSGQ LLIVEGDGRK GYPPNAPYNA IHVGAAAPDT PTELINQLAS GGRLIVPVGP DGGSQYMQQY DKDANGKVEM TRLMGVMYVP LTDLRS // ID PIP1_DROME STANDARD; PRT; 1312 AA. AC P25455; Q9VPN9; DT 01-MAY-1992 (Rel. 22, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase classes I DE and II (EC 3.1.4.11) (Phosphoinositide phospholipase C). GN PLC21C OR PLC-21 OR CG4574. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., CHARACTERIZATION, AND ALTERNATIVE SPLICING. RX MEDLINE=91286274; PubMed=2061323; RA Shortridge R.D., Yoon J., Lending C.R., Bloomquist B.T., RA Perdew M.H., Pak W.L.; RT "A Drosophila phospholipase C gene that is expressed in the central RT nervous system."; RL J. Biol. Chem. 266:12474-12480(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PRODUCTION OF THE SECOND MESSENGER MOLECULES CC DIACYLGLYCEROL (DAG) AND INOSITOL 1,4,5-TRISPHOSPHATE (IP3) IS CC MEDIATED BY ACTIVATED PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE CC C ENZYMES. CC -!- CATALYTIC ACTIVITY: 1-PHOSPHATIDYL-1D-MYO-INOSITOL 4,5- CC BISPHOSPHATE + H(2)O = D-MYO-INOSITOL 1,4,5-TRISPHOSPHATE + CC DIACYLGLYCEROL. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Class-II; CC IsoId=P25455-1; Sequence=Displayed; CC Name=2; Synonyms=Class-I; CC IsoId=P25455-2; Sequence=VSP_004727; CC -!- TISSUE SPECIFICITY: NEURONAL CELL BODIES OF THE OPTIC LOBE, CC CENTRAL BRAIN, AND THORACIC GANGLIA IN ADULTS, AND THE BRAIN OF CC LARVAE. CC -!- SIMILARITY: CONTAINS 1 PI-PLC X-BOX CATALYTIC DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PI-PLC Y-BOX CATALYTIC DOMAIN. CC -!- SIMILARITY: CONTAINS 1 C2 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60452; AAA28819.1; -. DR EMBL; M60453; AAA28820.1; -. DR EMBL; AE003589; AAF51507.1; -. DR PIR; B40879; B40879. DR HSSP; P10688; 1QAS. DR FlyBase; FBgn0004611; Plc21C. DR InterPro; IPR000008; C2. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR001192; PI_PLC. DR InterPro; IPR000909; PI_PLC_Xdom. DR InterPro; IPR001711; PI_PLC_Y. DR Pfam; PF00168; C2; 1. DR Pfam; PF00388; PI-PLC-X; 1. DR Pfam; PF00387; PI-PLC-Y; 1. DR PRINTS; PR00390; PHPHLIPASEC. DR ProDom; PD001202; PI_PLC_Y; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00148; PLCXc; 1. DR SMART; SM00149; PLCYc; 1. DR PROSITE; PS50004; C2_DOMAIN_2; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1. KW Hydrolase; Lipid degradation; Transducer; Alternative splicing. FT DOMAIN 318 466 PI-PLC X-BOX. FT DOMAIN 599 715 PI-PLC Y-BOX. FT DOMAIN 722 820 C2 DOMAIN. FT ACT_SITE 333 333 BY SIMILARITY. FT ACT_SITE 378 378 BY SIMILARITY. FT VARSPLIC 1057 1063 Missing (in isoform 2). FT /FTId=VSP_004727. FT CONFLICT 508 508 G -> A (IN REF. 1). SQ SEQUENCE 1312 AA; 145717 MW; B8DD0EF5A48C2665 CRC64; MMSAGGTYIS TASVEVPQAL QDGEKFIRWD DDSGTGTPVT MRVDAKGFFL YWVDQNNELD ILDIATIRDV RTGQYAKRPK DNKLRQIVTL GPQDTLEEKT VTVCHGSDFV NMTFVNFCCT RRDIAQLWTD GLIKLAYSLA QLNGSAIMFL QKAHTKLCLQ VDKSGRIPVK NIIKLFAQNK EDRKRVEKAL DVTGLPSGKV DSISVSKFQF EDFYNLYKYL TQRSEVERLF DSIVGNSKRK CMSIAQLVEF LNKTQRDPRL NEILYPYANP ARAKELIQQY EPNKFNAQKG QLSLDGFLRY LMGDDNPIMA PSKLDLCDDM DQPMSHYFIN SSHNTYLTGH QLTGKSSVEI YRQCLLAGCR CVELDFWNGR TEEPVIVHGY TFVPEIFAKD VLEAIAESAF KTSEYPVILS FENHCNPRQQ AKIANYCREI FGDMLLDKPL DSHPLEPNMD LPPPAMLRRK IIIKNKKKHH HHHHHHHHKK PAQVGTPAAN NKLTTANSVD AKAAQQVGLS ASHEDGGVTR STANGDVATG TGTGSAAGTA GHAPPLQQIR QSSKDSTGSS DSDSSSEDES LPNTTPNLPS GNEPPPEKAQ KETEAGAEIS ALVNYVQPIH FSSFENAEKK NRCYEMSSFD EKQATTLLKE RPIEFVNYNK HQLSRVYPAG TRFDSSNFMP QLFWNAGCQL VALNFQTLDL AMQLNLGIFE YNARSGYLLK PEFMRRSDRR LDPFAESTVD GIIAGTVSIT VLSGQFLTDK RANTFVEVDM YGLPADTVRK KFRTKTVRDN GMNPLYDEEP FVFKKVVLPE LASIRIAAYE EGGKLIGHRV LPVIGLCPGY RHVNLRSEVG QPIALASLFL CVVVKDYVPD DLSNFAEALA NPIKYQSELE KRDIQLSVLT DEAEALGSAD EDLSKSCGQK KELRPVESLA TSPKHRPSIS AAAAMSVDVT VDRTDGGRGE DSISIVAPSI QHQHSLDQSV STSIRQVESS QFDVDLVLAE PLEKILDHKS VKEKRLEMEK KLESLRKKHD KEKIKIAGQK SSPLEGKKPK FAITNKLVKR LSNKSLNCLS PHSEPGVEIP ACPLDLGDSS EESAAADAGE DLAGGSSSLD GRTQESRLRS ACREYTSQYR ELQEKYHEAI YSAAEKVLKT SQTGQTKQLK ASLDKVTGEV MHQLQEARRN EVKNLATVHR DRDELIRMKR EVASSVVERG VAERVRLKQT FDRRTDELQK QHDSVRNALA EHRSKARQIL DKEAESRSCV SSNGFLVLFH GPHHHGCTGS GSSALSGNNL TLNLDAGAAG SHSAISPAKS HNSIAAAAEM KT // ID PIPA_DROME STANDARD; PRT; 1095 AA. AC P13217; Q9U4G4; Q9W4K9; DT 01-JAN-1990 (Rel. 13, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase DE (EC 3.1.4.11) (Phosphoinositide phospholipase C) (No receptor DE potential A protein). GN NORPA OR CG3620. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88311074; PubMed=2457447; RA Bloomquist B.T., Shortridge R.D., Schneuwly S., Perdew M.H., RA Montell C., Steller H., Rubin G., Pak W.L.; RT "Isolation of a putative phospholipase C gene of Drosophila, norpA, RT and its role in phototransduction."; RL Cell 54:723-733(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1089-1095. RX MEDLINE=21391705; PubMed=11500369; RA Kimple M.E., Siderovski D.P., Sondek J.; RT "Functional relevance of the disulfide-linked complex of the N- RT terminal PDZ domain of InaD with NorpA."; RL EMBO J. 20:4414-4422(2001). CC -!- FUNCTION: THE PRODUCTION OF THE SECOND MESSENGER MOLECULES CC DIACYLGLYCEROL (DAG) AND INOSITOL 1,4,5-TRISPHOSPHATE (IP3) IS CC MEDIATED BY ACTIVATED PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE CC C ENZYMES. NORPA IS INVOLVED IN PHOTOTRANSDUCTION. CC -!- CATALYTIC ACTIVITY: 1-PHOSPHATIDYL-1D-MYO-INOSITOL 4,5- CC BISPHOSPHATE + H(2)O = D-MYO-INOSITOL 1,4,5-TRISPHOSPHATE + CC DIACYLGLYCEROL. CC -!- SUBUNIT: INTERACTS WITH INAD. CC -!- SIMILARITY: CONTAINS 1 PI-PLC X-BOX CATALYTIC DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PI-PLC Y-BOX CATALYTIC DOMAIN. CC -!- SIMILARITY: CONTAINS 1 C2 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03138; AAA28724.1; -. DR EMBL; AE003430; AAF45942.2; -. DR EMBL; AF181641; AAD55427.1; -. DR PIR; A31225; A31225. DR PDB; 1IHJ; 22-AUG-01. DR FlyBase; FBgn0004625; norpA. DR GO; GO:0016027; C:inaD signaling complex; IPI. DR GO; GO:0005624; C:membrane fraction; IDA. DR GO; GO:0009628; P:response to abiotic stimulus; IMP. DR InterPro; IPR000008; C2. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR001192; PI_PLC. DR InterPro; IPR000909; PI_PLC_Xdom. DR InterPro; IPR001711; PI_PLC_Y. DR Pfam; PF00168; C2; 1. DR Pfam; PF00388; PI-PLC-X; 1. DR Pfam; PF00387; PI-PLC-Y; 1. DR PRINTS; PR00390; PHPHLIPASEC. DR ProDom; PD001202; PI_PLC_Y; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00148; PLCXc; 1. DR SMART; SM00149; PLCYc; 1. DR PROSITE; PS50004; C2_DOMAIN_2; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1. KW Hydrolase; Lipid degradation; Vision; Transducer; 3D-structure. FT DOMAIN 319 469 PI-PLC X-BOX. FT DOMAIN 550 666 PI-PLC Y-BOX. FT DOMAIN 673 771 C2 DOMAIN. FT ACT_SITE 334 334 BY SIMILARITY. FT ACT_SITE 381 381 BY SIMILARITY. FT DISULFID 1094 1094 INTERCHAIN (WITH C-31 IN INAD). FT CONFLICT 446 446 H -> R (IN REF. 1). FT CONFLICT 1094 1094 C -> Y (IN REF. 2 AND 3). SQ SEQUENCE 1095 AA; 124803 MW; CC64CABF9B065BB6 CRC64; MTKKYEFDWI IPVPPELTTG CVFDRWFENE KETKENDFER DALFKVDEYG FFLYWKSEGR DGDVIELCQV SDIRAGGTPK DPKILDKVTK KNGTNIPELD KRSLTICSNT DYINITYHHV ICPDAATAKS WQKNLRLITH NNRATNVCPR VNLMKHWMRL SYCVEKSGKI PVKTLAKTFA SGKTEKLVYT CIKDAGLPDD KNATMTKEQF TFDKFYALYH KVCPRNDIEE LFTSITKGKQ DFISLEQFIQ FMNDKQRDPR MNEILYPLYE EKRCTEIIND YELDEEKKKN VQMSLDGFKR YLMSDENAPV FLDRLDFYME MDQPLAHYYI NSSHNTYLSG RQIGGKSSVE MYRQTLLAGC RCVELDCWNG KGEDEEPIVT HGHAYCTEIL FKDCIQAIAD CAFVSSEYPV ILSFENHCNR AQQYKLAKYC DDFFGDLLLK EPLPDHPLDP GLPLPPPCKL KRKILIKNKR MKPEVEKVEL ELWLKGELKT DDDPEEDASA GKPPEAAAAP APAPEAAAAA EGAAEGGGGA EAEAAAANYS GSTTNVHPWL SSMVNYAQPI KFQGFDKAIE KNIAHNMSSF AESAGMNYLK QSSIDFVNYN KRQMSRIYPK GTRADSSNYM PQVFWNAGCQ MVSLNFQSSD LPMQLNQGKF EYNGGCGYLL KPDFMRRADK DFDPFADAPV DGVIAAQCSV KVIAGQFLSD KKVGTYVEVD MFGLPSDTVK KEFRTRLVAN NGLNPVYNED PFVFRKVVLP DLAVLRFGVY EESGKILGQR ILPLDGLQAG YRHVSLRTEA NFPMSLPMLF VNIELKIYVP DGFEDFMAML SDPRGFAGAA KQQNEQMKAL GIEEQSGGAA RDAGKAKEEE KKEPPLVFEP VTLESLRQEK GFQKVGKKQI KELDTLRKKH AKERTSVQKT QNAAIDKLIK GKSKDDIRND ANIKNSINDQ TKQWTDMIAR HRKEEWDMLR QHVQDSQDAM KALMLTVQAA QIKQLEDRHA RDIKDLNAKQ AKMSADTAKE VQNDKTLKTK NEKDRRLREK RQNNVKRFME EKKQIGVKQG RAMEKLKLAH SKQIEEFSTD VQKLMDMYKI EEEAYKTQGK TEFCA // ID PIT_DROME STANDARD; PRT; 680 AA. AC Q9VD51; O77001; Q8SYP5; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable ATP-dependent helicase pitchoune. GN PIT OR CG6375. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=98384314; PubMed=9716523; RA Zaffran S., Chartier A., Gallant P., Astier M., Arquier N., RA Doherty D., Gratecos D., Semeriva M.; RT "A Drosophila RNA helicase gene, pitchoune, is required for cell RT growth and proliferation and is a potential target of d-Myc."; RL Development 125:3571-3584(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLE RNA-DEPENDENT HELICASE. FUNCTIONS IN CELL CC GROWTH AND PROLIFERATION. MAY HAVE A ROLE IN RIBOSOME BIOGENESIS CC AND, CONSEQUENTLY, IN PROTEIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR; NUCLEOLAR. CC -!- MISCELLANEOUS: MUTATION IN THE PIT GENE PRODUCE LARVAE THAT CANNOT CC GROW BEYOND THE FIRST INSTAR LARVAL STAGE ALTHOUGH THEY CAN LIVE CC AS LONG AS 7-10 DAYS. ALL THE TISSUES ARE EQUALLY AFFECTED AND THE CC PERFECTLY SHAPED LARVAE ARE INDISTINGUISHABLE FROM FIRST INSTAR CC WILD-TYPE ANIMALS. CC -!- MISCELLANEOUS: 'PITCHOUNE' MEANS 'SMALL' IN PROVENCE (SOUTHERN CC PART OF FRANCE). CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. DDX18/PIT CC SUBFAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U84552; AAC27683.1; ALT_FRAME. DR EMBL; AE003737; AAF55951.2; -. DR EMBL; AY071402; AAL49024.1; -. DR EMBL; AY119620; AAM50274.1; -. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0025140; pit. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; FALSE_NEG. KW Helicase; ATP-binding; RNA-binding; Nuclear protein. FT NP_BIND 231 238 ATP (POTENTIAL). FT SITE 341 344 DEVD BOX. FT CONFLICT 30 30 N -> K (IN REF. 1). FT CONFLICT 115 115 V -> A (IN REF. 1). FT CONFLICT 512 517 DDPREY -> GDQASI (IN REF. 1). FT CONFLICT 634 644 GAAKRERPEKR -> ARPSGSDRKSD (IN REF. 1). SQ SEQUENCE 680 AA; 76927 MW; E71CD18B8A135FF1 CRC64; MSIREKLLMK KIVKREKMKK ELSQKKGNKN AQKQEPPKQN GNKPSKKPEK LSKKHVAKDE DDDLEEDFQE APLPKKKQQK QPPKKQQIQV ANSDSESDDD EQEDEADEDS DLDEVAEVDE EDVDSGSEDD DQQEDEDEEE PVPAKKTKLL PNKSKAQNGK PAKDDEPFTV ESSLAALDYR DSDDRSFASL KGAVSEATLR AIKEMGFTEM TEIQSKSLTP LLKGRDLVGA AQTGSGKTLA FLIPAVELIN KLRFMPRNGT GVIIISPTRE LSMQTFGVLK ELMAHHHHTY GLVMGGSNRQ VESEKLGKGI NILVATPGRL LDHLQNSPDF LYKNLQCLII DEVDRILEIG FEEELKQIIN LLPKRRQTML FSATQTARIE ALSKLALKSE PIYVGVHDNQ DTATVDGLEQ GYIVCPSEKR LLVLFTFLKK NRKKKVMVFF SSCMSVKYHH ELFNYIDLPV TSIHGKQKQT KRTTTFFQFC NAESGILLCT DVAARGLDIP QVDWIVQYDP PDDPREYIHR VGRTARGSGT SGHALLLMRP EELGFLRYLK AAKVPLNEFE FSWQKIADIQ LQLEKLIAKN YFLNQSAKEA FKSYVRAYDS HQLKQIFNVN TLDLQAVAKS FGFLVPPVVD LKVGAAKRER PEKRVGGGGF GFYKKMNEGS ASKQRHFKQV NRDQAKKFMR // ID PIWI_DROME STANDARD; PRT; 843 AA. AC Q9VKM1; O96674; O96675; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Piwi protein. GN PIWI OR CG6122. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=99069219; PubMed=9851978; RA Cox D.N., Chao A., Baker J., Chang L., Qiao D., Lin H.; RT "A novel class of evolutionarily conserved genes defined by piwi are RT essential for stem cell self-renewal."; RL Genes Dev. 12:3715-3727(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MEDIATES A SOMATIC SIGNALING MECHANISM REQUIRED FOR THE CC ASYMMETRIC DIVISION OF GERM-LINE STEM CELLS TO PRODUCE AND CC MAINTAIN A DAUGHTER GERM-LINE STEM CELL. IT IS NOT ESSENTIAL FOR CC THE FURTHER DIFFERENTIATION OF THE COMMITTED DAUGHTER CELL. CC -!- TISSUE SPECIFICITY: EXPRESSED SOMATICALLY IN THE OVARIOLE TERMINAL CC FILAMENT AND EPITHELIAL SHEATH CELLS. EXPRESSED IN THE GERMARIUM CC AT LOW LEVELS DURING OOGENESIS STAGES 1-6, AT A LOWER LEVEL DURING CC STAGES 7-9, STRONGLY AT STAGE 10 AND EVENTUALLY ACCUMULATING IN CC EARLY EMBRYOS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE ARGONAUTE FAMILY. CC -!- SIMILARITY: CONTAINS 1 PAZ DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PIWI DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF104354; AAD08704.1; -. DR EMBL; AF104355; AAD08705.1; -. DR EMBL; AE003630; AAF53043.1; -. DR FlyBase; FBgn0004872; piwi. DR GO; GO:0048132; P:female germ-line stem cell division; IMP. DR GO; GO:0048133; P:male germ-line stem cell division; IMP. DR GO; GO:0017145; P:stem cell renewal; IMP. DR InterPro; IPR003100; PAZ. DR InterPro; IPR003165; Piwi. DR Pfam; PF02170; PAZ; 1. DR Pfam; PF02171; Piwi; 1. DR PROSITE; PS50821; PAZ; 1. DR PROSITE; PS50822; PIWI; 1. KW Developmental protein. FT DOMAIN 262 372 PAZ. FT DOMAIN 538 829 PIWI. FT CONFLICT 67 67 T -> P (IN REF. 1; AAD08704). FT CONFLICT 84 84 A -> V (IN REF. 1; AAD08704). FT CONFLICT 122 124 EPS -> VPT (IN REF. 1; AAD08704). FT CONFLICT 576 577 NR -> KPY (IN REF. 1; AAD08705). SQ SEQUENCE 843 AA; 97177 MW; 9B4A95E688E9D9B7 CRC64; MADDQGRGRR RPLNEDDSST SRGSGDGPRV KVFRGSSSGD PRADPRIEAS RERRALEEAP RREGGPTERK PWGDQYDYLN TRPAELVSKK GTDGVPVMLQ TNFFRLKTKP EWRIVHYHVE FEPSIENPRV RMGVLSNHAN LLGSGYLFDG LQLFTTRKFE QEITVLSGKS KLDIEYKISI KFVGFISCAE PRFLQVLNLI LRRSMKGLNL ELVGRNLFDP RAKIEIREFK MELWPGYETS IRQHEKDILL GTEITHKVMR TETIYDIMRR CSHNPARHQD EVRVNVLDLI VLTDYNNRTY RINDVDFGQT PKSTFSCKGR DISFVEYYLT KYNIRIRDHN QPLLISKNRD KALKTNASEL VVLIPELCRV TGLNAEMRSN FQLMRAMSSY TRMNPKQRTD RLRAFNHRLQ NTPESVKVLR DWNMELDKNV TEVQGRIIGQ QNIVFHNGKV PAGENADWQR HFRDQRMLTT PSDGLDRWAV IAPQRNSHEL RTLLDSLYRA ASGMGLRIRS PQEFIIYDDR TGTYVRAMDD CVRSDPKLIL CLVPNDNAER YSSIKKRGYV DRAVPTQVVT LKTTKNRSLM SIATKIAIQL NCKLGYTPWM IELPLSGLMT IGFDIAKSTR DRKRAYGALI ASMDLQQNST YFSTVTECSA FDVLANTLWP MIAKALRQYQ HEHRKLPSRI VFYRDGVSSG SLKQLFEFEV KDIIEKLKTE YARVQLSPPQ LAYIVVTRSM NTRFFLNGQN PPPGTIVDDV ITLPERYDFY LVSQQVRQGT VSPTSYNVLY SSMGLSPEKM QKLTYKMCHL YYNWSGTTRV PAVCQYAKKL ATLVGTNLHS IPQNALEKKF YYL // ID PIX1_DROME STANDARD; PRT; 509 AA. AC O18400; Q9VA26; DT 15-JUL-1999 (Rel. 38, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Pituitary homeobox 1 homolog (D-PTX1). GN PTX1 OR CG1447. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR RP LOCATION. RC TISSUE=Embryo; RX MEDLINE=98092108; PubMed=9431811; RA Vorbrueggen G., Constien R., Zilian O., Wimmer E.A., Dowe G., RA Taubert H., Noll M., Jaeckle H.; RT "Embryonic expression and characterization of a Ptx1 homolog in RT Drosophila."; RL Mech. Dev. 68:139-147(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: APPEARS TO CONTROL PHYSIOLOGICAL CELL FUNCTIONS RATHER CC THAN PATTERN FORMATION DURING EMBRYOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: FIRST DETECTED IN THE POSTERIOR REGION OF CC THE BLASTODERM EMBRYO. IN LATER STAGES OF EMBRYONIC DEVELOPMENT, CC DETECTED IN THE POSTERIOR PORTION OF THE MIDGUT, IN THE CC DEVELOPING MALPIGHIAN TUBULES, IN A SUBSET OF VENTRAL SOMATIC CC MUSCLES, IN THE DEVELOPING CNS AND IN BOLWIG'S ORGAN. CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. BICOID CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- SIMILARITY: CONTAINS 1 OAR DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ001519; CAA04801.1; -. DR EMBL; AE003776; AAF57099.3; -. DR EMBL; BT009990; AAQ22459.1; -. DR HSSP; P06601; 1FJL. DR FlyBase; FBgn0020912; Ptx1. DR InterPro; IPR003654; Homeo_OAR. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF03826; OAR; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS50803; OAR; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation; Activator. FT DNA_BIND 262 322 HOMEOBOX. FT DOMAIN 460 473 OAR. FT DOMAIN 464 470 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 74 140 SER-RICH. FT CONFLICT 9 49 GCGGGGGLGVGVVTSSATALGPGGLTNGGGGVVSGALNGLE FT -> LRRGRRSGSGRGHQLGHGLGTGWPDQRGRRSGQWRTQR FT IG (IN REF. 1). FT CONFLICT 108 108 T -> A (IN REF. 1). FT CONFLICT 178 178 I -> SLFFSV (IN REF. 1). FT CONFLICT 283 283 F -> S (IN REF. 1). SQ SEQUENCE 509 AA; 53216 MW; 6C01616DB9D79C88 CRC64; MDRSSAVGGC GGGGGLGVGV VTSSATALGP GGLTNGGGGV VSGALNGLEA MSAESTGLCL QDLVSAGTAN GAGSAGSAES ATTTSTALSS GSTGSSTVNG GGSSTSGTEH LHSHHSLHDS SSSVSISPAI SSLMPISSLS HLHHSAGQDL VGGYSQHPHH TVVPPHTPKH EPLEKLRIWA ETGDFRDSHS SMTAVANSLD STHLNNFQTS STSSISNRSR DRKDGNRSVN ETTIKTENIS SSGHDEPMTT SGEEPKNDKK NKRQRRQRTH FTSQQLQELE HTFSRNRYPD MSTREEIAMW TNLTEARVRV WFKNRRAKWR KRERNAMNAA VAAADFKSGF GTQFMQPFAD DSLYSSYPYN NWTKVPSPLG TKPFPWPVNP LGSMVAGNHH QNSVNCFNTG ASGVAVSMNN ASMLPGSMGS SLSNTSNVGA VGAPCPYTTP ANPYMYRSAA EPCMSSSMSS SIATLRLKAK QHASAGFGSP YSAPSPVSRS NSAGLSACQY TGVGVTDVV // ID PK61_DROME STANDARD; PRT; 819 AA. AC Q9W0V1; O62534; Q8IHG6; Q9W0V2; Q9W0V3; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine-protein kinase Pk61C (EC 2.7.1.37) (dSTPK61). GN PK61C OR CG1210/CG1201. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Berkeley; TISSUE=Embryo, and Testis; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 6-819 FROM N.A. (ISOFORM 1). RA MacDougall C.N.; RT "Cloning and characterisation of a gene encoding sex-specific RT transcripts in Drosophila melanogaster."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION. RX MEDLINE=98035195; PubMed=9368760; RA MacDougall C.N., Todman M., Bownes M.; RL Unpublished results, cited by: RL Alessi D.R., Deak M., Casamayor A., Caudwell F.B., Morrice N.A., RL Norman D.G., Gaffney P.R.J., Reese C.B., MacDougall C.N., Harbison D., RL Ashworth A., Bownes M.; RL Curr. Biol. 7:776-789(1997). CC -!- FUNCTION: IMPLICATED IN THE REGULATION OF SEXUAL DIFFERENTIATION, CC OOGENESIS AND SPERMATOGENESIS. MAY BE IMPLICATED IN THE ACTIVATION CC OF DPKB. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=C; CC IsoId=Q9W0V1-1; Sequence=Displayed; CC Name=2; Synonyms=A, D; CC IsoId=Q9W0V1-2; Sequence=VSP_004896; CC Note=No experimental confirmation available; CC Name=3; Synonyms=B, E; CC IsoId=Q9W0V1-3; Sequence=VSP_004897; CC Note=No experimental confirmation available; CC -!- PTM: PHOSPHORYLATED ON TYROSINE AND SERINE/THREONINE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. PDK1 CC SUBFAMILY. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 27. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS CC IN POSITIONS 453 AND 716. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003467; AAF47327.3; -. DR EMBL; AE003467; AAF47329.2; -. DR EMBL; AE003467; AAF47331.1; -. DR EMBL; BT001263; AAN71019.1; ALT_FRAME. DR EMBL; BT004489; AAO42653.1; -. DR EMBL; Y07908; CAA69216.1; ALT_FRAME. DR FlyBase; FBgn0020386; Pk61C. DR GO; GO:0005737; C:cytoplasm; ISS. DR GO; GO:0005886; C:plasma membrane; ISS. DR GO; GO:0004676; F:3-phosphoinositide-dependent protein kinase...; ISS. DR GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; ISS. DR GO; GO:0007292; P:female gamete generation; TAS. DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS. DR GO; GO:0030307; P:positive regulation of cell growth; NAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; ISS. DR GO; GO:0007548; P:sex differentiation; TAS. DR GO; GO:0007283; P:spermatogenesis; TAS. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Phosphorylation; Alternative splicing. FT DOMAIN 229 554 PROTEIN KINASE. FT NP_BIND 235 243 ATP (BY SIMILARITY). FT BINDING 258 258 ATP (BY SIMILARITY). FT ACT_SITE 353 353 BY SIMILARITY. FT DOMAIN 165 218 GLN-RICH. FT DOMAIN 399 428 ASP-RICH. FT DOMAIN 751 787 SER-RICH. FT VARSPLIC 1 64 Missing (in isoform 2). FT /FTId=VSP_004896. FT VARSPLIC 1 280 Missing (in isoform 3). FT /FTId=VSP_004897. FT CONFLICT 183 184 QQ -> HE (IN REF. 4). FT CONFLICT 426 426 G -> R (IN REF. 4). SQ SEQUENCE 819 AA; 92028 MW; EA36359C8364A3A7 CRC64; MNIIQINGTQ QQLQLPGSGA SGIAAAAVIT VASDCGENCS SNGTEHQQHF NIATTTATSA TEATMPAMAK EKASATVSLG ESNFRDINLK DLAVVVEAAS RLHHQQNVCG CGAVSSTENN NNSRYGSSKY LTNGHTSPLA AAVASNSSSV ATTPHCRMLH NCSLQQYQND IRQQTEILDM LRQQHQQGYQ SQQQQQQPQQ QQEQQQQQEQ SQQQQQLQNP APRRSPNDFI FGRYIGEGSY SIVYLAVDIH SRREYAIKVC EKRLILRERK QDYIKREREV MHQMTNVPGF VNLSCTFQDQ RSLYFVMTYA RKGDMLPYIN RVGSFDVACT RHYAAELLLA CEHMHRRNVV HRDLKPENIL LDEDMHTLIA DFGSAKVMTA HERALATEHC SEQRRSNSDE DDEDSDRLEN EDEDFYDRDS EELDDGDDEQ QQEEMDSPRH RQRRYNRHRK ASFVGTAQYV SPEVLQNGPI TPAADLWALG CIVYQMIAGL PPFRGSNDYV IFKEILDCAV DFPQGFDKDA EDLVRKLLRV DPRDRLGAQD EFGYYESIRA HPFFAGIDWQ TLRQQTPPPI YPYLPGVSQD EDFRSSYTVP GDLEPGLDER QISRLLSAEL GVGSSVAMPV KRSTAKNSFD LNDAEKLQRL EQQKTDKWHV FADGEVILKK GFVNKRKGLF ARKRMLLLTT GPRLIYIDPV QMIKKGEIPW SPDLRAEYKN FKIFFVHTPN RTYYLDDPEG YAIHWSEAIE NMRKLAYGDP SSTSAVSCSS GSSNSLAVIS NSSAASSSNS PTVKRSSPVN APQASTASDN RTLGSTRTGT SPSKKTASK // ID PLI_DROME STANDARD; PRT; 424 AA. AC O77237; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Pellino protein. GN PLI OR CG5212. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND INTERACTION WITH PLL. RX MEDLINE=99264282; PubMed=10330490; RA Grosshans J., Schnorrer F., Nuesslein-Volhard C.; RT "Oligomerisation of Tube and Pelle leads to nuclear localisation of RT dorsal."; RL Mech. Dev. 81:127-138(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: SCAFFOLD PROTEIN INVOLVED IN THE TOLL SIGNALING PATHWAY CC VIA ITS INTERACTION WITH PELLE/PLL KINASE. CC -!- SUBUNIT: INTERACTS WITH PLL. CC -!- SIMILARITY: BELONGS TO THE PELLINO FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF091624; AAC96298.1; -. DR EMBL; AE003745; AAF56198.1; -. DR EMBL; AY069632; AAL39777.1; -. DR FlyBase; FBgn0025574; Pli. DR InterPro; IPR006800; Pellino. DR Pfam; PF04710; Pellino; 1. SQ SEQUENCE 424 AA; 46770 MW; B6A99CB1C72C5F40 CRC64; MVKRTDGTES PILAEDGGDG HDKPRLRYGE LVILGYNGYL PQGDRGRRRS KFVLHKRTEA SGVKRSKHYI VQSPQTSKAI LDANQHSISY TLSRNQAVIV EYKEDTETDM FQVGRSSESP IDFVVMDTLP GDKKDAKVMQ STISRFACRI LVNRCEPAKA RIFAAGFDSS RNIFLGEKAT KWQDNVEIDG LTTNGVLIMH PKGSFCGGNA KCGLWRECSV GGDVFSLRES RSAQQKGQPI YDECNILQDG TLIDLCGATL LWRSAEGLQH SPTKHDLEKL IDAINAGRPQ CPVGLNTLVI PRKVNIGDQV NQPYVYLNCG HVQGHHDWGQ DENTGARRCP MCLELGPVVT LCMGLEPAFY VDVGAPTYAF NPCGHMATEK TVKYWANVEI PHGTNGFQAV CPFCATPLDG ATGYIKLIFQ DNLD // ID PLU_DROME STANDARD; PRT; 174 AA. AC P42570; Q9V910; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA replication inhibitor plutonium. GN PLU OR CG9183. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1; RX MEDLINE=94147993; PubMed=8313891; RA Axton J.M., Shamanski F.L., Young L.M., Henderson D.S., Boyd J.B., RA Orr-Weaver T.L.; RT "The inhibitor of DNA replication encoded by the Drosophila gene RT plutonium is a small, ankyrin repeat protein."; RL EMBO J. 13:462-470(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INHIBITS DNA REPLICATION EARLY IN DEVELOPMENTS. MAY BIND CC AND BLOCK THE ACTION OF A REPLICATION OR INITIATION FACTOR. CC -!- SIMILARITY: CONTAINS 2 ANK REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03986; AAB60211.1; -. DR EMBL; AE003792; AAF57492.1; -. DR PIR; S41713; S41713. DR FlyBase; FBgn0003114; plu. DR InterPro; IPR002110; ANK. DR Pfam; PF00023; ank; 2. DR SMART; SM00248; ANK; 2. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. KW DNA replication; ANK repeat; Repeat. FT REPEAT 39 68 ANK 1. FT REPEAT 72 103 ANK 2. FT VARIANT 97 97 S -> W. SQ SEQUENCE 174 AA; 19319 MW; E3506DD6D8BBC3FD CRC64; MGEINALSCV GQDDVVSLRI VCTMARDGKQ HNLEDVDMYG NTALLKACYL GRFECARTLL EFGANIFAMN YFGQNALTLA TYAGHLTLVK ELLRRRSYKD FNLSSMIPAL CVATLQKHSA LVAYFTQLDS RGVQETQTVH GLGVAELRGM IKAAGRLDKR NVRSPPTFIS NRLR // ID PNR_DROME STANDARD; PRT; 540 AA. AC P52168; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GATA-binding factor-A (Transcription factor GATA-A) (dGATA-A) (Pannier DE protein). GN PNR OR GATA-A OR CG3978. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94139551; PubMed=7916677; RA Winick J., Abel T., Leonard M.W., Michelson A.M., RA Chardon-Loriaux I., Holmgren R.A., Maniatis T., Engel J.D.; RT "A GATA family transcription factor is expressed along the embryonic RT dorsoventral axis in Drosophila melanogaster."; RL Development 119:1055-1065(1993). RN [2] RP SEQUENCE FROM N.A., AND MUTANTS PNRD1; PNRD2; PNRD3 AND PNRD4. RX MEDLINE=94139568; PubMed=7916679; RA Ramain P., Heitzler P., Haenlin M., Simpson P.; RT "Pannier, a negative regulator of achaete and scute in Drosophila, RT encodes a zinc finger protein with homology to the vertebrate RT transcription factor GATA-1."; RL Development 119:1277-1291(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP INTERACTION WITH OSA. RX MEDLINE=22515897; PubMed=12629041; RA Heitzler P., Vanolst L., Biryukova I., Ramain P.; RT "Enhancer-promoter communication mediated by Chip during RT Pannier-driven proneural patterning is regulated by Osa."; RL Genes Dev. 17:591-596(2003). CC -!- FUNCTION: TRANSCRIPTIONAL REGULATOR INVOLVED IN SEVERAL CC DEVELOPMENTAL PROCESSES DURING EMBRYONIC AND IMAGINAL DISKS CC DEVELOPMENT. INVOLVED IN DETERMINING DORSAL CELL FATE. ACTS AS AN CC ESSENTIAL TRANSCRIPTIONAL REGULATOR OF PRONEURAL ACHAETE-SCUTE CC COMPLEX (AS-C) AND IS REQUIRED FOR ITS SPATIAL REGULATION DURING CC DEVELOPMENT OF THE ADULT PERIPHERAL NERVOUS SYSTEM, AND HENCE FOR CC THE POSITIONING OF NEURAL PRECURSORS. IT IS THE ONLY FACTOR TO CC DIRECTLY ACTIVATE AS-C GENES. CC -!- SUBUNIT: INTERACTS WITH OSA. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: IT IS FIRST SEEN IN THE DORSAL PORTION OF THE CC EMBRYO JUST AFTER CELLULARIZATION AND IS EXPRESSED AT HIGH LEVELS CC DURING EARLY EMBRYOGENESIS AND AS DEVELOPMENT PROGRESSES HIGH CC LEVELS ARE SEEN IN THE DORSAL EPIDERMIS. CC -!- SIMILARITY: CONTAINS 2 GATA-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S68798; AAB29874.1; -. DR EMBL; S68909; AAB29874.1; JOINED. DR EMBL; S68793; AAB29874.1; JOINED. DR EMBL; S68795; AAB29874.1; JOINED. DR EMBL; S68803; AAB29876.2; -. DR EMBL; S68802; AAB29876.2; JOINED. DR EMBL; AE003711; AAN13693.1; -. DR HSSP; P17679; 1GNF. DR FlyBase; FBgn0003117; pnr. DR GO; GO:0007350; P:blastoderm segmentation; IMP. DR GO; GO:0007389; P:pattern specification; NAS. DR GO; GO:0042440; P:pigment metabolism; IMP. DR GO; GO:0045893; P:positive regulation of transcription, DNA-d...; NAS. DR InterPro; IPR000679; Znf_GATA. DR Pfam; PF00320; GATA; 2. DR PRINTS; PR00619; GATAZNFINGER. DR SMART; SM00401; ZnF_GATA; 2. DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2. DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2. KW Transcription regulation; Activator; DNA-binding; Zinc-finger; KW Nuclear protein. FT ZN_FING 169 193 GATA-TYPE 1. FT ZN_FING 226 250 GATA-TYPE 2. FT DOMAIN 333 336 POLY-SER. FT DOMAIN 345 364 POLY-GLN. FT DOMAIN 448 451 POLY-HIS. FT DOMAIN 462 465 POLY-ALA. FT DOMAIN 471 477 POLY-ALA. FT MUTAGEN 168 168 E->K: IN PNRD4; ABOLISHES DNA-BINDING. FT MUTAGEN 169 169 C->Y: IN PNRD1; ABOLISHES DNA-BINDING. FT MUTAGEN 186 186 G->E: IN PNRD2; ABOLISHES DNA-BINDING. FT MUTAGEN 190 190 C->S: IN PNRD3; ABOLISHES DNA-BINDING. FT CONFLICT 413 413 Y -> S (IN REF. 2). SQ SEQUENCE 540 AA; 57035 MW; 46557C0754BEEB59 CRC64; MGILLSDGDS TSDQQSTRDY PHFSGDYQNV TLSAASASTS ASASATHVAA VKMYHSSAVA AYTDLAAAGS AASAGVGVGV SGYHQQAVNA PVYVPSNRQY NHVAAHFGSA AAQNAWTTEG FGSAHAQFYS PNAAVMMGSW RSAYDPSGFQ RSSPYESAMD FQFGEGRECV NCGAISTPLW RRDGTGHYLC NACGLYHKMN GMNRPLIKPS KRLVSATATR RMGLCCTNCG TRTTTLWRRN NDGEPVCNAC GLYYKLHGVN RPLAMRKDGI QTRKRKPKKT GSGSAVGAGT GSGTGSTLEA IKECKEEHDL KPSLSLERHS LSKLHTDMKS GTSSSSTLMG HHSAQQQQQQ QQQQQQQQQQ QQQQSAHQQC FPLYGQTTTQ QQHQQHGHSM TSSSGQAHLS ARHLHGAAGT QLYTPGSSSG GGSASAYTSH SAETPALSNG TPSPHYQHHH HLGGTHGHHV TAAAAHHHFH AAAAVAAYGV KTEASATNYD YVNNCYFGGT FGALGGAATT TAMAGGAASE LAGYHHQHNV IQAAKLMATS // ID PNT1_DROME STANDARD; PRT; 623 AA. AC P51022; P19420; DT 01-NOV-1990 (Rel. 16, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE ETS-like protein pointed, isoform P1 (D-ETS-2). GN PNT OR ETS58AB OR ETS2 OR CG17077. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX MEDLINE=94038653; PubMed=8223245; RA Klaembt C.; RT "The Drosophila gene pointed encodes two ETS-like proteins which are RT involved in the development of the midline glial cells."; RL Development 117:163-176(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 456-613 FROM N.A. RX MEDLINE=92249640; PubMed=1577186; RA Chen T., Bunting M., Karim F.D., Thummel C.S.; RT "Isolation and characterization of five Drosophila genes that encode RT an ets-related DNA binding domain."; RL Dev. Biol. 151:176-191(1992). RN [5] RP SEQUENCE OF 445-603 FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=88196618; PubMed=2834248; RA Pribyl L.J., Watson D.K., McWilliams M.J., Ascione R., Papas T.S.; RT "The Drosophila ets-2 gene: molecular structure, chromosomal RT localization, and developmental expression."; RL Dev. Biol. 127:45-53(1988). CC -!- FUNCTION: REQUIRED FOR GLIAL-NEURONAL CELL INTERACTIONS AT THE CC VENTRAL MIDLINE WHICH ARE NECESSARY FOR THE PROPER ELABORATION OF CC COMMISSURES IN THE EMBRYONIC CNS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=P1; Synonyms=C; CC IsoId=P51022-1; Sequence=Displayed; CC Name=P2; Synonyms=B; CC IsoId=P51023-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN A COMPLEX DYNAMIC PATTERN IN CC EARLY EMBRYOS, INCLUDING THE MIDLINE AND MIDLINE GLIAL CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT WITH LOWER CC LEVELS DURING LARVAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69166; CAA48916.1; -. DR EMBL; AE003742; AAN13943.1; -. DR EMBL; M88472; AAC34200.1; -. DR EMBL; M20408; AAA28521.1; -. DR PIR; S33167; S33167. DR PIR; S33168; S33168. DR HSSP; P14921; 2STT. DR FlyBase; FBgn0003118; pnt. DR GO; GO:0005026; F:type II transforming growth factor-beta rec...; NAS. DR GO; GO:0006916; P:anti-apoptosis; IGI. DR GO; GO:0007173; P:EGF receptor signaling pathway; NAS. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0007179; P:TGFbeta receptor signaling pathway; NAS. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR GO; GO:0007424; P:tracheal system development (sensu Insecta); NAS. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR Pfam; PF00178; Ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW DNA-binding; Nuclear protein; Developmental protein; KW Alternative splicing. FT DOMAIN 38 46 POLY-SER. FT DOMAIN 47 50 POLY-ASN. FT DOMAIN 75 88 POLY-HIS. FT DOMAIN 103 111 POLY-GLN. FT DOMAIN 119 124 POLY-GLN. FT DOMAIN 128 134 POLY-GLN. FT DOMAIN 156 159 POLY-THR. FT DOMAIN 160 174 POLY-SER. FT DOMAIN 246 252 POLY-GLN. FT DOMAIN 264 267 POLY-ASN. FT DOMAIN 294 298 POLY-ASN. FT DOMAIN 310 320 POLY-ASN. FT DOMAIN 323 326 POLY-ALA. FT DOMAIN 386 389 POLY-GLY. FT DNA_BIND 515 595 ETS-DOMAIN. FT CONFLICT 467 467 Q -> R (IN REF. 5). SQ SEQUENCE 623 AA; 66866 MW; F47083D860EB6480 CRC64; MPPSAFLVNA SIISAANALD SDKEQQLQEH LNQSHFTSSS SSSNSSNNNN CHTAPNYNMV LQSYENYPSY HLAQHHHHHH HHHSHPHHQL AQQTGLHSHH TMQQQLQQQQ QSLLLQHPQQ QQQQHSHQSQ QQQQHGYGSS AQLPHHRLSG GSTGSTTTTS SGSSSSGSSS SASSQGFANG SATANNLVGA LSSSTAASLG LGYFNDMAPF VGDANAYYTD SDVNFFSSGY NTSNTHDRIN NSTPPQQQQS QQPTVNGSGS ASSNNNNSML PPAVQQSNNE NNNTSSSNTN NSSNNNNNSG GSNNSNAGSN NNNNNNNNIN FMAAAAIFQH HLKEEPGTQN GNIGGYGGGS NSQNDPTDLS SYGLPAHLAA YGGGSGSGPT GGRSSGGGGD ESDYHSTISA QDHQSQQSSG GNGSGGASGG STGNSNGYLD SSSEFYGSYA GRNRFHDGYP PEFTPYDAQS FQSMGPQPTA MDQWGAAHAH QHPAAYMSTL GLDKGLLGGY TTQGGVPCFT GSGPIQLWQF LLELLLDKTC QSFISWTGDG WEFKLTDPDE VARRWGIRKN KPKMNYEKLS RGLRYYYDKN IIHKTAGKRY VYRFVCDLQN LVGHTPEELV AKYDLKIEKK DVD // ID PNT2_DROME STANDARD; PRT; 718 AA. AC P51023; Q8IG92; Q9VCN2; DT 01-OCT-1996 (Rel. 34, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE ETS-like protein pointed, isoform P2 (D-ETS-2). GN PNT OR ETS58AB OR ETS2 OR CG17077. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX MEDLINE=94038653; PubMed=8223245; RA Klaembt C.; RT "The Drosophila gene pointed encodes two ETS-like proteins which are RT involved in the development of the midline glial cells."; RL Development 117:163-176(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-323 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 551-708 FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Canton-S; TISSUE=Larva; RX MEDLINE=92249640; PubMed=1577186; RA Chen T., Bunting M., Karim F.D., Thummel C.S.; RT "Isolation and characterization of five Drosophila genes that encode RT an ets-related DNA binding domain."; RL Dev. Biol. 151:176-191(1992). CC -!- FUNCTION: REQUIRED FOR GLIAL-NEURONAL CELL INTERACTIONS AT THE CC VENTRAL MIDLINE WHICH ARE NECESSARY FOR THE PROPER ELABORATION OF CC COMMISSURES IN THE EMBRYONIC CNS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=P2; Synonyms=B; CC IsoId=P51023-1; Sequence=Displayed; CC Name=P1; Synonyms=C; CC IsoId=P51022-1; Sequence=External; CC -!- TISSUE SPECIFICITY: EXPRESSED IN A COMPLEX DYNAMIC PATTERN IN CC EARLY EMBRYOS, INCLUDING THE MIDLINE AND MIDLINE GLIAL CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT WITH LOWER CC LEVELS DURING LARVAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -!- SIMILARITY: CONTAINS 1 POINTED (PNT) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69167; CAA48917.1; -. DR EMBL; AE003742; AAF56125.1; -. DR EMBL; BT001893; AAN71682.1; ALT_SEQ. DR EMBL; M88472; AAC34200.1; -. DR PIR; S33168; S33168. DR HSSP; P14921; 2STT. DR FlyBase; FBgn0003118; pnt. DR GO; GO:0005026; F:type II transforming growth factor-beta rec...; NAS. DR GO; GO:0006916; P:anti-apoptosis; IGI. DR GO; GO:0007173; P:EGF receptor signaling pathway; NAS. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0007179; P:TGFbeta receptor signaling pathway; NAS. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR GO; GO:0007424; P:tracheal system development (sensu Insecta); NAS. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR InterPro; IPR003118; SAM_PNT. DR Pfam; PF00178; Ets; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SMART; SM00251; SAM_PNT; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW DNA-binding; Nuclear protein; Developmental protein; KW Alternative splicing. FT DOMAIN 166 250 POINTED. FT DOMAIN 341 347 POLY-GLN. FT DOMAIN 359 362 POLY-ASN. FT DOMAIN 389 393 POLY-ASN. FT DOMAIN 405 415 POLY-ASN. FT DOMAIN 418 421 POLY-ALA. FT DOMAIN 481 484 POLY-GLY. FT DNA_BIND 610 690 ETS-DOMAIN. FT CONFLICT 133 135 DIS -> VYP (IN REF. 1). SQ SEQUENCE 718 AA; 77683 MW; FD6AFD0F4BCD69C5 CRC64; MELAICKTDL SATKFMLPPA LPSSAAIGSS SAVASTASHF LDKAAHELFQ LNAINGHLFK SPASSHLNSV GSPSILSQLN GIGNSGNHSG QVSTMRLKKN RKVTFLSSLV ESKNIFIKEE PIHGCKDLCS LSDISDHEAS LEVPTALPPL TPGTNRKVNE VLKASFASWE KEVQKCNITK DPREWTEEHV IYWLNWAKNE FSLVSMNLDP FYKMKGRAMV DLGKEKFLAI TPPFTGDILW EHLDILQKDC EKPNEDIVHG NSFESATTAS VCGSDHQVAN YPNETHANSN NSSINSRLSM DYVTSAGNSD NKNFHRATPH SHNGYNTSNT HDRINNSTPP QQQQSQQPTV NGSGSASSNN NNSMLPPAVQ QSNNENNNTS SSNTNNSSNN NNNSGGSNNS NAGSNNNNNN NNNINFMAAA AIFQHHLKEE PGTQNGNIGG YGGGSNSQND PTDLSSYGLP AHLAAYGGGS GSGPTGGRSS GGGGDESDYH STISAQDHQS QQSSGGNGSG GASGGSTGNS NGYLDSSSEF YGSYAGRNRF HDGYPPEFTP YDAQSFQSMG PQPTAMDQWG AAHAHQHPAA YMSTLGLDKG LLGGYTTQGG VPCFTGSGPI QLWQFLLELL LDKTCQSFIS WTGDGWEFKL TDPDEVARRW GIRKNKPKMN YEKLSRGLRY YYDKNIIHKT AGKRYVYRFV CDLQNLVGHT PEELVAKYDL KIEKKDVD // ID PNUT_DROME STANDARD; PRT; 539 AA. AC P40797; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Peanut protein. GN PNUT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94236682; PubMed=8181057; RA Neufeld T.P., Rubin G.M.; RT "The Drosophila peanut gene is required for cytokinesis and encodes a RT protein similar to yeast putative bud neck filament proteins."; RL Cell 77:371-379(1994). CC -!- FUNCTION: INVOLVED IN CYTOKINESIS AND POSSIBLY CELLULARIZATION. CC ALSO ACTS AS AN ENHANCER OF THE SINA GENE, THUS HAVING A ROLE IN CC PHOTORECEPTOR DEVELOPMENT. CC -!- SUBUNIT: MAY WELL ASSEMBLE INTO A MULTICOMPONENT STRUCTURE. CC -!- SUBCELLULAR LOCATION: LOCALIZED TO THE CLEAVAGE FURROW OF DIVIDING CC CELLS DURING CYTOKINESIS AND TO THE INTERCELLULAR BRIDGE CC CONNECTING POSTMITOTIC DAUGHTER CELLS. EQUALLY FOUND ON THE CELL CC SURFACES OF THE EMBRYONIC CENTRAL NERVOUS SYSTEM AND ON THE APICAL CC MEMBRANES OF DEVELOPING PHOTORECEPTOR CELLS IN THE EYE IMAGINAL CC DISC. CC -!- DEVELOPMENTAL STAGE: MATERNAL GENE PRODUCTS FOUND IN THE EARLY CC EMBRYO PRIOR TO ZYGOTIC TRANSCRIPTION. CC -!- SIMILARITY: BELONGS TO THE SEPTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U08103; AAA19603.1; -. DR PIR; A54294; A54294. DR FlyBase; FBgn0013726; pnut. DR GO; GO:0003779; F:actin binding; IDA. DR GO; GO:0008017; F:microtubule binding; IDA. DR InterPro; IPR000038; GTP_Cell_Div. DR Pfam; PF00735; GTP_CDC; 1. DR ProDom; PD002565; GTP_Cell_Div; 1. KW Cell division; GTP-binding; Coiled coil. FT NP_BIND 149 156 GTP (POTENTIAL). FT DOMAIN 420 516 COILED COIL (POTENTIAL). SQ SEQUENCE 539 AA; 60200 MW; 9299244FE4E0E95D CRC64; MNSPRSNAVN GGSGGAISAL PSTLAQLALR DKQQAASASA SSATNGSSGS ESLVGVGGRP PNQPPSVPVA ASGKLDTSSG GASNGDSNKL THDLQEKEHQ QAQKPQKPPL PVRQKPMEIA GYVGFANLPN QVYRKAVKRG FEFTLMVVGA SGLGKSTLIN SMFLSDIYNA EQYPGPSLRK KKTVAVEATK VMLKENGVNL TLTVVDTPGF GDAVDNSNCW VPILEYVDSK YEEYLTAESR VYRKTISDNR VHCCLYFIAP SGHGLLPLDI ACMQSLSDKV NLVPVIAKAD TMTPDEVHLF KKQILNEIAQ HKIKIYDFPA TLEDAAEEAK TTQNLRSRVP FAVVGANTII EQDGKKVRGR RYPWGLVEVE NLTHCDFIAL RNMVIRTHLQ DLKDVTNNVH YENYRCRKLS ELGLVDGKAR LSNKNPLTQM EEEKREHEQK MKKMEAEMEQ VFDMKVKEKM QKLRDSELEL ARRHEERKKA LELQIRELEE KRREFEREKK EWEDVNHVTL EELKRRSLGA NSSTDNVDGK KEKKKKGLF // ID POF_DROME STANDARD; PRT; 495 AA. AC Q9W123; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Painting of fourth protein (Zeste-interacting protein 16) (Zip16 DE protein). GN POF OR CG3691. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; RX MEDLINE=21267405; PubMed=11353870; RA Larsson J., Chen J.D., Rasheva V., Rasmuson-Lestander A., Pirrotta V.; RT "Painting of fourth, a chromosome-specific protein in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 98:6273-6278(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP PARTIAL SEQUENCE FROM N.A., AND INTERACTION WITH ZESTE. RA Chen J.D.; RL Thesis (1992), Baylor College of Medicine / Houston, U.S.A. CC -!- FUNCTION: PROBABLE RNA-BINDING PROTEIN THAT SPECIFICALLY BINDS TO CC THE FOURTH CHROMOSOME AND MAY BIND A RNA THAT SPREADS THE FOURTH CC CHROMOSOME. MAY BE A REMINISCENCE OF X CHROMOSOME DOSAGE CC COMPENSATION OF ANCESTRAL DROSOPHILA SPECIES IN WHICH THE X AND CC THE FOURTH CHROMOSOMES ARE ONE SINGLE CHROMOSOME. CC -!- SUBUNIT: INTERACTS WITH ZESTE. CC -!- SUBCELLULAR LOCATION: NUCLEAR; SPECIFICALLY BINDS TO THE FOURTH CC CHROMOSOME. CC -!- TISSUE SPECIFICITY: WEAKLY EXPRESSED IN EMBRYOS. EXPRESSION CC INCREASES DURING LARVAL AND PUPAL STAGES. IN ADULTS, IT IS CC PREDOMINANTLY EXPRESSED IN MALES, WHILE IT IS WEAKLY EXPRESSED IN CC FEMALES. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ295236; CAC16735.1; -. DR EMBL; AE003464; AAM68326.1; -. DR EMBL; AY052060; AAK93484.1; -. DR FlyBase; FBgn0035047; Pof. DR GO; GO:0000228; C:nuclear chromosome; IDA. DR GO; GO:0003723; F:RNA binding; NAS. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW RNA-binding; Nuclear protein. FT DOMAIN 215 289 RNA-BINDING (RRM). FT DOMAIN 351 367 BIPARTITE NUCLEAR LOCALIZATION SIGNAL FT (POTENTIAL). SQ SEQUENCE 495 AA; 55103 MW; F880E426EA88766D CRC64; MDSKRAALES GDGPDAKRLD TTDDQDKEAS GGDGSQVMLA KHVAPYTGHG CTPPMESYLF EPTPAGSQLL PWKTSVDLDN DAELEKPTSD KKPDTAKLSR RELAKMRREH TLRALALERE LTNKPGQTPA SEVLLVRFPD PEITAPMLAG LSKDIRDVVL PISVAPRYCL VHLKAGADVE ATICDINRVR FGTGHLRAEL KPFSDEEQAE FIDPCSLYVG NIPFNMTTSA IKAYFANAMR VDIGVLKREK RARYAFVRYA SPDQTMEAFK ELVDSPLNSR TLTVRYRRLR KRAGMPMVQC ATSFQALQSP NGDDDNTDCK VISPPPLESI IISDSDNCSD SSGNGKEDGK RKKKINEQER EIEKLKRQMA EYGAIIKSLQ FRQNSLEDTF IPDLTPKVEP SVNPTGCLLG SNAVHLMRDI KKECDYLGIP DPVPATKPTT QAQDDSQKKA KRSCFGRLFT GPFRRGTSAM KTADEYEKDD RLEELYAQLE RDPDP // ID POK_DROME STANDARD; PRT; 732 AA. AC Q01842; Q9VQ81; DT 01-OCT-1993 (Rel. 27, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Ets DNA-binding protein pokkuri (Protein yan) (Protein anterior open). GN AOP OR POK OR YAN OR CG3166. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92370682; PubMed=1505027; RA Lai Z.C., Rubin G.M.; RT "Negative control of photoreceptor development in Drosophila by the RT product of the yan gene, an ETS domain protein."; RL Cell 70:609-620(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92357729; PubMed=1495974; RA Tei H., Nihonmatsu I., Yokokura T., Ueda R., Sano Y., Okuda T., RA Sato K., Hirata K., Fujita S.C., Yamamoto D.; RT "Pokkuri, a Drosophila gene encoding an E-26-specific (Ets) domain RT protein, prevents overproduction of the R7 photoreceptor."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6856-6860(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NEGATIVE REGULATOR OF PHOTORECEPTOR DEVELOPMENT THAT CC ACTS ANTAGONISTICALLY TO THE PRONEURAL SIGNAL MEDIATED BY RAS. CC IT ACTS UPSTREAM OF SINA TO INHIBIT R7 DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EYE. CC -!- DEVELOPMENTAL STAGE: EMBRYO. CC -!- MISCELLANEOUS: 'POKKURI' MEANS 'DROPPING DEAD' IN JAPANESE. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. CC -!- SIMILARITY: CONTAINS 1 POINTED (PNT) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97693; AAA29023.1; -. DR EMBL; D10228; BAA01080.1; -. DR EMBL; AE003584; AAF51297.1; -. DR PIR; A43315; A43315. DR PIR; A46193; A46193. DR HSSP; P28324; 1BC8. DR TRANSFAC; T01396; -. DR FlyBase; FBgn0000097; aop. DR GO; GO:0003700; F:transcription factor activity; NAS. DR GO; GO:0016564; F:transcriptional repressor activity; NAS. DR GO; GO:0001709; P:cell fate determination; IMP. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0006917; P:induction of apoptosis; IMP. DR GO; GO:0007254; P:JNK cascade; NAS. DR GO; GO:0045596; P:negative regulation of cell differentiation; NAS. DR GO; GO:0046580; P:negative regulation of RAS protein signal t...; NAS. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. DR InterPro; IPR003118; SAM_PNT. DR Pfam; PF00178; Ets; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SMART; SM00251; SAM_PNT; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW DNA-binding; Nuclear protein; Photoreceptor; Developmental protein; KW Transcription regulation; Repressor. FT DOMAIN 31 117 POINTED. FT DOMAIN 313 322 POLY-GLN. FT DOMAIN 332 349 GLN-RICH. FT DNA_BIND 396 479 ETS-DOMAIN. FT DOMAIN 528 539 GLN-RICH. FT CONFLICT 27 27 R -> C (IN REF. 2). FT CONFLICT 182 284 PPPSVDSQASSPPQAPYQNGGATGAAPGSAGGSAPAAGGAT FT NTSNPTSSSASSTGSNGSQPNIMPMKGISSASSNHSDSEEE FT YSETSGGVSKMPPAPLSYSTA -> VLRPRWIPRRVVLPRH FT LTKMEEPLVQHQDQQEISTSCRRSHKHQQSHVVECQQHRQQ FT WLPAEHYAHEGYLAVPAVITLIPRRSTLRPVVEEQDAYLAH FT CPTARP (IN REF. 2). FT CONFLICT 505 505 G -> S (IN REF. 1). FT CONFLICT 527 527 P -> A (IN REF. 2). FT CONFLICT 553 573 VAAVAAAAAAAYGPPPTSPLF -> RCSGTTSGCCGLWSTT FT HIAAL (IN REF. 2). FT CONFLICT 614 614 P -> S (IN REF. 2). FT CONFLICT 695 732 ASSSPRPMDQASEQAQPVPMESDCNGGESEDSFRHMQQ -> FT VQQSHPGPWIRPVNRHSQCRWKAIAMAASRRTPSDTCSSRR FT RSVLRQSPHYIHLPLPPKHTQHYLS (IN REF. 2). SQ SEQUENCE 732 AA; 78573 MW; 25D36A652BA67176 CRC64; MSKMKMLPVQ LSLNSLNPGI WSDVLWRCPP APSSQLAELK TQLPPSLPSD PRLWSREDVL VFLRFCVREF DLPKLDFDLF QMNGKALCLL TRADFGHRCP GAGDVLHNVL QMLIIESHMM QWHLPNSPVT PTSRYPLSPH SHPPTPTWPP LNAPPENSPF HSSAHSLAGH HFMAPNSVTL SPPPSVDSQA SSPPQAPYQN GGATGAAPGS AGGSAPAAGG ATNTSNPTSS SASSTGSNGS QPNIMPMKGI SSASSNHSDS EEEYSETSGG VSKMPPAPLS YSTASPPGTP ILKDIKPNWT QQLTNSFVNS WSQQQQQQQQ QQAAAVAAVA AQAQQHQLQQ QQQQQQLPQK LTLDNTAGPV VTPAGGSISA PTTPSYMYKA KREFFPENSE PNTNGRLLWD FLQQLLNDRN QKYSDLIAWK CRDTGVFKIV DPAGLAKLWG IQKNHLSMNY DKMSRALRYY YRVNILRKVQ GERHCYQFLR NPTELKNIKN ISLLRQSTPA NGNGGSPSMP QGSSQAPGSP AGQNWNPQQQ SQQQQQSPQR PASRNGPMSL PAVAAVAAAA AAAYGPPPTS PLFMHAINGA FHYLSAAAAG PPPNSPALNT PSAVGGPDKF QFHPLKLENG SGSGSESAGE DLKPTDLSVS SKSTATSNED CYPLIRNADG LTTIKLIRYN EHQVAASPAG QSPKHDDQQA GASNASSSPR PMDQASEQAQ PVPMESDCNG GESEDSFRHM QQ // ID POL2_DROME STANDARD; PRT; 1059 AA. AC P20825; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Retrovirus-related Pol polyprotein from transposon 297 [Contains: DE Protease (EC 3.4.23.-); Reverse transcriptase (EC 2.7.7.49); DE Endonuclease]. GN POL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86108354; PubMed=2417839; RA Inouye S., Yuki S., Saigo K.; RT "Complete nucleotide sequence and genome organization of a Drosophila RT transposable genetic element, 297."; RL Eur. J. Biochem. 154:417-425(1986). CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -!- SIMILARITY: THE PROTEASE BELONGS TO PEPTIDASE FAMILY U22. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03431; CAB57796.1; ALT_SEQ. DR PIR; B24872; B24872. DR MEROPS; A02.052; -. DR FlyBase; FBgn0027622; 297\pol. DR InterPro; IPR001969; Aspprotease_AS. DR InterPro; IPR009007; Pept_A_acid. DR InterPro; IPR001995; Peptidase_A2. DR InterPro; IPR001584; Rve. DR InterPro; IPR000477; RVTse. DR Pfam; PF00665; rve; 1. DR Pfam; PF00077; rvp; 1. DR Pfam; PF00078; rvt; 1. DR PROSITE; PS00141; ASP_PROTEASE; 1. KW Hydrolase; Aspartyl protease; RNA-directed DNA polymerase; KW Endonuclease; Transferase; Polyprotein; Transposable element. FT ACT_SITE 30 30 PROTEASE (BY SIMILARITY). SQ SEQUENCE 1059 AA; 123310 MW; 3905CF38E914173D CRC64; TKRKFSVNSS GKYEYIKIVY KGRSYKCLLD TGSTINMINE NIFCLPIQNS RCEVLTSNGP ITLNDLIMLP RNSIFKKTEP FYVHRFSNNY DMLIGRKLLK NAQSVINYKN DTVTLFDQTY KLITSESERN QNLYIQRTPE SIASSDQESI KKLDFSQFRL DHLNQEETFK LKGLLNKFRN LEYKEGEKLT FTNTIKHVLN TTHNSPIYSK QYPLAQTHEI EVENQVQEML NQGLIRESNS PYNSPTWVVP KKPDASGANK YRVVIDYRKL NEITIPDRYP IPNMDEILGK LGKCQYFTTI DLAKGFHQIE MDEESISKTA FSTKSGHYEY LRMPFGLRNA PATFQRCMNN ILRPLLNKHC LVYLDDIIIF STSLTEHLNS IQLVFTKLAD ANLKLQLDKC EFLKKEANFL GHIVTPDGIK PNPIKVKAIV SYPIPTKDKE IRAFLGLTGY YRKFIPNYAD IAKPMTSCLK KRTKIDTQKL EYIEAFEKLK ALIIRDPILQ LPDFEKKFVL TTDASNLALG AVLSQNGHPI SFISRTLNDH ELNYSAIEKE LLAIVWATKT FRHYLLGRQF LIASDHQPLR WLHNLKEPGA KLERWRVRLS EYQFKIDYIK GKENSVADAL SRIKIEENHH SEATQHSAEE DNSNLIHLTE KPINYFKKQI IFIKSDKNKV EHSKIFGNSI TTIQYDVMTL EKAKQILLDH FIHRNITIYI ESDVDFEIVQ RAHIEIVNTT YTKVIRSLFL LKNVGSYAEF KEIILQSHEK LLHPGIQKMT KLFKENHFFP NSQLLIQNII NECNICNLAK TEHRNTKMPL KITPNPEHCR EKFVVDIYSS EGKHYISCID IYSKFATLEQ IKTKDWIECR NALMRIFNQL GKPKLLKADR DGAFSSLALK RWLEEEEVEL QLNTAKNGVA DVERLHKTIN EKIRIINSSD DEEVKLSKIE TILYTYNQKI KHDTTGQRPA QIFLYAGHPI LDTQKIKEKK IEKINEDRRE FNIDTNYRKG PLQKGKLENP FKPTKNVEQT DPDHYKITNR NRVTHYYKTQ FKKQKKNNKL SISQAPGTR // ID POL3_DROME STANDARD; PRT; 1058 AA. AC P04323; DT 20-MAR-1987 (Rel. 04, Created) DT 20-MAR-1987 (Rel. 04, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Retrovirus-related Pol polyprotein from transposon 17.6 [Contains: DE Protease (EC 3.4.23.-); Reverse transcriptase (EC 2.7.7.49); DE Endonuclease]. GN POL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85061628; PubMed=6209583; RA Saigo K., Kugimiya W., Matsuo Y., Inouye S., Yoshioka K., Yuki S.; RT "Identification of the coding sequence for a reverse transcriptase- RT like enzyme in a transposable genetic element in Drosophila RT melanogaster."; RL Nature 312:659-661(1984). CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -!- MISCELLANEOUS: THE OPEN READING FRAME IS LOCATED IN A COPIA-LIKE CC TRANSPOSABLE ELEMENT CALLED 17.6. CC -!- SIMILARITY: THE PROTEASE BELONGS TO PEPTIDASE FAMILY U22. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01472; CAA25702.1; -. DR PIR; A03971; GNFF17. DR MEROPS; A02.052; -. DR FlyBase; FBgn0014453; 17.6\pol. DR InterPro; IPR001969; Aspprotease_AS. DR InterPro; IPR009007; Pept_A_acid. DR InterPro; IPR001995; Peptidase_A2. DR InterPro; IPR001584; Rve. DR InterPro; IPR000477; RVTse. DR Pfam; PF00665; rve; 1. DR Pfam; PF00077; rvp; 1. DR Pfam; PF00078; rvt; 1. DR PROSITE; PS00141; ASP_PROTEASE; 1. KW Hydrolase; Aspartyl protease; RNA-directed DNA polymerase; KW Endonuclease; Transferase; Polyprotein; Transposable element. FT ACT_SITE 30 30 PROTEASE (BY SIMILARITY). SQ SEQUENCE 1058 AA; 122697 MW; C893F5C4A7E1F091 CRC64; TGRKFSATSL GKPQYITIKY KENNLKCLID TGSTVNMTSK NIFDLPIQNT STFIHTSNGP LIVNKSIIIP SKILFPTTNE FLLHPFSENY DLLLGRKLLA EAKATISYRD QEVTLYNNKY KLIEGIATHE QSHFQNVNMI PDTMLRQPNK ISPILESDLY RLEHLNNEEK QRLCALLQKY HDIQYHEGDK LTFTNQTKHT INTKHNLPLY SKYSYPQAYE QEVESQIQDM LNQGIIRTSN SPYNSPIWVV PKKQDASGKQ KFRIVIDYRK LNEITVGDRH PIPNMDEILG KLGRCNYFTT IDLAKGFHQI EMDPESVSKT AFSTKHGHYE YLRMPFGLKN APATFQRCMN DILRPLLNKH CLVYLDDIIV FSTSLDEHLQ SLGLVFEKLA KANLKLQLDK CEFLKQETTF LGHVLTPDGI KPNPEKIEAI QKYPIPTKPK EIKAFLGLTG YYRKFIPNFA DIAKPMTKCL KKNMKIDTTN PEYDSAFKKL KYLISEDPIL KVPDFTKKFT LTTDASDVAL GAVLSQDGHP LSYISRTLNE HEINYSTIEK ELLAIVWATK TFRHYLLGRH FEISSDHQPL SWLYRMKDPN SKLTRWRVKL SEFDFDIKYI KGKENCVADA LSRIKLEETY LSEQTQHSAE EDNSDLIFIT ERPLNTFNRQ VIFSKGPPDI KVTKYFKKHI TQIFYDIMTR EKAEQYLIDH FCGKKSALYI ESDADFEVIQ AAHKLAINTK YTKILRSTIL LKNITTYAEF KELILTAHEK LLHPGIQKTT KLFGETYYFP NSQLLIQNII NECSICNLAK TEHRNTDMPT KTTPKPEHCR EKFMIDIYSS EGKHYVSCID IYSKFATLEE IKTKDWIECK NALMRIFNQL GKPKLLKADR DGAFSSLALK RWLESEEVEL QLNTTKTGVA DIERLHKTIN EKIRIIKTSD DEETKLSKME TVLNIYNHKT KHDTTGQTPA HIFLYAGQPI LDTQQNKENK INKINNDRVE YEVDTRYRKG PLQKGKLENP FKPTKNVEQT DSDHYKITNR NRITHYYKTQ FKKRKKNNQL SISQAPGT // ID POL4_DROME STANDARD; PRT; 1237 AA. AC P10394; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Retrovirus-related Pol polyprotein from transposon 412 [Contains: DE Protease (EC 3.4.23.-); Reverse transcriptase (EC 2.7.7.49); DE Endonuclease]. GN POL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86274717; PubMed=2426108; RA Yuki S., Inouye S., Ishimaru S., Saigo K.; RT "Nucleotide sequence characterization of a Drosophila retrotransposon, RT 412."; RL Eur. J. Biochem. 158:403-410(1986). CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -!- SIMILARITY: THE PROTEASE BELONGS TO PEPTIDASE FAMILY U22. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04132; CAA27750.1; -. DR PIR; D29349; GNFF42. DR MEROPS; A02.UPW; -. DR FlyBase; FBgn0043847; 412\ORF3. DR InterPro; IPR001969; Aspprotease_AS. DR InterPro; IPR009007; Pept_A_acid. DR InterPro; IPR001995; Peptidase_A2. DR InterPro; IPR001584; Rve. DR InterPro; IPR000477; RVTse. DR Pfam; PF00665; rve; 1. DR Pfam; PF00077; rvp; 1. DR Pfam; PF00078; rvt; 1. DR PROSITE; PS00141; ASP_PROTEASE; 1. DR PROSITE; PS50175; ASP_PROT_RETROV; 1. KW Hydrolase; Aspartyl protease; RNA-directed DNA polymerase; KW Endonuclease; Transferase; Polyprotein; Transposable element. FT ACT_SITE 63 63 PROTEASE (BY SIMILARITY). SQ SEQUENCE 1237 AA; 143041 MW; AC57F1C159D14B65 CRC64; QQSEQLQQKQ CQCTSNPRTG QLATAFRYSV EEDRRVYTIN YNLNIFSTFI HAKTGVKLVF LLDTGADISI LKENSDKFSN IQITNKINIQ GIGQQKIQSR GQTFIEIQTG KYVIPHDFHL VDKNFPIPCD GIIGIDFIKK YNCQIDLNQE EDWFIIRPNN LKFPIYIPIA YSSGINTTLL PARSQVVRRL IVSSKDDNIL IPNQEIQTGI YVANTIATSS NTFVRILNTT DSDQLVNMDT LKYEPLSNYN VVQANSEHRN KTVLSQLKKN FPELFKSQLE NICSEYIDIF ALESEPITVN NLYKQQLRLK DDEPVYTKNY RSPHSQVEEI QAQVQKLIKD KIVEPSVSQY NSPLLLVPKK SSPNSDKKKW RLVIDYRQIN KKLLADKFPL PRIDDILDQL GRAKYFSCLD LMSGFHQIEL DEGSRDITSF STSNGSYRFT RLPFGLKIAP NSFQRMMTIA FSGIEPSQAF LYMDDLIVIG CSEKHMLKNL TEVFGKCREY NLKLHPEKCS FFMHEVTFLG HKCTDKGILP DDKKYDVIQN YPVPHDADSA RRFVAFCNYY RRFIKNFADY SRHITRLCKK NVPFEWTDEC QKAFIHLKSQ LINPTLLQYP DFSKEFCITT DASKQACGAV LTQNHNGHQL PVAYASRAFT KGESNKSTTE QELAAIHWAI IHFRPYIYGK HFTVKTDHRP LTYLFSMVNP SSKLTRIRLE LEEYNFTVEY LKGKDNHVAD ALSRITIKEL KDITGNILKV TTRFQSRQKS CAGKEQLDLQ KQTKEIASEP NVYEVITNDE VRKVVTLQLN DSICLFKHGK KIIARYDVGD LYTNGILDLD QFLQRLELQA GIYDISQIKM APWKKIFEHV SIDKFKNMGN KILKNLKVAL LNPVTQINNE KEKEAILSTL HDDPIQGGHT GITKTLAKVK RHYYWKNMSK YIKEYVRKCQ KCQKAKTTKH TKTPMTITET PEHAFDRVVV DTIGPLPKSE NGNEYAVTLI CDLTKYLVAI PIANKSAKTV AKAIFESFIL KYGPMKTFIT DMGTEYKNSI ITDLCKYLKI KNITSTAHHH QTVGVVERSH RTLNEYIRSY ISTDKTDWDV WLQYFVYCFN TTQSMVHNYC PYELVFGRTS NLPKHFNKLH SIEPIYNIDD YAKESKYRLE VAYARARKLL EAHKEKNKEN YDLKVKDIEL EVGDKVLLRN EVGHKLDFKY TGPYKIESIG DNNNITLLTN KNKKQIVHKD RLKKFHS // ID POL5_DROME STANDARD; PRT; 1003 AA. AC Q8I7P9; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Retrovirus-related Pol polyprotein from transposon opus [Contains: DE Protease (EC 3.4.23.-); Reverse transcriptase (EC 2.7.7.49); DE Endonuclease]. GN POL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426070; PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J.W., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY180918; AAN87271.1; -. DR FlyBase; FBgn0025875; opus\pol. DR InterPro; IPR009007; Pept_A_acid. DR InterPro; IPR001584; Rve. DR InterPro; IPR000477; RVTse. DR Pfam; PF00665; rve; 1. DR Pfam; PF00078; rvt; 1. KW Hydrolase; Transferase; Protease; Endonuclease; KW RNA-directed DNA polymerase; Polyprotein; Transposable element. SQ SEQUENCE 1003 AA; 114634 MW; C28AA23D6CEB8655 CRC64; MITHRLVGKF FKPLGNDSDI TFFVLPNLHS FDGIIGDDTL KDLKAIVDRK NNCLIITPGI KIPLLARASI NVNPLLAAEH PDGTQEILNS LLGEFPRIFE PPLSGMSVET AVKAEIRTNT QDPIYAKSYP YPVNMRGEVE RQIDELLQDG IIRPSNSPYN SPIWIVPKKP KPNGEKQYRM VVDFKRLNTV TIPDTYPIPD INATLASLGN AKYFTTLDLT SGFHQIHMKE SDIPKTAFST LNGKYEFLRL PFGLKNAPAI FQRMIDDILR EHIGKVCYVY IDDIIVFSED YDTHWKNLRL VLASLSKANL QVNLEKSHFL DTQVEFLGYI VTADGIKADP KKVRAISEMP PPTSVKELKR FLGMTSYYRK FIQDYAKVAK PLTNLTRGLY ANIKSSQSSK VPITLDETAL QSFNDLKSIL CSSEILAFPC FTKPFHLTTD ASNWAIGAVL SQDDQGRDRP IAYISRSLNK TEENYATIEK EMLAIIWSLD NLRAYLYGAG TIKVYTDHQP LTFALGNRNF NAKLKRWKAR IEEYNCELIY KPGKSNVVAD ALSRIPPQLN QLSTDLDANP EDDMQSLATA HSALHDSSRL IPHVESPINV FKNQLIFDTT RSKYLCEHPF PGYTRHLIPL KDGSLADLTN SLQSCLRPVI INGVKIPEAH LQRFQSICLA NFLLYKIRIT QRLVADVSGA EEICEIIEKE HRRAHRGPTE IRLQLLEKYY FPRMSSTIRL QTSSCQCCKL YKYERHPNKP NLQPTPIPNY PCEILHIDIF ALEKRLYLSC IDKFSKFAKL FHLQSKASVH LRETLVEALH YFTAPKVLVS DNERGLLCPT VLNYLRSLDI DLYYAPTQKS EVNGQVERFH STFLEIYRCL KDELPTFKPV ELVHIAVDRY NTSVHSVTNR KPADVFFDRS SRVNYQGLTD FRRQTLEDIK GLIEYKQIRG NMARNKNRDE PKSYGPGDEV FVANKQIKTK EKARFRCEKV QEDNKITVKT RSGKIFHKSD LRN // ID POLO_DROME STANDARD; PRT; 576 AA. AC P52304; Q9VWB2; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein kinase polo (EC 2.7.1.-). GN POLO OR CG12306. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92084090; PubMed=1660828; RA Llamazares S., Moreira A., Tavares A., Girdham C., Spruce B.A., RA Gonzalez C., Karess R.E., Glover D.M., Sunkel C.E.; RT "Polo encodes a protein kinase homolog required for mitosis in RT Drosophila."; RL Genes Dev. 5:2153-2165(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY PLAY A ROLE IN REGULATING BOTH NUCLEAR AND CC CYTOPLASMIC ASPECTS OF THE MITOTIC CYCLE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: LARVAL DISCS, BRAIN AND TESTIS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CDC5/POLO SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 POLO BOX DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63361; CAA44963.1; -. DR EMBL; AE003514; AAF49036.1; -. DR PIR; S22127; S22127. DR HSSP; Q63450; 1A06. DR FlyBase; FBgn0003124; polo. DR GO; GO:0005813; C:centrosome; IDA. DR GO; GO:0005819; C:spindle; IDA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA. DR GO; GO:0007140; P:male meiosis; IMP. DR GO; GO:0007067; P:mitosis; IMP. DR InterPro; IPR000959; POLO_box. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00659; POLO_box; 2. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS50078; POLO_BOX; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; Repeat. FT DOMAIN 25 277 PROTEIN KINASE. FT NP_BIND 31 39 ATP (BY SIMILARITY). FT BINDING 54 54 ATP (BY SIMILARITY). FT ACT_SITE 148 148 BY SIMILARITY. FT DOMAIN 398 461 POLO BOX 1. FT DOMAIN 496 564 POLO BOX 2. FT CONFLICT 187 187 P -> A (IN REF. 1). SQ SEQUENCE 576 AA; 66973 MW; 5022B9AC0E888FAD CRC64; MAAKPEDKST DIPDRLVDIN QRKTYKRMRF FGKGGFAKCY EIIDVETDDV FAGKIVSKKL MIKHNQKEKT AQEITIHRSL NHPNIVKFHN YFEDSQNIYI VLELCKKRSM MELHKRRKSI TEFECRYYIY QIIQGVKYLH DNRIIHRDLK LGNLFLNDLL HVKIGDFGLA TRIEYEGERK KTLCGTPNYI APEILTKKGH SFEVDIWSIG CVMYTLLVGQ PPFETKTLKD TYSKIKKCEY RVPSYLRKPA ADMVIAMLQP NPESRPAIGQ LLNFEFLKGS KVPMFLPSSC LTMAPRIGSN DTIEDSMHRK PLMEMNGIRP DDTRLESTFL KANLHDAITA SAQVCRHSED YRSDIESLYQ QLTNLINGKP RILQGNLGDE NTDPAAQPLF WISKWVDYSD KYGFGYQLCD EGIGVMFNDT TKLILLPNQI NVHFIDKDGK ETYMTTTDYC KSLDKKMKLL SYFKRYMIEH LVKAGANNVN IESDQISRMP HLHSWFRTTC AVVMHLTNGS VQLNFSDHMK LILCPRMSAI TYMDQEKNFR TYRFSTIVEN GVSKDLYQKI RYAQEKLRKM LEKMFT // ID POLR_DROME STANDARD; PRT; 1057 AA. AC P16423; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Retrovirus-related POL polyprotein from type II retrotransposable DE element R2DM [Contains: Protease (EC 3.4.23.-); Reverse transcriptase DE (EC 2.7.7.49); Endonuclease]. GN POL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90204545; PubMed=1690812; RA Jakubczak J.L., Xiong Y., Eickbush T.H.; RT "Type I (R1) and type II (R2) ribosomal DNA insertions of Drosophila RT melanogaster are retrotransposable elements closely related to those RT of Bombyx mori."; RL J. Mol. Biol. 212:37-52(1990). CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -!- SIMILARITY: TO CORRESPONDING ORF OF BOMBYX MORI (R2BM). CC -!- SIMILARITY: TO A RETROVIRAL GAG-POL FUSION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51967; CAA36225.1; -. DR PIR; S09112; S09112. DR FlyBase; FBgn0016699; R2-element\ORF. DR InterPro; IPR000477; RVTse. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00078; rvt; 1. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. KW Hydrolase; Aspartyl protease; Transferase; Nuclease; KW RNA-directed DNA polymerase; Endonuclease; Polyprotein; KW Transposable element; Zinc-finger; Metal-binding. FT ZN_FING 61 84 C2H2-TYPE. SQ SEQUENCE 1057 AA; 120040 MW; 64989B5E215CD2AF CRC64; FERKNFSDGL VPQRKFIHIG TTSTNNEPRI PLHNLMTTRP SVDIFPEDQY EPNAAATLSR VPCTVCGRSF NSKRGLGVHM RSRHPDELDE ERRRVDIKAR WSDEEKWMMA RKEVELTANG CKHINKQLAV YFANRSVEAI KKLRQRGDYK EKIEQIRGQS ALAPEVANLT IRRRPSRSEQ DHQVTTSETT PITPFEQSNR EILRTLRGYS PVECHSKWRA QELQTIIDRA HLEGKETTLQ CLSLYLLGIF PAQGVRHTLT RPPRRPRNRR ESRRQQYAVV QRNWDKHKGR CIKSLLNGTD ESVMPSQEIM VPYWREVMTQ PSPSSCSGEV IQMDHSLERV WSAITEQDLR ASRVSLSSSP GPDGITPKSA REVPSGIMLR IMNLILWCGN LPHSIRLART VFIPKTVTAK RPQDFRPISV PSVLVRQLNA ILATRLNSSI NWDPRQRGFL PTDGCADNAT IVDLVLRHSH KHFRSCYIAN LDVSKAFDSL SHASIYDTLR AYGAPKGFVD YVQNTYEGGG TSLNGDGWSS EEFVPARGVK QGDPLSPILF NLVMDRLLRT LPSEIGAKVG NAITNAAAFA DDLVLFAETR MGLQVLLDKT LDFLSIVGLK LNADKCFTVG IKGQPKQKCT VLEAQSFYVG SSEIPSLKRT DEWKYLGINF TATGRVRCNP AEDIGPKLQR LTKAPLKPQQ RLFALRTVLI PQLYHKLALG SVAIGVLRKT DKLIRYYVRR WLNLPLDVPI AFVHAPPKSG GLGIPSLRWV APMLRLRRLS NIKWPHLTQN EVASSFLEAE KQRARDRLLA EQNELLSRPA IEKYWANKLY LSVDGSGLRE GGHYGPQHGW VSQPTRLLTG KEYMDGIRLR INALPTKSRT TRGRHELERQ CRAGCDAPET TNHIMQKCYR SHGRRVARHN CVVNRIKRGL EERGCVVIVE PSLQCESGLN KPDLVALRQN HIDVIDTQIV TDGHSMDDAH QRKINRYDRP DIRTELRRRF EAAGDIEFHS ATLNWRGIWS GQSVKRLIAK GLLSKYDSHI ISVQVMRGSL GCFKQFMYLS GFSRDWT // ID POLY_DROME STANDARD; PRT; 1035 AA. AC P10401; P10402; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Retrovirus-related POL polyprotein from transposon gypsy [Contains: DE Reverse transcriptase (EC 2.7.7.49); Endonuclease]. GN POL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87064379; PubMed=3023871; RA Marlor R.L., Parkhurst S.M., Corces V.G.; RT "The Drosophila melanogaster gypsy transposable element encodes RT putative gene products homologous to retroviral proteins."; RL Mol. Cell. Biol. 6:1129-1134(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92293139; PubMed=1318501; RA Smith P.A., Corces V.G.; RT "The suppressor of Hairy-wing binding region is required for gypsy RT mutagenesis."; RL Mol. Gen. Genet. 233:65-70(1992). RN [3] RP SEQUENCE OF 21-950 FROM N.A. RX MEDLINE=86176782; PubMed=2421255; RA Yuki S., Ishimaru S., Inouye S., Saigo K.; RT "Identification of genes for reverse transcriptase-like enzymes in two RT Drosophila retrotransposons, 412 and gypsy; a rapid detection method RT of reverse transcriptase genes using YXDD box probes."; RL Nucleic Acids Res. 14:3017-3030(1986). CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12927; AAA70219.1; ALT_INIT. DR EMBL; X03734; CAA27371.1; -. DR PIR; B25666; GNFFG1. DR MEROPS; A02.UPW; -. DR FlyBase; FBgn0014966; gypsy\pol. DR InterPro; IPR009007; Pept_A_acid. DR InterPro; IPR001995; Peptidase_A2. DR InterPro; IPR001584; Rve. DR InterPro; IPR000477; RVTse. DR Pfam; PF00665; rve; 1. DR Pfam; PF00077; rvp; 1. DR Pfam; PF00078; rvt; 1. KW Hydrolase; Endonuclease; Transferase; RNA-directed DNA polymerase; KW Polyprotein; Transposable element. FT CONFLICT 31 32 DA -> AR (IN REF. 3). FT CONFLICT 60 60 G -> R (IN REF. 3). FT CONFLICT 232 232 F -> S (IN REF. 3). FT CONFLICT 490 490 D -> V (IN REF. 3). FT CONFLICT 883 883 S -> T (IN REF. 3). FT CONFLICT 923 923 N -> S (IN REF. 3). FT CONFLICT 947 950 RPIE -> NQLR (IN REF. 3). SQ SEQUENCE 1035 AA; 117818 MW; 7B985CA272B8A5A6 CRC64; RLVEFFRGRS RLPFIERRLA GRTLKMLIDT DAAKNYIRPV KELKNVMPVA SPFSVSSIHG STEIKHKCLM KVFKHISPFF LLDSLNAFDA IIGLDLLTQA GVKLNLAEDS LEYQGIAEKL HYFSCPSVNF TDVNDIVVPD SVKKEFKDTI IRRKKAFSTT NEALPFNTAV TATIRTVDNE PVYSRAYPTL MGVSDFVNNE VKQLLKDGII RPSRSPYNSP TWVVDKKGTD AFGNPNKRLV IDFRKLNEKT IPDRYPMPSI PMILANLGKA KFFTTLDLKS GYHQIYLAEH DREKTSFSVN GGKYEFCRLP FGLRNASSIF QRALDDVLRE QIGKICYVYV DDVIIFSENE SDHVRHIDTV LKCLIDANMR VSQEKTRFFK ESVEYLGFIV SKDGTKSDPE KVKAIQEYPE PDCVYKVRSF LGLASYYRVF IKDFAAIARP ITDILKGENG SVSKHMSKKI PVEFNETQRN AFQRLRNILA SEDVILKYPD FKKPFDLTTD ASASGIGAVL SQEGRPITMI SRTLKQPEQN YATNERELLA IVWALGKLQN FLYGSREINI FTDHQPLTFA VADRNTNAKI KRWKSYIDQH NAKVFYKPGK ENFVADALSR QNLNALQNEP QSDAATIHSE LSLTYTVETT DKPLNCFRNQ IILEAARFPL KRNLVLFRSK SRHLISFTDK SWLLKTLKEV VNPDVVNAIH CDLPTLASFQ HDLIAHFPAT QFRHCKNVVL DITDKNEQIE IVTAEHNRAH RAAQENIKQV LRDYYFPKMG SLAKEVVANC RVCTQAKYDR HPKKQELGET PIPSYTGEMV HIDIFSTDRK LFLTCIDKFS KYAIVQPVVS RTIVDITAPL LQIINLFPNI KTVYCDNEPA FNSETVTSML KNSFGIDIVN APPLHSSSNG QVERFHSTLA EIARCLKLDK KTNDTVELIL RATIEYNKTV HSVTRERPIE VVHPGAHERC LEIKARLVKA QQDSIGRNNP SRQNRVFEVG ERVFVKNNKR LGNKLTPLCT EQKVQADLGT SVLIKGRVVH KDNLK // ID PORI_DROME STANDARD; PRT; 282 AA. AC Q94920; Q94997; Q9VKP1; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Voltage-dependent anion-selective channel (Porin protein). GN PORIN OR VDAC OR POR-1 OR CG6647. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Ryerse J., Blachly-Dyson E., Forte M., Nagel B.; RT "Cloning and molecular characterization of a voltage dependent RT anion-selective channel (VDAC) from Drosophila melanogaster."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=96390820; PubMed=8797793; RA Messina A., Neri M., Perosa F., Caggese C., Marino M., Caizzi R., RA De Pinto V.; RT "Cloning and chromosomal localization of a cDNA encoding a RT mitochondrial porin from Drosophila melanogaster."; RL FEBS Lett. 384:9-13(1996). RN [3] RP SEQUENCE FROM N.A. RA Oliva M., Messina A., De Pinto V.; RT "Drosophila melanogaster gene for mitochondrial porin. Discovery of RT two alternatively spliced exons in the 5'untranslated region."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: FORMS A CHANNEL THROUGH THE CELL MEMBRANE THAT ALLOWS CC DIFFUSION OF SMALL HYDROPHILIC MOLECULES (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: OUTER MITOCHONDRIAL MEMBRANE. CC -!- DOMAIN: CONSISTS MAINLY OF MEMBRANE-SPANNING SIDED BETA-SHEETS. CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC MITOCHONDRIAL PORIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U70314; AAC02635.1; -. DR EMBL; X92408; CAA63143.1; -. DR EMBL; X95692; CAA64988.1; -. DR EMBL; AJ000880; CAA04370.1; -. DR EMBL; AE003630; AAF53022.1; -. DR FlyBase; FBgn0004363; porin. DR GO; GO:0005741; C:mitochondrial outer membrane; NAS. DR InterPro; IPR001925; Porin_Euk. DR Pfam; PF01459; Euk_porin; 1. DR PRINTS; PR00185; EUKARYTPORIN. DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1. KW Outer membrane; Porin; Mitochondrion. FT CONFLICT 231 231 S -> R (IN REF. 2). FT CONFLICT 252 252 D -> T (IN REF. 2). SQ SEQUENCE 282 AA; 30550 MW; 173E165C3A2D297D CRC64; MAPPSYSDLG KQARDIFSKG YNFGLWKLDL KTKTSSGIEF NTAGHSNQES GKVFGSLETK YKVKDYGLTL TEKWNTDNTL FTEVAVQDQL LEGLKLSLEG NFAPQSGNKN GKFKVAYGHE NVKADSDVNI DLKGPLINAS AVLGYQGWLA GYQTAFDTQQ SKLTTNNFAL GYTTKDFVLH TAVNDGQEFS GSIFQRTSDK LDVGVQLSWA SGTSNTKFAI GAKYQLDDDA SVRAKVNNAS QVGLGYQQKL RDGVTLTLST LVDGKNFNAG GHKIGVGLEL EA // ID POXM_DROME STANDARD; PRT; 402 AA. AC P23757; Q9VHS5; DT 01-NOV-1991 (Rel. 20, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Paired box pox-meso protein (Paired box mesodermal protein). GN POXM OR POX-M OR CG9610. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 33-170 FROM N.A. RX MEDLINE=90059940; PubMed=2573516; RA Bopp D., Jamet E., Baumgartner S., Burri M., Noll M.; RT "Isolation of two tissue-specific Drosophila paired box genes, Pox RT meso and Pox neuro."; RL EMBO J. 8:3447-3457(1989). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: SOMATIC MESODERM. CC -!- SIMILARITY: CONTAINS 1 PAIRED BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003678; AAF54224.1; -. DR EMBL; X16992; CAA34860.1; -. DR PIR; S06950; S06950. DR HSSP; P26367; 6PAX. DR FlyBase; FBgn0003129; Poxm. DR InterPro; IPR001523; Paired_box. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00034; PAIRED_BOX; 1. KW DNA-binding; Developmental protein; Nuclear protein; Paired box; KW Transcription regulation. FT DOMAIN 41 165 PAIRED BOX. FT DOMAIN 221 229 POLY-HIS. FT DOMAIN 232 238 POLY-ALA. FT DOMAIN 261 264 POLY-ALA. FT DOMAIN 296 302 POLY-ALA. FT DOMAIN 386 391 POLY-HIS. FT CONFLICT 33 36 HIRK -> MDPE (IN REF. 2). SQ SEQUENCE 402 AA; 42202 MW; 59365496D8536440 CRC64; MRQGEIFASS LKVHFRTFRA FKLCFPSHNR GTHIRKSQCP QYGEVNQLGG VFVNGRPLPN ATRMRIVELA RLGIRPCDIS RQLRVSHGCV SKILARYHET GSILPGAIGG SKPRVTTPKV VNYIRELKQR DPGIFAWEIR DRLLSEGICD KTNVPSVSSI SRILRNKLGS LGHQHTPGTV MGSGSSSGGG SVSSNGGQNN GTSASNNINL SNLGNPGGGP HHPHHHHHHQ SAAAAASAHH VHAHAHAHAH LYNSIYQPYS AAAAYSMKTP CGSPSPPQGA GGQGSVPHPH QLRSVAAAAA AAHWPSSHSV SDILAHHQAV ALRASCQVGV GVGGMGGMGS TVSPLPMTPS PVAGTAGGQP LLDCEGGAGQ QSPYNYYMYF QNGGMHHHHH HGGMMAAGAT GL // ID POXN_DROME STANDARD; PRT; 425 AA. AC P23758; Q9V7F3; DT 01-NOV-1991 (Rel. 20, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Paired box pox-neuro protein (Paired box neuronal protein). GN POXN OR POX-N OR CG8246. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92208941; PubMed=1348214; RA Dambly-Chaudiere C., Jamet E., Burri M., Bopp D., Basler K., RA Hafen E., Dumont N., Spielmann P., Ghysen A., Noll M.; RT "The paired box gene pox neuro: a determinant of poly-innervated RT sense organs in Drosophila."; RL Cell 69:159-172(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-35 FROM N.A. RX MEDLINE=90059940; PubMed=2573516; RA Bopp D., Jamet E., Baumgartner S., Burri M., Noll M.; RT "Isolation of two tissue-specific Drosophila paired box genes, Pox RT meso and Pox neuro."; RL EMBO J. 8:3447-3457(1989). RN [4] RP FUNCTION. RX MEDLINE=94121914; PubMed=8292359; RA Nottebohm E., Usui A., Therianos S., Kimura K., Dambly-Chaudiere C., RA Ghysen A.; RT "The gene poxn controls different steps of the formation of RT chemosensory organs in Drosophila."; RL Neuron 12:25-34(1994). RN [5] RP FUNCTION. RX MEDLINE=97326936; PubMed=9183748; RA Awasaki T., Kimura K.; RT "pox-neuro is required for development of chemosensory bristles in RT Drosophila."; RL J. Neurobiol. 32:707-721(1997). CC -!- FUNCTION: TRANSCRIPTIONAL REGULATOR THAT SPECIFIES POLY-INNERVATED CC ORGANS (CHEMOSENSORY BRISTLE). ALSO CONTROLS THE NUMBER OF CC NEURONS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: CENTRAL AND PERIPHERAL NERVOUS SYSTEMS. CC -!- SIMILARITY: CONTAINS 1 PAIRED BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86927; AAA28832.1; -. DR EMBL; AE003809; AAF58104.1; -. DR EMBL; X58917; CAA41721.1; -. DR PIR; A38153; A38153. DR HSSP; P26367; 6PAX. DR FlyBase; FBgn0003130; Poxn. DR GO; GO:0007469; P:antennal morphogenesis; IMP. DR GO; GO:0007480; P:leg morphogenesis (sensu Holometabola); IMP. DR GO; GO:0007423; P:sensory organ development; IMP. DR GO; GO:0007476; P:wing morphogenesis; IMP. DR InterPro; IPR001523; Paired_box. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00034; PAIRED_BOX; 1. KW DNA-binding; Developmental protein; Nuclear protein; Paired box; KW Transcription regulation; Neurogenesis; Differentiation. FT DOMAIN 5 130 PAIRED BOX. FT DOMAIN 146 160 ALA-RICH. FT DOMAIN 173 217 PRO-RICH. FT DOMAIN 146 157 POLY-ALA. FT DOMAIN 173 176 POLY-PRO. FT DOMAIN 281 287 POLY-ALA. FT CONFLICT 343 343 P -> T (IN REF. 1). FT CONFLICT 377 377 S -> R (IN REF. 1). FT CONFLICT 411 411 A -> G (IN REF. 1). SQ SEQUENCE 425 AA; 44328 MW; 59B01A4F97C1B126 CRC64; MPHTGQAGVN QLGGVFVNGR PLPDCVRRRI VDLALCGVRP CDISRQLLVS HGCVSKILTR FYETGSIRPG SIGGSKTKQV ATPTVVKKII RLKEENSGMF AWEIREQLQQ QRVCDPSSVP SISSINRILR NSGLWTDEMT SSQQNAAAAA AAAAAAAHQA GSGPSNGYGG QAPPPPVTVA PPTPAATPSI ARYAKPPALM MNSAGEMPIK PAPKMPPSMG HGHSHGLNPN VSGLDLSYSA LHKHWLWNPS LLYYTQAHIQ AQAAASGGQF LPYAGGYLPH AMAAAAASST SALGGFTKSE SSIDLSTPGA AGDALSDCDS GKSSPAALSL TASGGGNGAG SAPEASPGST LSHSRKRNPY SIEELLKKPE KRLRLDSNRL ECLESSSCES SQDSPVAPPL ETPEDEDPAE AEEEQEEEDS VEVVN // ID PP11_DROME STANDARD; PRT; 327 AA. AC P48461; Q9VC69; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase alpha-1 isoform (EC 3.1.3.16). GN PP1-ALPHA-96A OR PP1-96A OR CG6593. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91099353; PubMed=2176604; RA Dombradi V., Axton J.M., Brewis N.D., da Cruz e Silva E.F., RA Alphey L., Cohen P.T.W.; RT "Drosophila contains three genes that encode distinct isoforms of RT protein phosphatase 1."; RL Eur. J. Biochem. 194:739-745(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON ION AND 1 MANGANESE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-1 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56438; CAA39820.1; -. DR EMBL; AE003748; AAF56306.1; -. DR PIR; S13827; S13827. DR HSSP; P08129; 1FJM. DR FlyBase; FBgn0003134; Pp1-alpha-96A. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Metal-binding; Iron; Manganese; Multigene family. FT METAL 62 62 IRON (BY SIMILARITY). FT METAL 64 64 IRON (BY SIMILARITY). FT METAL 90 90 IRON AND MANGANESE (BY SIMILARITY). FT METAL 122 122 MANGANESE (BY SIMILARITY). FT ACT_SITE 123 123 GENERAL ACID (BY SIMILARITY). FT METAL 171 171 MANGANESE (BY SIMILARITY). FT METAL 246 246 MANGANESE (BY SIMILARITY). SQ SEQUENCE 327 AA; 37370 MW; 372390FBBB3CA8F0 CRC64; MSDIMNIDSI ISRLLEVRGA RPGKNVQLSE SEIRSLCLKS REIFLSQPIL LELEAPLKIC GDIHGQYYDL LRLFEYGGFP PESNYLFLGD YVDRGKQSLE TICLLLAYKI KYAENFFLLR GNHECASINR IYGFYDECKR RYTIKLWKTF TDCFNCLPVA AIVDEKIFCC HGGLSPDLSS MEQIRRIMRP TDVPDQGLLC DLLWSDPDKD TMGWGENDRG VSFTFGAEVV GKFLQKHEFD LICRAHQVVE DGYEFFAKRQ LVTLFSAPNY CGEFDNAGAM MSVDDTLMCS FQILKPADKR RFVYPNFGSS GRPLTPPRGA NNKNKKK // ID PP12_DROME STANDARD; PRT; 302 AA. AC P12982; Q9VG75; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase alpha-2 isoform (EC 3.1.3.16). GN PP1-87B OR CG5650. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=89377827; PubMed=2550221; RA Dombradi V., Axton J.M., Glover D.M., Cohen P.T.W.; RT "Cloning and chromosomal localization of Drosophila cDNA encoding the RT catalytic subunit of protein phosphatase 1 alpha. High conservation RT between mammalian and insect sequences."; RL Eur. J. Biochem. 183:603-610(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP CHARACTERIZATION. RX MEDLINE=91085574; PubMed=2175717; RA Dombradi V., Axton J.M., Barker H.M., Cohen P.T.W.; RT "Protein phosphatase 1 activity in Drosophila mutants with RT abnormalities in mitosis and chromosome condensation."; RL FEBS Lett. 275:39-43(1990). CC -!- FUNCTION: IS ESSENTIAL FOR THE REGULATION OF MITOTIC CHROMOSOMAL CC SEGREGATION AS WELL AS REGULATION OF CHROMATIN CONDENSATION DURING CC INTERPHASE. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON ION AND 1 MANGANESE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-1 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15583; CAA33609.1; -. DR EMBL; X55198; CAA38983.1; -. DR EMBL; AE003695; AAF54810.1; -. DR EMBL; AY061063; AAL28611.1; -. DR PIR; S12960; PAFF1A. DR HSSP; P08129; 1FJM. DR FlyBase; FBgn0004103; Pp1-87B. DR GO; GO:0000163; F:protein phosphatase type 1 activity; IMP. DR GO; GO:0008344; P:adult locomotory behavior; IMP. DR GO; GO:0030261; P:chromosome condensation; IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0007611; P:learning and/or memory; NAS. DR GO; GO:0040011; P:locomotion; NAS. DR GO; GO:0007067; P:mitosis; IMP. DR GO; GO:0007399; P:neurogenesis; IMP. DR GO; GO:0008355; P:olfactory learning; IMP. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IMP. DR GO; GO:0008542; P:visual learning; IMP. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Metal-binding; Iron; Manganese; Multigene family. FT METAL 62 62 IRON (BY SIMILARITY). FT METAL 64 64 IRON (BY SIMILARITY). FT METAL 90 90 IRON AND MANGANESE (BY SIMILARITY). FT METAL 122 122 MANGANESE (BY SIMILARITY). FT ACT_SITE 123 123 GENERAL ACID (BY SIMILARITY). FT METAL 171 171 MANGANESE (BY SIMILARITY). FT METAL 246 246 MANGANESE (BY SIMILARITY). SQ SEQUENCE 302 AA; 34542 MW; 68FE054996C9A062 CRC64; MGDVMNIDSI ISRLLEVRGA RPGKNVQLSE GEIRGLCLKS REIFLSQPIL LELEAPLKIC GDIHGQYYDL LRLFEYGGFP PESNYLFLGD YVDRGKQSLE TICLLLAYKI KYSENFFLLR GNHECASINR IYGFYDECKR RYSIKLWKTF TDCFNCLPVA AIVDEKIFCC HGGLSPDLTS MEQIRRIMRP TDVPDQGLLC DLLWSDPDKD TMGWGENDRG VSFTFGAEVV AKFLQKHEFD LICRAHQVVE DGYEFFAKRM LVTLFSAPNY CGEFDNAGAM MSVDDTLMCS FQILKPADKR KK // ID PP13_DROME STANDARD; PRT; 302 AA. AC Q05547; Q9VXW0; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase alpha-3 isoform (EC 3.1.3.16). GN PP1-13C OR CG9156. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93185622; PubMed=8383037; RA Dombradi V., Mann D.J., Saunders R.D., Cohen P.T.W.; RT "Cloning of the fourth functional gene for protein phosphatase 1 in RT Drosophila melanogaster from its chromosomal location."; RL Eur. J. Biochem. 212:177-183(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON ION AND 1 MANGANESE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-1 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69974; CAA49594.1; -. DR EMBL; AE003498; AAF48448.1; -. DR EMBL; AY060272; AAL25311.1; -. DR PIR; S29396; S29396. DR HSSP; P08129; 1FJM. DR FlyBase; FBgn0003132; Pp1-13C. DR GO; GO:0008598; F:protein phosphatase type 1, intrinsic catal...; IDA. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Metal-binding; Iron; Manganese; Multigene family. FT METAL 62 62 IRON (BY SIMILARITY). FT METAL 64 64 IRON (BY SIMILARITY). FT METAL 90 90 IRON AND MANGANESE (BY SIMILARITY). FT METAL 122 122 MANGANESE (BY SIMILARITY). FT ACT_SITE 123 123 GENERAL ACID (BY SIMILARITY). FT METAL 171 171 MANGANESE (BY SIMILARITY). FT METAL 246 246 MANGANESE (BY SIMILARITY). SQ SEQUENCE 302 AA; 34558 MW; B01ACC651F5DAE14 CRC64; MAEVLNLESI ISRLLEVRGA RPGKNVQLSE GEIRGLCLKS REILLAQPIL LELEAPLKIC GDIHGQYYDL LRLFEYGGYP PEANYLFLGD YVDRGKQSLE TICLLLAYKI KYSENFFLLR GNHECASINR IYGFYDECKR RYTIKLWKTF TDCFNCLPVV AIVDEKIFCC HGGLSPDLTS MEQIRRIMRP TDVPDQGLLC DLLWSDPDKD TIGWGENDRG VSFTFGAEVV VKFLQKHDLD LICRAHQVVE DGYEFFAKRQ LVTLFSAPNY CGEFDNAGAM MSVDNTLMCS FQILKPVEKR KK // ID PP1B_DROME STANDARD; PRT; 330 AA. AC P48462; Q9W2V5; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase beta isoform (EC 3.1.3.16) (Flap DE wing protein). GN FLW OR PP1-9C OR PP1-BETA-9C OR CG2096. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91099353; PubMed=2176604; RA Dombradi V., Axton J.M., Brewis N.D., da Cruz e Silva E.F., RA Alphey L., Cohen P.T.W.; RT "Drosophila contains three genes that encode distinct isoforms of RT protein phosphatase 1."; RL Eur. J. Biochem. 194:739-745(1990). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND MUTAGENESIS OF TYR-133 AND VAL-284. RX MEDLINE=20180517; PubMed=10712908; RA Raghavan S., Williams I., Aslam H., Thomas D., Szoor B., Morgan G., RA Gross S., Turner J., Fernandes J., VijayRaghavan K., Alphey L.; RT "Protein phosphatase 1beta is required for the maintenance of muscle RT attachments."; RL Curr. Biol. 10:269-272(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR CELL ADHESION IN NON-MUSCLE TISSUES AND IN CC MAINTENANCE OF MUSCLE ATTACHMENT. VITAL FOR LARVAL DEVELOPMENT. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON ION AND 1 MANGANESE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-1 SUBFAMILY. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56439; CAA39821.1; -. DR EMBL; AJ249214; CAB59732.1; -. DR EMBL; AJ249215; CAB59732.1; JOINED. DR EMBL; AE003450; AAF46583.1; ALT_SEQ. DR PIR; S13828; S13828. DR HSSP; P08129; 1FJM. DR FlyBase; FBgn0000711; flw. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Cell adhesion; Hydrolase; Metal-binding; Iron; Manganese; KW Multigene family. FT METAL 63 63 IRON (BY SIMILARITY). FT METAL 65 65 IRON (BY SIMILARITY). FT METAL 91 91 IRON AND MANGANESE (BY SIMILARITY). FT METAL 123 123 MANGANESE (BY SIMILARITY). FT ACT_SITE 124 124 GENERAL ACID (BY SIMILARITY). FT METAL 172 172 MANGANESE (BY SIMILARITY). FT METAL 247 247 MANGANESE (BY SIMILARITY). FT MUTAGEN 133 133 Y->F: SEMI LETHAL, ADULT ESCAPERS EXHIBIT FT MUSCLE AND WING MUTANT PHENOTYPE; ALLELE FT FLW-6. FT MUTAGEN 284 284 V->A: MUSCLE AND WING MUTANT PHENOTYPE; FT ALLELE FLW-1. SQ SEQUENCE 330 AA; 37740 MW; 9233DFC06EAE17AD CRC64; MGDFDLNVDS LIQRLLEMRS CRTGKQVQMT EAEVRGLCLK SREIFLQQPI LLELEAPLII CGDIHGQYTD LLRLFEYGGF PPAANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRYNVKLWKT FTDCFNCLPV AAIIDEKIFC CHGGLSPDLQ GMEQIRRLMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGVDV VSKFLNRHEL DLICRAHQVV EDGYEFFARR QLVTLFSAPN YCGEFDNAGG MMTVDDTLMC SFQILKPSEK KAKYLYSGMN SSRPTTPQRS APMLATNKKK // ID PPA1_DROME STANDARD; PRT; 155 AA. AC P82890; Q9VFR9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Low molecular weight phosphotyrosine protein phosphatase 1 DE (EC 3.1.3.48) (Low molecular weight cytosolic acid phosphatase 1) DE (EC 3.1.3.2) (PTPase 1). GN PRIMO-1 OR CG31311/CG9599. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B), TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Embryo, and Pupae; RX MEDLINE=20156363; PubMed=10675607; RA Miller D.T., Read R., Rusconi J., Cagan R.L.; RT "The Drosophila primo locus encodes two low-molecular-weight tyrosine RT phosphatases."; RL Gene 243:1-9(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: ACTS ON TYROSINE PHOSPHORYLATED PROTEINS, LOW-MW ARYL CC PHOSPHATES AND NATURAL AND SYNTHETIC ACYL PHOSPHATES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- CATALYTIC ACTIVITY: AN ORTHOPHOSPHORIC MONOESTER + H(2)O = AN CC ALCOHOL + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; Synonyms=D; CC IsoId=P82890-1; Sequence=Displayed; CC Name=E; CC IsoId=P82890-2; Sequence=VSP_007676, VSP_007677; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: CONE CELLS AND PRIMARY PIGMENT CELLS IN CC DEVELOPING PUPAL RETINA. CC -!- DEVELOPMENTAL STAGE: LARVAE, PUPAE AND ADULT. CC -!- SIMILARITY: BELONGS TO THE LOW MOLECULAR WEIGHT PHOSPHOTYROSINE CC PROTEIN PHOSPHATASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003701; AAN13591.2; -. DR EMBL; AE003701; AAO41565.1; -. DR HSSP; P11064; 1DG9. DR FlyBase; FBgn0040077; primo-1. DR InterPro; IPR000106; Low_mwt_PTPase. DR Pfam; PF01451; LMWPc; 1. DR PRINTS; PR00719; LMWPTPASE. DR SMART; SM00226; LMWPc; 1. KW Hydrolase; Alternative splicing. FT ACT_SITE 9 9 NUCLEOPHILE (BY SIMILARITY). FT ACT_SITE 15 15 BY SIMILARITY. FT ACT_SITE 124 124 PROTON DONOR (BY SIMILARITY). FT VARSPLIC 128 131 ERGA -> VRYF (in isoform E). FT /FTId=VSP_007676. FT VARSPLIC 132 155 Missing (in isoform E). FT /FTId=VSP_007677. SQ SEQUENCE 155 AA; 17556 MW; 26C05D1EC3B1A07C CRC64; MVRKVLMICL GNICRSPIAE VVMVDTLEKA NVKDVEVDSA AIGGWHVGNR ADPRAISTLQ KHGLKCTHIV RQIRKQDFSE FDYIFGMDED NMSELRRLAP KGSKAELLML GDFGLEKKNR IIEDPYYERG AEGFETAYQQ CVVACAAFMK ERLQK // ID PPA2_DROME STANDARD; PRT; 164 AA. AC P82891; Q9VFR9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Low molecular weight phosphotyrosine protein phosphatase 2 DE (EC 3.1.3.48) (Low molecular weight cytosolic acid phosphatase 2) DE (EC 3.1.3.2) (PTPase 2). GN PRIMO-2 OR CG31311/CG9599. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., MUTAGENESIS OF CYS-14, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC TISSUE=Embryo, and Pupae; RX MEDLINE=20156363; PubMed=10675607; RA Miller D.T., Read R., Rusconi J., Cagan R.L.; RT "The Drosophila primo locus encodes two low-molecular-weight tyrosine RT phosphatases."; RL Gene 243:1-9(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ACTS ON TYROSINE PHOSPHORYLATED PROTEINS, LOW-MW ARYL CC PHOSPHATES AND NATURAL AND SYNTHETIC ACYL PHOSPHATES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- CATALYTIC ACTIVITY: AN ORTHOPHOSPHORIC MONOESTER + H(2)O = AN CC ALCOHOL + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: CONE CELLS AND PRIMARY PIGMENT CELLS IN CC DEVELOPING PUPAL RETINA. CC -!- DEVELOPMENTAL STAGE: EMBRYO AND ADULT. CC -!- SIMILARITY: BELONGS TO THE LOW MOLECULAR WEIGHT PHOSPHOTYROSINE CC PROTEIN PHOSPHATASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003701; AAF54981.3; -. DR EMBL; AY089477; AAL90215.1; -. DR HSSP; P11064; 1DG9. DR FlyBase; FBgn0040076; primo-2. DR InterPro; IPR000106; Low_mwt_PTPase. DR Pfam; PF01451; LMWPc; 1. DR PRINTS; PR00719; LMWPTPASE. DR SMART; SM00226; LMWPc; 1. KW Hydrolase. FT ACT_SITE 14 14 NUCLEOPHILE (BY SIMILARITY). FT ACT_SITE 20 20 BY SIMILARITY. FT ACT_SITE 130 130 PROTON DONOR (BY SIMILARITY). FT MUTAGEN 14 14 C->S: COMPLETE LOSS OF ACTIVITY. FT CONFLICT 31 31 L -> V (IN REF. 1). FT CONFLICT 111 111 A -> V (IN REF. 1). SQ SEQUENCE 164 AA; 18541 MW; 320485DF557E4CCD CRC64; MGKRSQKSSV LMVCVGNLCR SPIAEAVMRD LVARAGLQGE WHVESAGIED WHSGHQPDER ALNVLARHNI EYNGKARVLA PEDFLEFDYI FAMDLSNLAA LRRMAPKGTT AKLLILGNFG LKPDERIIED PYYDIGEASF EEIYRQCSIA CRNFLKQARL KQIM // ID PPAN_DROME STANDARD; PRT; 460 AA. AC Q9VDE5; O97133; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Peter pan protein. GN PPAN OR CG5786. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RX MEDLINE=99287720; PubMed=10359593; RA Migeon J.C., Garfinkel M.S., Edgar B.A.; RT "Cloning and characterization of peter pan, a novel Drosophila gene RT required for larval growth."; RL Mol. Biol. Cell 10:1733-1744(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR INITIATION OF LARVAL GROWTH AND NORMAL CC MITOTIC GROWTH BUT IS NOT ABSOLUTELY REQUIRED FOR GENERAL CC BIOSYNTHESIS OR DNA REPLICATION. REQUIRED FOR PROGRESSION OF CC NORMAL OOGENESIS AND MATURATION OF SOME IMAGINAL TISSUES INTO CC ADULT STRUCTURES. CC -!- TISSUE SPECIFICITY: UBIQUITOUS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY, CC HIGHEST EXPRESSION LEVEL IS DURING EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 BRIX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF102805; AAD16459.1; -. DR EMBL; AE003733; AAF55851.1; -. DR FlyBase; FBgn0010770; ppan. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0007444; P:imaginal disc development; IMP. DR GO; GO:0002164; P:larval development; IMP. DR InterPro; IPR007109; Brix. DR Pfam; PF04427; Brix; 1. DR PROSITE; PS50833; BRIX; 1. KW Coiled coil; Developmental protein. FT DOMAIN 28 290 BRIX. FT DOMAIN 295 350 COILED COIL (POTENTIAL). FT CONFLICT 70 70 K -> Q (IN REF. 1). FT CONFLICT 74 74 S -> C (IN REF. 1). FT CONFLICT 438 438 R -> G (IN REF. 1). SQ SEQUENCE 460 AA; 53093 MW; BA35F43BBF291EF6 CRC64; MGGKKKVHPK TRTAAFKASE PSEIVEAPHS FVIHRGLACP YITDLTLDFR RIMEPFTASN LREKRMNRIK DFVSLSSFFH VSHMGIFNKA STQLSFKVVR LPRGPSLTFK VHQFTLARDV ISLSKKQMID NDHFKHAPLV IMNNFSGDGK HLKLMATTFQ NMFPSINLAT VNIGTIRRCV LFSYNPDTKL VEMRHYSVQV VPVGLKRAVQ KIVKGTVPNL GKCNEVVDFV TKDGYASESE AEDDEQSHVV LAQTLKSKGN LEDKKSSIKL HEIGPRLTMQ LIKIEEGLLT GEVLYHDHVV KTEDEKETLR KLVEKKRKQK EQRKKEQAEN RARNLKLKKD EKWAAKRAAE GRTDSDPEDD AEYYKEEVGE EPDEELFKME AKSSRKRPSL GGGMKYKNKR AKLDTKDKND KSERTDKYDR KDKFDRKDKK DKFDPKNRRA KFDPKNKRAK FDHRKSRKSK // ID PPCK_DROME STANDARD; PRT; 647 AA. AC P20007; Q9V8J0; DT 01-FEB-1991 (Rel. 17, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Phosphoenolpyruvate carboxykinase [GTP] (EC 4.1.1.32) DE (Phosphoenolpyruvate carboxylase) (PEPCK). GN PEPCK OR ZDF4 OR CG17725. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87316942; PubMed=3114718; RA Gundelfinger E.D., Hermans-Borgmeyer I., Grenningloh G., Zopf D.; RT "Nucleotide and deduced amino acid sequence of the RT phosphoenolpyruvate carboxykinase (GTP) from Drosophila RT melanogaster."; RL Nucleic Acids Res. 15:6745-6745(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: GTP + OXALOACETATE = GDP + PHOSPHOENOLPYRUVATE CC + CO(2). CC -!- PATHWAY: RATE-LIMITING GLUCONEOGENIC ENZYME WHOSE ACTIVITY IS CC AFFECTED BY A NUMBER OF HORMONES REGULATING THIS METABOLIC CC PROCESS. CC -!- SIMILARITY: BELONGS TO THE PHOSPHOENOLPYRUVATE CARBOXYKINASE [GTP] CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00402; CAA68463.1; -. DR EMBL; AE003799; AAF57676.1; -. DR PIR; A26809; QYFFGM. DR FlyBase; FBgn0003067; Pepck. DR InterPro; IPR008210; PEPCK_N. DR InterPro; IPR008209; PEP_carboxykin. DR Pfam; PF00821; PEPCK; 1. DR ProDom; PD004738; PEPCK_N; 1. DR PROSITE; PS00505; PEPCK_GTP; 1. KW Gluconeogenesis; Lyase; Decarboxylase; GTP-binding. FT NP_BIND 263 270 GTP (POTENTIAL). FT ACT_SITE 314 314 BY SIMILARITY. FT CONFLICT 302 302 E -> V (IN REF. 1). FT CONFLICT 408 408 Q -> R (IN REF. 1). SQ SEQUENCE 647 AA; 71129 MW; 0DB81B3D9E1B1FBB CRC64; MPELIEQSKI ISGNVCGLPQ LHKLRQDNCG LYSHIRGIPI SYGNVDLLTT GVRAFVEEGI ALCQPDQVHI CDGSEQENKV LIKSLLEAGT IVPLPKYDNC WLARTNPADV ARVESRTFIC TERREETIPT PVEGVKGTLG NWISPSDMDA AVQQRFPGCM KGRTMYVVPF SMGPVGSPLS KIGIELTDSA YVVASMRIMT RMGAAVLRQL AKKEEFVRAL HSVGAPANGQ VEQPSWPCDP ERTIILHKPA ENLIVSYGSG YGGNSLLGKK CFALRIGSTI AKQEGWLAEH MLILGITDPK GEKKYITAAF PSACGKTNLA MLNPSLANYK VECVGDDIAW MKFDSQGVLR AINPENGFFG VAPGTSMETN PIAMNTVFKN TIFTNVASTS DGGVFWEGME SSLAPNVQIT DWLGKPWTKD SGKPAAHPNS RFCTPAAQCP IIDEAWEDPA GVPISAMLFG GRRPAGVPLI YEARDWTHGV FIGAAMRSEA TAAAEHKGKV IMHDPFAMRP FFGYNFGDYV AHWLSMEKRG QVPKIFHVNW FRKSAEGKFM WPGYGENSRV LEWILRRVNG ESCYVDSAIG HIPAEGALNL DGMKDKVDVK EIFSLPKEFW SQEVKDIRTY FESQVGADLP ASIYQQLDEL SSRVDNL // ID PPIE_DROME STANDARD; PRT; 300 AA. AC Q9V3G3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Peptidyl-prolyl cis-trans isomerase E (EC 5.2.1.8) (PPIase E) DE (Rotamase E) (Cyclophilin E) (Cyclophilin 33). GN CYP33 OR CG4886. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Anderson M.S., Diaz M.O.; RT "Cyp33: a new family of cyclophilins."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PPIASES ACCELERATE THE FOLDING OF PROTEINS. IT CATALYZES CC THE CIS-TRANS ISOMERIZATION OF PROLINE IMIDIC PEPTIDE BONDS IN CC OLIGOPEPTIDES. COMBINES RNA-BINDING AND PPIASE ACTIVITIES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: PEPTIDYLPROLINE (OMEGA=180) = PEPTIDYLPROLINE CC (OMEGA=0). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 1 CYCLOPHILIN-LIKE PPIASE DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF182826; AAF01031.1; -. DR EMBL; AE003803; AAF57839.1; -. DR EMBL; AY061421; AAL28969.1; -. DR HSSP; P05092; 2CPL. DR FlyBase; FBgn0028382; cyp33. DR InterPro; IPR002130; CSA_PPIase. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00160; pro_isomerase; 1. DR Pfam; PF00076; rrm; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SMART; SM00360; RRM; 1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. DR PROSITE; PS00030; RRM_RNP_1; 1. DR PROSITE; PS50102; RRM; 1. KW Isomerase; Rotamase; RNA-binding; Nuclear protein. FT DOMAIN 6 84 RNA-BINDING (RRM). FT DOMAIN 142 298 PPIASE, CYCLOPHILIN-TYPE. FT DOMAIN 60 63 POLY-ALA. SQ SEQUENCE 300 AA; 33276 MW; CEAC7156EE8632D6 CRC64; MSNDKRTIYV GGLADEVTER LLNNAFIPFG DIADIQMPAD YESQRHRGFA FIEYEQSEDA AAAIDNMNDS ELCGRTIRVN LAKPVRVKED SFKPIWADDD WLQKHAGATL QPEGEPEAEK VETPSTGPAV IEKAEKRNPQ VFFDIRIGGN DAGRIVMLLR ADVVPKTAEN FRQLCTHEQG YGYKGCSFHR VIPEFMCQGG DFTNNNGTGG KSIYGKKFND ENFNLKHNSF GTLSMANSGA NTNGSQFFIC TTKTDWLDNK HVVFGHVISG AEVVRKMERC GSKSGTPSQK IVIYSCGELK // ID PPOL_DROME STANDARD; PRT; 994 AA. AC P35875; Q9W5Q5; Q9W5S1; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Poly [ADP-ribose] polymerase (EC 2.4.2.30) (PARP) (ADPRT) (NAD(+) ADP- DE ribosyltransferase) (Poly[ADP-ribose] synthetase). GN PARP OR CG40411/CG17696/CG17718. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93234521; PubMed=8475096; RA Uchida K., Hanai S., Ishikawa K.-I., Ozawa Y.-I., Uchida M., RA Sugimura T., Miwa M.; RT "Cloning of cDNA encoding Drosophila poly(ADP-ribose) polymerase: RT leucine zipper in the auto-modification domain."; RL Proc. Natl. Acad. Sci. U.S.A. 90:3481-3485(1993). RN [2] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RC STRAIN=Canton-S; RX MEDLINE=98234380; PubMed=9565614; RA Hanai S., Uchida M., Kobayashi S., Miwa M., Uchida K.; RT "Genomic organization of Drosophila poly(ADP-ribose) polymerase and RT distribution of its mRNA during development."; RL J. Biol. Chem. 273:11881-11886(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). CC -!- FUNCTION: POLY[ADP-RIBOSE] POLYMERASE MODIFIES VARIOUS NUCLEAR CC PROTEINS BY POLY(ADP-RIBOSYL)ATION. THE MODIFICATION IS DEPENDENT CC ON DNA AND IS INVOLVED IN THE REGULATION OF VARIOUS IMPORTANT CC CELLULAR PROCESSES SUCH AS DIFFERENTIATION, PROLIFERATION, AND CC TUMOR TRANSFORMATION AND ALSO IN THE REGULATION OF THE MOLECULAR CC EVENTS INVOLVED IN THE RECOVERY OF CELL FROM DNA DAMAGE. CC -!- CATALYTIC ACTIVITY: NAD(+) + {ADP-D-RIBOSYL}(N)-ACCEPTOR = CC NICOTINAMIDE + {ADP-D-RIBOSYL}(N+1)-ACCEPTOR. CC -!- COFACTOR: ZINC, CONTAINS TWO MOLES OF ZINC PER MOLE OF PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P35875-1; Sequence=Displayed; CC Name=Short; CC IsoId=P35875-2; Sequence=VSP_004536; CC -!- TISSUE SPECIFICITY: EXPRESSED IN ADULT FEMALE OOCYTES, ANAL PLATES CC OF STAGE 12 EMBRYOS AND IN CELLS AROUND THE CENTRAL NERVOUS SYSTEM CC IN LATER EMBRYOS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY IN CC EMBRYOS, PUPAE AND ADULTS. EXPRESSION IS HIGHEST IN EMBRYOS. CC -!- MISCELLANEOUS: THE ADP-D-RIBOSYL GROUP OF NAD(+) IS TRANSFERRED TO CC AN ACCEPTOR CARBOXYL GROUP ON A HISTONE OR THE ENZYME ITSELF, AND CC FURTHER ADP-RIBOSYL GROUPS ARE TRANSFERRED TO THE 2'-POSITION OF CC THE TERMINAL ADENOSINE MOIETY, BUILDING UP A POLYMER WITH AN CC AVERAGE CHAIN LENGTH OF 20-30 UNITS. CC -!- SIMILARITY: BELONGS TO THE PARP FAMILY. CC -!- SIMILARITY: CONTAINS 1 BRCT DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D13806; BAA02964.1; -. DR EMBL; AF051548; AAC24518.1; -. DR EMBL; AF051544; AAC24518.1; JOINED. DR EMBL; AF051545; AAC24518.1; JOINED. DR EMBL; AF051546; AAC24518.1; JOINED. DR EMBL; AF051547; AAC24518.1; JOINED. DR PIR; A47474; A47474. DR HSSP; P26446; 1A26. DR FlyBase; FBgn0010247; Parp. DR GO; GO:0007001; P:chromosome organization and biogenesis (sen...; IMP. DR GO; GO:0007000; P:nucleolus organization and biogenesis; IMP. DR GO; GO:0006471; P:protein amino acid ADP-ribosylation; IMP. DR InterPro; IPR001357; BRCT. DR InterPro; IPR008288; NAD_ADPRT. DR InterPro; IPR001290; PARP. DR InterPro; IPR004102; PARP_reg. DR InterPro; IPR008893; WGR. DR InterPro; IPR001510; Znf_PolyADPpol. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF00644; PARP; 1. DR Pfam; PF02877; PARP_reg; 1. DR Pfam; PF05406; WGR; 1. DR Pfam; PF00645; zf-PARP; 2. DR PIRSF; PIRSF000489; NAD_ADPRT; 1. DR ProDom; PD004675; Znf_PolyADPpol; 2. DR SMART; SM00292; BRCT; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00347; PARP_ZN_FINGER_1; 1. DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2. KW Transferase; Glycosyltransferase; NAD; DNA-binding; Nuclear protein; KW ADP-ribosylation; Zinc-finger; Zinc; Alternative splicing. FT DNA_BIND 1 367 FT DOMAIN 368 507 AUTOMODIFICATION DOMAIN. FT DOMAIN 380 454 BRCT. FT DOMAIN 508 994 NAD-BINDING. FT ZN_FING 19 54 PARP-TYPE. FT ZN_FING 123 161 PARP-TYPE. FT DOMAIN 208 210 NUCLEAR LOCALIZATION SIGNAL 1ST PART. FT DOMAIN 223 228 NUCLEAR LOCALIZATION SIGNAL 2ND PART. FT VARSPLIC 376 564 Missing (in isoform Short). FT /FTId=VSP_004536. SQ SEQUENCE 994 AA; 113791 MW; ACA85A270DD29E08 CRC64; MDIELPYLAE YARTGRATCK GCKSTISKDT LRIAVMVQSA FHDAKVPNWF HKTCFFKNQR PSSVGDIQNI GNLRFADQKE LTDLVENIQE VISAQLGKKR SKAFNLALKD FGIEYAKSSR STCRGCEQKI NKDLVRLRKT VYDTEVGMKY GGQPLWHHLE CFAQLRSELG WFASGEDMPG FQSLADDDQA KVKNAIPPIK SEELPDTKRA KMELSDTNEE GEKKQRLKDQ NDAYFRFRDD IKNKMKKKDI DILLKFNNQQ PVTGDTEKLF DQTADLLTFG AIESCSECNS CQFIVNKSGY ICNGNHSEWT KCNKLLKEPT RSACIVPKEL KALYNFLNTV KEIPSTRIFN NFPPNKSTFS RSLLKTNKNN DVLVRPTIPR ISPPLYNLKF SIIGLKNQHK ELRKRIENLG GKFEVKISEN TIAIISTELE IQKKSTRMKF AEELGIHIVP IEFLDFVEAD TEGAIKYINS TCICSWGTDP KSRIPKETTK SLNSNSIYTK SMPVSRTFKV KDGLAVDPDS GLEDIAHVYV DSNNKYSVVL GLTDIQRNKN SYYKVQLLKA DKKEKYWIFR SWGRIGTNIG NSKLEEFDTS ESAKRNFKEI YADKTGNEYE QRDNFVKRTG RMYPIEIQYD DDQKLVKHES HFFTSKLEIS VQNLIKLIFD IDSMNKTLME FHIDMDKMPL GKLSAHQIQS AYRVVKEIYN VLECGSNTAK LIDATNRFYT LIPHNFGVQL PTLIETHQQI EDLRQMLDSL AEIEVAYSII KSEDVSDACN PLDNHYAQIK TQLVALDKNS EEFSILSQYV KNTHASTHKS YDLKIVDVFK VSRQGEARRF KPFKKLHNRK LLWHGSRLTN FVGILSHGLR IAPPEAPPTG YMFGKGIYFA DMVSKSANYC CTSQQNSTGL MLLSEVALGD MMECTSAKYI NKLSNNKHSC FGRGRTMPDP TKSYIRSDGV EIPYGETITD EHLKSSLLYN EYIVYDVAQV NIQYLFRMEF KYSY // ID PPV_DROME STANDARD; PRT; 303 AA. AC Q27884; Q9W3Z8; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase PP-V (EC 3.1.3.16). GN PPV OR PPPV6A OR CG12217. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Oregon-R; TISSUE=Eye imaginal disk, and Head; RX MEDLINE=94038968; PubMed=8223492; RA Mann D.J., Dombradi V., Cohen P.T.W.; RT "Drosophila protein phosphatase V functionally complements a SIT4 RT mutant in Saccharomyces cerevisiae and its amino-terminal region can RT confer this complementation to a heterologous phosphatase catalytic RT domain."; RL EMBO J. 12:4833-4842(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY BE INVOLVED IN CONTROLLING CELLULARIZATION OR IN CC REGULATING TRANSCRIPTION OF THE GENES INVOLVED IN THIS PROCESS. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON ION AND 1 MANGANESE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT HIGHEST LEVELS IN 2-4 H CC EMBRYOS. CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-V SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75980; CAA53588.1; -. DR EMBL; AE003437; AAF46163.1; -. DR PIR; S39611; S39611. DR HSSP; P08129; 1FJM. DR FlyBase; FBgn0003139; PpV. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0000074; P:regulation of cell cycle; IGI. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Metal-binding; Iron; Manganese. FT METAL 51 51 IRON (BY SIMILARITY). FT METAL 53 53 IRON (BY SIMILARITY). FT METAL 79 79 IRON AND MANGANESE (BY SIMILARITY). FT METAL 111 111 MANGANESE (BY SIMILARITY). FT ACT_SITE 112 112 GENERAL ACID (BY SIMILARITY). FT METAL 161 161 MANGANESE (BY SIMILARITY). FT METAL 235 235 MANGANESE (BY SIMILARITY). SQ SEQUENCE 303 AA; 34759 MW; 5269F971416E55EC CRC64; MGDVDKWIED VKKCKYLPEN ELKKLCEMVC DILLEETNIL PVSTPVTVCG DIHGQFYDLE QLFRTGGQVP HTNYIFMGDF VDRGYYSLET FTRLLTLKAR YPSRITLLRG NHETRQITKV YGFFDECFSK YGNANGWKYC CKVFDLLTIA AIIDEEVLCV HGGLSPEIIT LDQIRTIDRN GEIPYKGAFC DLVWSDPEDM EYWGQSPRGA GWLFGHNVTK DFMAINNLNL ICRAHQLVNE GIKYMFDGKL VTVWSAPNYC YRCGNVAAIL SFETAEKRQT KIFLAVPDAE RVIPKQNTTP YFL // ID PPY_DROME STANDARD; PRT; 314 AA. AC P11612; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase PP-Y (EC 3.1.3.16). GN PPY-55A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=89232161; PubMed=2541022; RA Dombradi V., Axton J.M., Glover D.M., Cohen P.T.W.; RT "Molecular cloning and chromosomal localization of a novel Drosophila RT protein phosphatase."; RL FEBS Lett. 247:391-395(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90346193; PubMed=2166691; RA Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J.; RT "Protein serine/threonine phosphatases; an expanding family."; RL FEBS Lett. 268:355-359(1990). CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON ION AND 1 MANGANESE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. PP-Y SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y07510; CAA68808.1; -. DR PIR; S03963; PAFFY. DR HSSP; P08129; 1FJM. DR FlyBase; FBgn0003140; PpY-55A. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Metal-binding; Iron; Manganese. FT METAL 60 60 IRON (BY SIMILARITY). FT METAL 62 62 IRON (BY SIMILARITY). FT METAL 88 88 IRON AND MANGANESE (BY SIMILARITY). FT METAL 120 120 MANGANESE (BY SIMILARITY). FT ACT_SITE 121 121 GENERAL ACID (BY SIMILARITY). FT METAL 169 169 MANGANESE (BY SIMILARITY). FT METAL 244 244 MANGANESE (BY SIMILARITY). SQ SEQUENCE 314 AA; 36022 MW; DEAFC521A509F0D8 CRC64; MAVLTTHEID CIIKELTSLN GSECTLKEEL IERLIQQTRE VIKWQPMLLE LQAPVNICGD IHGQFTDLLR IFKACGFPPK ANYLFLGDYV DRGKQSLETI CLLFAYKVKY PLNFFLLRGN HECASINKIY GFYDEIKRRH TVRLWHNFTD CFNWLPVAAL VGERIFCCHG GLSPSLRNLQ QINHIQRPTD IPDEGIMCDL LWADLNHTTK GWGHNDRGVS FTFDKVIVRD FLKAFDLQLM VRAHEVVEDG YEFFANRQLV TVFSAPNYCG MMNNAGGVMS VSTDLICSFV IILPCHKYKM IATDANQMPT NEEE // ID PR2_DROME STANDARD; PRT; 1337 AA. AC Q9I7F7; Q24316; Q960Z6; Q9V6K0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase PR2 (EC 2.7.1.112). GN PR2 OR CG3969. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 13-917 FROM N.A. (ISOFORM LONG). RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94156202; PubMed=8112607; RA Ito M., Matsui T., Taniguchi T., Chihara K.; RT "Alternative splicing generates two distinct transcripts for the RT Drosophila melanogaster fibroblast growth factor receptor homolog."; RL Gene 139:215-218(1994). RN [5] RP SEQUENCE OF 266-321 FROM N.A. RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9I7F7-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q9I7F7-2; Sequence=VSP_005006; CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. CC -!- SIMILARITY: CONTAINS 1 CRIB DOMAIN. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS CC IN POSITIONS 752, 806, 816 AND 827. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003819; AAF58423.4; -. DR EMBL; AE003819; AAG22275.3; -. DR EMBL; AY051755; AAK93179.1; -. DR EMBL; D17551; BAA04489.1; ALT_FRAME. DR EMBL; AJ002909; CAA05744.1; -. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0013955; PR2. DR GO; GO:0004713; F:protein-tyrosine kinase activity; NAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; NAS. DR InterPro; IPR000095; PAKbox/Rhobndng. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00786; PBD; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00018; SH3; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00285; PBD; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50108; CRIB; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. KW Transferase; Kinase; Tyrosine-protein kinase; ATP-binding; KW Alternative splicing. FT DOMAIN 133 399 PROTEIN KINASE. FT NP_BIND 139 147 ATP (BY SIMILARITY). FT BINDING 164 164 ATP (BY SIMILARITY). FT ACT_SITE 260 260 BY SIMILARITY. FT DOMAIN 488 502 CRIB. FT VARSPLIC 1 82 Missing (in isoform Short). FT /FTId=VSP_005006. FT CONFLICT 450 450 F -> FSTPFWKGVLSTGKTGYF (IN REF. 4). FT CONFLICT 484 484 R -> A (IN REF. 4). FT CONFLICT 906 906 A -> P (IN REF. 4). FT CONFLICT 913 913 D -> V (IN REF. 4). SQ SEQUENCE 1337 AA; 147475 MW; 12650E9DF5A82724 CRC64; MEYPQIDLYE FLTESELQQY YNAVKNELKI TNAAQFKYAA DEDLRFIGLS RPEIRRLRKF YEKHFPHSYL SKIKRLLQAP GTMVKREEAP GGGSQVALDG SSASACSSLA AKNGASSPSK VPNNKHIIPA DSISVNKQLG TGEFGIVQQG VWSNGNERIQ VAIKCLCRER MQSNPMEFLK EAAIMHSIEH ENIVRLYGVV LATDSLMLVT ELAHLRSLLE CLKDSGLRVS FLTIPTLCEF ALQICNGMRY LEQKRLIHRD LAARNILVFS KDKVKISDFG LSRALGVGKD YYKTNFNVNL KLPIAWCAPE CINYLRFTNA SDVWAFGVCL WEMFSYGFQP WAALTGLQIL EAIDAPNYQR LEQPDCCPSE YYTLMMKCWQ DDAAKRPRFG EIYDQLPDMK PEQLKAVVNC TEPKKDHLLY RQGDIISVLD RNTGTPFWKG VLSTGKTGYF NPSNTVAFLE GLPSSTRDSF SRVSDHRISK RKLRTEMISK PQNDFKHTGH VGIDGATFGD IAFLGSSQNY NHVPKQIVTP YKPSEDIEQT PLLLPPTPTS PDSLQTASGY FPEGANSGGA MGTSMNPTFI PSAEHTPKLI ATNGQSSFDF ASGSTNPFFP NRGDDELEFG LHNYGADGKS VHSETGWRPT SRSIVDDPHE YHEISDDEIA ADKLDFGPSL LDEINSMFGS ISAATGSHPK SPGFDHVNNK NEITEMSAKL GQKSGDTNGN KHGHGLLPTL SKKKSSGTVK PISVKDEKIL NHAIEIANEI SARSMIDLVS DQTPVIHSPK RKFSFRFPHL SNNGSGDKSG GLGTSGSAHT PTHGNASPFP KKKNFTEELQ SIPDIQSLIG KEGLEAYNSL IERKALLDIG PSPAATLLRH LDTDEFDLQS LHQSQRPMTL PTRGATQRVR KAELAAGLSR HNDENSNSLE ACESPSYMTH GSYKFPEAQP TEQLPEPESP NPIPLPPREG KKQVKTSTKR HVRKYPLIIP ANGLQRTLSK LADFGDEAAK SPEISTSSQP QPGRAIEVVA AVRPSGMRRP SRPSEREYEN MPTVGKESAH TYQNLDKLTP ADAAGLTDTA SLQFESIMEA DTSKEGILQS PDVTDGFYNF SIQKEHYNKG KDAEFEATQI SGLYVNDDEL RNLDIESSRR TATPCSSCSA LESEHSQPDA LPSTESVSEV SRFSSVDNEL AGNALFKKVR ASVNMAMNRK SVAETSLTSN QPGGASAKPQ TEAEYFAATA ARLADSNSVS CEDLLEFSDK KPKGCERGVD SDEVRIMVKV LGKDSTPNRC LGALEFINWD VHKSIKLIKL QNLVSEANLS LEASFEALQQ HEWDLHTTAH KLNGLKL // ID PRI1_DROME STANDARD; PRT; 438 AA. AC Q24317; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA primase small subunit (EC 2.7.7.-) (DNA primase 50 kDa subunit) DE (DNA polymerase subunit A) (DPRI50). GN PRI50. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Cotterill S.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA PRIMASE IS THE POLYMERASE THAT SYNTHESIZES SMALL RNA CC PRIMERS FOR THE OKAZAKI FRAGMENTS MADE DURING DISCONTINUOUS DNA CC REPLICATION. CC -!- SUBUNIT: HETERODIMER OF A SMALL SUBUNIT AND A LARGE SUBUNIT. CC -!- MISCELLANEOUS: THE BOUND ZINC ION IS NOT A COFACTOR. IT IS BOUND CC TO A ZINC KNUCKLE MOTIF THAT MAY BE INVOLVED IN SEQUENCE CC RECOGNITION AND THE BINDING OF SSDNA (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC-TYPE PRIMASE SMALL SUBUNIT CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X79801; CAA56196.1; -. DR FlyBase; FBgn0011762; DNApol-alpha-50. DR InterPro; IPR002755; DNA_primase_S. DR Pfam; PF01896; DNA_primase_S; 1. DR TIGRFAMs; TIGR00335; primase_sml; 1. KW Transferase; DNA replication; DNA-directed RNA polymerase; Primosome; KW Zinc-finger. FT ACT_SITE 63 63 POTENTIAL. FT ACT_SITE 127 127 POTENTIAL. FT ACT_SITE 129 129 POTENTIAL. FT ZN_FING 139 149 KNUCKLE-TYPE (BY SIMILARITY). SQ SEQUENCE 438 AA; 50167 MW; 76E5F86B85647A9B CRC64; MPEQVTDQEN QAPQQQTTAV HAYNPEVLQD MLPVYYRRLF PHLPFYRWLS YGSSEDAIFS NREISFTLQD DIYIRYLCFD TQAELEKEIC SRNPIKIDIG PVMHSKPKNH RSIPGGLTPV QRELVFDIDM TDYDEVRTCC SGAGVCLKCW KFMVLAARVL DVALAEDFGF EHIIWIFSGR RGIHCWVCDY QARHLDGRGR YAEAEYLNII TYASFAGGNS PRCSMGDRPH HSIKRALKIV EPMFEEIVLE DQNLFGTPKG VTKLLNMVHD DAARGELESY MQKNLEDGAH SRLVWESFIK YANSMRTSTT SAWSRKLKNI VAEIQLGLLY PRLDINVTRG FNHLLKAPFC IHPATGKVCV PFSVSAVAKF DPTTVPTITQ LLHEINAFDD KSKSYMEAPE DKSRIKDHKK TSMFKGVVVF EEFLRKLERS EKSASLQF // ID PRI2_DROME STANDARD; PRT; 533 AA. AC Q9VPH2; Q9U9Q5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE DNA primase large subunit (EC 2.7.7.-). GN DNAPRIM OR S(FAF)240 OR BCDNA:GM13640 OR CG5553. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND MUTAGENESIS OF GLU-136. RX MEDLINE=20556146; PubMed=11102374; RA Chen X., Li Q., Fischer J.A.; RT "Genetic analysis of the Drosophila DNAprim gene. The function of the RT 60-kd primase subunit of DNA polymerase opposes the fat facets RT signaling pathway in the developing eye."; RL Genetics 156:1787-1795(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: DNA PRIMASE IS THE POLYMERASE THAT SYNTHESIZES SMALL RNA CC PRIMERS FOR THE OKAZAKI FRAGMENTS MADE DURING DISCONTINUOUS DNA CC REPLICATION. PLAYS A ROLE IN THE FAT FACETS (FAF)-DEPENDENT CELL- CC COMMUNICATIONS PATHWAY. CC -!- SUBUNIT: HETERODIMER OF A SMALL SUBUNIT AND A LARGE SUBUNIT. CC -!- MISCELLANEOUS: MUTANTS EXHIBIT EYE DEFECTS AND A DELAY IN THE S- CC PHASE OF THE CELL CYCLE. CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC-TYPE PRIMASE LARGE SUBUNIT CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF291873; AAG01548.1; -. DR EMBL; AE003591; AAF51580.2; -. DR EMBL; AF160895; AAD46835.1; -. DR FlyBase; FBgn0011425; DNAprim. DR InterPro; IPR007238; DNA_primase_lrg. DR Pfam; PF04104; DNA_primase_lrg; 1. KW Transferase; DNA replication; DNA-directed RNA polymerase; Primosome; KW DNA-binding. FT MUTAGEN 136 136 E->K: IN DNAPRIM-T2; PUPAL LETHAL. FT CONFLICT 142 142 Y -> F (IN REF. 3). FT CONFLICT 149 149 S -> G (IN REF. 3). SQ SEQUENCE 533 AA; 61435 MW; 92CE6049AA8685E5 CRC64; MEFGLKKRAR HEVKVEVASL ETKYPHNVML YHYPPTEDVH IDEFEELALE RLRLLRVLDR ASTRNLRVLS DEWKEIVSAD LTREGLRSYL RLCSTGGSAK HEADIQTRRR DYLSHFILRL AYCRSEDLAR WFVAREMELF RYKFAALSSF EVKQFLEANG FEIHPLTEAQ KDEVKDGLYE STVGQSVAKI ELLDFYKVPF TQVLDLVRGR RCFLKAGYAY VNTHDLVSLV GTKQQDEIEQ GLQAAKTMVE DVEADERISR TLKALHNSYT GRDYTVCRDA AVPIESLDQL SKTSMPLCMR MCHEHIRANH HIKHSGRMQY GLFLKGIGVA LEDSLRFWRE EFTKKMDADK FTRSYEYNIY HNYGKKGSMV NYTPYSCAKI IKDVAGPGDC HGCPYKNMDQ GSLKTKLSSY GLSASAIDEV MFFVSRGHYQ IGCGKYFQLT HNSPVEPSIN HPNNYFEESQ IAMGNRQKRA NGSAPPKARI RPDIKGHGDR SMLMGDDDDE LWRIAETQER IMQSQKDISE AFNDDLDLTQ IDY // ID PRML_DROME STANDARD; PRT; 1013 AA. AC P82295; Q95RK1; Q9VZV0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Prominin-like protein. GN CG7740. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RA Corbeil D., Roper K., Huttner W.B.; RT "Sequence analysis of a Drosophila ortholog of mouse prominin and RT human prominin(mouse)-like 1."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 482-1013 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PROMININ FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF127935; AAD22487.2; -. DR EMBL; AF197345; AAF07212.1; -. DR EMBL; AE003477; AAF47716.2; -. DR EMBL; AY061324; AAL28872.1; ALT_INIT. DR EMBL; BT003602; AAO39605.1; -. DR FlyBase; FBgn0026189; prominin-like. DR InterPro; IPR008795; Prominin. DR Pfam; PF05478; Prominin; 1. KW Transmembrane; Glycoprotein. FT TRANSMEM 32 52 POTENTIAL. FT TRANSMEM 215 235 POTENTIAL. FT TRANSMEM 489 509 POTENTIAL. FT TRANSMEM 535 555 POTENTIAL. FT TRANSMEM 852 872 POTENTIAL. FT CARBOHYD 99 99 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 116 116 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 576 576 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 618 618 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 803 803 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 824 824 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 949 949 N-LINKED (GLCNAC...) (POTENTIAL). FT DOMAIN 22 30 POLY-ARG. FT DOMAIN 956 962 POLY-GLY. SQ SEQUENCE 1013 AA; 115105 MW; 88B69163AF5FAFB3 CRC64; MGEVAATVEP LAAVKSKSMR SRKRRQRRRR QIAYLAICGL SVAIFGFALA TLIRPTTAQA DADPGSWRKG YVGHGTTHEQ LGQPHWPPVQ YTVYRPTTNY TKAPPPPTSA MNPIFNFTHF LYDKVLYRDE PIPEGYIVVK NSDTLSLGPK VEENDWRDLL AHYWMVLIWV VILVVLIIVI PFIAVCYCCF CCCRRCRQGC PPCTSKQDAQ RRFCCGICLL ILIIGLIFGI IIAFVTNKMI DSGFAETSET MKRGSEDTCT YLKDVADHVH HLMMYNYEEM ETHVLDQLTH AHRHIFLDLS DTSESNSLAE MERVLENMPE ALELMRQVEK MEKDLRFYGS QLRDGVRGIK RDVNFAVANL CQLQMCQKFL ISSNIEHIDS SQCLHFDNLP NTKEFVEGME NIVASEYYAI PQRGLSRLKK VSDKVKTQLS FVVPPMMRDL TKGRTIFREH ATNVRNIVEG VLSDIHIKTL HSTKSFEDVY ERFGHDRNVV SLIVCLLILL VLFILIFALL CGCFGRRRTG YGDECCSKST GATCLLLAIL LIFCVFSFIA LVGLFYFMLG MVTYQGACAP LRDQENNTLF RQLDASIDLN HYLPPSESNK EVVQPLKMSS AIKACHANQT IFDMMRQHNI YDINDLTRIK VMSHSQENTD SIKVFDEDLS TVVLLTKEER DELKTAGESK LAKYHSSLYM PSLCTQFTPM NLNALSEQLY KLSNDLEYPA YGWAKVSFWN EGLNTKAFYR NFVPKLTSLV EKMKANLKKI DELISYENHD FTNTIKILTA TAINSEQFIQ TRGKDYINAL GGNLTNSIDQ MIDDYIDMII KEANESVGHC APLSYIYYRG VDLICHRIVD PINGFWVGIL LCALLFLPIL FVAHRLMCLY KKIYPYLATV GAAGVVEGGS DYLYDAYSER DREHVPLANV PKKRRKAYER RREQQDYFED ASPSVSRGNR SGGDRGGGGG DGAPGSSSMR YNDMAPTHWD HEPPRYHNPP AAPPSSEYER PPPYYYPGAS EQD // ID PROD_DROME STANDARD; PRT; 669 AA. AC Q04499; O61349; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Proline oxidase, mitochondrial precursor (EC 1.5.3.-) (Proline DE dehydrogenase) (Protein sluggish-A). GN SLGA OR SLG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93219408; PubMed=8096642; RA Hayward D.C., Delaney S.J., Campbell H.D., Ghysen A., Benzer S., RA Kasprzak A.B., Cotsell J.N., Young I.G., Miklos G.L.G.; RT "The sluggish-A gene of Drosophila melanogaster is expressed in the RT nervous system and encodes proline oxidase, a mitochondrial enzyme RT involved in glutamate biosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 90:2979-2983(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98188272; PubMed=9520435; RA Maleszka R., de Couet H.G., Miklos G.L.G.; RT "Data transferability from model organisms to human beings: insights RT from the functional genomics of the flightless region of RT Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998). CC -!- FUNCTION: CONVERTS PROLINE TO DELTA-1-PYRROLINE-5-CARBOXYLATE. CC REDUCED PROLINE OXIDASE ACTIVITY PRODUCES SLUGGISH BEHAVIOR. CC -!- PATHWAY: CONVERSION FROM PROLINE TO GLUTAMATE; FIRST STEP. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- TISSUE SPECIFICITY: MOST ABUNDANT IN DEVELOPING NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN DEVELOPING EMBRYO AS WELL AS IN CC ADULT. CC -!- SIMILARITY: BELONGS TO THE PROLINE OXIDASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L07330; AAA02748.1; -. DR EMBL; AF017777; AAC28410.1; -. DR PIR; A47302; A47302. DR FlyBase; FBgn0003423; slgA. DR InterPro; IPR002872; Pro_dh. DR Pfam; PF01619; Pro_dh; 1. KW Oxidoreductase; Proline metabolism; Mitochondrion; Transit peptide. FT TRANSIT 1 30 MITOCHONDRION (POTENTIAL). FT CHAIN 31 669 PROLINE OXIDASE. FT CONFLICT 42 42 N -> S (IN REF. 2). FT CONFLICT 147 149 NLV -> KLF (IN REF. 2). SQ SEQUENCE 669 AA; 75965 MW; D9C37A99D4BEC705 CRC64; MALLRSLSAQ RTAISLVYGR NSSKSSNSVA VAACRSFHQR GNGSTSIAGE GAASESTRGV NGARFLHSGD RPLQASTLVQ PEVVSSETVK RSMKQESSQE KNPSPAGSPQ RDPLDVSFND PIAAFKSKTT GELIRAYLVY MICSSENLVE HNMTLMKWSK NVLGQRLFTL LMKATFYGHF VAGEDQIKII PTLERLRSFG VKPILDYSVE EDITQEEAEK REVESSVSSA GDKKEEGSMP QYHVDKSFAD RRYKVSSART YFYLNEATCE RNMEIFIKCL EAVSGATFGT GITAIKLTAL GRPQLLLQLS EVIMRTRKYM EDMVGGQGNV LTHHKTIKDL EKYYATLGDN KDVKEFLNNV TSDKEGILHL FPWSGIVDED SQLSDTFRVP DPQTGQMRRL ISQIPPKEEE MFRNMIRRLN TIVKAAADLD VRIMVDAEQT YFQPAISRIT LEMMRKYNKD KAIVFNTYQC YLRETFREVN TDLEQAKRQN FYFGAKLVRG AYMDQERDRA KSLGYPDPVN PTFEATTDMY HRTLSECLRR IKLMKDCDDD ARKIGIMVAS HNEDTVRFAI QQMKEIGISP EDKVICFGQL LGMCDYITFP LGQAGYSAYK YIPYGPVEEV LPYLSRRAQE NKGVLKKIKK EKRLLLSEIR RRLMRGQLFY KPKGNYVPI // ID PROF_DROME STANDARD; PRT; 126 AA. AC P25843; Q9VMJ9; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Profilin (Chickadee protein). GN CHIC OR CHI OR CG9553. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92208942; PubMed=1339308; RA Cooley L., Verheyen E., Caverly K.; RT "Chickadee encodes a profilin required for intercellular cytoplasm RT transport during Drosophila oogenesis."; RL Cell 69:173-184(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS TO ACTIN AND AFFECTS THE STRUCTURE OF THE CC CYTOSKELETON. AT HIGH CONCENTRATIONS, PROFILIN PREVENTS THE CC POLYMERIZATION OF ACTIN, WHEREAS IT ENHANCES IT AT LOW CC CONCENTRATIONS. BY BINDING TO PIP2, IT INHIBITS THE FORMATION OF CC IP3 AND DG. THIS PROFILIN IS REQUIRED FOR INTERCELLULAR CYTOPLASM CC TRANSPORT DURING DROSOPHILA OOGENESIS. CC -!- SUBUNIT: OCCURS IN MANY KINDS OF CELLS AS A COMPLEX WITH MONOMERIC CC ACTIN IN A 1:1 RATIO. CC -!- SIMILARITY: BELONGS TO THE PROFILIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84528; AAA28418.1; -. DR EMBL; M84529; AAA28419.1; -. DR EMBL; AE003612; AAF52315.1; -. DR PIR; A38154; A38154. DR HSSP; P07763; 1ACF. DR FlyBase; FBgn0000308; chic. DR GO; GO:0007300; P:nurse cell/oocyte transport (sensu Insecta); IMP. DR InterPro; IPR002097; Profilin. DR InterPro; IPR005455; Profilin_plant. DR Pfam; PF00235; profilin; 1. DR PRINTS; PR00392; PROFILIN. DR PRINTS; PR01640; PROFILINPLNT. DR SMART; SM00392; PROF; 1. DR PROSITE; PS00414; PROFILIN; 1. KW Actin-binding; Cytoskeleton. SQ SEQUENCE 126 AA; 13723 MW; 6E2942C12A81ADEA CRC64; MSWQDYVDNQ LLASQCVTKA CIAGHDGNIW AQSSGFEVTK EELSKLISGF DQQDGLTSNG VTLAGQRYIY LSGTDRVVRA KLGRSGVHCM KTTQAVIVSI YEDPVQPQQA ASVVEKLGDY LITCGY // ID PROS_DROME STANDARD; PRT; 1403 AA. AC P29617; Q95SP0; Q9U6A2; Q9VGP8; DT 01-APR-1993 (Rel. 25, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein prospero. GN PROS OR CG17228. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92069760; PubMed=1720353; RA Vaessin H., Grell E., Wolff E., Bier E., Jan L.Y., Jan Y.N.; RT "Prospero is expressed in neuronal precursors and encodes a nuclear RT protein that is involved in the control of axonal outgrowth in RT Drosophila."; RL Cell 67:941-953(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92171948; PubMed=1540176; RA Matsuzaki F., Koizumi K., Hama C., Yoshioka T., Nabeshima Y.; RT "Cloning of the Drosophila prospero gene and its expression in RT ganglion mother cells."; RL Biochem. Biophys. Res. Commun. 182:1326-1332(1992). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=93083413; PubMed=1842358; RA Chu-Lagraff Q., Wright D.M., McNeil L.K., Doe C.Q.; RT "The prospero gene encodes a divergent homeodomain protein that RT controls neuronal identity in Drosophila."; RL Development Suppl. 2:79-85(1991). RN [4] RP SEQUENCE FROM N.A. (ISOFORM C). RX MEDLINE=20503846; PubMed=11051550; RA Xu C., Kauffmann R.C., Zhang J., Kladny S., Carthew R.W.; RT "Overlapping activators and repressors delimit transcriptional RT response to receptor tyrosine kinase signals in the Drosophila eye."; RL Cell 103:87-97(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [7] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [8] RP SIMILARITY TO C.ELEGANS CEH-26. RX MEDLINE=94212446; PubMed=7909177; RA Buerglin T.R.; RT "A Caenorhabditis elegans prospero homologue defines a novel domain."; RL Trends Biochem. Sci. 19:70-71(1994). CC -!- FUNCTION: REQUIRED FOR PROPER NEURONAL DIFFERENTIATION OF MOST OR CC ALL NEURONS AND THEIR PRECURSORS IN CENTRAL AND PERIPHERAL NERVOUS CC SYSTEMS, AXONAL OUTGROWTH AND PATHFINDING. NOT REQUIRED FOR THE CC SPECIFICATION OF NEURONAL IDENTITY. MAY REGULATE TRANSCRIPTION BY CC BINDING TO DNA. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=C; Synonyms=L; CC IsoId=P29617-1; Sequence=Displayed; CC Name=A; CC IsoId=P29617-2; Sequence=VSP_002307, VSP_002308; CC Name=B; CC IsoId=P29617-3; Sequence=VSP_002307, VSP_002309; CC Name=S; Synonyms=D; CC IsoId=P29617-4; Sequence=VSP_002308; CC -!- TISSUE SPECIFICITY: NEURONAL PRECURSORS. EXPRESSED IN THE CC DEVELOPING CNS, LENS-SECRETING CONE CELLS OF THE EYE, AND MIDGUT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN NEURONAL PRECURSORS EARLY DURING CC FORMATION. CC -!- SIMILARITY: BELONGS TO THE PROSPERO HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- CAUTION: REF.7 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 1122. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81389; AAA28841.1; -. DR EMBL; D10609; BAA01464.1; -. DR EMBL; Z11743; CAA77802.1; -. DR EMBL; AF190403; AAF05703.1; -. DR EMBL; AE003691; AAF54628.2; -. DR EMBL; AE003691; AAN13500.2; -. DR EMBL; AE003691; AAN13501.2; -. DR EMBL; AY060680; AAL28228.1; ALT_FRAME. DR PIR; S24548; S24548. DR PDB; 1MIJ; 04-DEC-02. DR FlyBase; FBgn0004595; pros. DR GO; GO:0045179; C:apical cortex; IDA. DR GO; GO:0045180; C:basal cortex; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003700; F:transcription factor activity; NAS. DR GO; GO:0007409; P:axonogenesis; IMP. DR GO; GO:0007417; P:central nervous system development; IMP. DR GO; GO:0016358; P:dendrite morphogenesis; IMP. DR GO; GO:0007422; P:peripheral nervous system development; IMP. DR GO; GO:0045664; P:regulation of neuron differentiation; IMP. DR InterPro; IPR007738; Prox1. DR Pfam; PF05044; Prox1; 1. KW Nuclear protein; Transcription regulation; DNA-binding; Homeobox; KW Developmental protein; Alternative splicing; 3D-structure. FT DOMAIN 4 12 POLY-ALA. FT DOMAIN 28 31 POLY-SER. FT DOMAIN 32 35 POLY-ASN. FT DOMAIN 188 191 POLY-ALA. FT DOMAIN 216 264 GLN-RICH. FT DOMAIN 270 286 ASN-RICH. FT DOMAIN 318 354 SER-RICH. FT DOMAIN 431 437 POLY-ASP. FT DOMAIN 505 508 POLY-ALA. FT DOMAIN 700 1048 GLN-RICH. FT DOMAIN 934 937 POLY-ALA. FT DOMAIN 991 998 NUCLEAR LOCALIZATION SIGNAL. FT DOMAIN 1074 1082 POLY-PRO. FT DOMAIN 1127 1137 HIS-RICH. FT DNA_BIND 1241 1303 HOMEOBOX (ATYPICAL). FT DOMAIN 1304 1403 PROSPERO-LIKE. FT VARSPLIC 916 916 S -> SGNNGSLLLANSQMPSQTTASGSSAQQQQQQNAQQQ FT HQGSQQQQQQNVVQQQNVAQQQHMQQQQQQQQSHPLLPPNC FT QQLISAPRLNGSQLSFASPAAAAAAAMGLQMHHAAAAAAMS FT AQQQQQQSGDPGANTNPNSGPANPTNSSLSTLNIPPPHIRP FT SPT (in isoform A and isoform B). FT /FTId=VSP_002307. FT VARSPLIC 1216 1244 Missing (in isoform A and isoform S). FT /FTId=VSP_002308. FT VARSPLIC 1236 1403 Missing (in isoform B). FT /FTId=VSP_002309. FT CONFLICT 76 98 AKMLNELFGRQMKQAQDATSGLP -> GQDAERAVWPPDEA FT GPGRNEWPA (IN REF. 1 AND 4). FT CONFLICT 120 144 IGSLNSTSKLLQQQHNNNSIAPANS -> NLALQFHVQVAA FT AAAITTALLPPIG (IN REF. 1 AND 4). FT CONFLICT 418 418 H -> Q (IN REF. 2). FT CONFLICT 677 677 A -> C (IN REF. 1). FT CONFLICT 802 802 A -> S (IN REF. 1). FT CONFLICT 958 958 T -> S (IN REF. 1). FT CONFLICT 1048 1048 Q -> QQQQQ (IN REF. 1). SQ SEQUENCE 1403 AA; 153569 MW; 9EFB9973E24E238E CRC64; MSSAAAAAAG AAGGGALFQP QSVSTANSSS SNNNNSSTPA ALATHSPTSN SPVSGASSAS SLLTAAFGNL FGGSSAKMLN ELFGRQMKQA QDATSGLPQS LDNAMLAAAM ETATSAELLI GSLNSTSKLL QQQHNNNSIA PANSTPMSNG TNASISPGSA HSSSHSHQGV SPKGSRRVSA CSDRSLEAAA ADVAGGSPPR AASVSSLNGG ASSGEQHQSQ LQHDLVAHHM LRNILQGKKE LMQLDQELRT AMQQQQQQLQ EKEQLHSKLN NNNNNNIAAT ANNNNNTTME SINLIDDSEM ADIKIKSEPQ TAPQPQQSPH GSSHSSRSGS GSGSHSSMAS DGSLRRKSSD SLDSHGAQDD AQDEEDAAPT GQRSESRAPE EPQLPTKKES VDDMLDEVEL LGLHSRGSDM DSLASPSHSD MMLLDKDDVL DEDDDDDCVE QKTSGSGCLK KPGMDLKRAR VENIVSGMRC SPSSGLAQAG QLQVNGCKKR KLYQPQQHAM ERYVAAAAGL NFGLNLQSMM LDQEDSESNE LESPQIQQKR VEKNALKSQL RSMQEQLAEM QQKYVQLCSR MEQESECQEL DQDQDVEQEQ EPDNGSSDHI ELSPSPTLTG DGDVSPNHKE ETGQERPGSS SPSPSPLKPK TSLGESSDSG ANMLSQMMSK MMSGKLHNPL VGVGHPALPQ GFPPLLQHMG DMSHAAAMYQ QFFFEQEARM AKEAAEQQQQ QQQQQQQQQQ QQQQEQQRRF EQEQQEQQRR KEEQQQQIQR QQQHLQQLQQ QQMEQQHVAT AAPRPQMHHP APARLPTRMG GAAGHTALKS ELSEKFQMLR ANNNSSMMRM SGTDLEGLAD VLKSEITTSL SALVDTIVTR FVHQRRLFSK QADSVTAAAE QLNKDLLLAS QILDRKSPRT KVADRPQNGP TPATQSAAAM FQAPKTPQGM NPVAAAALYN SMTGPFCLPP DQQQQQQTAQ QQQSAQQQQQ SSQQTQQQLE QNEALSLVVT PKKKRHKVTD TRITPRTVSR ILAQDGVVPP TGGPPSTPQQ QQQQQQQQQQ QQQQQQQQAS NGGNSNATPA QSPTRSSGGA AYHPQPPPPP PPMMPVSLPT SVAIPNPSLH ESKVFSPYSP FFNPHAAAGQ ATAAQLHQHH QQHHPHHQSM QLSSSPPGSL GALMDSRDSP PLPHPPSMLH PALLAAAHHG GSPDYKTCLR AVMDAQDRQS ECNSADMQFD GMAPTISFYK QMQLKTEHQE SLMAKHCESL TPLHSSTLTP MHLRKAKLMF FWVRYPSSAV LKMYFPDIKF NKNNTAQLVK WFSNFREFYY IQMEKYARQA VTEGIKTPDD LLIAGDSELY RVLNLHYNRN NHIEVPQNFR FVVESTLREF FRAIQGGKDT EQSWKKSIYK IISRMDDPVP EYFKSPNFLE QLE // ID PRS4_DROME STANDARD; PRT; 439 AA. AC P48601; Q9VCG1; DT 01-FEB-1996 (Rel. 33, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 26S protease regulatory subunit 4 (P26s4). GN PROS26.4 OR P26S4 OR CG5289. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96404010; PubMed=8808288; RA Hoyle J., Fisher E.M.C.; RT "Genomic organization and mapping of the mouse P26s4 ATPase gene: a RT member of the remarkably conserved AAA gene family."; RL Genomics 31:115-118(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE 26S PROTEASE IS INVOLVED IN THE ATP-DEPENDENT CC DEGRADATION OF UBIQUITINATED PROTEINS. THE REGULATORY (OR ATPASE) CC COMPLEX CONFERS ATP DEPENDENCY AND SUBSTRATE SPECIFICITY TO THE CC 26S COMPLEX (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE AAA ATPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U39303; AAB34134.1; -. DR EMBL; AE003745; AAF56205.1; -. DR EMBL; AY058759; AAL13988.1; -. DR FlyBase; FBgn0015282; Pros26.4. DR GO; GO:0005838; C:proteasome regulatory particle (sensu Eukarya); IDA. DR GO; GO:0004299; F:proteasome endopeptidase activity; IDA. DR GO; GO:0006508; P:proteolysis and peptidolysis; IDA. DR InterPro; IPR005937; 26S_p45. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR Pfam; PF00004; AAA; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01242; 26Sp45; 1. DR PROSITE; PS00674; AAA; 1. KW Proteasome; ATP-binding; Nuclear protein. FT NP_BIND 225 232 ATP (POTENTIAL). FT CONFLICT 57 57 C -> A (IN REF. 1). FT CONFLICT 172 172 V -> M (IN REF. 1). SQ SEQUENCE 439 AA; 49323 MW; A7E210A292FDC96C CRC64; MGQNQSAQGG AGEKKDDKDK KKKYEPPIPT RVGKKKRRAK GPDAAMKLPQ VTPHTRCRLK LLKLERIKDY LMMEDEFIRN QERLKPQDEK NEEERSKVDD LRGTPMSVGN LEEIIDDNHA IVSTSVGSEH YVSILSFVDK DQLEPGCSVL LNHKVHAVVG VLSDDTDPMV TVMKLEKAPQ ETYADIGGLD TQIQEIKESV ELPLTHPEYY EEMGIKPPKG VILYGPPGTG KTLLAKAVAN QTSATFLRVV GSELIQKYLG DGPKLVRELF RVAEEHAPSI VFIDEIDAVG TKRYDSNSGG EREIQRTMLE LLNQLDGFDS RGDVKVIMAT NRIETLDPAL IRPGRIDRKI EFPLPDEKTK RRIFTIHTSR MTLAEDVNLS ELIMAKDDLS GADIKAICTE AGLMALRERR MKVTNEDFKK SKESVLYRKK EGTPEGLYL // ID PRS8_DROME STANDARD; PRT; 405 AA. AC O18413; O45023; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 26S protease regulatory subunit 8. GN PROS45 OR UG OR DUG OR CG1489. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=98137788; PubMed=9469929; RA Mounkes L.C., Fuller M.T.; RT "The DUG gene of Drosophila melanogaster encodes a structural and RT functional homolog of the S. cerevisiae SUG1 predicted ATPase RT associated with the 26S proteasome."; RL Gene 206:165-174(1998). RN [2] RP SEQUENCE FROM N.A. RA Cheng L., Roemer N., Smyth K.-A., Belote J., Nambu J., Schwartz L.M.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE 26S PROTEASE IS INVOLVED IN THE ATP-DEPENDENT CC DEGRADATION OF UBIQUITINATED PROTEINS. THE REGULATORY (OR ATPASE) CC COMPLEX CONFERS ATP DEPENDENCY AND SUBSTRATE SPECIFICITY TO THE CC 26S COMPLEX (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE AAA ATPASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U97538; AAC48284.1; -. DR EMBL; AF043734; AAC63219.1; -. DR EMBL; AE003568; AAF50835.1; -. DR EMBL; AY051732; AAK93156.1; -. DR FlyBase; FBgn0020369; Pros45. DR GO; GO:0005838; C:proteasome regulatory particle (sensu Eukarya); IDA. DR GO; GO:0004299; F:proteasome endopeptidase activity; IDA. DR GO; GO:0006508; P:proteolysis and peptidolysis; IDA. DR InterPro; IPR005937; 26S_p45. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR Pfam; PF00004; AAA; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01242; 26Sp45; 1. DR PROSITE; PS00674; AAA; 1. KW Proteasome; ATP-binding; Nuclear protein. FT NP_BIND 189 196 ATP (POTENTIAL). FT CONFLICT 94 94 F -> S (IN REF. 1). SQ SEQUENCE 405 AA; 45857 MW; C098EEE56B348211 CRC64; MTVTNRMEIE SAYHKGEGFR SYYIQKIEEL QLVVAEKHQN LRRLQAQRNE LNAKVRMLRE ELQLLQEQGS YVGEVVKPMD KKKVLVKVHP EGKFVVDLDK NIDINDVTPN CRVALRNESY TLHKILPNKV DPLVSLMMVE KVPDSTYEMV GGLDKQIKEI KEVIELPVKH PELFDALGIA QPKGVLLYGP PGTGKTLLAR AVAHHTECTF IRVSGSELVQ KFIGEGSRMV RELFVMAREH APSIIFMDEI DSIGSSRIES GSGGDSEVQR TMLELLNQLD GFEATKNIKV IMATNRIDIL DPALLRPGRI DRKIEFPPPN EEARLDILKI HSRKMNLTRG INLRKIAELM PGASGAEVKG VCTEAGMYAL RERRVHVTQE DFEMAVAKVM QKDSEKNMSI KKLWK // ID PS4L_DROME STANDARD; PRT; 251 AA. AC Q9VA12; Q8IS89; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 4-like (EC 3.4.25.1). GN PROS-ALPHA-3T OR CG1736. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX MEDLINE=22309036; PubMed=12421421; RA Ma J., Katz E., Belote J.M.; RT "Expression of proteasome subunit isoforms during spermatogenesis in RT Drosophila melanogaster."; RL Insect Mol. Biol. 11:627-639(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: TESTIS, PROMINENT AFTER MEIOSIS II. AFTER CC MEIOSIS, PREDOMINANTLY LOCALIZED TO THE HAPLOID SPERMATID NUCLEI CC OF THE 64-CELL CYSTS, REMAINING DURING THE ELONGATION AND CC CONDENSATION OF THE SPERMATID NUCLEI. IN MATURE, MOTILE SPERM, CC EXPRESSION IS SEEN EXCLUSIVELY IN THE SPERM HEAD. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003776; AAF57116.1; -. DR EMBL; AY147240; AAN63094.1; -. DR HSSP; P23638; 1RYP. DR MEROPS; T01.973; -. DR FlyBase; FBgn0039819; Pros-alpha-3T. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Hydrolase; Protease; Nuclear protein; Proteasome; Threonine protease. FT CONFLICT 74 75 CA -> WP (IN REF. 1). FT CONFLICT 133 133 F -> L (IN REF. 1). FT CONFLICT 141 142 RF -> AS (IN REF. 1). SQ SEQUENCE 251 AA; 28169 MW; B1AFF83978DB14D3 CRC64; MARFFDSRTT IFSPEGRLYQ VEYAMEAASQ SGTCVGLLAK NGVLLATERS VDKLMDTSIP VPRISWLNEN IACCATGNTA DGNVLVNQLR MIAQQYQFNF GEMIPCEQLV TNLCDIKQAY TQYGGKRPFG VSFLYMGWDC RFGFQLYQSD PSGNYSGWKA TCIGRKSGAA MEMLQKELFS KGYVSPSVEE AKDVAIKVMG MTLGRDSLTP EKLEIAFVQR YGNTTVFHIL EKNEIHRLIE RNNNLKRRVG S // ID PS71_DROME STANDARD; PRT; 249 AA. AC P22769; Q9VXI9; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 7-1 (EC 3.4.25.1) (Proteasome 28 kDa DE subunit 1) (PROS-Dm28.1). GN PROS28.1 OR PROS-28.1 OR CG3422. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90382671; PubMed=2169443; RA Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., Kloetzel P.-M.; RT "The Drosophila PROS-28.1 gene is a member of the proteasome gene RT family."; RL Gene 90:235-241(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92249308; PubMed=1374331; RA Frentzel S., Troxell M., Haass C., Pesold-Hurt B., Glaetzer K.H., RA Kloetzel P.-M.; RT "Molecular characterization of the genomic regions of the Drosophila RT alpha-type subunit proteasome genes PROS-Dm28.1 and PROS-Dm35."; RL Eur. J. Biochem. 205:1043-1051(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M57712; AAA62768.1; -. DR EMBL; X62286; CAA44174.1; ALT_SEQ. DR EMBL; AE003501; AAF48573.1; -. DR PIR; JQ0681; JQ0681. DR PIR; S23451; S23451. DR HSSP; P40303; 1RYP. DR MEROPS; T01.974; -. DR FlyBase; FBgn0004066; Pros28.1. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. FT CONFLICT 224 224 T -> N (IN REF. 1 AND 2). SQ SEQUENCE 249 AA; 27973 MW; 56987932DADD02B3 CRC64; MSSRYDRAVT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKK SVAQLQEDRK VRKICMLDNH VVMAFAGLTA DARIMINRAQ VECQSHRLNV EDPVTLEYIT RFIAQLKQKY TQSNGRRPFG ISCLIGGFDA DGSAHLFQTE PSGIFYEYKA NATGRSAKVV REFFEKSYRE EEVANEHGAV KLAIRALLEV AQSGQNNLEV AIMENGKPLK MLDTDVITDY VKIIEKEKEE ELEKKKQKK // ID PS72_DROME STANDARD; PRT; 249 AA. AC Q24178; Q9VDJ1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 7-1A (EC 3.4.25.1) (Testis-specific DE proteasome 28 kDa subunit 1A). GN PROS28.1A OR CG17268. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97032933; PubMed=8878681; RA Yuan X., Miller M., Belote J.M.; RT "Duplicated proteasome subunit genes in Drosophila melanogaster RT encoding testes-specific isoforms."; RL Genetics 144:147-157(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: TESTIS SPECIFIC. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U46008; AAC47280.1; -. DR EMBL; AE003731; AAF55802.1; -. DR PIR; S72225; S72225. DR HSSP; P40303; 1RYP. DR MEROPS; T01.974; -. DR FlyBase; FBgn0017557; Pros28.1A. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. FT CONFLICT 24 24 A -> G (IN REF. 1). FT CONFLICT 123 123 C -> V (IN REF. 1). FT CONFLICT 127 128 RP -> PS (IN REF. 1). SQ SEQUENCE 249 AA; 27940 MW; 18B642DE3F1AE453 CRC64; MSSRYGRALT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKS SVSEMQEDRT VRKISMLDRH VALAFAGLTA DARILINRGQ VECQSHRLNF ENQVTLEYIT RYLAQLKQKY TQCNGRRPFG ISCLIGGIDA DGSARLFHTE PSGIFHEYKA TATGRWANTV REFFEKAYSD HEVTTKCDAI KLAMRALLEV TQMSQMRLEV AVLENGKPMK MLDSVVISEI VKIVQNEKEL QAKAHKMKR // ID PS73_DROME STANDARD; PRT; 252 AA. AC Q27575; Q9W162; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 7-1B (EC 3.4.25.1) (Testis-specific DE proteasome 28 kDa subunit 1B). GN PROS28.1B OR CG4569. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=97032933; PubMed=8878681; RA Yuan X., Miller M., Belote J.M.; RT "Duplicated proteasome subunit genes in Drosophila melanogaster RT encoding testes-specific isoforms."; RL Genetics 144:147-157(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: TESTIS SPECIFIC. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U46009; AAC47281.1; -. DR EMBL; AE003464; AAF47215.1; -. DR PIR; S72226; S72226. DR HSSP; P40303; 1RYP. DR MEROPS; T01.974; -. DR FlyBase; FBgn0017556; Pros28.1B. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. FT CONFLICT 3 4 QR -> HG (IN REF. 1). FT CONFLICT 188 190 AAA -> RG (IN REF. 1). FT CONFLICT 243 249 AEASRRP -> PSESA (IN REF. 1). SQ SEQUENCE 252 AA; 28719 MW; 00116788A4813146 CRC64; MAQRYDRAVT IYSPDGHLLQ VEYAQEAVRR GSTVMGLRTN NAIVIGVEKR SVGDLQEERM VRKICMLDDH VVMTFSGLTA DARILVSRAQ MEAQSHRLNF EKPTTVEYIT RYIAQLKQNY TQSNGRRPFG LSCLVGGFDE DGTPHLFQTD PSGIFYEWRA NTTGRSSQPV RDYMEKHADE ILTIADEAAA IKHIVRTLVS VSSLNHTQME VAVLKYRQPL RMIDHQVLAD LERTVRREIE DEAEASRRPR AP // ID PSA1_DROME STANDARD; PRT; 279 AA. AC P12881; Q9VL23; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 1 (EC 3.4.25.1) (Proteasome 35 kDa DE subunit) (PROS-Dm35). GN PROS35 OR PROS-35 OR CG4904. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 4-18 AND 194-206. RC STRAIN=Oregon-R; RX MEDLINE=90005444; PubMed=2477245; RA Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., RA Kloetzel P.-M.; RT "The PROS-35 gene encodes the 35 kd protein subunit of Drosophila RT melanogaster proteasome."; RL EMBO J. 8:2373-2379(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92249308; PubMed=1374331; RA Frentzel S., Troxell M., Haass C., Pesold-Hurt B., Glaetzer K.H., RA Kloetzel P.-M.; RT "Molecular characterization of the genomic regions of the Drosophila RT alpha-type subunit proteasome genes PROS-Dm28.1 and PROS-Dm35."; RL Eur. J. Biochem. 205:1043-1051(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15497; CAA33520.1; -. DR EMBL; X62285; CAA44173.1; -. DR EMBL; AE003627; AAF52875.1; -. DR PIR; S23450; SNFF5K. DR HSSP; P40302; 1RYP. DR MEROPS; T01.976; -. DR FlyBase; FBgn0003151; Pros35. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Phosphorylation; Threonine protease. FT MOD_RES 103 103 PHOSPHORYLATION (POTENTIAL). SQ SEQUENCE 279 AA; 31058 MW; 1478BDC2C61EF3F1 CRC64; MFRNQYDSDV TVWSPQGRLH QVEYAMEAVK LGTATVGLKN KDYAVLVALC KPTSELSDTQ RKIIPIDDHL GISIAGLTAD ARVLSRYLRS ECLNYKHSYD TTYPVSRLIT NLGNKMQTTT QRYDRRPYGV GLLVAGYDER GPHIYQVTPS ATFFNCKANS IGSRSQSART YLEKNLNKFL DSSKDEIIRH GIRAILGTLP TDEQGKDAGQ YDITVAIVGK DQPFTILSNK DSAKHVAIAK ENDNDTPRND DDDDRPSPPE EPAAGPRDPE VLVATEQRP // ID PSA2_DROME STANDARD; PRT; 234 AA. AC P40301; Q9VG71; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Proteasome subunit alpha type 2 (EC 3.4.25.1) (Proteasome 25 kDa DE subunit) (PROS-Dm25). GN PROS25 OR PROS-25 OR CG5266. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93363644; PubMed=8357840; RA Seelig A., Troxell M., Kloetzel P.-M.; RT "Sequence and genomic organization of the Drosophila proteasome PROS- RT Dm25 gene."; RL Biochim. Biophys. Acta 1174:215-217(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X70304; CAA49783.1; -. DR EMBL; AE003696; AAF54814.1; -. DR EMBL; AY069280; AAL39425.1; -. DR PIR; S36116; S36116. DR HSSP; P23639; 1RYP. DR MEROPS; T01.972; -. DR FlyBase; FBgn0010405; Pros25. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Threonine protease; Nuclear protein. SQ SEQUENCE 234 AA; 25906 MW; BC6F98060BD9D7C2 CRC64; MATERYSFSL TTFSPSGKLV QLEYALAAVS GGAPSVGIIA SNGVVIATEN KHKSPLYEQH SVHRVEMIYN HIGMVYSGMG PDYRLLVKQA RKIAQTYYLT YKEPIPVSQL VQRVATLMQE YTQSGGVRPF GVSLLICGWD NDRPYLYQSD PSGAYFAWKA TAMGKNAVNG KTFLEKRYSE DLELDDAVHT AILTLKEGFE GKMTADNIEI GICDQNGFQR LDPASIKDYL ASIP // ID PSA3_DROME STANDARD; PRT; 253 AA. AC Q9V5C6; O17313; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 3 (EC 3.4.25.1) (20S proteasome subunit DE alpha-7). GN PROS-ALPHA-7 OR CG1519. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Belote J.M., Smyth K.A., Katz E., Miller M.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF025793; AAB82572.1; -. DR EMBL; AE003832; AAF58889.1; -. DR HSSP; P21242; 1RYP. DR MEROPS; T01.977; -. DR FlyBase; FBgn0023175; Pros-alpha-7. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. FT CONFLICT 17 17 P -> A (IN REF. 1). FT CONFLICT 30 30 MISSING (IN REF. 1). FT CONFLICT 62 62 D -> H (IN REF. 1). FT CONFLICT 167 167 MISSING (IN REF. 1). FT CONFLICT 182 182 M -> T (IN REF. 1). FT CONFLICT 235 253 ARKAGDAANKDEDSDNETH -> DEDTACGQQDEGRRQRQ FT (IN REF. 1). SQ SEQUENCE 253 AA; 27675 MW; 7B19D8DA350E2B7E CRC64; MSTIGTGYDL SASQFSPDGR VFQIDYASKA VEKSGTVIGI RGKDAVVLAV EKIITSKLYE PDAGGRIFTI EKNIGMAVAG LVADGNFVAD IARQEAANYR QQFEQAIPLK HLCHRVAGYV HAYTLYSAVR PFGLSIILAS WDEVEGPQLY KIEPSGSSFG YFACASGKAK QLAKTEMEKL KMDMRTDELV ESAGEIIYKV HDELKDKDFR FEMGLVGRVT GGLHLINPSE LTEKARKAGD AANKDEDSDN ETH // ID PSA4_DROME STANDARD; PRT; 264 AA. AC P18053; Q9W2N9; DT 01-NOV-1990 (Rel. 16, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 4 (EC 3.4.25.1) (Proteasome 29 kDa DE subunit) (PROS-Dm29). GN PROS29 OR PROS-29 OR CG9327. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90326554; PubMed=2374736; RA Haass C., Pesold-Hurt B., Kloetzel P.-M.; RT "The Drosophila PROS-29 gene is a new member of the PROS-gene RT family."; RL Nucleic Acids Res. 18:4018-4018(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52319; CAA36555.1; -. DR EMBL; AE003452; AAF46651.1; -. DR PIR; S10318; S10318. DR HSSP; P23638; 1RYP. DR MEROPS; T01.973; -. DR FlyBase; FBgn0003150; Pros29. DR InterPro; IPR001353; Peptidase_T1. DR InterPro; IPR000426; Pept_T1_subA. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. FT CONFLICT 68 68 L -> R (IN REF. 1). SQ SEQUENCE 264 AA; 29411 MW; E5209BC634008B8B CRC64; MARRYDSRTT IFSPEGRLYQ VEYAMEAISH AGTCLGILAE DGILLAAECR STNKLLDSAI PSEKIYRLND NMVCSVAGIT SDANVLTSEL RLIAQRYQFS YGEVIPCEQL VSHLCDIKQA YTQYGGKRPF GVSLLYMGWD NKYGYQLYQS DPSGNYGGWK ATCIGNNFGA AISMLKQELA DKENVKLTLA DAKDLAIKVL SMTLDTTKLT PEKVEMATLQ RVDNKTVYSV LEKPDVEKLI EKYTKVQAEA EAAKKEKQAK QPTK // ID PSA5_DROME STANDARD; PRT; 244 AA. AC Q95083; Q9V809; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 5 (EC 3.4.25.1). GN PROSMA5 OR CG10938. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98072434; PubMed=9409776; RA Zaiss D., Belote J.M.; RT "Molecular cloning of the Drosophila melanogaster gene alpha5_dm RT encoding a 20S proteasome alpha-type subunit."; RL Gene 201:99-105(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U64721; AAB93421.1; -. DR EMBL; AE003803; AAM70874.1; -. DR EMBL; AY061404; AAL28952.1; -. DR HSSP; P32379; 1RYP. DR MEROPS; T01.975; -. DR FlyBase; FBgn0016697; ProsMA5. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. FT CONFLICT 166 166 R -> G (IN REF. 1). SQ SEQUENCE 244 AA; 26883 MW; C58F3232A17FB711 CRC64; MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI CTPEGVVLAV EKRITSPLMV PSTVEKIVEV DKHIGCATSG LMADARTLIE RARVECQNHW FVYNERMSIE SCAQAVSTLA IQFGDSGDSD GAAAMSRPFG VAILFAGIEA GQPQLWHMDP SGTFVRHGAK AIGSGSEGAQ QNLQDLFRPD LTLDEAIDIS LNTLKQVMEE KLNSTNVEVM TMTKEREFYM FTKEEVEQHI KNIA // ID PSA6_DROME STANDARD; PRT; 244 AA. AC Q9XZJ4; Q9V324; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit alpha type 6 (EC 3.4.25.1) (20S proteasome subunit DE alpha-1). GN PROSALPHA6 OR CG18495. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Belote J.; RT "Drosophila melanogaster 20S proteasome subunit alpha1 cDNA."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF144749; AAD33944.1; -. DR EMBL; AE003839; AAF59184.1; -. DR HSSP; P21243; 1RYP. DR MEROPS; T01.971; -. DR FlyBase; FBgn0026781; Pros-alpha-6. DR InterPro; IPR000426; Pept_T1_subA. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. FT CONFLICT 94 94 A -> G (IN REF. 1). FT CONFLICT 122 122 N -> T (IN REF. 1). SQ SEQUENCE 244 AA; 27162 MW; D217B272CA339D05 CRC64; MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AIAQENITTV ALKSGDCAVV ATQKKVTEKN IVPETVTHLF RITKDIGCAM TGRIADSRSQ VQKARYEAAN FRYKYGYEMP VDVLCRRIAD INQVYTQNAE MRPLGCSMVL IAYDNEIGPS VYKTDPAGYF SGFKACSVGA KTLEANSYLE KKYKPNLSEE KAIQLAISCL SSVLAIDFKP NGIEIGVVSK SDPTFRILDE REIEEHLTKI AEKD // ID PSB1_DROME STANDARD; PRT; 235 AA. AC P40304; Q9VV84; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit beta type 1 (EC 3.4.25.1) (Proteasome 26 kDa DE subunit). GN PROS26 OR PROS-26 OR L(3)73AI OR CG4097. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94022270; PubMed=8415617; RA Saville K.J., Belote J.M.; RT "Identification of an essential gene, l(3)73Ai, with a dominant RT temperature-sensitive lethal allele, encoding a Drosophila proteasome RT subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 90:8842-8846(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1B. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U00790; AAC46465.1; -. DR EMBL; AE003526; AAF49435.1; -. DR EMBL; AY051697; AAK93121.1; -. DR HSSP; P23724; 1RYP. DR MEROPS; T01.986; -. DR FlyBase; FBgn0002284; Pros26. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00854; PROTEASOME_B; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. FT CONFLICT 192 192 R -> W (IN REF. 1). SQ SEQUENCE 235 AA; 25842 MW; 592307AAEDD98B25 CRC64; MSRLGFEQFP DYQVPGMKHP DFSPYESNGG SIVAIAGDDF AVIAADTRLS SGYNIHSRTQ SKLFKLSPQT VLGSAGCWAD TLSLTGSIKV RMQSYEHTHL RTMTTEAVAQ MLSIAMYNRR FFPYYVSNIL AGIDNEGKGV VYSYDPIGHC EKATYRAGGT AGTLLQPVLD NQIGHKNMNL EDADKIKLTK ERAVSVASDT FISAAERDIY TGDSVLINII TKDGIEVRTL TLRQD // ID PSB3_DROME STANDARD; PRT; 205 AA. AC Q9XYN7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Proteasome subunit beta type 3 (EC 3.4.25.1) (20S proteasome subunit DE beta-3). GN PROS-BETA-3 OR CG11980. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Samarkand; RA Smyth K.A., Belote J.M.; RT "20S proteasome beta3 subunit gene of Drosophila melanogaster."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT PEPTIDE BONDS WITH VERY BROAD CC SPECIFICITY. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1B. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF116898; AAD22968.1; -. DR EMBL; AE003681; AAF54320.1; -. DR HSSP; P25451; 1RYP. DR MEROPS; T01.983; -. DR FlyBase; FBgn0026380; Pros-beta-3. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR001353; Peptidase_T1. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00854; PROTEASOME_B; 1. KW Proteasome; Hydrolase; Protease; Threonine protease. SQ SEQUENCE 205 AA; 23234 MW; 3AE365887AF3A247 CRC64; MSILAYNGGC VVAMRGKDCV AIATDHRFGI QAQTISTDFK KVFHIGPRMF LGLTGLQTDI LTVRDRLMFR KNLYETRENR EMCPKPFSAM MSSFLYEHRF GPYFIEPVVA GLDPKTMEPF ICNMDLIGCP NAPDDFVVAG TCAEQLYGMC ETLWKPDLEP DQLFEVIAQS IVNAFDRDAM SGWGATVYII EKDKITERTL KTRMD // ID PSC_DROME STANDARD; PRT; 1603 AA. AC P35820; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Posterior sex combs protein. GN PSC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92018190; PubMed=1833647; RA Brunk B.P., Martin E.C., Sharp E., Adler P.N.; RT "Drosophila genes Posterior Sex Combs and Suppressor two of zeste RT encode proteins with homology to the murine bmi-1 oncogene."; RL Nature 353:351-353(1991). CC -!- FUNCTION: THE POLYCOMB GROUP (PC-G) GENES ARE NEEDED TO MAINTAIN CC EXPRESSION PATTERNS OF THE HOMEOTIC SELECTOR GENES OF THE CC ANTENNAPEDIA (ANTP-C) AND BITHORAX (BX-C) COMPLEXES, AND HENCE FOR CC THE MAINTENANCE OF SEGMENTAL DETERMINATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X59275; CAA41965.1; -. DR PIR; S17983; S17983. DR FlyBase; FBgn0005624; Psc. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Zinc-finger; Developmental protein; DNA-binding; Nuclear protein. FT DOMAIN 47 53 POLY-THR. FT DOMAIN 83 88 POLY-THR. FT DOMAIN 91 98 POLY-THR. FT DOMAIN 145 152 POLY-THR. FT DOMAIN 184 202 POLY-SER. FT ZN_FING 265 304 RING-TYPE. FT DOMAIN 642 651 POLY-SER. FT DOMAIN 1066 1069 POLY-GLY. FT DOMAIN 1185 1189 POLY-PRO. FT DOMAIN 1214 1217 POLY-PRO. FT DOMAIN 1391 1396 POLY-PRO. FT DOMAIN 1458 1461 POLY-ALA. FT DOMAIN 1517 1520 POLY-GLY. SQ SEQUENCE 1603 AA; 169999 MW; 77024F4097736473 CRC64; MMTPESKAIQ PAAATTKQTA EATPEATATT TMAHTQQKSQ LSTLAKTTTT TATNKAAKSV VSNANSSGNN SSKKLALSQS QKTTTTTTPP TTTTTTTTAA EATTNADKMQ KQQQLKQQLF AACSIKVKSE NALATTATAA LAAATTTTTT ATPALATGKA AKTILENGIK KESTPPAVES VEASSSSSSS SSSSSSSSSS WSTTRRATSE DASSNGGASA DEEKSEEDPT AAVAASSTAT TTSDLATTSR PRPVLLTAVN PHIICHLCQG YLINATTIVE CLHSFCHSCL INHLRKERFC PRCEMVINNA KPNIKSDTTL QAIVYKLVPG LYERELMRKR AFYKDRPEEA ALATPEQRGD DTEHLIFSPS DDMSLSLEYA ELGELKTDSE PELVDTLRPR YLQCPAMCRV SHLKKFVYDK FEIDAQRFSI DIMYKVKTIV LLDYYTLMDI AYTYTWKRDA PMRFYYRVYE SPQPLVKPAP RRVLPLKLEK QERENQEQQL AVEVASSKVE PVSLAEDQKA EASIKVEGEE STREIVKEVI KDVAATPPTE TLKLVINRNM LDKREKSHSP QLSSKSSSKS SPCTPVSSPS EPNIKLKIDL SKQNSVTIID MSDPERREIV KPLKPEKESR SKKKDKDGSP KSSSSSSSSS SGERKRKSPS PLTVPPLTIR TERIMSPSGV STLSPRVTSG AFSEDPKSEF LKSFALKPIK VKVESPERTL NNRAITPPSP SVQQSASPKS KGNNLDDSIL MKPPSCMPPK SIASSKRKSK EPVKAVSKKQ KLSPPLPTVD FKIRLPVTNG NSSGTASPKI EKPLMPPPAK PPMLAPRKLQ PSAQFAPPPS PIHHHAGVQM SAPGNRTPIA KRYQPILPKA SRPNPFANIP NDVNRLLKDA GTEIKSIGGG SVENNSNSAQ KPHLYGPKGE TKMGPPALPA TTPSQGNKNV GKQAGNLPMS APPNKGNSSN NYLNLALFNS NKCKGKEAPP GCRTPMYTPN SPIYSPSSPQ YVPSYNIPTM PTYKYTPKPT PNSGSGNGGS GSYLQNMLGG GNGGSLGGLF PSPPTKSDQN TNPAQGGGGS SSATQSGGNN GIVNNNIYMP NEDAPEKQQV KVKSLLNSCN INIPSSLSIT ISRDNGDSSS PNNGQHPKHK SPVNNYIEIV KLPDQPQDQV QAAKEAQKRQ SPPAAVPGHL AAKLPPPPPS KAIPSPQHLV SRMTPPQLPK VATPPPPSSP RVITPPKTSP PANAAKVTPL KPVLTPTQVD KKTPSPEKRT AAQMGSHSPT ASENKSPKGG AAGVANSTGG TQNGDPAAKK FRPILPRQNG MPELAPKLPT LAPFVGFNPL QNPAAGKKVP PSKKSPNAGA AAHQSGQQKL VNGGQPQSAQ QKTSPPAQKN QQQVKKVSKN PTPPPPSLPA VGKMMPHPVM HSQNAPLSIA SSASAAAVAS GQLDLSNFLK ENLRRVHAAQ AAQAAQVAAA ANQSNMMYNL AQMGHMTPAM YNYQQAYFRE QLSRMQRVGN EVFNDYLQKL KTAAATGGGG PVEGELKPML PTVTLPSPGA TPPAASPKTS PLPAGKLTAA ATAPQTKGNS SSGAANARQQ TAATGNNGAT VPAASLPPAT KSK // ID PSD3_DROME STANDARD; PRT; 494 AA. AC P25161; Q9VJ09; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable 26S proteasome non-ATPase regulatory subunit 3 (26S DE proteasome subunit S3) (Diphenol oxidase A2 component) (DOX-A2). GN DOX-A2 OR CG10484. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91365251; PubMed=1909680; RA Pentz E.S., Wright T.R.F.; RT "Drosophila melanogaster diphenol oxidase A2: gene structure and RT homology with the mouse mast-cell tum- transplantation antigen, RT P91A."; RL Gene 103:239-242(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTS AS A REGULATORY SUBUNIT OF THE 26 PROTEASOME WHICH CC IS INVOLVED IN THE ATP-DEPENDENT DEGRADATION OF UBIQUITINATED CC PROTEINS (BY SIMILARITY). CC -!- SUBUNIT: THE 26S PROTEASOME IS COMPOSED OF A CORE PROTEASE, KNOWN CC AS THE 20S PROTEASOME, CAPPED AT ONE OR BOTH ENDS BY THE 19S CC REGULATORY COMPLEX (RC). THE RC IS COMPOSED OF AT LEAST 18 CC DIFFERENT SUBUNITS IN TWO SUBCOMPLEXES, THE BASE AND THE LID, CC WHICH FORM THE PORTIONS PROXIMAL AND DISTAL TO THE 20S PROTEOLYTIC CC CORE, RESPECTIVELY (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: BLOOD (CRYSTAL) CELLS AND CUTICLE. CC -!- SIMILARITY: CONTAINS 1 PCI DOMAIN. CC -!- SIMILARITY: BELONGS TO THE PROTEASOME SUBUNIT S3 FAMILY. CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT TO BE THE DIPHENOL OXIDASE CC A2 COMPONENT INVOLVED IN CATECHOLAMINE METABOLISM, MELANIN CC FORMATION, AND SCLEROTIZATION OF THE CUTICLE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63010; AAB00732.1; -. DR EMBL; AE003661; AAF53749.1; -. DR PIR; JH0665; JH0665. DR FlyBase; FBgn0000486; Dox-A2. DR GO; GO:0005838; C:proteasome regulatory particle (sensu Eukarya); IDA. DR GO; GO:0004299; F:proteasome endopeptidase activity; IDA. DR GO; GO:0006508; P:proteolysis and peptidolysis; IDA. DR InterPro; IPR000717; PCI. DR InterPro; IPR001440; TPR. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. KW Proteasome. SQ SEQUENCE 494 AA; 56004 MW; 8659CBCAFF95B735 CRC64; MTNATDIGAN DVEMEVDPTA ETLADEKKNQ DVAAVQEIRE QIRQIEKGVA SKESRFILRV LRNLPNTRRK LNGVVFRNLA QSIYPAGADR EAAVALMPAV EKDATELPDV PKKQVATKAP IAEVDAYFYL LLLVKLIDAS DLKRAGISAD ALMAKISIQN RRTLDLIGAK SYFYFSRVAE LKNSLEGIRS FLHARLRTAT LRNDFEGQAV LINCLLRNYL HYALYDQADK LVKKSVYPES ASNNEWARFL YYLGRIKAAK LEYSDAHKHL VQALRKSPQH AAIGFRQTVQ KLIIVVELLL GNIPERVVFR QAGLRQSLGA YFQLTQAVRL GNLKRFGDVV SQYGPKFQLD HTFTLIIRLR HNVIKTAIRS IGLSYSRISP QDIAKRLMLD SAEDAEFIVS KAIRDGVIEA TLDPAQNFMR SKESTDIYST REPQLAFHER ISFCLNLHNQ SVKAMRYPPK SYGKDLESAE ERREREQQDL ELAKEMAEDD EDGF // ID PSD4_DROME STANDARD; PRT; 396 AA. AC P55035; Q9V473; DT 01-OCT-1996 (Rel. 34, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome DE regulatory subunit S5A) (Multiubiquitin chain binding protein) (54 kDa DE subunit of mu particle) (p54). GN PROS54 OR PROS-54 OR CG7619. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95377304; PubMed=7649173; RA Haracska L., Udvardy A.; RT "Cloning and sequencing a non-ATPase subunit of the regulatory RT complex of the Drosophila 26S protease."; RL Eur. J. Biochem. 231:720-725(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: BINDS AND PRESUMABLY SELECTS UBIQUITIN-CONJUGATES FOR CC DESTRUCTION. CC -!- SUBUNIT: THE 26S PROTEASOME IS COMPOSED OF A CORE PROTEASE, KNOWN CC AS THE 20S PROTEASOME, CAPPED AT ONE OR BOTH ENDS BY THE 19S CC REGULATORY COMPLEX (RC). THE RC IS COMPOSED OF AT LEAST 18 CC DIFFERENT SUBUNITS IN TWO SUBCOMPLEXES, THE BASE AND THE LID, CC WHICH FORM THE PORTIONS PROXIMAL AND DISTAL TO THE 20S PROTEOLYTIC CC CORE, RESPECTIVELY (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PROTEASOME SUBUNIT S5A FAMILY. CC -!- SIMILARITY: CONTAINS 3 UBIQUITIN-INTERACTING MOTIF (UIM) REPEATS. CC -!- SIMILARITY: CONTAINS 1 VWFA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S79502; AAB35145.1; -. DR EMBL; AE003594; AAF51741.1; -. DR EMBL; AF132175; AAD34763.1; -. DR PIR; S66528; S66528. DR FlyBase; FBgn0015283; Pros54. DR GO; GO:0005838; C:proteasome regulatory particle (sensu Eukarya); IDA. DR GO; GO:0004299; F:proteasome endopeptidase activity; IDA. DR GO; GO:0006508; P:proteolysis and peptidolysis; IDA. DR InterPro; IPR003903; UIM. DR InterPro; IPR002035; VWF_A. DR Pfam; PF02809; UIM; 3. DR SMART; SM00726; UIM; 3. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50330; UIM; 3. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Proteasome; Repeat. FT DOMAIN 1 188 VWFA. FT DOMAIN 212 231 UIM 1. FT DOMAIN 276 295 UIM 2. FT DOMAIN 303 322 UIM 3. FT CONFLICT 9 9 C -> S (IN REF. 1). SQ SEQUENCE 396 AA; 42618 MW; 061418F6F7FE819F CRC64; MVLESTMICF DNSDFQRNGD YFPTRLIVQR DGINLVCLTK LRSNPENNVG LMTLSNTVEV LATLTSDAGR IFSKMHLVQP KGEINLLTGI RIAHLVLKHR QGKNHKMRIV VFVGSPINHE EGDLVKQAKR LKKEKVNVDI VSFGDHGNNN EILTAFINAL NGKDGTGSHL VSVPRGSVLS DALLSSPIIQ GEDGMGGAGL GGNVFEFGVD PNEDPELALA LRVSMEEQRQ RQESEQRRAN PDGAPPTGGD AGGGGGVSGS GPGNEESAGA ENEANTEEAM LQRALALSTE TPEDNLPDFA NMTEEEQIAF AMQMSMQDAP DDSVTQQAKR PKTDEANAPM DVDEDYSEVI GDPAFLQSVL ENLPGVDPQS EAVRDAVGSL NKDKDKKSDG KDSQKK // ID PSD6_DROME STANDARD; PRT; 389 AA. AC Q9V3G7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome DE regulatory subunit S10) (Rpn7 protein). GN RPN7 OR CG5378. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RA Hoelzl H., Kapelari B., Kellermann J., Nitsch M., Seemueller E., RA Voges D., Udvardy A., Mueller S.A., Engel A., Baumeister W.; RT "The regulatory complex of the Drosophila 26S proteasomes."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ACTS AS A REGULATORY SUBUNIT OF THE 26S PROTEASOME WHICH CC IS INVOLVED IN THE ATP-DEPENDENT DEGRADATION OF UBIQUITINATED CC PROTEINS (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 1 PCI DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF145308; AAF08389.1; -. DR EMBL; AE003739; AAF56000.1; -. DR EMBL; AY052008; AAK93432.1; -. DR FlyBase; FBgn0028688; Rpn7. DR GO; GO:0005838; C:proteasome regulatory particle (sensu Eukarya); IDA. DR GO; GO:0016887; F:ATPase activity; ISS. DR GO; GO:0004299; F:proteasome endopeptidase activity; IDA. DR GO; GO:0006510; P:ATP-dependent proteolysis; ISS. DR InterPro; IPR000717; PCI. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. KW Proteasome. FT DOMAIN 191 358 PCI. SQ SEQUENCE 389 AA; 45381 MW; CCC1DE0C7393B6FA CRC64; MPAENLEEQG LEKNPNLELA QTKFLLTLAE YKQDAALKAK LLEAIRTENM APWYEHICSE LGWTVDKDLL ARMKENNRVE VEQLDAAIED AEKNLGEMEV REANLKKSEY LCRIGDKAAA ETAFRKTYEK TVSLGHRLDI VFHLIRLGLF YLDHDLITRN IDKAKYLIEE GGDWDRRNRL KVYQGVYSVA VRDFKAAATF FLDTVSTFTS YELMDYPTFV RYTVYVAMIA LPRNELRDKV IKGSEIQEVL HGLPDVKQFL FSLYNCQYEN FYVHLAGVEK QLRLDYLIHP HYRYYVREMR ILGYTQLLES YRSLTLQYMA ESFGVTVEYI DQELARFIAA GRLHAKVDRV GGIVETNRPD NKNWQYQATI KQGDLLLNRI QKLSRVINI // ID PSD7_DROME STANDARD; PRT; 338 AA. AC P26270; DT 01-MAY-1992 (Rel. 22, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 26S proteasome non-ATPase regulatory subunit 7 (26S proteasome DE regulatory subunit S12) (Proteasome subunit p40) (Mov34 protein). GN MOV34. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=91005870; PubMed=2209467; RA Gridley T., Gray D.A., Orr-Weaver T., Soriano P., Barton D.E., RA Francke U., Jaenisch R.; RT "Molecular analysis of the Mov 34 mutation: transcript disrupted by RT proviral integration in mice is conserved in Drosophila."; RL Development 109:235-242(1990). CC -!- FUNCTION: ACTS AS A REGULATORY SUBUNIT OF THE 26S PROTEASOME WHICH CC IS INVOLVED IN THE ATP-DEPENDENT DEGRADATION OF UBIQUITINATED CC PROTEINS. CC -!- SIMILARITY: CONTAINS 1 MPN (JAB/MOV34) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M64643; AAA28695.1; -. DR FlyBase; FBgn0002787; Mov34. DR GO; GO:0005837; C:26S proteasome; IDA. DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomp...; NAS. DR GO; GO:0004299; F:proteasome endopeptidase activity; IDA. DR GO; GO:0006508; P:proteolysis and peptidolysis; IDA. DR InterPro; IPR003640; Mov34. DR InterPro; IPR003639; Pept_M67_Mov34. DR InterPro; IPR000555; Peptidase_M67. DR Pfam; PF01398; Mov34; 1. DR ProDom; PD363422; Mov34_1; 1. DR ProDom; PD005425; Mov34_2; 1. DR SMART; SM00232; JAB_MPN; 1. KW Proteasome. FT DOMAIN 289 338 GLU/LYS-RICH (KEKE DOMAIN). SQ SEQUENCE 338 AA; 38493 MW; 232B3E94575939C3 CRC64; MPSQEVSVNK VIVHPLVLLS VVDHFNRMGK IGNQKRVVGV LLGCWRSKGV LDVSNTFAVP FDVDDKDKSV WFLDHDYLEN MYGMFKKVNA RERVVGWYHT GPKLHQNDIA INELVRRYCP TPCWSSSTPS PRIWACPQRR TYRWRKVHDD GSPTSKTFEH VPSEIGPEEA EEVGVEHLLR DIKDTTVGSL SQKITNQLMG LKGLNAQLRD IKQYLQRVGD SKMPINHQIV YQLQDIFNLL PDITNDQFTG TMYVKTNDQM LVVYLASMVR SIIALHNLIN NKLANRDAEE GKSDSKEAKE KNKDSKDKDN KETKDKDGKK AEEKADKGKD EGGKGSRK // ID PSN_DROME STANDARD; PRT; 541 AA. AC O02194; O02395; O76802; O96340; Q9TY80; Q9V3L9; Q9V3S1; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Presenilin homolog (dPS) (DmPS). GN PSN OR PS OR CG18803/CG5868. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=97285868; PubMed=9141085; RA Boulianne G.L., Livne-Bar I., Humphreys J.M., Liang Y., Lin C., RA Rogaev E., St George-Hyslop P.H.; RT "Cloning and characterization of the Drosophila presenilin RT homologue."; RL NeuroReport 8:1025-1029(1997). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 2), AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Embryo, and Head; RX MEDLINE=97260623; PubMed=9106743; RA Hong C.-S., Koo E.H.; RT "Isolation and characterization of Drosophila presenilin homolog."; RL NeuroReport 8:665-668(1997). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING. RX MEDLINE=99279250; PubMed=10349633; RA Ye Y., Fortini M.E.; RT "Characterization of Drosophila Presenilin and its colocalization with RT Notch during development."; RL Mech. Dev. 79:199-211(1998). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), AND FUNCTION IN S3 CLEAVAGE OF RP NOTCH. RX MEDLINE=99221488; PubMed=10206647; RA Ye Y., Lukinova N., Fortini M.E.; RT "Neurogenic phenotypes and altered Notch processing in Drosophila RT Presenilin mutants."; RL Nature 398:525-529(1999). RN [5] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; RX MEDLINE=98331525; PubMed=9666900; RA Marfany G., Del-Favero J., Valero R., De Jonghe C., Woodrow S., RA Hendriks L., Van Broeckhoven C., Gonzalez-Duarte R.; RT "Identification of a Drosophila presenilin homologue: evidence of RT alternatively spliced forms."; RL J. Neurogenet. 12:41-54(1998). RN [6] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RX MEDLINE=99423881; PubMed=10493744; RA Guo Y., Livne-Bar I., Zhou L., Boulianne G.L.; RT "Drosophila presenilin is required for neuronal differentiation and RT affects notch subcellular localization and signaling."; RL J. Neurosci. 19:8435-8442(1999). RN [7] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [8] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [9] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [10] RP ALTERNATIVE SPLICING (ISOFORM 3), AND CLEAVAGE. RX MEDLINE=20130801; PubMed=10662508; RA Nowotny P., Gorski S.M., Han S.W., Philips K., Ray W.J., Nowotny V., RA Jones C.J., Clark R.F., Cagan R.L., Goate A.M.; RT "Posttranslational modification and plasma membrane localization of RT the Drosophila melanogaster presenilin."; RL Mol. Cell. Neurosci. 15:88-98(2000). RN [11] RP FUNCTION IN S3 CLEAVAGE OF NOTCH. RX MEDLINE=99221487; PubMed=10206646; RA Struhl G., Greenwald I.; RT "Presenilin is required for activity and nuclear access of Notch in RT Drosophila."; RL Nature 398:522-525(1999). RN [12] RP INTERACTION WITH METL. RX MEDLINE=21601112; PubMed=11738826; RA Zhang S.X., Guo Y., Boulianne G.L.; RT "Identification of a novel family of putative methyltransferases that RT interact with human and Drosophila presenilins."; RL Gene 280:135-144(2001). RN [13] RP FUNCTION IN THE GAMMA-SECRETASE COMPLEX, AND INTERACTION WITH PEN-2; RP APH-1 AND NCT. RX MEDLINE=22547312; PubMed=12660785; RA Takasugi N., Tomita T., Hayashi I., Tsuruoka M., Niimura M., RA Takahashi Y., Thinakaran G., Iwatsubo T.; RT "The role of presenilin cofactors in the gamma-secretase complex."; RL Nature 422:438-441(2003). CC -!- FUNCTION: PROBABLE CATALYTIC SUBUNIT OF THE GAMMA-SECRETASE CC COMPLEX, AN ENDOPROTEASE COMPLEX THAT CATALYZES THE INTRAMEMBRANE CC CLEAVAGE OF INTEGRAL MEMBRANE PROTEINS SUCH AS NOTCH RECEPTOR. CC REQUIRED FOR S3 CLEAVAGE OF NOTCH, WHICH RELEASES ACTIVATED NOTCH CC PROTEIN FROM THE CELL MEMBRANE. INVOLVED IN THE PATTERNING OF THE CC OPTIC LOBES. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). COMPONENT OF THE GAMMA- CC SECRETASE COMPLEX, A COMPLEX COMPOSED OF A PRESENILIN (PSN) CC HOMODIMER, NICASTRIN (NCT), APH-1 AND PEN-2. INTERACTS WITH METL. CC ISOFORM 2 SHOWS A BETTER INTERACTION WITH METL THAN ISOFORM 1. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=A2, A, DLA-b; CC IsoId=O02194-1; Sequence=Displayed; CC Name=2; Synonyms=A1, B, PS-d, DLA-a; CC IsoId=O02194-2; Sequence=VSP_005195; CC Name=3; CC IsoId=O02194-3; Sequence=VSP_007988; CC -!- TISSUE SPECIFICITY: MATERNALLY EXPRESSED IN NURSE AND FOLLICLE CC CELLS. IN EARLY EMBRYOS, EXPRESSED IN ALL OR MOST CELLS AND LATER CC INCREASES IN CNS AND EPIDERMAL TISSUES. IN LARVAE, EXPRESSION IS CC SEEN IN ALL IMAGINAL DISKS, BRAIN AND OPTIC LOBES. IN PUPAE, CC EXPRESSION IS SEEN IN EYE DISK AND BRAIN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT. CC -!- PTM: CLEAVED. THE CLEAVAGE, WHICH PROBABLY TAKES PLACE BETWEEN THE CC 6TH AND THE 7TH TRANSMEMBRANE REGIONS, MAY BE REQUIRED FOR CC ACTIVATION OF THE GAMMA-SECRETASE ACTIVITY. CC -!- SIMILARITY: BELONGS TO THE PRESENILIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U77934; AAB61139.1; -. DR EMBL; U78084; AAB53369.1; -. DR EMBL; AF084184; AAC33129.1; -. DR EMBL; AF084184; AAC33128.1; -. DR EMBL; AF017024; AAD01610.1; -. DR EMBL; AF017025; AAD01611.1; -. DR EMBL; AF017026; AAD01612.1; -. DR EMBL; AF093402; AAD52707.1; -. DR EMBL; AF093402; AAD52708.1; -. DR EMBL; AE003591; AAN12132.1; -. DR EMBL; AE003591; AAF51598.1; -. DR EMBL; AY061316; AAL28864.1; -. DR MEROPS; A22.UPW; -. DR FlyBase; FBgn0019947; Psn. DR GO; GO:0016324; C:apical plasma membrane; IDA. DR GO; GO:0005938; C:cell cortex; IDA. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; IMP. DR InterPro; IPR006639; Peptidase_A22. DR InterPro; IPR001108; Peptidase_A22A. DR Pfam; PF01080; Presenilin; 1. DR PRINTS; PR01072; PRESENILIN. DR SMART; SM00730; PSN; 1. KW Transmembrane; Glycoprotein; Alternative splicing. FT TRANSMEM 107 127 1 (POTENTIAL). FT TRANSMEM 155 175 2 (POTENTIAL). FT TRANSMEM 183 203 3 (POTENTIAL). FT TRANSMEM 217 237 4 (POTENTIAL). FT TRANSMEM 243 263 5 (POTENTIAL). FT TRANSMEM 480 500 6 (POTENTIAL). FT TRANSMEM 507 527 7 (POTENTIAL). FT DOMAIN 320 481 INTERACTION WITH METL. FT CARBOHYD 129 129 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 339 339 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 410 410 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 365 397 Missing (in isoform 3). FT /FTId=VSP_007988. FT VARSPLIC 384 397 Missing (in isoform 2). FT /FTId=VSP_005195. FT CONFLICT 80 81 GG -> RS (IN REF. 2). SQ SEQUENCE 541 AA; 59304 MW; A3B3D54348A2C03F CRC64; MAAVNLQASC SSGLASEDDA NVGSQIGAAE RLERPPRRQQ QRNNYGSSNQ DQPDAAILAV PNVVMREPCG SRPSRLTGGG GGSGGPPTNE MEEEQGLKYG AQHVIKLFVP VSLCMLVVVA TINSISFYNS TDVYLLYTPF HEQSPEPSVK FWSALANSLI LMSVVVVMTF LLIVLYKKRC YRIIHGWLIL SSFMLLFIFT YLYLEELLRA YNIPMDYPTA LLIMWNFGVV GMMSIHWQGP LRLQQGYLIF VAALMALVFI KYLPEWTAWA VLAAISIWDL IAVLSPRGPL RILVETAQER NEQIFPALIY SSTVVYALVN TVTPQQSQAT ASSSPSSSNS TTTTRATQNS LASPEAAAAS GQRTGNSHPR QNQRDDGSVL ATEGMPLVTF KSNLRGNAEA AGFTQEWSAN LSERVARRQI EVQSTQSGNA QRSNEYRTVT APDQNHPDGQ EERGIKLGLG DFIFYSVLVG KASSYGDWTT TIACFVAILI GLCLTLLLLA IWRKALPALP ISITFGLIFC FATSAVVKPF MEDLSAKQVF I // ID PTP1_DROME STANDARD; PRT; 1631 AA. AC P35992; DT 01-JUN-1994 (Rel. 29, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein-tyrosine phosphatase 10D precursor (EC 3.1.3.48) (Receptor- DE linked protein-tyrosine phosphatase 10D). GN PTP10D. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC TISSUE=Embryo; RX MEDLINE=92034989; PubMed=1657402; RA Tian S.-S., Tsoulfas P., Zinn K.; RT "Three receptor-linked protein-tyrosine phosphatases are selectively RT expressed on central nervous system axons in the Drosophila embryo."; RL Cell 67:675-685(1991). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=92034988; PubMed=1657401; RA Yang X., Seow K.T., Bahri S.M., Oon S.H., Chia W.; RT "Two Drosophila receptor-like tyrosine phosphatase genes are RT expressed in a subset of developing axons and pioneer neurons in the RT embryonic CNS."; RL Cell 67:661-673(1991). CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P35992-1; Sequence=Displayed; CC Name=Short; CC IsoId=P35992-2; Sequence=VSP_005143, VSP_005144; CC -!- TISSUE SPECIFICITY: SELECTIVELY EXPRESSED IN A SUBSET OF AXONS AND CC PIONEER NEURONS IN THE EMBRYO. CC -!- SIMILARITY: CONTAINS 12 FIBRONECTIN TYPE III DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PROTEIN-TYROSINE PHOSPHATASE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M80538; AAA28952.1; -. DR EMBL; M80465; AAA28484.1; -. DR PIR; D41214; D41214. DR HSSP; P18052; 1YFO. DR FlyBase; FBgn0004370; Ptp10D. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA. DR InterPro; IPR000282; Cytok_receptor_2. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003961; FN_III. DR InterPro; IPR003962; FnIII_subd. DR InterPro; IPR000387; TYR_phosphatase. DR InterPro; IPR000242; Tyr_PP. DR Pfam; PF00041; fn3; 10. DR Pfam; PF00102; Y_phosphatase; 1. DR PRINTS; PR00014; FNTYPEIII. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 11. DR SMART; SM00194; PTPc; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. KW Transmembrane; Hydrolase; Repeat; Signal; Alternative splicing. FT SIGNAL 1 42 POTENTIAL. FT CHAIN 43 1631 PROTEIN-TYROSINE PHOSPHATASE 10D. FT DOMAIN 43 1197 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1198 1218 POTENTIAL. FT DOMAIN 1219 1631 CYTOPLASMIC (POTENTIAL). FT DOMAIN 43 119 FIBRONECTIN TYPE-III 1. FT DOMAIN 120 214 FIBRONECTIN TYPE-III 2. FT DOMAIN 215 308 FIBRONECTIN TYPE-III 3. FT DOMAIN 309 402 FIBRONECTIN TYPE-III 4. FT DOMAIN 403 493 FIBRONECTIN TYPE-III 5. FT DOMAIN 494 580 FIBRONECTIN TYPE-III 6. FT DOMAIN 581 669 FIBRONECTIN TYPE-III 7. FT DOMAIN 670 766 FIBRONECTIN TYPE-III 8. FT DOMAIN 767 861 FIBRONECTIN TYPE-III 9. FT DOMAIN 862 955 FIBRONECTIN TYPE-III 10. FT DOMAIN 956 1048 FIBRONECTIN TYPE-III 11. FT DOMAIN 1049 1190 FIBRONECTIN TYPE-III 12. FT DOMAIN 1291 1533 PROTEIN-TYROSINE PHOSPHATASE. FT CARBOHYD 75 75 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 106 106 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 128 128 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 169 169 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 212 212 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 229 229 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 259 259 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 289 289 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 317 317 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 471 471 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 486 486 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 512 512 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 533 533 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 588 588 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 668 668 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 687 687 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 719 719 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 723 723 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 823 823 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 841 841 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 874 874 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 908 908 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 925 925 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1001 1001 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1104 1104 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1136 1136 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1195 1195 N-LINKED (GLCNAC...) (POTENTIAL). FT ACT_SITE 1468 1468 PHOSPHOCYSTEINE INTERMEDIATE (BY FT SIMILARITY). FT VARSPLIC 1549 1558 GQQVQLDENG -> DDEGIAESGM (in isoform FT Short). FT /FTId=VSP_005143. FT VARSPLIC 1559 1631 Missing (in isoform Short). FT /FTId=VSP_005144. FT CONFLICT 124 124 D -> I (IN REF. 2). FT CONFLICT 127 127 S -> L (IN REF. 2). SQ SEQUENCE 1631 AA; 185007 MW; 2A3753DE97EE7EE3 CRC64; MLYQLSKATT RIRLKRQKAV PQHRWLWSLA FLAAFTLKDV RCADLAISIP NNPGLDDGAS YRLDYSPPFG YPEPNTTIAS REIGDEIQFS RALPGTKYNF WLYYTNFTHH DWLTWTVTIT TAPDPPSNLS VQVRSGKNAI ILWSPPTQGS YTAFKIKVLG LSEASSSYNR TFQVNDNTFQ HSVKELTPGA TYQVQAYTIY DGKESVAYTS RNFTTKPNTP GKFIVWFRNE TTLLVLWQPP YPAGIYTHYK VSIEPPDAND SVLYVEKEGE PPGPAQAAFK GLVPGRAYNI SVQTMSEDEI SLPTTAQYRT VPLRPLNVTF DRDFITSNSF RVLWEAPKGI SEFDKYQVSV ATTRRQSTVP RSNEPVAFSD FRDIAEPGKT FNVIVKTVSG KVTSWPATGD VTLRPLPVRN LRSINDDKTN TMIITWEADP ASTQDEYRIV YHELETFNGD TSTLTTDRTR FTLESLLPGR NYSLSVQAVS KKMESNETSI FVVTRPSSPI IEDLKSIRMG LNISWKSDVN SKQEQYEVLY SRNGTSDLRT QKTKESRLVI KNLQPGAAYE LKVFAVSHDL RSEPHAYFQA VYPNPPRNMT IETVRSNSVL VHWSPPESGE FTEYSIRYRT DSEQQWVRLP SVRSTEADIT DMTKGEKYTI QVNTVSFGVE SPVPQEVNTT VPPNPVSNII QLVDSRNITL EWPKPEGRVE SYILKWWPSD NPGRVQTKNV SENKSADDLS TVRVLIGELM PGVQYKFDIQ TTSYGILSGI TSLYPRTMPL IQSDVVVANG EKEDERDTIT LSYTPTPQSS SKFDIYRFSS GDAEIRDKEK LANDTDRKVT FTGLVPGRLY NITVWTVSGG VASLPIQRQD RLYPEPITQL HATNITDTEI SLRWDLPKGE YNDFDIAYLT ADNLLAQNMT TRNEITISDL RPHRNYTFTV VVRSGTESSV LRSSSPLSAS FTTNEAVPGR VERFHPTDVQ PSEINFEWSL PSSEANGVIR QFSIAYTNIN NLTDAGMQDF ESEEAFGVIK NLKPGETYVF KIQAKTAIGF GPEREYRQTM PILAPPRPAT QVVPTEVYRS SSTIQIRFRK NYFSDQNGQV RMYTIIVAED DAKNASGLEM PSWLDVQSYS VWLPYQAIDP YYPFENRSVE DFTIGTENCD NHKIGYCNGP LKSGTTYRVK VRAFTGADKF TDTAYSFPIQ TDQDNTSLIV AITVPLTIIL VLLVTLLFYK RRRNNCRKTT KDSRANDNMS LPDSVIEQNR PILIKNFAEH YRLMSADSDF RFSEEFEELK HVGRDQPCTF ADLPCNRPKN RFTNILPYDH SRFKLQPVDD DEGSDYINAN YVPGHNSPRE FIVTQGPLHS TRDDFWRMCW ESNSRAIVML TRCFEKGREK CDQYWPNDTV PVFYGDIKVQ ILNDSHYADW VMTEFMLCRG SEQRILRHFH FTTWPDFGVP NPPQTLVRFV RAFRDRIGAE QRPIVVHCSA GVGRSGTFIT LDRILQQINT SDYVDIFGIV YAMRKERVWM VQTEQQYICI HQCLLAVLEG KENIVGPARE MHDNEGYEGQ QVQLDENGDV VATIEGHLSH HDLQQAEAEA IDDENAAILH DDQQPLTSSF TGHHTHMPPT TSMSSFGGGG GGHTNVDAPD R // ID PTP6_DROME STANDARD; PRT; 1462 AA. AC P16620; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein-tyrosine phosphatase DPTP precursor (EC 3.1.3.48) (Protein- DE tyrosine-phosphate phosphohydrolase). GN PTP69D OR DPTP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90046860; PubMed=2554325; RA Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.; RT "A family of receptor-linked protein tyrosine phosphatases in humans RT and Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989). CC -!- FUNCTION: IT IS POSSIBLE THAT DPTP IS A CELL ADHESION RECEPTOR. CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: CONTAINS 2 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -!- SIMILARITY: CONTAINS 2 FIBRONECTIN TYPE III DOMAINS. CC -!- SIMILARITY: CONTAINS 2 PROTEIN-TYROSINE PHOSPHATASE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27699; AAA28842.1; -. DR PIR; B36182; B36182. DR HSSP; P18052; 1YFO. DR FlyBase; FBgn0014007; Ptp69D. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA. DR GO; GO:0007415; P:defasciculation of motor neuron; IGI. DR GO; GO:0008045; P:motor axon guidance; IGI. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003961; FN_III. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR InterPro; IPR000387; TYR_phosphatase. DR InterPro; IPR000242; Tyr_PP. DR Pfam; PF00041; fn3; 3. DR Pfam; PF00047; ig; 2. DR Pfam; PF00102; Y_phosphatase; 2. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 3. DR SMART; SM00408; IGc2; 1. DR SMART; SM00194; PTPc; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. KW Hydrolase; Receptor; Glycoprotein; Signal; Transmembrane; KW Cell adhesion; Immunoglobulin domain; Repeat. FT SIGNAL 1 23 FT CHAIN 24 1462 PROTEIN-TYROSINE PHOSPHATASE DPTP. FT DOMAIN 24 805 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 806 823 POTENTIAL. FT DOMAIN 824 1462 CYTOPLASMIC (POTENTIAL). FT DOMAIN 24 125 IG-LIKE C2-TYPE 1. FT DOMAIN 131 230 IG-LIKE C2-TYPE 2. FT DOMAIN 332 437 FIBRONECTIN TYPE-III 1. FT DOMAIN 438 538 FIBRONECTIN TYPE-III 2. FT DOMAIN 912 1165 PROTEIN-TYROSINE PHOSPHATASE 1. FT DOMAIN 1208 1459 PROTEIN-TYROSINE PHOSPHATASE 2. FT ACT_SITE 1097 1097 PHOSPHOCYSTEINE INTERMEDIATE (BY FT SIMILARITY). FT ACT_SITE 1391 1391 PHOSPHOCYSTEINE INTERMEDIATE (BY FT SIMILARITY). FT DISULFID 45 112 POTENTIAL. FT DISULFID 154 214 POTENTIAL. FT CARBOHYD 40 40 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 58 58 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 64 64 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 85 85 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 105 105 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 109 109 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 119 119 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 162 162 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 191 191 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 196 196 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 209 209 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 255 255 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 288 288 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 302 302 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 429 429 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 442 442 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 451 451 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 516 516 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 613 613 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 701 701 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 755 755 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1462 AA; 167411 MW; F8091D69E88230EB CRC64; MALLYRRMSM LLNIILAYIF LCAICVQGSV KQEWAEIGKN VSLECASENE AVAWKLGNQT INKNHTRYKI RTEPLKSNDD GSENNDSQDF MKYKNVLTLL DVNINDSGNY TCTAQTGQNH STEFQVKPYL PSKVLQSTPD RIKRKIKQDV MLYCLIEMYP QNETTNRNLK WLKDGSQFEF LDTFSSISKL NDTHLNFTLE FTEVYKKENG TYKCTVFDDT GLEITSKEIT LFVMEVPQVS IDFAKAVGAN KIYLNWTVND GNDPIQKFFI TLQEAGTPTF TYHKDFINGS HTSYILDHFK PNTTYFLRIV GKNSIGNGQP TQYPQGITTL SYDPIFIPKV ETTGSTASTI TIGWNPPPPD LIDYIQYYEL IVSESGEVPK VIEEAIYQQN SRNLPYMFDK LKTATDYEFR VRACSDLTKT CGPWSENVNG TTMDGVATKP TNLSIQCHHD NVTRGNSIAI NWDVPKTPNG KVVSYLIHLL GNPMSTVDRE MWGPKIRRID EPHHKTLYES VSPNTNYTVT VSAITRHKKN GEPATGSCLM PVSTPDAIGR TMWSKVNLDS KYVLKLYLPK ISERNGPICC YRLYLVRINN DNKELPDPEK LNIATYQEVH SDNVTRSSAY IAEMISSKYF RPEIFLGAEK RFSENNDIIR GNDEICRKCL EGTPFLRKPE IIHIPPQGSL SNSDSELPIL SEKDNLIKGA NLTEHALKIL ESKLRDKRNA VTSDENPILS AVNPNVPLHD SSRDVFDGEI DINSNYTGFL EIIVRDRNNA LMAYSKYFDI ITPATEAEPI QSLNNMDYYL SIGVKAGAVL LGVILVFIVL WVFHHKKTKN ELQGEDTLTL RDSLSRALFG RRNHNHSHFI TSGNHKGFDA GPIHRLDLEN AYKNRHKDTD YGFLREYEML PNRFSDRTTK NSDLKENACK NRYPDIKAYD QTRVKLAVIN GLQTTDYINA NFVIGYKERK KFICAQGPME STIDDFWRMI WEQHLEIIVI LTNLEEYNKA KCAKYWPEKV FDTKQFGDIL VKFAQERKTG DYIERTLNVS KNKANVGEEE DRRQITQYHY LTWKDFMAPE HPHGIIKFIR QINSVYSLQR GPILVHCSAG VGRTGTLVAL DSLIQQLEEE DSVSIYNTVC DLRHQRNFLV QSLKQYIFLY RALLDTGTFG NTDICIDTMA SAIESLKRKP NEGKCKLEME FEKLLATADE ISKSCSVGEN EENNMKNRSQ EIIPYDRNRV ILTPLPMREN STYINASFIE GYDNSETFII AQDPFENTIG DFWRMISEQS VTTLVMISEI GDGPRKCPRY WADDEVQYDH ILVKYVHSES CPYYTRREFY VTNCKIDDTL KVTQFQYNGW PTVDGEVPEV CRGIIELVDQ AYNHYKNNKN SGCRSPLTVH CSLGTDRSSI FVAMCILVQH LRLEKCVDIC ATTRKLRSQR TGLINSYAQY EFLHRAIINY SDLHHIAEST LD // ID PTP9_DROME STANDARD; PRT; 1301 AA. AC P35832; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein-tyrosine phosphatase 99A precursor (EC 3.1.3.48) (Receptor- DE linked protein-tyrosine phosphatase 99A). GN PTP99A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC TISSUE=Eye imaginal disk; RX MEDLINE=92107930; PubMed=1662390; RA Hariharan I.K., Chuang P.-T., Rubin G.M.; RT "Cloning and characterization of a receptor-class phosphotyrosine RT phosphatase gene expressed on central nervous system axons in RT Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 88:11266-11270(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC TISSUE=Embryo; RX MEDLINE=92034989; PubMed=1657402; RA Tian S.-S., Tsoulfas P., Zinn K.; RT "Three receptor-linked protein-tyrosine phosphatases are selectively RT expressed on central nervous system axons in the Drosophila embryo."; RL Cell 67:675-685(1991). RN [3] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=92034988; PubMed=1657401; RA Yang X., Seow K.T., Bahri S.M., Oon S.H., Chia W.; RT "Two Drosophila receptor-like tyrosine phosphatase genes are RT expressed in a subset of developing axons and pioneer neurons in the RT embryonic CNS."; RL Cell 67:661-673(1991). CC -!- FUNCTION: MAY PLAY A KEY ROLE IN SIGNAL TRANSDUCTION AND GROWTH CC CONTROL. CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P35832-1; Sequence=Displayed; CC Name=Short; CC IsoId=P35832-2; Sequence=VSP_005142; CC -!- TISSUE SPECIFICITY: SELECTIVELY EXPRESSED IN A SUBSET OF AXONS AND CC PIONEER NEURONS IN THE EMBRYO. CC -!- SIMILARITY: CONTAINS 3 FIBRONECTIN TYPE III DOMAINS. CC -!- SIMILARITY: CONTAINS 2 PROTEIN-TYROSINE PHOSPHATASE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81795; AAA28483.1; -. DR EMBL; M80539; AAA28485.1; -. DR EMBL; M80464; AAA28486.1; -. DR PIR; A41622; A41622. DR HSSP; P18052; 1YFO. DR FlyBase; FBgn0004369; Ptp99A. DR GO; GO:0007415; P:defasciculation of motor neuron; IGI. DR GO; GO:0008045; P:motor axon guidance; IGI. DR InterPro; IPR003961; FN_III. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR000387; TYR_phosphatase. DR InterPro; IPR000242; Tyr_PP. DR Pfam; PF00041; fn3; 2. DR Pfam; PF00102; Y_phosphatase; 2. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 2. DR SMART; SM00194; PTPc; 2. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. KW Transmembrane; Hydrolase; Repeat; Signal; Alternative splicing. FT SIGNAL 1 29 POTENTIAL. FT CHAIN 30 1301 PROTEIN-TYROSINE PHOSPHATASE 99A. FT DOMAIN 30 394 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 395 415 POTENTIAL. FT DOMAIN 416 1301 CYTOPLASMIC (POTENTIAL). FT DOMAIN 64 168 FIBRONECTIN TYPE-III 1. FT DOMAIN 169 268 FIBRONECTIN TYPE-III 2. FT DOMAIN 269 368 FIBRONECTIN TYPE-III 3. FT DOMAIN 497 747 PROTEIN-TYROSINE PHOSPHATASE 1. FT DOMAIN 748 975 PROTEIN-TYROSINE PHOSPHATASE 2. FT ACT_SITE 682 682 PHOSPHOCYSTEINE INTERMEDIATE (BY FT SIMILARITY). FT DOMAIN 1076 1091 POLY-GLN. FT CARBOHYD 33 33 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 176 176 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 212 212 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 278 278 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 322 322 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 336 336 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1050 1119 Missing (in isoform Short). FT /FTId=VSP_005142. FT CONFLICT 586 586 P -> R (IN REF. 2 AND 3). FT CONFLICT 1205 1205 N -> H (IN REF. 3). SQ SEQUENCE 1301 AA; 145336 MW; 8241E3E19A4CA5BD CRC64; MPRPQHHALL RAMLKLLLFA SIAEHCATAL PTNSSNSPSS PSPFTVASLP PTTASSSSSP AVISTSSFDR NLADLVNPEA ETSGSGWESL ETEFNLATTV DSSTQKTAKE PVLGTAATSI EQQDQPPDVP ATTLAFANAF PVPVAGEMGN GNGNYNDATP PYAAVDDNYV PSKPQNLTIL DVSANSITMS WHPPKNQNGA IAGYHVFHIH DNQTGVEIVK NSRNSVETLI HFELQNLRPY TDYRVIVKAF TTKNEGEPSD QIAQRTDVGG PSAPAIVNLT CHSQESITIR WRRPYEFYNT IDFYIIKTRL AGQDTHRDIR INASAKELET AMILQNLTTN SYYEVKVAAA TFSVINPKKI VLGKFSESRI IQLQPNCEKL QPLLRQSHND YNLAVLVGII FSCFGIILII MAFFLWSRKC FHAAYYYLDD PPHHPNAPQV DWEVPVKIGD EIRAAVPVNE FAKHVASLHA DGDIGFSREY EAIQNECISD DLPCEHSQHP ENKRKNRYLN ITAYDHSRVH LHPTPGQKKN LDYINANFID GYQKGHAFIG TQGPLPDTFD CFWRMIWEQR VAIIVMITNL VERGRPKCDM YWPKDGVETY GVIQVKLIEE EVMSTYTVRT LQIKHLKLKK KKQCNTEKLV YQYHYTNWPD HGTPDHPLPV LNFVKKSSAA NPAEAGPIVV HCSAGVGRTG TYIVLDAMLK QIQQKNIVNV FGFLRHIRAQ RNFLVQTEEQ YIFLHDALVE AIASGETNLM AEQVEELKNC TPYLEQQYKN IIQFQPKDIH IASAMKQVNS IKNRGAIFPI EGSRVHLTPK PGEDGSDYIN ASWLHGFRRL RDFIVTQHPM AHTIKDFWQM VWDHNAQTVV LLSSLDDINF AQFWPDEATP IESDHYRVKF LNKTNKSDYV SRDFVIQSIQ DDYELTVKML HCPSWPEMSN PNSIYDFIVD VHERCNDYRN GPIVIVDRYG GAQACTFCAI SSLAIEMEYC STANVYQYAK LYHNKRPGVW TSSEDIRVIY NILSFLPGNL NLLKRTALRT EFEDVTTATP DLYSKICSNG NVPQHVILQQ QQLHMLQLQQ QHLETQQQQQ QQQQQQQQQQ QTALNETVST PSTDTNPSLL PILSLLPPTV APLSSSSSTT PPTPSTPTPQ PPQTIQLSSH SPSDLSHQIS STVANAASPV TPATASASAG ATPTTPMTPT VPPTIPTIPS LASQNSLTLT NANFHTVTNN AADLMEHQQQ QMLALMQQQT QLQQQYNTHP QQHHNNVGDL LMNNADNSPT ASPTITNNNH ITNNNVTSAA ATDAQNLDIV G // ID PTPS_DROME STANDARD; PRT; 168 AA. AC P48611; Q9VIP5; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 6-pyruvoyl tetrahydropterin synthase (EC 4.2.3.12) (PTPS) (PTP DE synthase) (Sepiapterin synthase A) (Protein purple). GN PR OR CG16784. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=96271532; PubMed=8846895; RA Kim N., Kim J., Park D., Rosen C., Dorsett D., Yim J.; RT "Structure and expression of wild-type and suppressible alleles of RT the Drosophila purple gene."; RL Genetics 142:1157-1168(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR PIGMENT AND BIOPTERINE SYNTHESIS. CC -!- CATALYTIC ACTIVITY: 6-[(1S,2R)-1,2-DIHYDROXY-3- CC TRIPHOSPHOOXYPROPYL]-7,8-DIHYDROPTERIN = 6-PYRUVOYL-5,6,7,8- CC TETRAHYDROPTERIN + TRIPHOSPHATE. CC -!- COFACTOR: BINDS 1 ZINC ION PER SUBUNIT (BY SIMILARITY). CC -!- PATHWAY: TETRAHYDROBIOPTERIN BIOSYNTHESIS; SECOND STEP. CC -!- SUBUNIT: HOMOHEXAMER FORMED OF TWO HOMOTRIMERS IN A HEAD TO HEAD CC FASHION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PTPS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36232; AAC47269.1; -. DR EMBL; AE003665; AAF53871.1; -. DR EMBL; AY061078; AAL28626.1; -. DR PIR; S68127; S68127. DR HSSP; P27213; 1B66. DR FlyBase; FBgn0003141; pr. DR GO; GO:0006728; P:pteridine biosynthesis; IDA. DR InterPro; IPR007116; PTPS. DR InterPro; IPR007115; PTPS_hypoth. DR Pfam; PF01242; PTPS; 1. DR ProDom; PD004049; PTPS_hypoth; 1. DR TIGRFAMs; TIGR00039; 6PTHBS; 1. DR PROSITE; PS00987; PTPS_1; 1. DR PROSITE; PS00988; PTPS_2; 1. KW Tetrahydrobiopterin biosynthesis; Lyase; Metal-binding; Zinc. FT METAL 19 19 ZINC (BY SIMILARITY). FT METAL 44 44 ZINC (BY SIMILARITY). FT METAL 46 46 ZINC (BY SIMILARITY). FT ACT_SITE 38 38 BY SIMILARITY. FT ACT_SITE 85 85 BY SIMILARITY. FT ACT_SITE 130 130 BY SIMILARITY. SQ SEQUENCE 168 AA; 19337 MW; BEBB45B046421B84 CRC64; MSQQPVAFLT RRETFSACHR LHSPQLSDAE NLEVFGKCNN FHGHGHNYTV EITVRGPIDR RTGMVLNITE LKEAIETVIM KRLDHKNLDK DVEYFANTPS TTENLAVYIW DNIRLQLKKP ELLYEVKIHE TPKNIISYRG PYPLNGIYNP INKRIAHDSC TNISSDSD // ID PUM_DROME STANDARD; PRT; 1533 AA. AC P25822; Q9VHH4; Q9VHH6; DT 01-MAY-1992 (Rel. 22, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Maternal pumilio protein. GN PUM OR CG9755. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=92249205; PubMed=1576962; RA Macdonald P.M.; RT "The Drosophila pumilio gene: an unusually long transcription unit RT and an unusual protein."; RL Development 114:221-234(1992). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=93093466; PubMed=1459455; RA Barker D.D., Wang C., Moore J., Dickinson L.K., Lehmann R.; RT "Pumilio is essential for function but not for distribution of the RT Drosophila abdominal determinant Nanos."; RL Genes Dev. 6:2312-2326(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP CHARACTERIZATION. RX MEDLINE=98067397; PubMed=9404893; RA Zamore P.D., Williamson J.R., Lehmann R.; RT "The Pumilio protein binds RNA through a conserved domain that RT defines a new class of RNA-binding proteins."; RL RNA 3:1421-1433(1997). CC -!- FUNCTION: SEQUENCE-SPECIFIC RNA-BINDING PROTEIN THAT BINDS TO THE CC NANOS RESPONSE ELEMENT (NRE), A 16 BP SEQUENCE IN THE HB MRNA CC 3'UTR. PUM IS THE ONLY GENE REQUIRED FOR NOS ACTIVITY THAT IS NOT CC ALSO REQUIRED FOR POSTERIOR LOCALIZATION OF GERM LINE CC DETERMINANTS. PUM IS REQUIRED DURING EMBRYOGENESIS WHEN NOS CC ACTIVITY APPARENTLY MOVES ANTERIORLY FROM THE POSTERIOR POLE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. IT IS CONCENTRATED IN THE CC CORTICAL REGION OF THE EMBRYO BENEATH THE NUCLEI. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P25822-1; Sequence=Displayed; CC Name=2; CC IsoId=P25822-2; Sequence=VSP_008216, VSP_008217; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE OVARIES AND DURING THE CC EMBRYOGENESIS. CC -!- DISEASE: LETHAL DEFECTIVE IN POSTERIOR PATTERN FORMATION. CC -!- SIMILARITY: CONTAINS 8 PUMILIO REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62589; CAA44474.1; -. DR EMBL; L07943; AAB59189.1; -. DR EMBL; AE003681; AAF54340.2; -. DR EMBL; AE003681; AAF54338.1; -. DR PIR; A46221; A46221. DR FlyBase; FBgn0003165; pum. DR GO; GO:0008258; P:head involution; IMP. DR InterPro; IPR008938; ARM. DR InterPro; IPR001313; Pumilio/Puf. DR Pfam; PF00806; PUF; 8. DR SMART; SM00025; Pumilio; 8. KW RNA-binding; Repeat; Developmental protein; Alternative splicing. FT REPEAT 1111 1146 PUMILIO 1. FT REPEAT 1147 1182 PUMILIO 2. FT REPEAT 1183 1218 PUMILIO 3. FT REPEAT 1219 1254 PUMILIO 4. FT REPEAT 1255 1290 PUMILIO 5. FT REPEAT 1291 1326 PUMILIO 6. FT REPEAT 1327 1362 PUMILIO 7. FT REPEAT 1367 1402 PUMILIO 8. FT DOMAIN 34 45 ALA-RICH. FT DOMAIN 57 77 GLY/VAL-RICH. FT DOMAIN 83 93 ALA-RICH. FT DOMAIN 130 174 GLY-RICH. FT DOMAIN 152 164 POLY-GLY. FT DOMAIN 181 212 ALA-RICH. FT DOMAIN 213 236 GLN-RICH. FT DOMAIN 262 274 POLY-GLN. FT DOMAIN 571 599 GLY-RICH. FT DOMAIN 708 725 POLY-GLN. FT DOMAIN 936 946 POLY-ALA. FT DOMAIN 1050 1062 POLY-ALA. FT VARSPLIC 1 349 Missing (in isoform 2). FT /FTId=VSP_008216. FT VARSPLIC 350 372 AMMPPQNQYMNSSAVAAANRNAA -> MKLLHDFILDARTA FT EDVALTQEM (in isoform 2). FT /FTId=VSP_008217. FT CONFLICT 362 362 S -> A (IN REF. 1). FT CONFLICT 1103 1103 R -> P (IN REF. 2). FT CONFLICT 1406 1407 PH -> KN (IN REF. 1). FT CONFLICT 1496 1496 V -> I (IN REF. 2). FT CONFLICT 1519 1519 S -> G (IN REF. 2). SQ SEQUENCE 1533 AA; 157529 MW; 0A343220BB1F0B27 CRC64; MKFLGGNDDR NGRGGVGVGT DAIVGSRGGV SQDAADAAGA AAAAAVGYVF QQRPSPGGVG VGVGGVGGGV PGVGAVGSTL HEAAAAEYAA HFAQKQQQTR WACGDDGHGI DNPDKWKYNP PMNPANAAPG GPPGNGSNGG PGAIGTIGMG SGLGGGGGGG AGGGNNGGSG TNGGLHHQSM AAAAANMAAM QQAAALAKHN HMISQAAAAV AAQQQHQHPH QQHPQQQQQQ QQAQNQGHPH HLMGGGNGLG NGNGLGIQHP GQQQQQQQQQ QQQQHPGQYN ANLLNHAAAL GHMSSYAQSG GSMYDHHGGA MHPGMNGGMP KQQPLGPPGA GGPQDYVYMG GQTTVPMGAA MMPPQNQYMN SSAVAAANRN AAITTSTAKK LWEKSDGKGV SSSTPGGPLH PLQIPGIGDP SSVWKDHTWS TQGENILVPP PSRAYAHGGA SDTSNSGNAG ILSPRDSTCA KVVEYVFSGS PTNKDSSLSG LEPHLRNLKF DDNDKSRDDK EKANSPFDTN GLKKDDQVTN SNGVVNGIDD DKGFNRTPGS RQPSPAEESQ PRPPNLLFPP LPFNHMLMDH GQGMGGGLGG VVGSGNGVGG GSGGGGAGGA YAAHQQMAAQ MSQLQPPMMN GVGGGMPMAA QSPMLNHQAA GPNHMESPGN LLQQQNFDVQ QLFRSQNPGL AAVATNAAAA AAAAAAATSA ASAAAAVGAP PVPNGSLQQS QQQQQQQQQQ QQQQQMHMAA ASQQFLAAQQ QAQNAAYAAQ QATSYVINPG QEAAPYMGMI AAAQMPYYGV APWGMYPGNL IPQQGTQPRR PLTPSQQGAE NQPYQVIPAF LDHTGSLLMG GPRTGTPMRL VSPAPVLVPP GATRAGPPPP QGPQLYQPQP QTAQQNLYSQ QNGSSVGGLA LNTSSLTGRR DSFDRSTSAF SPSTMDYTSS GVAAAANAVN STVAQAAAAA AAAAAARGKW PGAMSGAASG AYGALGAGNA SASPLGAPIT PPPSAQSCLL GSRAPGAESR QRQQQQQQLA AVGLPATAAA AQAAVAAAAN NMFGSNSSIF SNPLAIPGTA AVAAAAAAAA AANSRQVAAT AAAAAAVAAA AGGVGGAPQP GRSRLLEDFR NQRYPNLQLR DLANHIVEFS QDQHGSRFIQ QKLERATAAE KQMVFSEILA AAYSLMTDVF GNYVIQKFFE FGTPEQKNTL GMQVKGHVLQ LALQMYGCRV IQKALESISP EQQQEIVHEL DGHVLKCVKD QNGNHVVQKC IECVDPVALQ FIINAFKGQV YSLSTHPYGC RVIQRILEHC TAEQTTPILD ELHEHTEQLI QDQYGNYVIQ HVLEHGKQED KSILINSVRG KVLVLSQHKF ASNVVEKCVT HATRGERTGL IDEVCTFNDN ALHVMMKDQY ANYVVQKMID VSEPTQLKKL MTKIRPHMAA LRKYTYGKHI NAKLEKYYMK ITNPITVGTG AGGVPAASSA AAVSSGATSA SVTACTSGSS TTTTSTTNSL ASPTICSVQE NGSAMVVEPS SPDASESSSS VVSGAVNSSL GPIGPPTNGN VVL // ID PUR1_DROME STANDARD; PRT; 511 AA. AC Q27601; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Amidophosphoribosyltransferase precursor (EC 2.4.2.14) (Glutamine DE phosphoribosylpyrophosphate amidotransferase) (ATASE) (GPAT). GN PRAT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94200596; PubMed=8150282; RA Clark D.V.; RT "Molecular and genetic analyses of Drosophila Prat, which encodes the RT first enzyme of de novo purine biosynthesis."; RL Genetics 136:547-557(1994). CC -!- CATALYTIC ACTIVITY: 5-PHOSPHO-BETA-D-RIBOSYLAMINE + DIPHOSPHATE + CC L-GLUTAMATE = L-GLUTAMINE + 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE CC + H(2)O. CC -!- COFACTOR: BINDS 1 MAGNESIUM ION AND 1 4FE-4S CLUSTER PER SUBUNIT CC (BY SIMILARITY). CC -!- PATHWAY: DE NOVO PURINE BIOSYNTHESIS; FIRST STEP. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE CC PURINE/PYRIMIDINE PHOSPHORIBOSYLTRANSFERASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 TYPE-2 GLUTAMINE AMIDOTRANSFERASE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF017096; AAC39084.1; -. DR PIR; S47860; S47860. DR HSSP; P00497; 1AO0. DR MEROPS; C44.001; -. DR FlyBase; FBgn0004901; Prat. DR InterPro; IPR005854; Amd_phspho_trans. DR InterPro; IPR000583; GATase_2. DR InterPro; IPR002375; Pr/py_rp_transf. DR InterPro; IPR000836; PRTransferase. DR Pfam; PF00310; GATase_2; 1. DR Pfam; PF00156; Pribosyltran; 1. DR TIGRFAMs; TIGR01134; purF; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. DR PROSITE; PS00443; GATASE_TYPE_II; FALSE_NEG. KW Purine biosynthesis; Transferase; Glycosyltransferase; KW Glutamine amidotransferase; Metal-binding; Magnesium; Iron-sulfur; KW 4Fe-4S. FT PROPEP 1 18 PROBABLE. FT CHAIN 19 511 AMIDOPHOSPHORIBOSYLTRANSFERASE. FT ACT_SITE 19 19 GATASE (BY SIMILARITY). FT METAL 286 286 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT METAL 333 333 MAGNESIUM (BY SIMILARITY). FT METAL 395 395 MAGNESIUM (BY SIMILARITY). FT METAL 396 396 MAGNESIUM (BY SIMILARITY). FT METAL 432 432 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT METAL 493 493 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT METAL 496 496 IRON-SULFUR (4FE-4S) (BY SIMILARITY). SQ SEQUENCE 511 AA; 55517 MW; 46A6A9656CD52883 CRC64; MESESISASK ELTGLTHECG VFGAIACGDW PTQMDIAHVI CLGLVALQHR GQESAGIATS EGKCSKNFNV HKGMGMISTL FNDDSMKKLR GNLGIGHTRY STAGGSGVVN CQPFVVHTTH GALALAHNGE LVNNESLRRE VLARGVGLSS HSDSELIAQS LCCAPEDVSE LDGPNWPARI RHFMMLAPLS YSLVIMLKDK IYAVRDTYGN RPLCIGKIVP INAGHGNNLD TPADGWVVSS ESCGFLSIGA RYVREVEPGE IVELSRSGYR TVDIVERPDF KRMAFCIFEY VYFARGDSIF EGQMVYTVRL QCGRQLWREA PVEADIVSSV PESGTAAAHG YARESGIEFA EVLCRNRYVG RTFIQPSTRL RQLGVAKKFG ALSENVAGKR LVLIDDSIVR GNTIGPIIKL LRDAGAREVH IRIASPPLQY PCYMGINIPT REELIANKLN PDQLARHVGA DSLAYLSVEG LVEAVQLKHR DAGDSKSKGT GHCTACLTGE YPGGLPDELS W // ID PUR2_DROME STANDARD; PRT; 1353 AA. AC P00967; DT 21-JUL-1986 (Rel. 01, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trifunctional purine biosynthetic protein adenosine-3 [Includes: DE Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (GARS) (Glycinamide DE ribonucleotide synthetase) (Phosphoribosylglycinamide synthetase); DE Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIRS) DE (Phosphoribosyl-aminoimidazole synthetase) (AIR synthase); DE Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (GART) (GAR DE transformylase) (5'-phosphoribosylglycinamide transformylase)]. GN ADE3 OR GART. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S; RX MEDLINE=88112752; PubMed=3123310; RA Henikoff S., Eghtedarzadeh M.K.; RT "Conserved arrangement of nested genes at the Drosophila Gart locus."; RL Genetics 117:711-725(1987). RN [2] RP SEQUENCE OF 60-1353 FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo; RX MEDLINE=84002248; PubMed=6413075; RA Henikoff S., Sloan J.S., Kelly J.D.; RT "A Drosophila metabolic gene transcript is alternatively processed."; RL Cell 34:405-414(1983). RN [3] RP SEQUENCE OF 1147-1353 FROM N.A. (ISOFORM LONG). RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=83168902; PubMed=6300768; RA Henikoff S., Furlong C.E.; RT "Sequence of a Drosophila DNA segment that functions in Saccharomyces RT cerevisiae and its regulation by a yeast promoter."; RL Nucleic Acids Res. 11:789-800(1983). CC -!- CATALYTIC ACTIVITY: ATP + 5-PHOSPHO-D-RIBOSYLAMINE + GLYCINE = ADP CC + PHOSPHATE + N(1)-(5-PHOSPHO-D-RIBOSYL)GLYCINAMIDE. CC -!- CATALYTIC ACTIVITY: 10-FORMYLTETRAHYDROFOLATE + N(1)-(5-PHOSPHO-D- CC RIBOSYL)GLYCINAMIDE = TETRAHYDROFOLATE + N(2)-FORMYL-N(1)-(5- CC PHOSPHO-D-RIBOSYL)GLYCINAMIDE. CC -!- CATALYTIC ACTIVITY: ATP + 2-(FORMAMIDO)-N(1)-(5-PHOSPHO-D- CC RIBOSYL)ACETAMIDINE = ADP + PHOSPHATE + 5-AMINO-1-(5-PHOSPHO-D- CC RIBOSYL)IMIDAZOLE. CC -!- PATHWAY: DE NOVO PURINE BIOSYNTHESIS; SECOND STEP. CC -!- PATHWAY: DE NOVO PURINE BIOSYNTHESIS; THIRD STEP. CC -!- PATHWAY: DE NOVO PURINE BIOSYNTHESIS; FIFTH STEP. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P00967-1; Sequence=Displayed; CC Name=Short; CC IsoId=P00967-2; Sequence=VSP_005512, VSP_005513; CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE GARS FAMILY. CC -!- SIMILARITY: TO OTHER AIRS AND GART FROM BACTERIA AND EUKARYOTES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J02527; AAA28563.1; -. DR EMBL; J02527; AAA28562.1; -. DR EMBL; X00041; CAA24923.1; -. DR PIR; S01206; AJFFPM. DR HSSP; P08179; 1GAR. DR FlyBase; FBgn0000053; ade3. DR InterPro; IPR000728; AIR_synth. DR InterPro; IPR002376; formyl_transf. DR InterPro; IPR000115; Gars. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR004733; PurM_cligase. DR InterPro; IPR004607; PurN. DR Pfam; PF00586; AIRS; 2. DR Pfam; PF02769; AIRS_C; 2. DR Pfam; PF00551; formyl_transf; 1. DR Pfam; PF01071; GARS; 1. DR Pfam; PF02842; GARS_B; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR TIGRFAMs; TIGR00877; purD; 1. DR TIGRFAMs; TIGR00878; purM; 2. DR TIGRFAMs; TIGR00639; PurN; 1. DR PROSITE; PS00184; GARS; 1. DR PROSITE; PS00373; GART; 1. KW Multifunctional enzyme; Purine biosynthesis; Ligase; Transferase; KW Alternative splicing. FT DOMAIN 1 433 GARS. FT DOMAIN 434 1152 AIRS. FT DOMAIN 1153 1353 GART. FT ACT_SITE 1299 1299 BY SIMILARITY. FT VARSPLIC 434 434 I -> M (in isoform Short). FT /FTId=VSP_005512. FT VARSPLIC 435 1353 Missing (in isoform Short). FT /FTId=VSP_005513. SQ SEQUENCE 1353 AA; 144448 MW; A68DAB61A02DFD4F CRC64; MSHRVLVIGS GGREHAICWK LSQSPKVAQI YALPGSHGIQ LVEKCRNLDA KTLDPKDFEA IAKWSKENQI ALVVVGPEDP LALGLGDVLQ SAGIPCFGPG KQGAQIEADK KWAKDFMLRH GIPTARYESF TDTEKAKAFI RSAPYPALVV KAAGLAAGKG VVVAANAKEA CQAVDEILGD LKYGQAGATL VVEELLEGEE VSVLAFTDGK SVRAMLPAQD HKRLGNGDTG PNTGGMGAYC PCPLISQPAL ELVQKAVLER AVQGLIKERI NYQGVLYAGL MLTRDGPRVL EFNCRFGDPE TQVILPLLES DLFDVMEACC SGKLDKIPLQ WRNGVSAVGV ILASAGYPET STKGCIISGL PAANTPTQLV FHSGLAVNAQ KEALTNGGRV LIAIALDGSL KEAAAKATKL AGSISFSGSG AQYRTDIAQK AFKIASASTP GLSYKDSGVD IDAGDALVQR IKPLSRGTQR PGVIGGLGGF GGLFRLKELT YKEPVIAEAT QGVGAKIHLA LTHEFYENVG YDLFALAAND VLEVGAEPVA FLDYIACGKL QVPLAAQLVK GMADGCRDAR CALVGGETAE MPSLYAPGQH DMAGYCVGIV EHSRILPRFD LYQPGDLLIG LPSSGLHCAG FNEILTQLAA SKVNLRERSP VDGGDDGLTL AHVLATPTQL YVQQLLPHLQ KGDEIKSVAH VTHGLLNDIL RLLPDGFETT LDFGAVPVPK IFGWLAGKLK LSAQTILERH NCGIGMVLIL PQSSQLWRTS LPGAKVLGVL QRRSKVSGSP VQVRNFVEQL EKVASPFGGL GDRELPEELK KLPSNSDLSA PREECFENAA GRRLTRIPTH YKDPILILGT DGVGTKLKIA QQTNRNTSVG IDLVAMCVND ILCNGAEPIS FSSYYACGHW QEQLAKGVHS GVQEGARQAN SSFIDSHSAA LPLLYEPQVY DLAGFALGIA EHTGILPLLA EIQPGDVLIG LPSSGVHSNG FSLVHAVLKR VGLGLHDKAP FSDKTLGEEL LVPTKIYVKA LSTLLSRGKH GIKALAHITG GGLSENIPRV LRKDLAVRLD ANKFQLPPVF AWLAAAGNIS STELQRTYNC GLGMVLVVAP TEVEDVLKEL RYPQRAAVVG EVVARKDPKK SQVVVQNFEA SLARTQKMLS QRRKRVAVLI SGTGSNLQAL IDATRDSAQG IHADVVLVIS NKPGVLGLQR ATQAGIPSLV ISHKDFASRE VYDAELTRNL KAARVDLICL AGFMRVLSAP FVREWRGRLV NIHPSLLPKY PGLHVQKQAL EAGEKESGCT VHFVDEGVDT GAIIVQAAVP ILPDDDEDSL TQRIHKAEHW AFPRALAMLV NGTALISPEV SSQ // ID PUR4_DROME STANDARD; PRT; 1354 AA. AC P35421; Q9VMI7; DT 01-JUN-1994 (Rel. 29, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) (FGAM DE synthase) (FGAMS) (Formylglycinamide ribotide amidotransferase) DE (FGARAT) (Formylglycinamide ribotide synthetase) (Adenosine-2). GN ADE2 OR CG9127. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94095139; PubMed=8270203; RA Tiong S.Y.K., Nash D.; RT "The adenosine2 gene of Drosophila melanogaster encodes a RT formylglycineamide ribotide amidotransferase."; RL Genome 36:924-934(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: ATP + N(2)-FORMYL-N(1)-(5-PHOSPHO-D- CC RIBOSYL)GLYCINAMIDE + L-GLUTAMINE + H(2)O = ADP + PHOSPHATE + 2- CC (FORMAMIDO)-N(1)-(5-PHOSPHO-D-RIBOSYL)ACETAMIDINE + L-GLUTAMATE. CC -!- PATHWAY: DE NOVO PURINE BIOSYNTHESIS; FOURTH STEP. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE FGAMS CC FAMILY. CC -!- SIMILARITY: CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U00683; AAC46468.1; -. DR EMBL; AE003612; AAF52329.1; -. DR PIR; T13363; T13363. DR FlyBase; FBgn0000052; ade2. DR InterPro; IPR000728; AIR_synth. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 2. KW Purine biosynthesis; Ligase; ATP-binding; Glutamine amidotransferase. FT NP_BIND 327 338 ATP (POTENTIAL). FT ACT_SITE 1180 1180 GATASE (BY SIMILARITY). FT CONFLICT 558 558 I -> Y (IN REF. 1). FT CONFLICT 625 625 S -> F (IN REF. 1). SQ SEQUENCE 1354 AA; 148084 MW; 8AA167C2D2920B2C CRC64; MVILRYYDVQ AHSAAEEESV LRRLREEDGA VVSVRMERCY HLEYSAQAEH SLALDELLVW LVKQPLSKGQ SLSRQPALQS TGSSQLLLEI GPRFNFSTPY STNCVNIFQN LGYSEVRRME TSTRYLVTFG EGSKAPEAAR FVPLLGDRMT QCLYTEENTP KASFDEQLPE RQANWHFVPV LEEGRAALER INQELGLAFN DYDLDYYHDL FAKELGRNPT TVELFDCAQS NSEHSRHWFF RGRMVIDGVE QPKSLIRMIM DTQAHTNPNN TIKFSDNSSA MVGFDHQTIV PSSVVAPGAV RLQSVQSDLI FTAETHNMPT AVAPFSGATT GTGGRLRDVQ GVGRGGVPIA GTAGYCVGAL HIPGYKQPYE PLDFKYPATF APPLQVLIEA SNGASDYGNK FGEPVISGFA LSYGLNSAAD ASQRDEYVKP IMFSGGLGTM PATMREKLPP ARGQLLAKIG GPVYRIGVGG GAASSVEIQG SGDAELDFNA VQRGDAEMEN KLNRVVRACL DLGEQNPILA IHDQGAGGNG NVLKELVEPG FAGAVIFSKE FQLGDPTITA LELWGAEYQE NNAILCNADQ RELLEKICRR ERCPISFVGV VTGDGRVTLL EKPAPKDLEQ ALNASNRSEV SPFDLELKYV LGDMPKRTYD LKREQTPLKE LSLPKGLLLD EALERVLSLV AVGSKRFLTN KVDRCVGGLI AQQQCVGPLQ APLADYALTT VSHFSHSGIA TSIGTQPLKG LLDPAAMARM CVAEALSNLV FVKISELADV KCSGNWMWAA KLPGEGARMF DACKELCQIL EELHIAIDGG KDSLSMAAKV GGETIKSPGT LVISTYAPCP DVRLKVTPDL KGPGAGSKTS LLWINLENSA RLGGSALAQA YAQQGKDTPN LTRSDVLGKA FAVTQSLLGD GLIQAGHDVS DGGLLVCVLE MAIGGLSGLR VDLSEPLAKL KNFDKSVEKL NRPELAVLFA EECGWVVEVL DTDLERVRST YEKAGVPNYY LGVTEGFGLD SRVVLKNGKS ELLDQPLRVL YKKWERTSYE LEKLQANPEC AEAEYNSLEY RQAPQYRGPQ NVQAELTLKR SSAPVRVAVL REEGVNSERE MMACLLRANF EVHDVTMSDL LQGTASVSQY RGLIFPGGFS YADTLGSAKG WAANILHNPR LLPQFEAFKR RQDVFSLGIC NGCQLMTLIG FVGSAKSEVG ADPDVALLHN KSQRFECRWA TVKIPSNRSI MLGSMKDLVL GCWVAHGEGR FAFRDEKLIS HLQSEQLVTL QYVDDVGKPT ELYPLNPNGS PQGIAGLCSS DGRHLALMPH PERCSSMYQW PYVPSSFEVS PTQSESPWQI MFNNAYNWCV KSNQ // ID PYGO_DROME STANDARD; PRT; 815 AA. AC Q9V9W8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pygopus protein (Gammy legs protein). GN PYGO OR GAM OR CG11518. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21952490; PubMed=11955446; RA Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S., RA Murone M., Zuellig S., Basler K.; RT "Wnt/wingless signaling requires BCL9/legless-mediated recruitment of RT pygopus to the nuclear beta-catenin-TCF complex."; RL Cell 109:47-60(2002). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=22010046; PubMed=12015286; RA Parker D.S., Jemison J., Cadigan K.M.; RT "Pygopus, a nuclear PHD-finger protein required for wingless signaling RT in drosophila."; RL Development 129:2565-2576(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN SIGNAL TRANSDUCTION THROUGH THE WNT PATHWAY. CC -!- SUBUNIT: BINDS TO BCL9 VIA THE PHD-TYPE ZINC FINGER MOTIF, AND CC THEREBY BECOMES PART OF THE NUCLEAR ARM/PAN COMPLEX. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: UBIQUITOUS THROUGOUT EMBRYOGENESIS AND LARVAL CC DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: CONTAINS 1 PHD-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF457206; AAL91369.1; -. DR EMBL; AY075095; AAL79357.1; -. DR EMBL; AE003778; AAF57161.1; -. DR EMBL; AY058500; AAL13729.1; -. DR FlyBase; FBgn0043900; pygo. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0030528; F:transcription regulator activity; IPI. DR GO; GO:0030177; P:positive regulation of Wnt receptor signali...; IPI. DR GO; GO:0007367; P:segment polarity determination; IMP. DR GO; GO:0016055; P:Wnt receptor signaling pathway; IGI. DR InterPro; IPR001965; Znf_PHD. DR Pfam; PF00628; PHD; 1. DR SMART; SM00249; PHD; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. KW Nuclear protein; Trans-acting factor; Wnt signaling pathway; Zinc; KW Metal-binding; Zinc-finger; Segmentation polarity protein. FT DOMAIN 39 45 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT ZN_FING 747 805 PHD-TYPE. FT DOMAIN 48 65 ALA-RICH. FT DOMAIN 123 749 ASN/GLY/HIS/MET/PRO-RICH. FT CONFLICT 393 393 S -> P (IN REF. 1). SQ SEQUENCE 815 AA; 80493 MW; 369FD5A5D34BC136 CRC64; MTHNLGMAPY RLPGPAGGLC PPDFKPPPPT DIISAPSNPK KRRKTSSAAN SAAAVAAAAA AAAAANSMQQ QQAPPTPQDL LPPPPMGGFG DTIIASNPFD DSPQVSAMSS SAAAAMAAMN QMGGGPGGGH FGGGGPGGHP HWEDRMGMGG GPPPPPHMHP HMHPHHPGGP MGHPHGPHPH MGGPPPMRGM SPMHPHQMGP GPGVGLPPHM NHGRPGGPGG PGGPVPMGSP MGGIAGMGGM SPMGGMGGPS ISPHHMGMGG LSPMGGGPNG PNPRAMQGSP MGGPGQNSPM NSLPMGSPMG NPIGSPLGPP SGPGPGNPGN TGGPQQQQQQ PPQPPMNNGQ MGPPPLHSPL GNGPTGHGSH MPGGPIPGPG PGPGGLVGPG GISPAHGNNP GGSGNNMLGG NPGGGNSNNN GSNTSNASNN NQNPHLSPAA GRLGVPTSMQ SNGPSVSSVA SSSVPSPATP TLTPTSTATS MSTSVPTSSP APPAMSPHHS LNSAGPSPGM PNSGPSPLQS PAGPNGPNNN NSNNNNGPMM GQMIPNAVPM QHQQHMGGGP PGHGPGPMPG MGMNQMLPPQ QPSHLGPPHP NMMNHPHHPH HHPGGPPPHM MGGPGMHGGP AGMPPHMGGG PNPHMMGGPH GNAGPHMGHG HMGGVPGPGP GPGGMNGPPH PHMSPHHGHP HHHHNPMGGP GPNMFGGGGG GPMGPGGPMG NMGPMGGGPM GGPMGVGPKP MTMGGGKMYP PGQPMVFNPQ NPNAPPIYPC GMCHKEVNDN DEAVFCESGC NFFFHRTCVG LTEAAFQMLN KEVFAEWCCD KCVSSKHIPM VKFKC // ID PYR1_DROME STANDARD; PRT; 2236 AA. AC P05990; Q26376; DT 01-NOV-1988 (Rel. 09, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE CAD protein (Rudimentary protein) [Includes: Glutamine-dependent DE carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate DE carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3)]. GN R. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87226179; PubMed=2884325; RA Freund J.N., Jarry B.P.; RT "The rudimentary gene of Drosophila melanogaster encodes four enzymic RT functions."; RL J. Mol. Biol. 193:1-13(1987). RN [2] RP PARTIAL SEQUENCE FROM N.A. RX MEDLINE=87060929; PubMed=3023623; RA Freund J.N., Vergis W., Schedl P., Jarry B.P.; RT "Molecular organization of the rudimentary gene of Drosophila RT melanogaster."; RL J. Mol. Biol. 189:25-36(1986). RN [3] RP SEQUENCE OF 1-132 FROM N.A. RX MEDLINE=93027163; PubMed=1329025; RA Zerges W., Udvardy A., Schedl P.; RT "Molecular characterization of the 5' end of the rudimentary gene in RT Drosophila and analysis of three P element insertions."; RL Nucleic Acids Res. 20:4639-4647(1992). RN [4] RP REVISIONS TO 2068-2148. RX MEDLINE=95018278; PubMed=7932764; RA Davidson J.N., Kern C.B.; RT "Revision in sequence of CAD aspartate transcarbamylase domain of RT Drosophila."; RL J. Mol. Biol. 243:364-366(1994). CC -!- FUNCTION: THIS PROTEIN IS A "FUSION" PROTEIN ENCODING FOUR CC ENZYMATIC ACTIVITIES OF THE PYRIMIDINE PATHWAY (GATASE, CPSASE, CC ATCASE AND DHOASE). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-GLUTAMINE + CO(2) + H(2)O = 2 ADP + CC PHOSPHATE + L-GLUTAMATE + CARBAMOYL PHOSPHATE. CC -!- CATALYTIC ACTIVITY: CARBAMOYL PHOSPHATE + L-ASPARTATE = PHOSPHATE CC + N-CARBAMOYL-L-ASPARTATE. CC -!- CATALYTIC ACTIVITY: (S)-DIHYDROOROTATE + H(2)O = N-CARBAMOYL-L- CC ASPARTATE. CC -!- COFACTOR: DIHYDROOROTASE: BINDS 1 ZINC ION PER SUBUNIT CC (POTENTIAL). CC -!- PATHWAY: PYRIMIDINE BIOSYNTHESIS; FIRST STEP. CC -!- PATHWAY: PYRIMIDINE BIOSYNTHESIS; SECOND STEP. CC -!- PATHWAY: PYRIMIDINE BIOSYNTHESIS; THIRD STEP. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: GATASE (GLUTAMINE AMIDOTRANSFERASE) AND CPSASE CC (CARBAMOYL PHOSPHATE SYNTHASE) FORM TOGETHER THE CC GLUTAMINE-DEPENDENT CPSASE (GD-CPSASE) (EC 6.3.5.5). CC -!- SIMILARITY: THE CPSASE DOMAIN IS SIMILAR TO OTHER CPASES. CC -!- SIMILARITY: IN THE CENTRAL SECTION; BELONGS TO THE DHOASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04813; CAA28502.1; -. DR EMBL; X03875; CAA27509.1; -. DR EMBL; X03876; CAA27510.1; ALT_SEQ. DR EMBL; X03877; CAA27511.1; ALT_SEQ. DR EMBL; X03878; CAA27512.1; -. DR EMBL; X03879; CAA27513.1; -. DR EMBL; M37783; AAA28873.1; -. DR EMBL; S74010; AAB32204.1; -. DR PIR; A29106; QZFF. DR HSSP; P00479; 3CSU. DR FlyBase; FBgn0003189; r. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR006130; Asp/Orn_COtranf. DR InterPro; IPR002082; Asp_carbmltransf. DR InterPro; IPR006275; CarA_L_glu. DR InterPro; IPR001317; CP_synthGATase. DR InterPro; IPR002474; CP_synthsmall. DR InterPro; IPR005483; CPase_L. DR InterPro; IPR005479; CPase_L_D2. DR InterPro; IPR005480; CPase_L_D3. DR InterPro; IPR005481; CPase_L_N. DR InterPro; IPR000991; GATase_1. DR InterPro; IPR004362; MGS_like. DR InterPro; IPR006131; OTCace_O. DR InterPro; IPR006132; OTCace_P. DR InterPro; IPR002195; Pept_M38_nph. DR Pfam; PF01979; Amidohydro_1; 1. DR Pfam; PF00289; CPSase_L_chain; 2. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF00988; CPSase_sm_chain; 1. DR Pfam; PF00117; GATase; 1. DR Pfam; PF02142; MGS; 1. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00098; CPSASE. DR PRINTS; PR00099; CPSGATASE. DR PRINTS; PR00096; GATASE. DR TIGRFAMs; TIGR00670; asp_carb_tr; 1. DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. DR PROSITE; PS00442; GATASE_TYPE_I; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; FALSE_NEG. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. KW Pyrimidine biosynthesis; Ligase; Transferase; Hydrolase; Zinc; KW Multifunctional enzyme. FT DOMAIN 1 381 GATASE (GLUTAMINE AMIDOTRANSFERASE). FT DOMAIN 382 420 LINKER. FT DOMAIN 421 1473 CPSASE (CARBAMOYL-PHOSPHATE SYNTHASE). FT DOMAIN 1474 1487 LINKER. FT DOMAIN 1488 1802 DHOASE (DIHYDROOROTASE). FT DOMAIN 1803 1917 LINKER. FT DOMAIN 1918 2236 ATCASE (ASPARTATE TRANSCARBAMYLASE). FT ACT_SITE 274 274 GATASE (BY SIMILARITY). FT METAL 1489 1489 ZINC (POTENTIAL). FT METAL 1491 1491 ZINC (POTENTIAL). FT CONFLICT 2075 2104 VGDLKNGRTVHSLARLLTLYNVNLQYVAPN -> FT WRLEERTDRALAGPPADPVQCEPAVMWRRD (IN REF. FT 1). FT CONFLICT 2131 2145 NVLPDTDVLYMTRIQ -> ECAARHGCALHDSHS (IN FT REF. 1). SQ SEQUENCE 2236 AA; 249238 MW; 85A3D7CBA82E36A1 CRC64; MASTDCYLAL EDGTVLPGYS FGYVPSENES KVGVGGEVVF QTGMVGYTEA LTDRSYSAQI LVLTYPLIGN YGVPAPDEDE HGLPLHFEWT EGRRPGQPPW WWARLAKRQL FNWRKWKTLP ELAEATTRCP EFEFSIDTRA LTKKLREQGS MLGKIVYEKP PVEGAMPKSS FVDPNVQDLA KECSVKERQV YGNPNGKGPR IAILDCGLKL NQLRCLLQRG ASVTFVPWSA RLEDEQFDAL FLSNGPGNPE SCDQIVQQVR KVIEEGQKPV FGICLGHQLL AKAIGCSTYK MKIGNRGHNL PCLHRATGRC LMTSQNHGYA VDLEQLPDGW SELFVNANDG DQRGHCPCQQ ALLFGSVPSG ASCWTAGHGV PVRCLYGEHS TEGFDHSAAD RAATASDYAC HRFGSSDAAQ SPNPGIRGLS IGQAGEFDYS GSQAINGMRE SNIQTVLINP NIATVQTSKG MADKCYFLPL TPHYVEQVIK SERPNGVLLT LAARPSQLWR ATGASRSFLQ IQCPHFGHTH PVDHRDGGSQ ALCRAGNEIG EQVAPSEAVY SVAQALDAAS RLGYPVMARA AFSLGGLGSG FANNEEELQT PGPTALAHSS QLIVDKSLKG WKEVEYEVVR AMPTTTRITV CNMENFDPLG IHTGESIVVA PSQTLSDREI KVLRSTAWKV IRHFGVVGEC NIRYASVPRL QYYIIEVNER LSRTSALASK APGYPLAYVA AKVGLGLPLP DIKNSVTGMR RPAFEPSLDY CVVKMPRWDL AKFVRVSKHI GSSMKSVGEV MAIGRQLRGS VPKSPAHGGQ RMCLALNPDV VPLNKEQLAE QLSEPTDRRP FVIAAALQLG MSLRELHQLT NIDYWFLEKS ERIILLQSLL TRNGSRTDAA LLLKAKRFGF SDKQIAKYIK STELAVRHQR QEFGIRPHVK QIDTVAGEWP PDQLSVTTHI TEASRRSPVP RRTHYCGGLG VYRIGSSVEF IGSVGCLREL RKLQRPTIMI NYNPETVSTD YDMCDRLYFE EISFEEWSWT STRWRIARAS FCPMGGQLPN NIAMDLHRQQ EVLGTSPESI DCAENRFKFS RMLDQEGYLA ATLGKELTNL QSAIEFCEEV GYPCLVRPSY VLSGAAMNVA YSNQDLETYL NAASEVSREH PVVISKFLTE AKEIDVDAVA SMDASCARLF PEHVENAGVH SGDATLVTPP QDLNAETLEA IKRITCDLAS VLDVTGPFNM QLIAKNNELK VIECNVRVSR SFPFVSKTLD HDFVATATRA IVGLDVEPLD VLHASARWAS SAPVQFLAAP GAECTAGRRA WTSTGEVACF GDNRYEAYLK AMMSTGFQIP KNAVLLSIGS FKHKMELLPS YGIWPRWVTS YSFHGHCDFY ANGVNVESVQ WTFDKTTPDD INGELRHLAE FLANKQFDLV INLPMSGGVP RRVSSFMTHG YRTRRLAVEY SIPLVTDVKC TKLLVESMRM NGGKPPMKTH TDCMTSRRIV KLPGFIDVHV HLRSRSHAQG GLCQWNSSRS GWRLTLVCAM PNTNPSIVDR ETFTQFQELA KAGARCDYAL YVGASDDNWA QVNELASHAC GLKMYLNDTF GTLKLSDMTS WQRHLSHWPK RSPIVCHAER QSTAAVIMLA HLLDRSVHIC HVARKEEIQL IRSAKEKGVK VNLRVCPHHL FLSTKDVDGL GHGMSEVRPL LCSPEDQEAL WENIDYIDVF ATDHAPHTLA EKRSERPPPG FPGVETILPL LLQAVHEGRL TMEDIKRKFH RNPKIIFNLP DQAQTYVEVD LDEEWTITGN EMKSKSGWTP FEGTKVKGLV YRSVLRGELA FRRWPILLER LRGINGGAPN KDVHWRRRHH RICCPATTMP MTPLPASSPP KDPGGWPYTE YRPKVPLWDG ANFRAPSSPS PRIRLDSASN TTLREYLQRT TNSNPVAHSL MGKHILAVDM FNKDHLNDIF NLAQLLKLRG TKDRPVALLP GKIMASVFYE VSTRTPCSFA AAMLRLGGRV ISMDNITSSV KKGETWRTAS RLCPAMPTSW LLRHPSPGAV ARTTFSQSRL SMPACRREHS HQALLDIFTD PRVGGTVNGL TITMVGDLKN GRTVHSLARL LTLYNVNLQY VAPNSLQMPD EVVQFVHQRG VKQLFARDLK NVLPDTDVLY MTRIQRERFD NVEDYEKCCG HLVLTPEHMM RAKKRSIVLH PLPRLNEISR EIDLDPRAAY FRQAEYGMYI RMALLAMVVG GRNRRSRGFT MENHNL // ID PYR5_DROME STANDARD; PRT; 493 AA. AC Q01637; Q24221; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Uridine 5'-monophosphate synthase (UMP synthase) (Rudimentary-like DE protein) [Includes: Orotate phosphoribosyltransferase (EC 2.4.2.10) DE (OPRtase); Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) DE (OMPdecase)]. GN R-L. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Eisenberg M.T., Kirkpatrick R., Rawls J.; RL Submitted (XXX-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 1-78 FROM N.A. RX MEDLINE=91042409; PubMed=2122228; RA Eisenberg M.T., Gathy K., Vincent T., Rawls J.; RT "Molecular cloning of the UMP synthase gene rudimentary-like from RT Drosophila melanogaster."; RL Mol. Gen. Genet. 222:1-8(1990). CC -!- CATALYTIC ACTIVITY: OROTIDINE 5'-PHOSPHATE + DIPHOSPHATE = OROTATE CC + 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE. CC -!- CATALYTIC ACTIVITY: OROTIDINE 5'-PHOSPHATE = UMP + CO(2). CC -!- PATHWAY: PYRIMIDINE BIOSYNTHESIS; FIFTH AND SIXTH (LAST) STEPS. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE CC PURINE/PYRIMIDINE PHOSPHORIBOSYLTRANSFERASE FAMILY. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE OMP CC DECARBOXYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L00968; AAA29012.1; -. DR EMBL; X54230; CAA38138.1; -. DR PIR; JU0141; JU0141. DR HSSP; P03962; 1DQW. DR FlyBase; FBgn0003257; r-l. DR InterPro; IPR001754; OMPdecase. DR InterPro; IPR004467; Or_phspho_trans. DR InterPro; IPR002375; Pr/py_rp_transf. DR InterPro; IPR000836; PRTransferase. DR Pfam; PF00215; OMPdecase; 1. DR Pfam; PF00156; Pribosyltran; 1. DR TIGRFAMs; TIGR00336; pyrE; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. DR PROSITE; PS00156; OMPDECASE; 1. KW Pyrimidine biosynthesis; Multifunctional enzyme; Transferase; KW Glycosyltransferase; Lyase; Decarboxylase. FT DOMAIN 1 207 OPRTASE. FT DOMAIN 208 233 DOMAIN LINKER. FT DOMAIN 234 493 OMPDECASE. FT ACT_SITE 320 320 BY SIMILARITY. FT CONFLICT 47 51 LGLPQ -> YPDVM (IN REF. 2). SQ SEQUENCE 493 AA; 53327 MW; 56479CDAB1F6A308 CRC64; MVAQNSDKMR ALALKLFEIN AFKFGDFKMK VGINSPVYFD LRVIVSLGLP QQTVSDLLVE HIKDKQLSAK HVCGVPYTAL PRATIVSVQQ GTPMLVRRKE AKAYGTKKLV EGIFNAGDTC LIVEDVVTSG SSILDTVRDL QGEGIVVTDA VVVVDREQGG VANIAKHGVR MHSLFTLSFL LNTLHEAGRI EKSTVEAVAK YIAAVQINSD GTFVGGDKVT FPAANDLQRT KLTYESRANL AKSAVAKRLF NLIASKQTNL CLAADLTHAD EILDVADKCG PYICLLKTHV DIVEDFSDKF IADLQALAQR HNFLLMEDRK FADIGNTVSL QYGKGIYKIS SWADLVTAHT LPGRSILQGL KAGLGEGGAG KERGVFLLAE MSASGNLIDA KYKENSNKIA TEGADVDFVA GVVCQSSDAF AFPGLLQLTP GVKIDEGVDQ LGQQYQSPEH VVKERGADIG VVGRGILKAS SPKQAAQTYR DRLWAAYQDR VAK // ID PYRD_DROME STANDARD; PRT; 389 AA. AC P32748; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dihydroorotate dehydrogenase, mitochondrial precursor (EC 1.3.3.1) DE (Dihydroorotate oxidase) (DHOdehase). GN DHOD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93185923; PubMed=8444342; RA Rawls J., Kirkpatrick R., Yang J., Lacy L.; RT "The dhod gene and deduced structure of mitochondrial dihydroorotate RT dehydrogenase in Drosophila melanogaster."; RL Gene 124:191-197(1993). RN [2] RP PRELIMINARY SEQUENCE OF 331-389 FROM N.A. RX MEDLINE=90158502; PubMed=2482933; RA Jones W.K., Kirkpatrick R., Rawls J.M.; RT "Molecular cloning and transcript mapping of the dihydroorotate RT dehydrogenase dhod locus of Drosophila melanogaster."; RL Mol. Gen. Genet. 219:397-403(1989). CC -!- CATALYTIC ACTIVITY: (S)-DIHYDROOROTATE + O(2) = OROTATE + CC H(2)O(2). CC -!- COFACTOR: FAD. CC -!- PATHWAY: PYRIMIDINE BIOSYNTHESIS; FOURTH STEP. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE DIHYDROOROTATE DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L00964; AAB59185.1; -. DR EMBL; X17297; CAA35184.1; ALT_SEQ. DR FlyBase; FBgn0000447; Dhod. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IDA. DR InterPro; IPR001295; DHO_dh. DR InterPro; IPR005719; DHO_dh2. DR InterPro; IPR003009; FMN_enzyme. DR Pfam; PF01180; DHOdehase; 1. DR TIGRFAMs; TIGR01036; pyrD_sub2; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. KW Pyrimidine biosynthesis; Oxidoreductase; Flavoprotein; FAD; KW Transit peptide; Mitochondrion. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 389 DIHYDROOROTATE DEHYDROGENASE. FT NP_BIND 333 341 FAD (NAD PART) (POTENTIAL). SQ SEQUENCE 389 AA; 42376 MW; 92C8188BB327CC28 CRC64; MDQDHLKNAK NATRRVGRLR SLGIVTVGGA ALVAGITAYK NQDQLFRTFV MPAVRLLPAE ASHQLAVLAC KYRLCPVSQY HDDQNLHTSF FGRMLSNPIG IAAGFDKNAE AVDGLQDLGF GFIEVGTVTP AAQEGNPKPR VFRLTEDKAI INRYGFNSDG HQAVLQRLRL LRKKENFNGV VGVNLGRNKT TMSPIADYVQ GVRVFGPVAD YLVINVSSPN TKGLRDMQSK EKLRELLEQV NDTKSSLDKN KNVPILLKLS PDLSLDDMKD IVWVIKRKKS RVDGLIVSNT TVSRENIEKN KLAEETGGLS GPPLKARSTE MIAQMYQLTD GKIPIIGVGG VASGYDAYEK IEAGASYVQI YTALVYEGPA LVEDIKAGAV GADHTAGSH // ID QUAI_DROME STANDARD; PRT; 887 AA. AC Q23989; Q9VJC9; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Villin-like protein quail. GN QUA OR CG6433. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94320140; PubMed=8044841; RA Mahajan-Miklos S., Cooley L.; RT "The villin-like protein encoded by the Drosophila quail gene is RT required for actin bundle assembly during oogenesis."; RL Cell 78:291-301(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR THE FORMATION OF CYTOPLASMIC ACTIN FILAMENT CC BUNDLES IN NURSE CELLS, POSSIBLY BY REGULATING BOTH THE CC POLYMERIZATION AND ORGANIZATION OF ACTIN FILAMENTS. MUTATIONS IN CC QUAIL RESULT IN FEMALE STERILITY DUE TO THE DISRUPTION OF CC CYTOPLASMIC TRANSPORT FROM THE NURSE CELLS INTO THE OOCYTE LATE IN CC OOGENESIS. CC -!- TISSUE SPECIFICITY: GERMLINE SPECIFIC IN ADULT FLIES. CC -!- SIMILARITY: BELONGS TO THE VILLIN/GELSOLIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 GELSOLIN-LIKE REPEAT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U10070; AAC13765.1; -. DR EMBL; AE003655; AAF53623.1; -. DR PIR; A54832; A54832. DR HSSP; P02640; 1VII. DR FlyBase; FBgn0003187; qua. DR GO; GO:0003779; F:actin binding; IDA. DR GO; GO:0007300; P:nurse cell/oocyte transport (sensu Insecta); IMP. DR InterPro; IPR007122; Gelsolin. DR InterPro; IPR007123; Gelsoln. DR InterPro; IPR003128; VHP. DR Pfam; PF00626; Gelsolin; 1. DR Pfam; PF02209; VHP; 1. DR PRINTS; PR00597; GELSOLIN. DR SMART; SM00262; GEL; 6. DR SMART; SM00153; VHP; 1. KW Actin-binding; Actin capping. FT REPEAT 171 212 GELSOLIN-LIKE. FT DOMAIN 342 345 POLY-LYS. FT DOMAIN 639 648 POLY-SER. SQ SEQUENCE 887 AA; 100947 MW; 6B7449ACBC4E9EA7 CRC64; MPPFNFIKQE IRPNTIPDLK VDATFRKVAK HAITFAIWKI DEDRLEAVQR SHYGTFYDSC AYIIYAASLS GHYANHETIT REQKPNVSLE RYIHYWLGKN VSEQNRSNVV HKIQELDSYL GNISSIYRET QNLESARFLS YFKKGYDVRS GALISAPQRP RLFQLYARKW LRSIEVATID WSHFNSDYVM VLQTDNLTYV WIGRSSSGIE RRSALDWVQK HCSGSPITIV DDGYEQAMSQ EHKELWNTML PLKKRMVCQA SQLVSEYADY NSNKFRIYKC NQRGRLHLDQ LDVGMPAKDD LSDAHGVYLL DNYGQSIWLW VGGQAPQADA LSAMGNGRAF VKKKKYPDNT LVVRVLEGHE PVEFKRLFAN WLNVWQENTR GHKPVSTKFG KLDAHSLCER PKMAADTQLV DDGRGERVIY RVFGDQVQEV PISKTVVFTT NASFVVKYSV QCATVVPADL ASVGIKTIIY QWNGSEASVE SISRADKFAK ASFDGLKEPG MFVQLYEFDE PPHFLQIFEG KLIIRRGQRT EMPYNGNSNA LLDTFLLKVY GDASYNAKAV EETHLSSISS KDCYVIKTNH VWVWCGQSST GDAREMAKAV GALMGENSLV LEGKESKEFW QSVAMYFNQT LVINGNGNSC SSSTSSSSGA GSMCNGSSNG GNISPTLSNN CYLNTSVPSK PRPPVQLFLV WWQQSSLRYE EILGFDQQDL SSDCTYILDT GSLTYVWLGS QAPNQERYTA IAQSYVQNAP FGRRSATALA VVRQFQEPNV FKGFFESWQN DYGKNFHSYE KMRKDLGNKV TSNCCFASEG SALILNNRQK DFDGHKKYPL TVLIQEMDML PPDINPLKRE VHLTHDDFVS VFNMSFYEFD ELPKWKKMEL KKQFKLF // ID R27A_DROME STANDARD; PRT; 80 AA. AC P15357; Q9VKW6; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S27a. GN RPS27A OR UBI-M OR UB3-D OR UBI-F80 OR CG5271. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89096844; PubMed=2463465; RA Lee H., Simon J.A., Lis J.T.; RT "Structure and expression of ubiquitin genes of Drosophila RT melanogaster."; RL Mol. Cell. Biol. 8:4727-4735(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- MISCELLANEOUS: THIS RIBOSOMAL PROTEIN IS SYNTHESIZED AS A CC C-TERMINAL EXTENSION PROTEIN (CEP) OF UBIQUITIN. CC -!- SIMILARITY: BELONGS TO THE S27AE FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22536; AAA28998.1; ALT_INIT. DR EMBL; AE003628; AAF52941.1; ALT_INIT. DR FlyBase; FBgn0003942; RpS27A. DR InterPro; IPR002906; Ribosomal_S27. DR Pfam; PF01599; Ribosomal_S27; 1. KW Ribosomal protein; Zinc-finger; Metal-binding. FT DOMAIN 2 31 LYS-RICH (HIGHLY BASIC). FT ZN_FING 45 68 C4-TYPE. SQ SEQUENCE 80 AA; 9393 MW; 7CF19F53FDB8B619 CRC64; AKKRKKKNYS TPKKIKHKRK KVKLAVLKYY KVDENGKIHR LRRECPGENC GAGVFMAAHE DRHYCGKCNL TFVFSKPEEK // ID RA51_DROME STANDARD; PRT; 336 AA. AC Q27297; Q9VAA8; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA repair protein Rad51 homolog (RecA protein homolog). GN RAD51 OR DMR OR CG7948. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95161094; PubMed=7857671; RA Akaboshi E., Inoue Y., Ryo H.; RT "Cloning of the cDNA and genomic DNA that correspond to the recA-like RT gene of Drosophila melanogaster."; RL Jpn. J. Genet. 69:663-670(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96207535; PubMed=8625736; RA McKee B.D., Ren X.J., Hong C.S.; RT "A recA-like gene in Drosophila melanogaster that is expressed at RT high levels in female but not male meiotic tissues."; RL Chromosoma 104:479-488(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS TO SINGLE AND DOUBLE STRANDED DNA AND EXHIBITS CC DNA-DEPENDENT ATPASE ACTIVITY. UNDERWINDS DUPLEX DNA (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE RECA FAMILY. RAD51 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D37788; BAA07039.1; -. DR EMBL; D17726; BAA04580.1; -. DR EMBL; L41342; AAA64873.1; -. DR EMBL; AE003772; AAF57005.1; -. DR HSSP; Q06609; 1B22. DR FlyBase; FBgn0011700; Rad51. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR000445; HhH. DR InterPro; IPR003583; HHH_1. DR InterPro; IPR001553; RecA. DR Pfam; PF00633; HHH; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00278; HhH1; 1. DR PROSITE; PS50162; RECA_2; 1. DR PROSITE; PS50163; RECA_3; 1. KW DNA-binding; ATP-binding; Nuclear protein. FT NP_BIND 124 131 ATP (POTENTIAL). SQ SEQUENCE 336 AA; 36647 MW; F9E9B21405B15DB0 CRC64; MEKLTNVQAQ QEEEEEEGPL SVTKLIGGSI TAKDIKLLQQ ASLHTVESVA NATKKQLMAI PGLGGGKVEQ IITEANKLVP LGFLSARTFY QMRADVVQLS TGSKELDKLL GGGIETGSIT EIFGEFRCGK TQLCHTLAVT CQLPISQKGG EGKCMYIDTE NTFRPERLAA IAQRYKLNES EVLDNVAFTR AHNSDQQTKL IQMAAGMLFE SRYALLIVDS AMALYRSDYI GRGELAARQN HLGLFLRMLQ RLADEFGVAV VITNQVTASL DGAPGMFDAK KPIGGHIMAH SSTTRLYLRK GKGETRICKI YDSPCLPESE AMFAILPDGI GDARES // ID RAB3_DROME STANDARD; PRT; 220 AA. AC P25228; Q9V5N9; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-related protein Rab-3. GN RAB3 OR CG7576. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=91299329; PubMed=1648935; RA Johnston P.A., Archer B.T. III, Robinson K., Mignery G.A., Jahn R., RA Suedhof T.C.; RT "Rab3A attachment to the synaptic vesicle membrane mediated by a RT conserved polyisoprenylated carboxy-terminal sequence."; RL Neuron 7:101-109(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROTEIN TRANSPORT. PROBABLY INVOLVED IN VESICULAR CC TRAFFIC (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: SYNAPTIC VESICLES. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RAB FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M64621; AAA28843.1; -. DR EMBL; AE003828; AAF58762.1; -. DR EMBL; AY060449; AAL25488.1; -. DR PIR; JH0425; JH0425. DR HSSP; P05713; 3RAB. DR FlyBase; FBgn0005586; Rab3. DR GO; GO:0008021; C:synaptic vesicle; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016083; P:synaptic vesicle fusion; NAS. DR InterPro; IPR003579; GTPase_Rab. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Lipoprotein; Prenylation; Protein transport. FT NP_BIND 28 35 GTP (BY SIMILARITY). FT NP_BIND 76 80 GTP (BY SIMILARITY). FT NP_BIND 134 137 GTP (BY SIMILARITY). FT DOMAIN 50 58 EFFECTOR REGION (BY SIMILARITY). FT LIPID 218 218 S-geranylgeranyl cysteine. FT LIPID 220 220 S-geranylgeranyl cysteine. SQ SEQUENCE 220 AA; 24862 MW; B324A77DBEF847A1 CRC64; MASGGDPKWQ KDAADQNFDY MFKLLIIGNS SVGKTSFLFR YADDSFTSAF VSTVGIDFKV KTVFRHDKRV KLQIWDTAGQ ERYRTITTAY YRGAMGFILM YDVTNEDSFN SVQDWVTQIK TYSWDNAQVI LVGNKCDMED QRVISFERGR QLADQLGVEF FETSAKENVN VKAVFERLVD IICDKMSESL DADPTLVGGG QKGQRLTDQP QGTPNANCNC // ID RAC1_DROME STANDARD; PRT; 192 AA. AC P40792; Q9W0H7; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-related protein Rac1. GN RAC1 OR RACA OR CG2248. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95047333; PubMed=7958857; RA Luo L., Liao Y.J., Jan L.Y., Jan Y.; RT "Distinct morphogenetic functions of similar small GTPases: RT Drosophila Drac1 is involved in axonal outgrowth and myoblast RT fusion."; RL Genes Dev. 8:1787-1802(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95137009; PubMed=7835340; RA Hariharan I.K., Hu K.-Q., Asha H., Quintanilla A., Ezzell R.M., RA Settleman J.; RT "Characterization of rho GTPase family homologues in Drosophila RT melanogaster: overexpressing Rho1 in retinal cells causes a late RT developmental defect."; RL EMBO J. 14:292-302(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95237020; PubMed=7720592; RA Harden N., Loh H., Chia W., Lim L.; RT "A dominant inhibitory version of the small GTP-binding protein Rac RT disrupts cytoskeletal structures and inhibits developmental cell RT shape changes in Drosophila."; RL Development 121:903-914(1995). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN AXON OUTGROWTH AND MYOBLAST FUSION. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RHO FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11823; AAA62870.1; -. DR EMBL; L38309; AAA67040.1; -. DR EMBL; Z35642; CAA84709.1; -. DR EMBL; AE003471; AAF47469.1; -. DR EMBL; AY060408; AAL25447.1; -. DR PIR; I45715; I45715. DR PIR; S51718; S51718. DR PIR; S54295; S54295. DR HSSP; P15154; 1MH1. DR FlyBase; FBgn0010333; Rac1. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0003924; F:GTPase activity; NAS. DR GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; IMP. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0008283; P:cell proliferation; IGI. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR GO; GO:0042067; P:establishment of ommatidial polarity (sensu...; NAS. DR GO; GO:0007164; P:establishment of tissue polarity; NAS. DR GO; GO:0007017; P:microtubule-based process; NAS. DR GO; GO:0042052; P:rhabdomere development; IGI. DR InterPro; IPR003578; GTPase_Rho. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00174; RHO; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein. FT NP_BIND 10 17 GTP (BY SIMILARITY). FT NP_BIND 57 61 GTP (BY SIMILARITY). FT NP_BIND 115 118 GTP (BY SIMILARITY). FT DOMAIN 32 40 EFFECTOR REGION (POTENTIAL). FT LIPID 189 189 S-geranylgeranyl cysteine FT (By similarity). FT CONFLICT 135 135 A -> V (IN REF. 1). FT CONFLICT 143 146 LAMA -> SGHG (IN REF. 2). SQ SEQUENCE 192 AA; 21354 MW; F910B54BDBD8AFA3 CRC64; MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDAKP INLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVNPASF ENVRAKWYPE VRHHCPSTPI ILVGTKLDLR DDKNTIEKLR DKKLAPITYP QGLAMAKEIG AVKYLECSAL TQKGLKTVFD EAIRSVLCPV LQPKSKRKCA LL // ID RAC2_DROME STANDARD; PRT; 192 AA. AC P48554; Q9VS69; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-related protein Rac2. GN RAC2 OR RACB OR CG8556. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95137009; PubMed=7835340; RA Hariharan I.K., Hu K.-Q., Asha H., Quintanilla A., Ezzell R.M., RA Settleman J.; RT "Characterization of rho GTPase family homologues in Drosophila RT melanogaster: overexpressing Rho1 in retinal cells causes a late RT developmental defect."; RL EMBO J. 14:292-302(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95237020; PubMed=7720592; RA Harden N., Loh H., Chia W., Lim L.; RT "A dominant inhibitory version of the small GTP-binding protein Rac RT disrupts cytoskeletal structures and inhibits developmental cell RT shape changes in Drosophila."; RL Development 121:903-914(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L38310; AAA67041.1; -. DR EMBL; Z35643; CAA84710.1; -. DR EMBL; AE003559; AAF50559.1; -. DR PIR; S54296; S54296. DR HSSP; P15153; 1DS6. DR FlyBase; FBgn0014011; Rac2. DR InterPro; IPR003578; GTPase_Rho. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00174; RHO; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein. FT NP_BIND 10 17 GTP (BY SIMILARITY). FT NP_BIND 57 61 GTP (BY SIMILARITY). FT NP_BIND 115 118 GTP (BY SIMILARITY). FT DOMAIN 32 40 EFFECTOR REGION (POTENTIAL). FT LIPID 189 189 S-geranylgeranyl cysteine FT (By similarity). SQ SEQUENCE 192 AA; 21359 MW; 06AE11CC18019982 CRC64; MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDAKP INLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVNPASF ENVRAKWFPE VRHHCPSVPI ILVGTKLDLR DDKQTIEKLK DKKLTPITYP QGLAMAKEIA AVKYLECSAL TQKGLKTVFD EAIRSVLCPV VRGPKRHKCA LL // ID RALA_DROME STANDARD; PRT; 201 AA. AC P48555; Q9W4Q6; DT 01-FEB-1996 (Rel. 33, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-related protein Ral-a. GN RALA OR CG2849. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye imaginal disk; RA Winge P., Fleming J.T., Settleman J., Hariharan I.K.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RAS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U23800; AAC34902.1; -. DR EMBL; AE003428; AAF45889.1; -. DR HSSP; P01112; 1PLK. DR FlyBase; FBgn0015286; Rala. DR GO; GO:0007391; P:dorsal closure; NAS. DR InterPro; IPR003577; GTPase_Ras. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00173; RAS; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein. FT NP_BIND 18 25 GTP (BY SIMILARITY). FT NP_BIND 65 69 GTP (BY SIMILARITY). FT NP_BIND 124 127 GTP (BY SIMILARITY). FT DOMAIN 40 48 EFFECTOR REGION (BY SIMILARITY). FT LIPID 198 198 S-geranylgeranyl cysteine. SQ SEQUENCE 201 AA; 22938 MW; 37F27FD84A813838 CRC64; MSKKPTAGPA LHKVIMVGSG GVGKSALTLQ FMYDEFVEDY EPTKADSYRK KVVLDGEEVQ IDILDTAGQE DYAAIRDNYF RSGEGFLCVF SITDDESFQA TQEFREQILR VKNDESIPFL LVGNKCDLND KRKVPLSECQ LRAQQWAVPY VETSAKTREN VDKVFFDLMR EIRSRKTEDS KATSGRAKDR CKKRRLKCTL L // ID RAS1_DROME STANDARD; PRT; 189 AA. AC P08646; Q9V448; DT 13-AUG-1987 (Rel. 05, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-like protein 1. GN RAS85D OR RAS1 OR CG9375. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87248071; PubMed=3110012; RA Brock H.W.; RT "Sequence and genomic structure of ras homologues Dmras85D and RT Dmras64B of Drosophila melanogaster."; RL Gene 51:129-137(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=84259319; PubMed=6430564; RA Neuman-Silberberg F.S., Schejter E., Hoffmann F.M., Shilo B.-Z.; RT "The Drosophila ras oncogenes: structure and nucleotide sequence."; RL Cell 37:1027-1033(1984). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=W13; RX MEDLINE=20020328; PubMed=10552039; RA Gasperini R., Gibson G.; RT "Absence of protein polymorphism in the Ras genes of Drosophila."; RL J. Mol. Evol. 49:583-590(1999). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 1-46 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95178745; PubMed=7873789; RA Ezer S.T., Sahar D., Salzberg A., Lev Z.; RT "Differential expression during embryogenesis of three genes RT clustered in the Ras1 region of Drosophila melanogaster."; RL Dev. Dyn. 201:179-190(1994). CC -!- FUNCTION: MAY MEDIATE A SIGNAL THAT DETERMINES THE FATE OF CC PHOTORECEPTOR CELLS IN THE DEVELOPING COMPOUND EYE. RAS PROTEINS CC BIND GDP/GTP AND POSSESS INTRINSIC GTPASE ACTIVITY. CC -!- ENZYME REGULATION: ALTERNATE BETWEEN AN INACTIVE FORM BOUND TO GDP CC AND AN ACTIVE FORM BOUND TO GTP. ACTIVATED BY A GUANINE CC NUCLEOTIDE-EXCHANGE FACTOR (GEF) AND INACTIVATED BY A GTPASE- CC ACTIVATING PROTEIN (GAP). CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RAS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16429; AAA28847.1; -. DR EMBL; M16123; AAA28847.1; JOINED. DR EMBL; M16428; AAA28847.1; JOINED. DR EMBL; K01960; AAA28846.1; -. DR EMBL; X73219; CAA51689.1; -. DR EMBL; AE003683; AAF54388.1; -. DR EMBL; AF186648; AAF15514.1; -. DR PIR; A29048; TVFF85. DR PIR; S35097; S35097. DR HSSP; P01112; 1PLL. DR FlyBase; FBgn0003205; Ras85D. DR GO; GO:0006916; P:anti-apoptosis; NAS. DR GO; GO:0030381; P:eggshell pattern formation (sensu Insecta); IMP. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR InterPro; IPR003577; GTPase_Ras. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00173; RAS; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein. FT NP_BIND 10 17 GTP (BY SIMILARITY). FT NP_BIND 57 61 GTP (BY SIMILARITY). FT NP_BIND 116 119 GTP (BY SIMILARITY). FT DOMAIN 32 40 EFFECTOR REGION (BY SIMILARITY). FT LIPID 186 186 S-geranylgeranyl cysteine FT (By similarity). FT CONFLICT 11 11 A -> P (IN REF. 2). FT CONFLICT 44 45 VV -> RF (IN REF. 2). FT CONFLICT 84 84 V -> I (IN REF. 2). FT CONFLICT 102 102 R -> H (IN REF. 2). FT CONFLICT 114 114 V -> A (IN REF. 2). FT CONFLICT 182 182 R -> C (IN REF. 2). SQ SEQUENCE 189 AA; 21594 MW; 14236DCD65EACCD2 CRC64; MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG QEEYSAMRDQ YMRTGEGFLL VFAVNSAKSF EDIGTYREQI KRVKDAEEVP MVLVGNKCDL ASWNVNNEQA REVAKQYGIP YIETSAKTRM GVDDAFYTLV REIRKDKDNK GRRGRKMNKP NRRFKCKML // ID RAS2_DROME STANDARD; PRT; 192 AA. AC P04388; Q9VZH7; DT 20-MAR-1987 (Rel. 04, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-like protein 2. GN RAS64B OR RAS2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85187987; PubMed=3921827; RA Mozer B., Marlor R., Parkhusrt S., Corces V.G.; RT "Characterization and developmental expression of a Drosophila ras RT oncogene."; RL Mol. Cell. Biol. 5:885-889(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87248071; PubMed=3110012; RA Brock H.W.; RT "Sequence and genomic structure of ras homologues Dmras85D and RT Dmras64B of Drosophila melanogaster."; RL Gene 51:129-137(1987). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1 / Kennison; RX MEDLINE=95309683; PubMed=7789770; RA Harrison S.D., Solomon N., Rubin G.M.; RT "A genetic analysis of the 63E-64A genomic region of Drosophila RT melanogaster: identification of mutations in a replication factor C RT subunit."; RL Genetics 139:1701-1709(1995). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [7] RP SEQUENCE OF 28-192 FROM N.A. RX MEDLINE=84259319; PubMed=6430564; RA Neuman-Silberberg F.S., Schejter E., Hoffmann F.M., Shilo B.-Z.; RT "The Drosophila ras oncogenes: structure and nucleotide sequence."; RL Cell 37:1027-1033(1984). RN [8] RP SEQUENCE OF 28-192 FROM N.A. RC STRAIN=A1; RX MEDLINE=20020328; PubMed=10552039; RA Gasperini R., Gibson G.; RT "Absence of protein polymorphism in the Ras genes of Drosophila RT melanogaster."; RL J. Mol. Evol. 49:583-590(1999). RN [9] RP SEQUENCE OF 1-18 AND 44-64 FROM N.A., SPLICE SITES, AND MUTAGENESIS. RX MEDLINE=88255843; PubMed=2838380; RA Bishop J.G. III, Corces V.G.; RT "Expression of an activated ras gene causes developmental RT abnormalities in transgenic Drosophila melanogaster."; RL Genes Dev. 2:567-577(1988). RN [10] RP SEQUENCE OF 1-29 FROM N.A. RX MEDLINE=88319648; PubMed=3412773; RA Cohen N., Salzberg A., Lev Z.; RT "A bidirectional promoter is regulating the Drosophila ras2 gene."; RL Oncogene 3:137-142(1988). RN [11] RP CHARACTERIZATION. RX MEDLINE=94008534; PubMed=8404533; RA Salzberg A., Cohen N., Halachmi N., Kimchie Z., Lev Z.; RT "The Drosophila Ras2 and Rop gene pair: a dual homology with a yeast RT Ras-like gene and a suppressor of its loss-of-function phenotype."; RL Development 117:1309-1319(1993). CC -!- FUNCTION: MAY BE INVOLVED IN ENDOCYTIC PROCESSES AND/OR OTHER CC TRANSPORT PATHWAYS MEDIATED BY VESICLE TRAFFICKING. MAY INTERACT CC FUNCTIONALLY WITH ROP PROTEIN. RAS PROTEINS BIND GDP/GTP AND CC POSSESS INTRINSIC GTPASE ACTIVITY. CC -!- ENZYME REGULATION: ALTERNATE BETWEEN AN INACTIVE FORM BOUND TO GDP CC AND AN ACTIVE FORM BOUND TO GTP. ACTIVATED BY A GUANINE CC NUCLEOTIDE-EXCHANGE FACTOR (GEF) AND INACTIVATED BY A GTPASE- CC ACTIVATING PROTEIN (GAP). CC -!- DEVELOPMENTAL STAGE: A UNIFORM EXPRESSION IS SEEN IN UNFERTILIZED CC EGGS, EMBRYOS, LARVAE, PUPAE AND ADULT FLIES. EXPRESSION DURING CC EMBRYOGENESIS IS RESTRICTED TO THE CENTRAL NERVOUS SYSTEM (CNS) CC AND THE GARLAND CELLS, A SMALL GROUP OF NEPHROCYTES THAT TAKES UP CC WASTE MATERIALS FROM THE HEMOLYMPH BY ENDOCYTOSIS. IN POST- CC EMBRYONIC STAGES, EXPRESSION IS SEEN IN THE LARVAL SALIVARY GLANDS CC AND THE CENTRAL NERVOUS SYSTEM (CNS), AND IN THE ADULT CNS AND CC REPRODUCTIVE SYSTEMS. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RAS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M10804; AAA99202.1; ALT_SEQ. DR EMBL; M10759; AAA99202.1; JOINED. DR EMBL; M10803; AAA99202.1; JOINED. DR EMBL; M16431; AAA28849.1; -. DR EMBL; M16124; AAA28849.1; JOINED. DR EMBL; M16430; AAA28849.1; JOINED. DR EMBL; U15967; AAB60243.1; -. DR EMBL; AE003480; AAF47845.2; -. DR EMBL; AY119135; AAM50995.1; -. DR EMBL; K01962; AAA28848.1; ALT_SEQ. DR EMBL; K01961; AAA28848.1; JOINED. DR EMBL; AF186651; AAF15517.1; -. DR EMBL; X12559; CAA31072.1; -. DR EMBL; X12558; CAA31071.1; ALT_INIT. DR EMBL; X07255; CAA30242.1; -. DR PIR; S55022; S55022. DR HSSP; P01112; 1PLK. DR FlyBase; FBgn0003206; Ras64B. DR InterPro; IPR003577; GTPase_Ras. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00173; RAS; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein. FT NP_BIND 12 19 GTP (BY SIMILARITY). FT NP_BIND 59 63 GTP (BY SIMILARITY). FT NP_BIND 118 121 GTP (BY SIMILARITY). FT DOMAIN 34 42 EFFECTOR REGION (BY SIMILARITY). FT LIPID 189 189 S-farnesyl cysteine (By similarity). FT MUTAGEN 14 14 G->V: CAUSE DEVELOPMENTAL ABNORMALITIES. FT CONFLICT 28 29 SY -> VS (IN REF. 10). SQ SEQUENCE 192 AA; 22235 MW; 3F58A3A33E8FDEBC CRC64; MQMQTYKLVV VGGGGVGKSA ITIQFIQSYF VTDYDPTIED SYTKQCNIDD VPAKLDILDT AGQEEFSAMR EQYMRSGEGF LLVFALNDHS SFDEIPKFQR QILRVKDRDE FPMLMVGNKC DLKHQQQVSL EEAQNTSRNL MIPYIECSAK LRVNVDQAFH ELVRIVRKFQ IAERPFIEQD YKKKGKRKCC LM // ID RAS3_DROME STANDARD; PRT; 184 AA. AC P08645; Q9V3N0; DT 13-AUG-1987 (Rel. 05, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-like protein 3 (Roughened protein). GN R OR RAS3 OR RAS62B OR RAP OR RAP1 OR CG1956. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92034992; PubMed=1934069; RA Hariharan I.K., Carthew R.W., Rubin G.M.; RT "The Drosophila roughened mutation: activation of a rap homolog RT disrupts eye development and interferes with cell determination."; RL Cell 67:717-722(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85257468; PubMed=3926484; RA Schejter E.D., Shilo B.-Z.; RT "Characterization of functional domains of p21 ras by use of chimeric RT genes."; RL EMBO J. 4:407-412(1985). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=A1; RX MEDLINE=20020328; PubMed=10552039; RA Gasperini R., Gibson G.; RT "Absence of protein polymorphism in the Ras genes of Drosophila."; RL J. Mol. Evol. 49:583-590(1999). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: RAS PROTEINS BIND GDP/GTP AND POSSESS INTRINSIC GTPASE CC ACTIVITY. THE ROUGHENED MUTATION DISRUPTS THE EARLY STAGES OF CC PHOTORECEPTOR CELL DETERMINATION. CC -!- ENZYME REGULATION: ALTERNATE BETWEEN AN INACTIVE FORM BOUND TO GDP CC AND AN ACTIVE FORM BOUND TO GTP. ACTIVATED BY A GUANINE CC NUCLEOTIDE-EXCHANGE FACTOR (GEF) AND INACTIVATED BY A GTPASE- CC ACTIVATING PROTEIN (GAP). CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RAS FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN IN POSITIONS 76 CC TO 96 AND 160 TO 180 DUE TO FRAMESHIFTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M80535; AAA28845.1; -. DR EMBL; X02200; CAA26131.1; ALT_FRAME. DR EMBL; AF186654; AAF15520.1; -. DR EMBL; AE003473; AAF47583.1; -. DR PIR; A41217; A41217. DR HSSP; P01112; 1PLL. DR FlyBase; FBgn0004636; R. DR InterPro; IPR003577; GTPase_Ras. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00173; RAS; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein; Vision. FT CHAIN 1 181 RAS-LIKE PROTEIN 3. FT PROPEP 182 184 REMOVED IN MATURE FORM (BY SIMILARITY). FT NP_BIND 10 17 GTP (BY SIMILARITY). FT NP_BIND 57 61 GTP (BY SIMILARITY). FT NP_BIND 116 119 GTP (BY SIMILARITY). FT DOMAIN 32 40 EFFECTOR REGION (BY SIMILARITY). FT LIPID 181 181 S-geranylgeranyl cysteine FT (By similarity). FT VARIANT 157 157 F -> L (IN ROUGHENED MUTANTS). FT CONFLICT 45 49 EVDGQ -> KVNER (IN REF. 2). FT CONFLICT 56 57 LD -> VN (IN REF. 2). FT CONFLICT 69 69 D -> N (IN REF. 2). SQ SEQUENCE 184 AA; 20863 MW; 9A55889B61FEDE13 CRC64; MREYKIVVLG SGGVGKSALT VQFVQCIFVE KYDPTIEDSY RKQVEVDGQQ CMLEILDTAG TEQFTAMRDL YMKNGQGFVL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MVLVGNKCDL EEERVVGKEL GKNLATQFNC AFMETSAKAK VNVNDIFYDL VRQINKKSPE KKQKKPKKSL CVLL // ID RASP_DROME STANDARD; PRT; 500 AA. AC Q9VZU2; Q95VY0; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Protein-cysteine N-palmitoyltransferase (EC 2.3.1.-) (Rasp protein) DE (Skinny hedgehog protein) (Sightless protein). GN RASP OR SKI OR SIT OR CG11495. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC TISSUE=Embryo; RX MEDLINE=21400488; PubMed=11509241; RA Lee J.D., Treisman J.E.; RT "Sightless has homology to transmembrane acyltransferases and is RT required to generate active Hedgehog protein."; RL Curr. Biol. 11:1147-1152(2001). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RX MEDLINE=21442023; PubMed=11486055; RA Chamoun Z., Mann R.K., Nellen D., von Kessler D.P., Bellotto M., RA Beachy P.A., Basler K.; RT "Skinny hedgehog, an acyltransferase required for palmitoylation and RT activity of the hedgehog signal."; RL Science 293:2080-2084(2001). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION. RX MEDLINE=21850185; PubMed=11861468; RA Micchelli C.A., The I., Selva E., Mogila V., Perrimon N.; RT "Rasp, a putative transmembrane acyltransferase, is required for RT Hedgehog signaling."; RL Development 129:843-851(2002). CC -!- FUNCTION: REQUIRED IN HEDGEHOG (HH) EXPRESSING CELLS FOR CC PRODUCTION OF APPROPRIATE SIGNALING ACTIVITY IN EMBRYOS AND IN THE CC IMAGINAL PRECURSORS OF ADULT TISSUES. ACTS WITHIN THE SECRETORY CC PATHWAY TO CATALYZE AMINO-TERMINAL PALMITOYLATION OF HH; THIS CC LIPID MODIFICATION IS REQUIRED FOR THE EMBRYONIC AND LARVAL CC PATTERNING ACTIVITIES OF THE HH SIGNAL. NOT REQUIRED FOR WG CC SIGNALING. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE MEMBRANE-BOUND ACYLTRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF393157; AAK73748.1; -. DR EMBL; AF398410; AAK97480.1; -. DR EMBL; AE003477; AAF47725.1; -. DR EMBL; AY119202; AAM51062.1; -. DR FlyBase; FBgn0024194; rasp. DR GO; GO:0007225; P:patched receptor ligand processing; IMP. DR InterPro; IPR004299; MBOAT_fam. DR Pfam; PF03062; MBOAT; 1. KW Transferase; Acyltransferase; Developmental protein; KW Segmentation polarity protein; Transmembrane. FT TRANSMEM 15 35 POTENTIAL. FT TRANSMEM 73 93 POTENTIAL. FT TRANSMEM 105 125 POTENTIAL. FT TRANSMEM 134 154 POTENTIAL. FT TRANSMEM 206 226 POTENTIAL. FT TRANSMEM 243 263 POTENTIAL. FT TRANSMEM 293 313 POTENTIAL. FT TRANSMEM 372 392 POTENTIAL. FT TRANSMEM 429 449 POTENTIAL. FT TRANSMEM 461 481 POTENTIAL. FT ACT_SITE 381 381 POTENTIAL. FT CONFLICT 91 91 G -> V (IN REF. 1 AND 4). SQ SEQUENCE 500 AA; 58105 MW; 4498DC306976F2A2 CRC64; MSRLPDRSLL TRCEIFVYFG VYIAYIVVGL YKIYGLRDHI VKEAKFQFPE GWSLYPFSQR RRDDSNDELE NFGDFIVSFW PFYLLHVAVQ GFIRWKRPRL QCLGFIGVCA LALSVNLDWS SMVLLVTLIA SYYIVSLLSL KFLVWLLSAG WILCINVMQK NVWWTDRVGY TEYVLVIVTM SWSVLRGCSY SLSKIGAKQE DLTRYSLVQY LGYAMYFPCL TYGPIISYQR FAARREDEVQ NWLGFVGGVL RSAIWWLVMQ CALHYFYIHY MSRDVRMVEM MDSVFWQHSA GYFMGQFFFL YYVVTYGLGI AFAVQDGIPA PNRPRCIGRI HFYSDMWKYF DEGLYEFLFQ NIYAELCGKR SSAAAKFGAT ALTFAFVFVW HGCYTYVLIW SILNFLCLAA EKVFKTFTAM PEYQRWTQRH LGAVGAQRLY AMLATQLFIP AAFSNVYFIG GQEIGDFLMR GAYLSGVGNY VALCFCSYCF FQCSELLLTK SDGRSKTKTF // ID RB27_DROME STANDARD; PRT; 385 AA. AC P48809; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Heterogeneous nuclear ribonucleoprotein 27C (hnRNP 48) (HRP48.1). GN HRB27C OR HRP48. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=92112968; PubMed=1730754; RA Matunis E.L., Matunis M.J., Dreyfuss G.; RT "Characterization of the major hnRNP proteins from Drosophila RT melanogaster."; RL J. Cell Biol. 116:257-269(1992). CC -!- FUNCTION: THIS PROTEIN IS A COMPONENT OF RIBONUCLEOSOMES. COULD BE CC NEEDED TO ORGANIZE A CONCENTRATION GRADIENT OF A DORSALIZING CC MORPHOGEN (DM) ORIGINATING IN THE GERMINAL VESICLE. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND/OR CYTOPLASMIC. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62639; CAA44505.1; -. DR PIR; D41732; D41732. DR HSSP; P09651; 1HA1. DR FlyBase; FBgn0004838; Hrb27C. DR GO; GO:0005654; C:nucleoplasm; IDA. DR GO; GO:0030529; C:ribonucleoprotein complex; IDA. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 2. KW RNA-binding; Nuclear protein; Ribonucleoprotein; Repeat. FT DOMAIN 7 88 RNA-BINDING (RRM) 1. FT DOMAIN 96 173 RNA-BINDING (RRM) 2. SQ SEQUENCE 385 AA; 41030 MW; 7543E50FA96C9D4E CRC64; MEEDERGKLF VGGLSWETTQ ENLSRYFCRF GDIIDCVVMK NNESGRSRGF GFVTFADPTN VNHVLQNGPH TLDGRTIDPK PCNPRTLQKP KKGGGYKVFL GGLPSNVTET DLRTFFNRYG KVTEVVIMYD QEKKKSRGFG FLSFEEESSV EHVTNERYIN LNGKQVEIKK AEPRDGSGGQ NSNNSTVGGA YGKLGNECSH WGPHHAPINM MQGQNGQMGG PPLNMPIGAP NMMPGYQGWG TSPQQQQYGY GNSGPGSYQG WGAPSGPSGG GSWNSWNMPP NSAGPTGAPG AGAGTATDMY SRAQAWATGG PSTTGPVGGM PRTGPGNSAS KSGSEYDYGG YGSGYDYDYS NYVKQEGASN YGAGPRSAYG NDSSTQPPYA TSQAV // ID RB87_DROME STANDARD; PRT; 386 AA. AC P48810; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heterogeneous nuclear ribonucleoprotein 87F (HRP36.1 protein) (P11 DE protein). GN HRB87F OR HRP36. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Canton-S; TISSUE=Ovary; RX MEDLINE=91187645; PubMed=1849257; RA Haynes S.R., Johnson D., Raychaudhuri G., Beyer A.L.; RT "The Drosophila Hrb87F gene encodes a new member of the A and B hnRNP RT protein group."; RL Nucleic Acids Res. 19:25-31(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92112968; PubMed=1730754; RA Matunis E.L., Matunis M.J., Dreyfuss G.; RT "Characterization of the major hnRNP proteins from Drosophila RT melanogaster."; RL J. Cell Biol. 116:257-269(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=92020124; PubMed=1717937; RA Hovemann B.T., Dessen E., Mechler H., Mack E.; RT "Drosophila snRNP associated protein P11 which specifically binds to RT heat shock puff 93D reveals strong homology with hnRNP core protein RT A1."; RL Nucleic Acids Res. 19:4909-4914(1991). CC -!- FUNCTION: THIS PROTEIN IS A COMPONENT OF RIBONUCLEOSOMES. COULD BE CC NEEDED TO ORGANIZE A CONCENTRATION GRADIENT OF A DORSALIZING CC MORPHOGEN (DM) ORIGINATING IN THE GERMINAL VESICLE. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND/OR CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P48810-1; Sequence=Displayed; CC Name=2; Synonyms=HRP36.1; CC IsoId=P48810-2; Sequence=VSP_005807; CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54803; CAA38574.1; -. DR EMBL; X62636; CAA44502.1; -. DR EMBL; X59691; CAA42212.1; -. DR PIR; A41732; A41732. DR PIR; S22315; S22315. DR HSSP; P09651; 1UP1. DR FlyBase; FBgn0004237; Hrb87F. DR GO; GO:0005717; C:chromatin; IDA. DR GO; GO:0016607; C:nuclear speck; IDA. DR GO; GO:0005654; C:nucleoplasm; IDA. DR GO; GO:0030529; C:ribonucleoprotein complex; IDA. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 2. KW RNA-binding; Nuclear protein; Ribonucleoprotein; Repeat; KW Alternative splicing. FT DOMAIN 24 101 RNA-BINDING (RRM) 1. FT DOMAIN 115 192 RNA-BINDING (RRM) 2. FT VARSPLIC 315 374 Missing (in isoform 2). FT /FTId=VSP_005807. FT CONFLICT 271 271 S -> T (IN REF. 3). SQ SEQUENCE 386 AA; 39557 MW; 2036C04D01E3AFD7 CRC64; MAEQNDSNGN YDDGEEITEP EQLRKLFIGG LDYRTTDDGL KAHFEKWGNI VDVVVMKDPK TKRSRGFGFI TYSQSYMIDN AQNARPHKID GRTVEPKRAV PRQEIDSPNA GATVKKLFVG GLRDDHDEEC LREYFKDFGQ IVSVNIVSDK DTGKKRGFAF IEFDDYDPVD KIILQKTHSI KNKTLDVKKA IAKQDMDRQG GGGGRGGPRA GGRGGQGDRG QGGGGWGGQN RQNGGGNWGG AGGGGGFGNS GGNFGGGQGG GSGGWNQQGG SGGGPWNNQG GGNGGWNGGG GGGGYGGGNS NGSWGGNGGG GGGGGGFGNE YQQSYGGGPQ RNSNFGNNRP APYSQGGGGG GFNKGNQGGG QGFAGNNYNT GGGGQGGNMG GGNRRY // ID RB97_DROME STANDARD; PRT; 471 AA. AC Q02926; Q9VBA9; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ribonucleoprotein RB97D. GN RB97D OR HRB97D OR CG6354. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND ALTERNATIVE SPLICING. RX MEDLINE=93275754; PubMed=8502565; RA Karsch-Mizrachi I., Haynes S.R.; RT "The Rb97D gene encodes a potential RNA-binding protein required for RT spermatogenesis in Drosophila."; RL Nucleic Acids Res. 21:2229-2235(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR SPERMATOGENESIS. COULD BE REQUIRED TO CC PROCESS A SPECIFIC TRANSCRIPT ESSENTIAL FOR SPERMATOGENESIS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q02926-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q02926-2; Sequence=VSP_005808, VSP_005809; CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L02106; AAA99873.1; -. DR EMBL; L02106; AAA99872.1; -. DR EMBL; AE003758; AAF56633.1; -. DR PIR; S33679; S33679. DR PIR; S33680; S33680. DR HSSP; P09651; 1HA1. DR FlyBase; FBgn0004903; Rb97D. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 2. KW RNA-binding; Spermatogenesis; Repeat; Alternative splicing. FT DOMAIN 32 109 RNA-BINDING (RRM) 1. FT DOMAIN 123 198 RNA-BINDING (RRM) 2. FT DOMAIN 223 233 GLN-RICH. FT VARSPLIC 422 427 Missing (in isoform Short). FT /FTId=VSP_005808. FT VARSPLIC 428 428 A -> P (in isoform Short). FT /FTId=VSP_005809. SQ SEQUENCE 471 AA; 51476 MW; 6B044A253A4E7120 CRC64; MVKDEPLSDE SADVIVLADR EEDDICELEH LRKLFIGGLA PYTTEENLKL FYGQWGKVVD VVVMRDAATK RSRGFGFITY TKSLMVDRAQ ENRPHIIDGK TVEAKRALPR PERESRETNI SVKKLFVGGL KDNHDEECLR EYFLQFGNVV SVKLLTDKTT GKRRGFAFVE FDDYDAVDKA ILKKQHAIKY VHVDVKKSIY NLDKKEKQQP GGLANAIKPS LNQQQQQQGG GQQPPNGNMQ APSFRPPVPP QQAMGPYQQQ PPPAPMSAPP PNFNYWGPPP PAMPPYYQQP PPQQMNGWGP YPPPQQNGWN APPPPPPGAQ QWHANQWGCP PPVQQVPPVG AVPPPMGHNG PPPTAPGNWN MPPPVPGAAP PSHQQQSSQQ PTPQPNFGTG YQQNYGGGPS KHNNMNANRM NPYSAGPPNS YHTPQPPAYT GYNAGPLPPN GSVPPPTGAK AVGVSNGSVA TGGSANSKYR R // ID RBF_DROME STANDARD; PRT; 797 AA. AC Q24472; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Retinoblastoma-family protein. GN RBF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96217922; PubMed=8675008; RA Du W., Vidal M., Xie J.-E., Dyson N.; RT "RBF, a novel RB-related gene that regulates E2F activity and RT interacts with cyclin E in Drosophila."; RL Genes Dev. 10:1206-1218(1996). CC -!- FUNCTION: FUNCTIONS IN CELL CYCLE REGULATION. POTENT INHIBITOR OF CC E2F-MEDIATED TRANSACTIVATION. CC -!- SUBUNIT: FORMS A COMPLEX WITH THE DRTF1/E2F TRANSCRIPTION FACTOR CC THROUGH BINDING TO A C-TERMINAL REGION OF E2F. THIS BINDING CC INHIBITS THE E2F-MEDIATED TRANSACTIVATION ACTIVITY. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: PHOSPHORYLATION BY CYCLIN-E-DEPENDENT KINASES APPEARS TO CC NEGATIVELY REGULATE RBF ACTIVITY. CC -!- SIMILARITY: BELONGS TO THE RETINOBLASTOMA PROTEIN (RB) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X96975; CAA65661.1; -. DR HSSP; P06400; 1GUX. DR FlyBase; FBgn0015799; Rbf. DR GO; GO:0008285; P:negative regulation of cell proliferation; NAS. DR InterPro; IPR006670; Cyclin. DR InterPro; IPR002720; RB_A. DR InterPro; IPR002719; RB_B. DR Pfam; PF01858; RB_A; 1. DR Pfam; PF01857; RB_B; 1. DR SMART; SM00385; CYCLIN; 1. KW Transcription regulation; DNA-binding; Nuclear protein; Cell cycle; KW Phosphorylation. FT DOMAIN 374 711 POCKET. FT DOMAIN 374 566 DOMAIN A. FT DOMAIN 576 711 DOMAIN B. SQ SEQUENCE 797 AA; 91910 MW; 5EA0C4638A677303 CRC64; MSEPDPQELG AEVVSGLVAT SDDRLEMINA EYTNLCRDLN MDRQTELQGY ETYLEVSQRC SMEGTASHWM CCAIYTACRR TSTPTVTGQN AVVKGNCVSL NNLLRCCKMS IYEFKTKIKQ WCDMANLPQE FVNEIEDLDR KFSITFMLHK RFRIIMDMIF SCPPNEKKHS KYISLHGNHA HGKCSYIKLD DICWRLFLCA KNQKPSNTVD LVTSYNLMIC CIDLIYNNVL AEKRTDLINP KFEGLPSNWT ELDFRHNPHC ILSNFCDMTE EAKAMKATTF RQIMSSFFQA STIYGNKDTM LGLLANENFE RNLKSLNISY EQYVLSVGEF DERILSAYDA GEHTALNDQS LRPPVTPLTR KQDLPAQPAM AGDKFEPVRN ATNNVKQLSA FGRITEPTDF VKQAGEEVIA KLLSIIEEIE QKFLAKYPST EAKSRFQLAK SFFFYLLDQI LQAEIRNKPD IDLKRLLVQK VSLVIFNITL MACCVELVLE AYKTELKFPW VLDCFSISAF EFQKIIEIVV RHGSHEGCLN RSLIKHLNSI EETCLERLAW ARNSTVWEMI ASAQLPLPTW LMVNLDRAAG PLQIFLRKVY LLGWLRIQKL CSELSLCEKT PESIWHIFEH SITHETELMK DRHLDQNIMC AIYIYIRVKR MEDPKFSDIM RAYRNQPQAV NSVYREVFID INEDGEPKVK DIIHFYNHTY VPLMRQFVID YLNVTPDVSG RASDLQLSPH PKERAAQPKK VTQSHSLFVS QMSKNEIQQS PNQMVYSFFR SPAKDLQAMN EKVRGGKRML SFGDEPD // ID RBP1_DROME STANDARD; PRT; 135 AA. AC Q02427; Q26271; Q9VGW8; DT 15-DEC-1998 (Rel. 37, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE RNA-binding protein 1. GN RBP1 OR CG17136. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., CHARACTERIZATION, AND ALTERNATIVE SPLICING. RX MEDLINE=94040720; PubMed=1340470; RA Kim Y.-J., Zuo P., Manley J.L., Baker B.S.; RT "The Drosophila RNA-binding protein RBP1 is localized to RT transcriptionally active sites of chromosomes and shows a functional RT similarity to human splicing factor ASF/SF2."; RL Genes Dev. 6:2569-2579(1992). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 14-52 FROM N.A. RX MEDLINE=93109300; PubMed=8417324; RA Kim Y.J., Baker B.S.; RT "Isolation of RRM-type RNA-binding protein genes and the analysis of RT their relatedness by using a numerical approach."; RL Mol. Cell. Biol. 13:174-183(1993). RN [4] RP FUNCTION. RX MEDLINE=95393975; PubMed=7664738; RA Heinrichs V., Baker B.S.; RT "The Drosophila SR protein RBP1 contributes to the regulation of RT doublesex alternative splicing by recognizing RBP1 RNA target RT sequences."; RL EMBO J. 14:3987-4000(1995). CC -!- FUNCTION: CONTRIBUTES TO THE ACTIVATION OF FEMALE-SPECIFIC DSX CC SPLICING IN VIVO BY RECOGNIZING THE RBP1 TARGET SEQUENCES WITHIN CC THE PURINE-RICH POLYPYRIMIDINE TRACT OF THE FEMALE-SPECIFIC 3' CC SPLICE SITE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=RBP1-A; CC IsoId=Q02427-1; Sequence=Displayed; CC Name=2; Synonyms=RBP1-B; CC IsoId=Q02427-2; Sequence=VSP_005817; CC -!- TISSUE SPECIFICITY: UBIQUITOUS. CC -!- DEVELOPMENTAL STAGE: FOUND AT ALL DEVELOPMENTAL STAGES. CC -!- PTM: EXTENSIVELY PHOSPHORYLATED ON SERINE RESIDUES IN THE RS CC DOMAIN (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE SPLICING FACTOR SR FAMILY. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L04929; AAA28850.1; -. DR EMBL; AE003688; AAF54555.1; -. DR EMBL; S51691; AAB24622.1; -. DR PIR; A46398; A46398. DR PIR; A48110; A48110. DR FlyBase; FBgn0010252; Rbp1. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Nuclear protein; RNA-binding; mRNA splicing; Alternative splicing; KW Phosphorylation. FT DOMAIN 11 84 RNA-BINDING (RRM). FT DOMAIN 82 135 ARG/SER-RICH (RS DOMAIN). FT VARSPLIC 107 135 Missing (in isoform 2). FT /FTId=VSP_005817. FT CONFLICT 14 14 Y -> F (IN REF. 3). FT CONFLICT 65 65 R -> A (IN REF. 1). SQ SEQUENCE 135 AA; 15446 MW; 896DCE902518D991 CRC64; MPRYREWDLA CKVYVGNLGS SASKHEIEGA FAKYGPLRNV WVARNPPGFA FVEFEDRRDA EDATRALDGT RCCGTRIRVE MSSGRSRDRR RGEGGSSGRS GSGRYRSRSP RRSRSPRSRS FSRDRRSRSD SRDRH // ID RBXA_DROME STANDARD; PRT; 108 AA. AC Q9W5E1; O77429; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE RING-box protein 1A (Regulator of cullins 1a) (dRbx1). GN ROC1A OR CG16982 OR EG:115C2.11. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF RP ASN-59 AND CYS-68. RX MEDLINE=22057626; PubMed=12062088; RA Noureddine M.A., Donaldson T.D., Thacker S.A., Duronio R.J.; RT "Drosophila Roc1a encodes a RING-H2 protein with a unique function in RT processing the Hh signal transducer Ci by the SCF E3 ubiquitin RT ligase."; RL Dev. Cell 2:757-770(2002). RN [5] RP INTERACTION WITH LIN19 AND SLMB. RX MEDLINE=21391618; PubMed=11500045; RA Bocca S.N., Muzzopappa M., Silberstein S., Wappner P.; RT "Occurrence of a putative SCF ubiquitin ligase complex in RT Drosophila."; RL Biochem. Biophys. Res. Commun. 286:357-364(2001). RN [6] RP REVIEW ON E3 UBIQUITIN LIGASE COMPLEXES. RX MEDLINE=22736111; PubMed=12850443; RA Ou C.-Y., Pi H., Chien C.-T.; RT "Control of protein degradation by E3 ubiquitin ligases in Drosophila RT eye development."; RL Trends Genet. 19:382-389(2003). CC -!- FUNCTION: COMPONENT OF THE SCF (SKP1-CUL1-F-BOX PROTEIN) E3 CC UBIQUITIN LIGASE COMPLEX, WHICH MEDIATES THE UBIQUITINATION AND CC SUBSEQUENT PROTEASOMAL DEGRADATION OF TARGET PROTEINS. THROUGH THE CC RING-TYPE ZINC FINGER, SEEMS TO RECRUIT THE E2 UBIQUITINATION CC ENZYME TO THE COMPLEX AND BRINGS IT INTO CLOSE PROXIMITY TO THE CC SUBSTRATE. REQUIRED FOR THE SPECIFIC SCF-DEPENDENT PROTEOLYSIS OF CC CI, BUT NOT THAT OF ARM, SUGGESTING THAT IT ALSO PARTICIPATES IN CC THE SELECTION OF SUBSTRATES INSIDE THE SCF COMPLEX. CC -!- PATHWAY: UBIQUITIN CONJUGATION; THIRD STEP. CC -!- SUBUNIT: PART OF A SCF COMPLEX CONSISTING OF SKPA (SKP1), LIN19 CC (CUL1), ROC1A AND F-BOX PROTEIN SLMB. INTERACTS DIRECTLY WITH CC LIN19 AND SLMB. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED. EXPRESSED IN EMBRYONIC, CC LARVAL AND ADULT TISSUES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- DOMAIN: THE RING-TYPE ZINC FINGER DOMAIN IS ESSENTIAL FOR CC UBIQUITIN LIGASE ACTIVITY. IT COORDINATES AN ADDITIONAL THIRD ZINC CC ATOM (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE RING-BOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003418; AAF45536.1; -. DR EMBL; AL031581; CAA20888.1; ALT_SEQ. DR EMBL; AY119265; AAM51125.1; -. DR PIR; T13388; T13388. DR FlyBase; FBgn0025638; Roc1a. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00097; zf-C3HC4; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Ubl conjugation pathway; Nuclear protein; Developmental protein; Zinc; KW Zinc-finger; Metal-binding. FT ZN_FING 53 98 RING-TYPE. FT DOMAIN 12 15 POLY-SER. FT METAL 42 42 ZINC 1 (BY SIMILARITY). FT METAL 45 45 ZINC 1 (BY SIMILARITY). FT METAL 53 53 ZINC 3 (BY SIMILARITY). FT METAL 56 56 ZINC 3 (BY SIMILARITY). FT METAL 68 68 ZINC 3 (BY SIMILARITY). FT METAL 75 75 ZINC 2 (BY SIMILARITY). FT METAL 77 77 ZINC 2 (BY SIMILARITY). FT METAL 80 80 ZINC 1 (BY SIMILARITY). FT METAL 82 82 ZINC 3 (BY SIMILARITY). FT METAL 83 83 ZINC 1 (BY SIMILARITY). FT METAL 94 94 ZINC 2 (BY SIMILARITY). FT METAL 97 97 ZINC 2 (BY SIMILARITY). FT MUTAGEN 59 59 N->C: LOSS OF FUNCTION WHEN ASSOCIATED FT WITH R-68. FT MUTAGEN 68 68 C->R: LOSS OF FUNCTION WHEN ASSOCIATED FT WITH C-59. SQ SEQUENCE 108 AA; 12538 MW; 15784198281BCD13 CRC64; MEVDEDGYEV PSSSSKGDKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WDFQKYGH // ID RBXB_DROME STANDARD; PRT; 122 AA. AC Q9NHX0; Q9W0R1; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE RING-box protein 1B (Regulator of cullins 1b). GN ROC1B OR ROC2 OR CG16988. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=22057626; PubMed=12062088; RA Noureddine M.A., Donaldson T.D., Thacker S.A., Duronio R.J.; RT "Drosophila Roc1a encodes a RING-H2 protein with a unique function in RT processing the Hh signal transducer Ci by the SCF E3 ubiquitin RT ligase."; RL Dev. Cell 2:757-770(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPONENT OF THE SCF (SKP1-CUL1-F-BOX PROTEIN) E3 CC UBIQUITIN LIGASE COMPLEX, WHICH MEDIATES THE UBIQUITINATION AND CC SUBSEQUENT PROTEASOMAL DEGRADATION OF TARGET PROTEINS. THROUGH THE CC RING-TYPE ZINC FINGER, SEEMS TO RECRUIT THE E2 UBIQUITINATION CC ENZYME TO THE COMPLEX AND BRINGS IT INTO CLOSE PROXIMITY TO THE CC SUBSTRATE (BY SIMILARITY). CC -!- PATHWAY: UBIQUITIN CONJUGATION; THIRD STEP. CC -!- SUBUNIT: PART OF A SCF COMPLEX CONSISTING OF SKPA (SKP1), CC LIN19 (CUL1), ROC1B AND A F-BOX PROTEIN (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN EARLY EMBRYOS, AND IN CC PUPAE. WIDELY EXPRESSED IN ADULT MALES, WHILE IT IS WEAKLY CC EXPRESSED IN ADULT FEMALES. CC -!- DOMAIN: THE RING-TYPE ZINC FINGER DOMAIN IS ESSENTIAL FOR CC UBIQUITIN LIGASE ACTIVITY. IT COORDINATES AN ADDITIONAL THIRD ZINC CC ATOM (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE RING-BOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-16 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF218290; AAF32313.1; ALT_INIT. DR EMBL; AE003468; AAF47382.1; -. DR EMBL; AY070810; AAL48432.1; -. DR FlyBase; FBgn0040291; Roc1b. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Ubl conjugation pathway; Nuclear protein; Zinc; Zinc-finger; KW Metal-binding. FT ZN_FING 57 112 RING-TYPE. FT METAL 68 68 ZINC 3 (BY SIMILARITY). FT METAL 71 71 ZINC 3 (BY SIMILARITY). FT METAL 82 82 ZINC 3 (BY SIMILARITY). FT METAL 96 96 ZINC 3 (BY SIMILARITY). FT METAL 57 57 ZINC 1 (BY SIMILARITY). FT METAL 60 60 ZINC 1 (BY SIMILARITY). FT METAL 89 89 ZINC 2 (BY SIMILARITY). FT METAL 91 91 ZINC 2 (BY SIMILARITY). FT METAL 94 94 ZINC 1 (BY SIMILARITY). FT METAL 97 97 ZINC 1 (BY SIMILARITY). FT METAL 108 108 ZINC 2 (BY SIMILARITY). FT METAL 111 111 ZINC 2 (BY SIMILARITY). SQ SEQUENCE 122 AA; 14225 MW; F22CE00438725410 CRC64; MAEEIEVEET EDFHDMDFND EEPSCSGGAV QARTERFVVK KWVAHAMWGW DVAVDNCAIC RNHIMNLCIE CQADPNANQD ECTVAWGECN HAFHYHCIAR WLKTRLVCPL DNKEWVYQKY GR // ID RCC1_DROME STANDARD; PRT; 547 AA. AC P25171; Q9VRR5; DT 01-MAY-1992 (Rel. 22, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Regulator of chromosome condensation (Chromatin-binding protein Bj1). GN BJ1 OR CG10480. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91216118; PubMed=2022188; RA Frasch M.; RT "The maternally expressed Drosophila gene encoding the RT chromatin-binding protein BJ1 is a homolog of the vertebrate gene RT Regulator of Chromatin Condensation, RCC1."; RL EMBO J. 10:1225-1236(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP CHARACTERIZATION, AND SUBCELLULAR LOCATION. RX MEDLINE=91216122; PubMed=2022190; RA Ohtsubo M., Yoshida T., Seino H., Nishitani H., Clark K.L., RA Sprague G.F. Jr., Frasch M., Nishimoto T.; RT "Mutation of the hamster cell cycle gene RCC1 is complemented by the RT homologous genes of Drosophila and S.cerevisiae."; RL EMBO J. 10:1265-1273(1991). CC -!- FUNCTION: PROMOTES THE EXCHANGE OF RAN-BOUND GDP BY GTP. CC INVOLVED IN THE REGULATION OF ONSET OF CHROMOSOME CONDENSATION CC IN THE S PHASE. BINDS TO THE CHROMATIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR; BECOMES DISPERSED THROUGHOUT THE CC CYTOPLASM DURING MITOSIS. CC -!- SIMILARITY: CONTAINS 7 RCC1 REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58530; CAA41417.1; -. DR EMBL; AE003564; AAF50726.1; -. DR EMBL; AY070540; AAL48011.1; -. DR PIR; S15028; S15028. DR HSSP; P18754; 1A12. DR FlyBase; FBgn0002638; Bj1. DR InterPro; IPR000408; Reg_chr_condens. DR Pfam; PF00415; RCC1; 5. DR PRINTS; PR00633; RCCNDNSATION. DR PROSITE; PS00625; RCC1_1; 1. DR PROSITE; PS00626; RCC1_2; 4. DR PROSITE; PS50012; RCC1_3; 6. KW Guanine-nucleotide releasing factor; Cell cycle; Mitosis; Repeat; KW DNA-binding; Nuclear protein. FT REPEAT 41 91 RCC1 1. FT REPEAT 92 143 RCC1 2. FT REPEAT 145 195 RCC1 3. FT REPEAT 197 257 RCC1 4. FT REPEAT 260 310 RCC1 5. FT REPEAT 311 362 RCC1 6. FT REPEAT 363 416 RCC1 7. FT DOMAIN 417 519 3 X TANDEM REPEATS, BJ1. FT REPEAT 417 454 BJ1 1. FT REPEAT 455 489 BJ1 2. FT REPEAT 490 519 BJ1 3. FT DOMAIN 520 547 GLU/LYS-RICH. FT CONFLICT 490 490 V -> A (IN REF. 1). SQ SEQUENCE 547 AA; 58850 MW; 77D9744EBAF4597A CRC64; MPRRKALTNN NNAGEAEQQP PKAKRARIAF HLELPKRRTV LGNVLVCGNG DVGQLGLGED ILERKRLSPV AGIPDAVDIS AGGMHNLVLT KSGDIYSFGC NDEGALGRDT SEDGSESKPD LIDLPGKALC ISAGDSHSAC LLEDGRVFAW GSFRDSHGNM GLTIDGNKRT PIDLMEGTVC CSIASGADHL VILTTAGKVF TVGCAEQGQL GRLSERSISG EGRRGKRDLL RPTQLIITRA KPFEAIWATN YCTFMRESQT QVIWATGLNN FKQLAHETKG KEFALTPIKT ELKDIRHIAG GQHHTVILTT DLKCSVVGRP EYGRLGLGDV KDVVEKPTIV KKLTEKIVSV GCGEVCSYAV TIDGKLYSWG SGVNNQLGVG DGDDELEPIV VVSKNTQGKH MLLASGGGQH AIFLVKADKQ DQKENVPVKV SGSSSISKKD KTPPQDNVDK EAENVDKQEQ KENLPAKAST SSKKNKTPPQ DNADKEAENV DKQEQKENLP AKASTSSKKI KTPPQDDAAE EVEEESAQEP TPKKAKKPAA KRGGKKT // ID RCL1_DROME STANDARD; PRT; 307 AA. AC P56175; Q9VY90; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable RNA 3'-terminal phosphate cyclase-like protein. GN RCL1 OR RTC1 OR RTC2 OR CG11130. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 73-307 FROM N.A. RX MEDLINE=87146365; PubMed=3029679; RA Yan Y.L., Kunert C.J., Postlethwait J.H.; RT "Sequence homologies among the three yolk polypeptide (Yp) genes in RT Drosophila melanogaster."; RL Nucleic Acids Res. 15:67-85(1987). RN [3] RP SEQUENCE OF 73-307 FROM N.A. RX MEDLINE=87305580; PubMed=3114046; RA Garabedian M.J., Shirras A.D., Bownes M., Wensink P.C.; RT "The nucleotide sequence of the gene coding for Drosophila RT melanogaster yolk protein 3."; RL Gene 55:1-8(1987). RN [4] RP IDENTIFICATION. RX MEDLINE=97327572; PubMed=9184239; RA Genschik P., Billy E., Swianiewicz M., Filipowicz W.; RT "The human RNA 3'-terminal phosphate cyclase is a member of a new RT family of proteins conserved in Eucarya, Bacteria and Archaea."; RL EMBO J. 16:2955-2967(1997). CC -!- FUNCTION: DOES NOT HAVE CYCLASE ACTIVITY. PLAYS A ROLE IN 40S- CC RIBOSOMAL-SUBUNIT BIOGENESIS IN THE EARLY PRE-RRNA PROCESSING CC STEPS AT SITES A0, A1 AND A2 THAT ARE REQUIRED FOR PROPER CC MATURATION OF THE 18S RNA (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR; NUCLEOLAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. CC SUBFAMILY 2. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003493; AAF48313.1; -. DR EMBL; X04754; CAB55765.1; -. DR EMBL; M15898; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0020909; Rtc1. DR InterPro; IPR000228; RNA3'_term_cycl. DR Pfam; PF01137; RTC; 1. DR Pfam; PF05189; RTC_insert; 1. DR PROSITE; PS01287; RTC; 1. KW Nuclear protein. FT CONFLICT 88 91 PLGG -> SAGR (IN REF. 3). SQ SEQUENCE 307 AA; 33625 MW; FADBE52A57C079FE CRC64; MFSPGLLHGG QLNHDCCVQR GIGYYLDALI ALGPFCKSPL QCTLRGVTNS KDSPSVDHIK GAALSLLKRF LLVDEGLELK VVRRGVAPLG GGEIIFRCPV RKSLRAIQFQ SQGMVKRIRG TVYACKVSPA MANRTVEAAK GCMLKFLPDV YIYTDQNKGK MSGNSPGFGI CLIAETTDGV CFAADCCSNT REESEDTPSI PENLGKEVAL RLLDEIYRGG CVDSSYQWLA ALYIALGQKH VSKFLTGALS NYTVHFLQHL RDFFSITFKL ENPEAEDEDE AENVRGAQKV LMACVGIGYT NINKRVI // ID RDGB_DROME STANDARD; PRT; 1054 AA. AC P43125; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Retinal degeneration B protein (Probable calcium transporter RDGB). GN RDGB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=91231170; PubMed=1903119; RA Vihtelic T.S., Hyde D.R., O'Tousa J.E.; RT "Isolation and characterization of the Drosophila retinal RT degeneration B (rdgB) gene."; RL Genetics 127:761-768(1991). CC -!- FUNCTION: RDGB MUTANTS UNDERGO RAPID LIGHT-INDUCED RETINAL CC DEGENERATION. MAY CONTROL PHOSPHATIDYLINOSITOL CONCENTRATION IN CC TRANSPORT VESICLES FROM THE SUBRHABDOMERIC CISTERNAE (SRC) TO THE CC RHABDOMERE. MAY FUNCTION AS A CALCIUM TRANSPORTER. CC -!- TISSUE SPECIFICITY: EXPRESSED IN ADULT HEADS, NOT DETECTED IN CC BODIES. CC -!- SIMILARITY: THE N-TERMINAL IS SIMILAR TO MAMMALIAN CC PHOSPHATIDYLINOSITOL (PTDINS) TRANSFER PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57978; CAA41044.1; -. DR PIR; A61221; A61221. DR FlyBase; FBgn0003218; rdgB. DR GO; GO:0016029; C:subrhabdomeral cisterna; NAS. DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IDA. DR GO; GO:0008526; F:phosphatidylinositol transporter activity; IDA. DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP. DR GO; GO:0007608; P:olfaction; IMP. DR GO; GO:0016056; P:rhodopsin mediated signaling; IMP. DR InterPro; IPR004177; DDHD_dom. DR InterPro; IPR001666; PI_transfer. DR Pfam; PF02862; DDHD; 1. DR Pfam; PF02121; IP_trans; 1. DR PRINTS; PR00391; PITRANSFER. KW Transmembrane; Vision. FT DOMAIN 321 332 ASP/GLU-RICH (HIGHLY ACIDIC). FT TRANSMEM 501 519 POTENTIAL. FT TRANSMEM 734 750 POTENTIAL. FT CARBOHYD 194 194 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 414 414 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 612 612 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 658 658 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 852 852 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 928 928 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1054 AA; 116560 MW; 87F26EB871003CA8 CRC64; MLIKEYRIPL PLTVEEYRIA QLYMIAKKSR EESHGEGSGV EIIINEPYKD GPGGNGQYTK KIYHVGNHLP GWIKSLLPKS ALTVEEEAME CYPYTRTRYT CPFVEKFSLD IETYYYPDNG YQDNVFQLSG SDLRNRIVDV IDIVKDQLWG GDYVKEEDPK HFVSDKTGRG PLAEDWLEEY WREVKGKKQP TPRNMSLMTA YKICRVEFRY WGMQTKLEKF IHDVALRKMM LRAHRQAWAW QDEWFGLTIE DIRELERQTQ LALAKKMGGG EECSDDSVSE PYVSTAATAA STTGSERKKS APAVPPIVTQ QPPSAEASSD EEGEEEEDDD EDENDAIGTG VDLSANQGGS AQRSRSQSIQ MAQKGKFGSK GALHSPVGSA HSFDLQVANW RMERLEVDSK SNSDEEFFDC LDTNETNSLA KWSSLELLGE GDDSPPPHGG PSSAASVGGR GNSRQEDSIF NQDFLMRVAS ERGNKRQLRS SASVDRSHDS SPPGSPSTPS CPTTILILVV HAGSVLDAAS ELTAKKSDVT TFRGSFEAVM RHDYPSLLTH VTIKMVPCPS ICTDALGILS SLSPYSFDAS PSAADIPNIA DVPIGAIPLL SVASPEFHET VNKTVAAANI VCHEFLKSEE GHGFSGQIVM LGDSMGSLLA YEALCRSNGS QPGTASGASN SGGDAATNIN THNPLSPRNS RLDDDERFIE ADLDAKRLLV APSPRRRRSS SSSDSRATKL DFEVCDFFMF GSPLSVVLAA RKLHDAKAAL PRPNCHQVYN LFHPTDPIAS RLEPLLSARF SILAPVNVPR YAKYPLGNGQ PLHLLEVIQS HPQRFNDGNN LLAGRRLSDA SMQSTISGLI ENVSLSTIHA LQNKWWGTKR LDYALYCPEG LSNFPAHALP HLFHASYWES PDVIAFILRQ IGKFEGIPFV GSNDDKDNAS FHPGQPREKW IKKRTSVKLK NVAANHRAND VIVQEGREQR LNARFMYGPL DMITLHGEKV DVHIMKDPPA GQWTFLSTEV TDKNGRISYS IPDQVSLGYG IYPVKMVVRG DHTSVDCYMA VVPR // ID RDGC_DROME STANDARD; PRT; 661 AA. AC P40421; Q9VWA4; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase rdgC (EC 3.1.3.16) (Retinal DE degeneration C protein). GN RDGC OR CG6571. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92266398; PubMed=1316807; RA Steele F.R., Washburn T., Rieger R., O'Tousa J.E.; RT "Drosophila retinal degeneration C (rdgC) encodes a novel RT serine/threonine protein phosphatase."; RL Cell 69:669-676(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PHOSPHATASE REQUIRED TO PREVENT LIGHT-INDUCED RETINAL CC DEGENERATION. CC -!- CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN + CC PHOSPHATE. CC -!- COFACTOR: BINDS 1 IRON ION AND 1 MANGANESE ION PER SUBUNIT (BY CC SIMILARITY). CC -!- ENZYME REGULATION: REGULATED BY CALCIUM. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE VISUAL SYSTEMS OF THE FLY, AS CC WELL AS IN THE MUSHROOM BODIES OF THE CENTRAL BRAIN. CC -!- SIMILARITY: BELONGS TO THE PPP PHOSPHATASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 IQ DOMAIN. CC -!- SIMILARITY: CONTAINS 2 EF-HAND CALCIUM-BINDING DOMAINS. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M89628; AAB00734.1; -. DR EMBL; AE003514; AAF49044.1; ALT_SEQ. DR PIR; A42287; A42287. DR HSSP; Q08209; 1AUI. DR FlyBase; FBgn0004366; rdgC. DR GO; GO:0005516; F:calmodulin binding; IDA. DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP. DR GO; GO:0007602; P:phototransduction; IMP. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IMP. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00036; efhand; 3. DR Pfam; PF00612; IQ; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00054; EFh; 3. DR SMART; SM00015; IQ; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00018; EF_HAND; 2. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. DR PROSITE; PS50096; IQ; 1. KW Hydrolase; Calcium-binding; Metal-binding; Magnesium; Iron; Manganese; KW Vision; Repeat. FT DOMAIN 7 32 IQ. FT DOMAIN 105 413 CATALYTIC. FT DOMAIN 454 465 ANCESTRAL CALCIUM SITE. FT CA_BIND 539 550 EF-HAND 1 (POTENTIAL). FT CA_BIND 579 590 EF-HAND 2 (POTENTIAL). FT METAL 158 158 IRON (BY SIMILARITY). FT METAL 160 160 IRON (BY SIMILARITY). FT METAL 187 187 IRON AND MANGANESE (BY SIMILARITY). FT METAL 219 219 MANGANESE (BY SIMILARITY). FT ACT_SITE 220 220 GENERAL ACID (BY SIMILARITY). FT METAL 271 271 MANGANESE (BY SIMILARITY). FT METAL 360 360 MANGANESE (BY SIMILARITY). SQ SEQUENCE 661 AA; 75511 MW; A3DC42933E4CCA33 CRC64; MDENAIRAAI FIQKWYRRHQ ARREMQRRCN WQIFQNLEYA SEQDQAELYK FFNDLIKHMP QAAGRKNQYQ GSAHVSVLDD KDDLVEEFGD IVNAKIELPI RKNHIDLLID VFRKKRGNRL HPKYVALILR EAAKSLKQLP NISPVSTAVS QQVTVCGDLH GKLDDLLVVL HKNGLPSSSN PYVFNGDFVD RGKRGLEVLL LLLSLYLAFP NAVFLNRGNH EDSVMNARYG FIREVESKYP RNHKRILAFI DEVYRWLPLG SVLNSRVLIV HGGFSDSTSL DLIKSIDRGK YVSILRPPLT DGEPLDKTEW QQIFDIMWSD PQATMGCVPN TLRGAGVWFG PDVTDNFLQR HRLSYVIRSH ECKPNGHEFM HDNKIITIFS ASNYYAIGSN KGAYIRLNNQ LMPHFVQYIS AASQTKRLSF KQRMGIVESS ALKELAVRMR DHRDELEDEF RKYDPKDSGY ISISHWCKVM ENVTKLGLPW RLLRDKLAPG TDSQKVNYNR TLDLLDTDVI LEAEADGMSV MDALYANKAS LVAIFNIIDA DNSGEITLDE FETAIDLLVA HMPGAYSKAE MLEKCRMMDL NGDGKVDLNE FLEAFRLSDL HRKEQQDENI RRRSTGRPSV AKTATDPVTL LADKISKNTL VVEHDIDPTD CESKVIDPKK S // ID REG2_DROME STANDARD; PRT; 260 AA. AC Q94915; Q9W0P6; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Rhythmically expressed gene 2 protein (dREG-2). GN REG-2 OR CG3200. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96362140; PubMed=8749395; RA van Gelder R.N., Bae H., Palazzolo M.J., Krasnow M.A.; RT "Extent and character of circadian gene expression in Drosophila RT melanogaster: identification of twenty oscillating mRNAs in the fly RT head."; RL Curr. Biol. 5:1424-1436(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- INDUCTION: MAXIMALLY EXPRESSED AT PREDAWN OR EARLY MORNING. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U65492; AAC47289.1; -. DR EMBL; AE003468; AAF47397.1; -. DR FlyBase; FBgn0016715; Reg-2. DR InterPro; IPR005834; Hydrolase. DR Pfam; PF00702; Hydrolase; 1. SQ SEQUENCE 260 AA; 30113 MW; 5E074BB38B5668EE CRC64; MRSLSRFRLI TFDVTNTLLQ FRTTPGKQYG EIGALFGARC DNNELAKNFK ANWYKMNRDY PNFGRDTNPQ MEWQQWWRKL IAGTFAESGA AIPDEKLHNF SNHLIELYKT SICWQPCNGS VELLQQLRKE LKPEKCKLGV IANFDPRLPT LLQNTKLDQY LDFAINSYEV QAEKPDPQIF QKAMEKSGLK NLKPEECLHI GDGPTTDYLA AKELGWHSAL VHEKSYAYLV KKYGEDIDRD HVFPSLYDFH KKISDGAVVW // ID REG5_DROME STANDARD; PRT; 298 AA. AC Q94913; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Rhythmically expressed gene 5 protein (dREG-5). GN REG-5. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=96203080; PubMed=8612586; RA van Gelder R.N., Krasnow M.A.; RT "A novel circadianly expressed Drosophila melanogaster gene dependent RT on the period gene for its rhythmic expression."; RL EMBO J. 15:1625-1631(1996). CC -!- FUNCTION: INVOLVED IN THE GENERATION OF BIOLOGICAL RHYTHMS CC (POTENTIAL). IN THE HEAD, OSCILLATES IN ABUNDANCE WITH A DAILY CC PEAK DURING EARLY NIGHT, EVEN UNDER CONSTANT DARKNESS. OSCILLATION CC IS DEPENDENT ON PERIOD (PER) FUNCTION. CC -!- TISSUE SPECIFICITY: EXPRESSED IN HEAD, BUT NOT IN THE BODY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN 24 HOURS EMBRYO. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U65105; AAC47267.1; -. DR PIR; S69241; S69241. DR FlyBase; FBgn0015801; Reg-5. KW Biological rhythms. FT DOMAIN 22 25 POLY-SER. SQ SEQUENCE 298 AA; 32202 MW; FEFA90998F423893 CRC64; MTTAAKVILA CCLLGAFHIQ ISSSSAIPIW EFLTRNEKMS HLYSTFAQLV SVHCKSTAAV GGLPVNQCKH NLLGYGSAKL QTLSDVQLEA LDPYQRDANE LIWSSIMGDH PSGASLVTTR QPLQQPLPTP PASSLIILTR QQLPHGASHA HPIQSSGSAT NPIFESGEQK HKYAMDMDKA YGYGPQSSSE LPVAAALTSE PSKRFLTGPL VIRVRPDGSP VEEDKMMPLP RDEDLPYLSS WSGRRSAQQA PQDRHNQLLK AAALRLHPAE RPPATPPDAE ASVPPATGVR SRSEDPQA // ID RF2P_DROME STANDARD; PRT; 599 AA. AC P14199; Q04577; Q04578; Q24063; Q24064; Q24065; Q24066; Q24067; AC Q24068; Q24069; Q24070; Q24071; Q24072; Q9VIU1; DT 01-JAN-1990 (Rel. 13, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ref(2)P protein (Refractory to sigma P). GN REF(2)P OR CG10360. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90059939; PubMed=2510997; RA Dezelee S., Bras F., Contamine D., Lopez-Ferber M., Segretain D., RA Teninges D.; RT "Molecular analysis of ref(2)P, a Drosophila gene implicated in sigma RT rhabdovirus multiplication and necessary for male fertility."; RL EMBO J. 8:3437-3446(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Imaginal disks; RX MEDLINE=93216091; PubMed=8462852; RA Dru P., Bras F., Dezelee S., Gay P., Petitjean A.M., RA Pierre-Deneubourg A., Teninges D., Contamine D.; RT "Unusual variability of the Drosophila melanogaster ref(2)P protein RT which controls the multiplication of sigma rhabdovirus."; RL Genetics 133:943-954(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Various strains; RX MEDLINE=96139066; PubMed=8583891; RA Wayne M.L., Contamine D., Kreitman M.; RT "Molecular population genetics of ref(2)P, a locus which confers viral RT resistance in Drosophila."; RL Mol. Biol. Evol. 13:191-199(1996). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: IMPLICATED IN SIGMA RHABDOVIRUS MULTIPLICATION AND CC NECESSARY FOR MALE FERTILITY. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- POLYMORPHISM: POLYMORPHIC FOR TWO ALLELIC FORMS IN NATURAL CC POPULATIONS OF DROSOPHILA MELANOGASTER, REF(2)PO AND REF(2)PP. THE CC LATTER ALLELE CONFERS RESISTANCE TO THE RHABDOVIRUS SIGMA CC INFECTING WILD POPULATIONS. CC -!- SIMILARITY: CONTAINS 1 UBA DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ZZ-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16993; CAA34861.1; ALT_SEQ. DR EMBL; X69829; CAA49483.1; -. DR EMBL; X69830; CAA49484.1; -. DR EMBL; U23923; AAA98832.1; -. DR EMBL; U23924; AAA98833.1; -. DR EMBL; U23925; AAA98834.1; -. DR EMBL; U23926; AAA98835.1; -. DR EMBL; U23927; AAA98836.1; -. DR EMBL; U23928; AAA98837.1; -. DR EMBL; U23929; AAA98838.1; -. DR EMBL; U23931; AAA98839.1; -. DR EMBL; U23932; AAA98840.1; -. DR EMBL; U23933; AAA98841.1; -. DR EMBL; AE003663; AAF53824.1; -. DR PIR; S06785; S06785. DR FlyBase; FBgn0003231; ref(2)P. DR InterPro; IPR000270; OPR_PB1. DR InterPro; IPR000449; UBA_domain. DR InterPro; IPR000433; Znf_ZZ. DR Pfam; PF00564; PB1; 1. DR Pfam; PF00569; ZZ; 1. DR SMART; SM00165; UBA; 1. DR SMART; SM00291; ZnF_ZZ; 1. DR PROSITE; PS50030; UBA; 1. DR PROSITE; PS01357; ZF_ZZ_1; 1. DR PROSITE; PS50135; ZF_ZZ_2; 1. KW Zinc-finger; DNA-binding; Metal-binding; Nuclear protein; Repeat; KW Polymorphism. FT DOMAIN 51 80 OPR. FT ZN_FING 121 167 ZZ-TYPE. FT DOMAIN 550 595 UBA. FT DOMAIN 386 413 3 X 8 AA REPEATS OF S-A-N-Q-S-X-X-P. FT REPEAT 386 393 1. FT REPEAT 399 406 2. FT REPEAT 407 413 3. FT VARIANT 28 29 QN -> G (IN STRAIN FLORIDA1SLOW). FT VARIANT 32 32 I -> A (IN STRAINS AFRICAFAST AND FT WASHINGTONFAST). FT VARIANT 32 32 I -> M (IN STRAIN JAPANSLOW). FT VARIANT 32 32 I -> V (IN STRAINS FLORIDAFAST AND FT FLORIDA1SLOW). FT VARIANT 43 43 Q -> L (IN STRAINS AFRICAFAST, FT FLORIDAFAST, FLORIDA1SLOW, JAPANSLOW AND FT WASHINGTONFAST). FT VARIANT 60 60 D -> Y (IN STRAIN WASHINGTONFAST). FT VARIANT 231 231 T -> S (IN STRAIN FRENCHSLOW). FT VARIANT 331 331 S -> R (IN STRAINS AFRICASLOW, FT AFRICAFAST, FLORIDAFAST, FLORIDA1SLOW, FT FLORIDA2SLOW, FRENCHSLOW, FRENCHFAST, FT JAPANSLOW, JAPANFAST AND WASHINGTONFAST). FT VARIANT 397 397 P -> S (IN STRAIN FRENCHSLOW). FT VARIANT 403 410 MISSING (IN STRAINS AFRICAFAST, FT FLORIDAFAST, FLORIDA1SLOW, FLORIDA2SLOW FT AND WASHINGTONFAST). FT VARIANT 432 432 K -> M (IN STRAIN FRENCHFAST). FT VARIANT 542 542 D -> E (IN STRAINS AFRICASLOW, FT AFRICAFAST, FLORIDAFAST, FLORIDA1SLOW, FT FLORIDA2SLOW, FRENCHSLOW, JAPANSLOW AND FT WASHINGTONFAST). FT VARIANT 575 575 T -> S. FT CONFLICT 188 188 R -> S (IN REF. 1). FT CONFLICT 258 292 AAEQTESPPQAEPTVTAEKAAESEAKPTEPKKVNT -> FT LQNKLKVLHKLSPLLPLKRQLNPRPNQLSRRRLTP (IN FT REF. 1). SQ SEQUENCE 599 AA; 65303 MW; 946043CE19AAF126 CRC64; MPEKLLKITY QGAGPQKKIN AYLRMPSQNY TILRREIELY LFQERQLPKC DVRTFWIDAD KDEIEIVNQN DYEIFLAKCE SNMHVQVAPL APVEEPKATK QEGSSANAEA PSVDDPSNFT IHDAVECDGC GLAPLIGFRY KCVQCSNYDL CQKCELAHKH PEHLMLRMPT NNGPGMVDAW FTGPGLGRRS GRRSRGHCPF QETNQADPAG EPARDSRRER RQARRHAGVL TQFVEMMTNL PLNTTTATAP AEPQKPKAAE QTESPPQAEP TVTAEKAAES EAKPTEPKKV NTDQSVPRTE DPVTTPRSTQ PTTPVINLDN ISQIVPPEYM SAGIEILNNF SEMFSKIIDT TEGGDSGIFA PSTTPSAENK KPEEQGQSSG QSGASSANQS AVPSAAPSAN QSNVPSANQS ATPSISGSIP DAQLETEPLN PKPSETTTET EQERRRSDSL DPEWQLIDNA YSANNSNLIN LDTTNPTAAP QEPVRDFGQL GELLRQHMNE EARVEQASAN TQTAQVDTVS TSTSTTSVTT NSVGTSPAAP DDKRTVPVYH TDESINKSIH AMMAMGFSNE GAWLTQLLES VQGNISAALD VMNVSQNRN // ID RFA1_DROME STANDARD; PRT; 603 AA. AC Q24492; Q9VHU3; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Replication protein A 70 kDa DNA-binding subunit (RP-A) (RF-A) DE (Replication factor-A protein 1) (Single-stranded DNA-binding DE protein) (DmRPA1). GN RPA-70 OR RPA1 OR CG9633. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RA Perdigao J., Logarinho E., Avides C., Sunkel C.E.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PARTICIPATES IN A VERY EARLY STEP IN DNA REPLICATION. CC RP-A IS A SINGLE-STRANDED DNA-BINDING PROTEIN. CC -!- SUBUNIT: HETEROTRIMER OF 70, 32, AND 14 KDA CHAINS. THE CC DNA-BINDING ACTIVITY MAY RESIDE EXCLUSIVELY ON THE 70 KDA SUBUNIT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: TO OTHER SPECIES RFA2/RPA2. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z70277; CAA94241.1; -. DR EMBL; AE003678; AAF54206.1; -. DR EMBL; AY069331; AAL39476.1; -. DR HSSP; P27694; 1JMC. DR FlyBase; FBgn0010173; RpA-70. DR GO; GO:0005662; C:DNA replication factor A complex; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003697; F:single-stranded DNA binding; IDA. DR GO; GO:0006261; P:DNA dependent DNA replication; IDA. DR InterPro; IPR008994; Nucleic_acid_OB. DR InterPro; IPR007199; Rep-A_N. DR InterPro; IPR004591; Rpa1. DR InterPro; IPR004365; tRNA_anti. DR Pfam; PF04057; Rep-A_N; 1. DR Pfam; PF01336; tRNA_anti; 1. DR TIGRFAMs; TIGR00617; rpa1; 1. KW DNA replication; DNA-binding; Zinc-finger; Nuclear protein. FT ZN_FING 464 486 C4-TYPE (POTENTIAL). SQ SEQUENCE 603 AA; 66624 MW; 6E6E1D5C4FF38A95 CRC64; MVLASLSTGV IARIMHGEVV DAPVLQILAI KKINSAADSE RYRILISDGK YFNSYAMLAS QLNVMQHNGE LEEFTIVQLD KYVTSLVGKD GAGKRVLIIS ELTVVNPGAE VKSKIGEPVT YENAAKQDLA PKPAVTSNSK PIAKKEPSHN NNNNIVMNSS INSGMTHPIS SLSPYQNKWV IKARVTSKSG IRTWSNARGE GKLFSMDLMD ESGEIRATAF KEQCDKFYDL IQVDSVYYIS KCQLKPANKQ YSSLNNAYEM TFSGETVVQL CEDTDDDPIP EIKYNLVPIS DVSGMENKAA VDTIGICKEV GELQSFVART TNKEFKKRDI TLVDMSNSAI SLTLWGDDAV NFDGHVQPVI LVKGTRINEF NGGKSLSLGG GSIMKINPDI PEAHKLRGWF DNGGGDSVAN MVSARTGGGS FSTEWMTLKD ARARNLGSGD KPDYFQCKAV VHIVKQENAF YRACPQSDCN KKVVDEGNDQ FRCEKCNALF PNFKYRLLIN MSIGDWTSNR WVSSFNEVGE QLLGHTSQEV GEALENDPAK AEQIFSALNF TSHIFKLRCK NEVYGDMTRN KLTVQSVAPI NHKEYNKHLL KELQELTGIG SSN // ID RFC1_DROME STANDARD; PRT; 986 AA. AC P35600; O02031; DT 01-JUN-1994 (Rel. 29, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Activator 1 140 kDa subunit (Replication factor C large subunit) DE (Germline transcription factor 1). GN GNF1 OR CG1119. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DNA-BINDING ACTIVITY. RX MEDLINE=98371221; PubMed=9705493; RA Allen B.L., Uhlmann F., Gaur L.K., Mulder B.A., Posey K.L., RA Jones L.B., Hardin S.H.; RT "DNA recognition properties of the N-terminal DNA binding domain RT within the large subunit of replication factor C."; RL Nucleic Acids Res. 26:3877-3882(1998). RN [2] RP SEQUENCE FROM N.A. RA Frank L.H., Cohen R.S.; RT "Cloning and characterization of a putative transcription factor RT active during oogenesis and embryogenesis."; RL Submitted (XXX-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP INTERACTION WITH PCNA. RX MEDLINE=97153138; PubMed=8999859; RA Mossi R., Jonsson Z.O., Allen B.L., Hardin S.H., Hubscher U.; RT "Replication factor C interacts with the C-terminal side of RT proliferating cell nuclear antigen."; RL J. Biol. Chem. 272:1769-1776(1997). CC -!- FUNCTION: THE ELONGATION OF PRIMED DNA TEMPLATES BY DNA POLYMERASE CC DELTA AND EPSILON REQUIRES THE ACTION OF THE ACCESSORY PROTEINS CC PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) AND ACTIVATOR 1. SUBUNIT CC 2 BINDS TO THE PRIMER-TEMPLATE JUNCTION (BY SIMILARITY). CC -!- SUBUNIT: INTERACTS WITH C-TERMINUS OF PCNA. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE ACTIVATOR 1 140 KDA SUBUNIT FAMILY. CC -!- SIMILARITY: CONTAINS 1 BRCT DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L17340; AAA28573.1; -. DR EMBL; U97685; AAB58311.1; -. DR EMBL; AE003604; AAF52082.1; -. DR FlyBase; FBgn0004913; Gnf1. DR GO; GO:0005663; C:DNA replication factor C complex; NAS. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0006260; P:DNA replication; NAS. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR001357; BRCT. DR InterPro; IPR000862; RFCdomain. DR Pfam; PF00004; AAA; 1. DR Pfam; PF00533; BRCT; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00292; BRCT; 1. DR PROSITE; PS50172; BRCT; 1. KW DNA replication; ATP-binding; Transcription regulation; DNA-binding; KW Activator; Nuclear protein; Zinc-finger. FT DOMAIN 232 313 BRCT. FT NP_BIND 487 494 ATP (BY SIMILARITY). FT ZN_FING 585 602 C2HC-TYPE (POTENTIAL). FT DOMAIN 955 959 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT CONFLICT 559 559 G -> A (IN REF. 2). SQ SEQUENCE 986 AA; 108614 MW; A1E9C8EE0879545F CRC64; MQRGIDSFFK RLPAKAKSAE AENGETPSKA PKRRKAVIIS SDEDEVVSPP ETKKRKASKT ASSEDDVVAA TPEPIAKKAR NGQKPALSKL KRHVDPTELF GGETKRVIVP KPKTKAVLEF ENEDIDRSLM EVDLDESIKE AAPEKKVHSI TRSSPSPKRA KNSSPEPPKP KSTKSKATTP RVKKEKPAAD LESSVLTDEE RHERKRASAV LYQKYKNRSS CLNPGSKEIP KGSPDCLSGL TFVVTGVLES MEREEAESVI KEYGGKVMTV VGKKLKYLVV GEEAGPKKLA VAEELNIPIL SEDGLFDLIR EKSGIAKQVK EEKKSPKKEH SSEEKGKKEV KTSRRSSDKK EKEATKLKYG EKHDIAKHKV KEEHTSPKET KDKLNDVPAV TLKVKKEPSS QKEHPPSPRT ADLKTLDVVG MAWVDKHKPT SIKEIVGQAG AASNVTKLMN WLSKWYVNHD GNKKPQRPNP WAKNDDGSFY KAALLSGPPG IGKTTTATLV VKELGFDAVE FNASDTRSKR LLKDEVSTLL SNKSLSGYFT GQGQAVSRKH VLIMDEVDGM AGNEDRGGMQ ELIALIKDSS IPIICMCNDR NHPKIRSLVN YCYDLRFQRP RLEQIKGKIM SICFKEKVKI SPAKVEEIIA ATNNDIRQSI NHIALLSAKE DASQKSGQQV ATKDLKLGPW EVVRKVFTAD EHKHMSFADK SDLFFHDYSL APLFVQQNYL QVLPQGNKKD VLAKVAATAD ALSLGDLVEK RIRANSAWSL LPTQAFFSSV LPGEHMCGHF TGQINFPGWL GKNSKSGKRA RLAQELHDHT RVCTSGSRLS VRLDYAPFLL DNIVRPLAKD GQEGVPAALD VMKDYHLLRE DLDSLVELTS WPGKKSPLDA VDGRVKAALT RSYNKEVMAY SYSAQAGIKK KKSEAAGADD DYLDEGPGEE DGAGGHLSSE EDEDKDNLEL DSLIKAKKRT TTSKASGGSK KATSSTASKS KAKAKK // ID RFC2_DROME STANDARD; PRT; 331 AA. AC P53034; Q9VZH9; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Activator 1 40 kDa subunit (Replication factor C 40 kDa subunit) (A1 DE 40 kDa subunit) (RF-C 40 kDa subunit) (RFC40). GN RFC40 OR CG14999. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1 / Kennison; RX MEDLINE=95309683; PubMed=7789770; RA Harrison S.D., Solomon N., Rubin G.M.; RT "A genetic analysis of the 63E-64A genomic region of Drosophila RT melanogaster: identification of mutations in a replication factor C RT subunit."; RL Genetics 139:1701-1709(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE ELONGATION OF PRIMED DNA TEMPLATES BY DNA POLYMERASE CC DELTA AND EPSILON REQUIRES THE ACTION OF THE ACCESSORY PROTEINS CC PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) AND ACTIVATOR 1. SUBUNIT CC 2 BINDS ATP (BY SIMILARITY). CC -!- SUBUNIT: HETEROPENTAMER OF SUBUNITS OF 140/145, 40, 38, 37, AND CC 36.5 KDA THAT FORMS A COMPLEX WITH PCNA IN THE PRESENCE OF ATP (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE ACTIVATOR 1 SMALL SUBUNITS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U15967; AAB60241.1; -. DR EMBL; AE003480; AAF47843.1; -. DR PIR; S55020; S55020. DR FlyBase; FBgn0015287; RfC40. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR GO; GO:0007067; P:mitosis; IMP. DR GO; GO:0007076; P:mitotic chromosome condensation; IMP. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR008921; Pol_clamp_load_C. DR InterPro; IPR000862; RFCdomain. DR SMART; SM00382; AAA; 1. KW DNA replication; ATP-binding; Nuclear protein. FT NP_BIND 56 63 ATP (POTENTIAL). SQ SEQUENCE 331 AA; 37173 MW; 0ACE1C6DCBA8AF8F CRC64; MPEEPEKTAD DKRSHLPWIE KYRPVKFKEI VGNEDTVARL SVFATQGNAP NIIIAGPPGV GKTTTIQCLA RILLGDSYKE AVLELNASNE RGIDVVRNKI KMFAQQKVTL PRGRHKIVIL DEADSMTEGA QQALRRTMEI YSSTTRFALA CNTSEKIIEP IQSRCAMLRF TKLSDAQVLA KLIEVAKWEK LNYTEDGLEA IVFTAQGDMR QGLNNLQSTA QGFGDITAEN VFKVCDEPHP KLLEEMIHHC AANDIHKAYK ILAKLWKLGY SPEDIIANIF RVCKRINIDE HLKLDFIREI GITHMKIIDG INSLLQLTAL LAKLCIAAEK H // ID RG84_DROME STANDARD; PRT; 384 AA. AC P40809; Q9VI91; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GTPase activating protein RacGAP84C (Rotund RacGAP protein). GN RACGAP84C OR RNRACGAP OR CG2595. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=Oregon-R; TISSUE=Pupae; RX MEDLINE=93024458; PubMed=1406685; RA Agnel M., Roeder L., Vola C., Griffin-Shea R.; RT "A Drosophila rotund transcript expressed during spermatogenesis and RT imaginal disc morphogenesis encodes a protein which is similar to RT human Rac GTPase-activating (racGAP) proteins."; RL Mol. Cell. Biol. 12:5111-5122(1992). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=96194886; PubMed=8654933; RA Hoemann C.D., Bergeret E., Guichard A., Griffin-Shea R.; RT "Alternative splicing of the Drosophila melanogaster rotundRacGAP RT gene."; RL Gene 168:135-141(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: INVOLVED IN THE MORPHOGENESIS OF THE ADULT APPENDAGES. CC GTPASE-ACTIVATING PROTEIN FOR P21-RAC. PROMOTES THE EXCHANGE OF CC RAC-BOUND GDP BY GTP. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P40809-1; Sequence=Displayed; CC Name=2; CC IsoId=P40809-2; Sequence=VSP_001821; CC -!- TISSUE SPECIFICITY: IN PUPAE, EXPRESSED IN IMAGINAL DISKS AND ONLY CC IN THE MALE GONAD. IN ADULTS, ONLY FOUND IN THE TESTES, IN REGIONS CC FILLED WITH PRIMARY SPERMATOCYTES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING SPERMATOGENESIS, IN PRIMARY CC SPERMATOCYTES, AND IMAGINAL DISK MORPHOGENESIS. CC -!- SIMILARITY: CONTAINS 1 RHO-GAP DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ZINC-DEPENDENT PHORBOL-ESTER AND DAG CC BINDING DOMAIN. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-23 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M99702; AAA16480.2; -. DR EMBL; U22539; AAC47075.1; -. DR EMBL; U22539; AAC47076.1; -. DR EMBL; AE003672; AAF54034.1; -. DR EMBL; AE003672; AAN13349.1; -. DR PIR; A48122; A48122. DR FlyBase; FBgn0045843; RacGAP84C. DR GO; GO:0005096; F:GTPase activator activity; IDA. DR InterPro; IPR002219; DAG_PE-bind. DR InterPro; IPR008936; Rho_GAP. DR InterPro; IPR000198; RhoGAP. DR Pfam; PF00130; DAG_PE-bind; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00324; RhoGAP; 1. DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 1. DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 1. DR PROSITE; PS50238; RHOGAP; 1. KW Guanine-nucleotide releasing factor; Spermatogenesis; Testis; KW Alternative splicing; Zinc; Phorbol-ester binding. FT DOMAIN 87 136 PHORBOL-ESTER AND DAG BINDING. FT DOMAIN 147 330 RHO-GAP. FT VARSPLIC 378 384 NLSSTHL -> RPMVSL (in isoform 2). FT /FTId=VSP_001821. SQ SEQUENCE 384 AA; 44217 MW; D24959B833B7A2A8 CRC64; MISGSGSRTP SNRLYLSPVR PTMQNKRRLL REYRSYDDLS EHYRMFGSQS LDSLQDRVDM NPSGCDGLST DGLDFCSQSH SGLLREHNFK IKSYYYNVGN CVHCRKRIRF AMASLRCRAC PLRCHIGCCR QLTVNCIPQP QIGTKRGCLS DYAPRVAPMV PALIVHCVTE IEARGLQQEG LYRVSSTREK CKRLRRKLLR GKSTPHLGNK DTHTLCCCVK DFLRQLVHPL IPIYHRRDFE EATRHEDRLA VEMAVYLAVL ELHQAHRDTL AYLMLHWQKI AESPAVRMTV NNLAVIFAPT LFGDLDLTLE NVVTWQRVLK VLLLMPAGFW SQFLEVHPLP TSLGSTYDFE DRYNHRHWDS SSNLGWSSVK TYFRSMVNLS STHL // ID RGP1_DROME STANDARD; PRT; 596 AA. AC Q9VIW3; Q9XZI5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ran GTPase-activating protein (RanGAP) (Segregation distorter DE protein). GN SD OR CG9999. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Testis; RX MEDLINE=99174089; PubMed=10073941; RA Merrill C., Bayraktaroglu L., Kusano A., Ganetzky B.; RT "Truncated RanGAP encoded by the Segregation Distorter locus of RT Drosophila."; RL Science 283:1742-1745(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: GTPASE ACTIVATOR FOR THE NUCLEAR RAS-RELATED REGULATORY CC PROTEIN RAN, CONVERTING IT TO THE PUTATIVELY INACTIVE GDP-BOUND CC STATE (BY SIMILARITY). TRANS-ACTING FACTOR NECESSARY FOR MEIOTIC CC DISTORTION. DISTORTION IS ONLY SEEN IN INDIVIDUALS THAT CARRY THE CC SD TANDEM DUPLICATION AND EXPRESS AN SD TRUNCATED PROTEIN. BINDING CC OF TRUNCATED SD PRODUCT TO THE RSP LOCUS INITIATES EVENTS THAT CC LEAD TO SPERM DYSFUNCTION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: BOTH FULL LENGTH AND TRUNCATED PROTEIN ARE CC EXPRESSED IN TESTES. CC -!- SIMILARITY: CONTAINS 6 LEUCINE-RICH (LRR) REPEATS. CC -!- SIMILARITY: TO FUNGAL RNA1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF143860; AAD31518.1; -. DR EMBL; AE003663; AAF53801.1; -. DR EMBL; AY061219; AAL28767.1; -. DR HSSP; P41391; 1YRG. DR FlyBase; FBgn0003346; Sd. DR GO; GO:0005098; F:Ran GTPase activator activity; IDA. DR InterPro; IPR001611; LRR. DR InterPro; IPR007091; LRR_RNinh. DR Pfam; PF00560; LRR; 3. KW GTPase activation; Repeat; Leucine-rich repeat. FT REPEAT 44 71 LRR 1. FT REPEAT 107 134 LRR 2. FT REPEAT 137 164 LRR 3. FT REPEAT 203 230 LRR 4. FT REPEAT 231 258 LRR 5. FT REPEAT 259 286 LRR 6. FT DOMAIN 357 409 ASP/GLU-RICH (HIGHLY ACIDIC). FT CONFLICT 117 117 D -> E (IN REF. 1). SQ SEQUENCE 596 AA; 66069 MW; 257C9783E23464CD CRC64; MSTFNFASMA AQLGQEQGIS FENKVLSWNT AADVQDVVDA LNKQTTVHYL NLDGNTLGVE AAKAIGEGLK RHPEFRKALW KNMFTGRLIS EIPEALKHLG AALIVAGAKL TVLDLSDNAL GPNGMRGLEE LLRSPVCYSL QELLLCNCGL GPEGGSMLSR ALIDLHANAN KAGFPLQLRV FIGSRNRLED AGATEMATAF QTLKTFEEIV LEQNSIYIEG VEALAESFKH NPHLRVLNMN DNTLKSEGAE KIAEALPFLP LLREMSFGDC LIKTNGAYHF GEALERGNER LEVIDLGFNE INSDGGLVLV NAMGNKPKLR ILNLDGNSFG EEGSEKIISE MSKLPTAAAL QPFQHQEEED LEDEYQADKQ DADYEEEEEV HEHANDTTEE ADEDSEGDED DEEDEGDEEY SNVAEETAYV TTNAYTTKLF NDTTNSMASE TFAVANKTIS QKCTPEKFCL SQKPCSQEDF DSLDMDNKLE ALQSIVNQFT GDNHLLLLVF TTLKCAHLSQ SSKAALDLAV SLYQATFDYA IKTKQETRVL NYVLMQLRLL PCKEVFHSDY DVKNCRFALR EALKQPTFAN DNIKNSFKTF LEGAES // ID RHEB_DROME STANDARD; PRT; 182 AA. AC Q9VND8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GTP-binding protein Rheb homolog. GN RHEB OR CG1081. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: NOT KNOWN; BINDS GTP AND EXHIBITS INTRINSIC GTPASE CC ACTIVITY (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RHEB FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003602; AAF52005.3; -. DR EMBL; AY094697; AAM11050.1; -. DR HSSP; P01112; 1PLL. DR FlyBase; FBgn0041191; Rheb. DR InterPro; IPR003577; GTPase_Ras. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00173; RAS; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein. FT NP_BIND 12 19 GTP (BY SIMILARITY). FT NP_BIND 59 63 GTP (BY SIMILARITY). FT NP_BIND 118 121 GTP (BY SIMILARITY). FT DOMAIN 34 42 EFFECTOR REGION (BY SIMILARITY). FT LIPID 179 179 S-farnesyl cysteine (By similarity). SQ SEQUENCE 182 AA; 20731 MW; CAB8AE2A988A0179 CRC64; MPTKERHIAM MGYRSVGKSS LCIQFVEGQF VDSYDPTIEN TFTKIERVKS QDYIVKLIDT AGQDEYSIFP VQYSMDYHGY VLVYSITSQK SFEVVKIIYE KLLDVMGKKY VPVVLVGNKI DLHQERTVST EEGKKLAESW RAAFLETSAK QNESVGDIFH QLLILIENEN GNPQEKSGCL VS // ID RHO1_DROME STANDARD; PRT; 192 AA. AC P48148; Q9V3J0; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Ras-like GTP-binding protein Rho1. GN RHO1 OR CG8416. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95137009; PubMed=7835340; RA Hariharan I.K., Hu K.-Q., Asha H., Quintanilla A., Ezzell R.M., RA Settleman J.; RT "Characterization of rho GTPase family homologues in Drosophila RT melanogaster: overexpressing Rho1 in retinal cells causes a late RT developmental defect."; RL EMBO J. 14:292-302(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=20025934; PubMed=10556060; RA Magie C.R., Meyer M.R., Gorsuch M.S., Parkhurst S.M.; RT "Mutations in the Rho1 small GTPase disrupt morphogenesis and RT segmentation during early Drosophila development."; RL Development 126:5353-5364(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RHO FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L38311; AAA67042.1; -. DR EMBL; AF177871; AAF01183.1; -. DR EMBL; AF177872; AAF01184.1; -. DR EMBL; AF177873; AAF01185.1; -. DR EMBL; AF177874; AAF01186.1; -. DR EMBL; AE003808; AAF58066.1; -. DR EMBL; AY119536; AAM50190.1; -. DR EMBL; BT010085; AAQ22554.1; -. DR PIR; S54294; S54294. DR HSSP; P06749; 1FTN. DR FlyBase; FBgn0014020; Rho1. DR GO; GO:0003924; F:GTPase activity; NAS. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0007164; P:establishment of tissue polarity; NAS. DR GO; GO:0007369; P:gastrulation; NAS. DR GO; GO:0007254; P:JNK cascade; NAS. DR GO; GO:0046663; P:leading edge cell differentiation; IMP. DR GO; GO:0007405; P:neuroblast proliferation; IMP. DR GO; GO:0016318; P:ommatidial rotation; NAS. DR GO; GO:0007395; P:spreading of leading edge cells; IMP. DR InterPro; IPR003578; GTPase_Rho. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00174; RHO; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein. FT NP_BIND 12 19 GTP (BY SIMILARITY). FT NP_BIND 59 63 GTP (BY SIMILARITY). FT NP_BIND 117 120 GTP (BY SIMILARITY). FT DOMAIN 34 42 EFFECTOR REGION (POTENTIAL). FT LIPID 189 189 S-geranylgeranyl cysteine FT (By similarity). SQ SEQUENCE 192 AA; 21723 MW; B89C7D884E1743CF CRC64; MTTIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD LRNDPNTIRD LAKMKQEPVK PQEGRAMAEK INAFAYLECS AKSKEGVRDV FETATRAALQ VKKRKKTRCL LL // ID RHOL_DROME STANDARD; PRT; 190 AA. AC Q24192; Q9VHC9; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-like GTP-binding protein RhoL. GN RHOL OR CG9366. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96222365; PubMed=8636236; RA Murphy A.M., Montell D.J.; RT "Cell type-specific roles for Cdc42, Rac, and RhoL in Drosophila RT oogenesis."; RL J. Cell Biol. 133:617-630(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT ALL STAGES OF DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE SMALL GTPASE SUPERFAMILY. RHO FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U50314; AAB05666.1; -. DR EMBL; AE003683; AAF54385.1; -. DR HSSP; P21181; 1AM4. DR FlyBase; FBgn0014380; RhoL. DR InterPro; IPR003578; GTPase_Rho. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00174; RHO; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Prenylation; Lipoprotein. FT NP_BIND 18 25 GTP (BY SIMILARITY). FT NP_BIND 65 69 GTP (BY SIMILARITY). FT NP_BIND 123 126 GTP (BY SIMILARITY). FT DOMAIN 40 48 EFFECTOR REGION (POTENTIAL). FT LIPID 187 187 S-geranylgeranyl cysteine FT (By similarity). SQ SEQUENCE 190 AA; 21880 MW; 9E35F487F7445184 CRC64; MTANITKSPR PLKITIVGDG MVGKTCMLIT YTRNEFPEEY IPTVFDNHAC NIAVDDRDYN LTLWDTAGQE DYERLRPLSY PSTNCFLLCY SISSRTSFEN VKSKWWPEIR HFSAHVPVVL VGTKLDLRIP NSEKFVTTQE GKKMRKEIHA FNLVECSAKK KQNLQQVFEE AVRAVERKPK TTSKQSCKIL // ID RHOM_DROME STANDARD; PRT; 355 AA. AC P20350; Q9W0F2; DT 01-FEB-1991 (Rel. 17, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Rhomboid protein (EC 3.4.21.-) (Veinlet protein). GN RHO OR VE OR CG1004. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90249726; PubMed=2110920; RA Bier E., Jan L.Y., Jan Y.N.; RT "Rhomboid, a gene required for dorsoventral axis establishment and RT peripheral nervous system development in Drosophila melanogaster."; RL Genes Dev. 4:190-203(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION, AND MUTAGENESIS OF TRP-151; ARG-152; ASN-169; GLY-215; RP SER-217 AND HIS-281. RX MEDLINE=21526629; PubMed=11672525; RA Urban S., Lee J.R., Freeman M.; RT "Drosophila Rhomboid-1 defines a family of putative intramembrane RT serine proteases."; RL Cell 107:173-182(2001). CC -!- FUNCTION: ACTS EARLY IN EMBRYONIC DEVELOPMENT TO ESTABLISH CC POSITION ALONG THE DORSOVENTRAL AXIS AND THEN AGAIN LATER TO CC SPECIFY THE FATE OF NEURONAL PRECURSOR CELLS. INVOLVED IN EGF CC RECEPTOR SIGNALING; CLEAVES SPITZ TO RELEASE THE ACTIVE GROWTH CC FACTOR. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. GOLGI. CC -!- DEVELOPMENTAL STAGE: EARLY BLASTODERM STAGES AND LATER DURING CC NERVOUS DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S54. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52454; CAA36692.1; -. DR EMBL; AE003471; AAF47496.1; -. DR PIR; A34597; A34597. DR MEROPS; S54.001; -. DR FlyBase; FBgn0004635; rho. DR GO; GO:0005794; C:Golgi apparatus; IDA. DR GO; GO:0008236; F:serine-type peptidase activity; IDA. DR GO; GO:0007174; P:EGF receptor ligand processing; IGI. DR GO; GO:0007438; P:oenocyte development; IGI. DR GO; GO:0006508; P:proteolysis and peptidolysis; IGI. DR GO; GO:0007432; P:salivary gland determination; NAS. DR InterPro; IPR002610; Peptidase_S54. DR Pfam; PF01694; Rhomboid; 1. KW Hydrolase; Protease; Serine protease; Developmental protein; KW Transmembrane; Golgi stack. FT DOMAIN 1 98 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 99 119 POTENTIAL. FT DOMAIN 120 162 LUMENAL (POTENTIAL). FT TRANSMEM 163 183 POTENTIAL. FT DOMAIN 184 188 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 189 209 POTENTIAL. FT DOMAIN 210 210 LUMENAL (POTENTIAL). FT TRANSMEM 211 231 POTENTIAL. FT DOMAIN 232 244 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 245 265 POTENTIAL. FT DOMAIN 266 275 LUMENAL (POTENTIAL). FT TRANSMEM 276 296 POTENTIAL. FT DOMAIN 297 308 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 309 329 POTENTIAL. FT DOMAIN 330 355 LUMENAL (POTENTIAL). FT ACT_SITE 169 169 CHARGE RELAY SYSTEM. FT ACT_SITE 217 217 CHARGE RELAY SYSTEM. FT ACT_SITE 281 281 CHARGE RELAY SYSTEM. FT MUTAGEN 151 151 W->A: ABOLISHES PROTEASE ACTIVITY. FT MUTAGEN 152 152 R->A: ABOLISHES PROTEASE ACTIVITY. FT MUTAGEN 169 169 N->A: ABOLISHES PROTEASE ACTIVITY. FT MUTAGEN 215 215 G->A: ABOLISHES PROTEASE ACTIVITY. FT MUTAGEN 217 217 S->C,T: ABOLISHES PROTEASE ACTIVITY. FT MUTAGEN 281 281 H->A: ABOLISHES PROTEASE ACTIVITY. FT CONFLICT 4 4 L -> P (IN REF. 1). FT CONFLICT 33 33 A -> V (IN REF. 1). FT CONFLICT 46 46 S -> T (IN REF. 1). SQ SEQUENCE 355 AA; 39330 MW; 2E0572D08831C5D0 CRC64; MENLTQNVNE TKVDLGQEKE KEASQEEEHA TAAKETIIDI PAACSSSSNS SSYDTDCSTA SSTCCTRQGE HIYMQREAIP ATPLPESEDI GLLKYVHRQH WPWFILVISI IEIAIFAYDR YTMPAQNFGL PVPIPSDSVL VYRPDRRLQV WRFFSYMFLH ANWFHLGFNI VIQLFFGIPL EVMHGTARIG VIYMAGVFAG SLGTSVVDSE VFLVGASGGV YALLAAHLAN ITLNYAHMKS ASTQLGSVVI FVSCDLGYAL YTQYFDGSAF AKGPQVSYIA HLTGALAGLT IGFLVLKNFG HREYEQLIWW LALGVYCAFT VFAIVFNLIN TVTAQLMEEQ GEVITQHLLH DLGVS // ID RIR1_DROME STANDARD; PRT; 812 AA. AC P48591; Q9UB08; Q9VKZ3; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ribonucleoside-diphosphate reductase M1 chain (EC 1.17.4.1) DE (Ribonucleotide reductase large chain). GN RNRL OR CG5371. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [4] RP SEQUENCE OF 164-343 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94326648; PubMed=8050359; RA Duronio R.J., O'Farrell P.H.; RT "Developmental control of a G1-S transcriptional program in RT Drosophila."; RL Development 120:1503-1515(1994). CC -!- FUNCTION: PROVIDES THE PRECURSORS NECESSARY FOR DNA SYNTHESIS. CC -!- CATALYTIC ACTIVITY: 2'-DEOXYRIBONUCLEOSIDE DIPHOSPHATE + OXIDIZED CC THIOREDOXIN + H(2)O = RIBONUCLEOSIDE DIPHOSPHATE + REDUCED CC THIOREDOXIN. CC -!- PATHWAY: DNA REPLICATION PATHWAY; FIRST STEP. CC -!- SUBUNIT: HETERODIMER OF A LARGE AND A SMALL CHAIN. CC -!- SIMILARITY: BELONGS TO THE RIBONUCLEOSIDE DIPHOSPHATE REDUCTASE CC LARGE CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003628; AAF52913.2; -. DR EMBL; AF132143; AAD33590.1; -. DR EMBL; AY119149; AAM51009.1; -. DR EMBL; U09369; AAA56995.1; -. DR HSSP; P00452; 5R1R. DR FlyBase; FBgn0011703; RnrL. DR InterPro; IPR005144; ATP. DR InterPro; IPR000788; Ribonucleo_red. DR InterPro; IPR008926; Ribonucleo_red_N. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF00317; ribonuc_red_lg; 1. DR Pfam; PF02867; ribonuc_red_lgC; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR PROSITE; PS00089; RIBORED_LARGE; 1. KW Oxidoreductase; DNA replication. SQ SEQUENCE 812 AA; 91978 MW; 6E4FC608AC04A5FD CRC64; MLKNKSMKTS KLYVIKRDGR QEEVHFDKIT SRIQKLCYNL NMDFVDPVTI TLQVINGLYC GVTTQELDNL AAEIAAGLTC NHPDYAILAA RIAVSNLHKE TKKAFSDVFE DLYNHVNKET NQKVPLVSEF HYNVVKKNAT RLNSSIIYDR DFGYNYFGFK TLERSYLLKR NGKIAERPQH MLMRVAIGIH GEDIDAAVET YNLLSERYFT HASPTLFAAA TNRPQLSSCF LLTMTADSIE GIFKSVEQCA MISKSAGGIG LNVHCIRAKG TSICGTNGTS NGLVPMLRVF NNVARYVDQG GGKRPGAFAI YLEPWHSDVF EFLELKKNTG KEENRARDLF YALWIPDLFM KRVEANGDWS LMCPHKCPGL HDVWGDEFEK LYEKYEQEGR ANRTVKAQSL WFAIIEAQVE TGNPYMLFKD ACNRKSNQQN VGTIKCSNLC TEIVEYSAPD EIAVCNLASI ALNMFVTPEK TYDFKKLKEV TKIVTKNLNK IIDINYYPLP EARKSNLRHR PVGIGIQGFA DALILMRFPY ESEEAGLLNQ QIFETIYYGA LEASCELAQT EGPYETYEGS PVSKGILQYD MWDKVPTNLW DWQKLKESIR MHGVRNSLLV APMPTASTAQ IMGNNESFEP YTTNIYTRRV LSGEFQVVNH HLLRDLTELD LWDDDMKNQI ISSRGSIQNI ETIPPKVRDL YKTVWEISVK STIKMAADRG AFIDQSQSFN IHVAEPNYGK LTSIHFYSWK AGLKTGMYYL RTKPAANAIQ FTVNKKQGAV SMNGQNGTAE GSPQKYEEDR ERKMADMVCS LENKDACMSC GS // ID RIR2_DROME STANDARD; PRT; 393 AA. AC P48592; Q9V640; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ribonucleoside-diphosphate reductase M2 chain (EC 1.17.4.1) DE (Ribonucleotide reductase small chain). GN RNRS OR CG8975. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 149-362 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94326648; PubMed=8050359; RA Duronio R.J., O'Farrell P.H.; RT "Developmental control of a G1-S transcriptional program in RT Drosophila."; RL Development 120:1503-1515(1994). CC -!- FUNCTION: PROVIDES THE PRECURSORS NECESSARY FOR DNA SYNTHESIS. CC -!- CATALYTIC ACTIVITY: 2'-DEOXYRIBONUCLEOSIDE DIPHOSPHATE + OXIDIZED CC THIOREDOXIN + H(2)O = RIBONUCLEOSIDE DIPHOSPHATE + REDUCED CC THIOREDOXIN. CC -!- COFACTOR: BINDS 2 IRON IONS PER SUBUNIT (BY SIMILARITY). CC -!- PATHWAY: DNA REPLICATION PATHWAY; FIRST STEP. CC -!- SUBUNIT: HETERODIMER OF A LARGE (M1) AND A SMALL CHAIN (M2). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE RIBONUCLEOSIDE DIPHOSPHATE REDUCTASE CC SMALL CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003824; AAF58599.2; -. DR EMBL; AY051936; AAK93360.1; -. DR EMBL; U09370; AAA56996.1; -. DR HSSP; P11157; 1XSM. DR FlyBase; FBgn0011704; RnrS. DR InterPro; IPR000358; Ribonucl_redctse. DR Pfam; PF00268; ribonuc_red_sm; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. KW Oxidoreductase; DNA replication; Metal-binding; Iron. FT METAL 142 142 IRON 1 (BY SIMILARITY). FT METAL 173 173 IRON 1 AND 2 (BY SIMILARITY). FT METAL 176 176 IRON 1 (BY SIMILARITY). FT METAL 236 236 IRON 2 (BY SIMILARITY). FT METAL 270 270 IRON 2 (BY SIMILARITY). FT METAL 273 273 IRON 2 (BY SIMILARITY). FT ACT_SITE 180 180 BY SIMILARITY. SQ SEQUENCE 393 AA; 45114 MW; 0784173BCF1F6D9A CRC64; MASKENIADN MEKFSLKSPS KKILTDSTNN VRKMSIGHEA NGQLAKESST VNGIGKSANS LMEKSVTPFD PSLEPLLREN PRRFVIFPIQ YHDIWQMYKK AEASFWTVEE VDLSKDLTDW HRLKDDERHF ISHVLAFFAA SDGIVNENLV ERFSQEVQIT EARCFYGFQI AMENVHSEMY SVLIDTYIRD PHQREYLFNA IETMPAVKRK ADWALSWISS KSANFGERII AFAAVEGIFF SGSFASIFWL KKRGLMPGLT FSNELISRDE GLHCDFAVLM FQHLVQRPKR ERIIEIIRDA VAIEQEFLTD ALPVNLIGMN CDLMSQYIEF VADRLLVELG VGKIYNTKNP FNFMEMISLD GKTNFFEKKV GEYQRMGVVS NPLDNVFTLD ADF // ID RL10_DROME STANDARD; PRT; 218 AA. AC O61231; Q86NY2; Q9I813; Q9W5T1; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L10 (QM protein homolog) (dQM). GN RPL10 OR QM OR CG17521. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=CNS; RX MEDLINE=98185501; PubMed=9524813; RA Nguyen-Yue Y.H., Loftus T.M., Torok T., Bryant P., Stanbridge E.J.; RT "The isolation, localization and characterization of the QM homolog RT in Drosophila melanogaster."; RL DNA Seq. 7:337-347(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE L10E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U49721; AAC16108.1; -. DR EMBL; AE002786; AAF45440.1; -. DR EMBL; AY070910; AAL48532.1; -. DR EMBL; BT003580; AAO39584.1; ALT_INIT. DR FlyBase; FBgn0024733; Qm. DR InterPro; IPR001197; Ribosomal_L10E. DR Pfam; PF00826; Ribosomal_L10e; 1. DR TIGRFAMs; TIGR00279; L10e; 1. DR PROSITE; PS01257; RIBOSOMAL_L10E; 1. KW Ribosomal protein. FT CONFLICT 75 101 MISSING (IN REF. 4). SQ SEQUENCE 218 AA; 25527 MW; 2EFC207CEB832BE4 CRC64; MGRRPARCYR YCKNKPYPKS RFCRGVPDPK IRIFDLGRKK ATVEDFPLCV HLVSDEYEQL SSEALEAGRI CCNKYLVKYC GKDQFHIRMR LHPFHVIRIN KMLSCAGADR LQTGMRGAFG KPQGTVARVR IGQPIMSVRS SDRYKAQVIE ALRRAKFKFP GRQKIYVSKK WGFTKYERER YEELRDDNRL EPDGCNVKYR PEHGPIAAWE KAQRDVYA // ID RL11_DROME STANDARD; PRT; 184 AA. AC P46222; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 60S ribosomal protein L11. GN RPL11 OR RPL11A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95200964; PubMed=7893752; RA Larochelle S., Suter B.; RT "Molecular cloning of the Drosophila homologue of the rat ribosomal RT protein L11 gene."; RL Biochim. Biophys. Acta 1261:147-150(1995). CC -!- FUNCTION: PROBABLY ASSOCIATES WITH 5S RNA. CC -!- SIMILARITY: BELONGS TO THE L5P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U15643; AAC46585.1; -. DR PIR; S60245; S60245. DR FlyBase; FBgn0013325; RpL11. DR InterPro; IPR002132; Ribosomal_L5. DR Pfam; PF00281; Ribosomal_L5; 1. DR Pfam; PF00673; Ribosomal_L5_C; 1. DR PROSITE; PS00358; RIBOSOMAL_L5; 1. KW Ribosomal protein; rRNA-binding. SQ SEQUENCE 184 AA; 21084 MW; 31E6422E489F54C1 CRC64; MAAVTKKIKR DPAQEPDEDL HIRKLCLNIC VGESGDRLTR AAKVLEQLTG QQPVFSKARY TVRSFGIRRN EKIAVHCTVR GAKAEEILER GLKVREYELR RENFSSTGNF GFGIQEHIDL GIKYDPSIGI YGLDFYVVLG RPGYNVNHRK RKSGTVGFQH RLTKEDAMKW FQQKYDGIIL NTKK // ID RL13_DROME STANDARD; PRT; 218 AA. AC P41126; Q9VL55; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L13 (BBC1 protein homolog). GN RPL13 OR BBC1 OR CG4651. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Brighton; RX MEDLINE=96032351; PubMed=7557437; RA Helps N.R., Adams S.M., Brammar W.J., Varley J.M.; RT "The Drosophila melanogaster homologue of the human BBC1 gene is RT highly expressed during embryogenesis."; RL Gene 162:245-248(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE L13E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X77926; CAA54898.1; -. DR EMBL; AE003626; AAF52842.1; -. DR PIR; JC4260; JC4260. DR FlyBase; FBgn0011272; RpL13. DR InterPro; IPR001380; Ribosomal_L13E. DR Pfam; PF01294; Ribosomal_L13e; 1. DR ProDom; PD004443; Ribosomal_L13E; 1. DR PROSITE; PS01104; RIBOSOMAL_L13E; 1. KW Ribosomal protein. SQ SEQUENCE 218 AA; 24951 MW; 2DBCF34B2E650A63 CRC64; MGKGNNMIPN QHYHKWWQRH VKTWFNQPAR KVRRHANRVK KAKAVFPRPA SGALRPVVRC PTIRYHTKLR AGRGFTLEEL KGAGIGANFA KTIGIAVDRR RKNKSLESRQ RNIQRLKEYR SKLILFPINE KKIRAGESSL EECKLATQLK GPVLPIKNEQ PAVVEFREVT KDEKKFKAFA TLRKARTDAR LVGIRAKRAK EAAESEDAAK GDPKKAKK // ID RL14_DROME STANDARD; PRT; 166 AA. AC P55841; Q9VSM3; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L14. GN RPL14 OR CG6253. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Shahrinau; RA Saeboe-Larssen S., Mohebi B., Angel S., Lambertsson A.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Ovary; RA Haynes S.R.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE L14E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y10015; CAA71121.1; -. DR EMBL; Y10017; CAA71124.1; -. DR EMBL; Y09766; CAA70905.1; -. DR EMBL; AE003555; AAF50393.1; -. DR FlyBase; FBgn0017579; RpL14. DR InterPro; IPR005824; KOW. DR InterPro; IPR002784; Ribosomal_L14e. DR Pfam; PF00467; KOW; 1. DR Pfam; PF01929; Ribosomal_L14e; 1. KW Ribosomal protein. SQ SEQUENCE 166 AA; 19173 MW; 8600358A902E6A67 CRC64; MPFERFVQTG RIAKASAGPL KGRLVAIVDV IDQNRVLVDG PLTGVPRQEY RLNNLHLTKY RIKFPYTAPT RIVRKAWTES DLKAQWKVSP WSVKAQNICK RSSLNDFDRF KLRYAKRQRN KLLTIAFNTL KKRTKADGTP RVLKKDRRER LRAEKAKGGK KAAAKK // ID RL15_DROME STANDARD; PRT; 204 AA. AC O17445; Q9W5N1; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L15. GN RPL15 OR ZITI OR CG17420. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Inaguma Y., Joanisse D.R., Tanguay R.M.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). CC -!- SIMILARITY: BELONGS TO THE L15E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF030251; AAB84223.1; -. DR FlyBase; FBgn0028697; RpL15. DR InterPro; IPR000439; Ribosomal_L15e. DR Pfam; PF00827; Ribosomal_L15e; 1. DR PROSITE; PS01194; RIBOSOMAL_L15E; 1. KW Ribosomal protein. SQ SEQUENCE 204 AA; 24325 MW; BEB765555EB80EAC CRC64; MGAYRYMQEL YRKKQSDVMR YLLRIRVWQY RQLTKLHRSP RPTRPDKARR LGYRAKQGFV IYRIRVRRGG RKRPVPKGCT YGKPKSHGVN QLKPYRGLQS IAEERVGRRL GGLRVLNSYW IAQDASYKYF EVILIDTHHS AIRRDPKINW ICKHVHKHRE LRGLTSAGKS SRGIGKGYRY SQTIGGSRRA AWKRKNREHM HRKR // ID RL19_DROME STANDARD; PRT; 203 AA. AC P36241; Q9W0X4; DT 01-JUN-1994 (Rel. 29, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L19. GN RPL19 OR M(2)60E OR CG2746. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94128594; PubMed=8297785; RA Hart K., Klein T., Wilcox M.; RT "A Minute encoding a ribosomal protein enhances wing morphogenesis RT mutants."; RL Mech. Dev. 43:101-110(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE L19E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X74776; CAA52784.1; -. DR EMBL; AE003465; AAF47305.1; -. DR EMBL; AY061217; AAL28765.1; -. DR PIR; A61627; A61627. DR FlyBase; FBgn0002607; RpL19. DR InterPro; IPR000196; Ribosomal_L19e. DR Pfam; PF01280; Ribosomal_L19e; 1. DR ProDom; PD004823; Ribosomal_L19e; 1. DR PROSITE; PS00526; RIBOSOMAL_L19E; 1. KW Ribosomal protein. FT CONFLICT 73 73 G -> D (IN REF. 1). FT CONFLICT 100 102 RVL -> PFC (IN REF. 1). SQ SEQUENCE 203 AA; 23998 MW; 0FD89B8545C5C22F CRC64; MSSLKLQKRL AASVLRCGKK KVWLDPNEIN EIANTNSRQN IRKLIKDGLI IKKPVVVHSR YRVRKNTEAR RKGRHCGFGK RKGTANARMP TKLLWMQRQR VLRRLLKKYR DSKKIDRHLY HDLYMKCKGN VFKNKRVLME YIHKKKAEKQ RSKMLADQAE ARRQKVREAR KRREERIATK KQELIALHAK EDEIAAKAAT AGH // ID RL1X_DROME STANDARD; PRT; 177 AA. AC P41093; Q9V840; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L18a. GN RPL18A OR CG6510. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94289482; PubMed=8018724; RA Ntwasa M., Buchanan S.G.S.C., Gay N.J.; RT "Drosophila ribosomal protein L18a: cDNA sequence, expression and RT chromosomal localization of the gene."; RL Biochim. Biophys. Acta 1218:210-212(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE L18AE FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75339; CAA53089.1; -. DR EMBL; AE003803; AAF57838.1; -. DR PIR; S45364; S45364. DR FlyBase; FBgn0010409; RpL18A. DR InterPro; IPR002670; Ribosomal_L18ae. DR Pfam; PF01775; Ribosomal_L18ae; 1. KW Ribosomal protein. SQ SEQUENCE 177 AA; 21029 MW; 4BD5E9A9F0799FA2 CRC64; MRAKGLLKEY EVVGRKLPSE KEPQTPLYKM RIFAPDNIVA KSRFWYFLRQ LKKFKKTTGE IVSIKQVYET SPVKIKNFGI WLRYDSRSGT HNMYREYRDL TVGGAVTQCY RDMGARHRAR AHSIQIIKVD SIPAAKTRRV HVKQFHDSKI KFPLVQRVHH KGNRKLFSFR KPRTYFQ // ID RL22_DROME STANDARD; PRT; 299 AA. AC P50887; Q9V3X9; DT 01-OCT-1996 (Rel. 34, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L22. GN RPL22 OR EG:BACR19J1.4 OR CG7434. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Glover C.V.C., Bidwai A.P., Zhao W.F.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE L22E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U42587; AAB17433.1; -. DR EMBL; AL132792; CAB60023.1; -. DR EMBL; AE003418; AAF45546.1; -. DR FlyBase; FBgn0015288; RpL22. DR InterPro; IPR002671; Ribosomal_L22e. DR Pfam; PF01776; Ribosomal_L22e; 1. DR ProDom; PD007306; Ribosomal_L22e; 1. KW Ribosomal protein. FT DOMAIN 24 31 POLY-ALA. FT DOMAIN 46 50 POLY-ALA. FT DOMAIN 65 70 POLY-ALA. FT DOMAIN 93 98 POLY-ALA. FT DOMAIN 103 112 POLY-ALA. FT DOMAIN 136 152 POLY-ALA. FT DOMAIN 185 188 POLY-LYS. FT DOMAIN 292 299 ASP/GLU-RICH (HIGHLY ACIDIC). SQ SEQUENCE 299 AA; 30610 MW; 46A99005610E4EB0 CRC64; MAPTAKTNKG DTKTAAAKPA EKKAAPAAAA AKGKVEKPKA EAAKPAAAAA KNVKKASEAA KDVKAAAAAA KPAAAKPAAA KPAAASKDAG KKAPAAAAPK KDAKAAAAPA PAKAAPAKKA ASTPAAAPPA KKAAPAKAAA PAAAAPAPAA AAPAVAKPAP KPKAKAAPAP SKVVKKNVLR GKGQKKKKVS LRFTIDCTNI AEDSIMDVAD FEKYIKARLK VNGKVNNLGN NVTFERSKLK LIVSSDVHFS KAYLKYLTKK YLKKNSLRDW IRVVANEKDS YELRYFRISS NDDEDDDAE // ID RL23_DROME STANDARD; PRT; 140 AA. AC P48159; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 60S ribosomal protein L23 (L17A). GN RPL23 OR RPL17A. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92380514; PubMed=1511900; RA Noselli S., Vincent A.; RT "The Drosophila melanogaster ribosomal protein L17A-encoding gene."; RL Gene 118:273-278(1992). CC -!- SIMILARITY: BELONGS TO THE L14P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M85295; AAA28867.1; -. DR HSSP; P04450; 1WHI. DR FlyBase; FBgn0010078; RpL17A. DR InterPro; IPR000218; Ribosomal_L14. DR Pfam; PF00238; Ribosomal_L14; 1. DR ProDom; PD001093; Ribosomal_L14; 1. DR PROSITE; PS00049; RIBOSOMAL_L14; FALSE_NEG. KW Ribosomal protein. SQ SEQUENCE 140 AA; 14866 MW; F5839532151038E5 CRC64; MSKRGRGGTA GGKFRISLGL PVGAVMNCAD NTGAKNLYVI AVHGIRGRLN RLPAAGVGDM FVATVKKGKP ELRKKVSVVP SARQRKPFRR RDGVFIYFED NAGVIVNNKG EMKGSAITGP VAKECADLWP RIASNASSIA // ID RL29_DROME STANDARD; PRT; 76 AA. AC Q24154; Q9W2I3; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L29 (L43). GN RPL29 OR RPL43 OR CG10071. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97217688; PubMed=9063649; RA Fox M.G., Gaynor J.J.; RT "A cDNA encodes the Drosophila homolog of yeast 60S ribosomal protein RT YL43."; RL DNA Seq. 7:123-125(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE L29E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U40226; AAB01760.1; -. DR EMBL; AE003453; AAM70864.1; -. DR FlyBase; FBgn0016726; RpL29. DR InterPro; IPR002673; Ribosomal_L29e. DR Pfam; PF01779; Ribosomal_L29e; 1. DR ProDom; PD010314; Ribosomal_L29e; 1. KW Ribosomal protein. SQ SEQUENCE 76 AA; 8920 MW; 6F70D28C7B30A254 CRC64; MAKSKNHTNH NQNKKAHRNG IKRPLRKRHE STLGMDVKFL INQRYARKGN LSREESVKRY NERIASQKGK PKPVTL // ID RL2A_DROME STANDARD; PRT; 149 AA. AC P41092; Q94530; Q9VR02; DT 01-FEB-1995 (Rel. 31, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L27a. GN RPL27A OR RPL27AA OR RPL27AB OR RPL27A2 OR CG15442. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Larva; RX MEDLINE=94128125; PubMed=8297386; RA Garwood J., Lepesant J.-A.; RT "The Drosophila melanogaster homolog of ribosomal protein L27a."; RL Biochem. Biophys. Res. Commun. 198:748-754(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Eye imaginal disk; RX MEDLINE=97208882; PubMed=9055824; RA Soehnge H., Huang X., Becker M., Conover D., Stern M.; RT "Cloning and sequencing of ribosomal protein L27a and a gene similar RT to human GS1 in Drosophila."; RL Gene 185:257-263(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE L15P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X74484; CAA52601.1; -. DR EMBL; U66357; AAC47475.1; -. DR EMBL; U66358; AAC47472.1; -. DR EMBL; AE003576; AAF51006.3; -. DR EMBL; AY071144; AAL48766.1; -. DR PIR; JC2392; JC2392. DR PIR; JC6202; JC6202. DR FlyBase; FBgn0010410; RpL27A. DR InterPro; IPR001196; Ribosomal_L15. DR Pfam; PF00256; L15; 1. DR PROSITE; PS00475; RIBOSOMAL_L15; 1. KW Ribosomal protein. FT CONFLICT 2 2 S -> R (IN REF. 1). FT CONFLICT 36 36 A -> L (IN REF. 1). FT CONFLICT 140 140 K -> E (IN REF. 1). SQ SEQUENCE 149 AA; 17022 MW; 7777397307B89DCC CRC64; MSNIKRKKTR KLRGHVSHGH GRIGKHRKHP GGRGNAGGMH HHRINFDKYH PGYFGKVGMR NFHLRRQHKF RPEINLDKLW SLVGAEKFAE LEKEKSTKAP VIDLVKFGYY KLLGRGHLPA RPVIVKAKYF SKKAEDKIKK AGGVCLLSA // ID RL31_DROME STANDARD; PRT; 124 AA. AC Q9V597; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L31. GN RPL31 OR CG1821. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE L31E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003833; AAF58920.1; -. DR EMBL; AY113508; AAM29513.1; -. DR FlyBase; FBgn0025286; RpL31. DR GO; GO:0005842; C:cytosolic large ribosomal subunit (sensu Eu...; NAS. DR GO; GO:0003735; F:structural constituent of ribosome; NAS. DR GO; GO:0006412; P:protein biosynthesis; NAS. DR InterPro; IPR000054; Ribosomal_L31e. DR Pfam; PF01198; Ribosomal_L31e; 1. DR ProDom; PD006030; Ribosomal_L31e; 1. DR PROSITE; PS01144; RIBOSOMAL_L31E; 1. KW Ribosomal protein. SQ SEQUENCE 124 AA; 14533 MW; 191543AB701FBE57 CRC64; MTKTKGEKIN KSAINEVVTR ECTIHLAKRV HNIGFKKRAP RAIKEIRKFA EREMGTTDVR IDTRLNKHIW SKGIRSTPFR IRVRLARRRN DDEDSPNKLY TYVTYVPVST FKNLQTENVE SSDD // ID RL32_DROME STANDARD; PRT; 134 AA. AC P04359; O01386; Q9VAB2; DT 20-MAR-1987 (Rel. 04, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L32 (RP49). GN RPL32 OR RP49 OR M(3)99D OR CG7939. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84272233; PubMed=6087289; RA O'Connell P., Rosbash M.; RT "Sequence, structure, and codon preference of the Drosophila RT ribosomal protein 49 gene."; RL Nucleic Acids Res. 12:5495-5513(1984). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA McMahill M.S., Danielson P.D., Fogleman J.C.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=M66; RX MEDLINE=98140318; PubMed=9479691; RA Ramos-Onsins S., Segarra C., Rozas J., Aguade M.; RT "Molecular and chromosomal phylogeny in the obscura group of RT Drosophila inferred from sequences of the rp49 gene region."; RL Mol. Phylogenet. Evol. 9:33-41(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE L32E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X00848; CAA25404.1; -. DR EMBL; U92431; AAB51389.1; -. DR EMBL; Y13939; CAA74278.1; -. DR EMBL; AE003772; AAF57001.1; -. DR PIR; A02830; R5FF49. DR FlyBase; FBgn0002626; RpL32. DR InterPro; IPR001515; Ribosomal_L32E. DR Pfam; PF01655; Ribosomal_L32e; 1. DR ProDom; PD003823; Ribosomal_L32E; 1. DR PROSITE; PS00580; RIBOSOMAL_L32E; 1. KW Ribosomal protein. FT CONFLICT 18 18 H -> D (IN REF. 1). FT CONFLICT 45 45 R -> G (IN REF. 1). FT CONFLICT 92 107 RVYCGEIAHGVSSKKR -> PRLLREMPTASPPRS (IN FT REF. 1). FT CONFLICT 111 111 V -> I (IN REF. 1). FT CONFLICT 119 134 VRLTNPNGRLRSQENE -> LRSPTPTVACVSRRTR (IN FT REF. 1). SQ SEQUENCE 134 AA; 16020 MW; AC00FA7EEEE46D9A CRC64; MTIRPAYRPK IVKKRTKHFI RHQSDRYAKL SHKWRKPKGI DNRVRRRFKG QYLMPNIGYG SNKRTRHMLP TGFKKFLVHN VRELEVLLMQ NRVYCGEIAH GVSSKKRKEI VERAKQLSVR LTNPNGRLRS QENE // ID RL36_DROME STANDARD; PRT; 115 AA. AC P49630; Q9W5E5; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L36 (Minute(1)1B protein). GN RPL36 OR M(1)1B OR EG:115C2.7 OR CG7622. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Steinhauer W.R.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE L36E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U20543; AAA63151.1; -. DR EMBL; AL031581; CAA20892.1; -. DR EMBL; AE003418; AAF45531.1; -. DR PIR; T13383; T13383. DR FlyBase; FBgn0002579; RpL36. DR InterPro; IPR000509; Ribosomal_L36e. DR Pfam; PF01158; Ribosomal_L36e; 1. DR ProDom; PD009192; Ribosomal_L36e; 1. DR PROSITE; PS01190; RIBOSOMAL_L36E; 1. KW Ribosomal protein. SQ SEQUENCE 115 AA; 13502 MW; C9B657B7A6442545 CRC64; MAVRYELAIG LNKGHKTSKI RNVKYTGDKK VKGLRGSRLK NIQTRHTKFM RDLVREVVGH APYEKRTMEL LKVSKDKRAL KFLKRRLGTH IRAKRKREEL SNILTQLRKA QTHAK // ID RL39_DROME STANDARD; PRT; 51 AA. AC O16130; Q9W1B7; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L39 (Ribosomal protein 46). GN RPL46 OR RPL39 OR RP46 OR CG3997. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Kim J.K., Lee C.C., Chung K.W.; RT "Isolation and characterization of the ribosomal protein 46 gene in RT Drosophila melanogaster."; RL Korean J. Biol. Sci. 2:113-116(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE L39E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF012422; AAB65802.1; -. DR EMBL; AE003462; AAF47154.1; -. DR FlyBase; FBgn0023170; RpL46. DR InterPro; IPR000077; Ribosomal_L39. DR Pfam; PF00832; Ribosomal_L39; 1. DR ProDom; PD007914; Ribosomal_L39; 1. DR PROSITE; PS00051; RIBOSOMAL_L39E; 1. KW Ribosomal protein. FT CONFLICT 30 30 R -> A (IN REF. 1). SQ SEQUENCE 51 AA; 6299 MW; 48EADF9B69EBAAE5 CRC64; MAAHKSFRIK QKLAKKLKQN RSVPQWVRLR TGNTIRYNAK RRHWRRTKLK L // ID RL3_DROME STANDARD; PRT; 415 AA. AC O16797; Q9VGR4; Q9VGR5; Q9VGR6; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L3. GN RPL3 OR CG4863. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=98326317; PubMed=9661671; RA Chan H.Y.E., Zhang Y., Hoheisel J.D., O'Kane C.J.; RT "Identification and characterization of the gene for Drosophila L3 RT ribosomal protein."; RL Gene 212:119-125(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: THE L3 PROTEIN IS A COMPONENT OF THE LARGE SUBUNIT OF CC CYTOPLASMIC RIBOSOMES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=A; Synonyms=B, E; CC IsoId=O16797-1; Sequence=Displayed; CC Name=D; CC IsoId=O16797-2; Sequence=VSP_005715, VSP_005717; CC Name=C; CC IsoId=O16797-3; Sequence=VSP_005714, VSP_005716; CC -!- SIMILARITY: BELONGS TO THE L3P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF016835; AAC26144.1; -. DR EMBL; AE003690; AAF54609.1; ALT_INIT. DR EMBL; AE003690; AAF54610.2; -. DR EMBL; AE003690; AAF54611.1; ALT_INIT. DR EMBL; AE003690; AAF54612.2; -. DR FlyBase; FBgn0020910; RpL3. DR InterPro; IPR000597; Ribosomal_L3. DR InterPro; IPR009000; Translat_factor. DR Pfam; PF00297; Ribosomal_L3; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. KW Ribosomal protein; Alternative splicing. FT INIT_MET 0 0 BY SIMILARITY. FT VARSPLIC 121 137 WYKSKKKAFTKASKKWT -> CSSISLLRELFKSLNVV FT (in isoform C). FT /FTId=VSP_005714. FT VARSPLIC 123 160 KSKKKAFTKASKKWTDDLGKKSIENDFRKMLRYCKVIR -> FT VSEDHVVVLPTPFVAIFFAPGVHTHKMAADTCFLLESG FT (in isoform D). FT /FTId=VSP_005715. FT VARSPLIC 138 415 Missing (in isoform C). FT /FTId=VSP_005716. FT VARSPLIC 161 415 Missing (in isoform D). FT /FTId=VSP_005717. SQ SEQUENCE 415 AA; 46784 MW; DE5964681FAF8A15 CRC64; SHRKFSAPRH GSMAFYPKKR SARHRGKVKA FPKDDASKPV HLTCFIGYKA GMTHIVREAD RPGSKINKKE VVEAVTVLET PPMIVVGAVG YIETPFGLRA LVNVWAQHLS EECRRRFYKN WYKSKKKAFT KASKKWTDDL GKKSIENDFR KMLRYCKVIR VIAHSQIRLI KQRQKKAHVM EIQLNGGSIE DKVKWAREHL EKPIQVSNVF GQDEMIDCVG VTKGKGFKGV TSRWHTKKLP RKTHKGLRKV ACIGAWHPSR VSTTVARAGQ KGYHHRTEIN KKIYRIGAGI HTKDGKVIKN NASTEYDLTD KSITPMGGFP HYGEVNNDFV MIKGCCIGSK KRIITLRKSL LKHTKRSALE QIKLKFIDTS SKMGHGRFQT PADKLAFMGP LKKDRLKEEA AATTAAAAAA TTTSA // ID RL40_DROME STANDARD; PRT; 52 AA. AC P18101; Q9VQX7; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L40 (CEP52). GN RPL40 OR UBI-F OR UBI-F52 OR CG2960. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90326530; PubMed=2165256; RA Cabrera y Poch H.L., Arribas C., Izquierdo M.; RT "Sequence of a Drosophila cDNA encoding a ubiquitin gene fusion to a RT 52-aa ribosomal protein tail."; RL Nucleic Acids Res. 18:3994-3994(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92392292; PubMed=1381584; RA Cabrera H.L., Barrio R., Arribas C.; RT "Structure and expression of the Drosophila ubiquitin-52-amino-acid RT fusion-protein gene."; RL Biochem. J. 286:281-288(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- MISCELLANEOUS: THIS RIBOSOMAL PROTEIN IS SYNTHESIZED AS A CC C-TERMINAL EXTENSION PROTEIN (CEP) OF UBIQUITIN. CC -!- SIMILARITY: BELONGS TO THE L40E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53059; CAA37227.1; ALT_INIT. DR EMBL; X59943; CAA42568.1; ALT_INIT. DR EMBL; AE003577; AAF51034.1; ALT_INIT. DR FlyBase; FBgn0003941; RpL40. DR GO; GO:0005842; C:cytosolic large ribosomal subunit (sensu Eu...; IDA. DR InterPro; IPR001975; Ribosomal_L40E. DR Pfam; PF01020; Ribosomal_L40e; 1. KW Ribosomal protein. SQ SEQUENCE 52 AA; 6182 MW; 7B29D821B885BABA CRC64; IIEPSLRILA QKYNCDKMIC RKCYARLHPR ATNCRKKKCG HTNNLRPKKK LK // ID RL4_DROME STANDARD; PRT; 407 AA. AC P09180; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 60S ribosomal protein L4 (L1). GN RPL4 OR RPL1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=89098414; PubMed=2492096; RA Rafti F., Gargiulo G., Manzi A., Malva C., Graziani F.; RT "Sequence of the ribosomal protein cDNA of D. melanogaster homologous RT to the L1 ribosomal protein gene of X. laevis."; RL Nucleic Acids Res. 17:456-456(1989). RN [2] RP SEQUENCE OF 63-186 FROM N.A. RX MEDLINE=88262486; PubMed=3133637; RA Rafti F., Gargiulo G., Manzi A., Malva C., Grossi G., Andone S., RA Graziani F.; RT "Isolation and structural analysis of a ribosomal protein gene in RT D.melanogaster."; RL Nucleic Acids Res. 16:4915-4926(1988). CC -!- SIMILARITY: BELONGS TO THE L4E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13382; CAA31759.1; -. DR EMBL; X06881; CAA29998.1; -. DR PIR; S02209; R5FFL1. DR FlyBase; FBgn0003279; RpL1. DR InterPro; IPR002136; Ribosomal_L4/L1E. DR Pfam; PF00573; Ribosomal_L4; 1. DR PROSITE; PS00939; RIBOSOMAL_L1E; 1. KW Ribosomal protein. FT CONFLICT 117 117 K -> R (IN REF. 2). SQ SEQUENCE 407 AA; 45755 MW; F35D7898770B043C CRC64; MSLGNARPLV SVYTEKNEPA KDKNICLPAV FKAPIRPDVV NEVHQLLRRN NRQAYAVSEL AGHQTSAESW GTGRAVARIP RVRGGGTHRS GQGAFGNMCR GGRMFAPTKT FRRWHRKVNV NQRRYALVSA IAASGVPALV QSKGHVIDGV SEFPLVVSDE VQKVQKTKQA VIFLRRLKIW ADIQKVYKSQ RFRAGRGTMR DRRRIARRGP LVVYDKDEGL RKAFRNIPGI ETINVDKLNV LKLAPGGHVG RFVIWTESAF ARLNDLFGTW KKPSTLKKGY NLPQPKMANT DLSRLLKSEE IRKVLRDPRK RVFRSVRRLN PLTNVRQLIK LNPYAEVLKR RAALAAEKRT VAKVLAKAKK QNVELAKSHF ANVATKARPI APSSGRPQEE GRRQEASGQE VNLLSPE // ID RL7A_DROME STANDARD; PRT; 271 AA. AC P46223; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 60S ribosomal protein L7a. GN RPL7A OR SURF-3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95257916; PubMed=7739520; RA Armes N., Fried M.; RT "The genomic organization of the region containing the Drosophila RT melanogaster rpL7a (Surf-3) gene differs from those of the mammalian RT and avian Surfeit loci."; RL Mol. Cell. Biol. 15:2367-2373(1995). CC -!- SIMILARITY: BELONGS TO THE L7AE FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X82782; CAA58023.1; -. DR FlyBase; FBgn0014026; RpL7A. DR InterPro; IPR004038; Ribosomal_L7A. DR InterPro; IPR004037; Ribosomal_L7Ae. DR Pfam; PF01248; Ribosomal_L7Ae; 1. DR PRINTS; PR00881; L7ARS6FAMILY. DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1. KW Ribosomal protein. SQ SEQUENCE 271 AA; 30677 MW; 4D183B0895EB6496 CRC64; MVVKKPRPKK KPVTKKVAPA PLAVKKPVVK KVVNQLFEKR PKNFGIGQNV QPKRDLSRFV RWPKYIRVQR QKAVLQKRLK VPPPIHQFSQ TLDKTTAVKL FKLLEKYRPE SALAKNVRLK KIAEAKAKGK DVEPKKKPSY VSAGTNTVTK LIEQKKAQLV VIAHDVDPLE LVLFLPALCR KMGVPYCIVK GKARLGRLVR RKTCTTLALT TVDNNDKANF GKVLEAVKTN FNERHEEIRR HWGGGILGSK SLARISKLER AKARELAQKQ G // ID RL7_DROME STANDARD; PRT; 252 AA. AC P32100; Q9VL30; DT 01-OCT-1993 (Rel. 27, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L7. GN RPL7 OR CG4897. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 14-252 FROM N.A. RC STRAIN=Canton-S; RA Quan F., Forte M.A.; RL Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: BINDS TO G-RICH STRUCTURES IN 28S RRNA AND IN MRNAS. CC PLAYS A REGULATORY ROLE IN THE TRANSLATION APPARATUS; INHIBITS CC CELL-FREE TRANSLATION OF MRNAS (BY SIMILARITY). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE L30P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003627; AAF52868.1; -. DR EMBL; X15109; CAA33207.1; -. DR PIR; S21500; S21500. DR FlyBase; FBgn0005593; RpL7. DR InterPro; IPR000517; Ribosomal_L30. DR InterPro; IPR005998; Ribosomal_L7_euk. DR Pfam; PF00327; Ribosomal_L30; 1. DR TIGRFAMs; TIGR01310; L7; 1. DR PROSITE; PS00634; RIBOSOMAL_L30; 1. KW Ribosomal protein; RNA-binding. SQ SEQUENCE 252 AA; 29552 MW; 958439D03E83EB44 CRC64; MPAPVVKKPA AKKLPAVPES KLKFSKKQIS KRVAESKRRL KKAAVIALRK KENLVRAEKY QNEYIKAEQR EIKLRRLAKK RNQFYVPAEA KLAFVVRIRG INKVAPKVRK VLQLFRLRQI NNGVFIKLNK ATINMLRIAE PYITWGYPNL KSVRELIYKR GFVKHNRQRV PITDNFVIER KLRQAHQIQC VEDLVHEIFT VGPNFKYASN FLWPFKLNTP TGGWRKKANH YVNGGDFGNR EDQINRLLRK MV // ID RL9_DROME STANDARD; PRT; 190 AA. AC P50882; Q9VKL6; Q9VKL7; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L9. GN RPL9 OR M(2)32D OR CG6141. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96262192; PubMed=8676882; RA Schmidt A., Hollmann M., Schaefer U.; RT "A newly identified Minute locus, M(2)32D, encodes the ribosomal RT protein L9 in Drosophila melanogaster."; RL Mol. Gen. Genet. 251:381-387(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- SIMILARITY: BELONGS TO THE L6P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X94613; CAA64319.1; -. DR EMBL; AE003630; AAF53048.2; -. DR PIR; JC6062; JC6062. DR FlyBase; FBgn0015756; RpL9. DR InterPro; IPR000702; Ribosomal_L6. DR InterPro; IPR002359; Ribosomal_L6_2. DR Pfam; PF00347; Ribosomal_L6; 2. DR PROSITE; PS00700; RIBOSOMAL_L6_2; 1. KW Ribosomal protein. FT CONFLICT 37 37 S -> T (IN REF. 1). SQ SEQUENCE 190 AA; 21392 MW; 689B2520ACDA12D3 CRC64; MRTINSNQCV KIPKDIKASV KARVVTITGT RGTLKRSFKH LALDMYMPDK RTLKVEKWFG TKKELAAVRT VCSHIENMIK GVTFGFQYKM RAVYAHFPIN CVTSENNTVI EIRNFLGEKY IRRVEMAPGV TVVNSTAQKD ELIVEGNDIE SVSGSAALIQ QSTTVKNKDI RKFLDGLYVS EKTTVVKLES // ID RLA0_DROME STANDARD; PRT; 317 AA. AC P19889; Q9VNV9; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S acidic ribosomal protein P0 (DNA-(apurinic or apyrimidinic site) DE lyase) (EC 4.2.99.18) (Apurinic-apyrimidinic endonuclease). GN RPP0 OR APE OR AP3 OR CG7490. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89261760; PubMed=2471063; RA Kelley M.R., Venugopal S., Harless J., Deutsch W.A.; RT "Antibody to a human DNA repair protein allows for cloning of a RT Drosophila cDNA that encodes an apurinic endonuclease."; RL Mol. Cell. Biol. 9:965-973(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SIMILARITY TO RIBOSOMAL PROTEIN P0. RX MEDLINE=91334151; PubMed=1870984; RA Grabowski D.T., Deutsch W.A., Derda D., Kelley M.R.; RT "Drosophila AP3, a presumptive DNA repair protein, is homologous to RT human ribosomal associated protein P0."; RL Nucleic Acids Res. 19:4297-4297(1991). RN [4] RP DNA REPAIR ACTIVITY. RX MEDLINE=97086697; PubMed=8932386; RA Yacoub A., Kelley M.R., Deutsch W.A.; RT "Drosophila ribosomal protein PO contains apurinic/apyrimidinic RT endonuclease activity."; RL Nucleic Acids Res. 24:4298-4303(1996). CC -!- FUNCTION: RIBOSOMAL PROTEIN P0 IS THE FUNCTIONAL EQUIVALENT OF CC E.COLI PROTEIN L10. CC -!- CATALYTIC ACTIVITY: THE C-O-P BOND 3' TO THE APURINIC OR CC APYRIMIDINIC SITE IN DNA IS BROKEN BY A BETA-ELIMINATION REACTION, CC LEAVING A 3'-TERMINAL UNSATURATED SUGAR AND A PRODUCT WITH A CC TERMINAL 5'-PHOSPHATE. CC -!- SUBUNIT: P0 FORMS A PENTAMERIC COMPLEX BY INTERACTION WITH DIMERS CC OF P1 AND P2 (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- DEVELOPMENTAL STAGE: ALL STAGES OF DEVELOPMENT. A LARGER CC TRANSCRIPT IS RESTRICTED TO THE EMBRYONIC AND EARLY LARVAL CC STAGES. CC -!- SIMILARITY: BELONGS TO THE L10P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M25772; AAA53372.1; -. DR EMBL; AE003596; AAF51807.1; -. DR PIR; A30223; R5FFP0. DR FlyBase; FBgn0000100; RpP0. DR GO; GO:0005830; C:cytosolic ribosome (sensu Eukarya); NAS. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase a...; NAS. DR GO; GO:0003735; F:structural constituent of ribosome; NAS. DR GO; GO:0006412; P:protein biosynthesis; NAS. DR InterPro; IPR001813; Ribosomal_60S. DR InterPro; IPR001790; Ribosomal_L10. DR Pfam; PF00428; 60s_ribosomal; 1. DR Pfam; PF00466; Ribosomal_L10; 1. KW Ribosomal protein; Phosphorylation; Hydrolase; Lyase; Nuclease; KW Endonuclease; DNA repair; Nuclear protein. FT MOD_RES 304 304 PHOSPHORYLATION (BY CK1) (POTENTIAL). SQ SEQUENCE 317 AA; 34202 MW; 36E9DD5DD8CF7E1F CRC64; MVRENKAAWK AQYFIKVVEL FDEFPKCFIV GADNVGSKQM QNIRTSLRGL AVVLMGKNTM MRKAIRGHLE NNPQLEKLLP HIKGNVGFVF TKGDLAEVRD KLLESKVRAP ARPGAIAPLH VIIPAQNTGL GPEKTSFFQA LSIPTKISKG TIEIINDVPI LKPGDKVGAS EATLLNMLNI SPFSYGLIVN QVYDSGSIFS PEILDIKPED LRAKFQQGVA NLAAVCLSVG YPTIASAPHS IANGFKNLLA IAATTEVEFK EATTIKEYIK DPSKFAAAAS ASAAPAAGGA TEKKEEAKKP ESESEEEDDD MGFGLFD // ID RLA1_DROME STANDARD; PRT; 112 AA. AC P08570; Q9VPP6; DT 01-AUG-1988 (Rel. 08, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE 60S acidic ribosomal protein P1 (RP21C) (Acidic ribosomal protein DE RPA2). GN RPP2 OR M(2)21C OR RPA2 OR RP21C OR CG4087. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88096510; PubMed=3122177; RA Wigboldus J.D.; RT "cDNA and deduced amino acid sequence of Drosophila rp21C, another RT 'A'-type ribosomal protein."; RL Nucleic Acids Res. 15:10064-10064(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93273819; PubMed=8501137; RA Olson P.F., Salo T., Garrison K., Fessler J.H.; RT "Drosophila acidic ribosomal protein rpA2: sequence and RT characterization."; RL J. Cell. Biochem. 51:353-359(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PLAYS AN IMPORTANT ROLE IN THE ELONGATION STEP OF CC PROTEIN SYNTHESIS. CC -!- SUBUNIT: P1 AND P2 EXIST AS DIMERS AT THE LARGE RIBOSOMAL SUBUNIT. CC -!- SIMILARITY: BELONGS TO THE L12P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00504; CAA68557.1; -. DR EMBL; S62170; AAB26902.1; -. DR EMBL; AE003589; AAF51499.1; -. DR EMBL; AY069125; AAL39270.1; -. DR PIR; S00659; R5FF2E. DR FlyBase; FBgn0002593; RpP2. DR InterPro; IPR001813; Ribosomal_60S. DR InterPro; IPR001859; Ribosomal_P2. DR Pfam; PF00428; 60s_ribosomal; 1. DR PRINTS; PR00456; RIBOSOMALP2. KW Ribosomal protein. FT CONFLICT 9 9 C -> S (IN REF. 1). FT CONFLICT 53 53 G -> A (IN REF. 1). SQ SEQUENCE 112 AA; 11513 MW; 2EA9CA3E884A7CCF CRC64; MSTKAELACV YASLILVDDD VAVTGEKINT ILKAANVEVE PYWPGLFAKA LEGINVKDLI TNIGSGVGAA PAGGAAPAAA AAAPAAESKK EEKKKEEESD QSDDDMGFGL FD // ID RLA2_DROME STANDARD; PRT; 113 AA. AC P05389; Q9V7R6; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S acidic ribosomal protein P2 (Acidic ribosomal protein RPA1). GN RPP1 OR RPA1 OR CG4918. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=87146465; PubMed=3103101; RA Qian S., Zhang J.-Y., Kay M.A., Jacobs-Lorena M.; RT "Structural analysis of the Drosophila rpA1 gene, a member of the RT eucaryotic 'A' type ribosomal protein family."; RL Nucleic Acids Res. 15:987-1003(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PLAYS AN IMPORTANT ROLE IN THE ELONGATION STEP OF CC PROTEIN SYNTHESIS. CC -!- SUBUNIT: P1 AND P2 EXIST AS DIMERS AT THE LARGE RIBOSOMAL SUBUNIT. CC -!- PTM: PHOSPHORYLATED (BY SIMILARITY). CC -!- MISCELLANEOUS: THE CANTON-S STRAIN SEQUENCE IS SHOWN. CC -!- SIMILARITY: BELONGS TO THE L12P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05016; CAA28672.1; -. DR EMBL; X05466; CAA29026.1; -. DR EMBL; AE003806; AAF57979.1; -. DR PIR; A26401; R6FFP2. DR FlyBase; FBgn0003274; RpP1. DR InterPro; IPR001813; Ribosomal_60S. DR Pfam; PF00428; 60s_ribosomal; 1. KW Ribosomal protein; Phosphorylation. FT VARIANT 21 21 S -> G (IN STRAIN OREGON-R). SQ SEQUENCE 113 AA; 11757 MW; DDA5F5A4219BD65A CRC64; MRYVAAYLLA VLGGKDSPAN SDLEKILSSV GVEVDAERLT KVIKELAGKS IDDLIKEGRE KLSSMPVGGG GAVAAADAAP AAAAGGDKKE AKKEEKKEES ESEDDDMGFA LFE // ID RM09_DROME STANDARD; PRT; 248 AA. AC Q9VF89; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L9, mitochondrial precursor. GN MRPL9 OR CG4923. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP IDENTIFICATION. RX MEDLINE=21293042; PubMed=11279069; RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., RA Watanabe K.; RT "Structural compensation for the deficit of rRNA with proteins in the RT mammalian mitochondrial ribosome. Systematic analysis of protein RT components of the large ribosomal subunit from mammalian RT mitochondria."; RL J. Biol. Chem. 276:21724-21736(2001). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE L9P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003708; AAF55172.2; -. DR EMBL; AY071462; AAL49084.1; -. DR EMBL; AY118435; AAM48464.1; -. DR FlyBase; FBgn0038319; mRpL9. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; TAS. DR GO; GO:0003735; F:structural constituent of ribosome; TAS. DR GO; GO:0006412; P:protein biosynthesis; TAS. DR InterPro; IPR009027; L9_N_like. DR InterPro; IPR000244; Ribosomal_L9. DR Pfam; PF01281; Ribosomal_L9_N; 1. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 248 60S RIBOSOMAL PROTEIN L9. SQ SEQUENCE 248 AA; 28804 MW; 1AC0E20DF5AC08FF CRC64; MLKNIYVTPL NLLKSATSLQ QQVRTTFVLK RKYDPPLHKT NEKPRRMRAK NFIYELVDDT LVKKRPNIEV VLKTFVEGVG DKGDVVSMKP HFVYNKLLLP GLAAYNTPEN VAKYAKTEAE KSTVKHSSPY AQRTVNMLET IVLAVVMNKD EPWVLEPWHI KASLRKTGFY CREECITLPK ERIEGPDLKK ENKDFYCTVT INKLEQARLK CRLHHWSTDP SERLPYVLEH WKLQSEPLLD VCSPEKTP // ID RM11_DROME STANDARD; PRT; 196 AA. AC Q9VFJ2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L11, mitochondrial precursor. GN MRPL11 OR CG3351. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE L11P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003705; AAF55063.1; -. DR EMBL; AY094892; AAM11245.1; -. DR HSSP; P29395; 1MMS. DR FlyBase; FBgn0038234; mRpL11. DR InterPro; IPR000911; Ribosomal_L11. DR Pfam; PF00298; Ribosomal_L11; 1. DR Pfam; PF03946; Ribosomal_L11_N; 1. DR ProDom; PD001367; Ribosomal_L11; 1. DR SMART; SM00649; RL11; 1. DR PROSITE; PS00359; RIBOSOMAL_L11; FALSE_NEG. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 196 60S RIBOSOMAL PROTEIN L11. SQ SEQUENCE 196 AA; 21611 MW; 47C0B351EC625139 CRC64; MSKAAGKLKS LKKTVERVTH TSKLKTNIPA GMAAAGPPLG PMLGQRAINI AAFCKDFNAK TAEMKEGVPL PCRISVNSDR SYDLAIHHPP ATFFLKQAAG IQRGTMTPGK EVAGMITLKH LYEIAAIKIQ DPPNVLLTMQ QMCEMLISIA RTCGIKVVRE IDPAAYGEFL EERKLIVEQQ RRELQEKREA KMLRTG // ID RM13_DROME STANDARD; PRT; 178 AA. AC Q9VJ38; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L13, mitochondrial (L13mt). GN MRPL13 OR CG10603. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- SIMILARITY: BELONGS TO THE L13P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003660; AAF53719.2; -. DR FlyBase; FBgn0032720; mRpL13. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS. DR GO; GO:0003735; F:structural constituent of ribosome; ISS. DR GO; GO:0006412; P:protein biosynthesis; ISS. DR InterPro; IPR005822; Ribosomal_L13. DR InterPro; IPR005823; Ribosomal_L13b/o. DR Pfam; PF00572; Ribosomal_L13; 1. DR ProDom; PD001791; L13_bact_org; 1. DR PROSITE; PS00783; RIBOSOMAL_L13; FALSE_NEG. KW Ribosomal protein; Mitochondrion. SQ SEQUENCE 178 AA; 21090 MW; 4F2E4FA6D12360C8 CRC64; MSIAKRVQQW ATFARTWHIY DCTWQNPFES AKLVKTHLLG LQKPIYHPMN DCGDHVVLIN TREIALPGDE WVKRVYFHHT GYPGGASWTL AWQLHEKDPT MVMKKAVYNS MRGNLQRRHT MQRLHLFADD QVPEEILQNV TNQIRTPRSI PQRLDHIDKE TLENFPNIMD YPKDYILR // ID RM19_DROME STANDARD; PRT; 306 AA. AC Q9VHN6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L19, mitochondrial precursor. GN MRPL19 OR CG8039. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., RA Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE L19P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003680; AAF54266.1; -. DR EMBL; AY061413; AAL28961.1; -. DR FlyBase; FBgn0037608; mRpL19. DR InterPro; IPR001857; Ribosomal_L19. DR Pfam; PF01245; Ribosomal_L19; 1. DR ProDom; PD002979; Ribosomal_L19; 1. DR PROSITE; PS01015; RIBOSOMAL_L19; FALSE_NEG. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 306 60S RIBOSOMAL PROTEIN L19. SQ SEQUENCE 306 AA; 36192 MW; 1A575360C6E7744E CRC64; MNLSTRVMLN RLTQQCVYKR IVTFSTKTAE HVIENQEEQK KEAPPTTPTS PVNRKTIIPA NYRFVYPEFL PDPKVEWRNL VREKLERLDM LDRRKQIDLP EFYVGSVLAV TSSDPHAAGK TSRFVGICIN RDRCGLRARF ILRNVIDHQG MEVVYELYDP TILKIEVLRL EKRLDDSLFY LRDALPEYST FDENMEAEPL EEGAPVPVND IKVVLRPRPW LERWERQNLR GVANIDEYLK DKHRLSAAKV QKPWEKYDMM KDYRSSIPEE EQTEIFAEVH TELHALELQR KRNKRKRTFI KPKQLA // ID RM28_DROME STANDARD; PRT; 302 AA. AC Q9VMX0; Q8SXZ1; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE 39S ribosomal protein L28, mitochondrial precursor (L28mt) (MRP-L28). GN MRPL28 OR CG3782. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE L28P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003608; AAF52188.1; -. DR EMBL; AY075494; AAL68304.1; -. DR FlyBase; FBgn0031660; mRpL28. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 302 39S RIBOSOMAL PROTEIN L28. FT CONFLICT 86 87 IW -> MG (IN REF. 2). SQ SEQUENCE 302 AA; 34950 MW; D6BDDE8B868062FE CRC64; MAHATPQGVK LLNGWKRPGR FDKGLGAQLP EAYRKFWREW KLTTPAAVHY IPKEQQWERD EVTHAIKPVQ NIPLPLIDTP ESHRGIWGGE AVIKGFQKRE QTKRRVPHFW VPNLRRSVVH SHVLDCYMSV VVTERTLEQI HECHGFDHYL LKNRACDLRS ALALKLKREV LQALQNGVPA LADEPERQQE VLKEYRRYLE PYTPEEIDWY GHTYLEAIRK LQKQLREAEK VVPHKLEFRG KLIEQLRQAG ISEAGKLEKP DALAAESSVE HKDSDIEALT KLESSPSSSW LSKINPFGKK ET // ID RM32_DROME STANDARD; PRT; 195 AA. AC Q9V9Z1; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 60S ribosomal protein L32, mitochondrial precursor. GN MRPL32 OR CG12220. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE L32P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003777; AAF57137.1; -. DR FlyBase; FBgn0039835; mRpL32. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 195 60S RIBOSOMAL PROTEIN L32. SQ SEQUENCE 195 AA; 22642 MW; D8148CB3392F4900 CRC64; MSRNLFLSIT NFIRNLESLF LPHGGHPPAL ALAGFQHDHS PKSSQEFSLK QLIGDGLLWA VPKHRRSVEK RLKRKFGYPE YNWKPLREKR NLRSCLQCGH DHEMGVLCPF CYQKVLKETE LMQSKIQETL GLDPVDKEVI VLYEGEKAEQ STDDLKNKRI VEMKKPRPMW FTKNLLQKST QQLSETKEVK PSDLA // ID RM39_DROME STANDARD; PRT; 333 AA. AC Q9VUJ0; Q8SYN5; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial 39s ribosomal protein L39 (MRP-L39) (MRP-L5). GN MRPL5 OR CG17166. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: TO THE N-TERMINAL OF THREONYL-TRNA SYNTHETASES. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 282. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003532; AAF49686.2; -. DR EMBL; AY071425; AAL49047.1; ALT_FRAME. DR FlyBase; FBgn0036462; mRpL5. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; NAS. DR GO; GO:0003735; F:structural constituent of ribosome; NAS. DR GO; GO:0006412; P:protein biosynthesis; NAS. DR InterPro; IPR004095; TGS_dom. DR Pfam; PF02824; TGS; 1. KW Ribosomal protein; Mitochondrion. SQ SEQUENCE 333 AA; 37324 MW; 27C6515156D35D70 CRC64; MSAATKLHKT SWCALRQLQQ YRTKANFSGS SASLAKRNDL FNQEQRRQRD AVGRIDKIEV RYLGLPEDVT LVMNGNISTP FNCAQHLSEG HCKRSALALI DGSVPWDMHR PLQESCTLQL LNFHVSEPHV VNKAFWRTCS FMLGAALNRA FKPEANLQLH SFPGPNIKSG SFVHDIVLQT QNWEPGKEEM RALSAEMVKL AAQDLRIERL DVQQDLAQEM FKDSKYKSEQ LPSISQQTNG RVTLYRLGDH IDISRGPMVA STSFLGKCVI SAAHKVAEEG PSGAFYRIQG VALPSGFQLN HVAFGVLEER SKKPSPARLP NEPFEEQQQL QLS // ID RM45_DROME STANDARD; PRT; 361 AA. AC Q9VCX3; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable 39S ribosomal protein L45, mitochondrial precursor. GN MRPL45 OR CG6949. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE L45 FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003739; AAF56032.1; -. DR EMBL; AY071013; AAL48635.1; -. DR FlyBase; FBgn0038996; mRpL45. DR GO; GO:0005739; C:mitochondrion; ISS. DR GO; GO:0003735; F:structural constituent of ribosome; ISS. DR GO; GO:0006412; P:protein biosynthesis; ISS. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 361 PROBABLE 39S RIBOSOMAL PROTEIN L45. SQ SEQUENCE 361 AA; 41611 MW; F0EE800484E4F6D4 CRC64; MEKLASAKTC LKLLQVMPGV QQAALLPGGG LGVLASPLQN LIQMQQVRHR QTKHWKPEFK RLRKLKFVKM DLPNLREKQE DITKEEMRSR MKERGVLPPR PWMERPFHIS CTGGIFEAYV PPEGDGKKSI ISTSGAKQKL EFLEKKSKSL MAVRKIRSYD ENFSSDDFGA EAQDIYIQAH THMAAKDKYK IREFVSERCY PEMMHNVKDK TIRWKFLQSL EPPRVVHARV TEVITKENQF AQVTVRFHSQ QMLAIYDRFG RLMHGSEIIT KDVLEYVVFE KHISNEYGKW RLHDKIIPDW LPAKQPAPIT YRLIEDAEEP PKELSAGDAE VKQVDSVGEQ SKEQLPLATP VESHTKPSLA I // ID RM49_DROME STANDARD; PRT; 179 AA. AC Q9VYI3; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial 60s ribosomal protein L49 (MRP-L49). GN MRPL49 OR CG4647. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE L49EM FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003490; AAF48212.1; -. DR FlyBase; FBgn0030433; mRpL49. DR InterPro; IPR007740; Img2. DR InterPro; IPR001950; TIF_SUI1. DR Pfam; PF05046; Img2; 1. DR PROSITE; PS50296; SUI1; UNKNOWN_1. KW Ribosomal protein; Mitochondrion. SQ SEQUENCE 179 AA; 20658 MW; 5B8BEAE6A3E5A9FF CRC64; MATSAKLMLG SGLCQKLSQL TRQIHMQPAL MSSFRSSREV QELDKYPEVE VVANPPEWRF VERLLPAKTV PQPVEKPKYP SGWQPQKEDG SELGYHVART KNHMVPVYLH TRFRGQRRIT VVRRVQGDIW TLEKDLRAVV EQSRNGKVCA TRINELSGQI HFHGDHVDVL RDYLKEKGF // ID RM62_DROME STANDARD; PRT; 719 AA. AC P19109; Q8IGL7; Q95TB8; Q9I7P5; Q9VNK4; DT 01-NOV-1990 (Rel. 16, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative ATP-dependent RNA helicase P62. GN RM62 OR P62 OR CG10279. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM D). RX MEDLINE=91016833; PubMed=2170937; RA Dorer D.R., Christensen A.C., Johnson D.H.; RT "A novel RNA helicase gene tightly linked to the Triplo-lethal locus RT of Drosophila."; RL Nucleic Acids Res. 18:5489-5494(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM C). RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=A; CC IsoId=P19109-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=C; Synonyms=B, F; CC IsoId=P19109-2; Sequence=VSP_007413, VSP_007415; CC Note=No experimental confirmation available; CC Name=D; CC IsoId=P19109-3; Sequence=VSP_007414; CC Name=E; CC IsoId=P19109-4; Sequence=VSP_007413, VSP_007416; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. DDX5/DDX17 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52846; CAA37037.1; -. DR EMBL; AE003601; AAF51926.1; ALT_INIT. DR EMBL; AE003601; AAF51927.2; -. DR EMBL; AE003601; AAG22212.1; -. DR EMBL; AE003601; AAG22213.2; -. DR EMBL; AE003601; AAN14331.1; -. DR EMBL; AY060243; AAL25282.1; ALT_SEQ. DR EMBL; BT001716; AAN71471.1; -. DR PIR; S11485; S11485. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0003261; Rm62. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. KW ATP-binding; RNA-binding; Helicase; Nuclear protein; KW Alternative splicing. FT DOMAIN 153 225 GLY-RICH. FT NP_BIND 325 332 ATP (BY SIMILARITY). FT SITE 435 438 DEAD BOX. FT DOMAIN 671 713 GLY-RICH. FT VARSPLIC 1 141 Missing (in isoform C and isoform E). FT /FTId=VSP_007413. FT VARSPLIC 1 144 Missing (in isoform D). FT /FTId=VSP_007414. FT VARSPLIC 142 144 EGV -> MMM (in isoform C). FT /FTId=VSP_007415. FT VARSPLIC 142 145 EGVM -> MRAK (in isoform E). FT /FTId=VSP_007416. FT CONFLICT 195 195 R -> A (IN REF. 1). FT CONFLICT 675 675 R -> P (IN REF. 1). SQ SEQUENCE 719 AA; 78547 MW; A70A071A920B24FC CRC64; MLKLVQYIAP RVGGATPRPT ACGWGNLLLI SPRSGASSEK CITQRRHFLF SSASSSGTFA SSSSLCTEQR QQFHGSRRNR ETILFPSTYS SLQAQSQRAF RDSSKPDSDD YVDSIPKAEQ RTRTRKSLFN DPDERTEEIK IEGVMAPHDR DFGHSGRGGR GGDRGGDDRR GGGGGGNRFG GGGGGGDYHG IRNGRVEKRR DDRGGGNRFG GGGGFGDRRG GGGGGSQDLP MRPVDFSNLA PFKKNFYQEH PNVANRSPYE VQRYREEQEI TVRGQVPNPI QDFSEVHLPD YVMKEIRRQG YKAPTAIQAQ GWPIAMSGSN FVGIAKTGSG KTLGYILPAI VHINNQQPLQ RGDGPIALVL APTRELAQQI QQVATEFGSS SYVRNTCVFG GAPKGGQMRD LQRGCEIVIA TPGRLIDFLS AGSTNLKRCT YLVLDEADRM LDMGFEPQIR KIVSQIRPDR QTLMWSATWP KEVKQLAEDF LGNYIQINIG SLELSANHNI RQVVDVCDEF SKEEKLKTLL SDIYDTSESP GKIIIFVETK RRVDNLVRFI RSFGVRCGAI HGDKSQSERD FVLREFRSGK SNILVATDVA ARGLDVDGIK YVINFDYPQN SEDYIHRIGR TGRSNTKGTS FAFFTKNNAK QAKALVDVLR EANQEINPAL ENLARNSRYD GGGGRSRYGG GGGGGRFGGG GFKKGSLSNG RGFGGGGGGG GEGRHSRFD // ID RNT1_DROME STANDARD; PRT; 1180 AA. AC Q9VYS3; Q95RG9; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Regulator of nonsense transcripts 1 homolog. GN UPF1 OR CG1559. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Li P.W., Liao G., Miranda A., Mungall C.J., RA Nunoo J., Pacleb J.M., Paragas V., Park S., Phouanenavong S., RA Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ELIMINATES THE PRODUCTION OF NONSENSE-CONTAINING CC RNAS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE DNA2/NAM7 HELICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003487; AAF48115.2; -. DR EMBL; AY061379; AAL28927.1; -. DR FlyBase; FBgn0030354; Upf1. KW Hypothetical protein; Hydrolase; Helicase; ATP-binding; Zinc-finger. FT ZN_FING 108 136 C2H2-TYPE (ATYPICAL) (POTENTIAL). FT ZN_FING 160 190 C4-TYPE (Potential). FT NP_BIND 473 480 ATP (POTENTIAL). FT DOMAIN 931 1105 GLY-RICH. SQ SEQUENCE 1180 AA; 129912 MW; 150EAA970D221D0E CRC64; MSVDTYAPSS ALSFLDMDDN ELLPGADTQP TQYDYRDFTM PSTSQSQTQN DQLEIAQRCS AGDSHPRLAS ITNDLADLQF EEEDDEPGSS YVKELPPHAC KYCGIHDPAT VVMCNNCRKW FCNGRGSTSG SHIINHLVRA KHREVTLHGE GPLGETILEC YSCGVRNVFV LGFIPAKADS VVVLLCRQPC AAQNSLKDMN WDQEQWKPLI ADRCFLAWLV KQPSEQGQLR ARQISAAQIN KLEELWKENI EATFQDLEKP GIDSEPAHVL LRYEDGYQYE KTFGPLVRLE AEYDQKLKES ATQENIEVRW DVGLNKKTIA YFTLAKTDSD MKLMHGDELR LHYVGELYNP WSEIGHVIKV PDNFGDDVGL ELKSSTNAPV KCTSNFTVDF IWKCTSFDRM TRALCKFAID RNSVSNFIYS RLLGHGRADS NDEVLFRGPQ PKLFSAPHLP DLNRSQVYAV KHALQRPLSL IQGPPGTGKT VTSATIVYQL VKLHGGTVLV CAPSNTAVDQ LTEKIHRTNL KVVRVCAKSR EAIDSPVSFL ALHNQIRNME TNSELKKLQQ LKDETGELSS ADEKRYRNLK RAAENQLLEA ADVICCTCVG AGDGRLSRVK FTSILIDESM QSTEPECMVP VVLGAKQLIL VGDHCQLGPV VMCKKAARAG LSQSLFERLV VLGIRPFRLE VQYRMHPELS QFPSNFFYEG SLQNGVCAED RRLKLDFPWP QPERPMFFLV TQGQEEIAGS GTSFLNRTEA ANVEKITTRF LKAGIKPEQI GIITPYEGQR AYLVQYMQYQ GSLHSRLYQE IEIASVDAFQ GREKDIIIMS CVRSNERQGI GFLNDPRRLN VALTRAKFGI IIVGNPKVLA KQQLWNHLLN FYKDRKVLVE GSLNNLKESL IHFQKPKKLV NSMNIGAHFM STIIADAKEV MVPGSIYDRS GGYGQGRQMV GQSMNGGQYG GSGGGPYGNS PLGYGTPSSN SMVGFGLGNG GNGAAGGNNN FGGAGPSWAA AHLHHDSIGY ISNEHGAAAL GNMPVPVGMF MNMSNIPPRF YNQHQQAIMA VKQNRAIQQQ TGNFSPGNSG PGVTGVGVGR SATPGGNKKT NKLGKSRVTG GGTGGAPLTQ GSSVCNAAPY SQHPMPLSLQ MTQPSGFALS QQPELSQDFG QISQMDGLLS QDVAFNASGE RSLNQFSQPY // ID ROA1_DROME STANDARD; PRT; 365 AA. AC P07909; Q24359; Q24360; Q99361; Q9VAU7; Q9VAU8; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heterogeneous nuclear ribonucleoprotein A1 (hnRNP core protein A1-A) DE (PEN repeat clone P9). GN HRB98DE OR PEN9 OR CG9983. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Oregon-R; TISSUE=Pupae; RX MEDLINE=87175568; PubMed=3031652; RA Haynes S.R., Rebbert M.L., Mozer B.A., Forquignon F., Dawid I.B.; RT "Pen repeat sequences are GGN clusters and encode a glycine-rich RT domain in a Drosophila cDNA homologous to the rat helix destabilizing RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 84:1819-1823(1987). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS A; B; D AND E), AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo, Ovary, and Pupae; RX MEDLINE=90097842; PubMed=2104660; RA Haynes S.R., Raychaudhuri G., Beyer A.L.; RT "The Drosophila Hrb98DE locus encodes four protein isoforms RT homologous to the A1 protein of mammalian heterogeneous nuclear RT ribonucleoprotein complexes."; RL Mol. Cell. Biol. 10:316-323(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM D). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THIS PROTEIN IS A COMPONENT OF RIBONUCLEOSOMES. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=B; Synonyms=C; CC IsoId=P07909-1; Sequence=Displayed; CC Name=A; CC IsoId=P07909-2; Sequence=VSP_005827; CC Name=E; CC IsoId=P07909-3; Sequence=VSP_005828; CC Name=D; Synonyms=F; CC IsoId=P07909-4; Sequence=VSP_005829; CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC HIGHEST ZYGOTIC EXPRESSION FOUND IN ADULT FEMALES AND PUPAE. CC -!- SIMILARITY: BELONGS TO THE A/B GROUP OF HNRNP, WHICH ARE BASIC AND CC GLY-RICH PROTEINS. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M15766; AAA70426.1; -. DR EMBL; M25545; AAA28621.1; -. DR EMBL; M28871; AAA28621.1; JOINED. DR EMBL; M28872; AAA28621.1; JOINED. DR EMBL; M33955; AAA28621.1; JOINED. DR EMBL; M31560; AAA28621.1; JOINED. DR EMBL; M25545; AAA28622.1; -. DR EMBL; M28870; AAA28622.1; JOINED. DR EMBL; M28872; AAA28622.1; JOINED. DR EMBL; M33955; AAA28622.1; JOINED. DR EMBL; M31560; AAA28622.1; JOINED. DR EMBL; M25545; AAA28623.1; -. DR EMBL; M28870; AAA28623.1; JOINED. DR EMBL; M28872; AAA28623.1; JOINED. DR EMBL; M33955; AAA28623.1; JOINED. DR EMBL; M31560; AAA28623.1; JOINED. DR EMBL; M25545; AAA28624.1; -. DR EMBL; M28871; AAA28624.1; JOINED. DR EMBL; M28872; AAA28624.1; JOINED. DR EMBL; M33955; AAA28624.1; JOINED. DR EMBL; M31560; AAA28624.1; JOINED. DR EMBL; AE003766; AAF56800.2; -. DR EMBL; AE003766; AAF56801.1; -. DR EMBL; AE003766; AAN14141.1; -. DR EMBL; AE003766; AAN14143.1; -. DR EMBL; AY061448; AAL28996.1; -. DR PIR; A26459; A26459. DR HSSP; P09651; 1UP1. DR FlyBase; FBgn0001215; Hrb98DE. DR GO; GO:0030529; C:ribonucleoprotein complex; IDA. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 2. KW Nuclear protein; RNA-binding; Repeat; Ribonucleoprotein; KW Alternative splicing. FT DOMAIN 31 107 RNA-BINDING (RRM) 1. FT DOMAIN 122 199 RNA-BINDING (RRM) 2. FT DOMAIN 206 365 GLY-RICH. FT VARSPLIC 1 16 MVNSNQNQNGNSNGHD -> MGGHDNWNNGQNEEQ (in FT isoform A). FT /FTId=VSP_005827. FT VARSPLIC 1 21 MVNSNQNQNGNSNGHDDDFPQ -> MGGHDNWNNGQNEEQD FT (in isoform E). FT /FTId=VSP_005828. FT VARSPLIC 18 21 Missing (in isoform D). FT /FTId=VSP_005829. SQ SEQUENCE 365 AA; 39038 MW; BCC707CA2A2EC580 CRC64; MVNSNQNQNG NSNGHDDDFP QDSITEPEHM RKLFIGGLDY RTTDENLKAH FEKWGNIVDV VVMKDPRTKR SRGFGFITYS HSSMIDEAQK SRPHKIDGRV VEPKRAVPRQ DIDSPNAGAT VKKLFVGALK DDHDEQSIRD YFQHFGNIVD INIVIDKETG KKRGFAFVEF DDYDPVDKVV LQKQHQLNGK MVDVKKALPK QNDQQGGGGG RGGPGGRAGG NRGNMGGGNY GNQNGGGNWN NGGNNWGNNR GGNDNWGNNS FGGGGGGGGG YGGGNNSWGN NNPWDNGNGG GNFGGGGNNW NNGGNDFGGY QQNYGGGPQR GGGNFNNNRM QPYQGGGGFK AGGGNQGNYG GNNQGFNNGG NNRRY // ID ROP_DROME STANDARD; PRT; 597 AA. AC Q07327; Q24010; Q9VZH8; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ROP protein. GN ROP OR CS1 OR CG15811. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94008534; PubMed=8404533; RA Salzberg A., Cohen N., Halachmi N., Kimchie Z., Lev Z.; RT "The Drosophila Ras2 and Rop gene pair: a dual homology with a yeast RT Ras-like gene and a suppressor of its loss-of-function phenotype."; RL Development 117:1309-1319(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Iso-1 / Kennison; RX MEDLINE=95000659; PubMed=7917291; RA Harrison S.D., Broadie K., de Goor J., Rubin G.M.; RT "Mutations in the Drosophila Rop gene suggest a function in general RT secretion and synaptic transmission."; RL Neuron 13:555-566(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY BE A COMPONENT OF ONE OF THE VESICLE TRAFFICKING CC PATHWAYS. MAY INTERACT FUNCTIONALLY WITH RAS2 PROTEIN. CC -!- SUBCELLULAR LOCATION: SOLUBLE OR BOUND TO MEMBRANES (PROBABLE). CC -!- DEVELOPMENTAL STAGE: EXPRESSION IS LOW IN UNFERTILIZED EGGS AND CC EARLY EMBRYOS, INCREASES IN OLDER EMBRYOS AND YOUNG LARVAE, IS LOW CC IN MATURE LARVAE AND INCREASES STRONGLY IN PUPAE AND ADULT FLIES. CC EXPRESSION DURING EMBRYOGENESIS IS RESTRICTED TO THE CENTRAL CC NERVOUS SYSTEM (CNS) AND THE GARLAND CELLS, A SMALL GROUP OF CC NEPHROCYTES THAT TAKES UP WASTE MATERIALS FROM THE HEMOLYMPH BY CC ENDOCYTOSIS. IN POST EMBRYONIC STAGES, EXPRESSION IS SEEN IN THE CC LARVAL SALIVARY GLANDS AND THE CENTRAL NERVOUS SYSTEM (CNS), AND CC IN THE ADULT CNS AND REPRODUCTIVE SYSTEMS. CC -!- SIMILARITY: BELONGS TO THE STXBP/UNC-18/SEC1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67218; CAA47658.1; -. DR EMBL; X67219; CAA47659.1; -. DR EMBL; U15967; AAB60242.1; -. DR EMBL; AE003480; AAF47844.1; -. DR EMBL; AY052094; AAK93518.1; -. DR PIR; S33578; S33578. DR FlyBase; FBgn0004574; Rop. DR GO; GO:0005737; C:cytoplasm; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; IMP. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localiz...; IMP. DR GO; GO:0009416; P:response to light; IMP. DR GO; GO:0045045; P:secretory pathway; IMP. DR GO; GO:0007268; P:synaptic transmission; IMP. DR GO; GO:0016082; P:synaptic vesicle priming; NAS. DR InterPro; IPR001619; Sec1-like. DR Pfam; PF00995; Sec1; 1. KW Protein transport. FT CONFLICT 524 524 S -> L (IN REF. 1). SQ SEQUENCE 597 AA; 67850 MW; A70DB303C743821D CRC64; MALKVLVGQK LMNEVVKYKP PPPKKQGVTS AAGAGGMEWR VLVVDKLGMR MVSACTKMHE ISAEGITLVE DINKKREPLP TMDAIYLITP SDESVRGLIR DFENPARPMY RYAHVFFTEV CPEELFNDLC KSCAAGKIKT LKEINIAFLP YECQVFSLDS PDTFQCLYSP AFASIRSKHI ERIAEQIATL CATLGEYPNV RYRSDWDRNI DLAASVQQKL DAYKADDATM GEGPEKARSQ LLILDRGFDC VSPLLHELTL QAMAYDLLPI VNDVYRYTPG PNQPDKEVLL DENDDLWVEL RHEHIAVVST QVTQNLKKFT DSKRMGSADK SSMRDLSQMI KKMPQYQKEL SKYSTHLHLA EDCMKSYQNY VDKLCRVEQD LAMGTDAEGE KIKDHMRNIV PILLDANVSN YDKVRIIALY VMIKNGISEE NLTKLFTHAQ LSPKDQDMVR NLSCLGINVI ADSRKKQYSV PRKERTTEST YQMSRWTPVI KDIMEDCIED KLDLRHFPFL EGRAQNTNYH APTSARYGHW HKDKGQAQVK NVPRLIVFIV GGVSMSEMRC AYEVTNAVRN WEVLVGSSHI LSPEIFLSDL GSLSKED // ID ROR1_DROME STANDARD; PRT; 685 AA. AC Q24488; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase transmembrane receptor Ror precursor DE (EC 2.7.1.112) (dRor). GN ROR OR CG4926. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Larval brain; RX MEDLINE=93348222; PubMed=8394009; RA Wilson C., Goberdhan D.C.I., Steller H.; RT "Dror, a potential neurotrophic receptor gene, encodes a Drosophila RT homolog of the vertebrate Ror family of Trk-related receptor tyrosine RT kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 90:7109-7113(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 545-597 FROM N.A. RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). CC -!- FUNCTION: TYROSINE-PROTEIN KINASE RECEPTOR THAT FUNCTIONS DURING CC EARLY STAGES OF NEURONAL DEVELOPMENT. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN NEURONS OF THE DEVELOPING NERVOUS CC SYSTEM. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. ROR CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 FRIZZLED (FZ) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 KRINGLE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L20297; AAA28860.1; -. DR EMBL; AE003628; AAF52885.1; -. DR EMBL; AJ002908; CAA05743.1; -. DR PIR; A48289; A48289. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0010407; Ror. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004713; F:protein-tyrosine kinase activity; NAS. DR GO; GO:0007417; P:central nervous system development; IEP. DR GO; GO:0006468; P:protein amino acid phosphorylation; NAS. DR InterPro; IPR000024; Fz_domain. DR InterPro; IPR000001; Kringle. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002011; RecepttyrkinsII. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00051; kringle; 1. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00018; KRINGLE. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000395; Kringle; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00130; KR; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS00021; KRINGLE_1; 1. DR PROSITE; PS50070; KRINGLE_2; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. KW Transferase; Kinase; Tyrosine-protein kinase; ATP-binding; Receptor; KW Transmembrane; Signal; Glycoprotein; Kringle; Phosphorylation; KW Developmental protein. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 685 TYROSINE-PROTEIN KINASE TRANSMEMBRANE FT RECEPTOR ROR. FT DOMAIN 25 317 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 318 338 POTENTIAL. FT DOMAIN 339 685 CYTOPLASMIC (POTENTIAL). FT DOMAIN 36 225 FZ. FT DOMAIN 236 310 KRINGLE. FT DOMAIN 410 677 PROTEIN KINASE. FT NP_BIND 416 424 ATP (BY SIMILARITY). FT BINDING 442 442 ATP (BY SIMILARITY). FT ACT_SITE 539 539 BY SIMILARITY. FT MOD_RES 565 565 PHOSPHORYLATION (AUTO-) (BY FT SIMILARITY). FT MOD_RES 569 569 PHOSPHORYLATION (AUTO-) (BY FT SIMILARITY). FT MOD_RES 570 570 PHOSPHORYLATION (AUTO-) (BY FT SIMILARITY). FT CARBOHYD 45 45 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 63 63 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 129 129 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 144 144 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 250 250 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 685 AA; 78142 MW; 526162D27D5FD7C7 CRC64; MNKYSAFIVC ISLVLLFTKK DVGSHNVDSR IYGFQQSSGI CHIYNGTICR DVLSNAHVFV SPNLTMNDLE ERLKAAYGVI KESKDMNANC RMYALPSLCF SSMPICRTPE RTNLLYFANV ATNAKQLKNV SIRRKRTKSK DIKNISIFKK KSTIYEDVFS TDISSKYPPT RESENLKRIC REECELLENE LCQKEYAIAK RHPVIGMVGV EDCQKLPQHK DCLSLGITIE VDKTENCYWE DGSTYRGVAN VSASGKPCLR WSWLMKEISD FPELIGQNYC RNPGSVENSP WCFVDSSRER IIELCDIPKC ADKIWIAIVG TTAAIILIFI IIFAIILFKR RTIMHYGMRN IHNINTPSAD KNIYGNSQLN NAQDAGRGNL GNLSDHVALN SKLIERNTLL RINHFTLQDV EFLEELGEGA FGKVYKGQLL QPNKTTITVA IKALKENASV KTQQDFKREI ELISDLKHQN IVCILGVVLN KEPYCMLFEY MANGDLHEFL ISNSPTEGKS LSQLEFLQIA LQISEGMQYL SAHHYVHRDL AARNCLVNEG LVVKISDFGL SRDIYSSDYY RVQSKSLLPV RWMPSESILY GKFTTESDVW SFGVVLWEIY SYGMQPYYGF SNQEVINLIR SRQLLSAPEN CPTAVYSLMI ECWHEQSVKR PTFTDISNRL KTWHEGHFKA SNPEM // ID ROR2_DROME STANDARD; PRT; 724 AA. AC Q9V6K3; O02001; O96391; Q9TYH9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase transmembrane receptor Ror2 precursor DE (EC 2.7.1.112) (Neurospecific receptor tyrosine kinase). GN NRK OR ROR2 OR CG4007. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Frith K.J., Scott M.J.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 17-724 FROM N.A., AND CHARACTERIZATION. RC TISSUE=Imaginal disks; RX MEDLINE=97277331; PubMed=9115253; RA Oishi I., Sugiyama S., Liu Z.J., Yamamura H., Nishida Y., Minami Y.; RT "A novel Drosophila receptor tyrosine kinase expressed specifically RT in the nervous system. Unique structural features and implication in RT developmental signaling."; RL J. Biol. Chem. 272:11916-11923(1997). RN [5] RP SEQUENCE OF 586-638 FROM N.A. RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). CC -!- FUNCTION: TYROSINE-PROTEIN KINASE RECEPTOR THAT FUNCTIONS DURING CC EARLY STAGES OF NEURONAL DEVELOPMENT (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN NEURAL CELL LINEAGE FROM CC EMBRYONIC STAGE 11 ONWARDS, RESULTING IN EXPRESSION IN THE BRAIN CC AND VENTRAL NERVE CORD AT THE END OF EMBRYOGENESIS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT HIGH LEVELS IN EMBRYOS AND CC LARVAE, LOW LEVELS IN ADULTS AND PUPAE SHOW MAXIMAL EXPRESSION. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. ROR CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 FRIZZLED (FZ) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 KRINGLE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF037164; AAD02091.1; -. DR EMBL; AE003819; AAF58420.2; -. DR EMBL; AB001420; BAA20134.1; -. DR EMBL; AJ002920; CAA05755.1; -. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0020391; Nrk. DR GO; GO:0004713; F:protein-tyrosine kinase activity; IDA. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR GO; GO:0007165; P:signal transduction; IDA. DR InterPro; IPR000024; Fz_domain. DR InterPro; IPR000001; Kringle. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF01392; Fz; 1. DR Pfam; PF00051; kringle; 1. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00018; KRINGLE. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000395; Kringle; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS00021; KRINGLE_1; 1. DR PROSITE; PS50070; KRINGLE_2; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. KW Transferase; Kinase; Tyrosine-protein kinase; ATP-binding; Receptor; KW Transmembrane; Signal; Glycoprotein; Kringle; Phosphorylation; KW Developmental protein. FT SIGNAL 1 41 POTENTIAL. FT CHAIN 42 724 TYROSINE-PROTEIN KINASE TRANSMEMBRANE FT RECEPTOR ROR2. FT DOMAIN 42 322 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 323 343 POTENTIAL. FT DOMAIN 344 724 CYTOPLASMIC (POTENTIAL). FT DOMAIN 441 711 PROTEIN KINASE. FT NP_BIND 447 455 ATP (BY SIMILARITY). FT BINDING 475 475 ATP (BY SIMILARITY). FT ACT_SITE 580 580 BY SIMILARITY. FT MOD_RES 606 606 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT MOD_RES 610 610 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT MOD_RES 611 611 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT CONFLICT 51 51 V -> A (IN REF. 1). FT CONFLICT 192 192 H -> Y (IN REF. 4). FT CONFLICT 306 306 V -> G (IN REF. 1). FT CONFLICT 387 387 G -> V (IN REF. 4). FT CONFLICT 391 391 T -> M (IN REF. 4). FT CONFLICT 547 547 Q -> R (IN REF. 1 AND 4). FT CONFLICT 706 724 EINHCIQHSIAESECKAML -> RSTTASSTASPRASARQC FT FRGLPEK (IN REF. 4). SQ SEQUENCE 724 AA; 81836 MW; 0FFB9E1F7E4F6A26 CRC64; MAAGQWVGVV ERVLRGMVLK WGANLAVLGL CVFLFASATH ANSLNAIEEP VTRRHHQRHH EREREENGYC APYSGKVCKE YLTGQVWYSL EDPTGGWKNE QVTTALWDEL ISDLTGLCRE AAEKMLCAYA FPNCHMEGGR AVKAPLCFED CQATHLQFCY NDWVLIEEKK ERNMFIKSRG HFRLPNCSSL PHYNASMRRP NCSYIGLTEL KESEVSYDCR NGNGRFYMGT MNVSKSGIPC QRWDTQYPHK HFQPPLVFHQ LLEGENYCRN AGGEEPHPWC YTVDESVRWQ HCDIPMCPDY VDPNAVDLNT PIKMEKFFTP SMIFLLAGIG FVAIVTLHLM ILLVYKLSKH KDYSQPAGAA TAECSVSMRG GGDCGGNLNT SRETLGGNGN TNTLAKWGTI RSTATIHSNC VALTTVTNVS DAKGTKPNAR LEKLEYPRGD IVYVRSLGQG AFGRVFQARA PGLVPDQEDL LVAVKMLKDD ASDQMQMDFE REACLLAEFD HPNIVRLLGV CALGRPMCLL FEYMAPGDLS EFLRACSPYA THQAPTQDRL QLNELHLLQM AANIAAGMLY LSERKFVHRD LATRNCLINE HMAVKIADFG LSHKIYLQDY YKGDENDFIP IRWMPLESIL YNKFSLESDV WAYGICLWEV FSFALQPYFG LTHEEVIKYI KEGNVLGCPD NTPLSVYALM RRCWNRKPSE RPGFAEINHC IQHSIAESEC KAML // ID ROST_DROME STANDARD; PRT; 275 AA. AC O44252; Q9VLF9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Rolling stone protein. GN ROST OR CG9552. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Canton-S; TISSUE=Embryo, and Mesoderm; RX MEDLINE=97375664; PubMed=9230076; RA Paululat A., Goubeaud A., Damm C., Knirr S., Burchard S., RA Renkawitz-Pohl R.; RT "The mesodermal expression of rolling stone (rost) is essential for RT myoblast fusion in Drosophila and encodes a potential transmembrane RT protein."; RL J. Cell Biol. 138:337-348(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY HAVE A CENTRAL ROLE IN THE FUSION PROCESS DURING CC MYOGENESIS, WITHIN THE SOMATIC MESODERM. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED IN CELLS OF THE SOMATIC MESODERM, CC MOST NOTABLY THE MUSCLE FOUNDER CELLS, BETWEEN EMBRYONIC STAGES 12 CC AND 14, IN GROWING MUSCLE FIBERS IN DORSAL, LATERAL AND VENTRAL CC POSITIONS. AT STAGE 16 STRONGEST EXPRESSION IS IN SOME VENTRAL CC MUSCLES AND MUSCLE 8. AT STAGES 16/17 EXPRESSION IS RESTRICTED TO CC SOME CELLS OF THE CNS, THE BRAIN AND THE GONADS. CC -!- DEVELOPMENTAL STAGE: MATERNAL EXPRESSION IS SEEN IN EARLY 0-4HR CC EMBRYOS AND HIGH LEVELS OF ZYGOTIC EXPRESSION ARE SEEN IN EMBRYOS CC FROM STAGE 12 ONWARDS AND IN ADULTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF006955; AAB96894.1; -. DR EMBL; AE003623; AAF52733.1; -. DR FlyBase; FBgn0011705; rost. KW Developmental protein; Muscle protein; Transmembrane. FT TRANSMEM 45 65 POTENTIAL. FT TRANSMEM 72 92 POTENTIAL. FT TRANSMEM 127 147 POTENTIAL. FT TRANSMEM 162 182 POTENTIAL. FT TRANSMEM 185 205 POTENTIAL. FT TRANSMEM 232 252 POTENTIAL. FT CONFLICT 120 120 R -> T (IN REF. 1). SQ SEQUENCE 275 AA; 32635 MW; E166C66459B15C96 CRC64; MQLFDDFCKS FNKELQRANF GFAYNRVHLF YRSQWQKDEI NTIYLLYRWI WALFFLGVYI MCVIVQFCDG KFFIYMTNWG FGLCTITMLI SAVQVTCWHF DVRSTRSLVQ ESGHKAETSR GLKIYWWLYN MTLSLALIIS TVYWVFLHGK MNKPMRFPAI SIITHGMNSV MMLIDFLVIA FPLRILHMVY GMSLAIFFFL FTLIYHLCGG TDEFGNHYVY PILDWNNPNR CMVTFVGIFL LIMCYWVLLF GLYKLKRMFN RAFSVVWSPH AVGLI // ID RP16_DROME STANDARD; PRT; 1098 AA. AC Q9GQN0; Q9VXL6; Q9VXL7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ran-binding protein 16. GN RANBP16 OR CG9136/CG9126. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Goerlich D., Hartmann E.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY FUNCTION AS A NUCLEAR TRANSPORT RECEPTOR (BY CC SIMILARITY). CC -!- SUBUNIT: BINDS TO NUCLEOPORINS AND THE GTP-BOUND FORM OF RAN (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC, NUCLEAR AND NUCLEAR PORE CC COMPLEX (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE EXPORTIN FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF222744; AAG44254.1; -. DR EMBL; AE003500; AAF48541.2; ALT_SEQ. DR FlyBase; FBgn0053180; Ranbp16. DR GO; GO:0005737; C:cytoplasm; ISS. DR GO; GO:0005643; C:nuclear pore; ISS. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0005049; F:nuclear export signal receptor activity; ISS. DR GO; GO:0007391; P:dorsal closure; NAS. DR GO; GO:0006611; P:protein-nucleus export; ISS. DR InterPro; IPR008938; ARM. DR InterPro; IPR001494; Importinb_N. DR Pfam; PF03810; IBN_NT; 1. KW Nuclear protein; Transport; Protein transport. SQ SEQUENCE 1098 AA; 125532 MW; C8A3885CB3FDAEF5 CRC64; MDIQQLEVLC KQLYEATDIR IRSEAEKALV TFVSSQDALP KCQLLLQRAD SSYAQLLAAS TLTKLIQGLS LQERIDIRSY ALNYLATVPN LQHFVVQALV SLLAKLTKYG WFDSYKEEMV FQNLLEDVKK FLQGSVEHCT IGVQILSQLV CEMNSVVEMD VQVSFSKMRK IATSFRDQQL LETFLLSCSL LVSARDNSKN ISFMDESQQA LISHVLRLTK NCLSFDFIGS STDESADDMN NVQIPTAWRP AFLDSNTLKL FFDLYQILPN GLASYSISCL VQITSVRRSL FNNSERTKFL THLVEGVKDI LTTLHGLSDP DNYHEFCRLL ARLKSNYQLG ELIAVPCYPE AIQLIAKFTV ESLHLWLFAP NSVHYLLTLW QRMVASVPYV KSPDPHLLGT YTPEVIKAYI ESRLDAVPVI IRDNLDDPLD DFCMVQQQLE QLSVIERCEY NKTCNLLVQH FDQKAREYEN LLQTPNANSI DITIHELQLT WLVYIIGSAI VGRLTVATSD EHDTMDAELV IRVLQLMTLT DARLPQAGCE KLELAILSFL DQVRKMHSSE QAQKANLNKR LSEVFGLTDE QMLLSFINRK IITNLKFWGR SESIITKTLM LLSELSVHFN SVRKLARLEE VQFMLTHHTS EHFPFLGTNS SLSEMRCRTM FYTSLGRLLM FDLGEDEERF YNFLEPLTNQ FESLGSVMMD NNIFSNEEAK KVIIGLARDL RGLALPLNAR IQYTMLFEWL YYADYLPILL RAMDLWAHDP AVTTPILKLF AELVHCRTQR LAGNVSSPMG ILLFREASKL ICIYGNRILH QEVPRERLYP MRLKGIAICF LILKNSLGGN YVNCGVFKLY GDDTLDSVLN IIAKLILTIE QRDLIEYPKL STAYYNLLNC LSQDHVSYLA ALEPAAFVYI LKSLTKGLAA LDSATYISCC TILDSIVSYI FKQLQMKVST FPNKKLRSLN QENVQFLKVV EMNSELLQSM MSSLLNNVLQ EDCRNQWSMS RPLLVLILLY EDYYRSLKDR IICAQPIEKQ QTMAQWFDDL MVGIERNVSS KNKEKFTQNM STFRRDVVNL PKSTAAFSCD RPMCDGGFEP SEPESSPH // ID RPA1_DROME STANDARD; PRT; 1644 AA. AC P91875; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE DNA-directed RNA polymerase I largest subunit (EC 2.7.7.6). GN RPA1 OR RPI1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=97218024; PubMed=9065685; RA Knackmuss S., Bautz E.K.F., Petersen G.; RT "Identification of the gene coding for the largest subunit of RNA RT polymerase I (A) of Drosophila melanogaster."; RL Mol. Gen. Genet. 253:529-534(1997). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES. RNA POLYMERASE I IS ESSENTIALLY USED TO TRANSCRIBE CC RIBOSOMAL DNA UNITS. CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: EACH CLASS OF RNA POLYMERASE IS ASSEMBLED FROM 9 TO 14 CC DIFFERENT POLYPEPTIDES. THIS SUBUNIT IS THE LARGEST COMPONENT OF CC RNA POLYMERASE I. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES ARE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE RNA POLYMERASE BETA' CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y09103; CAA70321.1; -. DR PIR; T13803; T13803. DR FlyBase; FBgn0019938; RpI1. DR InterPro; IPR006592; RNA_polA_N. DR InterPro; IPR000722; RNA_pol_A. DR InterPro; IPR007080; RNA_pol_Rpb1_1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 1. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. DR SMART; SM00663; RPOLA_N; 1. KW Transferase; DNA-directed RNA polymerase; Transcription; Zinc; KW Zinc-finger; Nuclear protein. FT ZN_FING 66 81 C2H2-TYPE (POTENTIAL). SQ SEQUENCE 1644 AA; 185579 MW; D2CCA43B709910EA CRC64; MGSKRAMDVH MFPSDLEFAV FTDQEIRKLS VVKVITGITF DALGHAIPGG LYDIRMGSYG RCMDPCGTCL KLQDCPGHMG HIELGTPVYN PFFIKFVQRL LCIFCLHCYK LQMKDHECEI IMLQLRLIDA GYIIEAQELE LFKSEIVCQN TENLVAIKNG DMVHPHIAAM YKLLEKNEKN SSNSTKTSCS LRTAITHSAL QRLGKKCRHC NKSMRFVRYM HRRLVFYVTL ADIKERVGTG AETGGQNKVI FADECRRYLR QIYANYPELL KLLVPVLGLS NTDLTQGDRS PVDLFFMDTL PVTPPRARPL NMVGDMLKGN PQTDIYINII ENNHVLNVVL KYMKGGQEKL TEEAKAAYQT LKGETAHEKL YTAWLALQMS VDVLLDVNMS REMKSGEGLK QIIEKKCGLI RSHMMGKRVN YAARTVITPA YPNINVDEIG IPDIFAKKLS YPVPVTEWNV TDVRKMVMNG PDVHPGANYI QDKNGFTTYI PADNASKRES LAKLLLSNPK DGIKIVHRHV LNGDVLLLNR QPSLHKPSIM GHKARILHGE KTFRLHYSNC KAYNADFDGD EMNAHYPQSE VARAEAYNLV NVASNYLVPK DGTPLGGLIQ DHVISGVKLS IRGRFFNRED YQQLVFQGLS QLKKDIKLLP PTILKPAVLW SGKQILSTII INIIPEGYER INLDSFAKIA GKNWNVSRPR PPICGTNPEG NDLSESQVQI RNGELLVGVL DKQQYGATTY GLIHCMYELY GGDVSTLLVT AFTKVFTFFL QLEGFTLGVK DILVTDVADR KRRKIIRECR NVGNSAVAAA LELEDEPPHD ELVEKMEAAY VKDSKFRVLL DRKYKSLLDG YTNDINSTCL PRGLITKFPS NNLQLMVLSG AKGSMVNTMQ ISCLLGQIEL EGKRPPLMIS GKSLPSFTSF ETSPKSGGFI DGRFMTGIQP QDFFFHCMAG REGLIDTAVK TSRSGYLQRC LIKHLEGLSV HYDLTVRDSD NSVVQFLYGE DGLDILKSKF FNDKFCADFL TQNATAILRP AQLQLMKDEE QLVKVQRHEK HIRSWEKKKP AKLRAAFTHF SEELREEVEV KRPNEVNSKT GRRRFDEGLL KLWKKADAED KALYRKKYAR CPDPTVAVYK QDLYYGSVSE RTRKLITDYA KRKPALKETI ADIMRVKTIK SLAAPGEPVG LIAAQSIGEP STQMTLNTFH FAGRGEMNVT LGIPRLREIL MLASSNIKTP SMDIPIKPGQ QHQAEKLRIN LNSVTLANLL EYVHVSTGLT LDPERSYEYD MRFQFLPREV YKEDYGVRPK HIIKYMHQTF FKQLIPPPIL KVSNASRTTK IVVIDDKKDA DKDDDNDLDN GDEVGRSKAK ANDDDSSDDN DDDDATGVKL KQRKTDEKDY DDPDDVEELH DANDDDDEAE DEDDEEKGQD GNDNDGDDKA VERLLSNDMV KAYTYDKENH LWCQVKLNLS VRYQKPDLTS IIRELAGKSV VHQVQHIKRA IIYKGNDDDQ LLKTDGINIG EMFQHNKILD LNRLYSNDIH AIARTYGIEA ASQVIVKEVS NVFKVYGITV DRRHLSLIAD YMTFDGTFQP LSRKGMEHSS SPLQQMSFES SLQFLKSAAG FGRADELSSP SSRLMVGLPV RNGTGAFELL TKIC // ID RPA2_DROME STANDARD; PRT; 1129 AA. AC P20028; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE DNA-directed RNA polymerase I 135 kDa polypeptide (EC 2.7.7.6) DE (RNA polymerase I subunit 2). GN RPI135. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90158499; PubMed=2482932; RA Kontermann R., Sitzler S., Seifarth W., Petersen G., Bautz E.K.F.; RT "Primary structure and functional aspects of the gene coding for the RT second-largest subunit of RNA polymerase III of Drosophila."; RL Mol. Gen. Genet. 219:373-380(1989). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES. RNA POLYMERASE I IS ESSENTIALLY USED TO TRANSCRIBE CC RIBOSOMAL DNA UNITS. CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: EACH CLASS OF RNA POLYMERASE IS ASSEMBLED FROM 9 TO 14 CC DIFFERENT POLYPEPTIDES. THIS SUBUNIT IS THE SECOND LARGEST CC COMPONENT OF RNA POLYMERASE I. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES ARE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE RNA POLYMERASE BETA CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17298; CAA35185.1; -. DR PIR; JQ0354; JQ0354. DR FlyBase; FBgn0003278; RpI135. DR InterPro; IPR007121; RNA_pol_B. DR InterPro; IPR007644; RNA_pol_Rpb2_1. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007647; RNA_pol_Rpb2_5. DR InterPro; IPR007120; RNA_pol_Rpb2_6. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF04567; RNA_pol_Rpb2_5; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. KW Transferase; DNA-directed RNA polymerase; Transcription; Zinc; KW Zinc-finger; Nuclear protein. FT ZN_FING 1061 1093 C4-TYPE (POTENTIAL). SQ SEQUENCE 1129 AA; 128414 MW; E0A15FF1BCEF18D7 CRC64; MLEEMQQMKT IPVLTNSRPE FKQIPKKLSR HLANLGGPHV DSFDEMLTVG LDNSAKHMIP NHWLSPAGEK ISMKVESIWI AKPKVPQDVI DVRTREIYPT DSRQLHVSYS GMCSVRLGWS VNGVQKTPIN MDLGEVPIML RSKACNLGQA TPEEMVKHGE HDSEWGGIFV IRGNEKIVRM LIMTRRNHPI CVKRSSWKDR GQNFSDLGML VQTVREDESS LSNVVHYLNN GTAKFMFSHV KRLSYVPVCL ILKCLMDYTD EEIYNRLVQG YESDQYYVSC VQAMLREVQN ENVYTHAQCK SFIGNLFRAR FPEVPEWQPD DDVTDFILRE RVMIHLDTYE DKFQLIVFMI QKLFQCAQGK YKVENVDSSM MQEVLLPGHL YQKYLSERVE SWVSQVRRCL QKKLTSPDAL VTSAVMTQCM RQAGGVGRAI ESFLATGNIA SRTGLGLMQN SGLVIMAENI NRMRYMSHFR AIHRGSYFTT MRTTEARQLL PDAWGFICPV HTPDGTPCGL LNHLTLTCEI SMRPDPKLVK AIPKHLIDMG MMPLSNRRYL GEKLYVVFLD GKHLGHIHQS EAEKIVDELR YGKIFGTLPQ MMEIGFIPFK KNGQFPGLYI ATGPARLMRP VWNLKWKRVE YIGTLEQLYM EIAIDAKEMY PDFTTHLELA KTHFMSNLAN LIPMPDYNQS PRNMYQCQMG KQTMGTPCLN WPKQAANKLY RLQTPGTPLF RPVHYDIIQL DDFAMGTNAI VAVISYTGYD MEDAMIINKA AYERGFAYGS IYKTKFLTLD KKSSYFARHP HMPELIKHLD TDGLPHPGSK LSYGSPLYCY FDGEVATYKV VKMDEKEDCI VESIRQLGSF DLSPTKMVAI TLRVPRPATI GDKFASRAGQ KGICSQKYPA EDLPFTESGL IPDIVFNPHG FPSRMTIAMM IETMAGKGAA IHGNVYDATP FRFSEENTAI DYFGKMLEAG GYNYYGTERL YSGVDGREMT ADIFFGVVHY QRLRHMVFDK WQVRSTGAVE ARTHQPIKGR KRGGGVRFGE MERDALISHG AAFLLQDRLF HNSDKTHTLV CHKCGSILAP LQRIVKRNET GGLSSQPDTC RLCGDNSSVS MIEIPFSFKY LVTELSSVNI NARFKLNEI // ID RPB1_DROME STANDARD; PRT; 1887 AA. AC P04052; Q9VYX6; DT 01-NOV-1986 (Rel. 03, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-directed RNA polymerase II largest subunit (EC 2.7.7.6). GN RPII215 OR CG1554. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89218930; PubMed=2496296; RA Jokerst R.S., Weeks J.R., Zehring W.A., Greenleaf A.L.; RT "Analysis of the gene encoding the largest subunit of RNA polymerase RT II in Drosophila."; RL Mol. Gen. Genet. 215:266-275(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-27 FROM N.A. RX MEDLINE=87089662; PubMed=3025586; RA Searles L.L., Greenleaf A.L., Kemp W.E., Voelker R.A.; RT "Sites of P element insertion and structures of P element deletions in RT the 5' region of Drosophila melanogaster RpII215."; RL Mol. Cell. Biol. 6:3312-3319(1986). RN [4] RP SEQUENCE OF 1-472 FROM N.A. RX MEDLINE=85282618; PubMed=2992806; RA Biggs J., Searles L.L., Greenleaf A.L.; RT "Structure of the eukaryotic transcription apparatus: features of the RT gene for the largest subunit of Drosophila RNA polymerase II."; RL Cell 42:611-621(1985). RN [5] RP SEQUENCE OF 1441-1887 FROM N.A. RX MEDLINE=88094402; PubMed=3122024; RA Allison L.A., Wong J.K.-C., Fitzpatrick V.D., Moyle M., Ingles C.J.; RT "The C-terminal domain of the largest subunit of RNA polymerase II of RT Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a RT conserved structure with an essential function."; RL Mol. Cell. Biol. 8:321-329(1988). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES. CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: EACH CLASS OF RNA POLYMERASE IS ASSEMBLED FROM TEN TO CC TWELVE DIFFERENT POLYPEPTIDES. THE 215 KDA POLYPEPTIDE IS THE CC LARGEST COMPONENT OF RNA POLYMERASE II. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: THE TANDEM 7 RESIDUES REPEATS CAN BE HIGHLY PHOSPHORYLATED. CC THE PHOSPHORYLATION ACTIVATES POL2. CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES WERE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE RNA POLYMERASE BETA' CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27431; AAA28868.1; -. DR EMBL; AE003486; AAF48057.1; -. DR EMBL; M14203; AAA28864.1; -. DR EMBL; M11798; AAA28863.1; -. DR EMBL; M19537; AAA28827.1; -. DR PIR; S04457; RNFF2L. DR FlyBase; FBgn0003277; RpII215. DR InterPro; IPR006592; RNA_polA_N. DR InterPro; IPR000684; RNA_polII_repeat. DR InterPro; IPR000722; RNA_pol_A. DR InterPro; IPR007080; RNA_pol_Rpb1_1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR007075; RNA_pol_Rpb1_6. DR InterPro; IPR007073; RNA_pol_Rpb1_7. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 1. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. DR Pfam; PF04992; RNA_pol_Rpb1_6; 1. DR Pfam; PF04990; RNA_pol_Rpb1_7; 1. DR Pfam; PF05001; RNA_pol_Rpb1_R; 22. DR SMART; SM00663; RPOLA_N; 1. DR PROSITE; PS00115; RNA_POL_II_REPEAT; 11. KW Transferase; DNA-directed RNA polymerase; Transcription; Zinc; Repeat; KW DNA-binding; Nuclear protein; Phosphorylation; Zinc-finger. FT ZN_FING 67 83 C2H2-TYPE (POTENTIAL). FT DOMAIN 1579 1881 CARBOXYL-TERMINAL 7-RESIDUE REPEATS. FT CONFLICT 319 324 RAMQKS -> GYAKV (IN REF. 4). FT CONFLICT 450 450 F -> G (IN REF. 4). FT CONFLICT 455 458 TLHK -> RCTT (IN REF. 4). FT CONFLICT 463 472 GHRVKVLPWS -> VTGESVASST (IN REF. 4). FT CONFLICT 741 741 R -> H (IN REF. 1). FT CONFLICT 1485 1524 SMLGGAAMFIGGGSTPSMTPPMTPWANCNTPRYFSPPGHV FT -> I (IN REF. 5). FT CONFLICT 1506 1508 MTP -> ELDSA (IN REF. 1). FT CONFLICT 1887 1887 D -> DVRKGGRG (IN REF. 1). SQ SEQUENCE 1887 AA; 209167 MW; 4EC68C7708A167A3 CRC64; MSTPTDSKAP LRQVKRVQFG ILSPDEIRRM SVTEGGVQFA ETMEGGRPKL GGLMDPRQGV IDRTSRCQTC AGNMTECPGH FGHIDLAKPV FHIGFITKTI KILRCVCFYC SKMLVSPHNP KIKEIVMKSR GQPRKRLAYV YDLCKGKTIC EGGEDMDLTK ENQQPDPNKK PGHGGCGHYQ PSIRRTGLDL TAEWKHQNED SQEKKIVVSA ERVWEILKHI TDEECFILGM DPKYARPDWM IVTVLPVPPL AVRPAVVMFG AAKNQDDLTH KLSDIIKANN ELRKNEASGA AAHVIQENIK MLQFHVATLV DNDMPGMPRA MQKSGKPLKA IKARLKGKEG RIRGNLMGKR VDFSARTVIT PDPNLRIDQV GVPRSIAQNL TFPELVTPFN IDRMQELVRR GNSQYPGAKY IVRDNGERID LRFHPKSSDL HLQCGYKVER HLRDDDLVIF NRQPTLHKMS MMGHRVKVLP WSTFRMNLSC TSPYNADFDG DEMNLHVPQS METRAEVENI HITPRQIITP QANKPVMGIV QDTLTAVRKM TKRDVFITRE QVMNLLMFLP TWDAKMPQPC ILKPRPLWTG KQIFSLIIPG NVNMIRTHST HPDEEDEGPY KWISPGDTKV MVEHGELIMG ILCKKSLGTS AGSLLHICFL ELGHDIAGRF YGNIQTVINN WLLFEGHSIG IGDTIADPQT YNEIQQAIKK AKDDVINVIQ KAHNMELEPT PGNTLRQTFE NKVNRILNDA RDKTGGSAKK SLTEYNNLKA MVVSGSKGSN INISQVIACV GQQNVEGKRI PYGFRKRTLP HFIKDDYGPE SRGFVENSYL AGLTPSEFYF HAMGGREGLI DTAVKTAETG YIQRRLIKAM ESVMVNYDGT VRNSVGQLIQ LRYGEDGLCG ELVEFQNMPT VKLSNKSFEK RFKFDWSNER LMKKVFTDDV IKEMTDSSEA IQELEAEWDR LVSDRDSLRQ IFPNGESKVV LPCNLQRMIW NVQKIFHINK RLPTDLSPIR VIKGVKTLLE RCVIVTGNDR ISKQANENAT LLFQCLIRST LCTKYVSEEF RLSTEAFEWL VGEIETRFQQ AQANPGEMVG ALAAQSLGEP ATQMTLNTFH FAGVSSKNVT LGVPRLKEII NISKKPKAPS LTVFLTGGAA RDAEKAKNVL CRLEHTTLRK VTANTAIYYD PDPQRTVISE DQEFVNVYYE MPDFDPTRIS PWLLRIELDR KRMTDKKLTM EQIAEKINVG FGEDLNCIFN DDNADKLVLR IRIMNNEENK FQDEDEAVDK MEDDMFLRCI EANMLSDMTL QGIEAIGKVY MHLPQTDSKK RIVITETGEF KAIGEWLLET DGTSMMKVLS ERDVDPIRTS SNDICEIFQV LGIEAVRKSV EKEMNAVLQF YGLYVNYRHL ALLCDVMTAK GHLMAITRHG INRQDTGALM RCSFEETVDV LMDAAAHAET DPMRGVSENI IMGQLPKMGT GCFDLLLDAE KCRFGIEIPN TLGNSMLGGA AMFIGGGSTP SMTPPMTPWA NCNTPRYFSP PGHVSAMTPG GPSFSPSAAS DASGMSPSWS PAHPGSSPSS PGPSMSPYFP ASPSVSPSYS PTSPNYTASS PGGASPNYSP SSPNYSPTSP LYASPRYAST TPNFNPQSTG YSPSSSGYSP TSPVYSPTVQ FQSSPSFAGS GSNIYSPGNA YSPSSSNYSP NSPSYSPTSP SYSPSSPSYS PTSPCYSPTS PSYSPTSPNY TPVTPSYSPT SPNYSASPQY SPASPAYSQT GVKYSPTSPT YSPPSPSYDG SPGSPQYTPG SPQYSPASPK YSPTSPLYSP SSPQHSPSNQ YSPTGSTYSA TSPRYSPNMS IYSPSSTKYS PTSPTYTPTA RNYSPTSPMY SPTAPSHYSP TSPAYSPSSP TFEESED // ID RPB2_DROME STANDARD; PRT; 1176 AA. AC P08266; Q04155; Q95027; Q9VFM7; DT 01-AUG-1988 (Rel. 08, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-directed RNA polymerase II 140 kDa polypeptide (EC 2.7.7.6) DE (RNA polymerase II subunit 2). GN RPII140 OR CG3180. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=88011299; PubMed=3116266; RA Falkenburg D., Dworniczak B., Faust D.M., Bautz E.K.F.; RT "RNA polymerase II of Drosophila. Relation of its 140,000 Mr subunit RT to the beta subunit of Escherichia coli RNA polymerase."; RL J. Mol. Biol. 195:929-937(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 1-69 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=91276237; PubMed=1905256; RA Sitzler S., Oldenburg I., Peterson G., Bautz E.K.F.; RT "Analysis of the promoter region of the housekeeping gene DmRP140 by RT sequence comparison of Drosophila melanogaster and Drosophila RT virilis."; RL Gene 100:155-162(1991). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES. CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: EACH CLASS OF RNA POLYMERASE IS ASSEMBLED FROM 9 TO 14 CC DIFFERENT POLYPEPTIDES. RNA POLYMERASE II CONSISTS OF 10 DIFFERENT CC SUBUNITS. THIS SUBUNIT IS THE SECOND LARGEST COMPONENT OF RNA CC POLYMERASE II. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES ARE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE RNA POLYMERASE BETA CHAIN FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 43 LEADING TO AN ERRONEOUS GENE MODEL CC PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05709; CAA29180.2; ALT_FRAME. DR EMBL; AE003703; AAF55024.1; -. DR EMBL; BT003265; AAO25022.1; -. DR EMBL; M62972; AAA28476.1; -. DR PIR; A27826; A27826. DR FlyBase; FBgn0003276; RpII140. DR GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; NAS. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; NAS. DR GO; GO:0006366; P:transcription from Pol II promoter; NAS. DR InterPro; IPR007121; RNA_pol_B. DR InterPro; IPR007644; RNA_pol_Rpb2_1. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007646; RNA_pol_Rpb2_4. DR InterPro; IPR007647; RNA_pol_Rpb2_5. DR InterPro; IPR007120; RNA_pol_Rpb2_6. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF04566; RNA_pol_Rpb2_4; 1. DR Pfam; PF04567; RNA_pol_Rpb2_5; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. KW Transferase; DNA-directed RNA polymerase; Transcription; Zinc; KW Zinc-finger; Metal-binding; Nuclear protein. FT ZN_FING 1121 1142 C4-TYPE (POTENTIAL). FT CONFLICT 72 72 A -> R (IN REF. 1). FT CONFLICT 666 667 ID -> MY (IN REF. 1). SQ SEQUENCE 1176 AA; 134042 MW; 224821B335BED7F0 CRC64; MMYDNEEELY EEENAEEISH ELWQEACWIV INAYFDEKGL VRQQLDSFDE FIQMSVQRIV EDSPAIELQA EAQHTSGEVE TPPRFSLKFE QIYLSKPTHW EKDGSPSPMM PNEARLRNLT YSAPLYVDIT KTKNVEGLDP VETQHQKTFI GKIPIMLRST YCLLSQLTDR DLTELNECPL DPGGYFIING SEKVLIAQEK MATNTVYVFS MKDGKYAFKT EIRSCLEHSS RPTSTLWVNM MARGSQNIKK SAIGQRIIAI LPYIKQEIPI MIVFRALGFV ADRDILEHII YDFDDPEMME MVKPSLDEAF VVQEQNVALN FIGARGARPG VTKDKRIKYA KEILQKEMLP HVGVSDFCET KKAYFLGYMV HRLLLASLGR RELDDRDHYG NKRLDLAGPL LAFLFRGLFK NLMKEVRMYT QKFIDRGKDF NLELAIKTNI ITDGLRYSLA TGNWGDQKKA HQARAGVSQV LNRLTFASTL SHLRRVNSPI GRDGKLAKPR QLHNTLWGML CPAETPEGAA VGLVKNLALM AYISVGSQPS PILEFLEEWS MENLEEIAPS AIADATKIFV NGCWVGIHRD PEQLMATLRK LRRQMDIIVS EVSMIRDIRD REIRIYTDAG RICRPLLIVE NGSLLLKKTH VEMLKERDYN NYSWQVLVAS GVVEYIDTLE EETVMIAMSP YDLKQDKDYA YCTTYTHCEI HPAMILGVCA SIIPFPDHNQ SPRNTYQSAM GKQAMGVYIT NFHVRMDTLA HVLYYPMKPL VTTRSMEYLR FRELPAGINS IVAILCYTGY NQEDSVILNA SAVERGFFRS VFYRSYKDSE NKRVGDQEEN FEKPHRGTCQ GMRNAHYDKL DDDGIIAPGI RVSGDDVVIG KTITLPENDD ELDSNTKRFS KRDASTFLRN SETGIVDQVM LTLNSEGYKF CKIRVRSVRI PQIGDKFASR HGQKGTCGIQ YRQEDMAFTC EGLAPDIIIN PHAIPSRMTI GHLIECLQGK LGSNKGEIGD ATPFNDAVNV QKISTFLQEY GYHLRGNEVM YNGHTGRKIN AQVFLGPTYY QRLKHMVDDK IHSRARGPVQ ILVRQPMEGR ARDGGLRFGE MERDCQISHG AAQFLRERLF EVSDPYRVHI CNFCGLIAIA NLRNNTFECK GCKNKTQISQ VRLPYAAKLL FQELMSMNIA PRLMVT // ID RPB6_DROME STANDARD; PRT; 131 AA. AC Q24320; Q9VNA7; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-directed RNA polymerase II 14.4 kDa polypeptide (EC 2.7.7.6) DE (RPB6). GN RPII18 OR RPABC14 OR CG1163. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95379812; PubMed=7651387; RA Shpakovski G.V., Acker J., Wintzerith M., Lacroix J.F., Thuriaux P., RA Vigneron M.; RT "Four subunits that are shared by the three classes of RNA polymerase RT are functionally interchangeable between Homo sapiens and RT Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 15:4702-4710(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES. CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: RNA POLYMERASE II CONSISTS OF 12 DIFFERENT SUBUNITS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES ARE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE ARCHAEBACTERIA RPOK / EUKARYOTIC RPB6 CC RNA POLYMERASE SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z47726; CAA87655.1; -. DR EMBL; AE003603; AAF52039.1; -. DR PIR; S53013; S53013. DR FlyBase; FBgn0003275; RpII18. DR InterPro; IPR006111; RNA_polK_14kDa. DR InterPro; IPR006110; RNA_poly_Rpb6. DR InterPro; IPR009026; RNApol_RPB5_like. DR Pfam; PF01192; RNA_pol_Rpb6; 1. DR PROSITE; PS01111; RNA_POL_K_14KD; 1. KW Transferase; DNA-directed RNA polymerase; Transcription; KW Nuclear protein. SQ SEQUENCE 131 AA; 14722 MW; AAA7F7794EB3DF68 CRC64; MDDADYDNDD VGGDDFDDVD EDVDEDINQE EEADNIEIIA PGGAGGGGVP KSKRITTKYM TKYERARVLG TRALQIAMCA PIMVELDGET DPLQIAMKEL KQKKIPIIIR RYLPDHSYED WSIDELIMVD N // ID RPB9_DROME STANDARD; PRT; 129 AA. AC P36958; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE DNA-directed RNA polymerase II 15.1 kDa polypeptide (EC 2.7.7.6). GN RPII15. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92186877; PubMed=1545824; RA Harrison D.A., Mortin M.A., Corces V.G.; RT "The RNA polymerase II 15-kilodalton subunit is essential for RT viability in Drosophila melanogaster."; RL Mol. Cell. Biol. 12:928-935(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94063084; PubMed=8243669; RA Liu Z., Kontermann R.E., Schulze R.A., Petersen G., Bautz E.K.; RT "RPII15 codes for the M(r) 15,000 subunit 9 of Drosophila melanogaster RT RNA polymerase II."; RL FEBS Lett. 335:73-75(1993). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES. CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: RNA POLYMERASE II CONSISTS OF 12 DIFFERENT SUBUNITS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES ARE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE ARCHAEAL RPOM / EUKARYOTIC CC RPA12/RPB9/RPC11 RNA POLYMERASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 RIBBON-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S88139; AAB21674.1; -. DR EMBL; S66940; AAB29028.2; -. DR FlyBase; FBgn0004855; RpII15. DR InterPro; IPR001529; RNA_polM. DR InterPro; IPR001222; TFIIS. DR Pfam; PF02150; RNA_POL_M_15KD; 1. DR Pfam; PF01096; TFIIS; 1. DR SMART; SM00661; RPOL9; 1. DR SMART; SM00440; ZnF_C2C2; 1. DR PROSITE; PS00466; TFIIS; 1. DR PROSITE; PS01030; RNA_POL_M_15KD; 1. KW Transferase; DNA-directed RNA polymerase; Transcription; KW Nuclear protein; Zinc-finger. FT ZN_FING 21 46 C4-TYPE (POTENTIAL). FT ZN_FING 90 122 ZN-RIBBON (POTENTIAL). FT CONFLICT 51 53 KTN -> EAD (IN REF. 2). FT CONFLICT 100 100 F -> S (IN REF. 2). FT CONFLICT 102 102 K -> Q (IN REF. 2). SQ SEQUENCE 129 AA; 15126 MW; B2D1702B2B759301 CRC64; MTTAFDAAHT EGPGFVGIRF CQECNNMLYP KEDKENKILL YACRNCDYKQ KTNSNCIYVN KIMHEIDELT HIVPDVISDP TLPRTEDHAC PKCSHREAVF FKAQTRRAEE EMRLYYVCTN QNCTHRWTE // ID RPBX_DROME STANDARD; PRT; 67 AA. AC Q9VC49; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-directed RNA polymerase II 7.6 kDa polypeptide (EC 2.7.7.6) DE (RPB10) (RPB7.6). GN RPB10 OR CG13628. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES. CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: RNA POLYMERASE II CONSISTS OF 12 DIFFERENT SUBUNITS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES ARE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE ARCHAEBACTERIA RPON / EUKARYOTIC RPB10 CC RNA POLYMERASE SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003749; AAF56326.1; -. DR HSSP; O26147; 1EF4. DR FlyBase; FBgn0039218; Rpb10. DR InterPro; IPR000268; RNA_pol_N. DR Pfam; PF01194; RNA_pol_N; 1. DR ProDom; PD006539; RNA_pol_N; 1. DR PROSITE; PS01112; RNA_POL_N_8KD; 1. KW Transferase; DNA-directed RNA polymerase; Transcription; KW Nuclear protein; Zinc; Metal-binding. FT METAL 7 7 ZINC (BY SIMILARITY). FT METAL 10 10 ZINC (BY SIMILARITY). FT METAL 44 44 ZINC (BY SIMILARITY). FT METAL 45 45 ZINC (BY SIMILARITY). SQ SEQUENCE 67 AA; 7661 MW; D543D08667E97DAB CRC64; MIIPIRCFTC GKVIGNKWES YLGLLQAEYT EGDALDALGL KRYCCRRMLL GHVDLIEKLL NYAPLEK // ID RPBY_DROME STANDARD; PRT; 117 AA. AC Q9VJE4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-directed RNA polymerase II 13.3 kDa polypeptide (EC 2.7.7.6) DE (RPB11). GN RPB11 OR CG6840. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: RNA POLYMERASE II CONSISTS OF 12 DIFFERENT SUBUNITS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES ARE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE ARCHAEBACTERIA RPOL / EUKARYOTIC RPB11/ CC RPC19 RNA POLYMERASE SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003655; AAF53606.1; -. DR FlyBase; FBgn0032634; Rpb11. DR InterPro; IPR009025; RBP11-like_RNApo. DR InterPro; IPR008193; RNA_pol_L. DR InterPro; IPR008194; RNA_pol_L_sub. DR Pfam; PF01193; RNA_pol_L; 1. DR ProDom; PD004240; RNA_pol_L_sub; 1. DR PROSITE; PS01154; RNA_POL_L_13KD; 1. KW Transferase; DNA-directed RNA polymerase; Transcription; KW Nuclear protein. SQ SEQUENCE 117 AA; 13385 MW; EFCA3D43E4947943 CRC64; MNAPPTFESF LLYEGEKKII KELDTKVTNA AIFTINKEDH TLGNMIRNQL LKDPNVLFAG YKVPHPLEHK FVIRIQTTAD YSPQEAFMNA ITDLLAELSL FEERFKDAIK EKKEGGD // ID RPC2_DROME STANDARD; PRT; 1135 AA. AC P25167; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE DNA-directed RNA polymerase III 128 kDa polypeptide (EC 2.7.7.6) DE (RNA polymerase III subunit 2). GN RPIII128 OR RP128. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91375428; PubMed=1910149; RA Seifarth W., Petersen G., Kontermann R., Riva M., Huet J.-C., RA Bautz E.K.F.; RT "Identification of the genes coding for the second-largest subunits of RT RNA polymerases I and III of Drosophila melanogaster."; RL Mol. Gen. Genet. 228:424-432(1991). CC -!- FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION CC OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS CC SUBSTRATES. CC -!- CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE + CC {RNA}(N). CC -!- SUBUNIT: RNA POLYMERASE III CONSISTS OF ABOUT 15 DIFFERENT CC SUBUNITS. THIS SUBUNIT IS THE SECOND LARGEST COMPONENT OF RNA CC POLYMERASE III. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: THREE DISTINCT ZINC-CONTAINING RNA POLYMERASES WERE CC FOUND IN EUKARYOTIC NUCLEI: POLYMERASE I FOR THE RIBOSOMAL RNA CC PRECURSOR, POLYMERASE II FOR THE MRNA PRECURSOR, AND POLYMERASE CC III FOR 5S AND TRNA GENES. CC -!- SIMILARITY: BELONGS TO THE RNA POLYMERASE BETA CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58826; CAA41631.1; -. DR PIR; S16894; RNFF32. DR FlyBase; FBgn0004463; RpIII128. DR InterPro; IPR007121; RNA_pol_B. DR InterPro; IPR007644; RNA_pol_Rpb2_1. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007646; RNA_pol_Rpb2_4. DR InterPro; IPR007647; RNA_pol_Rpb2_5. DR InterPro; IPR007120; RNA_pol_Rpb2_6. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF04566; RNA_pol_Rpb2_4; 1. DR Pfam; PF04567; RNA_pol_Rpb2_5; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. KW Transferase; DNA-directed RNA polymerase; Transcription; Zinc; KW Zinc-finger; Nuclear protein. FT ZN_FING 1084 1099 C4-TYPE (POTENTIAL). SQ SEQUENCE 1135 AA; 128373 MW; 9BE52220B05C08D1 CRC64; MVELKMGDHN VEATTWDPGD SKDWSVPIKP LTEKWKLVPA FLQVKGLVKQ HIDSFNHFIN VDIKKIVKAN ELVTSGADPL FYLKYLDVRV GKPDIDDGFN ITKATTPHEC RLRDTTYSAP ITVDIEYTRG TQRIKRNNLL IGRMPLMLRS NCALTGKSEF ELSKLNECPL DPGGYFVVRG QEKVILIQEQ LSWNKMLTED FNGVVQCQVT SSTHEKKSRT LVLSKHGKYY LKHNSMTDDI PIVVIFKALG VVSDQEIQSL IGIDSKSQNR FGASLIDAYN LKVFTQQRAL EYMGSKLVVK RFQSATTKTP SEEARELLLT TILAHVPVDN FNLQMKAIYV SMMVRRVMAA ELDKTLFDDR DYYGNKRLEL AGSLLSMMFE DLFKRMNWEL KTIADKNIPK VKAAQFDVVK HMRAAQITAG LESAISSGNW TIKRFKMERA GVTQVLSRLS YISALGMMTR VNSQFEKTRK VSGPRSLQPS QWGMLCPSYT PEGEACGLVK NLALMTHITT EVEERPVMIV AFNAGVEDIR EVSGNPINNP NVFLVFINGN VLGLTLNHKH LVRNLRYMRR KGRMGSYVSV HTSYTQRCIY IHTDGGRLCR PYVIVENRRP LVKQHHLDEL NRGIRKFDDF LLDGLIEYLD VNEENDSFIA WNEDQIEDRT THLEIETFTL LGVCAGLVPY PHHNQSPRNT YQCAMGKQAM GMIGYNHNNR IDSLMYNLVY PHAPMVKSKT IELTNFDKLP AGQNATVAVM SYSGYDIEDA LILNKASIDR GYGRCLVYKN SKCTVKRYAN QTFDRIMGPM KDALTNKVIF KHDVLDTDGI VAPGEQVQNK QIMINKEMPA VTSMNPLQGQ SAQVPYTAVP ISYKGPEPSY IERVMVSANA EEDFLIKILL RQTRIPRGDK FSSRHGQKGV TGLIVEQEDM PFNDFGICPD MIMNPHGFPS RMTVGKTLEL LGGKAGLLEG KFHYGTAFGG SKVEDIQAEL ERHGFNYVGK DFFYSGITGT PLEAYIYSGP VYYQKLKHMV QDKMHARARG PKAVLTRQPT QGRSREGGLR LGEMERDCLI SYGASMLIME RLMISSDAFE VDVCRTCGRM AYCSWCHFCQ SSANVSKISM PYACKLLFQE LTSMNVVPKM ILENY // ID RPR_DROME STANDARD; PRT; 65 AA. AC Q24475; Q9VVP7; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Reaper protein. GN RPR OR CG4319. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Eye imaginal disk; RX MEDLINE=94225205; PubMed=8171319; RA White K., Grether M.E., Abrams J.M., Young L., Farrell K., Steller H.; RT "Genetic control of programmed cell death in Drosophila."; RL Science 264:677-683(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PLAYS A CENTRAL AND GLOBAL REGULATORY FUNCTION FOR THE CC INITIATION OF APOPTOSIS. ECTOPIC EXPRESSION IN THE DEVELOPING EYE CC RESULTS IN A SMALL EYE OWING TO EXCESS CELL DEATH. CC -!- DEVELOPMENTAL STAGE: EXPRESSION CORRESPONDS TO THE PATTERN OF CC PROGRAMMED CELL DEATH IN THE EMBRYO. CC -!- SIMILARITY: LIMITED AT THE N-TERMINAL, TO HID AND GRIM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L31631; AAA18983.1; -. DR EMBL; AE003520; AAF49264.1; -. DR FlyBase; FBgn0011706; rpr. DR GO; GO:0006917; P:induction of apoptosis; IGI. KW Apoptosis. SQ SEQUENCE 65 AA; 7682 MW; 57F231379AFEEA3C CRC64; MAVAFYIPDQ ATLLREAEQK EQQILRLRES QWRFLATVVL ETLRQYTSCH PKTGRKSGKY RKPSQ // ID RRP1_DROME STANDARD; PRT; 679 AA. AC P27864; Q9VQJ4; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Recombination repair protein 1 (DNA-(apurinic or apyrimidinic site) DE lyase) (EC 4.2.99.18). GN RRP1 OR CG3178. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91319767; PubMed=1713691; RA Sander M., Lowenhaupt K., Rich A.; RT "Drosophila Rrp1 protein: an apurinic endonuclease with homologous RT recombination activities."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6780-6784(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91360356; PubMed=1653418; RA Sander M., Lowenhaupt K., Lane W.S., Rich A.; RT "Cloning and characterization of Rrp1, the gene encoding Drosophila RT strand transferase: carboxy-terminal homology to DNA repair RT endo/exonucleases."; RL Nucleic Acids Res. 19:4523-4529(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Tsoi S.C.M., Huang S.M., Sander M.; RT "Genomic organization of the Drosophlia 23C genetic interval: RT identification of 3 genes in the 10Kb region surrounding the RRP1 RT gene."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP CHARACTERIZATION. RX MEDLINE=97078668; PubMed=8918793; RA Sander M., Benhaim D.; RT "Drosophila Rrp1 3'-exonuclease: demonstration of DNA sequence RT dependence and DNA strand specificity."; RL Nucleic Acids Res. 24:3926-3933(1996). CC -!- FUNCTION: COULD PROMOTE HOMOLOGOUS RECOMBINATION AT SITES OF DNA CC DAMAGE. RRP1 HAS APURINIC ENDONUCLEASE AND DOUBLE-STRANDED DNA 3' CC EXONUCLEASE, ACTIVITIES AND CARRIES OUT SINGLE-STRANDED DNA CC RENATURATION IN A MG(2+)-DEPENDENT MANNER. CC -!- CATALYTIC ACTIVITY: THE C-O-P BOND 3' TO THE APURINIC OR CC APYRIMIDINIC SITE IN DNA IS BROKEN BY A BETA-ELIMINATION REACTION, CC LEAVING A 3'-TERMINAL UNSATURATED SUGAR AND A PRODUCT WITH A CC TERMINAL 5'-PHOSPHATE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE AP/EXOA FAMILY OF DNA REPAIR ENZYMES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M62472; AAA62769.1; -. DR EMBL; AF073994; AAC27621.1; -. DR EMBL; AE003581; AAF51175.1; -. DR PIR; S28366; S28366. DR HSSP; P27695; 1HD7. DR FlyBase; FBgn0004584; Rrp1. DR InterPro; IPR000097; APendonclse1. DR InterPro; IPR005135; Exo_endo_phos. DR InterPro; IPR004808; ExoIII_xth. DR Pfam; PF03372; Exo_endo_phos; 1. DR TIGRFAMs; TIGR00195; exoDNase_III; 1. DR TIGRFAMs; TIGR00633; xth; 1. DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1. DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1. DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1. KW DNA repair; Lyase; Nuclear protein. FT DOMAIN 428 679 AP ENDONUCLEASE. FT METAL 461 461 MAGNESIUM OR MANGANESE (BY SIMILARITY). FT ACT_SITE 670 670 GENERAL BASE (BY SIMILARITY). FT CONFLICT 76 76 V -> A (IN REF. 4). SQ SEQUENCE 679 AA; 74662 MW; 161BFE44F7A8AEE2 CRC64; MPRVKAVKKQ AEALASEPTD PTPNANGNGV DENADSAAEE LKVPAKGKPR ARKATKTAVS AENSEEVEPQ KAPTAVARGK KKQPKDTDEN GQMEVVAKPK GRAKKATAEA EPEPKVDLPA GKATKPRAKK EPTPAPDEVT SSPPKGRAKA EKPTNAQAKG RKRKELPAEA NGGAEEAAEP PKQRARKEAV PTLKEQAEPG TISKEKVQKA ETAAKRARGT KRLADSEIAA ALDEPEVDEV PPKAASKRAK KGKMVEPSPE TVGDFQSVQE EVESPPKTAA APKKRAKKTT NGETAVELEP KTKAKPTKQR AKKEGKEPAP GKKQKKSADK ENGVVEEEAK PSTETKPAKG RKKAPVKAED VEDIEEAAEE SKPARGRKKA AAKAEEPDVD EESGSKTTKK AKKAETKTTV TLDKDAFALP ADKEFNLKIC SWNVAGLRAW LKKDGLQLID LEEPDIFCLQ ETKCANDQLP EEVTRLPGYH PYWLCMPGGY AGVAIYSKIM PIHVEYGIGN EEFDDVGRMI TAEYEKFYLI NVYVPNSGRK LVNLEPRMRW EKLFQAYVKK LDALKPVVIC GDMNVSHMPI DLENPKNNTK NAGFTQEERD KMTELLGLGF VDTFRHLYPD RKGAYTFWTY MANARARNVG WRLDYCLVSE RFVPKVVEHE IRSQCLGSDH CPITIFFNI // ID RS12_DROME STANDARD; PRT; 139 AA. AC P80455; Q9VU40; DT 01-NOV-1995 (Rel. 32, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S12. GN RPS12 OR RPS12E OR CG11271. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RA Greig S.R.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE S12E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X89659; CAA61806.1; ALT_INIT. DR EMBL; AE003539; AAF49851.1; -. DR EMBL; AY058531; AAL13760.1; -. DR FlyBase; FBgn0014027; RpS12. DR InterPro; IPR004038; Ribosomal_L7A. DR InterPro; IPR000530; Ribosomal_S12e. DR Pfam; PF01248; Ribosomal_L7Ae; 1. DR PRINTS; PR00972; RIBSOMALS12E. DR PROSITE; PS01189; RIBOSOMAL_S12E; 1. KW Ribosomal protein. SQ SEQUENCE 139 AA; 15168 MW; 4810D50ADC87C253 CRC64; MADVDVDVPS AAPVLDGAMD INTALQEVLK KSLIADGLVH GIHQACKALD KRQAVLCILA ESFDEPNYKK LVTALCNEHQ IPLIRVDSHK KLGEWSGLCK IDKEGKPRKV CGCSVVVIKD FGEETPALDV VKDHLRQNS // ID RS13_DROME STANDARD; PRT; 150 AA. AC Q03334; Q9VLN5; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S13. GN RPS13 OR RP17 OR M(2)32A OR CG13389. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=93281413; PubMed=8506150; RA McNabb S., Ashburner M.; RT "Identification of a Drosophila protein similar to rat S13 and RT archaebacterial S11 ribosomal proteins."; RL Nucleic Acids Res. 21:2523-2523(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=96363921; PubMed=8725235; RA Saeboe-Larssen S., Lambertsson A.; RT "A novel Drosophila Minute locus encodes ribosomal protein S13."; RL Genetics 143:877-885(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE S15P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X91854; CAA62965.1; -. DR EMBL; X91853; CAA62964.1; -. DR EMBL; Z19052; CAA79496.1; -. DR EMBL; AE003621; AAF52649.1; -. DR EMBL; AY058536; AAL13765.1; -. DR PIR; S70391; S33684. DR FlyBase; FBgn0010265; RpS13. DR InterPro; IPR000589; Ribosomal_S15. DR Pfam; PF00312; Ribosomal_S15; 1. DR PROSITE; PS00362; RIBOSOMAL_S15; 1. KW Ribosomal protein. FT INIT_MET 0 0 BY SIMILARITY. FT CONFLICT 39 48 LGKKGLTPSK -> AGQEGSDSLQ (IN REF. 1). SQ SEQUENCE 150 AA; 17047 MW; E4A79BF4B89FDC9D CRC64; GRMHAPGKGI SQSALPYRRT VPSWLKLNAD DVKEQIKKLG KKGLTPSKIG IILRDSHGVA QVRFVNGNKI LRIMKSVGLK PDIPEDLYHM IKKAVAIRKH LERNRKDKDG KFRLILVESR IHRLARYYKT KSVLPPNWKY ESSTASALVA // ID RS14_DROME STANDARD; PRT; 151 AA. AC P14130; Q9V3R5; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S14. GN (RPS14A OR CG1524) AND (RPS14B OR CG1527). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89039859; PubMed=3141788; RA Brown S.J., Rhoads D.D., Stewart M.J., van Slyke B., Chen I.-T., RA Johnson T.K., Denell R.E., Roufa D.J.; RT "Ribosomal protein S14 is encoded by a pair of highly conserved, RT adjacent genes on the X chromosome of Drosophila melanogaster."; RL Mol. Cell. Biol. 8:4314-4321(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE S11P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M21045; AAA28853.1; -. DR EMBL; M21045; AAA28852.1; -. DR EMBL; AE003442; AAF46297.1; -. DR EMBL; AE003442; AAF46299.1; -. DR PIR; A30815; A30815. DR FlyBase; FBgn0004403; RpS14a. DR FlyBase; FBgn0004404; RpS14b. DR InterPro; IPR001971; Ribosomal_S11. DR Pfam; PF00411; Ribosomal_S11; 1. DR ProDom; PD001010; Ribosomal_S11; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. KW Ribosomal protein. SQ SEQUENCE 151 AA; 16265 MW; 7FD3C0E7A32C4216 CRC64; MAPRKAKVQK EEVQVQLGPQ VRDGEIVFGV AHIYASFNDT FVHVTDLSGR ETIARVTGGM KVKADRDEAS PYAAMLAAQD VAEKCKTLGI TALHIKLRAT GGNKTKTPGP GAQSALRALA RSSMKIGRIE DVTPIPSDST RRKGGRRGRR L // ID RS17_DROME STANDARD; PRT; 130 AA. AC P17704; Q9V3P5; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S17. GN RPS17 OR M(3)67C OR CG3922. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90006758; PubMed=2507396; RA Maki C., Rhoads D.D., Stewart M.J., van Slyke B., Denell R.E., RA Roufa D.J.; RT "The Drosophila melanogaster RPS17 gene encoding ribosomal protein RT S17."; RL Gene 79:289-298(1989). RN [2] RP SEQUENCE FROM N.A. RA Zhang B., Georgiev O., Schaffner W.; RT "Characterization of the Drosophila gene for the heavy metal- RT responsive transcription factor MTF-1."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE S17E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22142; AAA28869.1; -. DR EMBL; AE003552; AAF50272.1; -. DR EMBL; AJ271817; CAB72251.1; -. DR PIR; JU0055; R4FF17. DR FlyBase; FBgn0005533; RpS17. DR InterPro; IPR001210; Ribosomal_S17E. DR Pfam; PF00833; Ribosomal_S17e; 1. DR PROSITE; PS00712; RIBOSOMAL_S17E; 1. KW Ribosomal protein. FT INIT_MET 0 0 SQ SEQUENCE 130 AA; 15153 MW; D191EECC2CE53DF2 CRC64; GRVRTKTVKK AAKVIIEKYY TRLTLDFHTN KRICEEVAII PTKPLRNKIA GYVTHLMGRL RHSQVRGISI KLQEEERERR DNYVPAVSAL EQDIIEVDAD TKEMLKLLDF HNIRGLQLTQ PNTNNFGRRN // ID RS18_DROME STANDARD; PRT; 152 AA. AC P41094; Q9V911; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S18. GN RPS18 OR CG8900. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Canton-S; RX MEDLINE=94215909; PubMed=8163194; RA Garwood J., Lepesant J.-A.; RT "The Drosophila melanogaster homolog of ribosomal protein S18."; RL Gene 141:231-235(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: LOCATED AT THE TOP OF THE HEAD OF THE 40S SUBUNIT, IT CC CONTACTS SEVERAL HELICES OF THE 18S RRNA (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P41094-1; Sequence=Displayed; CC Name=Short; CC IsoId=P41094-2; Sequence=VSP_005721, VSP_005722; CC -!- SIMILARITY: BELONGS TO THE S13P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L22959; AAA28870.1; -. DR EMBL; AE003792; AAM68401.1; -. DR EMBL; AE003792; AAM68402.1; -. DR FlyBase; FBgn0010411; RpS18. DR InterPro; IPR001892; Ribosomal_S13. DR Pfam; PF00416; Ribosomal_S13; 1. DR ProDom; PD001363; Ribosomal_S13; 1. DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1. DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1. KW Ribosomal protein; RNA-binding; rRNA-binding; Alternative splicing. FT VARSPLIC 58 101 ECTEEEVDKVVTIISNPLQYKVPNWFLNRQKDIIDGKYWQL FT TSS -> RQGGDHHLEPSAVQGAQLVPQQAEGHHRWQVLAA FT DLLQLGLEAA (in isoform Short). FT /FTId=VSP_005721. FT VARSPLIC 102 152 Missing (in isoform Short). FT /FTId=VSP_005722. SQ SEQUENCE 152 AA; 17611 MW; F52F9E8665B880EF CRC64; MSLVIPEKFQ HILRIMNTNI DGKRKVGIAM TAIKGVGRRY SNIVLKKADV DLTKRAGECT EEEVDKVVTI ISNPLQYKVP NWFLNRQKDI IDGKYWQLTS SNLDSKLRDD LERLKKIRSH RGLRHYWGLR VRGQHTKTTG RRGRTVGVSK KK // ID RS19_DROME STANDARD; PRT; 155 AA. AC P39018; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE 40S ribosomal protein S19. GN RPS19. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93376521; PubMed=8367309; RA Baumgartner S.W., Martin D., Chiquet-Ehrismann R.; RT "Drosophila ribosomal protein S19 cDNA sequence."; RL Nucleic Acids Res. 21:3897-3897(1993). CC -!- SIMILARITY: BELONGS TO THE S19E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73153; CAA51677.1; -. DR FlyBase; FBgn0010412; RpS19. DR InterPro; IPR001266; Ribosomal_S19E. DR Pfam; PF01090; Ribosomal_S19e; 1. DR ProDom; PD003854; Ribosomal_S19E; 1. DR PROSITE; PS00628; RIBOSOMAL_S19E; 1. KW Ribosomal protein. FT INIT_MET 0 0 BY SIMILARITY. SQ SEQUENCE 155 AA; 17174 MW; F77AB02833E7797F CRC64; PGVTVKDIDQ HAVTKAVAVF LKKTGKLKVP DQMDIIKTAK FKELAPYDPD WFYVRCASIL RHLYHRSPAG VGSITKIYGG RKRNGVHPSH FCRAADGAAR KALQALEHAR LVEKHPDGGR KLSSIGQRDL DRIANQIVFK QRDAAKQTGP IVISK // ID RS1A_DROME STANDARD; PRT; 129 AA. AC P48149; Q9VYE4; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S15A. GN RPS15A OR CG2033. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Lavoie C.L., Sonenberg N., Lasko P.F.; RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE S8P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z21673; CAA79771.1; -. DR EMBL; AE003492; AAF48256.1; -. DR PIR; S33498; S33498. DR FlyBase; FBgn0010198; RpS15A. DR InterPro; IPR000630; Ribosomal_S8. DR Pfam; PF00410; Ribosomal_S8; 1. DR ProDom; PD001098; Ribosomal_S8; 1. DR PROSITE; PS00053; RIBOSOMAL_S8; 1. KW Ribosomal protein. FT INIT_MET 0 0 BY SIMILARITY. SQ SEQUENCE 129 AA; 14640 MW; D800E6E9A05DED6F CRC64; VRMNVLADAL KCINNAEKRG KRQVLLRPCS KVIIKFLTVM MKHGYIGEFE IVDDHRSGKI VVNLTGRLNK CGVISPRFDV PINDIEKWTN NLLPSRQFGY VVLTTSGGIM DHEEARRKHL GGKILGFFF // ID RS20_DROME STANDARD; PRT; 120 AA. AC P55828; Q9VDI4; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S20. GN RPS20 OR CG15693. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RA Chan E.H.Y., Yong Z., Okane C.J.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE S10P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11119; CAA72004.1; -. DR EMBL; AE003732; AAF55809.1; -. DR FlyBase; FBgn0019936; RpS20. DR InterPro; IPR001848; Ribosomal_S10. DR InterPro; IPR005729; Ribosomal_S10e/a. DR Pfam; PF00338; Ribosomal_S10; 1. DR PRINTS; PR00971; RIBOSOMALS10. DR ProDom; PD001272; Ribosomal_S10; 1. DR TIGRFAMs; TIGR01046; S10_Arc_S20_Euk; 1. DR PROSITE; PS00361; RIBOSOMAL_S10; 1. KW Ribosomal protein. SQ SEQUENCE 120 AA; 13488 MW; 8810A345CA22CF04 CRC64; MAAAPKDIEK PHVGDSASVH RIRITLTSRN VRSLENVCRD LINGAKNQNL RVKGPVRMPT KTLRITTRKT PCGEGSKTWD RFQMRIHKRI IDLHSPSEIV KKITSINIEP GVEVEVTIAN // ID RS25_DROME STANDARD; PRT; 117 AA. AC P48588; Q8SZ71; Q9VGS0; DT 01-FEB-1996 (Rel. 33, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S25. GN RPS25 OR RPS31 OR CG6684. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 5-117 FROM N.A. RC STRAIN=Sevelin; TISSUE=Embryo; RA Edgar B.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE S25E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003690; AAF54605.2; -. DR EMBL; AY071076; AAL48698.1; -. DR EMBL; U03289; AAA03464.1; -. DR FlyBase; FBgn0010413; RpS25. DR InterPro; IPR004977; Ribosomal_S25. DR Pfam; PF03297; Ribosomal_S25; 1. DR ProDom; PD012268; Ribosomal_S25; 1. KW Ribosomal protein. FT CONFLICT 83 83 A -> D (IN REF. 4). SQ SEQUENCE 117 AA; 13201 MW; 1EBE36B8FD8896D6 CRC64; MPPKKDAKSS AKQPQKTQKK KEGSGGGKAK KKKWSKGKVR DKLNNQVLFD KATYEKLYKE VPAYKLITPS VVSERLKIRG SLAKRALIEL REKGLIKQVV QHHSQVIYTR ATKGDEA // ID RS26_DROME STANDARD; PRT; 114 AA. AC P13008; P10380; Q9VJ88; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S26 (DS31). GN RPS26 OR CG1030. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89098400; PubMed=2911474; RA Itoh N., Ohta K., Ohta M., Kawasaki T., Yamashina I.; RT "The nucleotide sequence of cDNA for a Drosophila ribosomal protein RT with homology to rat ribosomal protein S26."; RL Nucleic Acids Res. 17:441-441(1989). RN [2] RP SEQUENCE FROM N.A., AND REVISIONS. RC STRAIN=Canton-S; RX MEDLINE=89183616; PubMed=2928115; RA Itoh N., Ohta K., Ohta M., Kawasaki T., Yamashina I.; RT "The nucleotide sequence of a gene for a putative ribosomal protein RT S31 of Drosophila."; RL Nucleic Acids Res. 17:2121-2121(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE S26E FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13625; CAB38441.1; -. DR EMBL; X14247; CAA32463.1; -. DR EMBL; AE003659; AAF53666.1; -. DR PIR; S03724; R3FF26. DR FlyBase; FBgn0004413; RpS26. DR InterPro; IPR000892; Ribosomal_S26E. DR Pfam; PF01283; Ribosomal_S26e; 1. DR PROSITE; PS00733; RIBOSOMAL_S26E; 1. KW Ribosomal protein. SQ SEQUENCE 114 AA; 13266 MW; 0F0A6D8A8C6A8D7F CRC64; MTKKRRNGGR NKHNRGHVKP VRCTNCARCV PKDKAIKKFV IRNIVEAAAV RDITEASIWD SYVLPKLYAK LHYCVSCAIH SKVVRNRSRE ARRIRTPPLR SFPKDMARNN QNRK // ID RS2_DROME STANDARD; PRT; 267 AA. AC P31009; Q9VL74; DT 01-JUL-1993 (Rel. 26, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S2 (Strings of pearls protein). GN SOP OR RPS2 OR CG5920. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95073591; PubMed=7982558; RA Cramton S.E., Laski F.A.; RT "String of pearls encodes Drosophila ribosomal protein S2, has RT Minute-like characteristics, and is required during oogenesis."; RL Genetics 137:1039-1048(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-241 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93181212; PubMed=8441641; RA Barrio R., del Arco A., Cabrera H.L., Arribas C.; RT "Cloning and analysis of the S2 ribosomal protein cDNA from RT Drosophila."; RL Nucleic Acids Res. 21:351-351(1993). CC -!- SIMILARITY: BELONGS TO THE S5P FAMILY OF RIBOSOMAL PROTEINS. CC -!- SIMILARITY: CONTAINS 1 S5 DRBM DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69120; CAA48872.1; -. DR EMBL; AE003626; AAF52822.1; -. DR EMBL; U01334; AAC34198.1; -. DR EMBL; U01335; AAA87053.1; -. DR PIR; S30395; S30395. DR HSSP; P02357; 1PKP. DR FlyBase; FBgn0004867; sop. DR InterPro; IPR000851; Ribosomal_S5. DR InterPro; IPR005324; Ribosomal_S5_C. DR InterPro; IPR005711; Ribosomal_S5_e/a. DR Pfam; PF00333; Ribosomal_S5; 1. DR Pfam; PF03719; Ribosomal_S5_C; 1. DR TIGRFAMs; TIGR01020; rpsE_arch; 1. DR PROSITE; PS00585; RIBOSOMAL_S5; 1. DR PROSITE; PS50881; S5_DSRBD; 1. KW Ribosomal protein. FT DOMAIN 85 148 S5 DRBM. FT CONFLICT 19 20 GG -> PP (IN REF. 3). FT CONFLICT 194 194 K -> R (IN REF. 3). SQ SEQUENCE 267 AA; 28899 MW; ADA22CD28F100743 CRC64; MADEAPARSG FRGGFGSRGG RGGRGRGRGR WARGRGKEDS KEWVPVTKLG RLVREGKIKS LEEIYLYSLP IKEFEIIDFF LGSSLKDEVL KIMPVQKQTR AGQRTRFKAF VAIGDNNGHI GLGVKCSKEV ATAIRGAIIL AKLSVVPVRR GYWGNKIGKP HTVPCKVTGK CGSVSVRLIP APRGTGIVSA PVPKKLLTMA GIEDCYTSAR GSTGTLGNFA KATYAAIAKT YAYLTPDLWK EMPLGSTPYQ AYSDFLSKPT PRLHADA // ID RS3A_DROME STANDARD; PRT; 267 AA. AC P55830; O44389; Q9V4A9; DT 01-NOV-1997 (Rel. 35, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S3a (C3 protein). GN RPS3A OR C3 OR M(4)101 OR CG2168. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=98055162; PubMed=9393444; RA Reynaud E., Bolshakov V.N., Barajas V.N., Kafatos F.C., Zurita M.; RT "Antisense suppression of the putative ribosomal protein S3A gene RT disrupts ovarian development in Drosophila melanogaster."; RL Mol. Gen. Genet. 256:462-467(1997). RN [2] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=98416207; PubMed=9742251; RA van Beest M., Mortin M., Clevers H.; RT "Drosophila RpS3a, a novel minute gene situated between the segment RT polarity genes cubitus interruptus and dTCF."; RL Nucleic Acids Res. 26:4471-4475(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ESSENTIAL FOR OOGENESIS; REQUIRED FOR LATE FOLLICLE CELL CC DEVELOPMENT. MAY BIND TO THE 40S RIBOSOMAL SUBUNIT. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED IN STAGE 8 EMBRYOS. CC DURING OOGENESIS, EXPRESSION IS LOCATED BASALLY IN SOMATIC CC FOLLICULAR EPITHELIUM AND IN THE OOCYTE AT THE LATER STAGES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT ALL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE S3AE FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y10115; CAA71201.1; -. DR EMBL; AF034971; AAC62117.1; -. DR EMBL; AE003845; AAF59372.1; -. DR FlyBase; FBgn0017545; RpS3A. DR InterPro; IPR001593; Ribosomal_S3AE. DR Pfam; PF01015; Ribosomal_S3Ae; 1. DR ProDom; PD003035; Ribosomal_S3AE; 1. DR PROSITE; PS01191; RIBOSOMAL_S3AE; 1. KW Ribosomal protein. FT INIT_MET 0 0 BY SIMILARITY. FT CONFLICT 61 61 L -> F (IN REF. 1). FT CONFLICT 71 71 A -> VP (IN REF. 1). FT CONFLICT 81 81 R -> H (IN REF. 1). FT CONFLICT 159 160 QQ -> HE (IN REF. 1). FT CONFLICT 168 168 A -> SG (IN REF. 1). FT CONFLICT 252 260 VIDRPEGYE -> PKSTALKVK (IN REF. 1). FT CONFLICT 266 266 S -> A (IN REF. 3). SQ SEQUENCE 267 AA; 30225 MW; 3FF51141158455E7 CRC64; AVGKNKGLSK GGKKGGKKKV VDPFSRKDWY DVKAPNMFQT RQIGKTLVNR TQGQRIASDY LKGRVFEVSL ADLQKDIDPE RSFRKFRLIA EDVQDRNVLC NFHGMDLTTD KYRSMVKKWQ TLIEAIVEAK TVDGYLLRVF CIGFTAKDQQ SQRKTCYAQQ SQVRKIRARM TDIITNEVSG ADLKQLVNKL ALDSIAKDIE KSCQRIYPLH DVYIRKVKVL KKPRFDVSKL LELHGDGGGK SVEAVVSSEG AVIDRPEGYE PPVQESV // ID RS3_DROME STANDARD; PRT; 246 AA. AC Q06559; Q9VCM9; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S3. GN RPS3 OR M(3)95A OR CG6779. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93281407; PubMed=7685082; RA Wilson D.M. III, Deutsch W.A., Kelley M.R.; RT "Cloning of the Drosophila ribosomal protein S3: another RT multifunctional ribosomal protein with AP endonuclease DNA repair RT activity."; RL Nucleic Acids Res. 21:2516-2516(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Shahrinau / Wild type; RX MEDLINE=94350207; PubMed=8070662; RA Andersson S., Saeboe-Larssen S., Lambertsson A., Meriam J., RA Jacobs-Lorena M.; RT "A Drosophila third chromosome Minute locus encodes a ribosomal RT protein."; RL Genetics 137:513-520(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP DNA REPAIR ACTIVITY. RX MEDLINE=96208517; PubMed=8641296; RA Yacoub A., Augeri L., Kelley M.R., Doetsch P.W., Deutsch W.A.; RT "A Drosophila ribosomal protein contains 8-oxoguanine and abasic site RT DNA repair activities."; RL EMBO J. 15:2306-2312(1996). CC -!- FUNCTION: HAS DNA REPAIR ACTIVITY DIRECTED TOWARDS THE MUTAGENIC CC LESIONS 8-OXOGUANINE AND ABSIS SITES IN DNA. IT CAN CLEAVE DNA CC CONTAINING 8-OXOGUANINE RESIDUES EFFICIENTLY. ALSO ACTS AS AN CC AP LYASE, CLEAVING PHOSPHODIESTER BONDS VIA A BETA,DELTA CC ELIMINATION REACTION. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE S3P FAMILY OF RIBOSOMAL PROTEINS. CC -!- SIMILARITY: CONTAINS 1 KH TYPE-2 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13690; AAA28875.1; -. DR EMBL; X72921; CAA51425.1; -. DR EMBL; AE003743; AAF56129.1; -. DR PIR; S35620; S35620. DR FlyBase; FBgn0002622; RpS3. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR009019; KH_prok. DR InterPro; IPR004044; KH_TYPE_2. DR InterPro; IPR001351; Ribosomal_S3_C. DR InterPro; IPR005703; S3_euk_arch. DR Pfam; PF00013; KH; 1. DR Pfam; PF00189; Ribosomal_S3_C; 1. DR SMART; SM00322; KH; 1. DR TIGRFAMs; TIGR01008; rpsC_E_A; 1. DR PROSITE; PS50823; KH_TYPE_2; 1. DR PROSITE; PS00548; RIBOSOMAL_S3; 1. KW Ribosomal protein; Hydrolase; Nuclease; Endonuclease; DNA repair; KW Nuclear protein. FT DOMAIN 23 94 KH TYPE-2. FT CONFLICT 46 47 SR -> FG (IN REF. 2). FT CONFLICT 62 62 G -> A (IN REF. 2). FT CONFLICT 114 114 G -> E (IN REF. 2). SQ SEQUENCE 246 AA; 27471 MW; 122A6E775339E673 CRC64; MNANLPISKK RKFVSDGIFK AELNEFLTRE LAEDGYSGVE VRVTPSRTEI IIMATKTQQV LGEKGRRIRE LTAMVQKRFN FETGRIELYA EKVAARGLCA IAQAESLRYK LTGGLAVRRA CYGVLRYIME SGAKGCEVVV SGKLRGQRAK SMKFVDGLMI HSGDPCNDYV ETATRHVLLR QGVLGIKVKV MLPYDPKNKI GPKKPLPDNV SVVEPKEEKI YETPETEYKI PPPSKPLDDL SEAKVL // ID RS4_DROME STANDARD; PRT; 261 AA. AC P41042; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 40S ribosomal protein S4. GN RPS4 OR RP4. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94040769; PubMed=8224871; RA Yokokura T., Tei H., Yamamoto D.; RT "Sequence and expression of a gene encoding a ribosomal protein S4 RT homolog from Drosophila melanogaster."; RL Gene 132:251-254(1993). CC -!- SIMILARITY: BELONGS TO THE S4E FAMILY OF RIBOSOMAL PROTEINS. CC -!- SIMILARITY: CONTAINS 1 S4 RNA-BINDING DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D16257; BAA03786.1; -. DR PIR; JN0871; JN0871. DR FlyBase; FBgn0011284; RpS4. DR InterPro; IPR005824; KOW. DR InterPro; IPR006646; KOW_sub. DR InterPro; IPR000876; Ribosomal_S4E. DR InterPro; IPR002942; S4. DR Pfam; PF00467; KOW; 1. DR Pfam; PF00900; Ribosomal_S4e; 1. DR Pfam; PF01479; S4; 1. DR ProDom; PD002667; Ribosomal_S4E; 1. DR SMART; SM00739; KOW; 1. DR SMART; SM00363; S4; 1. DR PROSITE; PS00528; RIBOSOMAL_S4E; 1. DR PROSITE; PS50889; S4; 1. KW Ribosomal protein; RNA-binding. FT DOMAIN 42 104 S4 RNA-BINDING. SQ SEQUENCE 261 AA; 29170 MW; A218D676DF5167D0 CRC64; MARGPKKHLK RLAAPKAWML DKLGGVFAPR PSTGPHKLRE SLPLLTFLRN RLKYALNGAE VTKIVMQRLV KVYGKVRTDP TYPAGYMDVI TLEKTGEFFR LVYDVKGRFV IHRISAEEAK YKLCKVKKTQ LGAKGVPFLV THDGRTIRYP DPLIHANDSV QVDIASGKIT DYIKFDSGNL CMITGGRNLG RVGTVVNRER HPGSFDIVHI KDSQGHVFAT RLTNVFIIGK GNKPYISLPK GKGVKLSIAE ERDKRLAAKT H // ID RS5_DROME STANDARD; PRT; 228 AA. AC Q24186; Q9VX78; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S5. GN RPS5 OR M(1)15D OR CG8922. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97032939; PubMed=8878687; RA McKim K.S., Dahmus J., Hawley R.S.; RT "Cloning of the Drosophila melanogaster meiotic recombination gene RT mei-218: a genetic and molecular analysis of interval 15E."; RL Genetics 144:215-228(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE S7P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U48394; AAB61633.1; -. DR EMBL; AE003504; AAF48700.1; -. DR HSSP; P22744; 1HUS. DR FlyBase; FBgn0002590; RpS5. DR InterPro; IPR000235; Ribosomal_S7. DR InterPro; IPR005716; Ribosomal_S7e/a. DR Pfam; PF00177; Ribosomal_S7; 1. DR ProDom; PD000817; Ribosomal_S7; 1. DR TIGRFAMs; TIGR01028; S7_S5_E_A; 1. DR PROSITE; PS00052; RIBOSOMAL_S7; 1. KW Ribosomal protein. SQ SEQUENCE 228 AA; 25434 MW; 9206E1D8FE470C4C CRC64; MAEVAENVVE TFEEPAAPME AEVAETILET NVVSTTELPE IKLFGRWSCD DVTVNDISLQ DYISVKEKFA RYLPHSAGRY AAKRFRKAQC PIVERLTCSL MMKGRNNGKK LMACRIVKHS FEIIHLLTGE NPLQILVSAI INSGPREDST RIGRAGTVRR QAVDVSPLRR VNQAIWLLCT GAREAAFRNI KTIAECLADE LINAAKGSSN SYAIKKKDEL ERVAKSNR // ID RS6_DROME STANDARD; PRT; 248 AA. AC P29327; Q94993; Q9W3N4; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S6. GN RPS6 OR L(1)AIR8 OR HEN OR CG10944. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93087515; PubMed=1454811; RA Watson K.L., Konrad K.D., Woods D.F., Bryant P.J.; RT "Drosophila homolog of the human S6 ribosomal protein is required for RT tumor suppression in the hematopoietic system."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11302-11306(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93192329; PubMed=8448211; RA Spencer T.A., Mackie G.A.; RT "The nucleotide sequence of a cloned cDNA encoding ribosomal protein RT S6 from Drosophila melanogaster."; RL Biochim. Biophys. Acta 1172:332-334(1993). RN [3] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=94018587; PubMed=8412647; RA Stewart M.J., Denell R.; RT "The Drosophila ribosomal protein S6 gene includes a 3' triplication RT that arose by unequal crossing-over."; RL Mol. Biol. Evol. 10:1041-1047(1993). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY PLAY AN IMPORTANT ROLE IN CONTROLLING CELL GROWTH CC AND PROLIFERATION THROUGH THE SELECTIVE TRANSLATION OF PARTICULAR CC CLASSES OF MRNA. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=P29327-1; Sequence=Displayed; CC Name=B; Synonyms=C; CC IsoId=P29327-2; Sequence=VSP_005727, VSP_005728; CC -!- PTM: RIBOSOMAL PROTEIN S6 IS THE MAJOR SUBSTRATE OF PROTEIN CC KINASES IN EUKARYOTE RIBOSOMES. THE PHOSPHORYLATION IS STIMULATED CC BY GROWTH FACTORS, TUMOR PROMOTING AGENTS, AND MITOGENS. IT IS CC DEPHOSPHORYLATED AT GROWTH ARREST. CC -!- SIMILARITY: BELONGS TO THE S6E FAMILY OF RIBOSOMAL PROTEINS. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L01658; AAC34306.1; -. DR EMBL; L07881; AAA28871.1; -. DR EMBL; L02074; AAB05982.1; -. DR EMBL; L02074; AAB05983.1; -. DR EMBL; L02074; AAB05984.1; -. DR EMBL; L02075; AAB05985.1; -. DR EMBL; AE003442; AAF46288.1; ALT_SEQ. DR PIR; S30194; S30194. DR FlyBase; FBgn0004922; RpS6. DR InterPro; IPR001377; Ribosomal_S6E. DR Pfam; PF01092; Ribosomal_S6e; 1. DR ProDom; PD003460; Ribosomal_S6E; 1. DR PROSITE; PS00578; RIBOSOMAL_S6E; 1. KW Ribosomal protein; Phosphorylation; Alternative splicing. FT VARSPLIC 73 200 VRLLLKKGHSCYRPRRTGERKRKSVRGCIVDANMSVLALVV FT LKKGEKDIPGLTDTTIPRRLGPKRASKIRKLYNLSKEDDVR FT RFVVRRPLPAKDNKKATSKAPKIQRLITPVVLQRKHRRIAL FT KKKRQ -> LRLLKKIHSCFHPRCNKVRKCKTVRKYTVEAN FT VSALTLVVLKKNPSPCRLGPVRSSNISKIYYLCEEDDEVIP FT VKLQRRHQKKRQNATKEAIAEYVKLLVKRKKESKANRGRYV FT TIRKPKSSVFSGKK (in isoform B). FT /FTId=VSP_005727. FT VARSPLIC 201 248 Missing (in isoform B). FT /FTId=VSP_005728. SQ SEQUENCE 248 AA; 28407 MW; 4E781727C33B3B6D CRC64; MKLNVSYPAT GCQKLFEVVD EHKLRVFYEK RMGQVVEADI LGDEWKGYQL RIAGGNDKQG FPMKQGVLTH GRVRLLLKKG HSCYRPRRTG ERKRKSVRGC IVDANMSVLA LVVLKKGEKD IPGLTDTTIP RRLGPKRASK IRKLYNLSKE DDVRRFVVRR PLPAKDNKKA TSKAPKIQRL ITPVVLQRKH RRIALKKKRQ IASKEASADY AKLLVQRKKE SKAKREEAKR RRSASIRESK SSVSSDKK // ID RS9_DROME STANDARD; PRT; 196 AA. AC P55935; Q9XZU5; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 40S ribosomal protein S9. GN RPS9. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; TISSUE=Ovary; RX MEDLINE=94003404; PubMed=8400363; RA Zhang N., Bownes M.; RT "Sequence and expression of a Drosophila melanogaster cDNA encoding a RT putative ribosomal protein."; RL DNA Seq. 3:323-326(1993). RN [2] RP CONCEPTUAL TRANSLATION. RA Veuthey A.-L.; RL Unpublished observations (JUN-1997). CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE S4P FAMILY OF RIBOSOMAL PROTEINS. CC -!- SIMILARITY: CONTAINS 1 S4 RNA-BINDING DOMAIN. CC -!- CAUTION: THIS IS A CONCEPTUAL TRANSLATION, NUMEROUS FRAMESHIFTS CC WERE INTRODUCED SO AS TO MAXIMIZE THE SIMILARITY WITH OTHER CC MEMBERS OF THIS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69677; CAB41492.1; ALT_FRAME. DR FlyBase; FBgn0010408; RpS9. DR InterPro; IPR001912; Ribosomal_S4. DR InterPro; IPR005710; Ribosomal_S4/9. DR InterPro; IPR002942; S4. DR Pfam; PF00163; Ribosomal_S4; 1. DR Pfam; PF01479; S4; 1. DR TIGRFAMs; TIGR01018; rpsD_arch; 1. DR PROSITE; PS00632; RIBOSOMAL_S4; 1. DR PROSITE; PS50889; S4; FALSE_NEG. KW Ribosomal protein. SQ SEQUENCE 196 AA; 22714 MW; 4CEF2A2F9C003BE6 CRC64; MVNGRIPSVF SKTYVTPRRP YEKARLDQEL KIIGEYGLXN KREVWRVKYA LAKIRKVARE LLTLDEKDAK RLFQGKSLVR RLVRIGVLKX VRMKLDYVLG LKIQDFLERR LQTQVFKLGL AKSIHHARVL IRQRTFVLAS RWSTIPSFVV RLDSQKQHSN FSLRCPFGRG RPGRVKRKNL XKNQGGGGGA AEEEED // ID RSMB_DROME STANDARD; PRT; 199 AA. AC Q05856; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Small nuclear ribonucleoprotein associated protein B (snRNP-B) DE (Sm protein B) (Sm-B) (SmB). GN SMB OR CG5352. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Ovary; RX MEDLINE=93185934; PubMed=7680326; RA Brunet C., Quan T., Craft J.E.; RT "Comparison of the Drosophila melanogaster, human and murine Sm B RT cDNAs: evolutionary conservation."; RL Gene 124:269-273(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY HAVE A FUNCTIONAL ROLE IN PRE-MRNA SPLICING OR IN CC SNRNP STRUCTURE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L02919; AAA28858.1; -. DR EMBL; AE003628; AAF52947.1; -. DR EMBL; AY061171; AAL28719.1; -. DR PIR; JN0574; JN0574. DR HSSP; P14678; 1D3B. DR FlyBase; FBgn0010083; SmB. DR InterPro; IPR001163; snRNP_Sm. DR Pfam; PF01423; LSM; 1. DR SMART; SM00651; Sm; 1. KW Nuclear protein; Ribonucleoprotein; RNA-binding; Repeat. FT DOMAIN 111 197 4 X 3 AA REPEATS OF G-R-G. FT REPEAT 111 113 1. FT REPEAT 144 146 2. FT REPEAT 173 175 3. FT REPEAT 195 197 4. SQ SEQUENCE 199 AA; 21021 MW; EEEDBE1202E51848 CRC64; MTIGKNNKMI QHLNYRVRIV LQDSRTFIGT FKAFDKHMNL ILGDCEEFRK IRSKNSKVPE REEKRVLGFV LLRGENIVSL TVEGPPPPEE GLPRVPIPGA APGPGIGRVA GRGMPINLSA VPAGLQGPVR GVGGPAQQHM APMGRGVPRA PMMGAPPPGM IPGGMPSMPG NMGRGAPPPM RGPPPSMIRG APPPGRGGY // ID RSP4_DROME STANDARD; PRT; 270 AA. AC P38979; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 40S ribosomal protein SA (P40) (Stubarista protein) (Laminin receptor DE homolog) (K14). GN STA OR EG:80H7.6. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94063490; PubMed=7916731; RA Melnick M.B., Noll E., Perrimon N.; RT "The Drosophila stubarista phenotype is associated with a dosage RT effect of the putative ribosome-associated protein D-p40 on RT spineless."; RL Genetics 135:553-564(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE OF 18-270 FROM N.A. RC STRAIN=Canton-S; RA Kim Y.J., Baker B.S.; RL Submitted (XXX-1991) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE S2P FAMILY OF RIBOSOMAL PROTEINS. CC -!- CAUTION: WAS ORIGINALLY THOUGHT TO BE A LAMININ RECEPTOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M90422; AAA28741.1; -. DR EMBL; AL031027; CAA19839.1; -. DR EMBL; M77133; AAA28667.1; -. DR PIR; T13602; T13602. DR FlyBase; FBgn0003517; sta. DR InterPro; IPR001865; Ribosomal_S2. DR InterPro; IPR005707; Ribosomal_S2_e/a. DR Pfam; PF00318; Ribosomal_S2; 1. DR PRINTS; PR00395; RIBOSOMALS2. DR TIGRFAMs; TIGR01012; Sa_S2_E_A; 1. DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1. DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1. KW Ribosomal protein. SQ SEQUENCE 270 AA; 30228 MW; FEC452C3F1712C82 CRC64; MSGGLDILSL KEDDITKMLV ATTHLGSENV NFQMEQYVYK RRADGVNILN LGKTWEKLQL AARAIVAIDN PSDIFVISSR PIGQRAVLKF AKYTDTTPIA GRFTPGAFTN QIQPAFREPR LLVVTDPNTD HQPIMEASYV NIPVIAFTNT DSPLRYIDIA IPCNNKSAHS IGLMWWLLAR EVLRLRGTIS RSVEWPVVVD LFFYRDPEEA EKEEAAAKEL LPPPKIEEAV DHPVEETTNW ADEVAAETVG GVEDWNEDTV KTSWGSDGQF // ID RT06_DROME STANDARD; PRT; 147 AA. AC Q9VZD5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial 28S ribosomal protein S6 (MRP-S6). GN MRPS6 OR CG15016. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE S6P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003481; AAF47889.1; -. DR FlyBase; FBgn0035534; mRpS6. DR InterPro; IPR000529; Ribosomal_S6. DR PROSITE; PS01048; RIBOSOMAL_S6; FALSE_NEG. KW Ribosomal protein; Mitochondrion. SQ SEQUENCE 147 AA; 17015 MW; B2F0CF1FB6AA3F18 CRC64; MPSYELALVL RQLPRPELIS VIRRTAESIL DKGGIIRKLE NLGSRALPHK VSEHGVVHRE GTHFTIAFDT APTKIADLKE EFGRDIDIIR RYIFKVEEPE QKPCTLHEEM LPPAYRKDVQ EIIAAAQKKQ KKKFNYNSGL DYYPFQK // ID RT12_DROME STANDARD; PRT; 140 AA. AC P10735; Q9V3R2; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 40S ribosomal protein S12, mitochondrial precursor (MT-RPS12) DE (Technical knockout locus protein). GN TKO OR EG:BACH59J11.1 OR CG7925. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88027001; PubMed=3117373; RA Royden C.S., Pirrotta V., Jan L.Y.; RT "The tko locus, site of a behavioral mutation in D. melanogaster, RT codes for a protein homologous to prokaryotic ribosomal protein RT S12."; RL Cell 51:165-173(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- MISCELLANEOUS: MUTATION OF TKO CAUSES BEHAVIORAL MUTATION ("BANG CC SENSITIVITY" = TEMPORARILY PARALYSIS IN RESPONSE TO A PHYSICAL CC JOLT). CC -!- SIMILARITY: BELONGS TO THE S12P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19494; AAA28935.1; -. DR EMBL; AL133505; CAB65841.1; -. DR EMBL; AE003424; AAF45781.1; -. DR PIR; A29622; A29622. DR FlyBase; FBgn0003714; tko. DR GO; GO:0008049; P:male courtship behavior; IMP. DR GO; GO:0007638; P:mechanosensory behavior; IMP. DR GO; GO:0009592; P:perception of sound; IMP. DR GO; GO:0009612; P:response to mechanical stimulus; IMP. DR InterPro; IPR008994; Nucleic_acid_OB. DR InterPro; IPR006032; Ribosomal_S12_23. DR InterPro; IPR005679; Ribosomal_S12b/c. DR Pfam; PF00164; Ribosomal_S12; 1. DR PRINTS; PR01034; RIBOSOMALS12. DR ProDom; PD000576; Ribosomal_S12_23; 1. DR TIGRFAMs; TIGR00981; rpsL_bact; 1. DR PROSITE; PS00055; RIBOSOMAL_S12; 1. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 30 MITOCHONDRION (POTENTIAL). FT CHAIN 31 140 40S RIBOSOMAL PROTEIN S12. SQ SEQUENCE 140 AA; 15532 MW; 8187A7312C529F31 CRC64; MNFLRQSFGI TKQLASQAIQ CSYETAVRGM ASLQQMHRSG PHIKTRPPRQ PLDGKPFAKG VVLKTLIKKP KKPNSANRKC VLVRLSTGKE MVAYIPGIGH NLQEHNIVLC RVGRLQDVPG VKLKAVRGVY DLAHVVKKSQ // ID RT15_DROME STANDARD; PRT; 280 AA. AC Q8WTC1; Q9W231; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 28S ribosomal protein S15, mitochondrial precursor (MPR-S15) (Bonsai DE protein). GN MRPS15 OR BONSAI OR CG4207. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Galloni M.; RT "Bonsai, a mitochondrial ribosomal protein S15 homolog."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=99244690; PubMed=10225996; RA Galloni M., Edgar B.A.; RT "Cell-autonomous and non-autonomous growth-defective mutants of RT Drosophila melanogaster."; RL Development 126:2365-2375(1999). CC -!- FUNCTION: MIGHT BE INVOLVED IN TISSUE SPECIFIC GROWTH FACTOR CC PRODUCTION. CC -!- SUBUNIT: COMPONENT OF THE MITOCHONDRIAL RIBOSOME SMALL SUBUNIT CC (28S) WHICH COMPRISES A 12S RRNA AND ABOUT 30 DISTINCT PROTEINS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: LARVAL BRAIN AND IMAGINAL DISKS. CC -!- SIMILARITY: BELONGS TO THE S15P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF435962; AAL31972.1; -. DR EMBL; AE003458; AAF46869.1; -. DR EMBL; AY060712; AAL28260.1; -. DR HSSP; P05766; 1A32. DR FlyBase; FBgn0026261; bonsai. DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISS. DR GO; GO:0003735; F:structural constituent of ribosome; ISS. DR GO; GO:0006412; P:protein biosynthesis; ISS. DR GO; GO:0040008; P:regulation of growth; IMP. DR InterPro; IPR000589; Ribosomal_S15. DR Pfam; PF00312; Ribosomal_S15; 1. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 280 28S RIBOSOMAL PROTEIN S15. FT CONFLICT 30 30 M -> V (IN REF. 1). FT CONFLICT 47 47 A -> S (IN REF. 1). SQ SEQUENCE 280 AA; 33473 MW; 4CB921573734A08B CRC64; MNKLLNIAQA GHRQFVREYA FKSDLKIKWM RPEKIACYKP EKSGDLAKLP PLKADELLPE YRDCKELDKA DESVKSLFKL SNNASYLTTK FYRDEMVKEV QRHAQDFGSM EAKLAKMTAV IRRYQEHMDK HPRDKMIKVR LKELIDKRKK FLKYLRRWDY PRFEWILEKL DLVYKPPPTH FHWITRKESL QKLTDIYCEN LKEERLEAYH KQLQAQQIPF LEEAIKKMQF VRQEQISCDV PVTVTEEKIA DSKRQLEMLK ELQQAEAAAS SKKQNEDGFN // ID RT16_DROME STANDARD; PRT; 129 AA. AC Q9V6Y3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial 28S ribosomal protein S16 (MRP-S16). GN MRPS16 OR CG8338. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE S16P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003815; AAF58284.1; -. DR HSSP; P80379; 1EMW. DR FlyBase; FBgn0033907; mRpS16. DR InterPro; IPR000307; Ribosomal_S16. DR Pfam; PF00886; Ribosomal_S16; 1. DR ProDom; PD003791; Ribosomal_S16; 1. DR TIGRFAMs; TIGR00002; S16; 1. DR PROSITE; PS00732; RIBOSOMAL_S16; FALSE_NEG. KW Hypothetical protein; Ribosomal protein; Mitochondrion. SQ SEQUENCE 129 AA; 14519 MW; EAD759B96787935F CRC64; MSLSPASGIG RFYAKSAKII RFVRLGCTNR PFYHIVVMER RKNQHQPVIE QVGSFDPLPN DYNERLVALN TERIRYWLGK GAHLSTPAAE LLGIAGLLPI HPRTYMTAWR NRRTAAEAEA SPEKAESTA // ID RT25_DROME STANDARD; PRT; 167 AA. AC Q9VY28; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable mitochondrial 28S ribosomal protein S25 (S25mt) (MRP-S25). GN MRPS25 OR CG14413. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBUNIT: COMPONENT OF THE MITOCHONDRIAL RIBOSOME SMALL SUBUNIT CC (28S) WHICH COMPRISES A 12S RRNA AND ABOUT 30 DISTINCT PROTEINS CC (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003496; AAF48377.1; -. DR FlyBase; FBgn0030572; mRpS25. DR InterPro; IPR007741; L51_S25_CI-B8. DR Pfam; PF05047; L51_S25_CI-B8; 1. KW Hypothetical protein; Ribosomal protein; Mitochondrion. SQ SEQUENCE 167 AA; 19157 MW; D5D352DEF1B11E32 CRC64; MPFMKGREPI RRTLKYLNAG KLVLKDKVRI FSVNYNTYGA HHAGARDFVF WNIPQIQFKN PEVQVLTLKN MTPSPFVRCY FDDGRDMLID LDSRNRNDII DHLVKVVGKT REQLDAEERL KESKDNPANF GYGCGRHCIC EIPGQVPCPG TVPLPDHMRG KILFAPK // ID RT26_DROME STANDARD; PRT; 225 AA. AC Q9VVN2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable 28S ribosomal protein S26, mitochondrial precursor (MRP-S26). GN MRPS26 OR CG7354. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: COMPONENT OF THE MITOCHONDRIAL RIBOSOME SMALL SUBUNIT CC (28S) WHICH COMPRISES A 12S RRNA AND ABOUT 30 DISTINCT PROTEINS CC (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003521; AAF49279.1; -. DR EMBL; AY071284; AAL48906.1; -. DR FlyBase; FBgn0036774; mRpS26. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 225 PROBABLE 28S RIBOSOMAL PROTEIN S26. SQ SEQUENCE 225 AA; 26263 MW; 14B14FF222E597E4 CRC64; MLRAGCQLLT QSTLPTGKTV GNSFALEFVR WRRKPRWLPV AKSKMFRVPE RKKQSEEERT ELMRLHNQYK TQLRSVRQFL REEVVRHEET STADHIVLTP EQEEAEFQKC LDANAAWNAA IAKERDQRLA KKREEKVAYI QERLEAQQLR EEERKEQANQ RVLLEIERSK NYITRENLDA AIETALANPV DHNFAIDMAG NLYHGRSTSQ LPDATPEPNQ QVLSN // ID RTJK_DROME STANDARD; PRT; 916 AA. AC P21328; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE RNA-directed DNA polymerase from mobile element jockey (EC 2.7.7.49) DE (Reverse transcriptase). GN POL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89108009; PubMed=2463954; RA Priimaegi A.F., Mizrokhi L.J., Ilyin Y.V.; RT "The Drosophila mobile element jockey belongs to LINEs and contains RT coding sequences homologous to some retroviral proteins."; RL Gene 70:253-262(1988). RN [2] RP SEQUENCE OF 1-191 FROM N.A. RX MEDLINE=87303653; PubMed=3040362; RA Mizrokhi L.J., Priimaegi A.F., Ilyin Y.V.; RT "Drosophila mobile element jockey is a retroposon and encodes the GAG- RT specific protein sequence characteristic for retroviruses."; RL Dokl. Akad. Nauk SSSR 294:1235-1239(1987). RN [3] RP CHARACTERIZATION. RX MEDLINE=91330871; PubMed=1714378; RA Ivanov V.A., Melnikov A.A., Siunov A.V., Fodor I.I., Ilyin Y.V.; RT "Authentic reverse transcriptase is coded by jockey, a mobile RT Drosophila element related to mammalian LINEs."; RL EMBO J. 10:2489-2495(1991). CC -!- CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE = N DIPHOSPHATE CC + {DNA}(N). CC -!- COFACTOR: MAGNESIUM AND MANGANESE. CC -!- ENZYME REGULATION: INACTIVATED BY SULPHYDRYL REAGENT. CC -!- MISCELLANEOUS: PREFERS POLY(RC) AND POLY(RA) AS TEMPLATE AND CC ACTIVATED DNA IS NOT EFFECTIVE. HAS A TEMPERATURE OPTIMAL OF 26 CC DEGREES CELSIUS. CC -!- SIMILARITY: STRONG, TO THE PUTATIVE REVERSE TRANSCRIPTASE OF OTHER CC LONG INTERSPERSED ELEMENTS (LINES) IN EUKARYOTES. CC -!- SIMILARITY: STRONG TO THE EQUIVALENT PROTEIN OF DROSOPHILA CC FUNEBRIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22874; AAA28675.1; -. DR EMBL; M38643; AAA28940.1; -. DR PIR; JT0396; JT0396. DR FlyBase; FBgn0015952; jockey\pol. DR InterPro; IPR005135; Exo_endo_phos. DR InterPro; IPR000477; RVTse. DR Pfam; PF03372; Exo_endo_phos; 1. DR Pfam; PF00078; rvt; 1. KW Transferase; RNA-directed DNA polymerase; Transposable element. FT CONFLICT 185 191 TPSALDF -> LKFIRII (IN REF. 2). SQ SEQUENCE 916 AA; 103430 MW; 2105551F2E064CD1 CRC64; MTQPTLKIGL WNARGLTRGS EELRIFLSDH DIDVMLTTET HMRVGQRIYL PGYLMYHAHH PSGNSRGGSA VIIKSRLCHS PLTPISTNDR QIARVHLQTS VGTVTVAAVY LPPAERWIVD DFKSMFAALG NKFIAGGDYN AKHAWWGNPR SCPRGKMLQE VIAHGQYQVL ATGEPTFYSY NPLLTPSALD FFITCGYGMG RLDVQTLQEL SSDHLPILAV LHATPLKKPQ RVRLLAHNAD INIFKTHLEQ LSEVNMQILE AVDIDNATSL FMSKLSEAAQ LAAPRNRHEV EAFRPLQLPS SILALLRLKR RVRKEYARTG DPRMQQIHSR LANCLHKALA RRKQAQIDTF LDNLGADAST NYSLWRITKR FKAQPTPKSA IKNPSGGWCR TSLEKTEVFA NNLEQRFTPY NYAPESLCRQ VEEYLESPFQ MSLPLSAVTL EEVKNLIAKL PLKKAPGEDL LDNRTIRLLP DQALQFLALI FNSVLDVGYF PKAWKSASII MIHKTGKTPT DVDSYRPTSL LPSLGKIMER LILNRLLTCK DVTKAIPKFQ FGFRLQHGTP EQLHRVVNFA LEAMENKEYA VGAFLDIQQA FDRVWHPGLL YKAKRLFPPQ LYLVVKSFLE ERTFHVSVDG YKSSIKPIAA GVPQGSVLGP TLYSVFASDM PTHTPVTEVD EEDVLIATYA DDTAVLTKSK SILAATSGLQ EYLDAFQQWA ENWNVRINAE KCANVTFANR TGSCPGVSLN GRLIRHHQAY KYLGITLDRK LTFSRHITNI QQAFRTKVAR MSWLIAPRNK LSLGCKVNIY KSILAPCLFY GLQVYGIAAK SHLNKIRILQ AKTLRRISGA PWYMRTRDIE RDLKVPKLGD KLQNIAQKYM ERLNVHPNSL ARKLGTAAVV NADPRTRVKR RLKRHHPHDL PNLVLT // ID RU17_DROME STANDARD; PRT; 448 AA. AC P17133; Q9VM56; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE U1 small nuclear ribonucleoprotein 70 kDa (U1 snRNP 70 kDa) (snRNP70). GN SNRNP70K OR SNRNP27D OR CG8749. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90258833; PubMed=1692955; RA Mancebo R., Lo P.C.H., Mount S.M.; RT "Structure and expression of the Drosophila melanogaster gene for the RT U1 small nuclear ribonucleoprotein particle 70K protein."; RL Mol. Cell. Biol. 10:2492-2502(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MEDIATES THE SPLICING OF PRE-MRNA BY BINDING TO THE STEM CC LOOP I REGION OF U1-SNRNA. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M31162; AAA28859.1; -. DR EMBL; AE003615; AAF52471.1; -. DR EMBL; AY061501; AAL29049.1; -. DR PIR; A36311; A36311. DR HSSP; P09651; 1HA1. DR FlyBase; FBgn0016978; snRNP70K. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; 1. KW Nuclear protein; Ribonucleoprotein; RNA-binding; mRNA processing. FT DOMAIN 102 180 RNA-BINDING (RRM). FT DOMAIN 254 350 ARG/GLU-RICH (MIXED CHARGE). FT CONFLICT 278 278 N -> S (IN REF. 1). SQ SEQUENCE 448 AA; 52900 MW; 0DDFB5A39CA72AEB CRC64; MTQYLPPNLL ALFAAREPIP FMPPVDKLPH EKKSRGYLGV AKFMADFEDP KDTPLPKTVE TRQERLERRR REKAEQVAYK LEREIALWDP TEIKNATEDP FRTLFIARIN YDTSESKLRR EFEFYGPIKK IVLIHDQESG KPKGYAFIEY EHERDMHAAY KHADGKKIDS KRVLVDVERA RTVKGWLPRR LGGGLGGTRR GGNDVNIKHS GREDNERERE RYRLERERED REGPGRGGGS NGLDARPGRG FGAERRRSRS RERRDRERDR GRGAVASNGR SRSRSRERRK RRAGSRERYD EFDRRDRRDR ERERDRDRER EKKKKRSKSR ERESSRERRE RKRERRDRER GTGSGGDVKE RKPDFRDMDV IKIKEEPVDD GYPTFDYQNA TIKREIDDED EEKYRPPPAH HNMFSVPPPP ILGRGNASTN PNPDNGQQSS GDPSWWRQ // ID RU1A_DROME STANDARD; PRT; 216 AA. AC P43332; Q9W4D7; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE U1 small nuclear ribonucleoprotein A (U1 snRNP A protein) (Sex DE determination protein SNF). GN SNF OR D25 OR LIZ OR FS(1)1621 OR CG4528. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92350664; PubMed=1386424; RA Harper D.S., Fresco L.D., Keene J.D.; RT "RNA binding specificity of a Drosophila snRNP protein that shares RT sequence homology with mammalian U1-A and U2-B' proteins."; RL Nucleic Acids Res. 20:3645-3650(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95011590; PubMed=7926776; RA Flickinger T.W., Salz H.K.; RT "The Drosophila sex determination gene snf encodes a nuclear protein RT with sequence and functional similarity to the mammalian U1A snRNP RT protein."; RL Genes Dev. 8:914-925(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: BINDS STEM LOOP II OF U1 SNRNA. IT IS THE FIRST SN-RNP CC TO INTERACT WITH PRE-MRNA. THIS INTERACTION IS REQUIRED FOR THE CC SUBSEQUENT BINDING OF U2 SN-RNP AND THE U4/U6/U5 TRI-SN-RNP (BY CC SIMILARITY). PLAYS A ROLE IN REGULATING SEX-LETHAL SPLICING. CC -!- SUBUNIT: BELONGS TO THE SPLICEOSOME WHERE IT IS ASSOCIATED WITH CC SN-RNP U1. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE U1 A/B" FAMILY. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M89775; AAA28441.1; -. DR EMBL; L29521; AAA28903.1; -. DR EMBL; AE003433; AAF46017.1; -. DR EMBL; AY061491; AAL29039.1; -. DR PIR; A54279; A54279. DR HSSP; P09012; 3UTR. DR FlyBase; FBgn0003449; snf. DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IDA. DR GO; GO:0007539; P:primary sex determination, soma; NAS. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 1. KW Nuclear protein; RNA-binding; Ribonucleoprotein; Repeat; Spliceosome. FT DOMAIN 7 86 RNA-BINDING (RRM) 1. FT DOMAIN 142 216 RNA-BINDING (RRM) 2. FT VARIANT 49 49 R -> H (IN ALLELE SNF1621; STERILE). SQ SEQUENCE 216 AA; 24546 MW; 5B736FFE36523373 CRC64; MEMLPNQTIY INNLNEKIKK EELKKSLYAI FSQFGQILDI VALKTLKMRG QAFVIFKEIG SASNALRTMQ GFPFYDKPMQ IAYSKSDSDI VAKIKGTFKE RPKKVKPPKP APGTDEKKDK KKKPSSAENS NPNAQTEQPP NQILFLTNLP EETNEMMLSM LFNQFPGFKE VRLVPNRHDI AFVEFTTELQ SNAAKEALQG FKITPTHAMK ITFAKK // ID RU2A_DROME STANDARD; PRT; 265 AA. AC Q9V4Q8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable U2 small nuclear ribonucleoprotein A' (U2 snRNP-A'). GN U2A OR CG1406. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS PROTEIN IS ASSOCIATED WITH SN-RNP U2. IT HELPS THE CC A' PROTEIN TO BIND STEM LOOP IV OF U2 SNRNA (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 3 LEUCINE-RICH (LRR) REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003840; AAF59207.1; -. DR HSSP; P09661; 1A9N. DR FlyBase; FBgn0033210; U2A. DR InterPro; IPR001611; LRR. DR InterPro; IPR007092; LRR_SDS22. DR InterPro; IPR003603; LRRcap. DR Pfam; PF00560; LRR; 2. DR SMART; SM00446; LRRcap; 1. KW Nuclear protein; RNA-binding; Ribonucleoprotein; Leucine-rich repeat; KW Repeat. FT REPEAT 41 63 LRR 1. FT REPEAT 64 87 LRR 2. FT REPEAT 88 111 LRR 3. SQ SEQUENCE 265 AA; 29744 MW; FB09D8D1D96501A5 CRC64; MVKLTPELIN QSMQYINPCR ERELDLRGYK IPQIENLGAT LDQFDTIDLS DNDLRKLDNL PHLPRLKCLL LNNNRILRIS EGLEEAVPNL GSIILTGNNL QELSDLEPLV GFTKLETICL LINPVSTKPN YREYMAYKFP QLRLLDFRKI KQKDRQAAQE FFRTKQGKDV LKEISRKSKM SAAAAIAAEA GNGKGRGSEG GRLANPQDMQ RIREAIKRAS SLAEVERLSQ ILQSGQLPDK FQHEMEAVAQ NGAGHNGSGA VAMEY // ID RUNT_DROME STANDARD; PRT; 509 AA. AC P22814; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Segmentation protein Runt. GN RUN. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91065517; PubMed=2249771; RA Kania M.A., Bonner A.S., Duffy J.B., Gergen J.P.; RT "The Drosophila segmentation gene runt encodes a novel nuclear RT regulatory protein that is also expressed in the developing nervous RT system."; RL Genes Dev. 4:1701-1713(1990). RN [2] RP SIMILARITY TO AML1. RX MEDLINE=92220161; PubMed=1560822; RA Daga A., Tighe J.E., Calabi F.; RT "Leukaemia/Drosophila homology."; RL Nature 356:484-484(1992). CC -!- FUNCTION: PLAYS A PIVOTAL ROLE IN REGULATING THE EXPRESSION OF CC OTHER PAIR-RULE GENES SUCH AS EVE, FTZ, AND H. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: DEVELOPING CENTRAL AND PERIPHERAL NERVOUS CC SYSTEM. CC -!- DEVELOPMENTAL STAGE: MOST ABUNDANTLY EXPRESSED AT THE BLASTODERM CC STAGE OF EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 RUNT DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56432; CAA39817.1; -. DR PIR; A36392; A36392. DR HSSP; O60472; 1CMO. DR TRANSFAC; T01066; -. DR FlyBase; FBgn0003300; run. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; NAS. DR GO; GO:0007366; P:periodic partitioning by pair rule gene; NAS. DR GO; GO:0007540; P:sex determination, establishment of X:A ratio; NAS. DR GO; GO:0007530; P:sex determination; NAS. DR InterPro; IPR000040; AML1_Runt. DR InterPro; IPR008967; P53-like. DR Pfam; PF00853; Runt; 1. DR PRINTS; PR00967; ONCOGENEAML1. KW Developmental protein; Nuclear protein; Transcription regulation; KW ATP-binding; Segmentation polarity protein; Pair-rule protein. FT DOMAIN 18 29 POLY-ALA. FT DOMAIN 97 269 RUNT. FT NP_BIND 193 200 ATP (POTENTIAL). FT DOMAIN 354 359 POLY-ALA. FT VARIANT 31 31 A -> P. FT VARIANT 43 43 T -> A. SQ SEQUENCE 509 AA; 53257 MW; 49676C6B63237C9F CRC64; MHLPAGPTMV ANNTQVLAAA AAAAAAAAAV AQGPGPQQSS NATTASAIAI NPAQSLANTS THSASSTGSS TPDLSTNNTS SSSNATTSPQ NSAKMPSSMT DMFASLHEML QEYHGELAQT GSPSILCSAL PNHWRSNKSL PGAFKVIALD DWPDGTLVSI KCGNDENYCG ELRNCTTTMK NQVAKFNDLR FVGRSGRGKS FTLTITIATY PVQIASYSKA IKVTVDGPRE PRSKQSYGYP HPGAFNPFML NPAWLDAAYM TYGYADYFRH QAAAQAAQVH HPALAKSSAS SVSPNPNPSV ATSSSSAVQP SEYPHPAAAV AAAAGQPSAM MPSPPGAAPA TPYAIPQFPF NHVAAAAAAK AATPHAFHPY NFAAAAGLRA RNAALHHQSE PVHVSPASSR PSSSSPTQQH VLLKLNTSIE TSSIHEQSAS DGDSDDEQID VVKSEFDLDK SLDVAPLRMR CDLKAPSSMK PLYHESGPGA VANSRQPSPE TTTKIKSAAV QQKTVWRPY // ID RUXF_DROME STANDARD; PRT; 88 AA. AC Q24297; Q9V672; DT 15-JUL-1999 (Rel. 38, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Small nuclear ribonucleoprotein F (snRNP-F) (Sm protein F) (Sm-F) DE (SmF) (Membrane-associated protein Deb-B). GN DEBB OR CG16792. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90291029; PubMed=1694092; RA Vincent W.S. III, Goldstein E.S., Allen S.A.; RT "Sequence and expression of two regulated transcription units during RT Drosophila melanogaster development: Deb-A and Deb-B."; RL Biochim. Biophys. Acta 1049:59-68(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ASSOCIATED WITH SN-RNP U1, U2, U4/U6 AND U5 (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE SNRNP SM PROTEINS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L33341; AAA28445.1; -. DR EMBL; AE003823; AAF58559.2; -. DR EMBL; AY118862; AAM50722.1; -. DR FlyBase; FBgn0000426; DebB. DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; NAS. DR GO; GO:0008248; F:pre-mRNA splicing factor activity; NAS. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; NAS. DR InterPro; IPR006649; snRNP. DR InterPro; IPR001163; snRNP_Sm. DR Pfam; PF01423; LSM; 1. DR ProDom; PD020287; snRNP; 1. DR SMART; SM00651; Sm; 1. KW Nuclear protein; Ribonucleoprotein; mRNA splicing; mRNA processing; KW RNA-binding. FT CONFLICT 86 88 MRD -> CATSQWIHLHTPTPYF (IN REF. 1). SQ SEQUENCE 88 AA; 9739 MW; 198EF3AE27539880 CRC64; MSAGMPINPK PFLNGLTGKP VLVKLKWGQE YKGFLVSVDG YMNMQLANTE EVIEGSVTGN LGEVLIRCNN VLYIKGMEDD DEEGEMRD // ID RUX_DROME STANDARD; PRT; 335 AA. AC P50445; Q9W446; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cell cycle negative regulator roughex. GN RUX OR CG4336. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye imaginal disk; RX MEDLINE=94291191; PubMed=8020091; RA Thomas B.J., Gunning D.A., Cho J., Zipursky S.L.; RT "Cell cycle progression in the developing Drosophila eye: roughex RT encodes a novel protein required for the establishment of G1."; RL Cell 77:1003-1014(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NEGATIVE REGULATOR OF BOTH MITOSIS AND MEIOSIS. CC REQUIRED FOR THE ESTABLISHMENT OF THE G1 PHASE IN THE DEVELOPING CC EYE. CC -!- MISCELLANEOUS: THE RUX PHENOTYPE IS SUPPRESSED BY MUTATIONS OF CC GENES INVOLVED IN CELL CYCLE PROGRESSION SUCH AS CYC A AND STRING, CC AND ENHANCED BY MUTATIONS OF INTERCELLULAR SIGNALING GENES, RAS1 CC AND STAR. CC -!- MISCELLANEOUS: MUTATIONS OF RUX RESULT IN ROUGH EYE PHENOTYPE, CC AND/OR MALE STERILITY AND IN, SOME CASES, PUPAL DEATH. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U19583; AAA61580.1; -. DR EMBL; AE003436; AAF46113.1; -. DR PIR; A54458; A54458. DR FlyBase; FBgn0003302; rux. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0000278; P:mitotic cell cycle; IMP. DR GO; GO:0000074; P:regulation of cell cycle; IMP. FT CONFLICT 328 328 T -> M (IN REF. 1). SQ SEQUENCE 335 AA; 37898 MW; 0A48CECB08C8774F CRC64; MSAPEEHKET PLEVIHEFIN GVDDGTIRRD LGEDCILSFY SRNVRGAKAI TGFLRNQLTM RYKHEGFEEA AQIEWGDELL LKARFGRSFD SERRRIYEEK ERTGTTLHVR PESDDEEVNE KFSSTLITPP RPSSYNLNSL KYVEACGLLN KRNEHIYGGL DMGESCAVHL TLGYRSTFLP GGQVSGFEIC LAVYDRGLTS LKRSTLIPPL CSISFARRAS ARCNPTTDDE EDTEEDSTPP TARRCVRRTL FTEENTQKEE DADFIPVVEQ EQPAPQEQPA PQQAEETGEV VIPVDISTAL KTTNFSSCTP RKRQQATNGN EVVRKRATGP RRMRF // ID RX21_DROME STANDARD; PRT; 197 AA. AC Q24491; Q24424; Q9VL15; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE RNA binding protein Rsf1 (RNA binding protein Rox21). GN RSF1 OR ROX21 OR CG5655. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95197000; PubMed=7890163; RA Brand S.F., Pichoff S., Noselli S., Bourbon H.-M.; RT "Novel Drosophila melanogaster genes encoding RRM-type RNA-binding RT proteins identified by a degenerate PCR strategy."; RL Gene 154:187-192(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 8-50 FROM N.A. RA Brand S., Bourbon H.M.; RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY CONTROL IMPORTANT ASPECTS OF DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: EXTENSIVELY PHOSPHORYLATED ON SERINE RESIDUES IN THE RS CC DOMAIN (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SPLICING FACTOR SR FAMILY. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L34935; AAA73521.1; -. DR EMBL; AE003628; AAF52890.1; ALT_INIT. DR EMBL; L23835; AAA28729.1; -. DR FlyBase; FBgn0011305; Rsf1. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Nuclear protein; RNA-binding; Phosphorylation. FT DOMAIN 7 80 RNA-BINDING (RRM). FT DOMAIN 83 197 ARG/SER-RICH (RS DOMAIN). FT DOMAIN 88 193 GLY-RICH. SQ SEQUENCE 197 AA; 21133 MW; C93B72EA8225D463 CRC64; MGDQRGTRVY VGNLTDKVKK DDLEGEFTKY GKLNSVWIAF NPPGFAFVEF EHRDDAEKAC DILNGSELLG SQLRVEISKG RPRQGRRGGP MDRGGRRGDF GRHSITSGGS GGGGFRQRGS SGSSSRHTER GYSSGRSGAS SYNGREGGGS GFNRREVYGG GRDSSRYSSG SSASYGRTGG QSAGRFRSRS PVGNHRF // ID RX_DROME STANDARD; PRT; 873 AA. AC Q9W2Q1; O46035; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Retinal homeobox protein Rx (DRx1) (DRx). GN RX OR CG10052. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=98151514; PubMed=9482887; RA Eggert T., Hauck B., Hildebrandt N., Gehring W.J., Walldorf U.; RT "Isolation of a Drosophila homolog of the vertebrate homeobox gene Rx RT and its possible role in brain and eye development."; RL Proc. Natl. Acad. Sci. U.S.A. 95:2343-2348(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP PARTIAL SEQUENCE FROM N.A. RX MEDLINE=97320497; PubMed=9177348; RA Mathers P.H., Grinberg A., Mahon K.A., Jamrich M.; RT "The Rx homeobox gene is essential for vertebrate eye development."; RL Nature 387:603-607(1997). CC -!- FUNCTION: APPEARS TO FUNCTION IN BRAIN DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE PROCEPHALIC REGION AND IN CC THE CLYPEOLABRUM FROM STAGE 8 ON AND LATER IN THE BRAIN AND THE CC CENTRAL NERVOUS SYSTEM. CC -!- SIMILARITY: BELONGS TO THE PAIRED HOMEOBOX FAMILY. BICOID CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -!- SIMILARITY: CONTAINS 1 OAR DOMAIN. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ223300; CAA11241.1; ALT_INIT. DR EMBL; AE003452; AAF46639.2; ALT_SEQ. DR TRANSFAC; T03511; -. DR FlyBase; FBgn0020617; Rx. DR InterPro; IPR003654; Homeo_OAR. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR007104; Paired_homeo. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF03826; OAR; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS50803; OAR; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 116 123 OCTAPEPTIDE MOTIF. FT DNA_BIND 526 586 HOMEOBOX. FT DOMAIN 849 862 OAR. FT DOMAIN 855 859 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 329 333 POLY-PRO. FT DOMAIN 366 369 POLY-ASP. FT DOMAIN 437 453 POLY-GLN. FT DOMAIN 670 673 POLY-PRO. FT DOMAIN 683 691 POLY-PRO. FT DOMAIN 753 763 POLY-SER. FT DOMAIN 828 834 POLY-PRO. FT CONFLICT 4 4 S -> P (IN REF. 1). FT CONFLICT 136 136 R -> W (IN REF. 1). FT CONFLICT 384 384 S -> T (IN REF. 1). FT CONFLICT 645 672 PLSLAPGNLTMSSLAAMGHHHAHNGPPP -> QPGARKSDH FT EQSGGHGPPPCPQWAAA (IN REF. 1). FT CONFLICT 768 768 G -> L (IN REF. 1). SQ SEQUENCE 873 AA; 92897 MW; 87B56AD4693F6710 CRC64; MSGSGGVANS SSTAAANNTA ATFQHIFEQL VQQGGGNHKL PPKQLEQLRH LLGNVRDAKN LQMIVEKFKN LEQFHEHYAA HLANNNTVIS TEDSNDLVKD NARKYGSGGQ TLTPRHTIDA ILGLKNRNGA ANGSGRNPET VSDGSVDPSL GDDDATDLRC GMTLTQLRSM DNHMASMLQQ HAKNGGALPY GPPTPPGGQQ PQVPNATPLH HGQQMGGQAG HATHAGHGHP THHGHAPFGY HNAFGFGQGG HGYGHPEEAA GNYLNSMHQM VEANQLQTGA NGANPPPAPL PPSSFGSHQQ HLAALAAQAQ EQQNQHSKYA KSSPTGAGPP PPPGAYFMES QTAPVAPSQI NYDERSMSSA SDLEEDDDDA AKLQLDVTSP PTPSPRGQLA AKRKSAGVFC DDNEPKLANG QLPGGNYGIR PRSMEEVHHQ QQSHHHQQQQ QQQQQQQQLQ QQQGFQHDFR NSGNGNPNGN SNSGDHGERL NADSDSLVNG SCASSEDLNQ TNSSEQGEKI TSGSDDEGQD DNCAKKKHRR NRTTFTTYQL HELERAFEKS HYPDVYSREE LAMKVNLPEV RVQVWFQNRR AKWRRQEKSE SLRLGLTHFT QLPHRLGCGA SGLPVDPWLS PPLLSALPGF LSHPQTVYPS YLTPPLSLAP GNLTMSSLAA MGHHHAHNGP PPPHVGHGGH GQPQPPPPPP PHGVPHPHGS HHVVPLSHLS PHLSRMSPHA TSLGSPHHGV TPLGTPLHSS LPPSSTATTV AVSSSQSSSS SASLECSGPD VCMSPQNLSI GNADSNGDGR DLSSDLDAGS TSSNPGSSLD KCAASANIEL LDVGRDSPPP PPTPTGKGSS TPPTDMRSNS IATLRIKAKE HLDNLNKGMV SIV // ID RY44_DROME STANDARD; PRT; 5127 AA. AC Q24498; Q24321; Q24499; Q24500; Q24501; Q8MKS3; Q8MKS4; Q8MKS5; AC Q9V4Y7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ryanodine receptor 44F. GN RYA-R44F OR DRY OR RYR OR CG10844. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS A; B; C AND D), FUNCTION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=94102409; PubMed=8276118; RA Takeshima H., Nishi M., Iwabe N., Miyata T., Hosoya T., Masai I., RA Hotta Y.; RT "Isolation and characterization of a gene for a ryanodine RT receptor/calcium release channel in Drosophila melanogaster."; RL FEBS Lett. 337:81-87(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 4619-5127 FROM N.A., DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX MEDLINE=93202018; PubMed=1338312; RA Hasan G., Rosbash M.; RT "Drosophila homologs of two mammalian intracellular Ca(2+)-release RT channels: identification and expression patterns of the inositol RT 1,4,5-triphosphate and the ryanodine receptor genes."; RL Development 116:967-975(1992). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=20283930; PubMed=10811919; RA Sullivan K.M.C., Scott K., Zuker C.S., Rubin G.M.; RT "The ryanodine receptor is essential for larval development in RT Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 97:5942-5947(2000). CC -!- FUNCTION: COMMUNICATION BETWEEN TRANSVERSE-TUBULES AND CC SARCOPLASMIC RETICULUM. CONTRACTION OF MUSCLE IS TRIGGERED BY CC RELEASE OF CALCIUM IONS FROM SR FOLLOWING DEPOLARIZATION OF T- CC TUBULES (BY SIMILARITY). CC -!- FUNCTION: INTRACELLULAR CALCIUM CHANNEL THAT IS REQUIRED FOR CC PROPER MUSCLE FUNCTION DURING EMBRYONIC DEVELOPMENT AND MAY BE CC ESSENTIAL FOR EXCITATION-CONTRACTION COUPLING IN LARVAL BODY WALL CC MUSCLES. CC -!- SUBUNIT: HOMOTETRAMER (POTENTIAL). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=A; CC IsoId=Q24498-2; Sequence=Displayed; CC Name=B; CC IsoId=Q24498-3; Sequence=VSP_050196; CC Name=C; CC IsoId=Q24498-4; Sequence=VSP_050195; CC Name=D; CC IsoId=Q24498-5; Sequence=VSP_050195, VSP_050196; CC -!- TISSUE SPECIFICITY: DURING EMBRYONIC STAGES 9-10, EXPRESSION IS CC SEEN IN MESODERM OF ALL SEGMENTS IN PROGENITORS OF THE CEPHALIC CC AND SOMATIC MUSCLES. ADULTS EXHIBIT HIGH EXPRESSION IN TUBULAR CC 'JUMP' MUSCLES OF THORAX AND LEG, AND LOWER EXPRESSION IN THE CC BRAIN, VENTRAL GANGLION, HEAD MUSCLES AND PROBOSCIS MUSCLES. CC -!- DEVELOPMENTAL STAGE: ABUNDANT IN 6-12 HOUR EMBRYOS, REDUCED CC EXPRESSION IN SECOND AND THIRD INSTAR LARVAL STAGES AND ADULTS. CC -!- MISCELLANEOUS: THE CALCIUM RELEASE CHANNEL IS MODULATED BY CALCIUM CC IONS, MAGNESIUM IONS, ATP AND CALMODULIN (BY SIMILARITY). CC -!- MISCELLANEOUS: THE CALCIUM RELEASE CHANNEL ACTIVITY RESIDES IN THE CC C-TERMINAL REGION WHILE THE REMAINING PART OF THE PROTEIN CC CONSTITUTES THE 'FOOT' STRUCTURE SPANNING THE JUNCTIONAL GAP CC BETWEEN THE SR AND THE T-TUBULE. IT IS POSSIBLE THAT THE FOOT CC STRUCTURE INTERACTS WITH THE CYTOPLASMIC REGION OF THE CC DIHYDROPYRIDINE RECEPTOR (BY SIMILARITY). CC -!- MISCELLANEOUS: RYANODINE IS AN ALKALOID THAT BINDS TO THE CA- CC RELEASE CHANNEL IN JUNCTIONAL SR AND MODULATES ITS ACTIVITY (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE RYANODINE RECEPTOR FAMILY. CC -!- SIMILARITY: CONTAINS 5 MIR DOMAINS. CC -!- SIMILARITY: CONTAINS 3 SPRY DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D17389; BAA04212.1; -. DR EMBL; D17389; BAA41469.1; -. DR EMBL; D17389; BAA41470.1; -. DR EMBL; D17389; BAA41471.1; -. DR EMBL; AE003835; AAF59036.2; -. DR EMBL; AE003835; AAM71082.1; -. DR EMBL; AE003835; AAM71083.1; -. DR EMBL; AE003835; AAM71084.1; -. DR EMBL; Z18536; CAA79221.1; -. DR FlyBase; FBgn0011286; Rya-r44F. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0005219; F:ryanodine-sensitive calcium-release channel...; TAS. DR GO; GO:0006816; P:calcium ion transport; TAS. DR GO; GO:0006936; P:muscle contraction; IMP. DR InterPro; IPR000699; Ca-rel_channel. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR003608; MIR. DR InterPro; IPR001215; Ryanodn_receptor. DR InterPro; IPR003032; RyR. DR InterPro; IPR003877; SPRY_receptor. DR Pfam; PF00520; ion_trans; 1. DR Pfam; PF02815; MIR; 4. DR Pfam; PF01365; RYDR_ITPR; 2. DR Pfam; PF02026; RyR; 4. DR Pfam; PF00622; SPRY; 3. DR PRINTS; PR00795; RYANODINER. DR SMART; SM00472; MIR; 4. DR SMART; SM00449; SPRY; 3. DR PROSITE; PS50919; MIR; 5. KW Developmental protein; Receptor; Ionic channel; Calcium channel; KW Repeat; Transmembrane; Glycoprotein; Phosphorylation; KW Alternative splicing. FT DOMAIN 1 3232 CYTOPLASMIC. FT TRANSMEM 3233 3253 M' (POTENTIAL). FT TRANSMEM 3301 3321 M'' (POTENTIAL). FT TRANSMEM 3376 3396 M1 (POTENTIAL). FT TRANSMEM 3963 3983 M2 (POTENTIAL). FT TRANSMEM 4452 4472 M3 (POTENTIAL). FT TRANSMEM 4651 4671 M4 (POTENTIAL). FT TRANSMEM 4683 4703 M5 (POTENTIAL). FT TRANSMEM 4742 4762 M5 (POTENTIAL). FT TRANSMEM 4885 4905 M5 (POTENTIAL). FT TRANSMEM 4924 4944 M8 (POTENTIAL). FT TRANSMEM 4963 4983 M9 (POTENTIAL). FT TRANSMEM 5004 5024 M10 (POTENTIAL). FT DOMAIN 94 148 MIR 1. FT DOMAIN 155 200 MIR 2. FT DOMAIN 210 264 MIR 3. FT DOMAIN 270 328 MIR 4. FT DOMAIN 336 394 MIR 5. FT DOMAIN 663 802 SPRY 1. FT DOMAIN 1091 1216 SPRY 2. FT DOMAIN 1529 1672 SPRY 3. FT DOMAIN 4686 4711 GLY-RICH (ACIDIC). FT DOMAIN 845 3063 4 X APPROXIMATE REPEATS. FT REPEAT 845 956 1. FT REPEAT 957 1075 2. FT REPEAT 2822 2945 3. FT REPEAT 2946 3063 4. FT CARBOHYD 3454 3454 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4039 4039 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4167 4167 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4279 4279 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 4545 4545 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1135 1165 VTKMHAGSIEHFGVRYEAGDVIGCFIDVKEQ -> EEKVYG FT GVSESFGKQCGPGDIVGVFLDLADH (in isoform C FT and isoform D). FT /FTId=VSP_050195. FT VARSPLIC 1876 1889 Missing (in isoform B and isoform D). FT /FTId=VSP_050196. FT CONFLICT 314 316 CLR -> SW (IN REF. 1). FT CONFLICT 1045 1079 VRTLLVYGYVLDPPTGEGTEALLAEAQRLKFAGFR -> SA FT NAPGLRICLGSSDGRRNGGTSGRGTTPQVRRIP (IN FT REF. 1). FT CONFLICT 2282 2282 L -> I (IN REF. 1). FT CONFLICT 2550 2550 I -> S (IN REF. 1). FT CONFLICT 2927 2927 A -> P (IN REF. 1). FT CONFLICT 3214 3214 L -> Q (IN REF. 1). FT CONFLICT 3361 3361 A -> G (IN REF. 1). FT CONFLICT 4096 4096 T -> I (IN REF. 1). FT CONFLICT 4633 4633 Y -> D (IN REF. 4). FT CONFLICT 4695 4695 I -> T (IN REF. 4). FT CONFLICT 5022 5024 DAF -> AL (IN REF. 4). FT CONFLICT 5073 5073 M -> I (IN REF. 4). FT CONFLICT 5077 5077 M -> L (IN REF. 4). FT CONFLICT 5103 5127 WDFFPVGDCFRKQYEDELSGGGGGG -> GTSSQWETASAS FT NTRMSFPAEAAAA (IN REF. 4). SQ SEQUENCE 5127 AA; 581007 MW; 01B637D778DECE6A CRC64; MAEAEGGSEQ DDVSFLRTED MVTLSCTATG ERVCLAAEGF GNRHCFLENI ADKNVPPDLS QCVFVIEQAL SVRALQELVT AAGSETGKGT GSGHRTLLYG NAILLRHHNS DMYLACLSTS SSNDKLSFDV GLQEHSQGEA CWWTVHPASK QRSEGEKVRV GDDLILVSVA TERYLHTTKE NEQSIVNASF HVTHWSVQPY GTGISRMKYV GYVFGGDVLR FFHGGDECLT IPSTWGREAG QNIVIYEGGV VMAQARSLWR LELARTKWTG GFINWYHPMR IRHITTGRYL GVNDSNELIL VKKEEASIAT TTFCLRQEKD DEKKVLEDKD LEVIGSPIIK YGDTTVIVQH CETSLWLSYK SYETKKKGVG KVEEKQAILH EEGKMDDCLD FSRSQEEESK TARVIRKCSS LFTQFITALE TLQSNRRHSI FFQKVNLNEM VMCLEDLINY FSQPEDDMEH EEKQNRFRAL RNRQDLFQEE GVLNLILEAI DKINIITSQG FLASFLAGDE TGQSWDLIST YLYQLLAAII KGNHTNCAQF ANSNRLNWLF SRLGSQASSE GSGMLDVLHC VLIDSPEALN MMRDEHIKVI ISLLEKHGRD PKVLDVLCSL CVGNGVAVRS SQNNICDFLL PGKNLLLQTL LVDHVASIRP NIFVGRVDGS SMYQKWYFEV TMDHIEQTTH MMPHLRIGWA NTSGYVPYPG GGKKWGGNGV GDDLYSFGFD GAFLWTGGRK TLVVDALPEE PFIRKGDVIG VAIDLSVPII TFTFNGVKVR GSFRDFNLDG MFFPVMSCSS KLSCRFLFGG DHGRLKFAPP MGFSALVQCL MPQQILSLDP CFYFGNLAKN VLAGPWLIED DTAFVPKPVD TTGVTLPSSV DQIKEKLAEN IHEMWALNKI EAGWSWGEHR DDYHRIHPCL THFEKLPAAE KRYDNQLAVQ TLKTIISLGY YITMDKPPAR IRPVRLPNEI FMQGNGYKPA PLDLSAVTLT PKLEELVDQL AENTHNLWAR ERIQQGWTYG LNEDSENHRS PHLVPYAKVD EAIKKANRDT ASETVRTLLV YGYVLDPPTG EGTEALLAEA QRLKFAGFRT YRVERNYAVT SGKWYFEFEV LTSGPMRVGW ARADCYPGAM LGSEDTSWAF DGHNVTKMHA GSIEHFGVRY EAGDVIGCFI DVKEQTISFS LNGELLMDAL GGETTFADVT AEGVGFVPAC TLGVGQKARL IYGQDVDSLK FFTTCGLQEG YEPFCVNMRR PVTHWYTKDQ PIFENTEEMP DCRIDVTRIP GGADTPPHLK ISHNTFETME KANWEFLRLS LPVTCMGEFI SEQEKARRWD EIKNRQYRLM REAEIAAQMQ VQTQAAHMDH MLKGGFNMND IKGLTRNFDE HADAEADHMM RGPNRPPRKG SLTRNITFET DMSAALDEMQ RSTSVLDMNG LGEEMDDKKK RGRSPFKFFS KKSRDQSREK MGARTLDTSL ERRNTVAHGR NVVNQQMTTR APTLRLNNAE IPPSPVPQGP KQLSGSNLGQ QPVETSGDEM FDAECLKLIN EYFYGVRIFP GQDPTHVYVG WVTTQYHLHS REFNKNKVRR GSVYIEDDYE MAIERIDRQS CYVVRADELF NEVTQDASGK GASQGMFVGC FVDTATGIIR FTCEGKDTSH RWMMEPDTKL FPAIFVEATS KEILQIELGR TPTTLPLSAA VLPTSDKHIN PQSPPRLKVQ CLRPHQWARV PNTALQVHAL KLSDVRGWSM LCEDPVSMLA LHIPEEDRCI DILELIEMDK LLSFHAHSLT LYAALCYQSN YRAAHALCQH VDQKQLLYAI RSEYMSGPLR QGFYDLLIAL HLESHATTME VCKNEYITPL GAELKELYSD EEMQHSLRSL VTESVRPQLR MTEITPPVIA TSSMPSVSSE PIPDIDQLYS PKFPLEVVRQ FVMEALKDAV EINQVHNRDP IGWTNENLFL PLIKLTDRLL LVGVLTDEDV QRLLVMIDPE TWDQAFEREG KDEHRKGLLT MKMAEGAKLQ MCYLLHHLYD TQLRHRVESI IAFSHDFVGD LQTDQLRRYI EIKQSDLPSA VAAKKTKEFR CPPREQMNQI LCFKNLEPDD QDNCTCGLEL RGRLGDFHDS LMQKVSLNAL QEPDGVEGTA IEEVKTGPIT KIYNFINTVK ELEEGPKEVE EPEKKTPEEV FRKVLIKTIV SWAEESQIEN PKLVREMFSL LLRQYDTVGE LVRALEKTYV INTRARDDVA EMWVGLSQIR ALLPVQMSQE EEELMRKRLW KLVNNATFFQ HPDLIRILRV HENVMAVMMN TLGRRAQAQS DAPTQSEVAE GAPSKEKDTS HEMVVACCRF LCYFCRTGRQ NQKAMFDHFD FLLDNANILL ARPSLRGSTP LDVAYSSLME NTELALALRE HYLEKIAVYL SRCGLQSNSE LVEKGYPDLG WDPVEGERYL DFLRYCVWVN GESVEENANL VIRLLIRRPE CLGPALRGEG EGLFRAIVEA NRMSERISDR CKMQDEAEGT IAGLNFTHPL PEGEEDEDYI DTGAAILNFY CTLVDLLGRC APDASVIEQG KNESLRARAI LRSLVPLEDL QGVLSLKFTL SQTAPGEEKP KSDMPSGLLP NNKQSIVLFL ERVYGIEAQD LFYRLLEDAF LPDLRTATIL DKSDGSESDM ALAMNRYIGN SILPLLIKHS KFYNEAENYA SLLDATLHTV YRLSKNRMLT KGQREAVSDF LVALTSQMQP AMLLKLLRKL TVDVSKLSEY TTVALRLLTL HFDRCAKYYG STQGQGSYGA SSDEEKRLTM LLFSNIFDSL SNMDYDPELF GKALPCLIAI GCALPPDYSL SKNTDEDYYG RQMGAPDQPQ YMPNPIDTNN VHLDNDLNSL VQKFSEHYHD AWASRRLEGG WTYGDIRSDN DRKHPRLKPY NMLSEYERER YRDPVRECLK GLLAIGWTVE HSEVEVALNH RGSTRRQSKP QINEFQNEGS PFNYNPHPVD MSNLTLSREM QNMAERLAEN SHDIWAKKKN EELNGCGGVI HPQLVPYDLL TDKEKKKDRE RSQEFLKYMQ YQGYKLHKPS KGGAVEEGGA TQAAVELRFS YSLLEKLIQY LDRATINMKL LKPSTTFSRR SSFKTATRDI KFFSKVVLPL MEKYFSTHRN YFIAIATATN NIGAASLKEK EMVASIFCKL AALLRNRLSA FGPDVRITVR CLQVLVKGID ARTLTKNCPE FIRTSMLTFF NQTSDDLGNT ILNLQDGKYS HLRGTHLKTS TSLGYVNQVV LPVLTAMFDH LAACDYGSDL LLDEIQVASY KILAALYHLG TDGTLTHDRK YLKTEIERHR PALGSCLGAY SSCFPVAFLE PHLNKHNQYS LLNRIADHSL EAQDIMVKME SCMPNLETIL AEVDQFVESD KTYNDAPHII DVILPLLCAY LPFWWSQGPD NVSPTSGNHV TMVTADHMNP LLRNVLKMIK KNIGNDNAPW MTRIAAYTQQ IIINTSEELL KDPFLPLAER VKKRTENMLH KEDSMRGFIK SATDDTSQVE TQLQEDWNLL VRDIYSFYPL LIKYVDLQRN HWLKDNIPEA EELYNHVAEI FNIWSKSQYF LKEEQNFISA NEIDNMALIM PTATRRSAIS EGAPAVGGKV KKKKKNRDKK RDKDKEVQAS LMVACLKRLL PVGLNLFAGR EQELVQHCKD RYLKKMPEYD VIEFARNQLT LPDKLDPSDE MSWQHYLYSK LGKTEEPVDE QALEKANVNS NEKGKDKTQE TVDRIVAMAK VLFGLHMIDH PQQQSKNVYR SVVSIQRKRA VIACFRQTSL HSLPRHRACN IFARSYYEQW LQEENVGQEV MVEDLTQTFE DSEKSKKEGE ETDSKPDPLT QLVTTFCRGA MTERSGALQE DLLYMSYAQI AAKSTGKEEE EGGDEEGGEG GEEGEGTSIH EQEMEKQKLL FHQARLSNRG VAEMVLLHIS ASKGIPSEMV MTTLNLGIAI LRGGNIDIQM GMLNHLKEKK DVGFFTSIAG LMNSCSVLDL DAFERNTKAE GLGVGSEGAA GEKNMHDAEF TCALFRFIQL TCEGHNLEWQ NYLRTQAGNT TTVNVVICTV DYLLRLQESI MDFYWHYSSK EIIDPAGKAN FFKAIEVASQ VFNTLTEVIQ GPCTLNQQAL AHSRLWDAVG GFLFLFSHMQ DKLSKHSSQV DLLKELLNLQ KDMITMMLSM LEGNVVNGTI GKQMVDTLVE SASNVELILK YFDMFLKLAD LIESPSFHEV DMKNEGWVTP KDFREKMEQS KNYTPEEMDF LLACCERNHE GKIDYRAFVE HFHEPSKEIG FNLAVLLTNL SEHMPNEPRL ARFLETAGSV LNYFEPFLGR IEILGSSKRI ERVYFEIKDS NIEQWEKPQI RESKRAFFYS IVTEGGDKEK LEAFVNFCED AIFEMTHASG LMATDDGGGN VKRDTAYSSY MSEEEEERAA RDPIRRTITA VKEGLKFGVH MLSPANIKHQ IGVMQTKSIP ELIVGFFKII FYIFYYTGYA HFCVVRYIFG ILLNLMRGPA PEQEEEPVVE EETFGRALPP LPLEEPPGTV QAFGLDINKE ENGMYKVVVH ESPANSSMEE GGESSPEDGA AASGELVEGE PHQEPISIVD LLGGEAAKKA AQERQEAQKA QEAAMASIEA EAKKSSSAPQ ETPAVHQIDF SQYTHRAVSF LARNFYNLKY VALVLAFSIN FMLLFYKVTS FTEEADSSAE EELILGSGSG GGADITGSGF GGSGDGGSGD GEMEDEIPEL VHVDEDFFYM EHVLRIAACL HSLVSLAMLI AYYHLKVPLA IFKREKEIAR RLEFEGLFIA EQPEDDDFKS HWDKLVISAK SFPVNYWDKF VKKKVRQKYS ETYDFDSISN LLGMEKSTFA AQESEETGIF KYIMNIDWRY QVWKAGVTFT DNAFLYSLWY FSFSVMGNFN NFFFAAHLLD VAVGFKTLRT ILQSVTHNGK QLVLTVMLLT IIVYIYTVIA FNFFRKFYIQ EEDEEVDKKC HDMLTCFVFH LYKGVRAGGG IGDEIGDPDG DDYEVYRIIF DITFFFFVII ILLAIIQGLI IDAFGELRDQ LESVKDNMES NCFICGMGKD FFDIVPHGFD THVQKEHNLA NYMFFLMHLI NKPDTEYTGQ ETYVWNMYQQ RSWDFFPVGD CFRKQYEDEL SGGGGGG // ID RYK1_DROME STANDARD; PRT; 610 AA. AC Q27324; Q9U9Y3; Q9VIY6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase Drl precursor (EC 2.7.1.112) (Derailed DE protein). GN DRL OR LIO OR CG17348/CG10758. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RC TISSUE=Head; RX MEDLINE=95385805; PubMed=7656987; RA Dura J.-M., Taillebourg E., Preat T.; RT "The Drosophila learning and memory gene linotte encodes a putative RT receptor tyrosine kinase homologous to the human RYK gene product."; RL FEBS Lett. 370:250-254(1995). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=95327190; PubMed=7603568; RA Callahan C.A., Muralidhar M.G., Lundgren S.E., Scully A.L., RA Thomas J.B.; RT "Control of neuronal pathway selection by a Drosophila receptor RT protein-tyrosine kinase family member."; RL Nature 376:171-174(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 1-36 FROM N.A. RX MEDLINE=99289562; PubMed=10359803; RA Taillebourg E., Dura J.-M.; RT "A novel mechanism for P element homing in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 96:6856-6861(1999). RN [6] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=96379737; PubMed=8787750; RA Callahan C.A., Bonkovsky J.L., Scully A.L., Thomas J.B.; RT "derailed is required for muscle attachment site selection in RT Drosophila."; RL Development 122:2761-2767(1996). CC -!- FUNCTION: PLAYS AN ESSENTIAL ROLE IN NEURONAL PATHWAY RECOGNITION CC AND VENTRAL MUSCLE ATTACHMENT SITE SELECTION. NON-VITAL FOR CC DEVELOPMENT. MAY BE PART OF A SIGNAL TRANSDUCTION CASCADE INVOLVED CC IN LEARNING AND POSSIBLY MEMORY. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- TISSUE SPECIFICITY: IN THE EMBRYONIC ABDOMINAL HEMISEGMENT, CC EXPRESSION IS RESTRICTED TO CELL BODY, AXON AND GROWTH CONE OF A CC CLUSTER OF 20 VENTRAL NERVE CORD INTERNEURONS. DURING MUSCLE CC GROWTH AND ATTACHMENT EVENTS IN THE EMBRYONIC ABDOMINAL CC HEMISEGMENT, EXPRESSION IS IN SOMATIC MUSCLE FIBERS 21-23 AT 10-13 CC HOURS AND 2 PATCHES OF APPROXIMATELY 15 NEIGHBORING EPIDERMAL CC CELLS (DORSAL AND VENTRAL ATTACHMENT SITES) AT 6-13 CC HOURS. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. CC -!- SIMILARITY: CONTAINS 1 WIF DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36584; AAA79949.1; -. DR EMBL; L47260; AAA75347.1; -. DR EMBL; AE003662; AAF53776.1; -. DR EMBL; AY051852; AAK93276.1; -. DR EMBL; AF147883; AAD41343.1; -. DR PIR; S58885; S58885. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0015380; drl. DR GO; GO:0016021; C:integral to membrane; ISS. DR GO; GO:0004713; F:protein-tyrosine kinase activity; ISS. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0007611; P:learning and/or memory; IMP. DR GO; GO:0016203; P:muscle attachment; IMP. DR GO; GO:0006468; P:protein amino acid phosphorylation; ISS. DR GO; GO:0007165; P:signal transduction; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR InterPro; IPR003306; WIF. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF02019; WIF; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00219; TyrKc; 1. DR SMART; SM00469; WIF; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50814; WIF; 1. KW Transferase; Kinase; Tyrosine-protein kinase; ATP-binding; Receptor; KW Signal; Transmembrane; Glycoprotein; Phosphorylation; KW Developmental protein. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 610 TYROSINE-PROTEIN KINASE DRL. FT DOMAIN 21 242 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 243 263 POTENTIAL. FT DOMAIN 264 610 CYTOPLASMIC (POTENTIAL). FT DOMAIN 24 155 WIF. FT DOMAIN 343 606 PROTEIN KINASE. FT NP_BIND 349 357 ATP (BY SIMILARITY). FT BINDING 371 371 ATP (BY SIMILARITY). FT ACT_SITE 468 468 BY SIMILARITY. FT MOD_RES 498 498 PHOSPHORYLATION (AUTO-) (BY FT SIMILARITY). FT CARBOHYD 63 63 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 99 99 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 143 143 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 610 AA; 68311 MW; 728A3F272DAED4BE CRC64; MAPNLLTIGL LLTLIASGQA HLNIFLNLHE VLRLIGVSAE LYYVREGAIN DYALNFAVPV PANISDVTFT WQSLVDHPLP YSINIATSDT EVLPRPILNI SRIGDVPVEP QTWGIALKCS GTRNAEVTVT INVEVILDRA TNNNTNLIFK RKKICLREEQ DSAHEEYDDD DLDLLQTARK GHGGDIHYVD RNDEHVVANG HQAPEKQRPV VTESPVGRGN SGGSKRDFDP MLRENLVPPA SGLVTLIVGG ILALVLVSTL ILIAYCAKGP SKRHPSNGVH LIKTSSFQRL PTISSTAHNS IYVCPSTITP TYATLTRPFR EYEHEPEEFN RRLQELTVQK CRVRLSCLVQ EGNFGRIYRG TYNDCQEVLV KTVAQHASQL QVNLLLQESM MLYEASHPNV LSVLGISIED YATPFVLYAA TGSVRNLKSF LQDPSYARSV TTIQTVLMGS QLAMAMEHLH NHGVIHKDIA ARNCVIDDQL RVKLTDSALS RDLFPGDYNS LGDGEYRPIK WLSLEALQKS HYNEGSDVWS FGVLMWEMCT LGKLPYAEID PYEMEHYLKD GYRLAQPFNC PDELFTIMAY CWASMPAERP SFSQLQICLS EFHTQITRYV // ID RYK2_DROME STANDARD; PRT; 584 AA. AC Q9V422; O62533; Q95TI0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase Dnt precursor (EC 2.7.1.112) (Doughnut DE protein). GN DNT OR CG17559. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Embryo; RX MEDLINE=99077698; PubMed=9858720; RA Oates A.C., Bonkovsky J.L., Irvine D.V., Kelly L.E., Thomas J.B., RA Wilks A.F.; RT "Embryonic expression and activity of doughnut, a second RYK homolog RT in Drosophila."; RL Mech. Dev. 78:165-169(1998). RN [2] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=99250261; PubMed=10231580; RA Savant-Bhonsale S., Friese M., McCoon P., Montell D.J.; RT "A Drosophila derailed homolog, doughnut, expressed in invaginating RT cells during embryogenesis."; RL Gene 231:155-161(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 244-584 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY PLAY AN ESSENTIAL ROLE IN NEURONAL PATHWAY CC RECOGNITION AND VENTRAL MUSCLE ATTACHMENT SITE SELECTION. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN DYNAMIC DOMAINS IN THE EMBRYONIC CC EPIDERMIS, MANY OF WHICH BORDER ON SITES OF EPITHELIAL CC INVAGINATION INTO THE EMBRYO INTERIOR, INCLUDING VENTRAL FURROW, CC CEPHALIC FURROW, FORE- AND HINDGUT, OPTIC LOBE AND TRACHEAL PITS. CC LATER IN EMBRYOGENESIS, EXPRESSION IS SEEN IN IMAGINAL TISSUES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC FROM EMBRYOS TO ADULTS. HIGH EXPRESSION IS SEEN IN EMBRYOS, PUPAE CC AND ADULTS (HIGHEST IN EARLY PUPAE) AND LOW EXPRESSION IN CC LARVAE. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. CC -!- SIMILARITY: CONTAINS 1 WIF DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ224361; CAA11918.1; ALT_INIT. DR EMBL; AF123572; AAD31179.1; ALT_INIT. DR EMBL; AE003662; AAF53783.2; -. DR EMBL; AY058760; AAL13989.1; -. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0024245; dnt. DR GO; GO:0016021; C:integral to membrane; ISS. DR GO; GO:0004713; F:protein-tyrosine kinase activity; ISS. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0016203; P:muscle attachment; IMP. DR GO; GO:0006468; P:protein amino acid phosphorylation; ISS. DR GO; GO:0007165; P:signal transduction; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR InterPro; IPR003306; WIF. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF02019; WIF; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR SMART; SM00469; WIF; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50814; WIF; 1. KW Transferase; Kinase; Tyrosine-protein kinase; ATP-binding; Receptor; KW Signal; Transmembrane; Glycoprotein; Phosphorylation; KW Developmental protein. FT SIGNAL 1 40 POTENTIAL. FT CHAIN 41 584 TYROSINE-PROTEIN KINASE DNT. FT DOMAIN 41 208 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 209 229 POTENTIAL. FT DOMAIN 230 584 CYTOPLASMIC (POTENTIAL). FT DOMAIN 49 180 WIF. FT DOMAIN 317 577 PROTEIN KINASE. FT NP_BIND 323 331 ATP (BY SIMILARITY). FT BINDING 345 345 ATP (BY SIMILARITY). FT ACT_SITE 442 442 BY SIMILARITY. FT MOD_RES 472 472 PHOSPHORYLATION (AUTO-) (BY FT SIMILARITY). FT CARBOHYD 124 124 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 163 163 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 168 168 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 584 AA; 64937 MW; F46FCD024BD8447E CRC64; MESVNKCGKS ASTRNCTVKM SRKMWVLSLL ALAALQLHSG SEVAAHLNVF LNPVEVMRLL GVSAEVYYVR EGHINNYALN FIVPVPANVK DISFTWQSLA GRGLPYSINV VSSDQEVLPR PAINVSHSGE IPTTIQTWSI ALKCSGLKAA EVDVTVSLEV VLNRSLNNVT HLVFRRKKIC LMNDSAEDLS EDVDDPQLLE TVMLPPTGLI TLVVGVSVAM GSVCLLLMIA YCVKGAANKR QHHQHGGQPM RTSSFQRLNT HPPCQSSMGS AAYMTPSIIA PIHGSSLPRK VPVSVEQQHP EELHRRISEL TVERCRVRLS SLLQEGTFGR VYRGTYNDTQ DVLVKTVAQH ASQMQVLLLL QEGMLLYGAS HPGILSVLGV SIEDHTTPFV LYPALNNTRN LKQFLLDPAC ARTVTTIQIV MMASQLSMAL DHLHSHGVVH KDIATRNCVI DDQLRVKLSD SSLSRDLFPS DYNCLGDSEN RPVKWMSLEA LQHKQFSEAS DSWAFGVLMW ELCTSAKQPY AEVDPFEMEH YLKDGYRLAQ PFNCPDELFT IMAYCWALLP AERPTFAQLQ SCLSEFYSQI TRYV // ID S6A4_DROME STANDARD; PRT; 622 AA. AC P51905; Q9W177; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sodium-dependent serotonin transporter (5HT transporter) (5HTT) DE (Cocaine-sensitive serotonin transporter). GN SERT OR CG4545. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=94255490; PubMed=8197200; RA Demchyshyn L.L., Pristupa Z.B., Sugamori K.S., Barker E.L., RA Blakely R.D., Wolfgang W.J., Forte M.A., Niznik H.B.; RT "Cloning, expression, and localization of a chloride-facilitated, RT cocaine-sensitive serotonin transporter from Drosophila RT melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5158-5162(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TERMINATES THE ACTION OF SEROTONINE BY ITS HIGH AFFINITY CC SODIUM-DEPENDENT REUPTAKE INTO PRESYNAPTIC TERMINALS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: NERVOUS SYSTEM. CC -!- MISCELLANEOUS: THIS PROTEIN IS THE TARGET OF PSYCHOMOTOR CC STIMULANTS SUCH AS AMPHETAMINES OR COCAINE. CC -!- SIMILARITY: BELONGS TO THE SODIUM:NEUROTRANSMITTER SYMPORTER (SNF) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04809; AAA19430.1; -. DR EMBL; AE003464; AAF47200.1; -. DR FlyBase; FBgn0010414; SerT. DR InterPro; IPR000175; Na/ntran_symport. DR Pfam; PF00209; SNF; 1. DR PRINTS; PR00176; NANEUSMPORT. DR ProDom; PD000448; Na/ntran_symport; 1. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. KW Neurotransmitter transport; Transport; Transmembrane; Glycoprotein; KW Symport. FT DOMAIN 1 82 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 83 103 1 (POTENTIAL). FT TRANSMEM 111 130 2 (POTENTIAL). FT TRANSMEM 155 175 3 (POTENTIAL). FT DOMAIN 176 244 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 245 263 4 (POTENTIAL). FT TRANSMEM 272 289 5 (POTENTIAL). FT TRANSMEM 325 342 6 (POTENTIAL). FT TRANSMEM 354 375 7 (POTENTIAL). FT TRANSMEM 408 427 8 (POTENTIAL). FT TRANSMEM 455 473 9 (POTENTIAL). FT TRANSMEM 489 509 10 (POTENTIAL). FT TRANSMEM 530 549 11 (POTENTIAL). FT TRANSMEM 568 586 12 (POTENTIAL). FT DOMAIN 587 622 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 622 AA; 69325 MW; 8E100BA90905A98D CRC64; MDRSGSSDFA GAAATTGRSN PAPWSDDKES PNNEDDSNED DGDHTTPAKV TDPLAPKLAN NERILVVSVT ERTRETWGQK AEFLLAVIGF AVDLGNVWRF PYICYQNGGG AFLVPYCLFL IFGGLPLFYM ELALGQFHRC GCLSIWKRIC PALKGVGYAI CLIDIYMGMY YNTIIGWAVY YLFASFTSKL PWTSCDNPWN TENCMQVTSE NFTELATSPA KEFFERKVLE SYKGNGLDFM GPVKPTLALC VFGVFVLVYF SLWKGVRSAG KVVWVTALAP YVVLIILLVR GVSLPGADEG IKYYLTPEWH KLKNSKVWID AASQIFFSLG PGFGTLLALS SYNKFNNNCY RDALITSSIN CLTSFLAGFV IFSVLGYMAY VQKTSIDKVG LEGPGLVFIV YPEAIATMSG SVFWSIIFFL MLITLGLDST FGGLEAMITA LCDEYPRVIG RRRELFVLLL LAFIFLCALP TMTYGGVVLV NFLNVYGPGL AILFVVFVEA AGVFWFYGVD RFSSDVEQML GSKPGLFWRI CWTYISPVFL LTIFIFSIMG YKEMLGEEYY YPDWSYQVGW AVTCSSVLCI PMYIIYKFFF ASKGGCRQRL QESFQPEDNC GSVVPGQQGT SV // ID SA47_DROME STANDARD; PRT; 551 AA. AC Q960T2; Q24502; Q24503; Q8INC9; Q9VF07; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Synapse-associated protein of 47 kDa. GN SAP47 OR CG8884. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS C AND F). RC STRAIN=Berlin; TISSUE=Head; RX MEDLINE=96115108; PubMed=7494462; RA Reichmuth C., Becker S., Benz M., Debel K., Reisch D., Heimbeck G., RA Hofbauer A., Klagges B., Pflugfelder G.O., Buchner E.; RT "The sap47 gene of Drosophila melanogaster codes for a novel conserved RT neuronal protein associated with synaptic terminals."; RL Brain Res. Mol. Brain Res. 32:45-54(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=A; CC IsoId=Q960T2-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=B; CC IsoId=Q960T2-2; Sequence=VSP_007393, VSP_007394; CC Note=No experimental confirmation available; CC Name=C; Synonyms=2; CC IsoId=Q960T2-3; Sequence=VSP_007389, VSP_007390, VSP_007391, CC VSP_007392; CC Name=F; Synonyms=1; CC IsoId=Q960T2-4; Sequence=VSP_007389, VSP_007390, VSP_007393, CC VSP_007394; CC Name=G; CC IsoId=Q960T2-5; Sequence=VSP_007389; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: EXPRESSED SPECIFICALLY IN NEURONS AND CC TRANSPORTED TO SYNAPTIC TERMINALS. CC -!- SIMILARITY: CONTAINS 1 BSD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X80110; CAA56415.1; -. DR EMBL; X80111; CAA56416.1; -. DR EMBL; AE003711; AAN13682.1; -. DR EMBL; AE003711; AAN13687.1; -. DR EMBL; AE003711; AAN13688.1; -. DR EMBL; AE003711; AAF55255.2; -. DR EMBL; AY051871; AAK93295.1; -. DR FlyBase; FBgn0013334; Sap47. DR InterPro; IPR005607; BSD. DR Pfam; PF03909; BSD; 1. DR PROSITE; PS50858; BSD; 1. KW Alternative splicing. FT DOMAIN 295 347 BSD. FT VARSPLIC 72 88 RLPKSASLVDSLVSEAT -> S (in isoform C, FT isoform F and isoform G). FT /FTId=VSP_007389. FT VARSPLIC 197 204 GKGDEVKI -> V (in isoform C and isoform FT F). FT /FTId=VSP_007390. FT VARSPLIC 369 370 AN -> ED (in isoform C). FT /FTId=VSP_007391. FT VARSPLIC 371 551 Missing (in isoform C). FT /FTId=VSP_007392. FT VARSPLIC 370 374 NEVAT -> LAFNY (in isoform B and isoform FT F). FT /FTId=VSP_007393. FT VARSPLIC 375 551 Missing (in isoform B and isoform F). FT /FTId=VSP_007394. SQ SEQUENCE 551 AA; 56980 MW; 430392D0EAD5916E CRC64; MFSGLTNQFT SLVGAVKGGA GDEDVPAPTG DAPAAAPAAS TSVEATASSA VDPEAAAAAG GEGLEGEEAG KRLPKSASLV DSLVSEATGW LGSAKGWLGN ASIPSMPAMP SMPSMPAMPA MPSIPSIPGL RKGAGADGAE GAEGAVAGEG GAAASGAVSG GEDDDKSRYI SATEGADSHP ASGGGTPTGD EGQIGQGKGD EVKITTKVTQ QAKHFGSFLS SAISKAGSKI KETVKDNTIL DSFNKEQEAF IKGQGGVGNG AAPWIGHANE AKIKEEILGL SQDRRNFVRA PPAGVDFEFS YDTAYPTAIA IMAEDKALET MRFELVPKII TEENFWRNYF YRVSLIIQAA ELGTLGADGV GQASSGEDAN EVATKEKKSK TAEPAKGDSS VKAIAEQPKA VIEPEAQECD VQAAKSKAKA KAQAGKELGQ KISESEFVSD DFQASSESDL AEIQDGMRKL GIDSMTQQAL AATDEEQWEK DLEAELKDYE VVDEGGTGGD GGGGRRKGRK AGEDDTEADE DEPTISNLRT RSTNNDWEEY ADLIEDTDDL K // ID SAH2_DROME STANDARD; PRT; 492 AA. AC P50245; Q27587; Q8MYX7; Q9VEQ4; DT 01-OCT-1996 (Rel. 34, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative adenosylhomocysteinase (EC 3.3.1.1) (S-adenosyl-L- DE homocysteine hydrolase) (AdoHcyase). GN AHCY89E OR PH200 OR CG8956. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=89030618; PubMed=2903049; RA Delorenzi M., Ali N., Saari G., Henry C., Wilcox M., Bienz M.; RT "Evidence that the Abdominal-B r element function is conferred by a RT trans-regulatory homeoprotein."; RL EMBO J. 7:3223-3231(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95396803; PubMed=7667301; RA Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D., RA Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.; RT "Complete sequence of the bithorax complex of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-HOMOCYSTEINE + H(2)O = ADENOSINE CC + L-HOMOCYSTEINE. CC -!- COFACTOR: BINDS 1 NAD PER SUBUNIT (BY SIMILARITY). CC -!- PATHWAY: ACTIVATED METHYL CYCLE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN EXTENDED GERM BAND EMBRYOS AND IN CC SOMATIC MESODERM, YOLK CELLS AND MIDGUT DURING LATER EMBRYONIC CC STAGES. CC -!- SIMILARITY: BELONGS TO THE ADENOSYLHOMOCYSTEINASE FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13168; CAA31566.1; -. DR EMBL; U31961; AAA84400.1; ALT_SEQ. DR EMBL; AE003715; AAF55367.2; -. DR EMBL; AY113501; AAM29506.1; -. DR PIR; S01302; S01302. DR HSSP; P10760; 1D4G. DR FlyBase; FBgn0015011; Ahcy89E. DR InterPro; IPR000043; Ado_hcyase. DR Pfam; PF05221; AdoHcyase; 1. DR Pfam; PF00670; AdoHcyase_NAD; 1. DR TIGRFAMs; TIGR00936; ahcY; 1. DR PROSITE; PS00738; ADOHCYASE_1; 1. DR PROSITE; PS00739; ADOHCYASE_2; 1. KW Hydrolase; NAD; One-carbon metabolism. FT DOMAIN 244 411 NAD BINDING (BY SIMILARITY). FT CONFLICT 127 127 T -> A (IN REF. 1). FT CONFLICT 484 492 PFKANYYRY -> LLKPITTGWLPFFPFQFCTLVNNILISF FT ADINQYLMLYPVILVL (IN REF. 1). SQ SEQUENCE 492 AA; 54240 MW; F4916A43A2A3B288 CRC64; MAKMPETTFA DLSLADKTAV KKSSIEARRF SDVSTCSFSS TCFTGSSDEE DVSPKDNHQR NSAGGTDFCV KSISKSAFGR REIEIAESEM PGIMTLRKRA KDEKPLKGAN IVGCTHVNAQ SAVLIETLVQ LGATVRWAAC NIYSTQNAVA AALAEAGIPI FAWRGETEEE FWWCLDRAIY SDGWQPNLIL DDGGDATHLM LKKYPDYFKA IRGIVEESVT GVHRLYMLSK GGKLTVPAIN VNDSVTKNKF DTFYTCRDSI LDSLKRTTDI MFGGKQVVIC GYGDVGKGCA QSLKGQGCIV YVTEVDPICA LQAAMDGFRV VRLNEVIRTV DVVVTATGNK NVITRDHMNR MKNGCILCNM GHSCSEIDVN GLHTPELTWE RVRSQVDHIR WPDGRMIILL AEGRLVNLSC STISSFVVSV ASSTQALALI ELFSAPGRYK SDVYLLPKKM DEYVASLHLA TFDAHLTELT DEQSKFMGLN KAGPFKANYY RY // ID SAHH_DROME STANDARD; PRT; 431 AA. AC Q27580; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Adenosylhomocysteinase (EC 3.3.1.1) (S-adenosyl-L-homocysteine DE hydrolase) (AdoHcyase). GN AHCY13 OR AHCY. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97188525; PubMed=9037110; RA Caggese C., Ragone G., Barsanti P., Moschetti R., Messina A., RA Massari S., Caizzi R.; RT "The S-adenosyl-L-homocysteine hydrolase of Drosophila melanogaster: RT identification, deduced amino acid sequence and cytological RT localization of the structural gene."; RL Mol. Gen. Genet. 253:492-498(1997). CC -!- FUNCTION: ADENOSYLHOMOCYSTEINE IS A COMPETITIVE INHIBITOR OF CC S-ADENOSYL-L-METHININE-DEPENDENT METHYL TRANSFERASE REACTIONS; CC THEREFORE ADENOSYLHOMOCYSTEINASE MAY PLAY A KEY ROLE IN THE CC CONTROL OF METHYLATIONS VIA REGULATION OF THE INTRACELLULAR CC CONCENTRATION OF ADENOSYLHOMOCYSTEINE. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-HOMOCYSTEINE + H(2)O = ADENOSINE CC + L-HOMOCYSTEINE. CC -!- COFACTOR: BINDS 1 NAD PER SUBUNIT (BY SIMILARITY). CC -!- PATHWAY: ACTIVATED METHYL CYCLE. CC -!- SIMILARITY: BELONGS TO THE ADENOSYLHOMOCYSTEINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95636; CAA64892.1; -. DR HSSP; P10760; 1B3R. DR FlyBase; FBgn0014455; Ahcy13. DR InterPro; IPR000043; Ado_hcyase. DR Pfam; PF05221; AdoHcyase; 1. DR Pfam; PF00670; AdoHcyase_NAD; 1. DR TIGRFAMs; TIGR00936; ahcY; 1. DR PROSITE; PS00738; ADOHCYASE_1; 1. DR PROSITE; PS00739; ADOHCYASE_2; 1. KW Hydrolase; NAD; One-carbon metabolism. FT DOMAIN 183 350 NAD BINDING (BY SIMILARITY). SQ SEQUENCE 431 AA; 47252 MW; F883FAA7DF2D898A CRC64; MSKPSYKVAD ISLAEWGRKA IIIAENEMPG LMACRKKYGP SKPLKGARIT GCLHMTVQTA VLIETLVELG AQVQWSSCNI FSTQDNAAAA IAATGVPVYA WKGETDEEYM WCIEQTLVFP DGQPLNMILD DGGDLTNLVH EKFPQFLKNI KGLSEETTTG VHNLYKMFKE GRLGVPAINV NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVCCVAG YGDVGKGCAQ ALKGFGGRVI VTEVDPINAL QAAMEGYEVT TMEEGSKEAS IFVTTTGCRD IITSVHLQQM PDDRIVCNIG HFDIEIDVDW LNANAKEKVN VKPQVDRYTM KSGKHIILLA EGRLVNLGCA DGHPSFVMSN SFTNQVLAQI ELWTKSDKSV GVHVLPKILD EEVASLHLEK LGVKLTKLTE KQATYLGVSQ TGPFKPDHYR Y // ID SALA_DROME STANDARD; PRT; 142 AA. AC P21750; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Protein spalt-accessory. GN SALA OR SAL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Frei E., Schuh R., Baumgartner S., Burri M., Noll M., Juergens G., RA Seifert E., Nauber U., Jaeckle H.; RT "Molecular characterization of spalt, a homeotic gene required for RT head and tail development in the Drosophila embryo."; RL EMBO J. 7:197-204(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=89315821; PubMed=2568636; RA Reuter D., Schuh R., Jaeckle H.; RT "The homeotic gene spalt (sal) evolved during Drosophila speciation."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5483-5486(1989). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57474; CAA40712.1; -. DR PIR; S00262; S00262. DR FlyBase; FBgn0003313; sala. SQ SEQUENCE 142 AA; 14554 MW; 7386D6C8C12E5044 CRC64; MKLLIALFAL VTAVIAQNGF GQVGQGGYGG QGGFGGFGGI GGQAGFGGQI GFTGQGGVSG QVGIGQGGVH PGQGGFAGQG SPNQYQPGYG SPVGSGHFHG ANPVESGHFH ENPHEYPEHH GDHHREHHEH HGHHEHHGHH RH // ID SALM_DROME STANDARD; PRT; 1355 AA. AC P39770; DT 01-FEB-1995 (Rel. 31, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Homeotic protein spalt-major. GN SALM. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94139659; PubMed=7905822; RA Kuehnlein R.P., Frommer G., Friedrich M., Gonzalez-Gaitan M., RA Weber A., Wagner-Bernholz J.F., Gehring W.J., Jaeckle H., Schuh R.; RT "Spalt encodes an evolutionarily conserved zinc finger protein of RT novel structure which provides homeotic gene function in the head and RT tail region of the Drosophila embryo."; RL EMBO J. 13:168-179(1994). CC -!- FUNCTION: REQUIRED FOR THE ESTABLISHMENT OF THE POSTERIOR-MOST CC HEAD AND THE ANTERIOR-MOST TAIL SEGMENTS OF THE EMBRYO. PROBABLY CC FUNCTION AS A TRANSCRIPTIONAL REGULATOR. COULD REPRESS THE CC TRANSCRIPTION OF THE TSH GENE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: FIRST EXPRESSED AT BLASTODERM STAGE AND CC LATER IN RESTRICTED AERAS OF THE EMBRYONIC NERVOUS SYSTEM AS CC WELL AS IN THE DEVELOPING TRACHEA. CC -!- SIMILARITY: BELONGS TO THE SAL FAMILY OF C2H2-TYPE ZINC-FINGER CC PROTEINS. CC -!- SIMILARITY: CONTAINS 7 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75541; CAA53229.1; -. DR PIR; S40022; S40022. DR HSSP; P15822; 1BBO. DR FlyBase; FBgn0004579; salm. DR GO; GO:0016481; P:negative regulation of transcription; NAS. DR GO; GO:0007438; P:oenocyte development; IMP. DR GO; GO:0007467; P:photoreceptor differentiation (sensu Drosop...; IMP. DR GO; GO:0045465; P:R8 differentiation; NAS. DR GO; GO:0007423; P:sensory organ development; IMP. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 7. DR SMART; SM00355; ZnF_C2H2; 7. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7. KW Developmental protein; Zinc-finger; Metal-binding; DNA-binding; KW Nuclear protein; Transcription regulation; Repeat. FT ZN_FING 451 473 C2H2-TYPE 1. FT ZN_FING 479 501 C2H2-TYPE 2. FT ZN_FING 824 846 C2H2-TYPE 3. FT ZN_FING 852 874 C2H2-TYPE 4. FT ZN_FING 884 906 C2H2-TYPE 5. FT ZN_FING 1289 1311 C2H2-TYPE 6. FT ZN_FING 1317 1339 C2H2-TYPE 7. SQ SEQUENCE 1355 AA; 148995 MW; 6FC4EBDC0BC6355E CRC64; MKNHLSNVLC AMRSDFKDNH QETINKMIQF GTVKYGIVKQ LKDRARSADK DIGSDQEENG GCSPLTTATT TASPSRSPEP EEEQPEEQST SEQSIPEQST PDHQLENDIK SEAKSEIEPV EDNNNRVAMT KPSSEEREPN ASGSMPSSPV AEASAEEAAT ERTPEKEKEK DVEVDVEMPD EAPSSAVPST EVTLPGGAGA PVTLEAIQNM QMAIAQFAAK TIANGSNGAD NEAAMKQLAF LQQTLFNLQQ QQLFQIQLIQ QLQSQLALNQ AKQEEDTEED ADQEQDQEQE TDTYEEEERI ADMELRQKAE ARMAEAKARQ HLINAGVPLR ESSGSPAESL KRRREHDHES QPNRRTSLDN THKADTAQDA LAKLKEMENT PLPFGSDLAS SIITNHDDLP EPNSLDLLQK RAQEVLDSAS QGILANSMAD DFAFGEKSGE GKGRNEPFFK HRCRYCGKVF GSDSALQIHI RSHTGERPFK CNVCGSRFTT KGNLKVHFQR HAQKFPHVPM NATPIPEHMD KFHPPLLDQM SPTDSSPNHS PAPPPLGSAP ASFPPAFPGL QNLYRPPMEI LKSLGAAAPH QYFPQELPTD LRKPSPQLDE DEPQVKNEPV EEKDQREEHE QEMAECSEPE PEPLPLEVRI KEERVEEQEQ VKQEDHRIEP RRTPSPSSEH RSPHHHRHSH MGYPPVVQPI QPAALMHPQS SPGSQSHLDH LPTPGQLPPR EDFFAERFPL NFTTAKMLSP EHHSPVRSPA GGALPPGVPP PPHHHPHHMA RSPFFNPIKH EMAALLPRPH SNDNSWENFI EVSNTCETMK LKELMKNKKI SDPNQCVVCD RVLSCKSALQ MHYRTHTGER PFKCRICGRA FTTKGNLKTH MAVHKIRPPM RNFHQCPVCH KKYSNALVLQ QHIRLHTGEP TDLTPEQIQA AEIRDPPPSM MPGHFMNPFA AAAFHFGALP GGPGGPPGPN HGAHNGALGS ESSQGDMDDN MDCGEDYDDD VSSEHLSNSN LEQEGDRSRS GDDFKSLLFE QKLRIDATGV VNTNPVRPRS SASSHGHSVG STSAPTSPSV HASSQVIKRS SSPARSEASQ GALDLTPRAA PTSSSSSRSP LPKEKPVSPP SLPRSPSGSS HASANILTSP LPPTVGIDCL PKGLQHHLQQ QHQHLMQQQA AVAAAAAAQH HHHQQMAALD QHQEQLRREA AEAQQKAAAA AAAAAAAAAA QRQTPPQARD QRQEGGPGAG PPPNPLMGAR PPFGMFPNLP LFPPATTQNM CNAMNQIAQS VMPAAPFNPL ALSGVRGSTT CGICYKTFPC HSALEIHYRS HTKERPFKCS ICDRGFTTKG NLKQHMLTHK IRDMEQETFR NRAVK // ID SAS_DROME STANDARD; PRT; 1693 AA. AC Q04164; Q960M6; Q9VI73; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative epidermal cell surface receptor precursor (Stranded at second DE protein). GN SAS OR CG2507. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG). RX MEDLINE=92290115; PubMed=1339334; RA Schonbaum C.P., Organ E.L., Qu S., Cavener D.R.; RT "The Drosophila melanogaster stranded at second (sas) gene encodes a RT putative epidermal cell surface receptor required for larval RT development."; RL Dev. Biol. 151:431-445(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: VITAL FOR LARVAL DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q04164-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q04164-2; Sequence=VSP_004071; CC -!- TISSUE SPECIFICITY: EXPRESSED IN MOST, IF NOT ALL, ECTODERMAL CC TISSUES WHICH PRODUCE A CUTICLE. CC -!- DEVELOPMENTAL STAGE: THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: CONTAINS 1 FIBRONECTIN TYPE III DOMAIN. CC -!- SIMILARITY: CONTAINS 2 VWFC DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M68866; AAA28879.1; -. DR EMBL; AE003672; AAN13346.1; -. DR EMBL; AE003672; AAF54052.2; -. DR EMBL; AY051979; AAK93403.1; -. DR FlyBase; FBgn0002306; sas. DR GO; GO:0016324; C:apical plasma membrane; NAS. DR GO; GO:0005887; C:integral to plasma membrane; NAS. DR GO; GO:0004872; F:receptor activity; NAS. DR GO; GO:0002168; P:larval development (sensu Insecta); IMP. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003961; FN_III. DR InterPro; IPR001007; VWF_C. DR Pfam; PF00041; fn3; 1. DR SMART; SM00060; FN3; 3. DR SMART; SM00214; VWC; 4. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. KW Receptor; Developmental protein; Signal; Transmembrane; Glycoprotein; KW Repeat; Alternative splicing. FT SIGNAL 1 41 POTENTIAL. FT CHAIN 42 1693 PUTATIVE EPIDERMAL CELL SURFACE RECEPTOR. FT DOMAIN 42 1635 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1636 1656 POTENTIAL. FT DOMAIN 1657 1693 CYTOPLASMIC (POTENTIAL). FT DOMAIN 51 377 THR-RICH. FT DOMAIN 534 901 CYS-RICH. FT DOMAIN 997 1273 GLU/PRO-RICH. FT DOMAIN 663 708 VWFC 1. FT DOMAIN 828 902 VWFC 2. FT DOMAIN 1411 1501 FIBRONECTIN TYPE-III. FT CARBOHYD 106 106 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 109 109 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 330 330 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 473 473 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 538 538 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 622 622 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 685 685 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 827 827 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 846 846 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 929 929 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 939 939 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1323 1323 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1419 1419 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1517 1517 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 930 1274 Missing (in isoform Short). FT /FTId=VSP_004071. FT CONFLICT 591 591 V -> L (IN REF. 1). FT CONFLICT 1509 1509 V -> G (IN REF. 1). SQ SEQUENCE 1693 AA; 185253 MW; DA50F96677F41DC4 CRC64; MQTCRRRKAS GGQSTIKWSR MCLATLCGLL LLGIQIERAA SAPAGEDAAA TTMPPLDTTT DAPDAVAATT TPATTAAEQS SSISSITTEA ADGSTTSTTT TTEAANKSNA TETDFTTNVP VASSLPEETS VRSTSIEPIT STEPTTTPRQ ETEGPDQHMV FSNTEPDQSH IQHIPLRDEH AESSGADDAT TEMQRQREQD QQQNELNQIS NEQDDVVKDL NNFRHPATLI TASNSNSEEN VEIESDKQVE TTTTAVPAAA TSTSTEATGT PPTGTPATST STVPNEREED PYHVHILSEN HDRLAEHEDY QMLSTSTEES STTSTTSTTN STTESGIVAG IVVSQENKAT AEPSTATEST SISTSTTTAA TAATSTTSRA RAMHMNDPED EAATTIMPDS ESVPVINIVE GQHMLQQEDQ KDEEEEGVVK ESESSSTTEA STTTTEPSPF VAFAGEGRSA GGGNDIELFL HHNGSTHEQL MDLSDVSMDG DQNEGSSKTE SSTTSTTTTT AQPETEMPKI VEITASGDTM QRECLANNKS YKHGELMERD CDERCTCNRG DWMCEPRCRG LSYPRGSQRS MANPNCLEKM VEEDECCRVM ECSEPQLEPT VVATEGAAPS TNGTGESAVT LPTTDDEATP KPRTDCHYNS GVYKFRERLE IGCEQICHCA EGGVMDCRPR CPERNHTRLD KCVYVKDPKD VCCQLELCDV TLDDHEQQPT PLQSNNNEDP EEIDPFRFQE QARDAGGAKP TCTFKGAEYD VGQQFRDGCD QLCICNEQGI HCAKLECPSN FGLDVQDPHC IRWEPVPADF KPSPPNCCPE SMRCVDNGTC SYQGVQIENW SPVPANLTGC DQHCYCENGR VECRAACPPV PALPPADLPC HPALARLLPI PDDECCKHWM CAPQIPKIGG AGQDEETEAT STHSSIPANE TTTTTATANK STSIPSKVPQ IKKDEEKRPP ASGAFYPTLD GKPPKSIGGL GIFEKPEKPE KAHKKVQHQQ QQHQQQEQQE QQQHQNDVIF DGDRTEEQEE PLPPNGGFVP FQFGQQHPHQ PHLGPYGFYN PVKPVYEDYN PYEPYDINPN GTPQGKPPPV PTSQSDLFNI LGAEQPGHPV HPGHGGPPRI HPGQTQKDNH NLGPQVRIEQ ILQHLQQTVP GGPPPPPPHQ QHQSLTPQLH PQQQQISQQH PGHYVPIVHS GVPPPPPGHG IAIVDGQTVA YESYPVIPGL GVPQHHPQQH QTTPQQHLQQ TILPSSSTTS GLSTQASEHS LHQNQGKLAK QQQSGANNLQ PDIEVHTLEA IDPRSIRIVF TVPQVYVNLH GRVELRYSNG PSNDTSTWEQ QIFAPPEDLI ATSQMEFDLP SLEPNSLYKV KITLILRDLN SQPTSSIYTV KTPPERTITP PPPFPDYRPD FQDIFKNVED PELTVSETNA SWLQLTWKKL GDDQMEYVDG VQLRYKELTG MIYSSTPLIH RTLTSYTIQN LQPDTGYEIG LYYIPLAGHG AELRAGHMIK VRTAQKVDVY GFDVTVNVTK VKTQSVEISW NGVPYPEDKF VHIYRAIYQS DAGKEDSSVF KVAKRDSTTG TLIMDLKPGT KYRLWLEMYL TNGNTKKSNV VNFITKPGGP ATPGKTGKLL TAGTDQPVGD YYGPLVVVSV IAALAIMSTL ALLLIITRRR VHQTASITPP RKSDAAYDNP SYKVEIQQET MNL // ID SAV_DROME STANDARD; PRT; 608 AA. AC Q9VCR6; Q8MQH6; Q8T9A6; Q9VCR5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Scaffold protein salvador (Shar-pei). GN SAV OR SHRP OR CG33193/CG13831/CG13832. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH RP WTS. RX MEDLINE=22190660; PubMed=12202036; RA Tapon N., Harvey K.F., Bell D.W., Wahrer D.C.R., Schiripo T.A., RA Haber D.A., Hariharan I.K.; RT "Salvador promotes both cell cycle exit and apoptosis in Drosophila RT and is mutated in human cancer cell lines."; RL Cell 110:467-478(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION. RX MEDLINE=22308884; PubMed=12421711; RA Kango-Singh M., Nolo R., Tao C., Verstreken P., Hiesinger P.R., RA Bellen H.J., Halder G.; RT "Shar-pei mediates cell proliferation arrest during imaginal disc RT growth in Drosophila."; RL Development 129:5719-5730(2002). RN [6] RP FUNCTION WITH HPO. RX MEDLINE=22822129; PubMed=12941274; RA Harvey K.F., Pfleger C.M., Hariharan I.K.; RT "The Drosophila Mst ortholog, hippo, restricts growth and cell RT proliferation and promotes apoptosis."; RL Cell 114:457-467(2003). RN [7] RP PHOSPHORYLATION BY HPO. RX MEDLINE=22822128; PubMed=12941273; RA Wu S., Huang J., Dong J., Pan D.; RT "hippo encodes a Ste-20 family protein kinase that restricts cell RT proliferation and promotes apoptosis in conjunction with salvador and RT warts."; RL Cell 114:445-456(2003). CC -!- FUNCTION: REQUIRED FOR CELL CYCLE EXIT IN EYE IMAGINAL DISK AND CC HID-INDUCED APOPTOTIC CELL DEATHS THAT ARE PART OF NORMAL RETINAL CC DEVELOPMENT. ACTIVATION OF ICE IN EYE IMAGINAL DISK BY EITHER HID CC OR RPR IS ALMOST COMPLETELY BLOCKED BY SAV EXPRESSION. PROBABLY CC PART OF A SAME TUMOR SUPPRESSION PATHWAY WITH SAV AND WTS. CC -!- SUBUNIT: INTERACTS WITH WTS VIA ITS WW DOMAINS. CC -!- TISSUE SPECIFICITY: THIRD INSTAR LARVAE EYE DISK, EXPRESSED IN A CC STRIPE IN THE MORPHOGENETIC FURROW, DECREASES IN THE REGION OF THE CC SECOND MITOTIC WAVE (SMW) AND INCREASES ONCE AGAIN POSTERIOR TO CC THE SMW. CC -!- PTM: PHOSPHORYLATED BY HPO. CC -!- SIMILARITY: CONTAINS 2 WW DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY131211; AAM97280.1; -. DR EMBL; AE003741; AAF56090.3; -. DR EMBL; AY069854; AAL39999.1; -. DR FlyBase; FBgn0053193; sav. DR GO; GO:0006917; P:induction of apoptosis; IMP. DR GO; GO:0000074; P:regulation of cell cycle; IMP. DR GO; GO:0046666; P:retinal programmed cell death; IGI. DR InterPro; IPR001202; WW_Rsp5_WWP. DR Pfam; PF00397; WW; 2. DR SMART; SM00456; WW; 2. DR PROSITE; PS01159; WW_DOMAIN_1; FALSE_NEG. DR PROSITE; PS50020; WW_DOMAIN_2; 2. KW Apoptosis; Repeat; Coiled coil; Phosphorylation. FT DOMAIN 274 294 COILED COIL (POTENTIAL). FT DOMAIN 423 456 WW 1. FT DOMAIN 458 491 WW 2. FT DOMAIN 231 234 POLY-GLN. FT DOMAIN 275 289 POLY-GLN. FT DOMAIN 107 132 HIS-RICH. FT CONFLICT 119 119 S -> A (IN REF. 4). FT CONFLICT 194 194 L -> M (IN REF. 1). FT CONFLICT 275 275 MISSING (IN REF. 4). SQ SEQUENCE 608 AA; 68145 MW; 05DF47686EE3335E CRC64; MNYLTILLCN RKPTMLSRRN KEKSQHKEGV VGKYMKKDTP PDISVINVWS DQRAKKKSLQ RCASTSPSCE FHPRSSSTSR NTYSCTDSQP DYYHARRAQS QMPLQQHSHS HPHSLPHPSH PHVRSHPPLP PHQFRASSNQ LSQNSSNYVN FEQIERMRRQ QSSPLLQTTS SPAPGAGGFQ RSYSTTQRQH HPHLGGDSYD ADQGLLSASY ANMLQLPQRP HSPAHYAVPP QQQQHPQIHQ QHASTPFGST LRFDRAAMSI RERQPRYQPT SSPMQQQQQQ QQQQQQQLQH TQLAAHLGGS YSSDSYPIYE NPSRVISMRA TQSQRSESPI YSNTTASSAT LAVVPQHHHQ GHLAVPSGSG GGSLSGSGRG GSSGSVRGAS TSVQSLYVPP RTPPSAVAGA GGSANGSLQK VPSQQSLTEP EELPLPPGWA TQYTLHGRKY YIDHNAHTTH WNHPLEREGL PVGWRRVVSK MHGTYYENQY TGQSQRQHPC LTSYYVYTTS AEPPKAIRPE ASLYAPPTHT HNALVPANPY LLEEIPKWLA VYSEADSSKD HLLQFNMFSL PELEGFDSML VRLFKQELGT IVGFYERYRR ALILEKNRRA GQNQNQNQ // ID SC10_DROME STANDARD; PRT; 710 AA. AC Q9XTM1; Q95TZ8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Exocyst complex component Sec10. GN SEC10 OR CG6159. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Zhang Y.Q., Andrews H.K., Broadie K.S.; RT "Dissecting the functions of the sec6/8 complex in synaptic RT transmission."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 175-710 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPONENT OF THE EXOCYST COMPLEX INVOLVED IN THE DOCKING CC OF EXOCYSTIC VESICLES WITH FUSIONS SITE ON THE PLASMA MEMBRANE. CC -!- SUBUNIT: THE EXOCYST COMPLEX IS COMPOSED OF SEC3, SEC5, SEC6, CC SEC8, SEC10, SEC15, EXO70 AND EXO84 (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SEC10 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ242993; CAB44702.1; -. DR EMBL; AJ242992; CAB44701.1; -. DR EMBL; AE003746; AAF56241.1; -. DR EMBL; AY058414; AAL13643.1; ALT_INIT. DR FlyBase; FBgn0027103; sec10. DR GO; GO:0000145; C:exocyst; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016081; P:synaptic vesicle docking; NAS. DR GO; GO:0016080; P:synaptic vesicle targeting; NAS. DR GO; GO:0016192; P:vesicle-mediated transport; NAS. KW Exocytosis; Transport; Protein transport; Coiled coil. FT DOMAIN 44 96 COILED COIL (POTENTIAL). SQ SEQUENCE 710 AA; 82030 MW; 256F78D2C15AD41A CRC64; MLSQYMEEFE QEPFEVGEFI ERLTWRTNNE LQNSEDFHPV ALHDTFIQTI KDLKILQEKQ QSKCERLEES LRQEKESHAK KIAKLQERHQ TAIDVFGQLD EKINSVAGKI MHLGEQLENV NTPRSRSVEA QKLLNFMSEF LAAGPVIVND IFADAARLSE AADVIQKLYA ISQDLPPGNF AESKRKIEKK YDEVERRLIE EFATAQKSED IERMKTLAQI LSQFKGYTQC VDAYIEQSQM QPYSGKDIFI GIVPLCKHHY EIIQKVFANP QQVMSKFILN IYQLKLHQYA MTKLEDKKDE EKYLRTLYEL YSRTLKLSTD LQIYMSTIDD DLLQKLTQQI FIKHLAGYAE METKCLTAKC STELEKFYAS KKHQKTATTK GFRRNMEVLI ATRANINIAA IEDYGGETFL SEELAINMLQ EAKASLKRCR LLSNETELPG NAIKLNDILL RFLMHEHVDY ALELGLQAVP LAEGRVFPQL YFFDVVQKTN IIVHLLDKLC HTSVIPCVSN TPKYSDYVFK KRILMEQIET KLDQGLDRSI SAVIGWVKVY LQYEQKKTDY KPETDVDTIS SAACLQVVQN LQPVIVQIKK CVDGENLQNV LTEFGTRLHR VIYDHLQTMQ FNTAGAMCAI CDVNEYRKCI RELDSPLVTQ LFDILHALCN LLLVKPQNLQ EVCTGDTLNY LDKSVVRQFI QLRTDFRIIK NTNYLKGIIE // ID SC15_DROME STANDARD; PRT; 766 AA. AC Q9VDE6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Exocyst complex component Sec15. GN SEC15 OR CG7034. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COMPONENT OF THE EXOCYST COMPLEX INVOLVED IN THE DOCKING CC OF EXOCYSTIC VESICLES WITH FUSIONS SITE ON THE PLASMA MEMBRANE (BY CC SIMILARITY). CC -!- SUBUNIT: THE EXOCYST COMPLEX IS COMPOSED OF SEC3, SEC5, SEC6, CC SEC8, SEC10, SEC15, EXO70 AND EXO84 (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SEC15 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003733; AAF55848.1; -. DR FlyBase; FBgn0038856; sec15. DR GO; GO:0000145; C:exocyst; ISS. DR GO; GO:0007269; P:neurotransmitter secretion; ISS. DR GO; GO:0016081; P:synaptic vesicle docking; ISS. DR GO; GO:0016080; P:synaptic vesicle targeting; ISS. DR GO; GO:0016192; P:vesicle-mediated transport; ISS. DR InterPro; IPR007225; Sec15. DR Pfam; PF04091; Sec15; 1. KW Exocytosis; Transport; Protein transport; Coiled coil. FT DOMAIN 28 90 COILED COIL (POTENTIAL). SQ SEQUENCE 766 AA; 88725 MW; AACCE87335922C13 CRC64; MSKVTVQDIE AVDDYWGPTF RSILEGNNTK QIGDQLEQRI RSHDKEIERI CNLYYQGFID SIQELLQVRT QAQQLHNEVH SLDTSLRQIS ASLIQQGNDL VRARQIESNL ASAIEALKSC LPALECYMKF TQQAKNKQYY QALRTLETLE TEHLTRLKTH NYRFATQMQI QIPIIKENIR RSSASDFREF LENIRKFSPR IGELAITHTK QLQKRDINAI IAEHMQQMNG GEAGGAGAGG DDDGANVSAQ DLIDFSPIYR CLHIYMVLGQ REYFEKDYRQ QRRDQAKLVL QPPPNMHDNL EAYKTYICAI VGFFVVEDHV KNTAGDVVTS SYLEDLWSSS LTKFVNEISM SSSSCTDPNI LLRIKNLIML SINTFKCYGY TVNILWELLH NMRDHYNEVL LQRWVHVFRE ILDKEQFLPM VVQNTEEYEC IIERFPFHSE QLENAPFPKK FPFSRMVPEV YHQAKEFMYA CMKFAEELTL SPNEVAAMVR KAANLLLTRS FSGCLSVVFR QPSITLTQLI QIIIDTQYLE KAGPFLDEFV CHMTNTERSV SQTPSAMFHV ARQDAEKQVG LRICSKIDEF FELSAYDWLL VEPPGIASAF ITDMISYLKS TFDSFAFKLP HIAQAACRRT FEHIAEKIYS IMYDEDVKQI STGALTQINL DLMQCEFFAA SEPVPGLKEG ELSKYFLRNR QLLDLLILEE WSTYFHDYGK QENRYHLVQP QSIIVILEKI READKKPIFS LVRKNDKKKL LETVLKQLKH IADRQN // ID SCAL_DROME STANDARD; PRT; 440 AA. AC P30052; Q9VXN7; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Scalloped protein. GN SD OR CG8544. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92192450; PubMed=1547938; RA Campbell S.D., Inamdar M., Rodrigues V., Raghavan V., RA Palazzolo M., Chovnick A.; RT "The scalloped gene encodes a novel, evolutionarily conserved RT transcription factor required for sensory organ differentiation in RT Drosophila."; RL Genes Dev. 6:367-379(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLE TRANSCRIPTION FACTOR THAT FUNCTION IN THE CC REGULATION OF CELL-SPECIFIC GENE EXPRESSION DURING DROSOPHILA CC DEVELOPMENT, PARTICULARLY IN THE DIFFERENTIATION OF THE NERVOUS CC SYSTEM. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: SUBSET OF NEUROBLASTS IN THE CENTRAL NERVOUS CC SYSTEM AND IN THE PERIPHERAL SENSE ORGANS OF THE EMBRYO. CC -!- SIMILARITY: CONTAINS 1 TEA DNA-BINDING DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M83787; AAA28881.1; -. DR EMBL; AE003500; AAF48521.1; -. DR PIR; A42136; A42136. DR TRANSFAC; T02030; -. DR FlyBase; FBgn0003345; sd. DR InterPro; IPR000818; TEA/ATTS. DR Pfam; PF01285; TEA; 1. DR PRINTS; PR00065; TEADOMAIN. DR SMART; SM00426; TEA; 1. DR PROSITE; PS00554; TEA_DOMAIN; 1. KW Transcription regulation; Activator; DNA-binding; Zinc-finger; KW Nuclear protein; Developmental protein. FT DNA_BIND 88 155 TEA-DOMAIN. SQ SEQUENCE 440 AA; 49658 MW; B885D7F713473A79 CRC64; MKNITSSSTC STGLLQLQNN LSCSELEVAE KTEQQAVGPG TIPSPWTPVN AGPPGALGSA DTNGSMVDSK NLDVGDMSDD EKDLSSADAE GVWSPDIEQS FQEALSIYPP CGRRKIILSD EGKMYGRNEL IARYIKLRTG KTRTRKQVSS HIQVLARRKL REIQAKIKVQ FWQPGLQPST SQDFYDYSIK PFPQPPYPAG KTSTAVSGDE TGIPPSQLPW EGRAIATHKF RLLEFTAFME IQRDEIYHRH LFVQLGGKPS FSDPLLETVD IRQIFDKFPE KSGGLKDLYE KGPQNAFYLV KCWADLNTDL TTGSETGDFY GVTSQYESNE NVVLVCSTIV CSFGKQVVEK VESEYSRLEN NRYVYRIQRS PMCEYMINFI QKLKNLPERY MMNSVLENFT ILQVMRARET QETLLCIAYV FEVAAQNSGT THHIYRLIKE // ID SCA_DROME STANDARD; PRT; 799 AA. AC P21520; Q8MQI8; Q9V6G9; DT 01-MAY-1991 (Rel. 18, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Scabrous protein precursor. GN SCA OR CG17579. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91075223; PubMed=2175046; RA Baker N.E., Mlodzik M., Rubin G.M.; RT "Spacing differentiation in the developing Drosophila eye: a RT fibrinogen-related lateral inhibitor encoded by scabrous."; RL Science 250:1370-1377(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=22640859; PubMed=12756167; RA Li Y., Fetchko M., Lai Z.C., Baker N.E.; RT "Scabrous and Gp150 are endosomal proteins that regulate Notch RT activity."; RL Development 130:2819-2827(2003). CC -!- FUNCTION: INVOLVED IN REGULATION OF NEUROGENESIS. MAY ENCODE A CC LATERAL INHIBITOR OF R8 DIFFERENTIATION. IN CONJUNCTION WITH CC GP150, PROMOTES NOTCH ACTIVATION IN RESPONSE TO DELTA BY CC REGULATING ACQUISITION OF INSENSITIVITY TO DELTA IN A SUBSET OF CC CELLS. CC -!- SUBCELLULAR LOCATION: ENDOSOMAL. COLOCALIZES IN LATE ENDOSOMES CC WITH GP150. CC -!- PTM: POSSESSES FIVE PAIRS OF DIBASIC RESIDUES THAT MAY BE THE CC TARGET OF PROTEOLYTIC PROCESSING. CC -!- SIMILARITY: CONTAINS 1 FIBRINOGEN C-TERMINAL DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60065; AAA28880.1; ALT_INIT. DR EMBL; AE003821; AAM68655.2; -. DR EMBL; AY129456; AAM76198.1; -. DR PIR; A39832; A39832. DR HSSP; P02671; 1FZD. DR FlyBase; FBgn0003326; sca. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP. DR GO; GO:0046331; P:lateral inhibition; NAS. DR GO; GO:0045468; P:regulation of R8 spacing; NAS. DR InterPro; IPR002181; Fibrinogen_C. DR Pfam; PF00147; fibrinogen_C; 1. DR SMART; SM00186; FBG; 1. DR PROSITE; PS00514; FIBRIN_AG_C_DOMAIN; 1. KW Developmental protein; Neurogenesis; Signal. FT SIGNAL 1 51 POTENTIAL. FT CHAIN 52 799 SCABROUS PROTEIN. FT DOMAIN 529 729 FIBRINOGEN C-TERMINAL. FT DOMAIN 200 343 GLN-RICH. FT DISULFID 542 568 BY SIMILARITY. FT DISULFID 687 700 BY SIMILARITY. FT CARBOHYD 372 372 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 587 587 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 618 618 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 660 660 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 744 744 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 787 787 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 301 301 G -> C (IN REF. 1). SQ SEQUENCE 799 AA; 90119 MW; 87E1B4D60D4F5C29 CRC64; MRDWQTFPDL QKKKVSRDHL NCPATMAGSN VLWPILLAVV LLQISVAFVS GAASGGVVLS DVNNMLRDAK VVTSEKPVVH SKQETEAPES SVELLRFVDD DEDSEDISSI ERQDGRTMES KKMADQVRLL TKQLNALMLR RREDYEMLEH NLRKSLRLTT NANSVDADMR SELNQLREEL AALRSSQSGN KERLTVEWLQ QTISEIRKQL VDLQRTASNV AQDVQQRSST FEDLATIRSD YQQLKLDLAA QRERQQQTEV YVQELREEML QQEQDFQHAL VKLQQRTRKD GSSASVEEES GSQEANQEQT GLETTADHKR RHCRFQSEQI HQLQLAQRNL RRQVNGLRFH HIDERVRSIE VEQHRIANAN FNLSSQIASL DKLHTSMLEL LEDVEGLQTK MDKSIPELRH EISKLEFANA QITSEQSLIR EEGTNAARSL QAMAVSVSVL QEEREGMRKL SANVDQLRTN VDRLQSLVND EMKNKLTHLN KPHKRPHHQN VQAQMPQDDS PIDSVLAETL VSELENVETQ YEAIINKLPH DCSEVHTQTD GLHLIAPAGQ RHPLMTHCTA DGWTTVQRRF DGSADFNRSW ADYAQGFGAP GGEFWIGNEQ LHHLTLDNCS RLQVQMQDIY DNVWVAEYKR FYISSRADGY RLHIAEYSGN ASDALNYQQG MQFSAIDDDR DISQTHCAAN YEGGWWFSHC QHANLNGRYN LGLTWFDAAR NEWIAVKSSR MLVKRLPAVE CQANASASGA FVSVSGSAAD AAPSSGATTT TTTATAAPAT VTTPKTNNSV VQFVAAGQA // ID SCRT_DROME STANDARD; PRT; 666 AA. AC P45843; DT 01-NOV-1995 (Rel. 32, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Scarlet protein. GN ST. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Garcia R.L., Perkins H.D., Howells A.J.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 200-306 FROM N.A. RX MEDLINE=89339145; PubMed=2503416; RA Tearle R.G., Belote J.M., McKeown M., Baker B.S., Howells A.J.; RT "Cloning and characterization of the scarlet gene of Drosophila RT melanogaster."; RL Genetics 122:595-606(1989). CC -!- FUNCTION: PART OF A MEMBRANE-SPANNING PERMEASE SYSTEM NECESSARY CC FOR THE TRANSPORT OF PIGMENT PRECURSORS INTO PIGMENT CELLS CC RESPONSIBLE FOR EYE COLOR. SCARLET AND WHITE DIMERIZE FOR THE CC TRANSPORT OF TRYPTOPHAN. CC -!- SUBUNIT: HETERODIMER OF SCARLET WITH WHITE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U39739; AAA82056.1; -. DR EMBL; X76201; CAA53794.1; -. DR FlyBase; FBgn0003515; st. DR GO; GO:0006727; P:ommochrome biosynthesis; IMP. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transporter. DR InterPro; IPR005284; Pigment_permease. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR00955; 3a01204; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. KW Pigment; ATP-binding; Transmembrane; Transport. FT NP_BIND 108 115 ATP (POTENTIAL). FT TRANSMEM 418 438 POTENTIAL. FT TRANSMEM 445 465 POTENTIAL. FT TRANSMEM 491 511 POTENTIAL. FT TRANSMEM 519 539 POTENTIAL. FT TRANSMEM 552 572 POTENTIAL. FT TRANSMEM 577 597 POTENTIAL. FT TRANSMEM 640 660 POTENTIAL. SQ SEQUENCE 666 AA; 74506 MW; 6796ED4084B59CE4 CRC64; MSDSDSKRID VEAPERVEQH ELQVMPVGST IEVPSLDSTP KLSKRNSSER SLPLRSYSKW SPTEQGATLV WRDLCVYTNV GGSGQRMKRI INNSTGAIQP GTLMALMGSS GSGKTTLMST LAFRQPAGTV VQGDILINGR RIGPFMHRNH GYVYQDDLFL GSVSVLEHLN FMAHLRLDRR VSKEERRLII KELLERTGLL SAAQTRIGSG DDKKVLSGGE RKRLAFAVEL LNNPVILFCD EPTTGLDSYS AQQLVATLYE LAQKGTTILC TIHQPSSQLF DNFNNVMLLA DGRVAFTGSP QHALSFFANH GYYCPEAYNP ADFLIGVLAT DPGYEQASQR SAQHLCDQFA VSSAAKQRDM LVNLEIHMAQ SGNFPFDTEV ESFRGVAWYK RFHVVWLRAI VTLLRDPTIQ WLRFIQKIAM AFIIGACFAG TTEPSQLGVQ AVQGALFIMI SENTYHPMYS VLNLFPQGFP LFMRETRSGL YSTGQYYAAN ILALLPGMII EPLIFVIICY WLTGLRSTFY AFGVTAMCVV LVMNVATACG CFFSTAFNSV PLAMAYLVPL DYIFMITSGI FIQVNSLPVA FWWTQFLSWM LYANEAMTAA QWSGVQNITC FQESADLPCF HTGQDVLDKY TFNESNVYRN LLAMVGLYFG FHLLGYYCLW RRARKL // ID SCR_DROME STANDARD; PRT; 415 AA. AC P09077; DT 01-NOV-1988 (Rel. 09, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Homeotic Sex combs reduced protein. GN SCR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89231621; PubMed=2565809; RA Lemotte P.K., Kuroiwa A., Fessler L.I., Gehring W.J.; RT "The homeotic gene Sex Combs Reduced of Drosophila: gene structure RT and embryonic expression."; RL EMBO J. 8:219-227(1989). RN [2] RP REVISIONS. RA Baumgartner P.; RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 314-388 FROM N.A. RA Kuroiwa A., Kloter U., Baumgartner P., Gehring W.J.; RT "Cloning of the homeotic Sex Combs Reduced gene in Drosophila and in RT situ localization of its transcripts."; RL EMBO J. 4:3757-3764(1985). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- FUNCTION: HOMEOTIC PROTEIN CONTROLLING THE SEGMENTAL CC TRANSFORMATION OF THE FIRST TO THE SECOND THORACIC SEGMENT CC (PROTHORAX TO MESOTHORAX) AND OF THE LABIAL PALPS INTO MAXILLARY CC PALPS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ANTP HOMEOBOX FAMILY. DEFORMED CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14475; CAA32637.1; -. DR EMBL; X05228; CAA28857.1; ALT_SEQ. DR PIR; S03631; S03631. DR HSSP; P02833; 1SAN. DR TRANSFAC; T02096; -. DR FlyBase; FBgn0003339; Scr. DR GO; GO:0007379; P:segment specification; NAS. DR GO; GO:0045498; P:sex comb development; NAS. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DOMAIN 36 51 GLY/SER-RICH. FT DOMAIN 141 160 GLN-RICH. FT DOMAIN 186 198 ASN-RICH. FT SITE 302 307 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 322 381 HOMEOBOX. FT CONFLICT 321 321 E -> Q (IN REF. 3). FT CONFLICT 377 377 W -> L (IN REF. 3). SQ SEQUENCE 415 AA; 44261 MW; 060BFFD377DEB7C3 CRC64; MDPDCFAMSS YQFVNSLASC YPQQMNPQQN HPGAGNSSAG GSGGGAGGSG GVVPSGGTNG GQGSAGAATP GANDYFPAAA AYTPNLYPNT PQPTTPIRRL ADREIRIWWT TRSCSRSDCS CSSSSNSNSS NMPMQRQSCC QQQQQLAQQQ HPQQQQQQQQ ANISCKYAND PVTPGGSGGG GVSGSNNNNN SANSNNNNSQ SLASPQDLST RDISPKLSPS SVVESVARSL NKGVLGGSLA AAAAAAGLNN NHSGSGVSGG PGNVNVPMHS PGGGDSDSES DSGNEAGSSQ NSGNGKKNPP QIYPWMKRVH LGTSTVNANG ETKRQRTSYT RYQTLELEKE FHFNRYLTRR RRIEIAHALC LTERQIKIWF QNRRMKWKKE HKMASMNIVP YHMGPYGHPY HQFDIHPSQF AHLSA // ID SCW_DROME STANDARD; PRT; 400 AA. AC P54631; DT 01-OCT-1996 (Rel. 34, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Screw protein precursor. GN SCW. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95047397; PubMed=7958918; RA Arora K., Levine M.S., O'Connor M.B.; RT "The screw gene encodes a ubiquitously expressed member of the RT TGF-beta family required for specification of dorsal cell fates in RT the Drosophila embryo."; RL Genes Dev. 8:2588-2601(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PART OF THE SIGNAL THAT SPECIFIES DORSAL CELL FATES IN CC THE EMBRYO. ACTS TOGETHER WITH DPP. CC -!- SUBUNIT: HETERODIMERS OF SCW/DPP ARE THE ACTIVE SUBUNIT, DPP/DPP CC HOMODIMERS ELICIT A BASAL RESPONSE AND SCW/SCW HOMODIMERS ALONE CC ARE INEFFECTIVE IN SPECIFYING A DORSAL PATTERN. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED DURING EARLY STAGES OF CC EMBRYOGENESIS. CC -!- DEVELOPMENTAL STAGE: TRANSCRIPT IS FIRST DETECTED AT STAGE 4 CC EMBRYO, HIGHEST EXPRESSION IS FOUND DURING SYNCYTIAL BLASTODERM CC (NUCLEAR CYCLES 11-12). IT DECLINES RAPIDLY IN EMBRYOS AT CELLULAR CC BLASTODERM STAGE 5 AND IT IS NOT DETECTED DURING THE REST OF CC EMBRYONIC DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE TGF-BETA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17573; AAA56872.1; -. DR EMBL; AE003663; -; NOT_ANNOTATED_CDS. DR EMBL; AY051793; AAK93217.1; -. DR HSSP; P18075; 1BMP. DR FlyBase; FBgn0005590; scw. DR GO; GO:0007378; P:amnioserosa formation; NAS. DR GO; GO:0007179; P:TGFbeta receptor signaling pathway; NAS. DR InterPro; IPR002400; GF_cysknot. DR InterPro; IPR001839; TGFb. DR InterPro; IPR001111; TGFb_N. DR Pfam; PF00019; TGF-beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR PRINTS; PR00438; GFCYSKNOT. DR ProDom; PD000357; TGFb; 1. DR SMART; SM00204; TGFB; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. KW Growth factor; Differentiation; Glycoprotein; Signal. FT SIGNAL 1 16 POTENTIAL. FT PROPEP 17 277 POTENTIAL. FT CHAIN 278 400 SCREW PROTEIN. FT DOMAIN 283 297 PRO-RICH. FT DISULFID 300 365 BY SIMILARITY. FT DISULFID 329 397 BY SIMILARITY. FT DISULFID 333 399 BY SIMILARITY. FT DISULFID 364 364 INTERCHAIN (BY SIMILARITY). FT CARBOHYD 165 165 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 189 189 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 201 201 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 304 304 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 342 342 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 6 6 F -> L (IN REF. 1). SQ SEQUENCE 400 AA; 45890 MW; 2B42B7D28B9B8336 CRC64; MLNVFFLTSL FYAASATTYV TTNNHIEMPI YQKRPLSEQM EMIDILDLGD RPRRQAEPNL HNSASKFLLE VYNEISEDQE PKEVLHQRHK RSLDDDILIS NEDRQEIASC NSILTFSSRL KPEQLDNELD MHITFNTNDV PVDLSLVQAM LRIYKQPSLV DRRANFTVSV YRKLDNRQDF SYRILGSVNT TSSQRGWLEF NLTDTLRYWL HNKGLQRRNE LRISIGDSQL STFAAGLVTP QASRTSLEPF IVGYFNGPEL LVKIQKLRFK RDLEKRRAGG GSPPPPPPPP VDLYRPPQSC ERLNFTVDFK ELHMHNWVIA PKKFEAYFCG GGCNFPLGTK MNATNHAIVQ TLMHLKQPHL PKPCCVPTVL GAITILRYLN EDIIDLTKYQ KAVAKECGCH // ID SDC_DROME STANDARD; PRT; 395 AA. AC P49415; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Syndecan precursor. GN SDC OR SYD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94211858; PubMed=8159748; RA Spring J., Paine-Saunders S.E., Hynes R.O., Bernfield M.; RT "Drosophila syndecan: conservation of a cell-surface heparan sulfate RT proteoglycan."; RL Proc. Natl. Acad. Sci. U.S.A. 91:3334-3338(1994). CC -!- FUNCTION: CELL SURFACE PROTEOGLYCAN THAT BEARS HEPARAN SULFATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE SYNDECAN PROTEOGLYCAN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03282; AAC34307.1; -. DR PIR; A54949; A54949. DR FlyBase; FBgn0010415; Sdc. DR InterPro; IPR003585; Neurexin-like. DR InterPro; IPR001050; Syndecan. DR Pfam; PF01034; Syndecan; 1. DR SMART; SM00294; 4.1m; 1. DR PROSITE; PS00964; SYNDECAN; 1. KW Proteoglycan; Heparan sulfate; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 28 POTENTIAL. FT CHAIN 29 395 SYNDECAN. FT DOMAIN 29 335 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 336 360 POTENTIAL. FT DOMAIN 361 395 CYTOPLASMIC (POTENTIAL). FT DOMAIN 114 169 SER/THR/PRO-RICH. FT CARBOHYD 62 62 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 79 79 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 81 81 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 110 110 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). FT CARBOHYD 155 155 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 190 190 O-LINKED (GLYCOSAMINOGLYCAN) (POTENTIAL). SQ SEQUENCE 395 AA; 41853 MW; 4FF4AE3952240162 CRC64; MKPKQKISVE PLLLVAILIG VLVAATHAQD QKSVKPSAAR HPAAASRPHD EIYIDDDSIE GSGGRGGIHE DLEKDPDYSG SGFGPDDEDA EPDQHSHSSH NTRISQSSNS GINTAHTPTQ TSSTIPTTST STPMPTTTPA STTTAAATQI SSFANSSSTT TTTTLAPTIP AEPQQPLFPP FDKDLDTESS GDGIDADAED DDEDDGDDKD YDYNKELDKE IDIDGPEPGH LPPVVHHNTV ETGHIPTTDE IDVDGGDEDD NGDSDIDGPR IGGNDGDITE RGPGAGGSNV HELDPNTNVN SQPSDTKGID HRPNGNEVVI MSEDDRTSSF FSQPGILAAV IGGAVVGLLC AILVVMFIVY RMRKKDEGSY ALDEPKRSPA NNSYAKNANN REFYA // ID SEC5_DROME STANDARD; PRT; 894 AA. AC Q9VQQ9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable exocyst complex component Sec5. GN SEC5 OR CG8843. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPONENT OF THE EXOCYST COMPLEX INVOLVED IN THE DOCKING CC OF EXOCYSTIC VESICLES WITH FUSIONS SITE ON THE PLASMA MEMBRANE (BY CC SIMILARITY). CC -!- SUBUNIT: THE EXOCYST COMPLEX IS COMPOSED OF SEC3, SEC5, SEC6, CC SEC8, SEC10, SEC15, EXO70 AND EXO84 (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SEC5 FAMILY. CC -!- SIMILARITY: CONTAINS 1 TIG DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003579; AAF51106.1; -. DR EMBL; AY069793; AAL39938.1; -. DR FlyBase; FBgn0031537; sec5. DR GO; GO:0000145; C:exocyst; ISS. DR GO; GO:0007269; P:neurotransmitter secretion; ISS. DR GO; GO:0016081; P:synaptic vesicle docking; ISS. DR GO; GO:0016080; P:synaptic vesicle targeting; ISS. DR GO; GO:0016192; P:vesicle-mediated transport; ISS. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR002909; IPT_TIG. DR Pfam; PF01833; TIG; 1. KW Exocytosis; Transport; Protein transport. FT DOMAIN 5 89 TIG. SQ SEQUENCE 894 AA; 100728 MW; 3BE241DAAD7963D9 CRC64; MAPQPVVTGL SPKEGPPGTR VIIRGEFLGT RVQDLIGLKI CGSDCLLSAE WKSPNKIIAR TGPAKGKGDI IVTTLSGGVG TSTVQFRAYH ETIGPLKESA VWIEESPSQN FAWGRRTLAQ SGLTQEDPLG LSIEGNEQKI PEDLRDLFPE ACGDLSQEHF SPAWFLLENH LATSFEDLKA GLSYLKRKVE SQKEGQLSFL KSNAGSVIDQ LDTLMNIRDK LQEDVKLHGN ETLNILETSI ENSISESQKI FTDVLVRKEK ADSTRSVLFA LSRHKFLFCL PNSVDRRAKA GEYDIVVNDY SRAKNLFGKT EIPIFRKVLE EVDHRILSIR KQLHEKVVKM PQSVEQQKKL IKALISLELQ QSGTPIGDKL RNIDPAWDAI EARAKYLEWT FRQTFDQHTS KDSGAQEKAK NRDSSQAPNR VNFCEELCDI AASQLPDLWR LGQLYFTGEL RGPHDPKPGD FKRMVLNAIE KFCVYLRLAI LIATDQRALR QSSGLAWPIG SASATHQFLP WIPQCLRFTR IAYATLISLD LPSEALDIIQ KLIDEVRLFC FSIIFKRATD RCKKLGSQET WELGVEEYPG ATLLPAALET LLIETLDEVQ SVCMQRETRE GNLLEPQSDG QREVTQRLQE FLSAFSAVIE ELAFHSHDEE TPTHNVSQLL GFPNAQQPDS VAGSGGAAAV TWEQRMLCCL ANYAYCNKIF FPRLGDIFVR YGYPLPTLAI ETARYTVNQL FTNLLEEYVE HKGDPLVGTI EPSMYLGRFQ WDHEMEIGQL RPYAHECCDN LVGVYSEIYS ISPALLRPIL ESIVQTISEE LARLMSCVQR FSFTGAIQAH VDIRLLRDSL EGYVNETAKN YFMEALEAIN PPLSGEQKRK ADEILERVKR NMRLQLLCFS VKDP // ID SEC6_DROME STANDARD; PRT; 738 AA. AC Q9V8K2; Q95TT4; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Exocyst complex component Sec6. GN SEC6 OR CG5341. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPONENT OF THE EXOCYST COMPLEX INVOLVED IN THE DOCKING CC OF EXOCYSTIC VESICLES WITH FUSIONS SITE ON THE PLASMA MEMBRANE. CC -!- SUBUNIT: THE EXOCYST COMPLEX IS COMPOSED OF SEC3, SEC5, SEC6, CC SEC8, SEC10, SEC15, EXO70 AND EXO84 (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SEC6 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003799; AAF57664.2; -. DR EMBL; AY058549; AAL13778.1; -. DR FlyBase; FBgn0034367; sec6. DR GO; GO:0000145; C:exocyst; ISS. DR GO; GO:0007269; P:neurotransmitter secretion; ISS. DR GO; GO:0016081; P:synaptic vesicle docking; ISS. DR GO; GO:0016080; P:synaptic vesicle targeting; ISS. DR GO; GO:0016192; P:vesicle-mediated transport; ISS. KW Exocytosis; Transport; Protein transport; Coiled coil. FT DOMAIN 28 91 COILED COIL (POTENTIAL). SQ SEQUENCE 738 AA; 86663 MW; EA56ABF82AE7865A CRC64; MDLQQLEEQA RQAALKDIQN MLQRPGQLEK VEQYRHRIAR KKASVEALLK TGMQGQLDGV RVGLKQLETC MQDVREVRRR MDEVERLLRG VPEVYDALEV VREENTKHSQ YATAMENLKH IFNVDASVQK TMALIEDDKL LNAHQCLADL ENSRDDLLYE LHKQPKQHAS DKITLKRHFE KVDTVSQELE KKLRLILSRT LNTLRKKPTI IVTALRIIER EEKNDQFALQ QQKVTGFLPP GRPKAWRRMI MDVLQQSVIT RIEGSKLEER ADNKMWLVRD LEILRQIILE DLRVVKSLCV PCFPPHYDIF GEYVKFYHEG LSSYLDNIVR SGLEGNEYVS MMAWVTHTYP GVELMSHPDL NVDVHRQIGT LLRPEHLKAL EDEYLQNMQR NFQEWMTKAA ETEKQEWFTE TVPDQDEEYY HTSAPVIIFQ MIDQHLQVTN TIHQELTFKA LVMSIQQVEI FGQTYLKNVI ELKEHHFRNR DQIKYFTHYI ITIVNNSQQM VELAQQMKQL YWPKSRTEHY EDFERLLATF QRIRAHAASY LLEEAFLDME CHFNDLFTAK WLASNIAVDT ICVTLDDYFQ DYNHLRPNNF EMVINEAQKL LAKRYIRALL SKRLSKPRAE CDAITRKIKT EAKRFKLFFE KIAPKISLSD SPLDLISTLS ALLSSDIELL VLDLHTLLGS YPSLNEDHLV RLFYIRNDVK AAEVREKVQD AMKSKKAMVS IAKQDCIFKE IVFSDKLW // ID SELD_DROME STANDARD; PRT; 398 AA. AC O18373; O18597; Q9V700; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Selenide,water dikinase (EC 2.7.9.3) (Selenophosphate synthetase) DE (Selenium donor protein) (Patufet protein). GN SELD OR PTUF OR PTF1 OR CG8553. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=98062363; PubMed=9398525; RA Persson B.C., Boeck A., Jaeckle H., Vorbrueggen G.; RT "SelD homolog from Drosophila lacking selenide-dependent RT monoselenophosphate synthetase activity."; RL J. Mol. Biol. 274:174-180(1997). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=98151769; PubMed=9491069; RA Alsina B., Serras F., Baguna J., Corominas M.; RT "patufet, the gene encoding the Drosophila melanogaster homologue of RT selenophosphate synthetase, is involved in imaginal disc RT morphogenesis."; RL Mol. Gen. Genet. 257:113-123(1998). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: DOES NOT SEEM TO SYNTHESIZES SELENOPHOSPHATE FROM CC SELENIDE AND ATP. CC -!- CATALYTIC ACTIVITY: ATP + SELENIDE + H(2)O = AMP + SELENOPHOSPHATE CC + PHOSPHATE. CC -!- TISSUE SPECIFICITY: EXPRESSED AT LOW LEVELS THROUGHOUT THE EMBRYO. CC FROM STAGE 13 EXPRESSION IS HIGH IN CENTRAL NERVOUS SYSTEM AND CC MIDGUT, ESPECIALLY IN THE GASTRIC CAECAE. CC -!- SIMILARITY: BELONGS TO THE SELENOPHOSPHATE SYNTHETASE 1 FAMILY. CC CLASS II SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ000672; CAA04229.1; -. DR EMBL; U91994; AAB88790.1; -. DR EMBL; AE003815; AAM70998.1; -. DR FlyBase; FBgn0020615; SelD. DR GO; GO:0008283; P:cell proliferation; IMP. DR GO; GO:0007444; P:imaginal disc development; IMP. DR GO; GO:0016260; P:selenocysteine biosynthesis; IMP. DR InterPro; IPR000728; AIR_synth. DR InterPro; IPR004536; SelD. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR TIGRFAMs; TIGR00476; selD; 1. KW Transferase; Selenium; ATP-binding. FT ACT_SITE 51 51 POTENTIAL. FT SITE 52 52 IMPORTANT FOR CATALYTIC ACTIVITY (BY FT SIMILARITY). FT NP_BIND 290 296 ATP (POTENTIAL). FT CONFLICT 253 254 ED -> KN (IN REF. 2). SQ SEQUENCE 398 AA; 43446 MW; B265DAF4FDACC2D8 CRC64; MSYAADVLNS AHLELHGGGD AELRRPFDPT AHDLDASFRL TRFADLKGRG CKVPQDVLSK LVSALQQDYS AQDQEPQFLN VAIPRIGIGL DCSVIPLRHG GLCLVQTTDF FYPIVDDPYM MGKIACANVL SDLYAMGVTD CDNMLMLLAV STKMTEKERD VVIPLIMRGF KDSALEAGTT VTGGQSVVNP WCTIGGVAST ICQPNEYIVP DNAVVGDVLV LTKPLGTQVA VNAHQWIDQP ERWNRIKLVV SEEDVRKAYH RAMNSMARLN RVAARLMHKY NAHGATDITG FGLLGHAQTL AAHQKKDVSF VIHNLPVIAK MAAVAKACGN MFQLLQGHSA ETSGGLLICL PREQAAAYCK DIEKQEGYQA WIIGIVEKGN KTARIIDKPR VIEVPAKD // ID SEP1_DROME STANDARD; PRT; 361 AA. AC P42207; Q9VRH5; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Septin 1 (DIFF6 protein homolog) (Innocent bystander protein). GN SEP1 OR DIFF6 OR IBY OR CG1403. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RA Hayward D.C., Delaney S.J., Miklos G.L.G.; RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RA Fares H.F., Peifer M.A., Pringle J.R.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98188272; PubMed=9520435; RA Maleszka R., de Couet H.G., Miklos G.L.G.; RT "Data transferability from model organisms to human beings: insights RT from the functional genomics of the flightless region of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN CYTOKINESIS (POTENTIAL). CC -!- SUBUNIT: MAY ASSEMBLE INTO A MULTICOMPONENT STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE SEPTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67202; CAA47638.1; -. DR EMBL; L33246; AAC34305.1; -. DR EMBL; AF017777; AAC28401.1; -. DR EMBL; AE003568; AAF50825.1; -. DR PIR; S25063; S25063. DR FlyBase; FBgn0011710; Sep1. DR InterPro; IPR000038; GTP_Cell_Div. DR InterPro; IPR008113; Septin2. DR Pfam; PF00735; GTP_CDC; 1. DR PRINTS; PR01740; SEPTIN2. DR ProDom; PD002565; GTP_Cell_Div; 1. KW Cell division; GTP-binding. FT NP_BIND 42 49 GTP (POTENTIAL). SQ SEQUENCE 361 AA; 41131 MW; AE7D4860B625AB00 CRC64; MADTKGFSSI ETPGYVGFAN LPNQVHRKSV KKGFEFTLMV VGESGLGKST LVNSLFLTDL YPERIIPDAI EKQKQTVKLE ASTVEIEERG VKLRLTVVDT PGFGDAIDNS NSFGAILEYI DEQYERFLRD ESGLNRRNIV DNRIHCCFYF ISPFGHGLKP LDVEFMKKLH SKVNIVPVIA KADCLTKKEI LRLKCRIMQE IESHGIKIYP LPDCDSDEDE DYKEQVKQLK EAVPFAVCGA NTLLEVKGKK VRGRLYPWGV VEVENPDHCD FIKLRTMLIT HMQDLQEVTQ EVHYENYRSD RLAKGIKGKE NGVKAERDSS SQVVSNSVLG EKDRILQEKE AELRRMQEML AQMQARMQAQ Q // ID SEP2_DROME STANDARD; PRT; 419 AA. AC P54359; Q24092; Q9VDK8; DT 01-OCT-1996 (Rel. 34, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Septin 2. GN SEP2 OR CG4173. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Al-Awar O.S., Peifer M., Pringle J.R.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN CYTOKINESIS (POTENTIAL). CC -!- SUBUNIT: MAY ASSEMBLE INTO A MULTICOMPONENT STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE SEPTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U28966; AAB52512.1; -. DR EMBL; AE003731; AAF55783.1; -. DR EMBL; AY061281; AAL28829.1; -. DR FlyBase; FBgn0014029; Sep2. DR InterPro; IPR000038; GTP_Cell_Div. DR Pfam; PF00735; GTP_CDC; 1. DR ProDom; PD002565; GTP_Cell_Div; 1. KW Cell division; GTP-binding. FT NP_BIND 50 57 GTP (POTENTIAL). SQ SEQUENCE 419 AA; 48474 MW; 00D65B757C7DD0D4 CRC64; MSVEVDFVDK KEVHLRTLKQ SGHVGFDSLP DQLVNKSVQN GFVFNVMCIG ETGLGKSTLM DTLFNTSFES TPSPHTLPSV KLKAHTYELQ ESNVRLKLTI CDTVGYGDQI NKDDSFKAVV DYIDAQFENY LQEELKIKRS LVTCHDSRIH ICLYFICPTG HGLKSLDLVC MKKLDSKVNI IPVIAKADTI SKVELQRFKA KIIQELNANG VHIYQFPTDD ETVAETNTSM NSHIPFAVVG STEFIKVGNK LIRARQYPWG TVQVENETHC DFVKLREMLI RTNMEDMREK THTRHYELYR QKRLEQMGFS DVDSDNKPIS FQQTFEAKRS NHLAELQSKE EEVRQMFVQR VKEKEAELKE SEKDLHAKFE KLKRDHAEEK RKLEESRKAL EEDYLDFQRR KQQLATAHHT LTLGKSKKK // ID SER1_DROME STANDARD; PRT; 265 AA. AC P17205; Q9VAD9; Q9VAE0; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine proteases 1/2 precursor (EC 3.4.21.-). GN (SER99DA OR SER1 OR CG7877) AND (SER99DB OR SER2 OR CG15519). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89219063; PubMed=2469005; RA Yun Y., Davis R.L.; RT "Levels of RNA from a family of putative serine protease genes are RT reduced in Drosophila melanogaster dunce mutants and are regulated by RT cyclic AMP."; RL Mol. Cell. Biol. 9:692-700(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAJOR FUNCTION MAY BE TO AID IN DIGESTION. CC -!- TISSUE SPECIFICITY: ABUNDANTLY EXPRESSED IN THE LARVAL GUT. CC -!- DEVELOPMENTAL STAGE: BEGAN TO APPEAR AT LATE EMBRYO STAGE AND CC CONTINUED TO INCREASE IN ABUNDANCE THROUGHOUT THE LARVAL STAGE. CC THEY ARE NOT PRESENT IN PUPAE BUT REAPPEARED IN THE ADULT. CC -!- MISCELLANEOUS: THE SEQUENCE SHOWN IS THAT OF SER1. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24379; AAB02552.1; -. DR EMBL; M24379; AAB02553.1; -. DR EMBL; AE003771; AAN14201.1; -. DR EMBL; AE003771; AAF56972.1; -. DR PIR; A38894; A38894. DR PIR; JS0260; JS0260. DR HSSP; P00761; 1EPT. DR MEROPS; S01.UPA; -. DR FlyBase; FBgn0003356; Ser99Da. DR FlyBase; FBgn0003357; Ser99Db. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR008256; Peptidase_S1B_V8. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00839; V8PROTEASE. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Signal; Zymogen; Multigene family. FT SIGNAL 1 21 PROBABLE. FT PROPEP 22 35 BY SIMILARITY. FT CHAIN 36 265 SERINE PROTEASES 1/2. FT ACT_SITE 78 78 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 123 123 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 215 215 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 63 79 BY SIMILARITY. FT DISULFID 189 201 BY SIMILARITY. FT DISULFID 211 239 BY SIMILARITY. FT CONFLICT 14 14 A -> T (IN REF. 1; AAB02553). SQ SEQUENCE 265 AA; 28469 MW; 44848C523F03384B CRC64; MKLFVFLALA VAAATAVPAP AQKLTPTPIK DIQGRITNGY PAYEGKVPYI VGLLFSGNGN WWCGGSIIGN TWVLTAAHCT NGASGVTINY GASIRTQPQY THWVGSGDII QHHHYNSGNL HNDISLIRTP HVDFWSLVNK VELPSYNDRY QDYAGWWAVA SGWGGTYDGS PLPDWLQSVD VQIISQSDCS RTWSLHDNMI CINTDGGKST CGGDSGGPLV THDGNRLVGV TSFGSAAGCQ SGAPAVFSRV TGYLDWIRDN TGISY // ID SER3_DROME STANDARD; PRT; 272 AA. AC P17207; Q9VAD8; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine protease 3 precursor (EC 3.4.21.-). GN SER99DC OR SER3 OR CG17951. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 212-272 FROM N.A. RX MEDLINE=89219063; PubMed=2469005; RA Yun Y., Davis R.L.; RT "Levels of RNA from a family of putative serine protease genes are RT reduced in Drosophila melanogaster dunce mutants and are regulated by RT cyclic AMP."; RL Mol. Cell. Biol. 9:692-700(1989). CC -!- FUNCTION: ITS MAJOR FUNCTION MAY BE TO AID IN DIGESTION. CC -!- TISSUE SPECIFICITY: ABUNDANTLY EXPRESSED IN THE LARVAL GUT. CC -!- DEVELOPMENTAL STAGE: BEGAN TO APPEAR AT LATE EMBRYO STAGE AND CC CONTINUED TO INCREASE IN ABUNDANCE THROUGHOUT THE LARVAL STAGE. CC THEY ARE NOT PRESENT IN PUPAE BUT REAPPEARED IN THE ADULT. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003771; AAF56973.1; -. DR EMBL; M24380; AAB02551.1; -. DR PIR; PS0049; PS0049. DR HSSP; P00734; 1B7X. DR MEROPS; S01.UPA; -. DR FlyBase; FBgn0003358; Ser99Dc. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Signal; Zymogen; Multigene family. FT SIGNAL 1 17 POTENTIAL. FT PROPEP 18 40 BY SIMILARITY. FT CHAIN 41 272 SERINE PROTEASE 3. FT ACT_SITE 84 84 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 127 127 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 222 222 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 69 85 BY SIMILARITY. FT DISULFID 193 208 BY SIMILARITY. FT DISULFID 218 246 BY SIMILARITY. FT CONFLICT 212 212 P -> M (IN REF. 2). SQ SEQUENCE 272 AA; 29620 MW; A61E9DE3AFCA93AF CRC64; MRGLTLLSLA FLGVCSALTV PHSLVHPRDL EIRHGGIEGR ITNGNLASEG QVPYIVGVSL NSNGNWWWCG GSIIGHTWVL TAAHCTAGAD EASLYYGAVN YNEPAFRHTV SSENFIRYPH YVGLDHDLAL IKTPHVDFYS LVNKIELPSL DDRYNSYENN WVQAAGWGAI YDGSNVVEDL RVVDLKVISV AECQAYYGTD TASENTICVE TPDGKATCQG DSGGPLVTKE GDKLIGITSF VSAYGCQVGG PAGFTRVTKY LEWIKEETGI YY // ID SERR_DROME STANDARD; PRT; 1408 AA. AC P18168; DT 01-NOV-1990 (Rel. 16, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Serrate protein precursor (Beaded protein). GN SER OR BD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91347903; PubMed=1840519; RA Thomas U., Speicher S.A., Knust E.; RT "The Drosophila gene Serrate encodes an EGF-like transmembrane RT protein with a complex expression pattern in embryos and wing RT discs."; RL Development 111:749-761(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91099666; PubMed=2125287; RA Fleming R.J., Scottgale T.N., Diederich R.J., Artavanis-Tsakonas S.; RT "The gene Serrate encodes a putative EGF-like transmembrane protein RT essential for proper ectodermal development in Drosophila RT melanogaster."; RL Genes Dev. 4:2188-2201(1990). CC -!- FUNCTION: ESSENTIAL FOR PROPER ECTODERMAL DEVELOPMENT. SERRATE CC MAY REPRESENT AN ELEMENT IN A NETWORK OF INTERACTING MOLECULES CC OPERATING AT THE CELL SURFACE DURING THE DIFFERENTIATION OF CC CERTAIN TISSUES. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: APPEARS TO BE RESTRICTED EXCLUSIVELY TO CC CELLS OF ECTODERMAL ORIGIN. CC -!- MISCELLANEOUS: SEPARATION OF NEUROBLASTS FROM THE ECTODERM INTO CC THE INNER PART OF EMBRYO IS ONE OF THE FIRST STEPS OF CNS CC DEVELOPMENT IN INSECTS, THIS PROCESS IS UNDER CONTROL OF THE CC NEUROGENIC GENES. CC -!- MISCELLANEOUS: NOTCH AND SERRATE MAY INTERACT AT THE PROTEIN CC LEVEL, IT IS CONCEIVABLE THAT THE SERRATE AND DELTA PROTEINS MAY CC COMPETE FOR BINDING WITH THE NOTCH PROTEIN. CC -!- SIMILARITY: CONTAINS 14 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 DSL DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56811; CAA40148.1; -. DR EMBL; M35759; AAA28938.1; -. DR PIR; S16148; S16148. DR HSSP; P00743; 1CCF. DR FlyBase; FBgn0004197; Ser. DR GO; GO:0005112; F:Notch binding; NAS. DR GO; GO:0007219; P:N signaling pathway; NAS. DR GO; GO:0007435; P:salivary gland morphogenesis; NAS. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR001774; DSL. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR001438; EGF_II. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006552; VC_out. DR Pfam; PF01414; DSL; 1. DR Pfam; PF00008; EGF; 11. DR PRINTS; PR00010; EGFBLOOD. DR SMART; SM00051; DSL; 1. DR SMART; SM00179; EGF_CA; 7. DR SMART; SM00215; VWC_out; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 7. DR PROSITE; PS00022; EGF_1; 14. DR PROSITE; PS01186; EGF_2; 8. DR PROSITE; PS50026; EGF_3; 13. DR PROSITE; PS01187; EGF_CA; 5. KW Differentiation; Repeat; EGF-like domain; Transmembrane; KW Glycoprotein; Signal. FT SIGNAL 1 83 POTENTIAL. FT CHAIN 84 1408 SERRATE PROTEIN. FT DOMAIN 84 1223 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1224 1249 POTENTIAL. FT DOMAIN 1250 1408 CYTOPLASMIC (POTENTIAL). FT DOMAIN 221 283 DSL. FT DOMAIN 284 317 EGF-LIKE 1. FT DOMAIN 315 349 EGF-LIKE 2. FT DOMAIN 351 389 EGF-LIKE 3. FT DOMAIN 391 489 EGF-LIKE 4. FT DOMAIN 407 476 SER-RICH (INSERT). FT DOMAIN 491 527 EGF-LIKE 5, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 529 609 EGF-LIKE 6, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 611 646 EGF-LIKE 7, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 648 684 EGF-LIKE 8, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 686 721 EGF-LIKE 9. FT DOMAIN 723 797 EGF-LIKE 10. FT DOMAIN 737 769 THR-RICH (INSERT). FT DOMAIN 799 835 EGF-LIKE 11, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 837 877 EGF-LIKE 12. FT DOMAIN 879 915 EGF-LIKE 13. FT DOMAIN 917 953 EGF-LIKE 14, CALCIUM-BINDING (POTENTIAL). FT DISULFID 288 299 BY SIMILARITY. FT DISULFID 292 305 BY SIMILARITY. FT DISULFID 307 316 BY SIMILARITY. FT DISULFID 319 330 BY SIMILARITY. FT DISULFID 325 337 BY SIMILARITY. FT DISULFID 339 348 BY SIMILARITY. FT DISULFID 355 367 BY SIMILARITY. FT DISULFID 361 377 BY SIMILARITY. FT DISULFID 379 388 BY SIMILARITY. FT DISULFID 395 406 BY SIMILARITY. FT DISULFID 400 477 BY SIMILARITY. FT DISULFID 479 488 BY SIMILARITY. FT DISULFID 495 506 BY SIMILARITY. FT DISULFID 500 515 BY SIMILARITY. FT DISULFID 517 526 BY SIMILARITY. FT DISULFID 533 588 BY SIMILARITY. FT DISULFID 582 597 BY SIMILARITY. FT DISULFID 599 608 BY SIMILARITY. FT DISULFID 615 625 BY SIMILARITY. FT DISULFID 619 634 BY SIMILARITY. FT DISULFID 636 645 BY SIMILARITY. FT DISULFID 652 663 BY SIMILARITY. FT DISULFID 657 672 BY SIMILARITY. FT DISULFID 674 683 BY SIMILARITY. FT DISULFID 690 700 BY SIMILARITY. FT DISULFID 695 709 BY SIMILARITY. FT DISULFID 711 720 BY SIMILARITY. FT DISULFID 803 814 BY SIMILARITY. FT DISULFID 808 823 BY SIMILARITY. FT DISULFID 825 834 BY SIMILARITY. FT DISULFID 841 852 BY SIMILARITY. FT DISULFID 846 865 BY SIMILARITY. FT DISULFID 867 876 BY SIMILARITY. FT DISULFID 883 894 BY SIMILARITY. FT DISULFID 888 903 BY SIMILARITY. FT DISULFID 905 914 BY SIMILARITY. FT DISULFID 921 932 BY SIMILARITY. FT DISULFID 926 941 BY SIMILARITY. FT DISULFID 943 952 BY SIMILARITY. FT CARBOHYD 152 152 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 196 196 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 247 247 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 331 331 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 412 412 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 452 452 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 558 558 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 739 739 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 965 965 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 977 977 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1004 1004 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1030 1030 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1150 1150 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 14 17 MISSING (IN REF. 2). FT CONFLICT 27 27 P -> A (IN REF. 2). FT CONFLICT 1352 1352 T -> S (IN REF. 2). SQ SEQUENCE 1408 AA; 150660 MW; 569DA4270A9C7840 CRC64; MFRKHFRRKP ATSSSSLSSL ESTIESPDSL GMSKKTATKR QRPRHRVPKI ATLPSTIRDC RSLKSACNLI ALILILLVHK ISAAGNFELE ILEISNTNSH LLNGYCCGMP AELRATKTIG CSPCTTAFRL CLKEYQTTEQ GASISTGCSF GNATTKILGG SSFVLSDPGV GAIVLPFTFR WTKSFTLILQ ALDMYNTSYP DAERLIEETS YSGVILPSPE WKTLDHIGRN ARITYRVRVQ CAVTYYNTTC TTFCRPRDDQ FGHYACGSEG QKLCLNGWQG VNCEEAICKA GCDPVHGKCD RPGECECRPG WRGPLCNECM VYPGCKHGSC NGSAWKCVCD TNWGGILCDQ DLNFCGTHEP CKHGGTCENT APDKYRCTCA EGLSGEQCEI VEHPCATRPC RNGGTCTLKT SNRTQAQVYR TSHGRSNMGR PVRRSSSMRS LDHLRPEGQA LNGSSSSGLV SLGSLQLQQQ LAPDFTCDCA AGWTGPTCEI NIDECAGGPC EHGGTCIDLI GGFRCECPPE WHGDVCQVDV NECEAPHSAG IAANALLTTT ATAIIGSNLS STALLAALTS AVASTSLAIG PCINAKECRN QPGSFACICK EGWGGVTCAE NLDDCVGQCR NGATCIDLVN DYRCACASGF TGRDCETDID ECATSPCRNG GECVDMVGKF NCICPLGYSG SLCEEAKENC TPSPCLEGHC LNTPEGYYCH CPPDRAGKHC EQLRPLCSQP PCNEGCFANV SLATSATTTT TTTTTATTTR KMAKPSGLPC SGHGSCEMSD VGTFCKCHVG HTGTFCEHNL NECSPNPCRN GGICLDGDGD FTCECMSGWT GKRCSERATG CYAGQCQNGG TCMPGAPDKA LQPHCRCAPG WTGLFCAEAI DQCRGQPCHN GGTCESGAGW FRCVCAQGFS GPDCRINVNE CSPQPCQGGA TCIDGIGGYS CICPPGRHGL RCEILLSDPK SACQNASNTI SPYTALNRSQ NWLDIALTGR TEDDENCNAC VCENGTSRCT NLWCGLPNCY KVDPLSKSSN LSGVCKQHEV CVPALSETCL SSPCNVRGDC RALEPSRRVA PPRLPAKSSC WPNQAVVNEN CARLTILLAL ERVGKGASVE GLCSLVRVLL AAQLIKKPAS TFGQDPGMLM VLCDLKTGTN DTVELTVSSS KLNDPQLPVA VGLLGELLSS RQLNGIQRRK ELELQHAKLA ALTSIVEVKL ETARVADGSG HSLLIGVLCG VFIVLVGFSV FISLYWKQRL AYRTSSGMNL TPSLDALRHE EEKSNNLQNE ENLRRYTNPL KGSTSSLRAA TGMELSLNPA PELAASAASS SALHRSQPLF PPCDFERELD SSTGLKQAHK RTSQILLHKT QNSDMRKNTV GSLDSPRKDF GKRSINCKSM PPSSGDEGSD VLATTVMV // ID SET8_DROME STANDARD; PRT; 691 AA. AC Q9VFK6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone-lysine N-methyltransferase, H4 lysine-20 specific DE (EC 2.1.1.43) (Histone H4-K20 methyltransferase) (H4-K20-HMTase) DE (dSET8). GN PR-SET7 OR CG3307. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22166138; PubMed=12176937; RA Stapleton M., Liao G., Brokstein P., Hong L., Carninci P., Shiraki T., RA Hayashizaki Y., Champe M., Pacleb J., Wan K., Yu C., Carlson J., RA George R., Celniker S., Rubin G.M.; RT "The Drosophila gene collection: identification of putative RT full-length cDNAs for 70% of D. melanogaster genes."; RL Genome Res. 12:1294-1300(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=22082172; PubMed=12086618; RA Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J., RA Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T., RA Allis C.D., Reinberg D.; RT "PR-Set7 is a nucleosome-specific methyltransferase that modifies RT lysine 20 of histone H4 and is associated with silent chromatin."; RL Mol. Cell 9:1201-1213(2002). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=22117191; PubMed=12121615; RA Fang J., Feng Q., Ketel C.S., Wang H., Cao R., Xia L., RA Erdjument-Bromage H., Tempst P., Simon J.A., Zhang Y.; RT "Purification and functional characterization of SET8, a nucleosomal RT histone H4-Lysine 20-specific methyltransferase."; RL Curr. Biol. 12:1086-1099(2002). CC -!- FUNCTION: HISTONE METHYLTRANSFERASE. METHYLATES LYS-20 OF HISTONE CC H4. H4 LYS-20 METHYLATION REPRESENTS A SPECIFIC TAG FOR EPIGENETIC CC TRANSCRIPTIONAL REPRESSION. NUCLEOSOMES ARE PREFERRED AS SUBSTRATE CC COMPARED TO FREE HISTONES. MAY PLAY A ROLE IN MAINTAINING SILENT CC CHROMATIN BY PREVENTING NEIGHBORING ACETYLATION OF H4 TAIL. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE + HISTONE L-LYSINE = CC S-ADENOSYL-L-HOMOCYSTEINE + HISTONE N(6)-METHYL-L-LYSINE. CC -!- SUBCELLULAR LOCATION: NUCLEAR; ASSOCIATES TO CHROMATIN-DENSE AND CC TRANSCRIPTIONALLY SILENT EUCHROMATIC REGIONS. CC -!- SIMILARITY: BELONGS TO THE HISTONE-LYSINE METHYLTRANSFERASE CC FAMILY. CC -!- SIMILARITY: CONTAINS 1 SET DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY102673; AAM27502.1; -. DR EMBL; AE003704; AAF55047.2; -. DR FlyBase; FBgn0011474; pr-set7. DR InterPro; IPR001214; SET. DR Pfam; PF00856; SET; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS50280; SET; 1. KW Transferase; Methyltransferase; Chromatin regulator; Nuclear protein; KW Coiled coil. FT DOMAIN 161 181 COILED COIL (POTENTIAL). FT DOMAIN 554 680 SET. FT DOMAIN 414 437 GLN-RICH. FT DOMAIN 438 456 ASP-RICH. SQ SEQUENCE 691 AA; 76493 MW; 3462A761ED44A2D1 CRC64; MIMVRRRQRP AKEAASSSSG GASSGSGIPV DQALPLNVAG NLLEDQYFAS PKRKDCRLMK VTQNGQLPEA TMMAHNKDNK AGRTIGVPLA TRSQTRTIEN FFKANAAAKD SQKTIHTEEQ LNLGNQELKL DDEELNGQIK LDDEVLKLAD KQINENLPFA DEVDAKAEQK LMDEELQQVV EELLFDGSSR ASSNSPFYQH DMDVMQEIQQ TPEIPHIKKV TEPLEGLGSL ADFQTHRSAL RDSHSSTHSS STDNIFLQEP VLTLDIDRTP TKASSIKINR SFELAGAVFS SPPSVLNACL NGRFNQIVSL NGQKEALDLP HFDLDQHDSS SCDSGVACGL TANTESPAGQ PRRRKPATPH RILCPSPIKT ALKVTGGICK VGSADPLSPR KSPRKLPTTT AAVAACKSRR RLNQPKPQAP YQPQLQKPPS QQQQQQQDDI VVVLDDDDDE GDDEDDVRAL IKAAEERENQ NKAPATANSN KAGMKTMLKP APVKSKTKSK GPTKGQPPLP LAATNGNREM TDFFPVRRSV RKTKTAVKEE WMRGLEQAVL EERCDGLQVR HFMGKGRGVV ADRPFKRNEF VVEYVGDLIS IGEAAEREKR YALDENAGCY MYYFKHKSQQ YCIDATVDTG KLGRLINHSR AGNLMTKVVL IKQRPHLVLL AKDDIEPGEE LTYDYGDRSK ESLLHHPWLA F // ID SET_DROME STANDARD; PRT; 269 AA. AC P53997; Q9VFA5; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SET protein. GN SET OR CG4299. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95348188; PubMed=7622566; RA Kellogg D.R., Kikuchi A., Fugii-Nakata T., Turck C.W., Murray A.W.; RT "Members of the NAP/SET family of proteins interact specifically with RT B-type cyclins."; RL J. Cell Biol. 130:661-673(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBUNIT: INTERACTS SPECIFICALLY WITH B-TYPE CYCLINS. CC -!- SIMILARITY: BELONGS TO THE NUCLEOSOME ASSEMBLY PROTEIN (NAP) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U30470; AAA74264.1; -. DR EMBL; AE003708; AAF55155.1; -. DR FlyBase; FBgn0014879; Set. DR InterPro; IPR002164; NAP_family. DR Pfam; PF00956; NAP; 1. FT DOMAIN 230 269 ASP/GLU-RICH (HIGHLY ACIDIC). FT CONFLICT 15 15 MISSING (IN REF. 1). SQ SEQUENCE 269 AA; 30994 MW; 05F88CB85933BB09 CRC64; MSSVPKRAKL DGAPADGNTS AAAGNNEEES EALEQIDACQ NEIDALNEKA SEEILKVEQK YNKLRKPCYE KRSELVKRIP NFWVTSFINH PQVSGILDEE EEECLHALNK LEVEEFEDIK SGYRINFHFD ENPYFENKVL TKEFHLNSAA ASENGDWPAS TSTPIKWKEG KNLLKLLLTK PYGNKKKRNS EYKTFFDWFS DNTDPVNDEI AELIKDDLWP NPLQYYLVPD IEVEPEDEED NEDNDEEAFD DEDGEDGEGE EEEEDEDDK // ID SGG_DROME STANDARD; PRT; 1067 AA. AC P18431; O76881; P23646; Q27603; Q27604; Q27605; Q9NF42; Q9U094; AC Q9W4X3; DT 01-NOV-1990 (Rel. 16, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein kinase shaggy (EC 2.7.1.37) (Protein zeste-white 3). GN SGG OR ZW3 OR EG:BACR7C10.8 OR EG:155E2.3 OR CG2621. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=93223707; PubMed=8467811; RA Ruel L., Pantesco V., Lutz Y., Simpson P., Bourouis M.; RT "Functional significance of a family of protein kinases encoded at the RT shaggy locus in Drosophila."; RL EMBO J. 12:1657-1669(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORM ZYGOTIC), AND CHARACTERIZATION. RC STRAIN=DP CN BW; TISSUE=Embryo; RX MEDLINE=90361000; PubMed=2118107; RA Bourouis M., Moore P., Ruel L., Grau Y., Heitzler P., Simpson P.; RT "An early embryonic product of the gene shaggy encodes a RT serine/threonine protein kinase related to the CDC28/cdc2+ RT subfamily."; RL EMBO J. 9:2877-2884(1990). RN [3] RP SEQUENCE OF 193-1067 FROM N.A. (ISOFORMS SGG46 AND ZYGOTIC). RC TISSUE=Embryo, and Ovary; RX MEDLINE=90294930; PubMed=2113617; RA Siegfried E., Perkins L.A., Capaci T.M., Perrimon N.; RT "Putative protein kinase product of the Drosophila segment-polarity RT gene zeste-white3."; RL Nature 345:825-829(1990). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [7] RP PHOSPHORYLATION OF TYR-767. RX MEDLINE=93178457; PubMed=8382613; RA Hughes K., Nikolakaki E., Plyte S.E., Totty N.F., Woodgett J.R.; RT "Modulation of the glycogen synthase kinase-3 family by tyrosine RT phosphorylation."; RL EMBO J. 12:803-808(1993). RN [8] RP PHOSPHORYLATION OF ARM. RX MEDLINE=95113174; PubMed=7529201; RA Peifer M., Pai L.-M., Casey M.; RT "Phosphorylation of the Drosophila adherens junction protein RT Armadillo: roles for wingless signal and zeste-white 3 kinase."; RL Dev. Biol. 166:543-556(1994). RN [9] RP INTERACTION WITH WG AND EN. RC TISSUE=Embryo; RX MEDLINE=93113685; PubMed=1335365; RA Siegfried E., Chou T.B., Perrimon N.; RT "wingless signaling acts through zeste-white 3, the Drosophila homolog RT of glycogen synthase kinase-3, to regulate engrailed and establish RT cell fate."; RL Cell 71:1167-1179(1992). CC -!- FUNCTION: REQUIRED FOR SEVERAL DEVELOPMENTAL EVENTS SUCH AS CC SYNCTIAL BLASTODERM FORMATION AND EMBRYONIC SEGMENTATION. IS CC INVOLVED IN TRANSCRIPTIONAL REGULATION. SGG IS REQUIRED FOR ARM CC PHOSPHORYLATION. WG SIGNALING OPERATES BY INACTIVATING THE SGG CC REPRESSION OF EN AUTOACTIVATION. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=SGG46; Synonyms=Maternal, D; CC IsoId=P18431-1; Sequence=Displayed; CC Name=Zygotic; Synonyms=B, C; CC IsoId=P18431-2; Sequence=VSP_004849, VSP_004850; CC Name=SGG39; Synonyms=A; CC IsoId=P18431-3; Sequence=VSP_004849, VSP_004850, VSP_004851; CC -!- TISSUE SPECIFICITY: EXPRESSION IS OVER ALL THE EMBRYO AT ALL CC STAGES, NO LOCAL ACCUMULATION IS OBSERVED. CC -!- DEVELOPMENTAL STAGE: ISOFORM SGG46 IS EXPRESSED IN 12-24HR EMBRYOS CC AND PRESENT THROUGHOUT THE LARVAL, PUPAL AND ADULT STAGES. ISOFORM CC ZYGOTIC IS HIGHLY EXPRESSED IN 0-2HR EMBRYOS AND PRESENT BUT CC REDUCED THROUGHOUT LATER EMBRYONIC DEVELOPMENT. EXPRESSION CC PERSISTS THROUGHOUT LARVAL STAGES. ISOFORM SGG39 IS EXPRESSED IN CC 12-24HR EMBRYOS AND PRESENT THROUGHOUT THE LARVAL, PUPAL AND ADULT CC STAGES. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CDC2/CDKX SUBFAMILY; GSK-3 SUBSUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X70862; CAA50212.1; -. DR EMBL; X70863; CAA50213.1; -. DR EMBL; X70864; CAA50214.1; -. DR EMBL; X70865; CAA50215.1; -. DR EMBL; X53332; CAA37419.1; -. DR EMBL; X54005; CAA37951.1; -. DR EMBL; X54006; CAA37952.1; -. DR EMBL; AL024485; CAA19676.1; -. DR EMBL; AL034544; CAA19676.1; JOINED. DR EMBL; AL121804; CAB65860.1; -. DR EMBL; AL024485; CAB65860.1; JOINED. DR EMBL; AL121804; CAB72296.1; -. DR EMBL; AL024485; CAB72296.1; JOINED. DR EMBL; AE003425; AAF45801.2; -. DR EMBL; AE003425; AAN09082.1; -. DR EMBL; AE003425; AAN09083.1; -. DR PIR; S35327; S35327. DR HSSP; P24941; 1AQ1. DR FlyBase; FBgn0003371; sgg. DR GO; GO:0004696; F:glycogen synthase kinase 3 activity; NAS. DR GO; GO:0008407; P:bristle morphogenesis; NAS. DR GO; GO:0045475; P:locomotor rhythm; NAS. DR GO; GO:0007367; P:segment polarity determination; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Developmental protein; Segmentation polarity protein; Transferase; KW Serine/threonine-protein kinase; ATP-binding; Alternative splicing; KW Phosphorylation. FT DOMAIN 607 891 PROTEIN KINASE. FT DOMAIN 938 1067 GLY/ALA/SER-RICH. FT NP_BIND 613 621 ATP (BY SIMILARITY). FT BINDING 636 636 ATP (BY SIMILARITY). FT ACT_SITE 732 732 BY SIMILARITY. FT MOD_RES 767 767 PHOSPHORYLATION. FT VARSPLIC 1 553 Missing (in isoform Zygotic and isoform FT SGG39). FT /FTId=VSP_004849. FT VARSPLIC 554 582 ENVKTAKLARTQSCVSWTKVVQKFKNILG -> MSGRPRTS FT SFAEGNKQSPSLVLGGVKTCS (in isoform Zygotic FT and isoform SGG39). FT /FTId=VSP_004850. FT VARSPLIC 1066 1067 DS -> GSQSNSALNSSGSGGSGNGEAAGSGSGSGSGSGGG FT NGGDNDAGDSGAIASGGGAAETEAAASG (in isoform FT SGG39). FT /FTId=VSP_004851. FT CONFLICT 9 9 R -> A (IN REF. 4 AND 5; AAF45801). FT CONFLICT 193 193 T -> I (IN REF. 3). FT CONFLICT 257 259 MISSING (IN REF. 3). FT CONFLICT 259 259 MISSING (IN REF. 4). FT CONFLICT 539 540 AD -> RI (IN REF. 3). FT CONFLICT 750 750 C -> R (IN REF. 1; CAA50214). FT CONFLICT 797 797 V -> I (IN REF. 2). FT CONFLICT 948 948 G -> D (IN REF. 1; CAA50214). FT CONFLICT 950 950 A -> R (IN REF. 3). FT CONFLICT 959 959 T -> A (IN REF. 2). FT CONFLICT 999 999 A -> R (IN REF. 3). FT CONFLICT 1015 1015 A -> R (IN REF. 3). FT CONFLICT 1026 1067 GANAAVAGGAGGGGGAGAATAAATATGAIGATNAGGANVTD FT S -> EPMPPSLAVLVVVAEPVRRPQLQQQLAL (IN FT REF. 3). FT CONFLICT 1066 1067 DS -> GE (IN REF. 4). SQ SEQUENCE 1067 AA; 114440 MW; B4E98AFBF4807979 CRC64; MATTTTTQRA GAAPALNLLP ASNNNINNTL INNNNNNNNT SNSNNNNNNV ISQPIKIPLT ERFSSQTSTG SADSGVIVSS ASQQQLQLPP PRSSSGSLSL PQAPPGGKWR QKQQRQQLLL SQDSGIENGV TTRPSKAKDN QGAGKASHNA TSSKESGAQS NSSSESLGSN CSEAQEQQRV RASSALELSS VDTPVIVGGV VSGGNSILRS RIKYKSTNST GTQGFDVEDR IDEVDICDDD DVDCDDRGSE IEEEEEEEED DGVNVDDDVE EADNQSDNQS GIIINLKSQT EQEEEVDEVD AKPKNRLLPP DQAELTVAAA MARRRDAKSL ATDGHIYFPL LKISEDPHID SKLINRKDGL QDTMYYLDEF GSPKLREKFA RKQKQLLAKQ QKQLMKRERR SEEQRKKRNT TVASNLAASG AVVDDTKDDY KQQPHCDTSS RSKNNSVPNP PSSHLHQNHN HLVVDVQEDV DDVNVVATSD VDSGVVKMRR HSHDNHYDRI PRSNAATITT RPQIDQQSSH HQNTEDVEQG AEPQIDGEAD LDADADADSD GSGENVKTAK LARTQSCVSW TKVVQKFKNI LGRDGSKITT VVATPGQGTD RVQEVSYTDT KVIGNGSFGV VFQAKLCDTG ELVAIKKVLQ DRRFKNRELQ IMRKLEHCNI VKLLYFFYSS GEKRDEVFLN LVLEYIPETV YKVARQYAKT KQTIPINFIR LYMYQLFRSL AYIHSLGICH RDIKPQNLLL DPETAVLKLC DFGSAKQLLH GEPNVSYICS RYYRAPELIF GAINYTTKID VWSAGCVLAE LLLGQPIFPG DSGVDQLVEV IKVLGTPTRE QIREMNPNYT EFKFPQIKSH PWQKVFRIRT PTEAINLVSL LLEYTPSARI TPLKACAHPF FDELRMEGNH TLPNGRDMPP LFNFTEHELS IQPSLVPQLL PKHLQNASGP GGNRPSAGGA ASIAASGSTS VSSTGSGASV EGSAQPQSQG TAAAAGSGSG GATAGTGGAS AGGPGSGNNS SSGGASGAPS AVAAGGANAA VAGGAGGGGG AGAATAAATA TGAIGATNAG GANVTDS // ID SGPL_DROME STANDARD; PRT; 545 AA. AC Q9V7Y2; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Sphingosine-1-phosphate lyase (EC 4.1.2.27) (SP-lyase) (SPL) DE (Sphingosine-1-phosphate aldolase). GN SPLY OR SPL OR CG8946. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Van Veldhoven P.P.; RT "Functional expression of sphingosine-phosphate lyase from Arabidopsis RT and Drosophila."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: CLEAVES PHOSPHORYLATED SPHINGOID BASES (PSBS), SUCH AS CC SPHINGOSINE-1-PHOSPHATE, INTO FATTY ALDEHYDES AND CC PHOSPHOETHANOLAMINE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: SPHINGANINE 1-PHOSPHATE = PHOSPHOETHANOLAMINE CC + PALMITALDEHYDE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE (BY SIMILARITY). CC -!- PATHWAY: SPHINGOLIPID METABOLISM; LAST STEP. CC -!- SUBCELLULAR LOCATION: TYPE III MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GROUP II DECARBOXYLASE FAMILY. CC SPHINGOSINE-1-PHOSPHATE LYASE SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ297394; CAC10531.1; -. DR EMBL; AE003804; AAF57903.1; -. DR EMBL; AE003804; AAF57904.1; -. DR EMBL; AY052075; AAK93499.1; -. DR FlyBase; FBgn0010591; Sply. DR InterPro; IPR002129; Pyridoxal_deC. DR Pfam; PF00282; pyridoxal_deC; 1. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; FALSE_NEG. KW Lyase; Endoplasmic reticulum; Pyridoxal phosphate; Signal-anchor; KW Transmembrane. FT DOMAIN 1 26 LUMENAL (POTENTIAL). FT TRANSMEM 27 47 SIGNAL-ANCHOR (TYPE III MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 48 545 CYTOPLASMIC (POTENTIAL). FT BINDING 342 342 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 545 AA; 60305 MW; 26000F4AE43F85FD CRC64; MRPFSGSDCL KPVTEGINRA FGAKEPWQVA TITATTVLGG VWLWTVICQD ENLYIRGKRQ FFKFAKKIPA VRRQVETELA KAKNDFETEI KKSNAHLTYS ETLPEKGLSK EEILRLVDEH LKTGHYNWRD GRVSGAVYGY KPDLVELVTE VYGKASYTNP LHADLFPGVC KMEAEVVRMA CNLFHGNSAS CGTMTTGGTE SIVMAMKAYR DFAREYKGIT RPNIVVPKTV HAAFDKGGQY FNIHVRSVDV DPETYEVDIK KFKRAINRNT ILLVGSAPNF PYGTIDDIEA IAALGVKYDI PVHVDACLGS FVVALVRNAG YKLRPFDFEV KGVTSISADT HKYGFAPKGS SVILYSDKKY KDHQFTVTTD WPGGVYGSPT VNGSRAGGII AACWATMMSF GYDGYLEATK RIVDTARYIE RGVRDIDGIF IFGKPATSVI ALGSNVFDIF RLSDSLCKLG WNLNALQFPS GIHLCVTDMH TQPGVADKFI ADVRSCTAEI MKDPGQPVVG KMALYGMAQS IPDRSVIGEV TRLFLHSMYY TPSQK // ID SGS3_DROME STANDARD; PRT; 307 AA. AC P02840; Q9VTJ2; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Salivary glue protein Sgs-3 precursor. GN SGS3 OR CG11720. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83294545; PubMed=6411930; RA Garfinkel M.D., Pruitt R.E., Meyerowitz E.M.; RT "DNA sequences, gene regulation and modular protein evolution in the RT Drosophila 68C glue gene cluster."; RL J. Mol. Biol. 168:765-789(1983). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-28 FROM N.A. RX MEDLINE=88332966; PubMed=3138416; RA Martin C.H., Mayeda C.A., Meyerowitz E.M.; RT "Evolution and expression of the Sgs-3 glue gene of Drosophila."; RL J. Mol. Biol. 201:273-287(1988). RN [4] RP DEVELOPMENTAL STAGE. RX MEDLINE=94038699; PubMed=8223281; RA Huet F., Ruiz C., Richards G.; RT "Puffs and PCR: the in vivo dynamics of early gene expression during RT ecdysone responses in Drosophila."; RL Development 118:613-627(1993). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: SALIVARY GLAND SPECIFIC. CC -!- DEVELOPMENTAL STAGE: IN THE SALIVARY GLANDS OF MID INSTAR LARVAE CC LEVELS DRAMATICALLY INCREASE DURING PUFF STAGE 1 AT 98-106 HOURS CC OF DEVELOPMENT. LEVELS REMAIN CONSTANT AND ABUNDANT IN LATE LARVAE CC UNTIL PUFF STAGE 10, THEN DECREASE BY STAGE 11. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01918; CAA25994.1; -. DR EMBL; AE003544; AAF50056.1; -. DR EMBL; X78392; CAA55154.1; -. DR PIR; A03329; GSFF3. DR FlyBase; FBgn0003373; Sgs3. KW Repeat; Signal. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 307 SALIVARY GLUE PROTEIN SGS-3. SQ SEQUENCE 307 AA; 32196 MW; 45803DED16C418BC CRC64; MKLTIATALA SILLIGSANV ANCCDCGCPT TTTTCAPRTT QPPCTTTTTT TTTTCAPPTQ QSTTQPPCTT SKPTTPKQTT TQLPCTTPTT TKATTTKPTT TKATTTKATT TKPTTTKQTT TQLPCTTPTT TKQTTTQLPC TTPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTTKPTT TKPTTPKPCG CKSCGPGGEP CNGCAKRDAL CQDLNGVLRN LERKIRQCVC GEPQWLL // ID SGS4_DROME STANDARD; PRT; 297 AA. AC Q00725; Q9W4T2; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Salivary glue protein Sgs-4 precursor. GN SGS4 OR SGS-4 OR EG:96G10.6 OR CG12181. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, Karsnas, and Samarkand; RX MEDLINE=92223113; PubMed=1562607; RA Furia M., Digilio F.A., Artiaco D., Favia G., Polito L.C.; RT "Molecular characterization of a Drosophila melanogaster variant RT strain defective in the Sgs-4 gene dosage compensation."; RL Biochim. Biophys. Acta 1130:314-316(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: SALIVARY GLAND. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61943; CAA43949.1; -. DR EMBL; X61942; CAA43948.1; -. DR EMBL; X61944; CAA43950.1; -. DR EMBL; AL024484; CAA19673.1; -. DR EMBL; AE003427; AAF45860.1; -. DR PIR; S21085; S21085. DR FlyBase; FBgn0003374; Sgs4. KW Repeat; Signal. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 297 SALIVARY GLUE PROTEIN SGS-4. FT DOMAIN 26 178 REPEAT-RICH REGION. FT VARIANT 52 65 MISSING (IN STRAIN BERKELEY). FT VARIANT 55 55 E -> T (IN STRAINS KARSNAS AND FT SAMARKAND). FT VARIANT 58 58 R -> K (IN STRAIN SAMARKAND). FT VARIANT 58 60 RCE -> TCK (IN STRAIN KARSNAS). FT VARIANT 62 62 T -> E (IN STRAIN KARSNAS). FT VARIANT 62 62 T -> A (IN STRAIN SAMARKAND). FT VARIANT 63 63 T -> P (IN STRAINS KARSNAS AND FT SAMARKAND). FT VARIANT 65 65 K -> T (IN STRAINS KARSNAS AND FT SAMARKAND). FT VARIANT 67 67 E -> K (IN STRAIN KARSNAS). FT VARIANT 67 67 E -> R (IN STRAIN SAMARKAND). FT VARIANT 69 69 T -> E (IN STRAINS KARSNAS AND FT SAMARKAND). FT VARIANT 74 74 R -> K (IN STRAIN BERKELEY). FT VARIANT 97 97 K -> E (IN STRAINS KARSNAS AND BERKELEY). FT VARIANT 106 106 P -> A (IN STRAIN BERKELEY). FT VARIANT 109 109 R -> K (IN STRAIN BERKELEY). FT VARIANT 116 118 KTK -> RTE (IN STRAINS BERKELEY AND FT KARSNAS). FT VARIANT 119 125 MISSING (IN STRAIN SAMARKAND). FT VARIANT 130 130 K -> R (IN STRAIN BERKELEY). FT VARIANT 136 136 C -> CKTEPPTCKTEPPTCRTEPPTCKTEPPTCRTEPPTC FT KTEPPTCRTEPPTCKTEPPTC (IN STRAIN FT KARSNAS). FT VARIANT 159 159 T -> A (IN STRAIN BERKELEY). FT VARIANT 165 165 K -> R (IN STRAIN BERKELEY). FT VARIANT 177 177 C -> S (IN STRAIN BERKELEY). FT VARIANT 204 208 HHHNR -> LILPT (IN STRAIN KARSNAS). FT VARIANT 209 297 MISSING (IN STRAIN KARSNAS). FT VARIANT 247 252 PKPQAS -> SKSQASCKPA (IN STRAIN FT BERKELEY). FT VARIANT 249 249 P -> S (IN OREGON-R). FT VARIANT 252 252 S -> SCKPS (IN OREGON-R). FT VARIANT 267 267 T -> A (IN STRAINS BERKELEY AND OREGON- FT R). FT VARIANT 275 275 A -> V (IN STRAIN OREGON-R). SQ SEQUENCE 297 AA; 32309 MW; F121DDF2B177BE8C CRC64; MRLELLVVLL VGLAALAPSG STCCKTEPPR CETEPPRCET EPPRCETEPP RCETEPPRCE TTTPKCETTP PTCRTEPPTC KTEPPTCRTE PPTCKTKPPT CRTEPPTCRT EPPTCKTKPP TCKTEPPTCK TEPPTCRTEP PTCKTEPPTC RTEPPTCKTE PPTCKTEPPT CKTEPPCEKH CTKRIKRHRT KRTKRSKSTK KIVHHHNRPG TTPESGCGCG SKNESGGGGS GCILKDLLTP KCPDSKPKPQ ASPKCKSDPK PKAASKTTSK PKPKACDSGK KNTTKKPRKT QPQKGGC // ID SGS5_DROME STANDARD; PRT; 163 AA. AC P07701; Q9VEI5; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Salivary glue protein Sgs-5 precursor. GN SGS5 OR CG7596. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=87086754; PubMed=3098981; RA Shore E.M., Guild G.M.; RT "Larval salivary gland secretion proteins in Drosophila structural RT analysis of the Sgs-5 gene."; RL J. Mol. Biol. 190:149-158(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04269; CAA27820.1; -. DR EMBL; AE003718; AAF55436.1; -. DR PIR; A24504; A24504. DR FlyBase; FBgn0003375; Sgs5. KW Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 163 SALIVARY GLUE PROTEIN SGS-5. SQ SEQUENCE 163 AA; 18821 MW; 3A476F1D3B06D864 CRC64; MFNIKLLLLL LAVSWFHHGQ AVQETKIEEK PVSEPEIESE IKNSTSVPSK CNIYYRNYQW ALQDCVCRCF QNECLMQIES DQRKKEGRSP FVPVTEELCR SFICKKCSVG FPVVAEFPIP APCGCNRKPG SIATERFYSL CHLLKFSAEN SKPFLTYSYC WPF // ID SGS7_DROME STANDARD; PRT; 74 AA. AC P02841; Q9VTJ0; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Salivary glue protein Sgs-7 precursor. GN SGS7 OR CG18087. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83294545; PubMed=6411930; RA Garfinkel M.D., Pruitt R.E., Meyerowitz E.M.; RT "DNA sequences, gene regulation and modular protein evolution in the RT Drosophila 68C glue gene cluster."; RL J. Mol. Biol. 168:765-789(1983). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- DEVELOPMENTAL STAGE: PRODUCED BY THIRD-INSTAR LARVAE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01918; CAA25993.1; -. DR EMBL; AE003544; AAF50058.1; -. DR PIR; A03330; GSFF7. DR FlyBase; FBgn0003377; Sgs7. KW Signal. FT SIGNAL 1 23 FT CHAIN 24 74 SALIVARY GLUE PROTEIN SGS-7. SQ SEQUENCE 74 AA; 7919 MW; 914ACA5DB9153E29 CRC64; MKLIAVTIIA CILLIGFSDL ALGGACECQP CGPGGKACTG CPEKPQLCQQ LISDIRNLQQ KIRKCVCGEP QWMI // ID SGS8_DROME STANDARD; PRT; 75 AA. AC P02842; Q9VTI9; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Salivary glue protein Sgs-8 precursor. GN SGS8 OR CG6132. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83294545; PubMed=6411930; RA Garfinkel M.D., Pruitt R.E., Meyerowitz E.M.; RT "DNA sequences, gene regulation and modular protein evolution in the RT Drosophila 68C glue gene cluster."; RL J. Mol. Biol. 168:765-789(1983). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- DEVELOPMENTAL STAGE: PRODUCED BY THIRD-INSTAR LARVAE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01918; CAA25992.1; -. DR EMBL; AE003544; AAF50059.1; -. DR PIR; A03331; GSFF8. DR FlyBase; FBgn0003378; Sgs8. KW Signal. FT SIGNAL 1 24 FT CHAIN 25 75 SALIVARY GLUE PROTEIN SGS-8. SQ SEQUENCE 75 AA; 7917 MW; 27B818DFE158C636 CRC64; MKLLVVAVIA CIMLIGFADP ASGCKDCSCV ICGPGGEPCP GCSARVPVCK DLINIMEGLE RQVRQCACGE QVWLF // ID SH3B_DROME STANDARD; PRT; 158 AA. AC Q9NFP5; Q9VS58; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SH3 domain-binding glutamic acid-rich protein homolog (SH3BGR DE protein). GN SH3-BETA OR SH3BGR OR CG8582. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RA Scartezzini P., Egeo A., Mazzocco M.; RT "Cloning of the Drosophila Sh3bgr gene homolog of human Sh3bgr gene."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE SH3BGR FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ272505; CAB76915.1; -. DR EMBL; AE003559; AAF50570.2; -. DR EMBL; AY061162; AAL28710.1; -. DR FlyBase; FBgn0035772; Sh3-beta. DR InterPro; IPR006993; SH3BGR. DR Pfam; PF04908; SH3BGR; 1. KW SH3-binding. FT SITE 67 73 SH3-BINDING (POTENTIAL). FT CONFLICT 13 14 NK -> LL (IN REF. 1). FT CONFLICT 20 21 QQ -> HE (IN REF. 1). FT CONFLICT 64 64 D -> V (IN REF. 1). SQ SEQUENCE 158 AA; 17488 MW; 9DEF79C3D48CA463 CRC64; MVLKVYVSGM SGNKEVKKRQ QRVLMILDSK NIKYDTVDIT EPGKESEKEL MQNKSTSNGG TVSDPEPRHP LPPQLFNDDE YCGDYDAFDM ANEIDTLEVF LKLAPADTTA VSTAQIELKQ ENGDAKKEEA ETEAEDKKTE AGDGDVDVKE EAAEKAEV // ID SHAK_DROME STANDARD; PRT; 372 AA. AC P33085; Q24011; Q24520; Q26432; Q9VRB9; DT 01-OCT-1993 (Rel. 27, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Innexin shaking-B (Passover protein). GN SHAKB OR SHAK-B OR PAS OR CG1321. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM NEURAL). RC STRAIN=Oregon-R; TISSUE=Pupae; RX MEDLINE=93272337; PubMed=8500183; RA Krishnan S.N., Frei E., Swain G.P., Wyman R.J.; RT "Passover: a gene required for synaptic connectivity in the giant RT fiber system of Drosophila."; RL Cell 73:967-977(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORM LETHAL). RX MEDLINE=95199285; PubMed=7892218; RA Krishnan S.N., Frei E., Schalet A.P., Wyman R.J.; RT "Molecular basis of intracistronic complementation in the Passover RT locus of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 92:2021-2025(1995). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LETHAL). RC TISSUE=Embryo; RX MEDLINE=95324756; PubMed=7601305; RA Crompton D., Todman M., Wilkin M., Ji S., Davies J.; RT "Essential and neural transcripts from the Drosophila shaking-B locus RT are differentially expressed in the embryonic mesoderm and pupal RT nervous system."; RL Dev. Biol. 170:142-158(1995). RN [4] RP SEQUENCE FROM N.A. (ISOFORM LETHAL). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 1-122 FROM N.A. (ISOFORM LETHAL). RC STRAIN=Oregon-R; RX MEDLINE=93138414; PubMed=1487155; RA Crompton D.E., Griffin A., Davies J.A., Miklos G.L.G.; RT "Analysis of a cDNA from the neurologically active locus shaking-B RT (Passover) of Drosophila melanogaster."; RL Gene 122:385-386(1992). RN [6] RP ALTERNATIVE SPLICING. RX MEDLINE=99370093; PubMed=10440730; RA Zhang Z., Curtin K.D., Sun Y.A., Wyman R.J.; RT "Nested transcripts of gap junction gene have distinct expression RT patterns."; RL J. Neurobiol. 40:288-301(1999). RN [7] RP FUNCTION, AND SUBUNIT. RX MEDLINE=98089040; PubMed=9428764; RA Phelan P., Stebbings L.A., Baines R.A., Bacon J.P., Davies J.A., RA Ford C.; RT "Drosophila Shaking-B protein forms gap junctions in paired Xenopus RT oocytes."; RL Nature 391:181-184(1998). RN [8] RP FUNCTION. RX MEDLINE=98211899; PubMed=9552170; RA Shimohigashi M., Meinertzhagen I.A.; RT "The shaking B gene in Drosophila regulates the number of gap RT junctions between photoreceptor terminals in the lamina."; RL J. Neurobiol. 35:105-117(1998). CC -!- FUNCTION: STRUCTURAL COMPONENT OF THE GAP JUNCTIONS AT ELECTRICAL CC SYNAPSES IN DISTAL AND MID-DEPTH LEVELS IN THE LAMINA. THE LETHAL CC ISOFORM FORMS VOLTAGE SENSITIVE INTERCELLULAR CHANNELS THROUGH CC HOMOTYPIC INTERACTIONS. PASSOVER FLIES MUTANT FOR THE COMMON C- CC TERMINAL FAIL TO JUMP IN RESPONSE TO A LIGHT-OFF STIMULUS. NEURAL- CC SPECIFIC MUTATION MODIFIES GIANT FIBER SYSTEM AND GUSTATORY CC RESPONSE. CC -!- SUBUNIT: LETHAL ISOFORM IS A MONOMER. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=Lethal; CC IsoId=P33085-1; Sequence=Displayed; CC Name=Neural; CC IsoId=P33085-2; Sequence=VSP_002678, VSP_002679; CC -!- TISSUE SPECIFICITY: THE NEURAL ISOFORM IS EXPRESSED IN SYNAPSES OF CC GIANT FIBERS (GF), IN A LARGE THORACIC CELL IN LOCATION OF CC POSTSYNAPTIC TARGET AND OPTIC LOBE LAMINA AND MEDULLA. DURING CC METAMORPHOSIS, DYNAMICALLY EXPRESSED IN PUPAL NERVOUS SYSTEM. THE CC LETHAL ISOFORM IS EXPRESSED IN EMBRYONIC MESODERMAL DERIVATIVES. CC DURING METAMORPHOSIS, DYNAMICALLY EXPRESSED IN THE PUPAL NERVOUS CC SYSTEM. CC -!- SIMILARITY: BELONGS TO THE INNEXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13306; AAA28745.1; -. DR EMBL; U17330; AAC46584.1; -. DR EMBL; M98872; AAA89079.1; -. DR EMBL; AE003570; AAF50883.1; -. DR EMBL; S78495; AAB34769.1; -. DR EMBL; X65103; CAA46228.1; -. DR PIR; JN0441; JN0441. DR FlyBase; FBgn0003037; shakB. DR GO; GO:0007630; P:jump response; IMP. DR InterPro; IPR000990; Innexin. DR Pfam; PF00876; Innexin; 1. DR PRINTS; PR01262; INNEXIN. KW Gap junction; Transmembrane; Alternative splicing. FT DOMAIN 1 21 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 22 42 POTENTIAL. FT DOMAIN 43 110 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 111 131 POTENTIAL. FT DOMAIN 132 182 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 183 203 POTENTIAL. FT DOMAIN 204 267 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 268 288 POTENTIAL. FT DOMAIN 289 372 CYTOPLASMIC (POTENTIAL). FT VARSPLIC 1 58 MLDIFRGLKNLVKVSHVKTDSIVFRLHYSITVMILMSFSLI FT ITTRQYVGNPIDCVHTK -> MVSHVKIDSPVFRLHTNATV FT ILLITFSIAVTTRQYVGNPIDCVHTR (in isoform FT Neural). FT /FTId=VSP_002678. FT VARSPLIC 72 116 QSTYTLKSLFLKKQGVSVPYPGIGNSDGDPADKKHYKYYQW FT VCFC -> HSTYTVVDAFMKKQGSEVPFPGVHNSQGRGPLT FT IKHTKYYQWVAFT (in isoform Neural). FT /FTId=VSP_002679. FT CONFLICT 121 121 A -> P (IN REF. 5). FT CONFLICT 232 232 I -> M (IN REF. 1). FT CONFLICT 247 249 SGE -> GEV (IN REF. 2). SQ SEQUENCE 372 AA; 44355 MW; 3DD1049D8F1D4481 CRC64; MLDIFRGLKN LVKVSHVKTD SIVFRLHYSI TVMILMSFSL IITTRQYVGN PIDCVHTKDI PEDVLNTYCW IQSTYTLKSL FLKKQGVSVP YPGIGNSDGD PADKKHYKYY QWVCFCLFFQ AILFYTPRWL WKSWEGGKIH ALIMDLDIGI CSEAEKKQKK KLLLDYLWEN LRYHNWWAYR YYVCELLALI NVIGQMFLMN RFFDGEFITF GLKVIDYMET DQEDRMDPMI YIFPRMTKCT FFKYGSSGEV EKHDAICILP LNVVNEKIYI FLWFWFILLT FLTLLTLIYR VVIIFSPRMR VYLFRMRFRL VRRDAIEIIV RRSKMGDWFL LYLLGENIDT VIFRDVVQDL ANRLGHNQHH RVPGLKGEIQ DA // ID SHRK_DROME STANDARD; PRT; 939 AA. AC Q24145; Q26299; Q9V7K5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase shark (EC 2.7.1.112). GN SHARK OR TK7 OR CG18247. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=95199263; PubMed=7892198; RA Ferrante A.W. Jr., Reinke R., Stanley E.R.; RT "Shark, a Src homology 2, ankyrin repeat, tyrosine kinase, is RT expressed on the apical surfaces of ectodermal epithelia."; RL Proc. Natl. Acad. Sci. U.S.A. 92:1911-1915(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 793-849 FROM N.A. RX MEDLINE=92008631; PubMed=1915852; RA Shishido E., Emori Y., Saigo K.; RT "Identification of seven novel protein-tyrosine kinase genes of RT Drosophila by the polymerase chain reaction."; RL FEBS Lett. 289:235-238(1991). CC -!- FUNCTION: MAY BE INVOLVED IN SIGNAL TRANSDUCTION ON THE APICAL CC SURFACE OF ECTODERMAL EPITHELIA REGULATING THEIR POLARITY DURING CC INVAGINATION. CRUMBS (CRB) MAY BE THE INTRACELLULAR SIGNAL. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. APICAL EXPRESSION IN CEPHALIC CC FURROW AND TRACHEAL CELLS; LIMITED TO LUMINAL SURFACE AND ABSENT CC FROM THE BASAL SURFACE. CC -!- TISSUE SPECIFICITY: GASTRULATION EMBRYOS SHOW EXPRESSION IN CC ECTODERMAL CELLS ALONG THE CEPHALIC FURRROW AND VENTRAL MIDLINE. CC PROCTODEUM, STOMODEUM AND THEIR DERIVED STRUCTURES (FOREGUT, CC ATRIUM, PHARYNX, ESOPHAGUS AND HINDGUT) CONTINUE TO SHOW CC EXPRESSION FROM STAGE 8-9 TO LATE EMBRYOS. OTHER ECTODERMALLY CC DERIVED STRUCTURES (FRONTAL SAC, SALIVARY GLAND AND LABIUM) AND CC DEVELOPING TRACHEAL SYSTEM ALSO SHOW EXPRESSION. CC -!- DEVELOPMENTAL STAGE: EMBRYOS ONLY. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. CC -!- SIMILARITY: CONTAINS 2 SH2 DOMAINS. CC -!- SIMILARITY: CONTAINS 3 ANK REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37773; AAA79851.1; -. DR EMBL; AE003808; AAF58044.1; -. DR EMBL; AY051937; AAK93361.1; -. DR EMBL; S55982; AAB19909.1; -. DR PIR; S18015; S18015. DR HSSP; P08631; 1AD5. DR FlyBase; FBgn0015295; shark. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kina...; NAS. DR GO; GO:0007242; P:intracellular signaling cascade; IEP. DR GO; GO:0007254; P:JNK cascade; NAS. DR GO; GO:0045199; P:maintenance of epithelial cell polarity; IEP. DR InterPro; IPR002110; ANK. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000980; SH2. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00023; ank; 4. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00017; SH2; 2. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000093; SH2; 2. DR SMART; SM00248; ANK; 3. DR SMART; SM00252; SH2; 2. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50088; ANK_REPEAT; 3. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 2. KW Transferase; Tyrosine-protein kinase; ATP-binding; Phosphorylation; KW SH2 domain; ANK repeat; Repeat. FT DOMAIN 10 106 SH2 1. FT REPEAT 153 185 ANK 1. FT REPEAT 186 218 ANK 2. FT REPEAT 220 252 ANK 3. FT DOMAIN 288 403 SH2 2. FT DOMAIN 662 921 PROTEIN KINASE. FT NP_BIND 668 676 ATP (BY SIMILARITY). FT BINDING 698 698 ATP (BY SIMILARITY). FT ACT_SITE 789 789 BY SIMILARITY. FT MOD_RES 927 927 PHOSPHORYLATION (POTENTIAL). FT CONFLICT 19 19 A -> V (IN REF. 1). FT CONFLICT 39 39 S -> R (IN REF. 1). FT CONFLICT 50 50 L -> F (IN REF. 1). FT CONFLICT 85 85 D -> E (IN REF. 1). FT CONFLICT 129 129 S -> T (IN REF. 1). FT CONFLICT 199 199 P -> T (IN REF. 1). FT CONFLICT 341 341 C -> S (IN REF. 1). FT CONFLICT 505 506 GT -> RA (IN REF. 1). FT CONFLICT 597 597 M -> V (IN REF. 1). FT CONFLICT 611 611 A -> P (IN REF. 1). FT CONFLICT 732 732 A -> S (IN REF. 1). FT CONFLICT 898 898 A -> P (IN REF. 1). FT CONFLICT 935 939 QTVHI -> KRFTFNPVSIFHFFRC (IN REF. FT 1). SQ SEQUENCE 939 AA; 104272 MW; 37CC2C3DA25D3F52 CRC64; MSRDSDPMKW YHGNLSREAA DELLKQGYED GTFLVRESST AAGDFVLSLL CQGEVCHYQV RRHGGEDAFF SIDDKVQTKI LHGLDTLVDY YQQAANGLPT KLTVPLIRDL PPHNTRSHGV TNLLHRATSK NESKVVFELL KCGYRNFDAK NQDGQTALHL AALHSDEDIL KHLLNAKVQV NSSDSFGCQP LHYAARSKPA SFIRTLISAQ ANVQGRNIDN GYVPLHEAAK HGNLEAVQEL LLAEAPPLPR TSSGEFPFDL AKEAGQTAVE EFLLNYKLPP ANTTRDQWYH GTLTREEAVA ILKKHAKELL AKQPEVDTSG CFLVRYSESP AASGLVLTLL CDQVVKNFRI SQADLYQNGN KVQSGGSKFL YIDDGPYWPS VEHLIAHFMR FSYGLPVSLK YPVPPQPKPE VPSFATIPRS NMKPKAASPA TPPTPVSPHS HHQHPHVPAL TITKKKQKEN SSSMFNTLRL TSPKKALFDM NSLRKNKSKG KRSDSESSVS GSLAGTEQEL QAAAPMLKSL SFSTEFSTFN ADGVTGSGAA AAGEVYNVPR NNTPIEIDLP PIAQKTEAEV EYFTKSDVAI ERERAGQWIG NGYQPTMDVL SLLDQQIKAP AVARLNSLGP NASTESEMAS YLHRKCSGTP STPSATEVEA AKLRFFIEPE KLVLDREIGH GEFGSVHSGW LLRKSGAGEE SRLEVAIKML SDEHSNKQEF LREASVMMRL EHKCIVRLIG IAKGEMLMMV QELAPLGSML QYILDHGHEI TANAELKVWA SQIACGMHYL ESQHFVHRDL AARNILLTAR HQAKISDFGM SRSLRPGSTE YQFTQGGRWP IRWYAPESFN LGIFSHASDV WSFGVTIWEM FSLGAPPYGE ISNVDAIKLV DSGERLPQPN LCPAYIYAVM QSCWKERPKD RPTFVYLTEF FARDPDYQNL PELVQTVHI // ID SIF1_DROME STANDARD; PRT; 2064 AA. AC P91621; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Still life protein type 1 (SIF type 1). GN SIF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=97153054; PubMed=8999801; RA Sone M., Hoshino M., Suzuki E., Kuroda S., Kaibuchi K., Nakagoshi H., RA Saigo K., Nabeshima Y.-I., Hama C.; RT "Still life, a protein in synaptic terminals of Drosophila homologous RT to GDP-GTP exchangers."; RL Science 275:543-547(1997). RN [2] RP ERRATUM. RA Sone M., Hoshino M., Suzuki E., Kuroda S., Kaibuchi K., Nakagoshi H., RA Saigo K., Nabeshima Y.-I., Hama C.; RL Science 275:1405-1405(1997). CC -!- FUNCTION: REGULATES SYNAPTIC DIFFERENTIATION THROUGH THE CC ORGANIZATION OF ACTIN CYTOSKELETON POSSIBLY BY ACTIVATING RHO-LIKE CC GTPASES. IS LIKELY A FACTOR IN THE CASCADE OF RAC1 OR CDC42 IN THE CC NEURONS. CC -!- SUBCELLULAR LOCATION: LOCALIZES TO THE SUBMEMBRANOUS REGION OF CC SYNAPTIC TERMINALS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=SIF type 1; CC IsoId=P91621-1; Sequence=Displayed; CC Name=SIF type 2; CC IsoId=P91620-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: AT STAGE 14, EXPRESSION OCCURS IN EACH CC SEGMENT OF THE CENTRAL NERVOUS SYSTEM. AT STAGE 17, EXPRESSION CC BECOMES RESTRICTED TO THE SYNAPTIC REGIONS OF THE BRAIN AND CC VENTRAL NERVE CORD, WHERE SYNAPSES UNDERGO MATURATION. CC -!- SIMILARITY: CONTAINS 1 DBL-HOMOLOGY (DH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PDZ/DHR DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PH DOMAINS. CC -!- SIMILARITY: CONTAINS 1 RAS-BINDING (RBD) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D86547; BAA13109.1; -. DR PIR; T13707; T13707. DR HSSP; P08567; 1PLS. DR FlyBase; FBgn0019652; sif. DR InterPro; IPR001331; GDS_CDC24. DR InterPro; IPR001478; PDZ. DR InterPro; IPR001849; PH. DR InterPro; IPR003116; RBD. DR InterPro; IPR000219; RhoGEF. DR InterPro; IPR001960; WH1. DR Pfam; PF00169; PH; 1. DR Pfam; PF02196; RBD; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00233; PH; 2. DR SMART; SM00455; RBD; 1. DR SMART; SM00325; RhoGEF; 1. DR SMART; SM00461; WH1; 1. DR PROSITE; PS00741; DH_1; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50898; RBD; 1. KW Guanine-nucleotide releasing factor; Developmental protein; Repeat; KW Myristate; Synapse; Alternative splicing; Lipoprotein. FT DOMAIN 839 957 PH 1. FT DOMAIN 1121 1188 RAS-BINDING. FT DOMAIN 1204 1293 PDZ. FT DOMAIN 1428 1622 DH. FT DOMAIN 1694 1787 PH 2. FT DOMAIN 445 453 POLY-GLY. FT DOMAIN 545 548 POLY-GLN. FT DOMAIN 1315 1318 POLY-PRO. FT DOMAIN 1918 1929 POLY-GLN. FT DOMAIN 1949 1953 POLY-PRO. FT LIPID 2 2 N-myristoyl glycine (Potential). SQ SEQUENCE 2064 AA; 230489 MW; D3BDCC10A94D9E6C CRC64; MGNKLSCSCA PLMRKAYRYE DSPWQSSRRR DGHLLSSFRL WAEVFHVSAS GAGTVKWQQV SEDLVPVNIT CIQDSPECIF HITAYNSQVD KILDVRLVQP GTRIGQASEC FVYWKDPMTN DTWGLNFTSP IDAKQFRECC SPSFKFSRKA SSSYSLKLDP PGKGKVKAKR KPLSTPASPS RVRQEPQCTC MSAEQYARLR TDPRVRGSST LPRNVGSHRI TDVDGQQQVG SGKVVSAVSS TSLYDNVASG GPGTNQGADT LPRQMKGGQQ DRQDVANSGV NTNTPGVIVT GVGNVGSDMC GQNHVGSQVG NDDPAACQMV MDLSKSEGTQ AGGGLHQSVG TCTSSSKGTG TRNKDFGDDM TRDAHSHDMH QHNVINNNTR RKTKSTEDMN VDTSTLKRML KPMPSTESPV TSPEMGRRRY NYYNANAAQT LGHPPHMHQH GMAMGMGGGG GGGHHIMNNN TMGRASSQSS RFSGSRSSHE IGRGYPPRNL YLELERERSC IEGSPPSDNV MFDNQCYATT PSSSNGNSDQ DQSYGQQQSS GQHPQQQQGP PQRSSRHQHH HQQAPNVTPT PGSPTSRLLL EYEMHLRNTL AKGMDAESYS LHTFEALLSQ SMENLANAKS STLPLPPHRP LSTIRDKERD RDRDGYYSDR NELIRERERE RDRGYLSDHN SSFSNSRCAS CIGESARAQW FRHSDGWRSG SSTIGSGSGH GMMTQQIPGS GHKRSPWDSL PSLRQDSSLN DSGYKSARAD SLEQRAEFIR QDSLRSEYLS DRESRYGIVQ QASIESTDSR MCYLTSSEIS DDDRMSLTTA VSDEDDGESV MASPYKAKAT GTAASSFNCT GAVRKAGFLS VKKWLLRKKH QIELARKRGW KGYWVCLKGT TLLFYPCDSR EGRSVEAAPK HLIIVDGAIM QPIPEHPKRD YIFCLSTAFG DAYLFQAPCQ VELENWVNSI HSACAAAFAR HRGKTGTLHL LQEEIFRLEK AIESDHKLKH MAELQQSVVT DQETRHQIQT QILQWEENLE RLHCEQFRLR CYMASLQSGE LPNPKSLLTH VSRPTKNTLN KLGVFTVSSF HAFICARSPS LLNNLLAGRG ATKRRPPMLS RSNSGSSRRS MQMNSRDEPE KTFKVAMPDN AYSTVYLRDA MSVEEFLASA CARRNLNPME HFVRVKKRRD MEDHNYFVPH RNDLIENYLH NHEFVEVCMK ILYQVELQRT TLEQMWGFSV EAELIENAER QDELCCYVSR VEDKSVAMHN GIIKGDEIMV INGAIVSDLD MMYLESVLQE EQSLSMMMRS SRTEPPDLVG IMRVTDDMID SLVCPPPPTD PPVMSEEMIT GLIVPAPGWN GTSKDLYSPE AESSPATSFV DPAAMAAQLA VGGLGVAKPT SRTSSFEIEN LLKTAEQETR KSSPTGSVTS SVSTTALTPS RQLTDAEKLR KVVMELVDTE RTYVKHLNNL LEHYLEPMKR ETFLSNAEIN ALFGNIHEIV TFQRQFLQNL EESLDLEPDF NKFEHCGQFR NVLFAIGSAF LYYVNHFKLY SSFCASHSKA QKVLHPNEGN HALQEFLAAR NPKQQHSSTL ESYLIKPIQR ILKYPLLLQQ MRNLTDTRAD EHVHLCEALK GMEKVAEHIN EMQRIHEEYG AIFDHLFRQH QKSCKQPIDL SPGDLLYYGG VEWLNISDFL GKIKKGLELH AMCFVFKSAV VFLCKERLRQ KKKLMGVSSK NATNEVEIIR YQVLIPVTEV QVRASSAKDM DSHFLWELIH LRSQLQRRSE KVYVLSNSTA DFRNAFLKTI RQIIRESVRN MSIPMKNFGG SSGSVSGHSS QGMGSMGYPG NSQTLERPKQ QITIVHGSHT LGKPKKKSGS QRHSAGNIDY DNLSGSQEAD DLPPSVGVVH YASGHTHGQQ MQPAGFRGRS KTVGDVTEIT CSSPEPHQQQ QQQQQQQQQL MQQGHAHAHP HPHPHPREPP PPPIRQPHLH HHSSDIERID PGTKSEGEED SQQGTIRPKA TLGRTPNHLT LSTTSTLSVG STGSQARLIQ SSHPPASYQP VLMKDLGSPV WKPRDMINLG TDPQSTTRKD DVKN // ID SIF2_DROME STANDARD; PRT; 2044 AA. AC P91620; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Still life protein type 2 (SIF type 2). GN SIF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=97153054; PubMed=8999801; RA Sone M., Hoshino M., Suzuki E., Kuroda S., Kaibuchi K., Nakagoshi H., RA Saigo K., Nabeshima Y.-I., Hama C.; RT "Still life, a protein in synaptic terminals of Drosophila homologous RT to GDP-GTP exchangers."; RL Science 275:543-547(1997). RN [2] RP ERRATUM. RA Sone M., Hoshino M., Suzuki E., Kuroda S., Kaibuchi K., Nakagoshi H., RA Saigo K., Nabeshima Y.-I., Hama C.; RL Science 275:1405-1405(1997). CC -!- FUNCTION: REGULATES SYNAPTIC DIFFERENTIATION THROUGH THE CC ORGANIZATION OF ACTIN CYTOSKELETON POSSIBLY BY ACTIVATING RHO-LIKE CC GTPASES. IS LIKELY A FACTOR IN THE CASCADE OF RAC1 OR CDC42 IN THE CC NEURONS. CC -!- SUBCELLULAR LOCATION: LOCALIZES TO THE SUBMEMBRANOUS REGION OF CC SYNAPTIC TERMINALS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=SIF type 2; CC IsoId=P91620-1; Sequence=Displayed; CC Name=SIF type 1; CC IsoId=P91621-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: AT STAGE 14, EXPRESSION OCCURS IN EACH CC SEGMENT OF THE CENTRAL NERVOUS SYSTEM. AT STAGE 17, EXPRESSION CC BECOMES RESTRICTED TO THE SYNAPTIC REGIONS OF THE BRAIN AND CC VENTRAL NERVE CORD, WHERE SYNAPSES UNDERGO MATURATION. CC -!- SIMILARITY: CONTAINS 1 DBL-HOMOLOGY (DH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PDZ/DHR DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PH DOMAINS. CC -!- SIMILARITY: CONTAINS 1 RAS-BINDING (RBD) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D86546; BAA13108.1; -. DR PIR; T13704; T13704. DR HSSP; P08567; 1PLS. DR FlyBase; FBgn0019652; sif. DR InterPro; IPR001331; GDS_CDC24. DR InterPro; IPR001478; PDZ. DR InterPro; IPR001849; PH. DR InterPro; IPR003116; RBD. DR InterPro; IPR000219; RhoGEF. DR Pfam; PF00169; PH; 1. DR Pfam; PF02196; RBD; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00233; PH; 2. DR SMART; SM00455; RBD; 1. DR SMART; SM00325; RhoGEF; 1. DR PROSITE; PS00741; DH_1; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50898; RBD; 1. KW Guanine-nucleotide releasing factor; Developmental protein; Synapse; KW Repeat; Alternative splicing. FT DOMAIN 62 249 4 X 25 AA APPROXIMATE REPEAT. FT REPEAT 62 86 1. FT REPEAT 94 118 2. FT REPEAT 154 178 3. FT REPEAT 225 249 4. FT DOMAIN 819 937 PH 1. FT DOMAIN 1101 1168 RAS-BINDING. FT DOMAIN 1184 1273 PDZ. FT DOMAIN 1408 1602 DH. FT DOMAIN 1674 1767 PH 2. FT DOMAIN 467 470 POLY-PRO. FT DOMAIN 646 649 POLY-ARG. FT DOMAIN 1295 1298 POLY-PRO. FT DOMAIN 1898 1909 POLY-GLN. FT DOMAIN 1929 1933 POLY-PRO. SQ SEQUENCE 2044 AA; 228324 MW; 75D7CF21F49654B6 CRC64; MEQKCIRRKG SVRLTEPTGH AHVRIEQRPQ LPPRRQKSAE EVATMPKSAL RQPPEQLEWF DRRAQQRHSA RSAEGGQVRE ETMEWLKLQK TASPIQPVRT SSGPSEITVL KDELPDWLLD HLPRKKERER DRLPSDADKA VGSAYAKALA DLLKKPLSRQ GSGPCEFSLL KTDIVEWLTK MQSSSGTDRG KSRRSHHRRN GSGGDAQPRS NSQEDAQDQS KTSHRKRHSL GHSGAVSEEE QQQLTADWIA YPLHKLQSLG KQPPPAQPPE RMSIPSGYAV PSALSHTPLC QRREERSRER RLRHSASEVV GSGGAGAAST SNNAHLERLY AKPHKERYQY VPKTKESSGR KERSRRHQTQ RSATVSDMSA QRSGGHKRKS SSAERAPRSP SPGPCTDPDC PLLPICTDPH CRYQECQARQ CITSSVSSVN LARHQQLAQV QLHAVPAHLV GAIGSDVPTT PSTTATPPPP TGGGTMGVGA TGAGAGATSE RRLVICHDCR SCAPLLSCRN RKCLNAAKCN SLPRCAADFN RLRTQLSQPP TTLDDIEPAP LDDLEMQPLP SPPHPHPHHH YRSNSQPNTL QRGDSASSAG MGAGVGGAGH GGLGGPGSGL AWLEPTTTLV QPLPAYVHHS NGKLMKSASA ASLNSRRRRH KTVHFGENLL REVCQNRKLI KTEAQVPSGS APMKANIQML YNFVEGVLSA WVDDDEDQVR SGAESEPEHG VVPMQPIHRC NRLRYQCIRR VVEEAADLQG TLKLGNSRYR HRHWRSTAKQ CNEMFLRKIS DDDRMSLTTA VSDEDDGESV MASPYKAKAT GTAASSFNCT GAVRKAGFLS VKKWLLRKKH QIELARKRGW KGYWVCLKGT TLLFYPCDSR EGRSVEAAPK HLIIVDGAIM QPIPEHPKRD YIFCLSTAFG DAYLFQAPCQ VELENWVNSI HSACAAAFAR HRGKTGTLHL LQEEIFRLEK AIESDHKLKH MAELQQSVVT DQETRHQIQT QILQWEENLE RLHCEQFRLR CYMASLQSGE LPNPKSLLTH VSRPTKNTLN KLGVFTVSSF HAFICARSPS LLNNLLAGRG ATKRRPPMLS RSNSGSSRRS MQMNSRDEPE KTFKVAMPDN AYSTVYLRDA MSVEEFLASA CARRNLNPME HFVRVKKRRD MEDHNYFVPH RNDLIENYLH NHEFVEVCMK ILYQVELQRT TLEQMWGFSV EAELIENAER QDELCCYVSR VEDKSVAMHN GIIKGDEIMV INGAIVSDLD MMYLESVLQE EQSLSMMMRS SRTEPPDLVG IMRVTDDMID SLVCPPPPTD PPVMSEEMIT GLIVPAPGWN GTSKDLYSPE AESSPATSFV DPAAMAAQLA VGGLGVAKPT SRTSSFEIEN LLKTAEQETR KSSPTGSVTS SVSTTALTPS RQLTDAEKLR KVVMELVDTE RTYVKHLNNL LEHYLEPMKR ETFLSNAEIN ALFGNIHEIV TFQRQFLQNL EESLDLEPDF NKFEHCGQFR NVLFAIGSAF LYYVNHFKLY SSFCASHSKA QKVLHPNEGN HALQEFLAAR NPKQQHSSTL ESYLIKPIQR ILKYPLLLQQ MRNLTDTRAD EHVHLCEALK GMEKVAEHIN EMQRIHEEYG AIFDHLFRQH QKSCKQPIDL SPGDLLYYGG VEWLNISDFL GKIKKGLELH AMCFVFKSAV VFLCKERLRQ KKKLMGVSSK NATNEVEIIR YQVLIPVTEV QVRASSAKDM DSHFLWELIH LRSQLQRRSE KVYVLSNSTA DFRNAFLKTI RQIIRESVRN MSIPMKNFGG SSGSVSGHSS QGMGSMGYPG NSQTLERPKQ QITIVHGSHT LGKPKKKSGS QRHSAGNIDY DNLSGSQEAD DLPPSVGVVH YASGHTHGQQ MQPAGFRGRS KTVGDVTEIT CSSPEPHQQQ QQQQQQQQQL MQQGHAHAHP HPHPHPREPP PPPIRQPHLH HHSSDIERID PGTKSEGEED SQQGTIRPKA TLGRTPNHLT LSTTSTLSVG STGSQARLIQ SSHPPASYQP VLMKDLGSPV WKPRDMINLG TDPQSTTRKD DVKN // ID SIMA_DROME STANDARD; PRT; 1507 AA. AC Q24167; Q9VAA5; DT 15-DEC-1998 (Rel. 37, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Similar protein. GN SIMA OR CG7951. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96269413; PubMed=8682312; RA Nambu J.R., Chen W., Hu S., Crews S.T.; RT "The Drosophila melanogaster similar bHLH-PAS gene encodes a protein RT related to human hypoxia-inducible factor 1 alpha and Drosophila RT single-minded."; RL Gene 172:249-254(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: POSSIBLE DNA-BINDING TRANSCRIPTIONAL ACTIVATOR. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED IN THE EMBRYO. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PAS (PER-ARNT-SIM) DIMERIZATION DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PAS-ASSOCIATED C-TERMINAL (PAC) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U43090; AAC47303.1; -. DR EMBL; AE003772; AAF57008.2; -. DR PIR; JC4851; JC4851. DR FlyBase; FBgn0015542; sima. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS_domain. DR Pfam; PF00785; PAC; 1. DR Pfam; PF00989; PAS; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR PROSITE; PS50888; HLH; FALSE_NEG. DR PROSITE; PS50112; PAS; 2. KW Repeat; DNA-binding; Nuclear protein; Transcription regulation; KW Activator; Coiled coil. FT DNA_BIND 72 85 BASIC DOMAIN. FT DOMAIN 86 126 HELIX-LOOP-HELIX MOTIF (BY SIMILARITY). FT DOMAIN 167 240 PAS 1. FT DOMAIN 307 377 PAS 2. FT DOMAIN 381 422 PAC. FT DOMAIN 577 587 PRO-RICH. FT DOMAIN 880 908 COILED COIL (POTENTIAL). FT DOMAIN 982 1054 COILED COIL (POTENTIAL). FT DOMAIN 1110 1162 COILED COIL (POTENTIAL). FT DOMAIN 26 39 POLY-SER. FT DOMAIN 718 725 POLY-SER. FT DOMAIN 759 763 POLY-GLN. FT DOMAIN 767 776 POLY-GLN. FT DOMAIN 907 918 POLY-GLN. FT DOMAIN 945 948 POLY-GLN. FT DOMAIN 990 998 POLY-GLN. FT DOMAIN 1020 1038 POLY-GLN. FT DOMAIN 1113 1126 POLY-GLN. FT DOMAIN 1146 1162 POLY-GLN. FT DOMAIN 1205 1208 POLY-GLN. FT DOMAIN 1277 1284 POLY-GLN. FT DOMAIN 1298 1301 POLY-ASP. FT CONFLICT 38 38 S -> A (IN REF. 1). FT CONFLICT 345 345 S -> L (IN REF. 1). FT CONFLICT 492 492 A -> V (IN REF. 1). FT CONFLICT 588 588 T -> I (IN REF. 1). FT CONFLICT 709 709 T -> K (IN REF. 1). FT CONFLICT 776 776 Q -> QQQQ (IN REF. 1). FT CONFLICT 895 895 Q -> QQ (IN REF. 1). FT CONFLICT 902 902 G -> S (IN REF. 1). FT CONFLICT 982 982 A -> T (IN REF. 1). FT CONFLICT 1125 1126 MISSING (IN REF. 1). FT CONFLICT 1154 1157 MISSING (IN REF. 1). FT CONFLICT 1444 1444 F -> L (IN REF. 1). FT CONFLICT 1447 1447 G -> C (IN REF. 1). FT CONFLICT 1451 1451 S -> N (IN REF. 1). FT CONFLICT 1494 1494 D -> G (IN REF. 1). SQ SEQUENCE 1507 AA; 165824 MW; 4102939C8FBFB0C6 CRC64; MVSLIDTIEA AAEKQKQSQA VVTNTSASSS SCSSSFSSSP PSSSVGSPSP GAPKTNLTAS GKPKEKRRNN EKRKEKSRDA ARCRRSKETE IFMELSAALP LKTDDVNQLD KASVMRITIA FLKIREMLQF VPSLRDCNDD IKQDIETAED QQEVKPKLEV GTEDWLNGAE ARELLKQTMD GFLLVLSHEG DITYVSENVV EYLGITKIDT LGQQIWEYSH QCDHAEIKEA LSLKRELAQK VKDEPQQNSG VSTHHRDLFV RLKCTLTSRG RSINIKSASY KVIHITGHLV VNAKGERLLM AIGRPIPHPS NIEIPLGTST FLTKHSLDMR FTYVDDKMHD LLGYSPKDLL DTSLFSCQHG ADSERLMATF KSVLSKGQGE TSRYRFLGKY GGYCWILSQA TIVYDKLKPQ SVVCVNYVIS NLENKHEIYS LAQQTAASEQ KEQHHQAAET EKEPEKAADP EIIAQETKET VNTPIHTSEL QAKPLQLESE KAEKTIEETK TIATIPPVTA TSTADQIKQL PESNPYKQIL QAELLIKREN HSPGPRTITA QLLSGSSSGL RPEEKRPKSV TASVLRPSPA PPLTPPPTAV LCKKTPLGVE PNLPPTTTAT AAIISSSNQQ LQIAQQTQLQ NPQQPAQDMS KGFCSLFADD GRGLTMLKEE PDDLSHHLAS TNCIQLDEMT PFSDMLVGLM GTCLLPEDIN SLDSTTCSTT ASGQHYQSPS SSSTSAPSNT SSSNNSYANS PLSPLTPNST ATASNPSHQQ QQQHHNQQQQ QQQQQQHHPQ HHDNSNSSSN IDPLFNYREE SNDTSCSQHL HSPSITSKSP EDSSLPSLCS PNSLTQEDDF SFEAFAMRAP YIPIDDDMPL LTETDLMWCP PEDLQTMVPK EIDAIQQQLQ QLQQQHHQQY AGNTGYQQQQ QQPQLQQQHF SNSLCSSPAS TVSSLSPSPV QQHHQQQQAA VFTSDSSELA ALLCGSGNGT LSILAGSGVT VAEECNERLQ QHQQQQQQTS GNEFRTFQQL QQELQLQEEQ QQRQQQQQQQ QQQQQQQQLL SLNIECKKEK YDVQMGGSLC HPMEDAFEND YSKDSANLDC WDLIQMQVVD TEPVSPNAAS PTPCKVSAIQ LLQQQQQLQQ QQQQQQNIIL NAVPLITIQN NKELMQQQQQ QQQQQQQEQL QQPAIKLLNG ASIAPVNTKA TIRLVESKPP TTTQSRMAKV NLVPQQQQHG NKRHLNSATG AGNPVESKRL KSGTLCLDVQ SPQLLQQLIG KDPAQQQTQA AKRAGSERWQ LSAESKQQKQ QQQQSNSVLK NLLVSGRDDD DSEAMIIDED NSLVQPIPLG KYGLPLHCHT STSSVLRDYH NNPLISGTNF QLSPVFGGSD SSGGDGETGS VVSLDDSVPP GLTACDTDAS SDSGIDENSL MDGASGSPRK RLSSTSNSTN QAESAPPALD VETPVTQKSV EEEFEGGGSG SNAPSRKTSI SFLDSSNPLL HTPAMMDLVN DDYIMGEGGF EFSDNQLEQV LGWPEIA // ID SIM_DROME STANDARD; PRT; 697 AA. AC P05709; O96521; Q8MQI7; Q9VFZ3; DT 01-NOV-1988 (Rel. 09, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Single-minded protein. GN SIM OR CG7771. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99054545; PubMed=9840810; RA Kasai Y., Stahl S., Crews S.; RT "Specification of the Drosophila CNS midline cell lineage: direct RT control of single-minded transcription by dorsal/ventral patterning RT genes."; RL Gene Expr. 7:171-189(1998). RN [2] RP SEQUENCE FROM N.A. (ALLELE SIM-J1-47), FUNCTION, TISSUE SPECIFICITY, RP AND MUTAGENESIS OF SER-65. RX MEDLINE=22209202; PubMed=12221007; RA Pielage J., Steffes G., Lau D.C., Parente B.A., Crews S.T., RA Strauss R., Klambt C.; RT "Novel behavioral and developmental defects associated with Drosophila RT single-minded."; RL Dev. Biol. 249:283-299(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 25-42 FROM N.A., AND SIMILARITY TO HLH PROTEINS. RX MEDLINE=92103681; PubMed=1760843; RA Nambu J.R., Lewis J.O., Wharton K.A. Jr., Crews S.T.; RT "The Drosophila single-minded gene encodes a helix-loop-helix protein RT that acts as a master regulator of CNS midline development."; RL Cell 67:1157-1167(1991). RN [7] RP SEQUENCE OF 43-697 FROM N.A. RX MEDLINE=88151023; PubMed=3345560; RA Crews S.T., Thomas J.B., Goodman C.S.; RT "The Drosophila single-minded gene encodes a nuclear protein with RT sequence similarity to the per gene product."; RL Cell 52:143-151(1988). CC -!- FUNCTION: TRANSCRIPTION FACTOR THAT FUNCTIONS AS A MASTER CC DEVELOPMENTAL REGULATOR CONTROLLING MIDLINE DEVELOPMENT OF THE CC VENTRAL NERVE CORD. REQUIRED TO CORRECTLY SPECIFY THE FORMATION OF CC THE CENTRAL BRAIN COMPLEX, WHICH CONTROLS WALKING BEHAVIOR. ALSO CC REQUIRED FOR CORRECT PATTERNING OF THE EMBRYONIC GENITAL DISK AND CC ANAL PAD ANLAGE. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: EMBRYONIC NERVE CORD. CC -!- POLYMORPHISM: BERKELEY STRAIN HAS 11 A-A-Q REPEATS. CC -!- MISCELLANEOUS: MUTATIONS RESULT IN THE LOSS OF THE PRECURSOR CELLS CC THAT GIVE RISE TO MIDLINE CELLS OF THE EMBRYONIC CENTRAL NERVOUS CC SYSTEM. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PAS (PER-ARNT-SIM) DIMERIZATION DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PAS-ASSOCIATED C-TERMINAL (PAC) DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF071934; AAC64519.1; ALT_SEQ. DR EMBL; AE003698; AAF54902.3; -. DR EMBL; AY129457; AAM76199.1; -. DR EMBL; M19020; AAA28900.1; -. DR PIR; A29945; A29945. DR TRANSFAC; T00750; -. DR FlyBase; FBgn0004666; sim. DR GO; GO:0005634; C:nucleus; IEP. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; NAS. DR GO; GO:0007628; P:adult walking behavior; IMP. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR GO; GO:0007418; P:ventral midline development; IMP. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR001067; Nuc_translocat. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS_domain. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00785; PAC; 1. DR Pfam; PF00989; PAS; 1. DR PRINTS; PR00785; NCTRNSLOCATR. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR PROSITE; PS50888; HLH; 1. DR PROSITE; PS50112; PAS; 2. KW Developmental protein; Neurogenesis; Nuclear protein; Repeat; KW Transcription regulation; DNA-binding. FT DNA_BIND 21 37 BASIC DOMAIN. FT DOMAIN 38 78 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 100 172 PAS 1. FT DOMAIN 266 336 PAS 2. FT DOMAIN 406 446 14 X 3 AA REPEATS OF A-A-Q (APPROXIMATE). FT DOMAIN 553 672 SER-RICH. FT DOMAIN 673 693 GLN/HIS-RICH. FT VARIANT 406 414 MISSING (IN STRAIN BERKELEY). FT MUTAGEN 65 65 S->F: IN ALLELE SIM-J1-47; TEMPERATURE FT SENSITIVE EMBRYONIC MIDLINE AXON FT PHENOTYPE. FT CONFLICT 151 151 I -> Y (IN REF. 1). SQ SEQUENCE 697 AA; 76475 MW; 588414A4A17101AD CRC64; MTNHRRVRKD CYESRLHDIA KTCAMKEKSK NAARTRREKE NTEFCELAKL LPLPAAITSQ LDKASVIRLT TSYLKMRQVF PDGLGEAWGS SPAMQRGATI KELGSHLLQT LDGFIFVVAP DGKIMYISET ASVHLGLSQV ELTGNSIFEY IHNYDQDEMN AILSLHPHIN QHPLAQTHTP IGSPNGVQHP SAYDHDRGSH TIEIEKTFFL RMKCVLAKRN AGLTTSGFKV IHCSGYLKAR IYPDRGDGQG SLIQNLGLVA VGHSLPSSAI TEIKLHQNMF MFRAKLDMKL IFFDARVSQL TGYEPQDLIE KTLYQYIHAA DIMAMRCSHQ ILLYKGQVTT KYYRFLTKGG GWVWVQSYAT LVHNSRSSRE VFIVSVNYVL SEREVKDLVL NEIQTGVVKR EPISPAAQAA QAAQAAQAAQ AAQAAQAAQA AQAAQAAHVA QAVQAQVVVV PQQSVVVQPQ CAGATGQPVG PGTPVSLALS ASPKLDPYFE PELPLQPAVT PVPPTNNSSS SSNNNNGVWH HHHVQQQQQS GSMDHDSLSY TQLYPPLNDL VVSSSSSVGG GTASSAGGGS SASASSSGVY STEMQYPDTT TGNLYYNNNN HYYYDYDATV DVATSMIRPF SANSNSCSSS SESERQLSTG NASIVNETSP SQTTYSDLSH NFELSYFSDN SSQQHQHQQQ QQHLMEQQHL QYQYATW // ID SINA_DROME STANDARD; PRT; 314 AA. AC P21461; Q9VVB0; DT 01-MAY-1991 (Rel. 18, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Developmental protein seven in absentia. GN SINA OR CG9949. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91029488; PubMed=2146028; RA Carthew R.W., Rubin G.M.; RT "Seven in absentia, a gene required for specification of R7 cell fate RT in the Drosophila eye."; RL Cell 63:561-577(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR SPECIFICATION OF R7 PHOTORECEPTOR CELL CC FATE IN THE DROSOPHILA EYE. POSSIBLY ACTS BY REGULATING GENE CC EXPRESSION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: IN MANY OMMATIDIAL PRECURSOR CELLS. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M38384; AAA28901.1; -. DR EMBL; AE003526; AAF49403.1; -. DR EMBL; AY060358; AAL25397.1; -. DR PIR; A36195; A36195. DR FlyBase; FBgn0003410; sina. DR GO; GO:0007423; P:sensory organ development; IMP. DR InterPro; IPR004162; Sina. DR InterPro; IPR008974; Traf_dom. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF03145; Sina; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW Developmental protein; Vision; Nuclear protein; Zinc-finger. FT DOMAIN 14 21 POLY-ALA. FT DOMAIN 46 55 POLY-SER. FT DOMAIN 26 55 SER/THR-RICH. FT ZN_FING 73 108 RING-TYPE. SQ SEQUENCE 314 AA; 33707 MW; B58D7D5E8DA2F958 CRC64; MSNKINPKRR EPTAAAAGAG ATGVATNTST STGSSSAGNT SSANTSSSSS SSLSSAGGGD AGMSADLTSL FECPVCFDYV LPPILQCSSG HLVCVSCRSK LTCCPTCRGP LANIRNLAME KVASNVKFPC KHSGYGCTAS LVYTEKTEHE ETCECRPYLC PCPGASCKWQ GPLDLVMQHL MMSHKSITTL QGEDIVFLAT DINLPGAVDW VMMQSCFGHH FMLVLEKQEK YDGHQQFFAI VQLIGSRKEA ENFVYRLELN GNRRRLTWEA MPRSIHEGVA SAIHNSDCLV FDTSIAQLFA DNGNLGINVT ISLV // ID SING_DROME STANDARD; PRT; 512 AA. AC Q24524; Q9W3L8; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Singed protein. GN SN OR CG1536. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92146932; PubMed=1723709; RA Paterson J., O'Hare K.; RT "Structure and transcription of the singed locus of Drosophila RT melanogaster."; RL Genetics 129:1073-1084(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROBABLY ACTS AS AN ACTIN BUNDLING PROTEIN. MAY HAVE A CC ROLE IN THE ASYMMETRIC ORGANIZATION AND/OR MOVEMENT OF CYTOPLASMIC CC COMPONENTS. IT HAS A ROLE IN SOMATIC CELLS DURING THE FORMATION OF CC ADULT BRISTLES AND HAIRS, AND IN THE FEMALE GERMLINE DURING CC OOGENESIS. CC -!- SIMILARITY: BELONGS TO THE FASCIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17549; CAA35585.1; -. DR EMBL; X17550; CAA35585.1; JOINED. DR EMBL; AE003442; AAF46307.1; -. DR FlyBase; FBgn0003447; sn. DR InterPro; IPR008999; Actin_crosslink. KW Actin-binding. SQ SEQUENCE 512 AA; 57279 MW; A021886A9C7B6C48 CRC64; MNGQGCELGH SNGDIISQNQ QKGWWTIGLI NGQHKYMTAE TFGFKLNANG ASLKKKQLWT LEPSNTGESI IYLRSHLNKY LSVDQFGNVL CESDERDAGS RFQISISEDG SGRWALKNES RGYFLGGTPD KLVCTAKTPG ASEFWTVHLA ARPQVNLRSI GRKRFAHLSE SQDEIHVDAN IPWGEDTLFT LEFRAEEGGR YALHTCNNKY LNANGKLQVV CNEDCLFSAE YHGGHLALRD RQGQYLSPIG SKAVLKSRSS SVTRDELFSL EDSLPQASFI AGLNLRYVSV KQGVDVTANQ DEVGENETFQ LEYDWSAHRW ALRTTQDRYW CLSAGGGIQA TGNRRCADAL FELIWHGDGS LSFRANNGKF LATKRSGHLF ATSESIEEIA KFYFYLINRP ILVLKCEQGF VGYRTPGNLK LECNKATYET ILVERAQKGL VHLKAHSGKY WRIEGESISV DADAPSDGFF LELREPTRIC IRSQQGKYLG ATKNGAFKLL DDGTDSATQW EF // ID SLBP_DROME STANDARD; PRT; 276 AA. AC Q9VAN6; Q9GU71; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Histone RNA hairpin-binding protein (Histone stem-loop binding DE protein). GN SLBP OR CG11886. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=21100311; PubMed=11157774; RA Sullivan E.O., Santiago C., Parker E.D., Dominski Z., Yang X., RA Lanzotti D.J., Ingledue T.C., Marzluff W.F., Duronio R.J.; RT "Drosophila stem loop binding protein coordinates accumulation of RT mature histone mRNA with cell cycle progression."; RL Genes Dev. 15:173-187(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN HISTONE PRE-MRNA 3' PROCESSING AND COUPLES CC HISTONE MRNA PRODUCTION WITH THE CELL CYCLE. BOTH MATERNAL AND CC ZYGOTIC PROTEINS PLAY AN ESSENTIAL AND VITAL FUNCTION FOR CC DEVELOPMENT. CC -!- TISSUE SPECIFICITY: IN LATE EMBRYOS, EXPRESSION IS RESTRICTED TO CC PROLIFERATING (CNS AND PNS) AND ENDOREPLICATING (MIDGUT) CELL CC POPULATIONS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH ZYGOTICALLY AND MATERNALLY. CC EXPRESSION IS HIGHEST IN EARLY EMBRYOS AND ADULT FEMALES. CC -!- SIMILARITY: BELONGS TO THE SLBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF186594; AAG16723.1; -. DR EMBL; AE003768; AAF56867.1; -. DR FlyBase; FBgn0041186; Slbp. DR GO; GO:0007049; P:cell cycle; IMP. DR GO; GO:0006398; P:histone mRNA 3'-end processing; IMP. KW RNA-binding; mRNA processing; Developmental protein. FT DOMAIN 191 260 RNA-BINDING (BY SIMILARITY). FT CONFLICT 3 3 C -> G (IN REF. 1). FT CONFLICT 82 82 G -> C (IN REF. 1). SQ SEQUENCE 276 AA; 30624 MW; 915C9F308F09C607 CRC64; MLCEDQHMSV ENTPQKGSGS LNSSASSISI DVKPTMQSWA QEVRAEFGHS DEASSSLNSS AASCGSLAKK ETADGNLESK DGEGREMAFE FLDGVNEVKF ERLVKEEKLK TPYKRRHSFT PPSNENSRSN SPNSSNSSAN GDAAAPKGGN NPHSRNSKKS GNFRAHKEEK RVRHNSYTSS TSSSSSYTEA DPAILSRRQK QIDYGKNTAA YERYVEMVPK DERTRDHPRT PNKYGKYSRR AFDGLVKIWR KSLHIYDPPT QARDTAKDSN SDSDSD // ID SLIT_DROME STANDARD; PRT; 1504 AA. AC P24014; Q24526; Q8MLB9; Q9V7F8; Q9V7F9; Q9XYV4; DT 01-MAR-1992 (Rel. 21, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Slit protein precursor. GN SLI OR CG8355. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS A AND B). RX MEDLINE=91099665; PubMed=2176636; RA Rothberg J.M., Jacobs J.R., Goodman C.S., Artavanis-Tsakonas S.; RT "Slit: an extracellular protein necessary for development of midline RT glia and commissural axon pathways contains both EGF and LRR RT domains."; RL Genes Dev. 4:2169-2187(1990). RN [2] RP SEQUENCE FROM N.A. (ISOFORM C). RX MEDLINE=99200390; PubMed=10102267; RA Kidd T., Bland K.S., Goodman C.S.; RT "Slit is the midline repellent for the robo receptor in Drosophila."; RL Cell 96:785-794(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 898-1435 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89077533; PubMed=3144436; RA Rothberg J.M., Hartley D.A., Walther Z., Artavanis-Tsakonas S.; RT "slit: an EGF-homologous locus of D. melanogaster involved in the RT development of the embryonic central nervous system."; RL Cell 55:1047-1059(1988). CC -!- FUNCTION: A SHORT-RANGE REPELLENT, CONTROLLING AXON CROSSING OF CC THE MIDLINE AND A LONG-RANGE CHEMOREPELLENT, CONTROLLING MESODERM CC MIGRATION AND PATTERNING AWAY FROM THE MIDLINE. MAY INTERACT WITH CC EXTRACELLULAR MATRIX MOLECULES. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=C; CC IsoId=P24014-1; Sequence=Displayed; CC Name=A; CC IsoId=P24014-2; Sequence=VSP_001408; CC Name=B; CC IsoId=P24014-3; Sequence=VSP_001408, VSP_001409; CC -!- TISSUE SPECIFICITY: IN EMBRYOS, HIGHEST EXPRESSION OCCURS AROUND CC THE MIDLINE GLIA AND LOW EXPRESSION IS OBSERVED AROUND CNS AXONS CC LATERAL TO THE MIDLINE. CC -!- SIMILARITY: CONTAINS 7 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 24 LEUCINE-RICH (LRR) REPEATS. CC -!- SIMILARITY: CONTAINS 1 C-TERMINAL CYSTINE KNOT-LIKE (CTCK) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 LAMININ G-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53959; CAA37910.1; -. DR EMBL; AF126540; AAD26567.1; -. DR EMBL; AE003809; AAF58097.1; -. DR EMBL; AE003809; AAF58098.1; -. DR EMBL; AE003809; AAM70966.1; -. DR EMBL; M23543; AAA72722.1; ALT_INIT. DR HSSP; P00740; 1EDM. DR FlyBase; FBgn0003425; sli. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0045499; F:chemorepellant activity; IMP. DR GO; GO:0007411; P:axon guidance; IGI. DR GO; GO:0008347; P:glia cell migration; IMP. DR GO; GO:0007509; P:mesoderm migration; IMP. DR GO; GO:0030182; P:neuron differentiation; IMP. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR006208; Cys_knot. DR InterPro; IPR006207; Cys_knot_C. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR001611; LRR. DR InterPro; IPR000483; LRR_Cterm. DR InterPro; IPR000372; LRR_Nterm. DR InterPro; IPR003591; LRR_typ. DR Pfam; PF00007; Cys_knot; 1. DR Pfam; PF00008; EGF; 7. DR Pfam; PF00054; laminin_G; 1. DR Pfam; PF00560; LRR; 17. DR Pfam; PF01463; LRRCT; 4. DR Pfam; PF01462; LRRNT; 4. DR PRINTS; PR00011; EGFLAMININ. DR PRINTS; PR00019; LEURICHRPT. DR SMART; SM00041; CT; 1. DR SMART; SM00179; EGF_CA; 2. DR SMART; SM00282; LamG; 1. DR SMART; SM00369; LRR_TYP; 9. DR SMART; SM00082; LRRCT; 4. DR SMART; SM00013; LRRNT; 4. DR PROSITE; PS00010; ASX_HYDROXYL; 3. DR PROSITE; PS01185; CTCK_1; 1. DR PROSITE; PS01225; CTCK_2; 1. DR PROSITE; PS00022; EGF_1; 7. DR PROSITE; PS01186; EGF_2; 5. DR PROSITE; PS50026; EGF_3; 7. DR PROSITE; PS01187; EGF_CA; 2. DR PROSITE; PS50025; LAM_G_DOMAIN; 1. KW Neurogenesis; Glycoprotein; Signal; Alternative splicing; KW EGF-like domain; Repeat; Leucine-rich repeat. FT SIGNAL 1 36 FT CHAIN 37 1504 SLIT PROTEIN. FT CHAIN 37 1135 SLIT PROTEIN N-PRODUCT (BY SIMILARITY). FT CHAIN 1136 1504 SLIT PROTEIN C-PRODUCT (BY SIMILARITY). FT SITE 1135 1136 CLEAVAGE (BY SIMILARITY). FT REPEAT 99 122 LRR 1. FT REPEAT 123 146 LRR 2. FT REPEAT 147 170 LRR 3. FT REPEAT 171 194 LRR 4. FT REPEAT 195 218 LRR 5. FT REPEAT 219 242 LRR 6. FT REPEAT 244 270 LRR 7. FT REPEAT 345 368 LRR 8. FT REPEAT 369 392 LRR 9. FT REPEAT 393 416 LRR 10. FT REPEAT 417 440 LRR 11. FT REPEAT 441 464 LRR 12. FT REPEAT 569 593 LRR 13. FT REPEAT 594 617 LRR 14. FT REPEAT 619 641 LRR 15. FT REPEAT 642 665 LRR 16. FT REPEAT 667 690 LRR 17. FT REPEAT 702 725 LRR 18. FT REPEAT 744 767 LRR 19. FT REPEAT 769 788 LRR 20. FT REPEAT 789 812 LRR 21. FT REPEAT 814 836 LRR 22. FT REPEAT 837 860 LRR 23. FT REPEAT 862 885 LRR 24. FT DOMAIN 931 968 EGF-LIKE 1. FT DOMAIN 970 1007 EGF-LIKE 2. FT DOMAIN 1009 1046 EGF-LIKE 3, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1048 1086 EGF-LIKE 4. FT DOMAIN 1088 1124 EGF-LIKE 5, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1135 1173 EGF-LIKE 6. FT DOMAIN 1176 1349 LAMININ G-LIKE. FT DOMAIN 1377 1416 EGF-LIKE 7. FT DOMAIN 1433 1504 CTCK. FT DISULFID 935 946 BY SIMILARITY. FT DISULFID 940 956 BY SIMILARITY. FT DISULFID 958 967 BY SIMILARITY. FT DISULFID 974 985 BY SIMILARITY. FT DISULFID 979 995 BY SIMILARITY. FT DISULFID 997 1006 BY SIMILARITY. FT DISULFID 1013 1025 BY SIMILARITY. FT DISULFID 1019 1034 BY SIMILARITY. FT DISULFID 1036 1045 BY SIMILARITY. FT DISULFID 1052 1065 BY SIMILARITY. FT DISULFID 1059 1074 BY SIMILARITY. FT DISULFID 1076 1085 BY SIMILARITY. FT DISULFID 1092 1103 BY SIMILARITY. FT DISULFID 1097 1112 BY SIMILARITY. FT DISULFID 1114 1123 BY SIMILARITY. FT DISULFID 1139 1149 BY SIMILARITY. FT DISULFID 1144 1161 BY SIMILARITY. FT DISULFID 1163 1172 BY SIMILARITY. FT DISULFID 1381 1392 BY SIMILARITY. FT DISULFID 1386 1404 BY SIMILARITY. FT DISULFID 1406 1415 BY SIMILARITY. FT CARBOHYD 111 111 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 231 231 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 381 381 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 459 459 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 807 807 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 812 812 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 982 982 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1022 1022 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1084 1084 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1183 1183 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1199 1199 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1267 1267 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1316 1316 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 152 175 Missing (in isoform A and isoform B). FT /FTId=VSP_001408. FT VARSPLIC 1418 1428 Missing (in isoform B). FT /FTId=VSP_001409. FT CONFLICT 350 351 EL -> DV (IN REF. 1 and 2). FT CONFLICT 421 421 Q -> R (IN REF. 1). FT CONFLICT 468 468 I -> M (IN REF. 1). FT CONFLICT 527 527 D -> G (IN REF. 1). FT CONFLICT 560 560 G -> R (IN REF. 1). FT CONFLICT 691 692 WL -> CV (IN REF. 1). FT CONFLICT 751 751 R -> A (IN REF. 1). FT CONFLICT 843 843 L -> V (IN REF. 1). FT CONFLICT 1207 1208 AE -> G (IN REF. 5). FT CONFLICT 1429 1435 AASTCRK -> GTYIYHA (IN REF. 5). SQ SEQUENCE 1504 AA; 168597 MW; 836A3F5022BF234F CRC64; MAAPSRTTLM PPPFRLQLRL LILPILLLLR HDAVHAEPYS GGFGSSAVSS GGLGSVGIHI PGGGVGVITE ARCPRVCSCT GLNVDCSHRG LTSVPRKISA DVERLELQGN NLTVIYETDF QRLTKLRMLQ LTDNQIHTIE RNSFQDLVSL ERLRLNNNRL KAIPENFVTS SASLLRLDIS NNVITTVGRR VFKGAQSLRS LQLDNNQITC LDEHAFKGLV ELEILTLNNN NLTSLPHNIF GGLGRLRALR LSDNPFACDC HLSWLSRFLR SATRLAPYTR CQSPSQLKGQ NVADLHDQEF KCSGLTEHAP MECGAENSCP HPCRCADGIV DCREKSLTSV PVTLPDDTTE LRLEQNFITE LPPKSFSSFR RLRRIDLSNN NISRIAHDAL SGLKQLTTLV LYGNKIKDLP SGVFKGLGSL QLLLLNANEI SCIRKDAFRD LHSLSLLSLY DNNIQSLANG TFDAMKSIKT VHLAKNPFIC DCNLRWLADY LHKNPIETSG ARCESPKRMH RRRIESLREE KFKCSWDELR MKLSGECRMD SDCPAMCHCE GTTVDCTGRG LKEIPRDIPL HTTELLLNDN ELGRISSDGL FGRLPHLVKL ELKRNQLTGI EPNAFEGASH IQELQLGENK IKEISNKMFL GLHQLKTLNL YDNQISCVMP GSFEHLNSLT SLNLASNPFN CNCHLAWFAE WLRKKSLNGG AARCGAPSKV RDVQIKDLPH SEFKCSSENS EGCLGDGYCP PSCTCTGTVV RCSRNQLKEI PRGIPAETSE LYLESNEIEQ IHYERIRHLR SLTRLDLSNN QITILSNYTF ANLTKLSTLI ISYNKLQCLQ RHALSGLNNL RVLSLHGNRI SMLPEGSFED LKSLTHIALG SNPLYCDCGL KWFSDWIKLD YVEPGIARCA EPEQMKDKLI LSTPSSSFVC RGRVRNDILA KCNACFEQPC QNQAQCVALP QREYQCLCQP GYHGKHCEFM IDACYGNPCR NNATCTVLEE GRFSCQCAPG YTGARCETNI DDCLGEIKCQ NNATCIDGVE SYKCECQPGF SGEFCDTKIQ FCSPEFNPCA NGAKCMDHFT HYSCDCQAGF HGTNCTDNID DCQNHMCQNG GTCVDGINDY QCRCPDDYTG KYCEGHNMIS MMYPQTSPCQ NHECKHGVCF QPNAQGSDYL CRCHPGYTGK WCEYLTSISF VHNNSFVELE PLRTRPEANV TIVFSSAEQN GILMYDGQDA HLAVELFNGR IRVSYDVGNH PVSTMYSFEM VADGKYHAVE LLAIKKNFTL RVDRGLARSI INEGSNDYLK LTTPMFLGGL PVDPAQQAYK NWQIRNLTSF KGCMKEVWIN HKLVDFGNAQ RQQKITPGCA LLEGEQQEEE DDEQDFMDET PHIKEEPVDP CLENKCRRGS RCVPNSNARD GYQCKCKHGQ RGRYCDQGEG STEPPTVTAA STCRKEQVRE YYTENDCRSR QPLKYAKCVG GCGNQCCAAK IVRRRKVRMV CSNNRKYIKN LDIVRKCGCT KKCY // ID SLP1_DROME STANDARD; PRT; 322 AA. AC P32030; Q9VQV4; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fork head domain transcription factor slp1 (Sloppy paired locus DE protein 1). GN SLP1 OR FD6 OR CG16738. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=92275347; PubMed=1317319; RA Grossniklaus U., Pearson R.K., Gehring W.J.; RT "The Drosophila sloppy paired locus encodes two proteins involved in RT segmentation that show homology to mammalian transcription factors."; RL Genes Dev. 6:1030-1051(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTION FACTOR INVOLVED IN SEGMENTATION. REQUIRED CC FOR THE FORMATION OF THE MANDIBULAR LOBE. DIFFERENT LEVELS OF SLP CC ACTIVITY SEEM TO BE REQUIRED IN DIFFERENT SEGMENTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE POSTERIOR HALF OF EACH CC PARASEGMENT JUST ANTERIOR TO THE PARASEGMENTAL BOUNDARY. CC -!- DEVELOPMENTAL STAGE: PRESENT AT 0-3 HRS OF EMBRYOGENESIS. MAXIMAL CC EXPRESSION AT 3-6 HRS. STRONG RE-EXPRESSION IN FIRST-INSTAR CC LARVAE. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66095; CAA46889.1; -. DR EMBL; X66096; CAA46890.1; -. DR EMBL; AE003578; AAF51058.1; -. DR HSSP; Q63245; 2HFH. DR TRANSFAC; T01055; -. DR FlyBase; FBgn0003430; slp1. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; NAS. DR GO; GO:0007380; P:specification of segmental identity, head; IEP. DR InterPro; IPR001766; TF_Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR ProDom; PD000425; TF_Fork_head; 1. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation; Pair-rule protein; Polymorphism. FT DNA_BIND 119 210 FORK-HEAD. FT DOMAIN 256 262 POLY-ALA. FT VARIANT 246 246 P -> S (IN STRAIN OREGON-R AND BERKELEY). FT VARIANT 303 303 P -> Q (IN STRAIN OREGON-R AND BERKELEY). SQ SEQUENCE 322 AA; 36202 MW; 24CDE9F0102024C4 CRC64; MVKSEMEFKS NFSIDAILAK KPINTATQPI KTEPVHHHHQ YVHPYSNSDG ELSASEDFDS PSRTSTPMSS AAESLSSQNN DKLDVEFDDE LEDQLDEDQE SEDGNPSKKQ KMTAGSDTKK PPYSYNALIM MAIQDSPEQR LTLNGIYQYL INRFPYFKAN KRGWQNSIRH NLSLNKCFTK IPRSYDDPGK GNYWILDPSA EEVFIGETTG KLRRKNPGAS RTRLAAYRQA IFSPMMAASP YGAPAPSYGY PAVPFAAAAA AALYQRMNPA AYQAAYQQMQ YQQAPQAHHH QAPHPAQMQG YPPQLNAELF QRMQFFGKFP SS // ID SLP2_DROME STANDARD; PRT; 445 AA. AC P32031; Q9VQV5; DT 01-JUL-1993 (Rel. 26, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Fork head domain transcription factor slp2 (Sloppy paired locus DE protein 2). GN SLP2 OR CG2939. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=92275347; PubMed=1317319; RA Grossniklaus U., Pearson R.K., Gehring W.J.; RT "The Drosophila sloppy paired locus encodes two proteins involved in RT segmentation that show homology to mammalian transcription factors."; RL Genes Dev. 6:1030-1051(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TRANSCRIPTION FACTOR INVOLVED IN SEGMENTATION. MAY CC FUNCTION PRIMARILY AS A SEGMENT POLARITY GENE. DIFFERENT LEVELS CC OF SLP ACTIVITY SEEM TO BE REQUIRED IN DIFFERENT SEGMENTS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE POSTERIOR HALF OF EACH CC PARASEGMENT JUST ANTERIOR TO THE PARASEGMENTAL BOUNDARY. CC -!- DEVELOPMENTAL STAGE: EXPRESSION AT 3-6 HRS OF EMBRYOGENESIS. CC STRONG RE-EXPRESSION IN FIRST-INSTAR LARVAE. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66098; CAA46892.1; -. DR EMBL; X66097; CAA46891.1; -. DR EMBL; AE003578; AAF51057.1; ALT_SEQ. DR HSSP; Q63245; 2HFH. DR TRANSFAC; T01056; -. DR FlyBase; FBgn0004567; slp2. DR InterPro; IPR001766; TF_Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR ProDom; PD000425; TF_Fork_head; 1. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation; Segmentation polarity protein; Polymorphism. FT DNA_BIND 179 270 FORK-HEAD. FT DOMAIN 94 104 ASN-RICH. FT VARIANT 362 362 R -> P (IN STRAIN OREGON-R). FT VARIANT 378 378 S -> N (IN STRAIN OREGON-R). FT VARIANT 387 387 R -> Q (IN STRAIN CANTON-S). FT VARIANT 410 410 H -> Q (IN STRAIN OREGON-R). FT VARIANT 416 416 T -> I (IN STRAIN OREGON-R). FT CONFLICT 413 413 P -> L (IN REF. 1). SQ SEQUENCE 445 AA; 50660 MW; 3D9744F413585C8D CRC64; MVKIEEGLPS SEISAHSLHF QHHHHPLPPT THHSALQSPH PVGLNLTNLM KMARTPHLKS SFSINSILPE TVEHHDEDEE EDVEKKSPAK FPPNHNNNNL NTTNWGSPED HEAESDPESD LDVTSMSPAP VANPNESDPD EVDEEFVEED IECDGETTDG DAENKSNDGK PVKDKKGNEK PPYSYNALIM MAIRQSSEKR LTLNGIYEYI MTNHPYYRDN KQGWQNSIRH NLSLNKCFVK VPRHYDDPGK GNYWMLDPSA EDVFIGGSTG KLRRRTTAAS RSRLAAFKRS LIGPMFPGLA AYPQFGQFLT YPPTAPSLLA SMYQRYNPFA PKGGPGHPGL PPGLRDYPDH RDLKDRQDHH HRPSSHHPRA VSSTSDCSTN SCCINMRQPP LWRLIKGNSR WRQHRRRHNH RPPITTHTWR WVRRPFRLAA IPRDPRHSLF TNPSP // ID SLY1_DROME STANDARD; PRT; 639 AA. AC Q24179; O02560; Q8SZB1; Q9VQC9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sly1 protein homolog. GN SLH OR CG3539. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; RX MEDLINE=96217926; PubMed=8675012; RA Merli C., Bergstom D.E., Cygan J.A., Blackman R.K.; RT "Promoter specificity mediates the independent regulation of RT neighboring genes."; RL Genes Dev. 10:1260-1270(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: NON-VITAL FOR DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND MEMBRANE-ASSOCIATED (BY CC SIMILARITY). CC -!- TISSUE SPECIFICITY: IN EMBRYOS, FROM STAGE 14, EXPRESSION IS SEEN CC IN POSTERIOR MIDGUT, ESOPHAGUS AND SALIVARY GLANDS. NO EXPRESSION CC IS SEEN IN LARVAL IMAGINAL DISKS. CC -!- SIMILARITY: BELONGS TO THE STXBP/UNC-18/SEC1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U63852; AAC47550.1; -. DR EMBL; AE003583; AAF51247.3; -. DR EMBL; AY070995; AAL48617.1; -. DR FlyBase; FBgn0015816; Slh. DR GO; GO:0005737; C:cytoplasm; ISS. DR GO; GO:0016020; C:membrane; ISS. DR InterPro; IPR001619; Sec1-like. DR Pfam; PF00995; Sec1; 1. KW Repeat. FT DOMAIN 85 500 4 X APPROXIMATE REPEATS. FT REPEAT 85 121 1. FT REPEAT 203 245 2. FT REPEAT 423 460 3. FT REPEAT 464 500 4. FT CONFLICT 291 293 SAG -> R (IN REF. 1). FT CONFLICT 529 529 H -> HVSFSFQIQIQVLYQNCLQ (IN REF. FT 1). SQ SEQUENCE 639 AA; 72365 MW; 3D99ACBBA028A739 CRC64; MLTLRERQIN AIKQMLNLNS QQPKALAAEP VWKILIYDRV GQDIISPIIS IKELRELGVT LHVQLHSDRD SIPDVPAIYF CLPTDENLDR IQQDFSSGLY DVYHLNFLAP ITRSKIENLA AAALHAGCVA NIHRVYDQYV NFISLEDDFF ILKHQQSDQL SYYAINRANT RDEEMEALMD SIVDSLFALF VTLGNVPIIR CPRNSAAEMV ARKLEKKLRE NLWDARANLF HMDATQAGGG VFSFQRPVLL LLDRNMDLAT PLHHTWSYQA LVHDVLDLGL NLVYVEDETA SAGARKKPKA CDLDRNDRFW MTHKGSPFPT VAEAIQEELE SYRNSEEEIK RLKTSMGIEG ESDIAFSLVN DTTARLTNAV NSLPQLMEKK RLIDMHTKIA TAILNFIKAR RLDSFFEIEE KVMSKQTLDR PLLDLLRDGE FGQAEDKLRL YIIYFICAQQ LPESEQERLK EALQAAGCDL TALAYVQRWK GIMNRSPSIS QATQYEGGGT KTVSMFTKLV SQGSSFVMEG VKNLVVKRHN LPVTKITEQV MECRSNAETD DYLYLDPKLL KGGEVLPKNR APFQDAVVFM VGGGNYIEYQ NLVDFIKQKQ TSNVQRRIIY GASTLTNARQ FLKELSALGG EIQSPTATS // ID SM1A_DROME STANDARD; PRT; 771 AA. AC Q24322; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Semaphorin 1A precursor (Semaphorin-I) (Sema I). GN SEMA-1A OR DSEMA-I OR CG18405. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=94094332; PubMed=8269517; RA Kolodkin A.L., Matthes D.J., Goodman C.S.; RT "The semaphorin genes encode a family of transmembrane and secreted RT growth cone guidance molecules."; RL Cell 75:1389-1399(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PLAY A ROLE IN GROWTH CONES GUIDANCE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED BY SUBSETS OF NEURONS AND MUSCLES. CC -!- DEVELOPMENTAL STAGE: EXPRESSION BEGINS AROUND STAGE 10, PRIMARILY CC IN THE DEVELOPING CNS. IN STAGE 16 EMBRYOS, IT IS EXPRESSED AT CC HIGHEST LEVELS THROUGHOUT THE CNS, AND WEAK EXPRESSION IS SEEN IN CC PORTIONS OF THE PERIPHERAL NERVOUS SYSTEM, MOST CLEARLY IN THE CC LATERAL SENSORY CLUSTERS. CC -!- SIMILARITY: BELONGS TO THE SEMAPHORIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 SEMA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L26082; AAA88789.1; -. DR EMBL; AE003621; AAF52696.1; -. DR FlyBase; FBgn0011259; Sema-1a. DR InterPro; IPR003659; Plexin-like. DR InterPro; IPR002165; Plexin_repeat. DR InterPro; IPR001627; Sema. DR Pfam; PF01437; PSI; 1. DR Pfam; PF01403; Sema; 1. DR SMART; SM00423; PSI; 1. DR SMART; SM00630; Sema; 1. KW Signal; Developmental protein; Transmembrane; Glycoprotein; KW Neurogenesis. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 771 SEMAPHORIN 1A. FT DOMAIN 21 608 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 609 629 POTENTIAL. FT DOMAIN 630 771 CYTOPLASMIC (POTENTIAL). FT DOMAIN 210 519 SEMA. FT DOMAIN 689 694 POLY-PRO. FT CARBOHYD 41 41 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 68 68 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 138 138 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 158 158 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 262 262 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 355 355 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 771 AA; 86935 MW; 752E7DD516F32DA5 CRC64; MQVFLLLTVL VIGNQSAWQE NIRPKLYVEL GPEDVLKFVG NESVVDHFKL VTKDGNSLLI GARNTVFNLS IHDLVEQQRL VWTSPEDDTK MCLVKGKDEE ACQNYIRIMV VPSPGRLFVC GTNSFRPMCN TYIISDSNYT LEATKNGQAV CPYDPRHNST SVLADNELYS GTVADFSGSD PIIYREPLQT EQYDSLSLNA PNFVSSFTQG DFVYFFFRET AVEFINCGKA IYSRVARVCK WDKGGPHRFR NRWTSFLKSR LNCSIPGDYP FYFNEIQSAS NLVEGQYGSM SSKLIYGVFN TPSNSIPGSA VCAFALQDIA DTFEGQFKEQ TGINSNWLPV NNAKVPDPRP GSCHNDSRAL PDPTLNFIKT HSLMDENVPA FFSQPILVRT STIYRFTQIA VDAQIKTPGG KTYDVIFVGT DHGKIIKSVN AESADSADKV TSVVIEEIDV LTKSEPIRNL EIVRTMQYDQ PKDGSYDDGK LIIVTDSQVV AIQLHRCHND KITSCSECVA LQDPYCAWDK IAGKCRSHGA PRWLEENYFY QNVATGQHAA CPSGKINSKD ANAGEQKGFR NDMDLLDSRR QSKDQEIIDN IDKNFEDIIN AQYTVETLVM AVLAGSIFSL LVGFFTGYFC GRRCHKDEDD NLPYPDTEYE YFEQRQNVNS FPSSCRIQQE PKLLPQVEEV TYAEPVLLPQ PPPPNKMHSP KNTLRKPPMH QMHQGPNSET LFQFQPDGYN TQQSYRGRDN FGTLRSHQVM GDNYRRGDGF STTRSVKKVY L // ID SM2A_DROME STANDARD; PRT; 706 AA. AC Q24323; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Semaphorin 2A precursor (Semaphorin-II) (Sema II). GN SEMA-2A OR DSEMA-II. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=94094332; PubMed=8269517; RA Kolodkin A.L., Matthes D.J., Goodman C.S.; RT "The semaphorin genes encode a family of transmembrane and secreted RT growth cone guidance molecules."; RL Cell 75:1389-1399(1993). CC -!- FUNCTION: PLAY A ROLE IN GROWTH CONES GUIDANCE. REQUIRED FOR BOTH CC PROPER ADULT BEHAVIOR AND SURVIVAL. CAN FUNCTION IN VIVO AS A CC SELECTIVE TARGET-DERIVED SIGNAL THAT INHIBITS THE FORMATION OF CC SPECIFIC SYNAPTIC TERMINAL ARBORS. CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: TRANSIENTLY EXPRESSED BY A SINGLE LARGE MUSCLE CC DURING MOTONEURON OUTGROWTH AND SYNAPSE FORMATION. CC -!- DEVELOPMENTAL STAGE: EXPRESSION BEGINS AROUND STAGE 10 IN WEAK CC EPIDERMAL STRIPES. NERVOUS SYSTEM EXPRESSION IS FIRST DETECTED CC AROUND STAGE 15 AND AT STAGE 16 APPEARS TO REMAIN RESTRICTED TO A CC SMALL SUBSET OF NEURONS. BEGINNING AROUND STAGE 14, IT IS ALSO CC EXPRESSED AT A VERY HIGH LEVEL IN A SINGLE VENTRAL THORACIC MUSCLE CC FIBER IN SEGMENT T3. IT IS ALSO EXPRESSED IN THE EMBRYONIC GONADS CC AND IN ANTERIOR SENSORY ORGANS, INCLUDING THE MAXILLARY COMPLEX. CC -!- SIMILARITY: BELONGS TO THE SEMAPHORIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 SEMA DOMAIN. CC -!- SIMILARITY: CONTAINS 1 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L26083; AAC37187.1; -. DR FlyBase; FBgn0011260; Sema-2a. DR GO; GO:0016201; P:synaptic target inhibition; IMP. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003599; Ig. DR InterPro; IPR001627; Sema. DR Pfam; PF01403; Sema; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00630; Sema; 1. DR PROSITE; PS50835; IG_LIKE; 1. KW Signal; Immunoglobulin domain; Neurogenesis; Developmental protein; KW Glycoprotein. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 706 SEMAPHORIN 2A. FT DOMAIN 244 526 SEMA. FT DOMAIN 534 645 IG-LIKE C2-TYPE. FT DISULFID 629 665 BY SIMILARITY. FT CARBOHYD 95 95 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 145 145 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 172 172 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 296 296 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 383 383 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 545 545 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 640 640 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 652 652 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 690 690 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 706 AA; 81023 MW; 2C7D374E6CAA1D6D CRC64; MSLLQLSPLL ALLLLLCSSV SETAADYENT WNFYYERPCC TGNDQGNNNY GKHGADHVRE FNCGKLYYRT FHMNEDRDTL YVGAMDRVFR VNLQNISSSN CNRDAINLED CKNHVRVIQS MDQGDRLYVC GTNAHNPKDY VIYANLTHLP RSEYVIGVGL GIAKCPYDPL DNSTAIYVEN GNPGGLPGLY SGTNAEFTKA DTVIFRTDLY NTSAKRLEYK FKRTLKYDSK WLDKPNFVGS FDIGEYVYFF FRETAVEYIN CGKAVYSRIA RVCKKDVGGK NLLAHNWATY LKARLNCSIS GEFPFYFNEI QSVYQLPSDK SRFFATFTTS TNGLIGSAVC SFHINEIQAA FNGKFKEQSS SNSAWLPVLN SRVPEPRPGT CVNDTSNLPD TVLNFIRSHP LMDKAVNHEH NNPVYYKRDL VFTKLVVDKI RIDILNQEYI VYYVGTNLGR IYKIVQYYRN GESLSKLLDI FEVAPNEAIQ VMEISQTRKS LYIGTDHRIK QIDLAMCNRR YDNCFRCVRD PYCGWDKEAN TCRPYELDLL QDVANETSDI CDSSVLKKKI VVTYGQSVHL GCFVKIPEVL KNEQVTWYHH SKDKGRYEIR YSPTKYIETT ERGLVVVSVN EADGGRYDCH LGGSLLCSYN ITVDAHRCTP PNKSNDYQKI YSDWCHEFEK YKTAMKSWEK KQGQCSTRQN FSCNQHPNEI FRKPNV // ID SMD1_DROME STANDARD; PRT; 124 AA. AC Q9VU02; Q8SYR6; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable small nuclear ribonucleoprotein Sm D1 (snRNP core protein D1) DE (Sm-D1). GN SNRNP69D OR BCDNA:RE39488 OR CG10753. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ESSENTIAL FOR PRE-MRNA SPLICING. IMPLICATED IN THE CC FORMATION OF STABLE, BIOLOGICALLY ACTIVE SNRNP STRUCTURES (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SNRNP CORE PROTEIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003540; AAF49893.1; -. DR EMBL; AY071359; AAL48981.1; -. DR FlyBase; FBgn0016940; snRNP69D. DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; ISS. DR GO; GO:0008248; F:pre-mRNA splicing factor activity; ISS. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; ISS. DR InterPro; IPR001163; snRNP_Sm. DR Pfam; PF01423; LSM; 1. DR SMART; SM00651; Sm; 1. KW Nuclear protein; Ribonucleoprotein; mRNA splicing; mRNA processing. FT DOMAIN 86 124 ARG/LYS-RICH (BASIC). FT DOMAIN 100 118 9 X 2 AA TANDEM REPEATS OF R-G. FT CONFLICT 52 52 P -> H (IN REF. 2). SQ SEQUENCE 124 AA; 13796 MW; 36FA511D3FBE6B65 CRC64; MKLVRFLMKL SHETVTIELK NGTQIHGTIT GVDVAMNTHL KSVRMTIKNR DPVHLETLSI RGNNIRYFIL PDSLPLETLL IDDTPKSKTK KKDSGRVGNR GRGRGARGRG GPRGRGRGRA SGRR // ID SMD3_DROME STANDARD; PRT; 151 AA. AC O44437; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Small nuclear ribonucleoprotein SM D3 (snRNP core protein D3) (SM- DE D3). GN SMD3 OR GUF2 OR CG8427. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=98147796; PubMed=9488472; RA Ivanov I.P., Simin K., Letsou A., Atkins J.F., Gesteland R.F.; RT "The Drosophila gene for antizyme requires ribosomal frameshifting for RT expression and contains an intronic gene for snRNP Sm D3 on the RT opposite strand."; RL Mol. Cell. Biol. 18:1553-1561(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR PRE-MRNA SPLICING. REQUIRED FOR SNRNP CC BIOGENESIS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SNRNP CORE PROTEIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF038598; AAB92621.1; -. DR EMBL; AE003823; AAF58566.1; -. DR EMBL; AY113465; AAM29470.1; -. DR HSSP; P43331; 1D3B. DR FlyBase; FBgn0023167; SmD3. DR InterPro; IPR006649; snRNP. DR InterPro; IPR001163; snRNP_Sm. DR Pfam; PF01423; LSM; 1. DR ProDom; PD020287; snRNP; 1. DR SMART; SM00651; Sm; 1. KW Nuclear protein; Ribonucleoprotein; mRNA splicing; KW mRNA processing; Repeat. FT DOMAIN 84 120 ARG/LYS-RICH (BASIC). FT DOMAIN 108 113 3 X 2 AA TANDEM REPEATS OF RG. SQ SEQUENCE 151 AA; 15582 MW; 65F0B899EACA1C77 CRC64; MSIGVPIKVL HEAEGHIITC ETITGEVYRG KLIEAEDNMN CQMTQITVTY RDGRTANLEN VYIRGSKIRF LILPDMLKNA PMFKKQTGKG LGGTAGRGKA AILRAQARGR GRGGPPGGGR GTGGPPGAPG GSGGRGAWQG GPTGGRGRGG L // ID SMO_DROME STANDARD; PRT; 1036 AA. AC P91682; Q9VPM8; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Smoothened protein precursor (dSMO) (SMOH) (Smooth). GN SMO OR CG11561. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96319725; PubMed=8706127; RA Alcedo J., Ayzenzon M., von Ohlen T., Noll M., Hooper J.E.; RT "The Drosophila smoothened gene encodes a seven-pass membrane RT protein, a putative receptor for the hedgehog signal."; RL Cell 86:221-232(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96320560; PubMed=8700230; RA van den Heuvel M., Ingham P.W.; RT "smoothened encodes a receptor-like serpentine protein required for RT hedgehog signalling."; RL Nature 382:547-551(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: SEGMENT POLARITY PROTEIN REQUIRED FOR CORRECT PATTERNING CC OF EVERY SEGMENT. G PROTEIN-COUPLED RECEPTOR THAT ASSOCIATES WITH CC THE PATCHED PROTEIN (PTC) TO TRANSDUCE THE HEDGEHOG (HH) SIGNAL CC THROUGH THE ACTIVATION OF AN INHIBITORY G-PROTEIN. IN THE ABSENCE CC OF HH, PTC REPRESSES THE CONSTITUTIVE SIGNALING ACTIVITY OF SMO CC THROUGH FUSED (FU). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT ALL DEVELOPMENTAL STAGES, THOUGH CC THE LEVELS VARY. CC -!- SIMILARITY: BELONGS TO THE FZ/SMO G-PROTEIN COUPLED RECEPTOR CC FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1, MET-9, MET-13 OR MET-14 IS CC THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U87613; AAC33180.1; -. DR EMBL; AF030334; AAB84275.1; -. DR EMBL; AE003590; AAF51518.2; -. DR FlyBase; FBgn0003444; smo. DR GO; GO:0007350; P:blastoderm segmentation; IMP. DR GO; GO:0007455; P:eye-antennal disc metamorphosis; IGI. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP. DR InterPro; IPR000539; Frizzled. DR InterPro; IPR000024; Fz_domain. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF01534; Frizzled; 1. DR Pfam; PF01392; Fz; 1. DR PRINTS; PR00489; FRIZZLED. DR SMART; SM00063; FRI; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; Signal; KW Developmental protein. FT SIGNAL 1 31 POTENTIAL. FT CHAIN 32 1036 SMOOTHENED PROTEIN. FT DOMAIN 32 258 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 259 279 1 (POTENTIAL). FT DOMAIN 280 287 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 288 308 2 (POTENTIAL). FT DOMAIN 309 339 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 340 360 3 (POTENTIAL). FT DOMAIN 361 381 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 382 402 4 (POTENTIAL). FT DOMAIN 403 421 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 422 442 5 (POTENTIAL). FT DOMAIN 443 469 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 470 490 6 (POTENTIAL). FT DOMAIN 491 532 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 533 553 7 (POTENTIAL). FT DOMAIN 554 1036 CYTOPLASMIC (POTENTIAL). FT DOMAIN 85 206 FZ. FT DOMAIN 816 819 POLY-SER. FT CARBOHYD 55 55 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 95 95 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 184 184 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 195 195 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 213 213 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 336 336 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 419 419 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1036 AA; 116552 MW; 7797FC71A539A87A CRC64; MQYLNFPRMP NIMMFLEVAI LCLWVVADAS ASSAKFGSTT PASAQQSDVE LEPINGTLNY RLYAKKGRDD KPWFDGLDSR HIQCVRRARC YPTSNATNTC FGSKLPYELS SLDLTDFHTE KELNDKLNDY YALKHVPKCW AAIQPFLCAV FKPKCEKING EDMVYLPSYE MCRITMEPCR ILYNTTFFPK FLRCNETLFP TKCTNGARGM KFNGTGQCLS PLVPTDTSAS YYPGIEGCGV RCKDPLYTDD EHRQIHKLIG WAGSICLLSN LFVVSTFFID WKNANKYPAV IVFYINLCFL IACVGWLLQF TSGSREDIVC RKDGTLRHSE PTAGENLSCI VIFVLVYYFL TAGMVWFVFL TYAWHWRAMG HVQDRIDKKG SYFHLVAWSL PLVLTITTMA FSEVDGNSIV GICFVGYINH SMRAGLLLGP LCGVILIGGY FITRGMVMLF GLKHFANDIK STSASNKIHL IIMRMGVCAL LTLVFILVAI ACHVTEFRHA DEWAQSFRQF IICKISSVFE EKSSCRIENR PSVGVLQLHL LCLFSSGIVM STWCWTPSSI ETWKRYIRKK CGKEVVEEVK MPKHKVIAQT WAKRKDFEDK GRLSITLYNT HTDPVGLNFD VNDLNSSETN DISSTWAAYL PQCVKRRMAL TGAATGNSSS HGPRKNSLDS EISVSVRHVS VESRRNSVDS QVSVKIAEMK TKVASRSRGK HGGSSSNRRT QRRRDYIAAA TGKSSRRRES STSVESQVIA LKKTTYPNAS HKVGVFAHHS SKKQHNYTSS MKRRTANAGL DPSILNEFLQ KNGDFIFPFL QNQDMSSSSE EDNSRASQKI QDLNVVVKQQ EISEDDHDGI KIEELPNSKQ VALENFLKNI KKSNESNSNR HSRNSARSQS KKSQKRHLKN PAADLDFRKD CVKYRSNDSL SCSSEELDVA LDVGSLLNSS FSGISMGKPH SRNSKTSCDV GIQANPFELV PSYGEDELQQ AMRLLNAASR QRTEAANEDF GGTELQGLLG HSHRHQREPT FMSESDKLKM LLLPSK // ID SN25_DROME STANDARD; PRT; 212 AA. AC P36975; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Synaptosomal-associated protein 25 (SNAP-25). GN SNAP25. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=94043281; PubMed=8226991; RA Risinger C., Blomqvist A.G., Lundell I., Lambertsson A., RA Nassel D., Pieribone V.A., Brodin L., Larhammar D.; RT "Evolutionary conservation of synaptosome-associated protein 25 kDa RT (SNAP-25) shown by Drosophila and Torpedo cDNA clones."; RL J. Biol. Chem. 268:24408-24414(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=97417485; PubMed=9272858; RA Risinger C., Deitcher D.L., Lundell I., Schwarz T.L., Larhammar D.; RT "Complex gene organization of synaptic protein SNAP-25 in Drosophila RT melanogaster."; RL Gene 194:169-177(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). CC -!- FUNCTION: MAY PLAY AN IMPORTANT ROLE IN THE SYNAPTIC FUNCTION OF CC SPECIFIC NEURONAL SYSTEMS. ASSOCIATES WITH PROTEINS INVOLVED IN CC VESICLE DOCKING AND MEMBRANE FUSION. CC -!- SUBCELLULAR LOCATION: COMPLEXED WITH MACROMOLECULAR ELEMENTS OF CC THE NERVE TERMINAL. CC -!- TISSUE SPECIFICITY: EXCLUSIVELY FOUND IN BRAIN AND GANGLIA. CC -!- SIMILARITY: BELONGS TO THE SNAP-25 FAMILY. CC -!- SIMILARITY: CONTAINS 2 T-SNARE COILED-COIL HOMOLOGY DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L22021; AAA16059.1; -. DR EMBL; U81153; AAB39757.1; -. DR EMBL; U81147; AAB39757.1; JOINED. DR EMBL; U81148; AAB39757.1; JOINED. DR EMBL; U81149; AAB39757.1; JOINED. DR EMBL; U81150; AAB39757.1; JOINED. DR EMBL; U81151; AAB39757.1; JOINED. DR EMBL; U81152; AAB39757.1; JOINED. DR FlyBase; FBgn0011288; Snap25. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0005486; F:t-SNARE activity; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016081; P:synaptic vesicle docking; NAS. DR GO; GO:0016083; P:synaptic vesicle fusion; NAS. DR InterPro; IPR000928; SNAP-25. DR InterPro; IPR000727; T_SNARE. DR Pfam; PF00835; SNAP-25; 1. DR Pfam; PF05739; SNARE; 1. DR SMART; SM00397; t_SNARE; 2. DR PROSITE; PS50192; T_SNARE; 2. KW Synaptosome; Neurone; Repeat; Coiled coil. FT DOMAIN 26 88 T-SNARE COILED-COIL HOMOLOGY 1. FT DOMAIN 148 210 T-SNARE COILED-COIL HOMOLOGY 2. FT DOMAIN 91 99 CYS-RICH. SQ SEQUENCE 212 AA; 23685 MW; BDC90649A1AF3AC8 CRC64; MPADPSEEVA PQVPKTELEE LQINAQGVAD ESLESTRRML ALCEESKEAG IRTLVALDDQ GEQLDRIEEG MDQINADMRE AEKNLSGMEK CCGICVLPCN KSQSFKEDDG TWKGNDDGKV VNNQPQRVMD DRNGMMAQAG YIGRITNDAR EDEMEENMGQ VNTMIGNLRN MALDMGSELE NQNRQIDRIN RKGESNEARI AVANQRAHQL LK // ID SNAI_DROME STANDARD; PRT; 390 AA. AC P08044; Q9V3D3; DT 01-AUG-1988 (Rel. 08, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Snail protein. GN SNA OR BG:DS01845.1 OR CG3956. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88065862; PubMed=3683556; RA Boulay J.L., Dennefeld C., Alberga A.; RT "The Drosophila developmental gene snail encodes a protein with RT nucleic acid binding fingers."; RL Nature 330:395-398(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Alberga A.A., Boulay J.L., Dennefeld C., Mauhin V., Vicaire S.; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE OF 263-344 FROM N.A. RX MEDLINE=93066327; PubMed=1438276; RA Sommer R.J., Retzlaff M., Goerlich K., Sander K., Tautz D.; RT "Evolutionary conservation pattern of zinc-finger domains of RT Drosophila segmentation genes."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10782-10786(1992). CC -!- FUNCTION: ESSENTIAL FOR THE CORRECT SPECIFICATION OF VENTRAL- CC DORSAL PATTERNS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE SNAIL FAMILY OF ZINC FINGER PROTEINS. CC -!- SIMILARITY: CONTAINS 5 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00288; CAA68397.1; -. DR EMBL; AE003413; AAF44944.1; -. DR EMBL; AJ251486; CAB62556.1; -. DR EMBL; AE003647; AAF53463.1; -. DR EMBL; BT010255; AAQ23573.1; -. DR PIR; S06222; S06222. DR TRANSFAC; T00751; -. DR FlyBase; FBgn0003448; sna. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0009950; P:dorsal/ventral axis specification; NAS. DR GO; GO:0007499; P:ectoderm/mesoderm interaction; NAS. DR GO; GO:0007369; P:gastrulation; NAS. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 5. DR ProDom; PD000003; Znf_C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. KW Developmental protein; Zinc-finger; Metal-binding; DNA-binding; KW Nuclear protein; Repeat. FT DOMAIN 209 234 SER-RICH. FT ZN_FING 245 267 C2H2-TYPE 1. FT ZN_FING 280 302 C2H2-TYPE 2. FT ZN_FING 306 328 C2H2-TYPE 3. FT ZN_FING 334 356 C2H2-TYPE 4. FT ZN_FING 362 385 C2H2-TYPE 5. FT CONFLICT 93 93 A -> T (IN REF. 1 AND 3). SQ SEQUENCE 390 AA; 42955 MW; E50611680EC6F6EC CRC64; MAANYKSCPL KKRPIVFVEE RLPQTEALAL TKDSQFAQDQ PQDLSLKRGR DEETQDYQQP EPKRDYVLNL SKTPERNSSS SSNSCLLSPP VEAQDYLPTE IHMRGLTAGT TGYTTATPTT INPFQSAFVM AAGCNPISAL WSSYQPHLAA FPSPASSMAS PQSVYSYQQM TPPSSPGSDL ETGSEPEDLS VRNDIPLPAL FHLFDEAKSS SSGASVSSSS GYSYTPAMSA SSASVAANHA KNYRFKCDEC QKMYSTSMGL SKHRQFHCPA AECNQEKKTH SCEECGKLYT TIGALKMHIR THTLPCKCPI CGKAFSRPWL LQGHIRTHTG EKPFQCPDCP RSFADRSNLR AHQQTHVDVK KYACQVCHKS FSRMSLLNKH SSSNCTITIA // ID SNAK_DROME STANDARD; PRT; 430 AA. AC P05049; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Serine protease snake precursor (EC 3.4.21.-). GN SNK. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Delotto R., Spierer P.; RT "A gene required for the specification of dorsal-ventral pattern in RT Drosophila appears to encode a serine protease."; RL Nature 323:688-692(1986). CC -!- FUNCTION: THIS PROTEIN IS REQUIRED FOR THE SPECIFICATION OF DORSAL CC -VENTRAL PATTERN IN DROSOPHILA. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04513; CAA28197.1; -. DR PIR; A24702; A24702. DR HSSP; P20231; 1AAO. DR MEROPS; S01.200; -. DR FlyBase; FBgn0003450; snk. DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS. DR GO; GO:0009950; P:dorsal/ventral axis specification; NAS. DR GO; GO:0016485; P:protein processing; IGI. DR GO; GO:0008063; P:Tl signaling pathway; IGI. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Developmental protein; Serine protease; Hydrolase; Signal. FT SIGNAL 1 27 POTENTIAL. FT CHAIN 28 430 SERINE PROTEASE SNAKE. FT DOMAIN 184 430 SERINE PROTEASE. FT ACT_SITE 233 233 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 280 280 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 376 376 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 177 300 BY SIMILARITY. FT DISULFID 218 234 BY SIMILARITY. FT DISULFID 342 362 BY SIMILARITY. FT DISULFID 372 403 BY SIMILARITY. SQ SEQUENCE 430 AA; 47782 MW; A3D967CD607B3AD3 CRC64; MIILWSLIVH LQLTCLHLIL QTPNLEALDA LEIINYQTTK YTIPEVWKEQ PVQAIGEDVD DQDTEDEESY LKFGDDAEVR TSVSEGLHEG RFCRRTFDGR SGYASWPISG STSSESIGCM AIDICTHRNN VPVICCPLAD KHVLAQRISA TKCQEYNAAA RRLHLTDTVR TFSGKQCVPS VPLIVGGTPT RHGLFPHMAA LGWTQGSGSK DQDIKWGCGG ALVSELYVLT AAHCATSGAN HRTWFAWRPQ LNETSATQQD IKILIIVLHP KYRSSAYYHD IALLKLTRRV KFSEQVRPAC LWQCGAPHTT VVAAGWGRTE FLGAKSNALR QVDLDVSPQM TCKQIYRKER RLPRGIIEGQ FCAGYLQAQG HCQGDSGGPI HALLPEYNCV AFVVGITSFG KFCAAPNAPG VYTRLYSYLD WIEKIAFKQH // ID SNAP_DROME STANDARD; PRT; 292 AA. AC Q23983; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Soluble NSF attachment protein (SNAP) (N-ethylmaleimide-sensitive DE factor attachment protein). GN SNAP OR CG6625. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=94261657; PubMed=8202553; RA Ordway R.W., Pallanck L., Ganetzky B.; RT "Neurally expressed Drosophila genes encoding homologs of the NSF and RT SNAP secretory proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5715-5719(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR VESICULAR TRANSPORT BETWEEN THE ENDOPLASMIC CC RETICULUM AND THE GOLGI APPARATUS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC PERIPHERAL MEMBRANE PROTEIN (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SNAP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U09374; AAA83414.1; -. DR EMBL; AE003514; AAF49035.1; -. DR FlyBase; FBgn0011712; Snap. DR GO; GO:0005483; F:soluble NSF attachment protein activity; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016082; P:synaptic vesicle priming; NAS. DR InterPro; IPR000744; NSF_attach. DR InterPro; IPR008941; TPR-like. DR Pfam; PF02071; NSF; 5. DR PRINTS; PR00448; NSFATTACHMNT. KW Transport; Protein transport; Endoplasmic reticulum; Golgi stack. SQ SEQUENCE 292 AA; 33000 MW; 4EE50F038ACFEC5F CRC64; MGDNEQKALQ LMAEAEKKLT QQKGFLGSLF GGSNKVEDAI ECYQRAGNMF KMSKNWTKAG ECFCEAATLH ARAGSRHDAG TCYVDASNCY KKVDVESAVN CLMKSIDIYT DMGRFTMAAK HHQSIAEMYE SDPNNLAKSI QHYEQAADYF KGEESVSSAN KCMLKVAQYA AQLEDYEKAI SIYEQVAASS LESSLLKYSA KEYFFRAALC HLSVDLLNAQ HAIEKYAQQY PAFQDSREFK LIKVLCENLE EQNIEGFTEA VKDYDSISRL DQWYTTILLR IKKAADEDPD LR // ID SNPF_DROME STANDARD; PRT; 300 AA. AC Q9VIQ0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Short neuropeptide F precursor [Contains: sNPF-associated peptide DE (sNPF-AP); sNPF peptide 2 (sNPF-2)]. GN SNPF OR CG13968. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 99-109 AND 112-121. RC TISSUE=Larva; RX MEDLINE=22287343; PubMed=12171930; RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.; RT "Peptidomics of the larval Drosophila melanogaster central nervous RT system."; RL J. Biol. Chem. 277:40368-40374(2002). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q9VIQ0-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9VIQ0-2; Sequence=VSP_004072; CC Note=No experimental confirmation available; CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003665; AAF53865.1; -. DR EMBL; BT001780; AAN71535.1; -. DR FlyBase; FBgn0032840; sNPF. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0005184; F:neuropeptide hormone activity; NAS. DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS. KW Neuropeptide; Cleavage on pair of basic residues; Signal; KW Alternative splicing. FT SIGNAL 1 30 POTENTIAL. FT PROPEP 31 98 FT PEPTIDE 99 109 SNPF-ASSOCIATED PEPTIDE. FT PEPTIDE 112 121 SNPF PEPTIDE 2. FT PROPEP 123 300 FT VARSPLIC 37 55 Missing (in isoform B). FT /FTId=VSP_004072. FT CONFLICT 8 8 L -> Q (IN REF. 3). FT CONFLICT 119 119 K -> R (IN REF. 3). FT CONFLICT 266 266 R -> G (IN REF. 3). SQ SEQUENCE 300 AA; 34650 MW; E65E9FD46FAA9793 CRC64; MFHLKRELSQ GCALALICLV SLQMQQPAQA EVSSAQGEHL VQPPPEKQSS KDSFLGTPLS NLYDNLLQRE YAGPVVFPNH QVERKAQRSP SLRLRFGRSD PDMLNSIVEK RWFGDVNQKP IRSPSLRLRF GRRDPSLPQM RRTAYDDLLE RELTLNSQQQ QQQLGTEPDS DLGADYDGLY ERVVRKPQRL RWGRSVPQFE ANNADNEQIE RSQWYNSLLN SDKMRRMLVA LQQQYEIPEN VASYANDEDT DTDLNNDTSE FQREVRKPMR LRWGRSTGKA PSEQKHTPEE TSSIPPKTQN // ID SODC_DROME STANDARD; PRT; 152 AA. AC P00444; Q9VTF6; DT 21-JUL-1986 (Rel. 01, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1). GN SOD OR CG11793. OS Drosophila melanogaster (Fruit fly), OS Drosophila simulans (Fruit fly), OS Drosophila mauritiana (Fruit fly), and OS Drosophila sechellia (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7240, 7226, 7238; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Canton-S; RX MEDLINE=89160267; PubMed=2493630; RA Kwiatowski J., Patel M., Ayala F.J.; RT "Drosophila melanogaster Cu, Zn superoxide dismutase gene sequence."; RL Nucleic Acids Res. 17:1264-1264(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=89252924; PubMed=2470654; RA Seto N.O., Hayashi S., Tener G.M.; RT "Cloning, sequence analysis and chromosomal localization of the Cu-Zn RT superoxide dismutase gene of Drosophila melanogaster."; RL Gene 75:85-92(1989). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=87260017; PubMed=3110743; RA Seto N.O.L., Hayashi S., Tener G.M.; RT "Drosophila Cu-Zn superoxide dismutase cDNA sequence."; RL Nucleic Acids Res. 15:5483-5483(1987). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=88096604; PubMed=3122185; RA Seto N.O.L., Hayashi S., Tener G.M.; RT "The sequence of the Cu-Zn superoxide dismutase gene of Drosophila."; RL Nucleic Acids Res. 15:10601-10601(1987). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Canton-S; RA Phillips J.P.; RL Submitted (DEC-1989) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [7] RP SEQUENCE OF 90-121 FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Canton-S; RX MEDLINE=88185843; PubMed=3128462; RA Kirkland K.C., Phillips J.P.; RT "Isolation and chromosomal localization of genomic DNA sequences RT coding for cytoplasmic superoxide dismutase from Drosophila RT melanogaster."; RL Gene 61:415-419(1987). RN [8] RP SEQUENCE. RC SPECIES=D.melanogaster; RX MEDLINE=85140189; PubMed=3919383; RA Lee Y.M., Friedman D.J., Ayala F.J.; RT "Superoxide dismutase: an evolutionary puzzle."; RL Proc. Natl. Acad. Sci. U.S.A. 82:824-828(1985). RN [9] RP SEQUENCE. RC SPECIES=D.melanogaster; RX MEDLINE=85305751; PubMed=3929689; RA Lee Y.M., Friedman D.J., Ayala F.J.; RT "Complete amino acid sequence of copper-zinc superoxide dismutase RT from Drosophila melanogaster."; RL Arch. Biochem. Biophys. 241:577-589(1985). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=D.simulans; RX MEDLINE=89386009; PubMed=2780301; RA Kwiatowski J., Gonzales F., Ayala F.J.; RT "Drosophila simulans Cu-Zn superoxide dismutase gene sequence."; RL Nucleic Acids Res. 17:6735-6735(1989). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=D.mauritiana, and D.sechellia; RA Arxontaki K., Kastanis P., Tsakas S., Loukas M., Eliopoulos E.; RT "Phylogenetic analysis of Drosophila melanogaster group based on Cu-Zn RT superoxide dismutase gene sequences."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND WHICH ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 SUPEROXIDE + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: BINDS 1 COPPER ION AND 1 ZINC ION PER SUBUNIT. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE CU-ZN SUPEROXIDE DISMUTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18823; AAA28905.1; -. DR EMBL; Y00367; CAA68443.1; -. DR EMBL; M24421; AAA28906.1; -. DR EMBL; X13780; CAA32028.1; -. DR EMBL; X17332; CAA35210.1; -. DR EMBL; AE003546; AAF50095.1; -. DR EMBL; X15685; CAA33720.1; -. DR EMBL; Z19591; CAA79639.1; -. DR EMBL; AF127158; AAF23597.1; -. DR EMBL; AF127157; AAF23596.1; -. DR PIR; S02725; DSFFCZ. DR PIR; S05498; S05498. DR HSSP; P15107; 1XSO. DR FlyBase; FBgn0003462; Sod. DR FlyBase; FBgn0012854; Dsim\Sod. DR FlyBase; FBgn0029364; Dmau\Sod. DR FlyBase; FBgn0023627; Dsec\Sod. DR GO; GO:0008340; P:determination of adult life span; IMP. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Antioxidant; Oxidoreductase; Metal-binding; Copper; Zinc. FT INIT_MET 0 0 FT METAL 44 44 COPPER. FT METAL 46 46 COPPER. FT METAL 61 61 COPPER AND ZINC. FT METAL 69 69 ZINC. FT METAL 78 78 ZINC. FT METAL 81 81 ZINC. FT METAL 118 118 COPPER. FT DISULFID 55 144 FT CONFLICT 96 96 N -> K (IN REF. 7 AND 8). SQ SEQUENCE 152 AA; 15567 MW; AAD77785765417A4 CRC64; VVKAVCVING DAKGTVFFEQ ESSGTPVKVS GEVCGLAKGL HGFHVHEFGD NTNGCMSSGP HFNPYGKEHG APVDENRHLG DLGNIEATGD CPTKVNITDS KITLFGADSI IGRTVVVHAD ADDLGQGGHE LSKSTGNAGA RIGCGVIGIA KV // ID SODM_DROME STANDARD; PRT; 217 AA. AC Q00637; Q9V7T8; DT 01-JUL-1993 (Rel. 26, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Mn], mitochondrial precursor (EC 1.15.1.1). GN SOD2 OR CG8905. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=94266156; PubMed=8206377; RA Duttaroy A., Meidinger R., Kirby K., Carmichael S., Hilliker A., RA Phillips J.; RT "A manganese superoxide dismutase-encoding cDNA from Drosophila RT melanogaster."; RL Gene 143:223-225(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Phillips J.P., Kirby K.; RT "Sequence analysis of a genomic clone encoding for manganese RT superoxide dismutase (mnSOD) in D. melanogaster."; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 34-176 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92211732; PubMed=1556751; RA Smith M.W., Doolittle R.F.; RT "A comparison of evolutionary rates of the two major kinds of RT superoxide dismutase."; RL J. Mol. Evol. 34:175-184(1992). CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND WHICH ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 SUPEROXIDE + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: BINDS 1 MANGANESE ION PER SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO THE IRON/MANGANESE SUPEROXIDE DISMUTASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L18947; AAA20533.1; -. DR EMBL; L34276; AAA28694.1; -. DR EMBL; AE003805; AAF57955.1; -. DR EMBL; X64062; CAA45418.1; -. DR PIR; S23657; S23657. DR HSSP; P04179; 1ABM. DR FlyBase; FBgn0010213; Sod2. DR InterPro; IPR001189; SODismutase. DR Pfam; PF00081; sodfe; 1. DR Pfam; PF02777; sodfe_C; 1. DR PRINTS; PR01703; MNSODISMTASE. DR ProDom; PD000475; SODismutase; 1. DR PROSITE; PS00088; SOD_MN; 1. KW Oxidoreductase; Metal-binding; Manganese; Mitochondrion; KW Transit peptide. FT TRANSIT 1 17 MITOCHONDRION (BY SIMILARITY). FT CHAIN 18 217 SUPEROXIDE DISMUTASE [MN]. FT METAL 43 43 MANGANESE (BY SIMILARITY). FT METAL 91 91 MANGANESE (BY SIMILARITY). FT METAL 175 175 MANGANESE (BY SIMILARITY). FT METAL 179 179 MANGANESE (BY SIMILARITY). FT CONFLICT 9 14 PNCKPG -> QTASLA (IN REF. 2 AND 3). FT CONFLICT 127 127 L -> V (IN REF. 4). SQ SEQUENCE 217 AA; 24684 MW; 05900339EA92432B CRC64; MFVARKISPN CKPGVRGKHT LPKLPYDYAA LEPIICREIM ELHHQKHHQT YVNNLNAAEE QLEEAKSKSD TTKLIQLAPA LRFNGGGHIN HTIFWQNLSP NKTQPSDDLK KAIESQWKSL EEFKKELTTL TVAVQGSGWG WLGFNKKSGK LQLAALPNQD PLEASTGLIP LFGIDVWEHA YYLQYKNVRP SYVEAIWDIA NWDDISCRFQ EAKKLGC // ID SOG_DROME STANDARD; PRT; 1038 AA. AC Q24025; Q9VXS7; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dorsal-ventral patterning protein Sog (Short gastrulation protein). GN SOG OR CG9224. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95047398; PubMed=7958919; RA Francois V., Solloway M., O'Neill J.W., Emery J., Bier E.; RT "Dorsal-ventral patterning of the Drosophila embryo depends on a RT putative negative growth factor encoded by the short gastrulation RT gene."; RL Genes Dev. 8:2602-2616(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PUTATIVE NEGATIVE GROWTH FACTOR; ANTAGONIST OF DPP, A CC PROTEIN INVOLVED IN PATTERNING THE DORSAL REGION AND IN THE CC DEVELOPMENT OF THE NEUROECTODERM. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: ABUTS THE DORSAL DPP-EXPRESSING CELLS IN A CC LATERAL STRIPE 14-16 CELLS WIDE. LATER IN EMBRYOGENESIS IT IS CC EXPRESSED IN NEUROECTODERM AND IN THE ENDODERM SPACED ALONG THE CC ANTERIOR-POSTERIOR AXIS OF THE DEVELOPING GUT. CC -!- DEVELOPMENTAL STAGE: EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE CHORDIN FAMILY. CC -!- SIMILARITY: CONTAINS 4 CHRD DOMAINS. CC -!- SIMILARITY: CONTAINS 4 VWFC DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18774; AAA89117.1; -. DR EMBL; AE003499; AAF48481.1; -. DR PIR; T13177; T13177. DR FlyBase; FBgn0003463; sog. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR InterPro; IPR006559; SOG. DR InterPro; IPR001007; VWF_C. DR Pfam; PF00093; vwc; 4. DR SMART; SM00566; SOG; 3. DR SMART; SM00214; VWC; 3. DR PROSITE; PS50933; CHRD; 4. DR PROSITE; PS01208; VWFC_1; 2. DR PROSITE; PS50184; VWFC_2; 2. KW Transmembrane; Developmental protein; Repeat; Growth factor; KW Growth regulation; Signal-anchor. FT DOMAIN 1 53 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 54 74 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 75 1038 EXTRACELLULAR (POTENTIAL). FT DOMAIN 100 175 VWFC 1. FT DOMAIN 197 337 CHRD 1. FT DOMAIN 339 471 CHRD 2. FT DOMAIN 474 588 CHRD 3. FT DOMAIN 592 713 CHRD 4. FT DOMAIN 742 804 VWFC 2. FT DOMAIN 830 899 VWFC 3. FT DOMAIN 939 1020 VWFC 4. FT CARBOHYD 179 179 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 287 287 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 520 520 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 666 666 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 752 752 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 821 821 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1038 AA; 115514 MW; B0E833AFD79A9037 CRC64; MANKLRKSNA IEWATATGTV PLLERSCCHS EDAALEPQAS KTSHREQAPI LRHLSQLSHL LIIAGLLIVC LAGVTEGRRH APLMFEESDT GRRSNRPAVT ECQFGKVLRE LGSTWYADLG PPFGVMYCIK CECVAIPKKR RIVARVQCRN IKNECPPAKC DDPISLPGKC CKTCPGDRND TDVALDVPVP NEEEERNMKH YAALLTGRTS YFLKGEEMKS MYTTYNPQNV VATARFLFHK KNLYYSFYTS SRIGRPRAIQ FVDDAGVILE EHQLETTLAG TLSVYQNATG KICGVWRRVP RDYKRILRDD RLHVVLLWGN KQQAELALAG KVAKYTALQT ELFSSLLEAP LPDGKTDPQL AGAGGTAIVS TSSGAASSMH LTLVFNGVFG AEEYADAALS VKIELAERKE VIFDEIPRVR KPSAEINVLE LSSPISIQNL RLMSRGKLLL TVESKKYPHL RIQGHIVTRA SCEIFQTLLA PHSAESSTKS SGLAWVYLNT DGSLAYNIET EHVNTRDRPN ISLIEEQGKR KAKLEDLTPS FNFNQAIGSV EKLGPKVLES LYAGELGVNV ATEHETSLIR GRLVPRPVAD ARDSAEPILL KRQEHTDAQN PHAVGMAWMS IDNECNLHYE VTLNGVPAQD LQLYLEEKPI EAIGAPVTRK LLEEFNGSYL EGFFLSMPSA ELIKLEMSVC YLEVHSKHSK QLLLRGKLKS TKVPGHCFPV YTDNNVPVPG DHNDNHLVNG ETKCFHSGRF YNESEQWRSA QDSCQMCACL RGQSSCEVIK CPALKCKSTE QLLQRDGECC PSCVPKKEAA DYSAQSSPAT NATDLLQQRR GCRLGEQFHP AGASWHPFLP PNGFDTCTTC SCDPLTLEIR CPRLVCPPLQ CSEKLAYRPD KKACCKICPE GKQSSSNGHK TTPNNPNVLQ DQAMQRSPSH SAEEVLANGG CKVVNKVYEN GQEWHPILMS HGEQKCIKCR CKDSKVNCDR KRCSRSTCQQ QTRVTSKRRL FEKPDAAAPA IDECCSTQCR RSRRHHKRQP HHQQRSSS // ID SOH1_DROME STANDARD; PRT; 204 AA. AC Q8IH24; Q9VN40; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Mediator complex subunit TRAP18 (Protein SOH1) (dSOH1). GN TRAP18 OR CG1057. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP FUNCTION OF THE MEDIATOR COMPLEX, AND IDENTIFICATION IN A COMPLEX WITH RP TRAP170; TRAP80; CDK8; MED6; TRAP36; TRFP; DP28B/CG14802 AND TRAP19. RX MEDLINE=21160264; PubMed=11259581; RA Park J.M., Gim B.S., Kim J.M., Yoon J.H., Kim H.-S., Kang J.-G., RA Kim Y.-J.; RT "Drosophila Mediator complex is broadly utilized by diverse RT gene-specific transcription factors at different types of core RT promoters."; RL Mol. Cell. Biol. 21:2312-2323(2001). CC -!- FUNCTION: COMPONENT OF THE MEDIATOR COMPLEX IS ESSENTIAL FOR BASAL CC AND REGULATED EXPRESSION OF NEARLY ALL RNA POLYMERASE II-DEPENDENT CC GENES. MEDIATOR COMPLEX MAY ACT AS A BRIDGE, CONVEYING REGULATORY CC INFORMATION FROM ENHANCERS AND OTHER CONTROL ELEMENTS TO THE CC PROMOTER. CC -!- SUBUNIT: COMPONENT OF A MEDIATOR COMPLEX, WHICH CONTAINS TRAP170, CC TRAP80, CDK8, TRAP18/SOH1, MED6, TRAP36, TRFP, DP28B/CG14802, CC TRAP19. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8IH24-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IH24-2; Sequence=VSP_008708; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE MEDIATOR SOH1 SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003605; AAF52111.1; -. DR EMBL; AY061423; AAL28971.1; -. DR EMBL; BT001465; AAN71220.1; -. DR FlyBase; FBgn0037262; Trap18. DR InterPro; IPR008831; SOH1. DR Pfam; PF05669; SOH1; 1. KW Transcription regulation; Nuclear protein; Alternative splicing. FT DOMAIN 127 189 GLN-RICH. FT VARSPLIC 1 71 Missing (in isoform 2). FT /FTId=VSP_008708. SQ SEQUENCE 204 AA; 23530 MW; A387204AD57A9157 CRC64; MAKMYGKGKT AIESEELQKR RWQIELEFVQ CLSNPNYLNF LAQRGFFKDQ SFINYLKYLQ YWKEPDYAKY LMYPMCLYFL DLLQYEHFRR EIVNSQCCKF IDDQAILQWQ HYTRKRIKLI ENVTAAQQQQ QQLQQQQQQA NGMEAATGGE SAAPTPNVNG SASTADSQQT SSALQPVQAQ PGNPQQQQQI NGVASGANIK LELN // ID SOL_DROME STANDARD; PRT; 1597 AA. AC P27398; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Small optic lobes protein (EC 3.4.22.-). GN SOL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC TISSUE=Brain; RX MEDLINE=91334436; PubMed=1714593; RA Delaney S.J., Hayward D.C., Barleben F., Fischbach K.-F., RA Miklos G.L.G.; RT "Molecular cloning and analysis of small optic lobes, a structural RT brain gene of Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7214-7218(1991). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P27398-1; Sequence=Displayed; CC Name=Short; CC IsoId=P27398-2; Sequence=VSP_005246; CC -!- MISCELLANEOUS: THE SOL (SMALL OPTIC LOBES) MUTATION ELIMINATES CC CERTAIN CLASSES OF COLUMNAR NEURONS. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C2. CC -!- SIMILARITY: CONTAINS 6 RANBP2-TYPE ZINC FINGERS. CC -!- SIMILARITY: CONTAINS 1 CALPAIN CATALYTIC DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M64084; AAB95431.1; -. DR PIR; A41146; BVFFSL. DR HSSP; Q07009; 1DF0. DR MEROPS; C02.010; -. DR FlyBase; FBgn0003464; sol. DR InterPro; IPR001300; Peptidase_C2. DR InterPro; IPR000169; SHprot_acsite. DR InterPro; IPR001876; Znf_RanGDP. DR Pfam; PF00648; Peptidase_C2; 1. DR Pfam; PF00641; zf-RanBP; 6. DR PRINTS; PR00704; CALPAIN. DR SMART; SM00230; CysPc; 1. DR SMART; SM00547; ZnF_RBZ; 6. DR PROSITE; PS50203; CALPAIN_CAT; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; FALSE_NEG. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; FALSE_NEG. DR PROSITE; PS01358; ZF_RANBP2_1; 5. DR PROSITE; PS50199; ZF_RANBP2_2; 4. KW Alternative splicing; Zinc-finger; Repeat; Hydrolase; Thiol protease. FT ZN_FING 1 35 RANBP2-TYPE 1. FT ZN_FING 135 164 RANBP2-TYPE 2. FT ZN_FING 643 673 RANBP2-TYPE 3. FT DOMAIN 673 689 GLN-RICH. FT DOMAIN 690 697 POLY-HIS. FT ZN_FING 707 736 RANBP2-TYPE 4. FT ZN_FING 747 777 RANBP2-TYPE 5. FT ZN_FING 930 959 RANBP2-TYPE 6. FT DOMAIN 1017 1324 CALPAIN CATALYTIC. FT ACT_SITE 1082 1082 BY SIMILARITY. FT ACT_SITE 1248 1248 BY SIMILARITY. FT ACT_SITE 1268 1268 BY SIMILARITY. FT VARSPLIC 394 1297 Missing (in isoform Short). FT /FTId=VSP_005246. SQ SEQUENCE 1597 AA; 174714 MW; 11D10E6FDDA7DAE7 CRC64; MGTISSVLQW SCTKCNTINP TESLKCFNCG TVRKVFPQQQ QQQHRSSSIT ASWTADDALE QEQAEKGQER DKEKGRAAVA RSEYKHVYKS LLRGCLKRPQ RNSQNLPANC VDCEDTRKYI KSSIELYRHF SNPALNRRWV CHACGTDNSS VTWHCLICDT VSYLAPIYKD AIAADRGQDL AGSLGNRGEL LAADHSHPHH HHHYLHQELE EQHQHQLHSQ HLHKRHLKGR SASGSGSGPG SGSGLRRTQS LSTAIDKSAS GRSCHICYAN NQSKDIFNLP QIKPAPQLTG IPPVAACSNS RFAIANDTFC RRKQNNNNKN QNHKVVRESG AKRKYNFTIT TLSRSAAKDA GHGQMKPLRQ VVNLNLNLQQ EPQQKSPANP QQLHRKTQRE PAAVSMNPTQ FTIPRNGVFI AVNEWSEPMA SSSSVSSSSN HHHHHHSNSN SNSSGNSNII NNNSSSSSGS NKLYENECVA LAQQQLRAAA AQAAQAAATA VAIASSPSAK AMAEPAPTAT MPIYAQVNKQ HKLKKKQQIA SESQTNNNTG SGEIADAVSE SLTAGLGTST DGSGEASESE SQVEEHSIYA KVWKGPRKAT ESKIMHDPGS SSRLSGAASA AAGTASAGAI AAGVGAAAAS RHDNKTQLGN GSRSKMWICI KCSYAYNRLW LQTCEMCEAK AEQQQQQLHL QQQQQQQQQH HHHHHHHLQQ QQAEAPRDEP WTCKKCTLVN YSTAMACVVC GGSKLKSISS IEDMTLRKGE FWTCSHCTLK NSLHSPVCSA CKSHRQPQLS MAMEAVRERP DGQSYEEQDA AAVGGGGGSA HQSGANEVKA PTALNLPLTS VALPMPMLQL PTSTAAGLRG SRSPSPRMQL LPSLQQQRNS SSSGAIPKRH STGGSIVPRN ISIAGLANYN LQQGQGVGSA SVVSASGAGS GAGAVGASTS SKKWQCPACT YDNCAASVVC DICSSPRGLA SAVLGEALGR KSVRVALTPA DIRQESKLME NLRQLEETEA LTKWQNIIQY CRDNSELFVD DSFPPAPKSL YYNPASGAGE GNPVVQWRRP HEINCDGGAY PPWAVFRTPL PSDICQGVLG NCWLLSALAV LAEREDLVKE VLVTKEICGQ GAYQVRLCKD GKWTTVLVDD LLPCDKRGHL VYSQAKRKQL WVPLIEKAVA KIHGCYEALV SGRAIEGLAT LTGAPCESIP LQASSLPMPS EDELDKDLIW AQLLSSRCVR FLMGASCGGG NMKVDEEEYQ QKGLRPRHAY SVLDVKDIQG HRLLKLRNPW GHYSWRGDWS DDSSLWTDDL RDALMPHGAS EGVFWISFED VLNYFDCIDI CKVRSGWNEV RLQGTLQPLC SISCVLLTVL EPTEAEFTLF QEGQRNSEKS QRSQLDLCVV IFRTRSPAAP EIGRLVEHSK RQVRGFVGCH KMLERDIYLL VCLAFNHWHT GIEDPHQYPQ CILAIHSSKR LLVEQISPSP HLLADAIISL TLTKGQRHEG REGMTAYYLT KGWAGLVVMV ENRHENKWIH VKCDCQESYN VVSTRGELKT VDSVPPLQRQ VIIVLTQLEG SGGFSIAHRL THRLANSRGL HDWGPPGATH CPPIENVHGL HAPRLIT // ID SOS_DROME STANDARD; PRT; 1595 AA. AC P26675; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Son of sevenless protein. GN SOS. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92141820; PubMed=1736363; RA Bonfini L., Karlovich C.A., Dasgupta C., Banerjee U.; RT "The Son of sevenless gene product: a putative activator of Ras."; RL Science 255:603-606(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92034991; PubMed=1934068; RA Simon M.A., Bowtell D.D.L., Dodson G.S., Laverty T.R., Rubin G.M.; RT "Ras1 and a putative guanine nucleotide exchange factor perform RT crucial steps in signaling by the sevenless protein tyrosine RT kinase."; RL Cell 67:701-716(1991). CC -!- FUNCTION: PROMOTES THE EXCHANGE OF RAS-BOUND GDP BY GTP. SOS IS CC IMPLICATED IN NEURONAL DEVELOPMENT. CC -!- SUBUNIT: MAY FORM A COMPLEX WITH SEVENLESS AND DRK. CC -!- SIMILARITY: CONTAINS 1 DBL-HOMOLOGY (DH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 N-TERMINAL RAS-GEF DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- SIMILARITY: CONTAINS 1 RAS-GEF DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M83931; AAB04680.1; -. DR EMBL; M77501; AAA28904.1; -. DR PDB; 1AZE; 18-MAY-99. DR FlyBase; FBgn0001965; Sos. DR InterPro; IPR001331; GDS_CDC24. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR001849; PH. DR InterPro; IPR000651; RasGEFN. DR InterPro; IPR001895; RasGRF_CDC25. DR InterPro; IPR008937; Ras_GEF. DR InterPro; IPR000219; RhoGEF. DR Pfam; PF00169; PH; 1. DR Pfam; PF00617; RasGEF; 1. DR Pfam; PF00618; RasGEFN; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00147; RasGEF; 1. DR SMART; SM00229; RasGEFN; 1. DR SMART; SM00325; RhoGEF; 1. DR PROSITE; PS00741; DH_1; FALSE_NEG. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS00720; RASGEF; 1. DR PROSITE; PS50009; RASGEF_CAT; 1. DR PROSITE; PS50212; RASGEF_NTER; 1. KW Guanine-nucleotide releasing factor; Neurogenesis; 3D-structure. FT DOMAIN 636 791 N-TERMINAL RAS-GEF. FT DOMAIN 828 1065 RAS-GEF. FT DOMAIN 15 51 GLY-RICH. FT DOMAIN 247 433 DH. FT DOMAIN 479 587 PH. FT DOMAIN 1511 1516 GLN-RICH. FT DOMAIN 1525 1541 HIS-RICH. FT CONFLICT 232 243 TSCPVPCHFPRS -> HILPSPLSLPAQR FT (IN REF. 2). FT CONFLICT 1462 1462 V -> P (IN REF. 2). SQ SEQUENCE 1595 AA; 177837 MW; 33AE31F0767A219F CRC64; MFSGPSGHAH TISYGGGIGL GTGGGGGSGG SGSGSQGGGG GIGIGGGGVA GLQDCDGYDF TKCENAARWR GLFTPSLKKV LEQVHPRVTA KEDALLYVEK LCLRLLAMLC AKPLPHSVQD VEEKVNKSFP APIDQWALNE AKEVINSKKR KSVLPTEKVH TLLQKDVLQY KIDSSVSAFL VAVLEYISAD ILKMAGDYVI KIAHCEITKE DIEVVMNADR VLMDMLNQSE ATSCPVPCHF PRSASATYEE TVKELIHDEK QYQRDLHMII RVFREELVKI VSDPRELEPI FSNIMDIYEV TVTLLGSLED VIEMSQEQSA PCVGSCFEEL AEAEEFDVYK KYAYDVTSQA SRDALNNLLS KPGASSLTTA GHGFRDAVKY YLPKLLLVPI CHAFVYFDYI KHLKDLSSSQ DDIESFEQVQ GLLHPLHCDL EKVMASLSKE RQVPVSGRVR RQLAIERTRE LQMKVEHWED KDVGQNCNEF IREDSLSKLG SGKRIWSERK VFLFDGLMVL CKANTKKQTP SAGATAYDYR LKEKYFMRRV DINDRPDSDD LKNSFELAPR MQPPIVLTAK NAQHKHDWMA DLLMVITKSM LDRHLDSILQ DIERKHPLRM PSPEIYKFAV PDSGDNIVLE ERESAGVPMI KGATLCKLIE RLTYHIYADP TFVRTFLTTY RYFCSPQQLL QLLVERFNIP DPSLVYQDTG TAGAGGMGGV GGDKEHKNSH REDWKRYRKE YVQPVQFRVL NVLRHWVDHH FYDFEKDPML LEKLLNFLEH VNGKSMRKWV DSVLKIVQRK NEQEKSNKKI VYAYGHDPPP IEHHLSVPND EITLLTLHPL ELARQLTLLE FEMYKNVKPS ELVGSPWTKK DKEVKSPNLL KIMKHTTNVT RWIEKSITEA ENYEERLAIM QRAIEVMMVM LELNNFNGIL SIVAAMGTAS VYRLRWTFQG LPERYRKFLE ECRELSDDHL KKYQERLRSI NPPCVPFFGR YLTNILHLEE GNPDLLANTE LINFSKRRKV AEIIGEIQQY QNQPYCLNEE STIRQFFEQL DPFNGLSDKQ MSDYLYNESL RIEPRGCKTV PKFPRKWPHI PLKSPGIKPR RQNQTNSSSK LSNSTSSVAA AAAASSTATS IATASAPSLH ASSIMDAPTA AAANAGSGTL AGEQSPQHNP HAFSVFAPVI IPERNTSSWS GTPQHTRTDQ NNGEVSVPAP HLPKKPGAHV WANNNSTLAS ASAMDVVFSP ALPEHLPPQS LPDSNPFASD TEAPPSPLPK LVVSPRHETG NRSPFHGRMQ NSPTHSTAST VTLTGMSTSG GEEFCAGGFY FNSAHQGQPG AVPISPHVNV PMATNMEYRA VPPPLPPRRK ERTESCADMA QKRQAPDAPT LPPRDGELSP PPIPPRLNHS TGISYLRQSH GKSKEFVGNS SLLLPNTSSI MIRRNSAIEK RAAATSQPNQ AAAGPISTTL VTVSQAVATD EVLPLPISPA ASSSTTTSPL TPAMSPMSPN IPSHPVESTS SSYAHQLRMR QQQQQQTHPA IYSQHHQHHA THLPHHPHQH HSNPTQSRSS PKEFFPIATS LEGTPKLPPK PSLSANFYNN PDKGTMFLYP STNEE // ID SO_DROME STANDARD; PRT; 416 AA. AC Q27350; Q9V4L0; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sine oculis protein. GN SO OR CG11121. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=95203683; PubMed=7896096; RA Serikaku M.A., O'Tousa J.E.; RT "Sine oculis is a homeobox gene required for Drosophila visual system RT development."; RL Genetics 138:1137-1150(1994). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo, and Eye imaginal disk; RX MEDLINE=94242440; PubMed=7910468; RA Cheyette B.N.R., Green P.J., Martin K., Garren H., Hartenstein V., RA Zipursky S.L.; RT "The Drosophila sine oculis locus encodes a homeodomain-containing RT protein required for the development of the entire visual system."; RL Neuron 12:977-996(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR VISUAL SYSTEM DEVELOPMENT. MAY CC TRANSCRIPTIONALLY REGULATE GENES NECESSARY FOR OPTIC LOBE CC INVAGINATION AND BOLWIG'S NERVE FORMATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: IN DEVELOPING EMBRYOS, EXPRESSED IN THE EYE CC DISK EPITHELIUM, BOLWIG'S ORGAN AND THE OPTIC LOBE PRIMORDIUM AT CC AREAS OF INVAGINATION. IN ADULTS, PRESENT IN PHOTORECEPTOR CELLS CC IN THE APICAL REGIONS OF THE RETINA, AND IN OPTIC LOBES. CC -!- DEVELOPMENTAL STAGE: IN THE EYE IMAGINAL DISK, FIRST EXPRESSED AT CC THE ONSET OF THE THIRD INSTAR AND CONTINUES THROUGHOUT THIS STAGE. CC EXPRESSION IN THE OPTIC LOBE PRIMORDIUM BEGINS AT STAGE 5 AND CC DISAPPEARS WHEN INVAGINATION IS COMPLETED (STAGE 12). FURTHER CC EXPRESSION IS NOTED IN OPTIC LOBE GANGLIA IN LATE THIRD INSTAR. CC -!- MISCELLANEOUS: SO MUTANTS SPECIFICALLY DISPLAY VISUAL DEFECTS. CC THESE RANGE FROM REDUCED OCELLI AND OMMATIDIA NUMBER IN WEAK LOSS- CC OF-FUNCTION PHENOTYPES TO COMPLETE ABSENCE OF COMPOUND EYES AND CC BOLWIG'S ORGAN IN MORE SEVERE LETHAL PHENOTYPES. CC -!- SIMILARITY: BELONGS TO THE SIX/SINE OCULIS HOMEOBOX FAMILY. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S77459; AAB34685.1; -. DR EMBL; L31626; AAA21800.1; -. DR EMBL; AE003841; AAF59260.1; -. DR PIR; S50342; S50342. DR HSSP; P41778; 1DU6. DR TRANSFAC; T03273; -. DR FlyBase; FBgn0003460; so. DR GO; GO:0007623; P:circadian rhythm; IGI. DR GO; GO:0008347; P:glia cell migration; IMP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR000047; HTH_lambrepressr. DR InterPro; IPR007105; SIX. DR InterPro; IPR007106; SIX_SINE_homeo. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00031; HTHREPRESSR. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Developmental protein; Homeobox; DNA-binding; Nuclear protein. FT DOMAIN 42 47 POLY-ASN. FT DOMAIN 52 55 POLY-ASN. FT DOMAIN 80 85 POLY-GLY. FT DOMAIN 307 316 POLY-GLN (OPA REPEAT). FT DOMAIN 366 372 POLY-GLY. FT DOMAIN 375 379 POLY-ALA. FT DNA_BIND 218 277 HOMEOBOX. SQ SEQUENCE 416 AA; 45025 MW; 669E4BD95B857996 CRC64; MLQHPATDFY DLAAANAAAV LTARHTPPYS PTGLSGSVAL HNNNNNNSST SNNNNSTLDI MAHNGGGAGG GLHLNSSSNG GGGGGVVSGG GSGGRENLPS FGFTQEQVAC VCEVLQQAGN IERLGRFLWS LPQCDKLQLN ESVLKAKAVV AFHRGQYKEL YRLLEHHHFS AQNHAKLQAL WLKAHYVEAE KLRGRPLGAV GKYRVRRKFP LPRTIWDGEE TSYCFKEKSR SVLRDWYSHN PYPSPREKRD LAEATGLTTT QVSNWFKNRR QRDRAAEHKD GSTDKQHLDS SSDSEMEGSM LPSQSAQHQQ QQQQQQHSPG NSSGNNNGLH QQQLQHVAAE QGLQHHPHQP HPASNIANVA ATKSSGGGGG GGVSAAAAAQ MQMPPLTAAV AYSHLHSVMG AMPMTAMYDM GEYQHL // ID SP18_DROME STANDARD; PRT; 150 AA. AC Q9VEX9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable Sin3 associated polypeptide p18 (Bicoid interacting protein DE 1). GN BIN1 OR CG6046. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: ACTS IN TRANSCRIPTION REPRESSION. INVOLVED IN THE CC TETHERING OF THE SIN3 COMPLEX TO CORE HISTONE PROTEINS (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SAP18 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003712; AAF55284.1; -. DR FlyBase; FBgn0024491; Bin1. KW Transcription regulation; Repressor. SQ SEQUENCE 150 AA; 17288 MW; 94947F206D8FA0AD CRC64; MANVESMIVE EKTQVKQIDR EKTCPMLLRV FCSTGRHHSV SEYMFGNVPT NELQIYTWQD ATLHELTSLV RDVNPDTRKK GTYFDFAVVY PNFRSNHFQM REIGVTCTGQ KGIDDNKTLA QAKFSIGDFL DISITPPNRL PPTARRQRPY // ID SPCA_DROME STANDARD; PRT; 2415 AA. AC P13395; Q26340; Q8SZW7; Q9W085; DT 01-JAN-1990 (Rel. 13, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Spectrin alpha chain. GN ALPHA-SPEC OR SPEC-A OR CG1977. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90037215; PubMed=2808524; RA Dubreuil R.R., Byers T.J., Sillman A.L., Bar-Zvi D., RA Goldstein L.S.B., Branton D.; RT "The complete sequence of Drosophila alpha-spectrin: conservation of RT structural domains between alpha-spectrins and alpha-actinin."; RL J. Cell Biol. 109:2197-2205(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-150 AND 2192-2415 FROM N.A., AND CHARACTERIZATION. RX MEDLINE=94103334; PubMed=8276898; RA Lee J.K., Coyne R.S., Dubreuil R.R., Goldstein L.S.B., Branton D.; RT "Cell shape and interaction defects in alpha-spectrin mutants of RT Drosophila melanogaster."; RL J. Cell Biol. 123:1797-1809(1993). RN [4] RP SEQUENCE OF 1539-2415 FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP CHARACTERIZATION. RX MEDLINE=88059242; PubMed=3680372; RA Dubreuil R., Byers T.J., Branton D., Goldstein L.S.B., Kiehart D.P.; RT "Drosophilia spectrin. I. Characterization of the purified protein."; RL J. Cell Biol. 105:2095-2102(1987). RN [6] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX MEDLINE=20530668; PubMed=11076973; RA Sisson J.C., Field C., Ventura R., Royou A., Sullivan W.; RT "Lava lamp, a novel peripheral Golgi protein, is required for RT Drosophila melanogaster cellularization."; RL J. Cell Biol. 151:905-918(2000). RN [7] RP EMBRYONIC LOCALIZATION. RX MEDLINE=89234159; PubMed=2497103; RA Pesacreta T.C., Byers T.J., Dubreuil R., Kiehart D.P., Branton D.; RT "Drosophila spectrin: the membrane skeleton during embryogenesis."; RL J. Cell Biol. 108:1697-1709(1989). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1391-1497. RX MEDLINE=94090340; PubMed=8266097; RA Yan Y., Winograd E., Viel A., Cronin T., Harrison S.C., Branton D.; RT "Crystal structure of the repetitive segments of spectrin."; RL Science 262:2027-2030(1993). CC -!- FUNCTION: SPECTRIN IS THE MAJOR CONSTITUENT OF THE CYTOSKELETAL CC NETWORK UNDERLYING THE ERYTHROCYTE PLASMA MEMBRANE. IT ASSOCIATES CC WITH BAND 4.1 AND ACTIN TO FORM THE CYTOSKELETAL SUPERSTRUCTURE OF CC THE ERYTHROCYTE PLASMA MEMBRANE. ESSENTIAL FOR LARVAL SURVIVAL AND CC DEVELOPMENT. STABILIZES CELL TO CELL INTERACTIONS THAT ARE CC CRITICAL FOR THE MAINTENANCE OF CELL SHAPE AND SUBCELLULAR CC ORGANIZATION WITHIN EMBRYONIC TISSUES. LVA AND SPECTRIN MAY FORM A CC GOLGI-BASED SCAFFOLD THAT MEDIATES INTERACTION OF GOLGI BODIES CC WITH MICROTUBUBLES AND FACILITATES GOLGI-DERIVED MEMBRANE CC SECRETION REQUIRED FOR THE FORMATION OF FURROWS DURING CC CELLULARIZATION. CC -!- SUBUNIT: NATIVE SPECTRIN MOLECULE IS A TETRAMER COMPOSED OF TWO CC ANTIPARALLEL HETERODIMERS JOINED HEAD TO HEAD SO THAT EACH END OF CC THE NATIVE MOLECULE INCLUDES THE C-TERMINUS OF THE ALPHA SUBUNIT CC AND THE N-TERMINUS OF THE BETA SUBUNIT. INTERACTS WITH CALMODULIN CC IN A CALCIUM-DEPENDENT MANNER, INTERACTS WITH F-ACTIN AND ALSO CC INTERACTS WITH LVA. CC -!- SUBCELLULAR LOCATION: NEAR THE INNER SURFACE OF THE PLASMA CC MEMBRANE OF NEARLY ALL CELLS. LVA-ALPHA-SPECTRIN COMPLEXES ARE CC FOUND AT THE GOLGI. CC -!- TISSUE SPECIFICITY: A SUBSTANTIAL POOL OF MATERNAL PROTEIN IN THE CC EGG UNDERGOES DYNAMIC CHANGES IN DISTRIBUTION EARLY IN CC EMBRYOGENESIS. IN GASTRULATED EMBRYO, THE HIGHEST LEVEL OF PROTEIN CC IS FOUND IN THE RESPIRATORY TRACT CELLS AND THE LOWEST IN PARTS OF CC THE FORMING GUT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE SPECTRIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- SIMILARITY: CONTAINS 22 SPECTRIN REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M26400; AAA28907.1; -. DR EMBL; AE003472; AAF47569.1; -. DR EMBL; S67762; AAB29441.2; -. DR EMBL; S67765; AAB29442.1; -. DR EMBL; AY069741; AAL39886.1; -. DR PIR; A33733; A33733. DR PDB; 2SPC; 31-MAY-94. DR FlyBase; FBgn0003470; alpha-Spec. DR GO; GO:0005938; C:cell cortex; IDA. DR GO; GO:0045169; C:fusome; IDA. DR GO; GO:0005794; C:Golgi apparatus; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0045170; C:spectrosome; IDA. DR GO; GO:0003779; F:actin binding; IDA. DR GO; GO:0008017; F:microtubule binding; IDA. DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP. DR GO; GO:0007294; P:oocyte cell fate determination (sensu Insecta); IMP. DR GO; GO:0007308; P:oocyte construction; IMP. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR001452; SH3. DR InterPro; IPR002017; Spectrin. DR Pfam; PF00036; efhand; 2. DR Pfam; PF00018; SH3; 1. DR Pfam; PF00435; spectrin; 22. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000012; EF-hand; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00054; EFh; 2. DR SMART; SM00326; SH3; 1. DR SMART; SM00150; SPEC; 20. DR PROSITE; PS00018; EF_HAND; 2. DR PROSITE; PS50002; SH3; 1. KW Cytoskeleton; Membrane; Erythrocyte; Repeat; Actin-binding; KW Calcium-binding; SH3 domain; 3D-structure; Cell shape; KW Calmodulin-binding; Actin capping. FT REPEAT 18 122 SPECTRIN 1. FT REPEAT 123 228 SPECTRIN 2. FT REPEAT 229 334 SPECTRIN 3. FT REPEAT 335 440 SPECTRIN 4. FT REPEAT 441 546 SPECTRIN 5. FT REPEAT 547 651 SPECTRIN 6. FT REPEAT 652 757 SPECTRIN 7. FT REPEAT 758 863 SPECTRIN 8. FT REPEAT 864 969 SPECTRIN 9. FT REPEAT 970 1043 SPECTRIN 10. FT REPEAT 1044 1151 SPECTRIN 11. FT REPEAT 1152 1257 SPECTRIN 12. FT REPEAT 1258 1363 SPECTRIN 13. FT REPEAT 1364 1469 SPECTRIN 14. FT REPEAT 1470 1576 SPECTRIN 15. FT REPEAT 1577 1682 SPECTRIN 16. FT REPEAT 1683 1788 SPECTRIN 17. FT REPEAT 1789 1894 SPECTRIN 18. FT REPEAT 1895 2001 SPECTRIN 19. FT REPEAT 2002 2115 SPECTRIN 20. FT REPEAT 2116 2229 SPECTRIN 21. FT REPEAT 2230 2335 SPECTRIN 22. FT CA_BIND 2278 2289 EF-HAND 1 (POTENTIAL). FT CA_BIND 2321 2332 EF-HAND 2 (POTENTIAL). FT DOMAIN 970 1029 SH3. FT CONFLICT 110 110 Q -> D (IN REF. 3). FT CONFLICT 1555 1555 Q -> H (IN REF. 4). FT CONFLICT 1668 1668 Q -> R (IN REF. 1). FT HELIX 1393 1422 FT HELIX 1428 1494 FT TURN 1495 1495 SQ SEQUENCE 2415 AA; 278301 MW; F1F72FB990EB0A37 CRC64; MENFTPKEVK ILETVEDIQE RREQVLSRYN DFKIETRQKR EKLEDSRRFQ YFKRDADELE SWIHEKLQAA SEESYRDPTN LQAKIQKHQA FEAEVSAHSN AIVSLDNTGQ EMINQQHFAS ESIQVRLDEL HKLWELLLSR LAEKGLKLQQ ALVLVQFLRQ CEEVMFWIKD KETFVTADEF GQDLEHVEVL QRKFDEFQKD MASQEYRVTE VNQLADKLVQ DGHPERDTIT KRKEELNEAW QRLKQLAIVR QEKLFGAHEI QRFNRDADET VAWIAEKDVV LSSDDYGRDL ASVQALQRKH EGVERDLAAL EDKVSTLGAE AQRLCSIHAD HSDQIRDKQA EIANYWQSLT TKARERKQKL DESYYLHRFL ADFRDLVSWI NGMKAIISAD ELAKDVAGAE ALLERHQEHK GEIDAREDSF KLTTESGQKL LEREHYAAAE IQEKLAALEN DKSSLLSLWE DRRILYEQCM DLQLFYRDTE QADTWMAKQE AFLANEDLGD SLDSVEALIK KHEDFEKSLA AQEEKIKALD IFATKLIDGQ HYAADDVAQR RQMLLARRAA LQEKSSKRRQ LLEDSNRYQQ FERDCDETKG WISEKLKFAT DDSYLDPTNL NGKMQKHQNF EHELNANKSR IEDITNVGTE LIEKQHYAAD QINTRMQEIV VLWETLVQAS DKKGTKLNEA CQQQQFNRTI EDIELWLSEI EGQLLSEDHG KDLTSVQNLQ KKHALLEADV MAHQDRIESI KVAANKFIES GHFDADNIRN KEGNLSARYA ALAAPMGERK QHLLDSLQVQ QLFRDLEDEA AWIREKEPIA ASTNRGRDLI GVQNLIKKHQ AVLAEINNHE ARLLNVISSG ENMLKDQPFA SDDIRQRLEA LQEQWNTLKE KSSQRKQDLD DSLQAHQYFA DANEAESWMR EKEPIATGSD YGKDEDSSEA LLKKHEALVS DLEAFGNTIQ ALQEQAKNCR QQETPVVDIT GKECVVALYD YTEKSPREVS MKKGDVLTLL NSNNKDWWKV EVNDRQGFVP AAYIKKIDAG LSASQQNLVD NHSIAKRQNQ INSQYDNLLA LARERQNKLN ETVKAYVLVR EAADLAQWIR DKENHAQIAD VVGEDLEEVE VLQKKFDDFN DDLKANEVRL ANMNEIAVQL TSLGQTEAAL KIQTQMQDLN EKWNNLQTLT AEKASQLGSA HEVQRFHRDI DETKDWIAEK ANALNNDDLG KDLRSVQTLQ RKHEGVERDL AALRDKIRQL DETANRLMQS HPDTAEQTYA KQKEINEMWD QIITKSTARK EKLLDSYDLQ RFLSDYRDLL AWINSMMSLV TSDELANDVT GAEALIERHQ EHRTEIDARA GTFGAFEQFG NELLQANHYA SPEIKEKIED LAKAREDLEK AWTERRLQLE QNLDLQLYMR DCELAESWMS AREAFLNADD DANAGGNVEA LIKKHEDFDK AINGHEQKIA ALQTVADQLI AQNHYASNLV DEKRKQVLER WRHLKEGLIE KRSRLGDEQT LQQFSRDADE IENWIAEKLQ LATEESYKDP ANIQSKHQKH QAFEAELAAN ADRIQSVLAM GGNLIDKKQC SGSEDAVQKR LTQIADQWEY LTHKTTEKSL KLKEANKQRT YIAAVKDLDF WLGEVESLLT TEDSGKDLAS VQNLMKKHQL VEADIVAHED RIKDMNNQAD SLVESGQFDT AGIQEKRQSI NERYERICNL AAHRQARLNE ALTLHQFFRD IADEESWIKE KKLLVGSDDY GRDLTGVQNL KKKHKRLEAE LGSHEPAIQA VQEAGEKLMD VSNLGVPEIE QRLKALNQAW AELKNLAATR GQKLDESLTY QQFLAQVEEE EAWITEKQQL LSVEDYGDSM AAVQGLLKKH DAFETDFTAH KDRCSLICDQ GSELVEAKNH HGESIAQRCQ QLRLKLDNLS ALAARRKGAL LDNSAYLQFM WKADVVESWI DDKENYVRSD EFGRDLSTVQ TLLTKQETFD AGLNAFEQEG IHNITALKDQ LINASHAQSP AILKRHGDVI ARWQKLRDAS NTRKDRLLAM QEQFRQIEEL YLTFAKKASA FNSWFENAEE DLTDPVRCNS IEEIRALRDA HAQFQASLSS AEADFKALAA LDQKIKSFNV GPNPYTWFTM EALEETWRNL QKIIEERDGE LAKEAKRQEE NDKLRKEFAK HANLFHQWLT ETRTSMMEGS GSLEQQLEAL RVKATEVRAR RVDLKKIEEL GALLEEHLIL DNRYTEHSTV GLAQQWDQLD QLSMRMQHNL EQQIQARNHS GVSEDSLKEF SMMFKHFDKD KSGKLNHQEF KSCLRALGYD LPMVEEGQPD PEFEAILDVV DPNRDGYVSL QEYIAFMISK ETENVQSYEE IENAFRAITA ADRPYVTKEE LYCNLTKDMA DYCVQRMKPF SEPRSGQPIK DALDYIDFTR TLFQN // ID SPCB_DROME STANDARD; PRT; 2291 AA. AC Q00963; Q9VX30; DT 01-APR-1993 (Rel. 25, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Spectrin beta chain. GN BETA-SPEC OR SPEC-B OR CG5870. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92335263; PubMed=1631106; RA Byers T.J., Brandin E., Lue R., Winograd E., Branton D.; RT "The complete sequence of Drosophila beta-spectrin reveals RT supra-motifs comprising eight 106-residue segments."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6187-6191(1992). RN [2] RP SEQUENCE OF 1-800 FROM N.A. RX MEDLINE=90009037; PubMed=2677025; RA Byers T.J., Husain-Chishti A., Dubreuil R.R., Branton D., RA Goldstein L.S.B.; RT "Sequence similarity of the amino-terminal domain of Drosophila beta RT spectrin to alpha actinin and dystrophin."; RL J. Cell Biol. 109:1633-1641(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP CHARACTERIZATION. RX MEDLINE=88059242; PubMed=3680372; RA Dubreuil R., Byers T.J., Branton D., Goldstein L.S.B., Kiehart D.P.; RT "Drosophilia spectrin. I. Characterization of the purified protein."; RL J. Cell Biol. 105:2095-2102(1987). RN [5] RP STRUCTURE BY NMR OF 2145-2262. RX MEDLINE=96164435; PubMed=8591029; RA Zhang P., Talluri S., Deng H., Branton D., Wagner G.; RT "Solution structure of the pleckstrin homology domain of Drosophila RT beta-spectrin."; RL Structure 3:1185-1195(1995). CC -!- FUNCTION: SPECTRIN IS THE MAJOR CONSTITUENT OF THE CYTOSKELETAL CC NETWORK UNDERLYING THE ERYTHROCYTE PLASMA MEMBRANE. IT ASSOCIATES CC WITH BAND 4.1 AND ACTIN TO FORM THE CYTOSKELETAL SUPERSTRUCTURE OF CC THE ERYTHROCYTE PLASMA MEMBRANE. INTERACTS WITH CALMODULIN IN A CC CALCIUM-DEPENDENT MANNER. CC -!- SUBUNIT: NATIVE SPECTRIN MOLECULE IS A TETRAMER COMPOSED OF TWO CC ANTIPARALLEL HETERODIMERS JOINED HEAD TO HEAD SO THAT EACH END CC OF THE NATIVE MOLECULE INCLUDES THE C-TERMINUS OF THE ALPHA CC SUBUNIT AND THE N-TERMINUS OF THE BETA SUBUNIT. CC -!- SIMILARITY: BELONGS TO THE SPECTRIN FAMILY. CC -!- SIMILARITY: CONTAINS 2 CALPONIN-HOMOLOGY (CH) DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- SIMILARITY: CONTAINS 17 SPECTRIN REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M92288; AAA28399.1; -. DR EMBL; AE003506; AAF48751.1; -. DR PIR; A46147; A46147. DR PDB; 1DRO; 03-APR-96. DR FlyBase; FBgn0003471; beta-Spec. DR GO; GO:0045169; C:fusome; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0045170; C:spectrosome; IDA. DR GO; GO:0008017; F:microtubule binding; IDA. DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP. DR InterPro; IPR001589; Actbind_actnin. DR InterPro; IPR001715; Calponin-like. DR InterPro; IPR001849; PH. DR InterPro; IPR002017; Spectrin. DR InterPro; IPR001605; Spectrin_PH. DR Pfam; PF00307; CH; 2. DR Pfam; PF00169; PH; 1. DR Pfam; PF00435; spectrin; 17. DR PRINTS; PR00683; SPECTRINPH. DR SMART; SM00033; CH; 2. DR SMART; SM00233; PH; 1. DR SMART; SM00150; SPEC; 17. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS50003; PH_DOMAIN; 1. KW Cytoskeleton; Membrane; Calmodulin-binding; Actin-binding; Repeat; KW 3D-structure; Actin capping. FT DOMAIN 1 271 ACTIN-BINDING (BY SIMILARITY). FT DOMAIN 50 154 CH 1. FT DOMAIN 169 271 CH 2. FT REPEAT 298 408 SPECTRIN 1. FT REPEAT 418 522 SPECTRIN 2. FT REPEAT 524 633 SPECTRIN 3. FT REPEAT 635 739 SPECTRIN 4. FT REPEAT 741 844 SPECTRIN 5. FT REPEAT 846 950 SPECTRIN 6. FT REPEAT 952 1057 SPECTRIN 7. FT REPEAT 1059 1167 SPECTRIN 8. FT REPEAT 1169 1273 SPECTRIN 9. FT REPEAT 1275 1378 SPECTRIN 10. FT REPEAT 1380 1485 SPECTRIN 11. FT REPEAT 1487 1591 SPECTRIN 12. FT REPEAT 1593 1697 SPECTRIN 13. FT REPEAT 1699 1804 SPECTRIN 14. FT REPEAT 1806 1910 SPECTRIN 15. FT REPEAT 1912 2016 SPECTRIN 16. FT REPEAT 2018 2078 SPECTRIN 17. FT DOMAIN 2147 2259 PH. FT CONFLICT 2278 2278 D -> Y (IN REF. 2). FT STRAND 2150 2157 FT TURN 2166 2167 FT STRAND 2173 2179 FT STRAND 2185 2187 FT HELIX 2192 2195 FT TURN 2197 2198 FT STRAND 2206 2206 FT STRAND 2215 2216 FT TURN 2224 2225 FT STRAND 2226 2230 FT STRAND 2236 2240 FT HELIX 2245 2258 FT TURN 2259 2259 SQ SEQUENCE 2291 AA; 265737 MW; 5CDFB0C548BBC39B CRC64; MTTDISIVRW DPSQGPGNEY IDEYEYDGGN SSSRLFERSR IKALAEERES VQKKTFTKWV NSHLCRVNCR IADLYVDMRD GKHLIKLLEV LSGERLPKPT KGKMRIHCLE NVDKALQFLR EQRVHLENIG SHDIVDGNAS LNLGLIWTII LRFQIQDITI EEVDNKETKS AKDALLLWCQ MKTAGYHNVN VRNFTTSWRD GLAFNAIIHK HRPDLVQFEK LSKTNAIHNL NNAFDVAEDK LGLAKLLDAE DVFVEHPDEK SIITYVVTYY HYFSKLKQET VQGKRIGKVV GIAMENDKMV HDYENFTSDL LKWIETTIQS LGEREFENSL AGVQGQLAQF SNYRTIEKPP KFVEKGNLEV LLFTLQSKMR ANNQKPYTPK EGKMISDINK AWERLEKAEH ERELALREEL IRQEKLEQLA ARFDRKASMR ETWLSENQRL VSQDNFGFDL AAVEAAAKKH EAIETDIFAY EERVQAVVAV CDELESERYH DVKRILLRKD NVMRLWTYLL ELLRARRMRL EISLQLQQNF QEMLYILDNM EEIKQLLMTD DYGKHLMGVE DLLQKHSLVE ADINILGERV KVVVQNSQKF LSDDPESYKP CDPEIIVSRV QQLEDAYAEL VRLAVERRSR LEESRKLWQF YWDTADEENW IKEKEQIVST DEVGHDLTTV NLMLSKHKAL ESEITSHDPQ LQNVAKVGSE LITEGHFGAD RIKDRLKEIL NKWDHLLDLT KYRRQRLENA VEYFQLFADA DDVDNWMLDT LRIVSSEDVG RDEANVQSLL KKHKDVADEL KNYAEVIDAL HKQAESLKLN EAEKANVDKR LEAIDNRYKE LTELAKLRKQ RLLDALSLYK LMSEADGVEQ WIKEKTKMLD TMTPGKDIED VEIMKHRFEG FDKEMNANAS RVAVVNQLAR QLLHVEHPNS DEILERQNHL NQEWSTLREK AEAKMDDLKS AHGVQTFYIE CRETISWIED KKRILTETDS LEMDLTGVMT LQRRLSGMDR DLAAIQAKLS SLEREANSIE DEHPEEAKII RERIAQIELI WEQLTQMLKE RDSKLEEAGD LHRFLRDLDH FQTWLTKTQT DVASEDTPTS LPEAEKLLNQ HQSIREEIDN YTEDYKNMME YGERLTSEGS TSDDPQYMFL RERLNALKDG WEELHQMWEN RQVLLSQSLD QQLFNRDARQ TEVLLSQQEH FLSKDDTPVN LEQAENQLKR HEAFLTTMEA NDDKINTLLQ VADTLVEKDH FDADKIGKRA ENITGRRDDN RQRALDQHEK LKNQVKLHEF LQDLEELAEW VQEKYATSQD ESYRSAKTIH SKWTRHQAFE AEIAANKERL FEAEKSAQEL SKEKPEFKDV IEPKLKELAK QFDDLEVHTK EKGAMLFDAN REVLVQQTCD DIDSYITDLE KQIVSGDTAN DLTSVNILMQ KQQVIQTQMA VKARQVEEID KQTEYLQKTV PEEKIEPIVV KKTAVLERFE KIKAPLLERQ KALEKKKEAF QFCRDVEDEK LWIDEKLPVA NSPDYGNSLF NVHVLKKKNQ SLATEIDNHE PRINAICNNG RKLIDEGHED AKKFEALISD LTQKWQELKD AIENRRKHLL ESEKVQQYFF DAQEAESWMS EQELYMMVED RGKDEISAQN LMKKHENLEQ SVEDYANTIR QLGEVARQFS GDDISSGDAV AVKQSQLDKL YAGLKDLAGE RRARLNEALQ LFMLSREVDD LEQWITDREV VAGSQELGQD FDHVTLLSER FNEFARDTEA VGGERVAKVN GIADNLIQAG HSDSATIAEW KDNLNESWQD LLELIETRTQ MLAASRELHK FFHDCKDVLG RILEKQHGVS DELGRDAGSV STLQRKHYNF LQDLITLYSQ VQQIQEESAK LQDAYAGDKA KEITNREQEV LHAWDNLQAM CDARKQKLAD TGDLFRFFNM VRILMIWMED LVRQMNTSEK PRDVSGVELL MNNHQSLKAE IDTREDNFGA CISLGKELLT RNHYASADIK DRLMTLSNSR NALLRRWEER WENLQLILEV YQFARDAAVA EAWLIAQEPY LLSSELGHTI DEVENLIKKH EAFEKSAAAQ EERFSALERL TTFELKEMKR RQELAEEAER QRIKEEQEAK AASEAAEQAK REAERRDDVD VGASHDDSER GGTPGAGEGH EGYVTRKHEW DSTTKKASNR SWDKVYMAAK AGRISFYKDQ KGYKSNPELT FRGEPSYDLQ NAAIEIASDY TKKKHVLRVK LANGALFLLQ AHDDTEMSQW VTSLKAQSDS TAVAASRSQT LPATSQKDEP KRRSFFTLKK K // ID SPEN_DROME STANDARD; PRT; 5560 AA. AC Q8SX83; Q9NHN1; Q9NJ17; Q9U6C3; Q9VPL1; Q9VPL2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Split ends protein. GN SPEN OR CG18497. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 3 AND 4), FUNCTION, ALTERNATIVE PROMOTER RP USAGE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTANTS E9 AND RP D57. RC TISSUE=Embryo; RX MEDLINE=20025936; PubMed=10556062; RA Wiellette E.L., Harding K.W., Mace K.A., Ronshaugen M.R., Wang F.Y., RA McGinnis W.; RT "spen encodes an RNP motif protein that interacts with Hox pathways RT to repress the development of head-like sclerites in the Drosophila RT trunk."; RL Development 126:5373-5385(1999). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 4). RC TISSUE=Embryo; RX MEDLINE=20157049; PubMed=10655223; RA Rebay I., Chen F., Hsiao F., Kolodziej P.A., Kuang B.H., Laverty T., RA Suh C., Voas M., Williams A., Rubin G.M.; RT "A genetic screen for novel components of the Ras/mitogen-activated RT protein kinase signaling pathway that interact with the yan gene of RT Drosophila identifies split ends, a new RNA recognition motif- RT containing protein."; RL Genetics 154:695-712(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=20171275; PubMed=10704397; RA Kuang B.H., Wu S.C.-Y., Shin Y.-A., Luo L., Kolodziej P.A.; RT "split ends encodes large nuclear proteins that regulate neuronal RT cell fate and axon extension in the Drosophila embryo."; RL Development 127:1517-1529(2000). RN [4] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE OF 424-2002 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [7] RP FUNCTION. RX MEDLINE=20253107; PubMed=10790398; RA Lane M.E., Elend M., Heidmann D., Herr A., Marzodko S., Herzig A., RA Lehner C.F.; RT "A screen for modifiers of cyclin E function in Drosophila RT melanogaster identifies Cdk2 mutations, revealing the insignificance RT of putative phosphorylation sites in Cdk2."; RL Genetics 155:233-244(2000). RN [8] RP FUNCTION ON EGF RECEPTOR PATHWAY. RX MEDLINE=20414403; PubMed=10959845; RA Chen F., Rebay I.; RT "split ends, a new component of the Drosophila EGF receptor pathway, RT regulates development of midline glial cells."; RL Curr. Biol. 10:943-946(2000). RN [9] RP FUNCTION ON WG PATHWAY. RX MEDLINE=22668876; PubMed=12783785; RA Lin H.V., Doroquez D.B., Cho S., Chen F., Rebay I., Cadigan K.M.; RT "Splits ends is a tissue/promoter specific regulator of Wingless RT signaling."; RL Development 130:3125-3135(2003). CC -!- FUNCTION: PROBABLE COREPRESSOR PROTEIN, WHICH REGULATES DIFFERENT CC KEY PATHWAYS SUCH AS THE EGF RECEPTOR AND WG PATHWAYS. INVOLVED IN CC NEURONAL CELL FATE, SURVIVAL AND AXON GUIDANCE, CELL CYCLE CC REGULATION AND REPRESSION OF HEAD IDENTITY IN THE EMBRYONIC TRUNK. CC MAY ACT WITH THE HOX GENE DEFORMED AND THE EGF RECEPTOR SIGNALING CC PATHWAY. POSITIVE REGULATOR OF THE WG PATHWAY IN LARVAL TISSUES CC BUT NOT IN EMBRYONIC TISSUES. MAY ACT AS A TRANSCRIPTIONAL CC COREPRESSOR PROTEIN, WHICH REPRESS TRANSCRIPTION VIA THE CC RECRUITMENT OF LARGE COMPLEXES CONTAINING HISTONE DEACETYLASE CC PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter; CC Comment=2 isoforms, 1 (shown here) and 2, are produced by use of CC alternative promoters; CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8SX83-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8SX83-2; Sequence=VSP_008565, VSP_008566; CC Note=No experimental confirmation available; CC Name=3; Synonyms=SpenL; CC IsoId=Q8SX83-3; Sequence=VSP_008567; CC Note=Produced by alternative splicing of isoform 1; CC Name=4; Synonyms=SpenS; CC IsoId=Q8SX83-4; Sequence=VSP_008565, VSP_008566, VSP_008567; CC Note=Produced by alternative splicing of isoform 2; CC -!- TISSUE SPECIFICITY: UBIQUITOUS. EXPRESSED PRIOR TO CELLULARIZATION CC IN STAGE 3 EMBRYOS, AND IN BLASTODERM CELLS, INCLUDING POLE CELLS. CC EXPRESSED THROUGHOUT THE REST OF EMBRYOGENESIS. LATER, IT IS CC EXPRESSED AT HIGHER LEVEL IN EPIDERMAL CELLS AND CNS. CC -!- DEVELOPMENTAL STAGE: ISOFORM 3 IS EXPRESSED BOTH MATERNALLY AND CC ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE SPEN FAMILY. CC -!- SIMILARITY: CONTAINS 3 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -!- SIMILARITY: CONTAINS 1 SPOC DOMAIN. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-7 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF188205; AAF13218.1; -. DR EMBL; AF184612; AAF26299.1; -. DR EMBL; AF221715; AAF34661.1; ALT_INIT. DR EMBL; AE003590; AAF51534.2; -. DR EMBL; AE003590; AAF51535.2; -. DR EMBL; AE003590; AAN10511.1; -. DR EMBL; AY094788; AAM11141.1; ALT_SEQ. DR HSSP; P09651; 1HA1. DR FlyBase; FBgn0016977; spen. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0008347; P:glia cell migration; IMP. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 3. DR SMART; SM00360; RRM; 3. DR PROSITE; PS50102; RRM; 3. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. DR PROSITE; PS50917; SPOC; 1. KW Transcription regulation; Repressor; Developmental protein; KW Nuclear protein; Repeat; RNA-binding; Coiled coil; KW Alternative promoter usage; Alternative splicing. FT DOMAIN 554 632 RNA-BINDING (RRM) 1. FT DOMAIN 656 730 RNA-BINDING (RRM) 2. FT DOMAIN 734 806 RNA-BINDING (RRM) 3. FT DOMAIN 1449 1465 COILED COIL (POTENTIAL). FT DOMAIN 1902 2071 COILED COIL (POTENTIAL). FT DOMAIN 2732 2760 COILED COIL (POTENTIAL). FT DOMAIN 2925 2957 COILED COIL (POTENTIAL). FT DOMAIN 3026 3063 COILED COIL (POTENTIAL). FT DOMAIN 3905 3965 COILED COIL (POTENTIAL). FT DOMAIN 4465 4486 COILED COIL (POTENTIAL). FT DOMAIN 5393 5560 SPOC. FT DOMAIN 44 55 ASN-RICH. FT DOMAIN 440 538 SER-RICH. FT DOMAIN 823 939 SER-RICH. FT DOMAIN 1243 1260 HIS-RICH. FT DOMAIN 1356 1898 SER-RICH. FT DOMAIN 1709 1734 PRO-RICH. FT DOMAIN 1851 2013 LYS-RICH. FT DOMAIN 1924 2071 GLU-RICH. FT DOMAIN 3681 4114 GLN-RICH. FT DOMAIN 3804 3901 HIS-RICH. FT DOMAIN 4748 5078 GLN-RICH. FT VARSPLIC 1 57 Missing (in isoform 2 and isoform 4). FT /FTId=VSP_008565. FT VARSPLIC 58 59 LK -> MR (in isoform 2 and isoform 4). FT /FTId=VSP_008566. FT VARSPLIC 5167 5193 Missing (in isoform 3 and isoform 4). FT /FTId=VSP_008567. FT MUTAGEN 5471 5471 C->Y: IN E9; INDUCES HEAD-LIKE SKELETAL FT STRUCTURES IN THE TRUNK. FT MUTAGEN 5507 5507 G->D: IN D57; INDUCES HEAD-LIKE SKELETAL FT STRUCTURES IN THE TRUNK. FT CONFLICT 4074 4074 Q -> P (IN REF. 1). SQ SEQUENCE 5560 AA; 599996 MW; 58F19621AF40D2A8 CRC64; MFRCRNMVRD NSRNICFGKL AETTTTQQQQ QQQQFVVDSS TIINNNNNNN NNNNNQKLKR STEEPPTNSF ERNYYDRTTS RLVTQYQANN STSLANSNSS PSSVSASASV FATAAGGSSE RSRNRDRPYR NGSASVQGGG INSSNTTTTT AACTAGGSGS GAIGTGTGGL VGSGPGGVPQ ALGDRSSTQN IHQNHQSARV APPQSWYEAA TAATTAQLKS SGGSGNAGAS AAVGFTMSSS PINHHPHQHP HLQNPQHPHY TSSPVVGAGS CPSAAQGQPQ IQSQSQTTAV HRSVAYAGSA ADDLLNTATS RNMLLHSSKL NKLLKGAGAT GSGGERSGSE SPGRAGGATP LTTTSTITNN SFSSNSLNNT ITTATPTMPT IASGAAGSVG LGSGAEAGVC SNSGTASGDI LNVAAVLAAA VDNGVPTHPI RTRHNLHGRS TTSSSRSHSR SPSSYSSSHS SSSSSHSSSH SHASSPVQSS GNCAMAEGRS SRTVNSVTVT SNSSNPSGTA VTVSSAGVGG GCGSSSSSSS SSSSSGSSCL TANPVVHSED NRPLAIRVRN LPARSSDTSL KDGLFHEYKK HGKVTWVKVV GQNSERYALV CFKKPDDVEK ALEVSHDKHF FGCKIEVEPY QGYDVEDNEF RPYEAELDEY HPKSTRTLFI GNLEKDITAG ELRSHFEAFG EIIEIDIKKQ GLNAYAFCQY SDIVSVVKAM RKMDGEHLGS NRIKLGFGKS MPTNCVWIDG VDEKVSESFL QSQFTRFGAV TKVSIDRNRQ LALVLYDQVQ NAQAAVKDMR GTILRRKKLQ VDFASRECQD AFYDKQEKQQ QQSSGSNPRF SRYESSASSL QSRSRASSFS RHQNNSNDDC SPINTPGGAS SGISSASNLI NQSTSINISN IGTNACSAMP APSLASAVVS CNVNASGTVP ASTSMPSGVS SSSSSLPMSP AALAQRHRMV RNARQTVDCD FNEVGRLRFR SSEEVSGGAG NSTQFEDVRC DSPVTARQGS AVNCFTGPTA AVGESIDGTL NNNQITGGAE GFTGSGGSIL SRRRCGKTPK DLHPVHNQRI QLAEQVEECP SSGDEGVVSP RKRIKMDYHH HHHHSNASGV ESTGEHSSIN KPSPLLLSNC DVIHDPLNRK SEIRRVSETP SGSPSIKFPG HLPSAPQSLM LSCRRPSIDV GALSALSSSS AFRHGIVGAS SMDQQHMMNA SAAAKRRRVT TTMQQPSSSS TTNSSSGSGL GGISSLTPAD EYHHHVSRGR GHQLHSHHSH EASGGESADG SRPGTPLCDE RPEVLPTEPR RLPPPRERVR ERTRDVMWLP LPKFGVLFFQ QQQSRSSGGG GAGNSYLQQQ LGGGSTGGLG CIGAASSSAC SLNNSSLNAS QGMGSCSGST FLPSPSSRYW RSSSHHQNQQ NNHQQQSQQL HGSSSSNTCL MASPARPRSL SSNSSDSDVP GQNAGGSPSL DERLRNFEEN YERWSGGSSR EHISGHTPSS ATPSWQLSMH MNLSTGLNSH QTSSASGNSN SSSGTVSSSA SNSRHKFLDI DELQPSDIVK SVLAKKSVFD DDFQRLNKNQ WYDPSSSDFA LGSSSNIVTG SSLVANVSRH PGGPCSGNTS PALPNLAATK ATPIIGNCSG GLGNSTGSKS AGLLQRLSSL SPMNSPQASM SPYNSPSPSP SVGGVTACLG QLTKPAAPGT ASAGLSGGTA ASSSSPAANS GPTKGLQYPF PSHPPLPNTA APPPAVQPAP PPLPEMGKQS RLTGQSSGNN LTKSLSVPDG PQSSPARVQL QKSASVPGST NVGAPSSLSL DSTTASVETS ASISSSTSNG NSSLTSAAIH VQKPQQSTFV EEEHTKKSGT STSQSSSSSS KKISSTHDKL HSKHNNRSES DKKIKKSDKN ASSSDKRKNS STSQSSKSAT PRIEDDSSEA DDTADKAEKN QRHEKEKKER QEKREKDLRK QVEREEKDRK AQQEEREKED RKAKEEEKER EREKKAQEDR EKKEREEREL REKEQRDKEQ KEKEIREKDL REKEQRERDN REKELRDKDL REKEMREKEQ REKELHREKD QREREHREKE QSRRAMDVEQ EGRGGRMREL SSYQKSKMDI AGEASSLTAI DCQHNKENAM DTIAQGTPGA SPSTPSDNTP KERSRKLSRN SPVRLHKRRL SSQESNHSAG GGGSCGGSSH QIHHEDYVKR IRMENSQNIS VHSSNQRLND RRDSKEHKSS SFKEDKNSSS HISRPHGCGG SSASSSKHHH RRDKHHQKGS ASSIETNSSI EVVVDPISQT KHNLNTSEEE LQSHQPKREK EREHFSSHAN SSSSRHKSKR DHHHHREKKR HSVAESTNTD EEHTPQQHNP HRRISAAGSG SAGELSSAAT NTSSGKLHHQ HHRRSVERKS SRGSDEGHHS SSKSLRAKLM MLSSADSDDT DDASKKHSIF DIPDDCPNVS MYDKVKARSC KNMQRQAEEK KIKAKFSQLK QSRAKKKRST SYDGDSDTEF EDRQHRNSGS SSFHGRYPGL SSSDDDDDEE THQRRISSDS DAEHGGQDNQ GASTLADANR VRQMQQNLRR LCDGDDSSED EIRRNVMKHS HFGKRNSNST RIASDSESQS QPAPDLTIKQ EHPIAPAQEI KREQLSDEEQ KFKSRHDSNS SIEERKLKTE REIKTELGDF YNSSEYTYTG KLKEYSPETR KKHKKSKRRL KSSSTADTSA AQTPLVMTPL TPSIFDVHSS SECKTKFDNF DDLKTECSSI PLEISAGERR KHKERKEKKR EKLRNMTEAT VPNSPTTNDT SSEKLSKEER HRLKKSKKSK SMDNSCNTKI YNSSGAHPST SPSLPATPTS APSTAQTSKR GEDKMEFIFG IISDEEESQF PEQAETNKDI IPSSVSTTGP IVSAALQTYK QEPSTPNSKN EEAHIQLTVH EPEQQQQLER SRLSGGSSSS SHADRERHRR EKREKKRREK SQREQQNQIH QKSSKVETKV DDDNSVDMDE AGRALEAQLM SDFDTKPISE EATPSTAATY RSDMTDVFRF SDNEDNNSVD MTKQGVKSEQ QEQHKSKDKK KKKKRSKEEK QEKLLQQQRR ESLPNVASTS SAPPTPGKLT VNVQAASKHA DLQLDAKHIS SPPVCKPSPS LPCLIGDDDD DALHTPKAKP TTPSSRGNDG LTPSREKPRL ISPIPKTPTI ANSSTLSTQS AETPVSSGTV ISSSALATTP TSSTAAGVSA APGLDNSPTS ASAQCKKKES FIPGFDGQLD DRISESAVQS ISAEFNSTSL LDNIADEPKI PVASPPRATK PLDKLEESKS RVTISQEETE SAVSALLGES FGTSSTTDYS LDGMDEMSSV NELETPTLVI AEPDEEAALA AKAIETAGEP ASILEEPEME PEREAEPDPD PEAEIESEPV VEVLDPEELN KAVQSLKHED MMDIKADTPQ SERDLQIDTD TEENPDEADS SGPSLKIDET VQSSSSPEKS ISNNSPTPRE TANIDIPNVE SQPKLSNEST PQPSVITKLP FLDTPKTVPA GLPPSPVKIE PPTISKLQQP LVQPVQTVLP APHSTGSGIS ANSVINLDLS NVISSCSNTS AASATASASA SISFGSPTAS QNAMPQASTP KQGPITPQQA IRTQSLIMQP PTISIPEQTP HFAVPQMVLS PQSHHPQQPG TYMVGIRAPS PHSPLHSPGR GVAQSRLVGQ LSPVGRPMVS QPSPQQQVQQ TQQQHALITS PQSSNISPLA SPTTRVLSSS NSPTTSKVNS YQPRNQQVPQ QPSPKSVAEV QTTPQLMTIP LQKMTPIQVP HHPTIISKVV TVQPQQATQS QVASSPPLGS LPPHKNVHLN AHQNQQQPQV IAKMTAHQHQ QHMQQFMHQQ MIQRQQHMQQ QQLHGQSQQI TSAPQHQMHQ QHQAQQQQQH HNQQHLNQQL HAQQHPTQKQ HQAQQQFNQQ IQQHQSQQQH QVQQQNQAQQ QHLSQQQHQS QQQLNQQHQA QQQQLQQIQK LQQMHGPQQQ QKSPQGVGHL GGSTSIFASQ QHNSQLPARG VPQQQHPQQL SHSSPCKPNT LVSVNQGVQP PAILTRVGSH SQPNQQQQLP HQQSSSGHPH QKQLSSPGAN LPLQTPLNVI QNTPKIIVQQ HIVAQNQVPP PQTQGNAIHY PQNQGKDSTP PGHVEPTPAM SAQKTSESVS VIRTPTPTTG LAVISANTVG SLLTEENLIK ISQPKQDELI EQDSKEVDSD YWSAKEVNID SVIKKLDTPL ASKDAKRAVE MQAIAPAPIP NPQPGNQSMA QETALPTTSM SVNNSNDHDT EDETETRQLP PAKPPIPTVG RPPGRGGSAK RGRQPRGAKK VGGFPLNSVT AAPPGVDSLV VQPGDNGVQT RLRKPVTAPV TRGRKGRPPR NLLLQQQQLQ QQQLDIQRKG MEMVTSATSS TPLPTPIPTS SVLTAAEKKA RNQALTQAQE QNQVASQVGT GQDIYEFHED GGEEPKPKTI SSVAPSAEDQ RPRLILTINK TQPSIKNISE MEQTIQQQQQ QQSEVISNTD PIGGDNSESC NTRKSRRLQE KEDRSTVDDI IEDVVRNTNT PTGTGPHLPK GAQTPPRRSG RNAQAKKTDA VQIINAVGRP RRSKDRKTIG EQTANLIEEV TASNATVAAS HLAPPEGAGV ESHVPQLDAK EVEPVSVVTP ISTPAPVSVA APVTVPVPAM VPVKPTMPQH PKKKAIAAAE IESYQAINSS IPSGGLPMHQ TAAPATQKIT GGVADAVSKA LVDPVTGVIT AGMPQGKEGN LPAATAAAPA NSSNEDGQAA PPPQLQHQQQ QQHPQQPPQQ QANLQINTTL IPSGLPNPIT ALGKSVQLET SAAALLNKPV SVLVKGNASQ VIQQQQPQIV APAKQPIILQ QNPLPTVLHH AQHTTVRPPQ PLKAHVLNRE KNIQQQLTPT KQAVAQPPQH APHSGHMLLT DTAGNQQLVQ PQIIARHLQQ QQHLQVNVPP PTAHSPHSPR IPSQQQQLGP GASISPQQQQ PQTVVIKQAA SAAQPQILHV VSSKASVVPQ PQQQQLPPTS STGPHLQLAK PNYSYAPTVL TPTLPAVQQQ QQQHLYKQNN QQKGAQIQMP PHGIIMPTHP GMLLQQKLPA HLQPQQHQLN PSPPPGKPNP VLHGLQSGQI MPGSVGSPPP VSAAVLKTAQ QQVNSVVPVA GIRTAIPNIS PQSQPRVSPL VLPPGISGVP PFDASLHDLG AYVSGRRTQS PPPAHQQASP ITPNDSTYRG VTASRDFMLY QHHLMRGGDY DDKMGSSPPL ELRRPGSGPP RTIAVPHSLQ SPQDRTAADS PQMAQVYVHN TRIPPAHFSE IASRGLYDSG ALQLEPPPAH RPTATISVVV PQQMPAVSSG SPFIGRDGSV QPGSHHHPGK AMDMQLDEMD RMSMIAAVVQ QQQEHLPPAL PAGMELASQQ APPAMAPPPG DSLVTLLQRY PVMWQGLLAL KTDQAAVQMH FVHGNPNVAR ASLPSLVETN TPLLRIAQRM RLEQTQLEGV AKKMQVDKEH CMLLALPCGR DHADVLQHSR NLQTGFITYL QQKMAAGIVN IPIPGSEQAA YVVHIFPSCD FANENLERAA PDLKNRVAEL AHLLIVIATV // ID SPIT_DROME STANDARD; PRT; 230 AA. AC Q01083; Q9VIT4; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein Spitz precursor. GN SPI OR CG10334. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92354912; PubMed=1644292; RA Rutledge B.J., Zhang K., Bier E., Jan Y.N., Perrimon N.; RT "The Drosophila spitz gene encodes a putative EGF-like growth factor RT involved in dorsal-ventral axis formation and neurogenesis."; RL Genes Dev. 6:1503-1517(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=95134691; PubMed=7833286; RA Freeman M.; RT "The spitz gene is required for photoreceptor determination in the RT Drosophila eye where it interacts with the EGF receptor."; RL Mech. Dev. 48:25-33(1994). RN [4] RP SUBCELLULAR LOCATION, AND PROCESSING. RX MEDLINE=21526628; PubMed=11672524; RA Lee J.R., Urban S., Garvey C.F., Freeman M.; RT "Regulated intracellular ligand transport and proteolysis control EGF RT signal activation in Drosophila."; RL Cell 107:161-171(2001). RN [5] RP REVIEW. RX MEDLINE=21650354; PubMed=11790319; RA Klaembt C.; RT "EGF receptor signalling: roles of Star and Rhomboid revealed."; RL Curr. Biol. 12:R21-R23(2002). CC -!- FUNCTION: LIGAND FOR THE EGF RECEPTOR (GURKEN). INVOLVED IN A CC NUMBER OF UNRELATED DEVELOPMENTAL CHOICES, FOR EXAMPLE, DORSAL- CC VENTRAL AXIS FORMATION, GLIAL MIGRATION, SENSORY ORGAN CC DETERMINATION, AND MUSCLE DEVELOPMENT. IT IS REQUIRED FOR CC PHOTORECEPTOR DETERMINATION. CC -!- SUBUNIT: INTERACTS WITH STAR VIA THE LUMENAL DOMAIN. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN; FOUND IN THE CC ENDOPLASMIC RETICULUM. RELOCALIZATION TO THE GOLGI APPARATUS AND CC THE PLASMA MEMBRANE IS MEDIATED BY STAR. IN THE PRESENCE OF CC RHOMBOID, SPITZ IS FOUND ONLY IN THE GOLGI, NOT AT THE CELL CC SURFACE. CC -!- TISSUE SPECIFICITY: EXPRESSED THROUGHOUT THE EMBRYO. CC -!- PTM: PROTEOLYTIC PROCESSING BY RHOMBOID OCCURS IN THE GOLGI. CC CLEAVAGE TAKES PLACE WITHIN THE TRANSMEMBRANE DOMAIN CLOSE TO CC RESIDUE 144 AND THE ACTIVE GROWTH FACTOR IS RELEASED. CC -!- PTM: N-GLYCOSYLATED AND O-GLYCOSYLATED. CC -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95199; AAA28894.1; -. DR EMBL; AE003663; AAF53831.1; -. DR PIR; A44074; A44074. DR HSSP; P01132; 1EGF. DR FlyBase; FBgn0005672; spi. DR GO; GO:0005783; C:endoplasmic reticulum; IDA. DR GO; GO:0005794; C:Golgi apparatus; IGI. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0005155; F:epidermal growth factor receptor activating...; NAS. DR GO; GO:0007173; P:EGF receptor signaling pathway; NAS. DR GO; GO:0007438; P:oenocyte development; IGI. DR GO; GO:0045742; P:positive regulation of EGF receptor signali...; NAS. DR GO; GO:0045470; P:R8-mediated photoreceptor organization; NAS. DR GO; GO:0007432; P:salivary gland determination; NAS. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006210; IEGF. DR Pfam; PF00008; EGF; 1. DR SMART; SM00181; EGF; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. KW Neurogenesis; Developmental protein; Transmembrane; Signal; KW Glycoprotein; EGF-like domain; Endoplasmic reticulum; Golgi stack. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 230 PROTEIN SPITZ. FT DOMAIN 18 139 LUMENAL (POTENTIAL). FT TRANSMEM 140 160 POTENTIAL. FT DOMAIN 161 230 CYTOPLASMIC (POTENTIAL). FT DOMAIN 61 66 POLY-THR. FT DOMAIN 74 118 EGF-LIKE. FT DOMAIN 182 185 POLY-ASP. FT DISULFID 78 93 BY SIMILARITY. FT DISULFID 87 106 BY SIMILARITY. FT DISULFID 108 117 BY SIMILARITY. FT CARBOHYD 70 70 N-LINKED (GLCNAC...). SQ SEQUENCE 230 AA; 25967 MW; F830F4D2C51C15E2 CRC64; MSVQHGLVAL VLIGCLAHPW HVEACSSRTV PKPRSSISSS MSGTALPPTQ APVTSSTTMR TTTTTTPRPN ITFPTYKCPE TFDAWYCLND AHCFAVKIAD LPVYSCECAI GFMGQRCEYK EIDNTYLPKR PRPMLEKASI ASGAMCALVF MLFVCLAFYL RFEQRAAKKA YELEQELQQE YDDDDGQCEC CRNRCCPDGQ EPVILERKLP YHMRLEHALM SFAIRRSNKL // ID SPRI_DROME STANDARD; PRT; 1790 AA. AC Q8MQW8; Q8MQV9; Q8T4E9; Q9BK48; Q9BK49; Q9W2T4; Q9W2T7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein Sprint (SH2 poly-proline containing Ras-interactor protein). GN SPRI OR GN CG33175/CG12638/CG15297/CG15298/CG15299/CG15300/CG15301/CG32674. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RX MEDLINE=21152914; PubMed=11231087; RA Szabo K., Jekely G., Rorth P.; RT "Cloning and expression of sprint, a Drosophila homologue of RIN1."; RL Mech. Dev. 101:259-262(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORMS 2 AND 3). RC STRAIN=Berkeley; TISSUE=Embryo, and Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: POTENTIAL RAS EFFECTOR PROTEIN. MAY FUNCTION AS A CC GUANINE NUCLEOTIDE EXCHANGE (GEF), BY EXCHANGING BOUND GDP FOR CC FREE GTP (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Sprint-a, A; CC IsoId=Q8MQW8-1; Sequence=Displayed; CC Name=2; Synonyms=Sprint-b, B; CC IsoId=Q8MQW8-2; Sequence=VSP_007621, VSP_007622; CC Name=3; Synonyms=C; CC IsoId=Q8MQW8-3; Sequence=VSP_007623, VSP_007624, VSP_007625; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: IN LATE CELLULAR BLASTODERM EMBRYOS, IT IS CC EXPRESSED IN THE POSTERIOR END. THEN, AS DEVELOPMENT PROCEEDS, IT CC IS EXPRESSED IN THE DEVELOPING MIDGUT, AMNIOSEROSA AND IN A CC SPECIFIC SUBSET OF CNS NEURONS. ISOFORM 1 IS EXPRESSED EARLIER IN CC DEVELOPING MIDGUT AND AMNIOSEROSA, BUT IS NOT EXPRESSED IN THE CC CNS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE RIN (RAS INTERACTION/INTERFERENCE) CC FAMILY. CC -!- SIMILARITY: CONTAINS 1 RAS-ASSOCIATING DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 VPS9 DOMAIN. CC -!- CAUTION: REF.2 (AAF46604) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF312692; AAK28059.1; -. DR EMBL; AF312693; AAK28060.1; -. DR EMBL; AE003450; AAF46601.2; -. DR EMBL; AE003450; AAO41647.1; -. DR EMBL; AE003451; AAF46604.1; ALT_SEQ. DR EMBL; AY089220; AAL89958.1; -. DR EMBL; AY122253; AAM52765.1; -. DR EMBL; AY122263; AAM52775.1; -. DR HSSP; P08631; 3HCK. DR FlyBase; FBgn0030216; spri. DR InterPro; IPR000159; RA_domain. DR InterPro; IPR000980; SH2. DR InterPro; IPR003123; VPS9. DR Pfam; PF00788; RA; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF02204; VPS9; 1. DR PRINTS; PR00401; SH2DOMAIN. DR ProDom; PD000093; SH2; 1. DR SMART; SM00314; RA; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00167; VPS9; 1. DR PROSITE; PS50200; RA; 1. DR PROSITE; PS50001; SH2; 1. KW GTPase activation; SH2 domain; Developmental protein; KW Alternative splicing. FT DOMAIN 474 567 SH2. FT DOMAIN 1567 1670 VPS9. FT DOMAIN 1690 1778 RAS-ASSOCIATING. FT DOMAIN 35 57 THR-RICH. FT DOMAIN 86 115 ASN-RICH. FT DOMAIN 296 362 ASN-RICH. FT DOMAIN 1145 1155 GLN-RICH. FT DOMAIN 95 115 POLY-ASN. FT DOMAIN 296 305 POLY-ASN. FT DOMAIN 329 334 POLY-ASN. FT VARSPLIC 1 14 Missing (in isoform 2). FT /FTId=VSP_007621. FT VARSPLIC 15 267 LASDLDIMLNDLRSAPSHAATATATATTTATIATATATATT FT TTNRQQQHHNHHNQQQMQSRQLHAHHWQSINNNKNNNVSNN FT NNNNNNNNNNINNNNNNNNHSAHPPCLIDIKLKSSRSAATK FT ITHTTTANQLQQQQRRRVAPKPLPRPPRRTRPTGQKEVGPS FT EEDGDTDASDLANMTSPLSASAAATRINGLSPEVKKVQRLP FT LWNARNGNGSTTTHCHPTGVSVQRRLPIQSHQQRILNQRFH FT HQRMHHG -> MSHETAAAAVPGGAGASAGSIVSCAENASK FT VEVIVYTTKSDKTLKQNMNAKDDTLRKRTSLIIVPQQVHDI FT EVEDEDTKKVDQTKVRENPNRNSTASMDSCVSNTTSQSNQS FT SGSSSSTTSSSGSSSGSEDAHAAYQDLQNGNAGQDLNSPSP FT VPRCHSSSSTSSVSESTSCSSSADYSLREQLKNFANRNSEG FT GGTIDSTARLIKGMSLPVGDQSVQSVAPALCDSLLSPQEVP FT LGRRYAEVAQFKGHPKAR (in isoform 2). FT /FTId=VSP_007622. FT VARSPLIC 1 463 Missing (in isoform 3). FT /FTId=VSP_007623. FT VARSPLIC 1407 1407 H -> E (in isoform 3). FT /FTId=VSP_007624. FT VARSPLIC 1408 1790 Missing (in isoform 3). FT /FTId=VSP_007625. FT CONFLICT 46 48 IAT -> V (IN REF. 2; AAF46604). FT CONFLICT 57 57 T -> A (IN REF. 2; AAF46604). FT CONFLICT 93 95 VSN -> ISNK (IN REF. 2; AAF46604). FT CONFLICT 284 284 S -> A (IN REF. 1 AND 4). FT CONFLICT 304 304 H -> N (IN REF. 1 AND 4). FT CONFLICT 370 370 S -> I (IN REF. 1 AND 4). FT CONFLICT 601 601 L -> S (IN REF. 1 AND 4). FT CONFLICT 1037 1037 K -> Q (IN REF. 1 AND 4). FT CONFLICT 1380 1380 G -> A (IN REF. 1 AND 4). FT CONFLICT 1545 1545 Y -> N (IN REF. 1). FT CONFLICT 1570 1570 L -> F (IN REF. 1). SQ SEQUENCE 1790 AA; 193390 MW; ECEA1CC2869E6B39 CRC64; MVNAVMDAIA LLSSLASDLD IMLNDLRSAP SHAATATATA TTTATIATAT ATATTTTNRQ QQHHNHHNQQ QMQSRQLHAH HWQSINNNKN NNVSNNNNNN NNNNNNINNN NNNNNHSAHP PCLIDIKLKS SRSAATKITH TTTANQLQQQ QRRRVAPKPL PRPPRRTRPT GQKEVGPSEE DGDTDASDLA NMTSPLSASA AATRINGLSP EVKKVQRLPL WNARNGNGST TTHCHPTGVS VQRRLPIQSH QQRILNQRFH HQRMHHGTSE PIPSGVATPS SLDSASVDGG KSHTGNNNNI NNNHNGQQSQ KSQQQAGLAA KLNVLAQSNL NNNNTTNQPG SMTPASNRTG LDSNQNQKQN LNADSRRSSS VDPDADADDV VDAAHGGAFE DDMQALLPKC SRRSRDELSQ SRTSLVSSSE GGILAEGETS SEDDEEEPVE AEDEGEESSR DSSDNSPPCD LGLMERLLVT HPMWFLPGIQ RSGAVHLLQG KEEGTFIVRG SSQPNTMAVS VRLPQDTGPY IEHYLIQSHD NVLSLESSRF TFGSIPSLIA HYAQCCDELP VQLMLPRVLR EANNRKKLSS LALLGQEFWS YVSSPALLGP LTPSVAPSKD QQLLDAKSPL SLTETSGLGT ATFFSDTVSK PPPTGAPPLP GGGLFSPTGS GQLLGFFSQA GTPSDTTNSS LSSFTTSGGQ HMQLLSPNSV DSVILTMSPV DNPGHYLPGS TGAPMAPLCP SVVDQQLSTF KVAQTAPEVD QVRPQRPKPP NTLNLKPPAP PLRWSKPHSP DQNGSANGNF TVTTTVTFSM ENGGGGGSGP TVGNGNGKFV EVTTPAASNP FNALLNGQAS TFQTFAKRLS PEGECKDTLS SQGSSSNDSR WPPPARKLLT SPMTPLTPSG GSSSSGGKSR KSRAGKESQH YKESDILESP PMQYCASALS DKISDYEDVW SHDPSDRASL LTSFRPALDT VGGVMNRRPD LLAETPSTPT PTQQSHLTPC EEETTATPNE SSSQSLLQFS GDVPARSRAG LLLPNLSGQV PPVAMTKSMT AAEDDGGDTT PTAEGQANGA SRSKQGSPFY AEPADALRQA GLTSAATAIL RRQHRSQMLH ASQRHSEPLK AGFGGSGNGA MLQPSDLEKL AGSLDELKPK PKVSQQQQQS QQQQQPTKRA RNRIDHWQLD SSWEFMAKQD TGSHAGGDYD TAAIDWQEKE NSLGRDSRAD GQGKKRTLTI HQIIANRLPD LNLPELVRCS TPPQTAALQP HVLGQDKAGV GCDGSQKSFQ SQIGCRLSSY DNVFCQNSFG GIDSAQSDDG TIFSEPWDSS QWDTFLPHDD ATINSDTIHL SKCRPALSED DTIVEELQST KDGSNGSCNQ DTLKANRNGA GHHKLNNGNG NGKANNRPKV ATILRNPSMR DREVLCHPRN KMSIQSSGPG DSLRAYTLQL AQDPSSTFAR NIENFICCTK ESREAAPQVV MRNMRQFMSG MKNYLVKHGE GKFHAELETA RARLKSDEFL NLDAMLETVM HQLVVLPLRE HLYGIFVDHY QRSEDIQLLA QNVRYACERE AADFGIRPTV TPPSQAALRL IANLLWRLQE AELPLDKLEL FLCVISTVFD ATGCPRGQQL GADDFLPVLV YVVAKCGFVG AEIEAEFMWG LLQPTLLNGE PGYYLTALCS AVQVLKTFMA SEGESGSGSL DWRSSCLPAC SSVLRVIIPD ECNGSLQTRT LPVRPHTTTR EVCRIIAHKA RITNPQDYAL FKLVDGEETL LTDAECPQDA RLAAKGKHCM LAYKRIDAKI AWPTAQLAGH // ID SPY_DROME STANDARD; PRT; 589 AA. AC O44783; Q9VZP7; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein sprouty (Spry). GN STY OR CG1921. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98117253; PubMed=9458049; RA Hacohen N., Kramer S., Sutherland D., Hiromi Y., Krasnow M.A.; RT "Sprouty encodes a novel antagonist of FGF signaling that patterns RT apical branching of the Drosophila airways."; RL Cell 92:253-263(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=99387981; PubMed=10457022; RA Reich A., Sapir A., Shilo B.-Z.; RT "Sprouty is a general inhibitor of receptor tyrosine kinase RT signaling."; RL Development 126:4139-4147(1999). RN [4] RP FUNCTION. RX MEDLINE=99244704; PubMed=10226010; RA Kramer S., Okabe M., Hacohen N., Krasnow M.A., Hiromi Y.; RT "Sprouty: a common antagonist of FGF and EGF signaling pathways in RT Drosophila."; RL Development 126:2515-2525(1999). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=99189751; PubMed=10089881; RA Casci T., Vinos J., Freeman M.; RT "Sprouty, an intracellular inhibitor of Ras signaling."; RL Cell 96:655-665(1999). CC -!- FUNCTION: INHIBITOR OF TRACHEAL BRANCHING THAT RESTRICTS BRANCH CC BUDDING BY ANTAGONIZING THE BNL-FGF PATHWAY (BNL: BRANCHLESS, AN CC FGF INDUCER OF BRANCHING). ACTS AS AN ANTAGONIST OF EGFR-MEDIATED CC SIGNALING IN THE EYE (WHERE IT IS IMPORTANT FOR CELL CC DETERMINATION) MIDLINE GLIA, CHORDOTONAL ORGANS, WING AND OVARIAN CC FOLLICLE CELLS. CC -!- SUBUNIT: INTERACTS WITH DRK AND GAP1 PROTEIN OF THE RAS PATHWAY. CC -!- SUBCELLULAR LOCATION: ASSOCIATED WITH THE INNER SURFACE OF THE CC PLASMA MEMBRANE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE EMBRYONIC TRACHEAL SYSTEM, CC DEVELOPING EYE IMAGINAL DISK, EMBRYONIC CHORDOTONAL ORGAN CC PRECURSORS, MIDLINE GLIA, WING DISK AND OVARY. CC -!- DEVELOPMENTAL STAGE: FROM STAGE 7 OF OOGENESIS FOUND IN THE CC POSTERIOR FOLLICLE CELLS AND DURING STAGE 9 WHEN THE FOLLICLE CC CELLS MIGRATE POSTERIORLY OVER THE OOCYTE NUCLEUS, EXPRESSION IS CC SEEN IN THE DORSAL AND LATERAL CELLS, AND IS EXCLUDED FROM THE CC VENTRAL CELLS. ONCE THE MIGRATION OF FOLLICLE CELLS IS COMPLETE CC EXPRESSED IN THE DORSAL-ANTERIOR CORNER OF THE EGG CHAMBER. CC -!- INDUCTION: BY THE BNL-FGF PATHWAY IN THE TRACHEAL SYSTEM AND BY CC THE EGF RECEPTOR PATHWAY IN THE WING IMAGINAL DISK AND THE CC FOLLICLE CELLS OF THE OVARY. CC -!- DOMAIN: THE CYS-RICH DOMAIN IS RESPONSIBLE FOR THE LOCALIZATION OF CC THE PROTEIN TO THE PLASMA MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE SPROUTY FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF039842; AAC04257.1; -. DR EMBL; AE003478; AAF47772.1; -. DR FlyBase; FBgn0014388; sty. DR GO; GO:0005622; C:intracellular; NAS. DR InterPro; IPR007875; Sprouty. DR Pfam; PF05210; Sprouty; 1. KW Developmental protein; Membrane. FT DOMAIN 104 135 SER-RICH. FT DOMAIN 148 162 ASN-RICH. FT DOMAIN 207 271 GLN-RICH. FT DOMAIN 378 501 CYS-RICH. FT DOMAIN 492 551 GLY-RICH. FT DOMAIN 249 262 POLY-GLN. FT DOMAIN 503 514 POLY-GLY. FT CONFLICT 38 38 N -> T (IN REF. 1). FT CONFLICT 262 262 Q -> QQQ (IN REF. 1). FT CONFLICT 312 312 P -> L (IN REF. 1). SQ SEQUENCE 589 AA; 62388 MW; 7450E11987B17B20 CRC64; MDRRNGGDPL APPRPPKLLP RVHRPRAPEP TLSGVDHNAG ATASALASGA SSAAPVAIHN NNSQQQLSIS AAASNNNTIS IIPASPDFDD YQIHHLTFLP QRPSSLSRNS STASSTTATG ISVSGSGSVS GSSSSFTRRR PPAPVPLNNS ISNNNNNSIN NNFLSHFQSA EPASNALGQP PASPVTLAQP RPESERLTNE YVDTPLQHAT RSQHPAGQQD NGQTTTHHLL LLPQRNQHLH LQQHQQHLQQ QQQQQQQQQQ QQHLQHQQNQ QHARLATTTQ ATSVGSDHTD GLLHSHLQNS TTKPPASKQP APPRLGMGLG LGLGLGLNQP IITKQPTPAT QKERMHALEE LLQPGGAGGN GGPLVMAGDP SLLNPIVCPR CGRCRCEQCQ SPRPLPQTWV CNKTCLCSAE SVIDYASCLC CAKALFYHCA RDNDLDCDDG NGTPCVDNPC SCGPYKRTQR WGWLGALSIF LPCLWFYWPM RGCMKLCEKC YGRFAGRGCR CQGIGGGGAG SGGGVGSIGS TSSMLPIVPL GVNGSGLGGG VSLSGGVTDG GLNQANGKAM DHGCSAARSI LRKGDLTPEK RLLDSSPDY // ID SPZ_DROME STANDARD; PRT; 326 AA. AC P48607; Q95SU5; Q9VB84; DT 01-FEB-1996 (Rel. 33, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Spaetzle protein precursor. GN SPZ OR CG6134. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Embryo; RX MEDLINE=94170368; PubMed=8124709; RA Morisato D., Anderson K.V.; RT "The spatzle gene encodes a component of the extracellular signaling RT pathway establishing the dorsal-ventral pattern of the Drosophila RT embryo."; RL Cell 76:677-688(1994). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Oregon-R; TISSUE=Embryo; RA DeLotto Y., Smith C., DeLotto R.; RT "Multiple isoforms of the spatzle protein are encoded by alternatively RT spliced maternal mRNAs in the precellular blastoderm Drosophila RT embryo."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (ISOFORM 8.19). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM 8.23). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPONENT OF THE EXTRACELLULAR SIGNALING PATHWAY THAT CC ESTABLISHES THE DORSAL-VENTRAL PATHWAY OF THE DROSOPHILA EMBRYO. CC PROTEOLYTIC PROCESSING, LOCALIZED ON THE VENTRAL SIDE OF THE CC EMBRYO, APPEARS TO PRODUCE AN ACTIVE (ISOFORM 11.7), VENTRALLY- CC LOCALIZED FORM OF SPAETZLE, A POSSIBLE LIGAND FOR THE MEMBRANE CC PROTEIN TOLL. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=8.19; CC IsoId=P48607-1; Sequence=Displayed; CC Name=8.20; CC IsoId=P48607-2; Sequence=VSP_004420; CC Name=8.23; Synonyms=11.6; CC IsoId=P48607-3; Sequence=VSP_004418; CC Name=8.24; CC IsoId=P48607-4; Sequence=VSP_004418, VSP_004425, VSP_004427, CC VSP_004428; CC Name=8.29; CC IsoId=P48607-5; Sequence=VSP_004419, VSP_004424; CC Name=11.27; CC IsoId=P48607-6; Sequence=VSP_004422, VSP_004426; CC Name=11.32; CC IsoId=P48607-7; Sequence=VSP_004418, VSP_004423; CC Name=11.5; CC IsoId=P48607-8; Sequence=VSP_004421; CC Name=11.7; Synonyms=23 kDa; CC IsoId=P48607-9; Sequence=VSP_004422; CC -!- TISSUE SPECIFICITY: EXPRESSED IN OVARIES AND EARLY EMBRYOS. CC ISOFORM 11.7 IS FIRST DETECTED AFTER 1H OF EGG LAYING. CC -!- PTM: ISOFORM 11.7 MAY BE THE RESULT OF PROCESSING BY THE PROTEASE CC EASTER. CC -!- MISCELLANEOUS: 'SPAETZLE' MEANS 'NOODLES' IN GERMAN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05850; AAA17887.1; -. DR EMBL; AF237964; AAF98123.1; -. DR EMBL; AF237965; AAF98124.1; -. DR EMBL; AF237966; AAF98125.1; -. DR EMBL; AF237967; AAF98126.1; -. DR EMBL; AF237968; AAF98127.1; -. DR EMBL; AF237969; AAF98128.1; -. DR EMBL; AF237970; AAF98129.1; -. DR EMBL; AF237971; AAF98130.1; -. DR EMBL; AF237972; AAF98131.1; -. DR EMBL; AF237973; AAF98132.1; -. DR EMBL; AF237974; AAF82745.1; -. DR EMBL; AE003759; AAF56658.1; -. DR EMBL; AY060478; AAL25517.1; -. DR PIR; A53190; A53190. DR FlyBase; FBgn0003495; spz. DR GO; GO:0005576; C:extracellular; IDA. DR GO; GO:0005121; F:Toll binding; IGI. DR GO; GO:0006966; P:antifungal humoral response (sensu Inverteb...; IMP. DR GO; GO:0006967; P:antifungal polypeptide induction; IMP. DR GO; GO:0045087; P:innate immune response; NAS. DR GO; GO:0007310; P:oocyte dorsal/ventral axis determination; IEP. DR GO; GO:0008063; P:Tl signaling pathway; NAS. KW Developmental protein; Signal; Alternative splicing. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 326 SPAETZLE PROTEIN. FT VARSPLIC 23 48 Missing (in isoform 8.23, isoform 8.24 FT and isoform 11.32). FT /FTId=VSP_004418. FT VARSPLIC 23 67 YEAKEYERIIKELFTITNDEGVVLFNTSADSAPFMPIPTQH FT DDPT -> IVYINIELTKRHEAEVRAEKTVADYKALLATIN FT NGGPGKSASNHL (in isoform 8.29). FT /FTId=VSP_004419. FT VARSPLIC 23 121 Missing (in isoform 8.20). FT /FTId=VSP_004420. FT VARSPLIC 23 185 Missing (in isoform 11.5). FT /FTId=VSP_004421. FT VARSPLIC 49 121 Missing (in isoform 11.27 and isoform FT 11.7). FT /FTId=VSP_004422. FT VARSPLIC 65 189 Missing (in isoform 11.32). FT /FTId=VSP_004423. FT VARSPLIC 68 120 Missing (in isoform 8.29). FT /FTId=VSP_004424. FT VARSPLIC 101 121 Missing (in isoform 8.24). FT /FTId=VSP_004425. FT VARSPLIC 189 225 Missing (in isoform 11.27). FT /FTId=VSP_004426. FT VARSPLIC 197 226 THKLKNNFAKFFSNDLQPTDVSSRVGGSDE -> RRAIPLQ FT EHQEAGVPKKGLEGGRHLAVNCQ (in isoform FT 8.24). FT /FTId=VSP_004427. FT VARSPLIC 227 326 Missing (in isoform 8.24). FT /FTId=VSP_004428. FT CONFLICT 50 50 S -> T (IN REF. 2; AAF98130). FT CONFLICT 53 53 S -> T (IN REF. 2; AAF98124). FT CONFLICT 67 67 T -> P (IN REF. 1 AND 4). FT CONFLICT 75 75 N -> D (IN REF. 2; FT AAF98130/AAF98131/AAF98126). FT CONFLICT 99 99 F -> P (IN REF. 1). FT CONFLICT 147 147 S -> F (IN REF. 2; AAF98132). FT CONFLICT 163 163 R -> T (IN REF. 2; AAF98129). FT CONFLICT 172 172 C -> S (IN REF. 2; AAF98129). FT CONFLICT 197 197 T -> R (IN REF. 2; AAF98125). FT CONFLICT 206 206 K -> N (IN REF. 2; AAF98129). SQ SEQUENCE 326 AA; 37447 MW; 3252389129CFB1E0 CRC64; MMTPMWISLF KVLLLLFAFF ATYEAKEYER IIKELFTITN DEGVVLFNTS ADSAPFMPIP TQHDDPTQKQ KQNQNQSPIP ETNRHYHQYH SLIQPDQYFK VQRSPNGKLN LVFNDTFVSL QRTDTEVQSE QPIPPRHPSD TFVFPDSPIA KYRPPQSPAR PLRNDTKEHN PCAKDESQHL RNFCTNVDDY PDLSGLTHKL KNNFAKFFSN DLQPTDVSSR VGGSDERFLC RSIRKLVYPK KGLRADDTWQ LIVNNDEYKQ AIQIEECEGA DQPCDFAANF PQSYNPICKQ HYTQQTLASI KSDGELDVVQ NSFKIPSCCK CALKTG // ID SQD_DROME STANDARD; PRT; 345 AA. AC Q08473; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE RNA-binding protein squid (Heterogeneous nuclear ribonucleoprotein 40) DE (HNRNP 40). GN SQD OR HRP40. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=93279471; PubMed=7684991; RA Kelley R.L.; RT "Initial organization of the Drosophila dorsoventral axis depends on RT an RNA-binding protein encoded by the squid gene."; RL Genes Dev. 7:948-960(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92112968; PubMed=1730754; RA Matunis E.L., Matunis M.J., Dreyfuss G.; RT "Characterization of the major hnRNP proteins from Drosophila RT melanogaster."; RL J. Cell Biol. 116:257-269(1992). CC -!- FUNCTION: THIS PROTEIN IS A COMPONENT OF RIBONUCLEOSOMES. COULD BE CC NEEDED TO ORGANIZE A CONCENTRATION GRADIENT OF A DORSALIZING CC MORPHOGEN (DM) ORIGINATING IN THE GERMINAL VESICLE. AT LEAST ONE CC OF THE ISOFORMS IS ESSENTIAL IN SOMATIC TISSUES. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. IT IS POSSIBLE THAT CC SOME ISOFORMS ARE FOUND ONLY IN ONE OF THESE LOCATIONS. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=SqdS; Synonyms=HRP40.2; CC IsoId=Q08473-1; Sequence=Displayed; CC Name=SqdA; Synonyms=HRP40.1; CC IsoId=Q08473-2; Sequence=VSP_005876; CC Name=SqdB; CC IsoId=Q08473-3; Sequence=VSP_005877; CC -!- DISEASE: FEMALES WITH MUTATIONS IN SQD ARE STERILE AND LAY EGGS CC THAT DISPLAY ONLY DORSAL STRUCTURES. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S61875; AAB26988.1; -. DR EMBL; S62100; AAB26989.1; -. DR EMBL; S61875; AAB26989.1; JOINED. DR EMBL; X62637; CAA44503.1; -. DR EMBL; X62638; CAA44504.1; -. DR PIR; A47369; A47369. DR PIR; B41732; B41732. DR PIR; B47369; B47369. DR HSSP; P09651; 1HA1. DR FlyBase; FBgn0003498; sqd. DR GO; GO:0005717; C:chromatin; IDA. DR GO; GO:0016607; C:nuclear speck; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 2. KW RNA-binding; Nuclear protein; Ribonucleoprotein; Alternative splicing; KW Repeat. FT DOMAIN 56 138 RNA-BINDING (RRM) 1. FT DOMAIN 136 213 RNA-BINDING (RRM) 2. FT DOMAIN 221 337 GLY-RICH. FT VARSPLIC 286 345 DGYGYGGGFEGNGYGGGGGGGNMGGGRGGPRGGGGPKGGGG FT FNGGKQRGGGGRQQRHQPY -> GKYNKQQSSAQNNYYNNN FT TSSNYHQNKNNSNNYQQF (in isoform SqdA). FT /FTId=VSP_005876. FT VARSPLIC 286 322 Missing (in isoform SqdB). FT /FTId=VSP_005877. FT CONFLICT 169 169 L -> F (IN REF. 2). SQ SEQUENCE 345 AA; 36207 MW; A5CB61CA53E815C1 CRC64; MAENKQVDTE INGEDFTKDV TADGPGSENG DAGAAGSTNG SSDNQSAASG QRDDDRKLFV GGLSWETTEK ELRDHFGKYG EIESINVKTD PQTGRSRGFA FIVFTNTEAI DKVSAADEHI INSKKVDPKK AKARHGKIFV GGLTTEISDE EIKTYFGQFG NIVEVEMPLD KQKSQRKGFC FITFDSEQVV TDLLKTPKQK IAGKEVDVKR ATPKPENQMM GGMRGGPRGG MRGGRGGYGG RGGYNNQWDG QGSYGGYGGG YGGYGAGGYG DYYAGGYYNG YDYGYDGYGY GGGFEGNGYG GGGGGGNMGG GRGGPRGGGG PKGGGGFNGG KQRGGGGRQQ RHQPY // ID SR19_DROME STANDARD; PRT; 163 AA. AC P49963; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Signal recognition particle 19 kDa protein (SRP19). GN SRP19. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Samarkand; RX MEDLINE=98085976; PubMed=9426007; RA Lai C.Q., Langley C.H.; RT "A homologue of the 19 kDa signal recognition particle protein locus RT in Drosophila melanogaster."; RL Gene 203:59-63(1997). CC -!- FUNCTION: SIGNAL-RECOGNITION-PARTICLE ASSEMBLY, BINDS DIRECTLY CC TO 7S RNA AND MEDIATES BINDING OF THE 54 KDA SUBUNIT OF THE SRP. CC (BY SIMILARITY). CC -!- SUBUNIT: SIGNAL RECOGNITION PARTICLE CONSISTS OF A 7S RNA MOLECULE CC OF 300 NUCLEOTIDES AND SIX PROTEIN SUBUNITS: SRP72, SRP68, SRP54, CC SRP19, SRP14 AND SRP9 (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE SRP19 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U35682; AAA79181.1; -. DR FlyBase; FBgn0015298; Srp19. DR InterPro; IPR002778; SRP19. DR Pfam; PF01922; SRP19; 1. DR ProDom; PD006609; SRP19; 1. KW Signal recognition particle; RNA-binding; Ribonucleoprotein. FT DOMAIN 148 155 POLY-GLY. FT DOMAIN 156 163 BASIC REGION, POTENTIALLY INVOLVED IN FT RNA-BINDING. SQ SEQUENCE 163 AA; 18574 MW; 153F621F09D04E75 CRC64; MATGSHEKKL EPQHETQRYG AVGTRWICIY PAYINRKKTR QEGRRLPKEN CVDNPSYIEI RDAVSVSNLQ FLMENKKYCR ENSSEMEFRG RVRVQLRNVD GTLYNIDFPT RESIMLHIAS KIPQLKTRQN KSGDSYHQQS QPQSNASGSG GGGGGKKGKG KRR // ID SR42_DROME STANDARD; PRT; 517 AA. AC Q9V9J3; O18369; Q26297; Q94879; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase Src42A (EC 2.7.1.112) (Dsrc41). GN SRC42A OR SRC41 OR TK5 OR CG7873. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Canton-S; TISSUE=Pupae; RX MEDLINE=96268448; PubMed=8682295; RA Takahashi F., Endo S., Kojima T., Saigo K.; RT "Regulation of cell-cell contacts in developing Drosophila eyes by RT Dsrc41, a new, close relative of vertebrate c-src."; RL Genes Dev. 10:1645-1656(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 374-428 FROM N.A. RX MEDLINE=92008631; PubMed=1915852; RA Shishido E., Emori Y., Saigo K.; RT "Identification of seven novel protein-tyrosine kinase genes of RT Drosophila by the polymerase chain reaction."; RL FEBS Lett. 289:235-238(1991). RN [5] RP SEQUENCE OF 376-427 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). CC -!- FUNCTION: ESSENTIAL FOR CORRECT EYE MORPHOGENESIS (OMMATIDIAL R7 CC NEURON FORMATION), THIS REQUIRES THE RAS1/MAPK SIGNAL TRANSDUCTION CC PATHWAY. MAY BE INVOLVED IN THE REGULATON OF CYTOSKELETON CC ORGANIZATION AND CELL-CELL CONTACTS IN DEVELOPING OMMATIDIA. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- TISSUE SPECIFICITY: UBIQUITOUS IN EARLY EMBRYOS, IN STAGES 13-16 CC EXPRESSION IS SEEN IN VISCERAL MESODERM, HINDGUT, BRAIN, ANAL PADS CC AND VENTRAL GANGLIONS. IN LARVAE, EXPRESSION IS IN CNS, WING DISK, CC LEG DISK AND PHOTORECEPTOR PRECURSORS IN THE EYE-ANTENNA DISKS CC POSTERIOR TO THE MORPHOGENETIC FURROW. CC -!- DEVELOPMENTAL STAGE: IN EARLY EMBRYOS EXPRESSION IS VERY LOW, CC EXPRESSION INCREASES DURING EMBRYOGENESIS. ALSO EXPRESSED IN CC LARVAE AND PUPAE. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. SRC CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D42125; BAA07705.1; -. DR EMBL; AE003784; AAM68337.1; -. DR EMBL; AY058652; AAL13881.1; -. DR EMBL; S55977; AAB19907.1; -. DR EMBL; AJ002911; CAA05746.1; -. DR HSSP; P00523; 1SRL. DR FlyBase; FBgn0004603; Src42A. DR GO; GO:0005912; C:adherens junction; IDA. DR GO; GO:0004713; F:protein-tyrosine kinase activity; NAS. DR GO; GO:0007154; P:cell communication; IDA. DR GO; GO:0007456; P:eye morphogenesis (sensu Drosophila); IMP. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kin...; IGI. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW Transferase; Tyrosine-protein kinase; Developmental protein; KW ATP-binding; SH2 domain; SH3 domain. FT DOMAIN 63 124 SH3. FT DOMAIN 130 222 SH2. FT DOMAIN 248 504 PROTEIN KINASE. FT NP_BIND 254 262 ATP (BY SIMILARITY). FT BINDING 276 276 ATP (BY SIMILARITY). FT ACT_SITE 370 370 BY SIMILARITY. FT CONFLICT 65 65 A -> V (IN REF. 1). FT CONFLICT 376 376 V -> I (IN REF. 4 AND 5). FT CONFLICT 381 386 GNIVKI -> SNVVKM (IN REF. 4). SQ SEQUENCE 517 AA; 59069 MW; 1EF196E4D7AE61E9 CRC64; MGNCLTTQKG EPDKPADRIK LDDPPTIGVG VGVPQIPMPS HAGQPPEQIR PVPQIPESET AGANAKIFVA LYDYDARTDE DLSFRKGEHL EILNDTQGDW WLARSKKTRS EGYIPSNYVA KLKSIEAEPW YFRKIKRIEA EKKLLLPENE HGAFLIRDSE SRHNDYSLSV RDGDTVKHYR IRQLDEGGFF IARRTTFRTL QELVEHYSKD SDGLCVNLCK PCVQIEKPVT EGLSHRTRDQ WEIDRTSLKF VRKLGSGQFG DVWEGLWNNT TPVAIKTLKS GTMDPKDFLA EAQIMKKLRH TKLIQLYAVC TVEEPIYIIT ELMKHGSLLE YLQAIAGKGR SLKMQTLIDM AAQIAAGMAY LESQNYIHRD LAARNVLVGD GNIVKIADFG LARLIKEDEY EARVGARFPI KWTAPEAANY SKFSIKSDVW SFGILLTELV TYGRIPYPGM TNAEVLTQVE HGYRMPQPPN CEPRLYEIML ECWHKDPMRR PTFETLQWKL EDFYTSDQSD YKEAQAY // ID SR55_DROME STANDARD; PRT; 375 AA. AC P26686; Q24252; DT 01-AUG-1992 (Rel. 23, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Serine-arginine protein 55 (SRP55) (Enhancer of deformed) (52-kDa DE bracketing protein) (B52 protein). GN E(DFD) OR SR55 OR RS55 OR B52. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-14; 125-131 AND 136-147. RC STRAIN=CL; TISSUE=Embryo; RX MEDLINE=92011900; PubMed=1717489; RA Roth M.B., Zahler A.M., Stolk J.A.; RT "A conserved family of nuclear phosphoproteins localized to sites of RT polymerase II transcription."; RL J. Cell Biol. 115:587-596(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC TISSUE=Embryo; RX MEDLINE=91357476; PubMed=1885003; RA Champlin D.T., Frasch M., Saumweber H., Lis J.T.; RT "Characterization of a Drosophila protein associated with boundaries RT of transcriptionally active chromatin."; RL Genes Dev. 5:1611-1621(1991). RN [3] RP CHARACTERIZATION. RX MEDLINE=92159037; PubMed=1741384; RA Mayeda A., Zahler A.M., Krainer A.R., Roth M.B.; RT "Two members of a conserved family of nuclear phosphoproteins are RT involved in pre-mRNA splicing."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1301-1304(1992). RN [4] RP FUNCTION. RX MEDLINE=95021280; PubMed=7935465; RA Ring H.Z., Lis J.T.; RT "The SR protein B52/SRp55 is essential for Drosophila development."; RL Mol. Cell. Biol. 14:7499-7506(1994). CC -!- FUNCTION: ESSENTIAL FOR DEVELOPMENT. MAY HAVE A CRITICAL ROLE IN CC SPLICING OR IN CONTROLLING ALTERNATIVE SPLICE SITE USE OF AT LEAST CC SOME PRE-MRNA IN VIVO. NOT REQUIRED FOR ALL SPLICING. MAY PLAY A CC GENERAL ROLE IN THE CONDENSATION OR DECONDENSATION OF CHROMATIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR; ASSOCIATED WITH BOUNDARIES OF CC TRANSCRIPTIONALLY ACTIVE CHROMATIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P26686-1; Sequence=Displayed; CC Name=Short; CC IsoId=P26686-2; Sequence=VSP_005878; CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. CC -!- PTM: EXTENSIVELY PHOSPHORYLATED ON SERINE RESIDUES IN THE RS CC DOMAIN. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -!- SIMILARITY: BELONGS TO THE SR FAMILY OF SPLICING FACTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58720; CAA41556.1; -. DR EMBL; X62599; CAA44483.1; -. DR PIR; A40459; A40459. DR FlyBase; FBgn0004587; B52. DR GO; GO:0016607; C:nuclear speck; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Nuclear protein; Phosphorylation; mRNA splicing; RNA-binding; KW Repeat; Alternative splicing. FT INIT_MET 0 0 FT DOMAIN 3 73 RNA-BINDING (RRM) 1. FT DOMAIN 88 96 GLY-RICH (HINGE REGION). FT DOMAIN 119 192 RNA-BINDING (RRM) 2. FT DOMAIN 206 356 ARG/SER-RICH (RS DOMAIN). FT VARSPLIC 318 338 Missing (in isoform Short). FT /FTId=VSP_005878. FT CONFLICT 74 74 T -> S (IN REF. 1). FT CONFLICT 102 106 MISSING (IN REF. 1). FT CONFLICT 195 195 A -> R (IN REF. 1). FT CONFLICT 228 228 T -> S (IN REF. 1). FT CONFLICT 260 260 A -> R (IN REF. 1). FT CONFLICT 279 281 APV -> RSR (IN REF. 1). FT CONFLICT 293 293 S -> T (IN REF. 1). SQ SEQUENCE 375 AA; 42393 MW; 20BA327CB4A4194E CRC64; VGSRVYVGGL PYGVRERDLE RFFKGYGRTR DILIKNGYGF VEFEDYRDAD DAVYELNGKE LLGERVVVEP ARGTARGSNR DRYDDRYGGR RGGGGGRYNE KNKNSRSSSR YGPPLRTEYR LIVENLSSRV SWQDLKDYMR QAGEVTYADA HKQRRNEGVV EFASLSDMKT AIEKLDDTEL NGRRIHLVED RRGGASGGGG GSGRGRSRSS SSRSRSRSRR RSRSRRSTHS RSKSRSRSKS RGGRSKSKSP VKSRSRSRSA SNKSRDVSKS KSKSHSRTAP VSPKRERDSR SRSRSVSKRE SRSRSRSKSI HRDSRSRPPT VSFKSSFYKF TTMPFFCSDR SASAENKSRS RSRSRSASPK NGNASPDRNN ESMDD // ID SR64_DROME STANDARD; PRT; 552 AA. AC P00528; O18372; Q9VZA2; DT 21-JUL-1986 (Rel. 01, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine-protein kinase Src64B (EC 2.7.1.112) (Dsrc64). GN SRC64B OR SRC1 OR CG7524. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=86028179; PubMed=2996778; RA Simon M.A., Drees B., Kornberg T., Bishop J.M.; RT "The nucleotide sequence and the tissue-specific expression of RT Drosophila c-src."; RL Cell 42:831-840(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 249-552 FROM N.A. RX MEDLINE=84082064; PubMed=6317185; RA Hoffmann F.M., Fresco L.D., Hoffman-Falk H., Shilo B.-Z.; RT "Nucleotide sequences of the Drosophila src and abl homologs: RT conservation and variability in the src family oncogenes."; RL Cell 35:393-401(1983). RN [5] RP SEQUENCE OF 410-461 FROM N.A. RX MEDLINE=98401146; PubMed=9731193; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). CC -!- FUNCTION: MAY PLAY A ROLE IN THE DEVELOPMENT OF NEURAL TISSUE AND CC SMOOTH MUSCLE. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- TISSUE SPECIFICITY: AFTER THE FIRST 8 HR OF DEVELOPMENT, CC ACCUMULATES ALMOST EXCLUSIVELY IN NEURAL TISSUES SUCH AS THE CC BRAIN, VENTRAL NERVE CHORD, AND EYE-ANTENNAL DISKS, AND IN CC DIFFERENTIATING SMOOTH MUSCLE. CC -!- DEVELOPMENTAL STAGE: ABUNDANT IN EMBRYOS AND PUPAE, RARE IN LARVAE CC AND ADULTS. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. SRC CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11917; AAA28913.1; -. DR EMBL; AE003481; AAF47922.1; -. DR EMBL; AY051781; AAK93205.1; -. DR EMBL; K01043; AAA28489.1; -. DR EMBL; AJ002919; CAA05754.1; -. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0003501; Src64B. DR GO; GO:0007301; P:ovarian ring canal formation; IMP. DR GO; GO:0008335; P:ovarian ring canal stabilization; IMP. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW Kinase; Tyrosine-protein kinase; Proto-oncogene; Phosphorylation; KW Transferase; ATP-binding; SH3 domain; SH2 domain; KW Developmental protein. FT DOMAIN 95 156 SH3. FT DOMAIN 162 259 SH2. FT DOMAIN 284 537 PROTEIN KINASE. FT NP_BIND 290 298 ATP (BY SIMILARITY). FT BINDING 312 312 ATP (BY SIMILARITY). FT ACT_SITE 404 404 BY SIMILARITY. FT MOD_RES 434 434 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT CONFLICT 102 102 A -> S (IN REF. 1). FT CONFLICT 261 263 KPQ -> ASL (IN REF. 4). FT CONFLICT 266 269 MWDL -> TAAPDVGF (IN REF. 4). FT CONFLICT 272 272 E -> Q (IN REF. 4). FT CONFLICT 286 287 LL -> VV (IN REF. 4). FT CONFLICT 290 290 L -> V (IN REF. 4). FT CONFLICT 293 293 G -> R (IN REF. 4). FT CONFLICT 316 316 E -> A (IN REF. 4). FT CONFLICT 366 366 D -> N (IN REF. 4). FT CONFLICT 373 373 G -> D (IN REF. 4). FT CONFLICT 384 385 IA -> MH (IN REF. 4). FT CONFLICT 389 390 AS -> TT (IN REF. 4). FT CONFLICT 393 393 E -> Q (IN REF. 4). FT CONFLICT 400 400 L -> V (IN REF. 4). FT CONFLICT 406 407 AA -> TT (IN REF. 4). FT CONFLICT 435 435 C -> R (IN REF. 4). FT CONFLICT 460 460 K -> E (IN REF. 5). FT CONFLICT 471 471 M -> T (IN REF. 4). FT CONFLICT 484 484 M -> L (IN REF. 4). FT CONFLICT 507 507 F -> L (IN REF. 4). FT CONFLICT 536 536 F -> L (IN REF. 4). SQ SEQUENCE 552 AA; 63002 MW; 4A63CF4F16562864 CRC64; MGNKCCSKRQ DQELALAYPT GGYKKSDYTF GQTHINSSGG GNMGGVLGQK HNNGGSLDSR YTPDPNHRGP LKIGGKGGVD IIRPRTTPTG VPGVVLKRVV VALYDYKSRD ESDLSFMKGD RMEVIDDTES DWWRVVNLTT RQEGLIPLNF VAEERSVNSE DWFFENVLRK EADKLLLAEE NPRGTFLVRP SEHNPNGYSL SVKDWEDGRG YHVKHYRIKP LDNGGYYIAT NQTFPSLQAL VMAYSKNALG LCHILSRPCP KPQPQMWDLG PELRDKYEIP RSEIQLLRKL GRGNFGEVFY GKWRNSIDVA VKTLREGTMS TAAFLQEAAI MKKFRHNRLV ALYAVCSQEE PIYIVQEYMS KGSLLDFLRE GDGRYLHFED LIYIATQVAS GMEYLESKQL IHRDLAARNV LIGENNVAKI CDFGLARVIA DDEYCPKQGS RFPVKWTAPE AIIYGKFSIK SDVWSYGILL MELFTYGQVP YPGMHSREVI ENIERGFRMP KPTNHYFPDN IYQLLLQCWD AVPEKRPTFE FLNHYFESFS VTSEVPYREV QD // ID SRA_DROME STANDARD; PRT; 292 AA. AC Q9XZL8; Q9V391; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sarah protein (Nebula protein). GN SRA OR NLA OR CG6072. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA McCormick A.V., Goldberg M.L.; RT "Gene required for elongation of meiosis I spindle in Drosophila RT females."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR ELONGATION OF MEIOSIS I SPINDLE. CC -!- SIMILARITY: BELONGS TO THE DSCR1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF147700; AAD33987.1; -. DR EMBL; AE003712; AAF55285.1; -. DR EMBL; AY061194; AAL28742.1; -. DR FlyBase; FBgn0020250; sra. DR InterPro; IPR006931; Calcipressin. DR Pfam; PF04847; Calcipressin; 1. SQ SEQUENCE 292 AA; 31423 MW; 64F1BBF5F6EA6CF9 CRC64; MSDAAKSNNN ASADAPDPTT PDATGEADAA NAATPTTPRG NHNNNNSANG RSKNKLKSTQ NSSGGGSIDK LSPDQDIFIN AADGLPNQHP SLPKEGDVDS DTEPEVDADS FDDLPTSIIV TNIHSEVFAN PELKHAMEEL FRTFSESATF QWLRSFRRLR VNYDNAIAAA NARIKLHQYE FNKKTVITCY FAQPVTPVSN KNLQPPAPVK QFLISPPASP PAGWEPREEG EPLVNHDLLA ALASLTPGES HELHPQSEDQ PAIIVHTAML AETGPGLQVK APIVQTKCPE RA // ID SRF_DROME STANDARD; PRT; 450 AA. AC Q24535; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Serum response factor homolog (dSRF) (Blistered protein). GN BS OR SERF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=95324363; PubMed=7600954; RA Affolter M., Montagne J., Walldorf U., Groppe J.C., Kloter U., RA Larosa M., Gehring W.J.; RT "The Drosophila SRF homolog is expressed in a subset of tracheal RT cells and maps within a genomic region required for tracheal RT development."; RL Development 120:743-753(1994). CC -!- FUNCTION: MIGHT PLAY A ROLE IN THE PROPER FORMATION AND CC MAINTENANCE OF THE TRACHEA. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING SEVERAL PHASES OF EMBRYONIC CC DEVELOPMENT. IN THE EGG, BOTH THE RNA AND THE PROTEIN ARE MATERNAL CC IN ORIGIN AND SLOWLY DECREASE IN AMOUNT DURING GASTRULATION. AFTER CC GERM BAND RETRACTION, HIGH LEVELS OF ZYGOTIC EXPRESSION ARE CC OBSERVED IN A DISTINCT SUBSET OF PERIPHERAL TRACHEAL CELLS CC DISTRIBUTED THROUGHOUT THE EMBRYO AND LOW LEVELS IN SOMATIC CC MUSCLE. CC -!- SIMILARITY: CONTAINS 1 MADS-BOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X77532; CAA54670.1; -. DR PIR; S42825; S42825. DR HSSP; P11831; 1SRS. DR TRANSFAC; T03688; -. DR FlyBase; FBgn0004101; bs. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007430; P:terminal branching of trachea, cytoplasmic ...; IMP. DR InterPro; IPR002100; TF_MADSbox. DR Pfam; PF00319; SRF-TF; 1. DR PRINTS; PR00404; MADSDOMAIN. DR SMART; SM00432; MADS; 1. DR PROSITE; PS00350; MADS_BOX_1; 1. DR PROSITE; PS50066; MADS_BOX_2; 1. KW Transcription regulation; DNA-binding; Activator; Nuclear protein; KW Developmental protein. FT DOMAIN 167 221 MADS-box. FT DOMAIN 81 102 POLY-GLN. FT DOMAIN 357 360 POLY-GLY. SQ SEQUENCE 450 AA; 47777 MW; F49BF85ED597D3AE CRC64; MDPTRGDSRY NLNYSMRSIG LSLADPADMY GNPALGAGRP PSGGLLQNMG GVPPMQRPNP AAGAPPAPQC QTLHSPQHAS QQQQQQQQQQ QQHQQQQQQQ QQHPQQQRGL KRSGSDCYED HHRSSGGLTL QGLDNVASGA VDDSVDNYNP LPNKKSPPAN GKKTKGRVKI KMEYIDNKLR RYTTFSKRKT GIMKKAYELS TLTGTQVMLL VASETGHVYT FATRKLQPMI TSEAGKQLIQ TCLNSPDPPS VGGGDQRMSA TGFEETELSY NIADEDSKDD RSPTSSGNES DDSSDVEMPA EAAEVATKLP ASSKTEVSAP PAASCSAATA SSGHKTMPAL NYQTDTNSGP STSTAAGGGG SADSKYVYSA ASIANIPQKM LRQLIQSGHL QVHAEEDGNQ YVTIPLSSTA ANLIKSNKLT ASGSGASGSG TPVKNDASAD KPLTIKQEFD // ID SRP_DROME STANDARD; PRT; 779 AA. AC P52172; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Box A-binding factor (ABF) (Serpent protein) (GATA-binding factor-B) DE (Transcription factor GATA-B) (dGATA-B). GN SRP OR ABF. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94244465; PubMed=8187633; RA Abel T., Michelson A.M., Maniatis T.; RT "A Drosophila GATA family member that binds to Adh regulatory RT sequences is expressed in the developing fat body."; RL Development 119:623-633(1993). CC -!- FUNCTION: MAY FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR PROTEIN AND CC MAY PLAY A KEY ROLE IN THE ORGANOGENESIS OF THE FAT BODY. BINDS A CC SEQUENCE ELEMENT (5'-[TA]GATAA-3') FOUND IN THE LARVAL PROMOTERS CC OF ALL KNOWN ALCOHOL DEHYDROGENASE (ADH) GENES. ACTS AS A HOMEOTIC CC GENE DOWNSTREAM OF THE TERMINAL GAP GENE HKB TO PROMOTE CC MORPHOGENESIS AND DIFFERENTIATION OF ANTERIOR AND POSTERIOR CC MIDGUT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: INITIALLY OBSERVED IN THE ANALGEN OF CC THE ANTERIOR AND POSTERIOR MIDGUT AND THE CEPHALIC MESODERM. IT IS CC FOUND IN BOTH THE ENDODERMAL AND MESODERMAL GERM LAYERS AND FOR A CC BRIEF PERIOD DURING GASTRULATION IT IS EXPRESSED IN THE CC AMNIOSEROSA. DURING GERM BAND RETRACTION IT BECOMES RESTRICTED TO CC THE FAT BODY. CC -!- SIMILARITY: CONTAINS 1 GATA-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76217; CAA53807.1; -. DR PIR; S40382; S40382. DR HSSP; P17678; 1GAT. DR FlyBase; FBgn0003507; srp. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0016563; F:transcriptional activator activity; IDA. DR GO; GO:0046665; P:amnioserosa maintenance; IMP. DR GO; GO:0007492; P:endoderm development; NAS. DR GO; GO:0007503; P:fat body development; IEP. DR GO; GO:0007390; P:germ-band shortening; IMP. DR GO; GO:0008258; P:head involution; NAS. DR GO; GO:0007516; P:hemocyte development; IMP. DR GO; GO:0001710; P:mesoderm cell fate commitment; IMP. DR GO; GO:0045893; P:positive regulation of transcription, DNA-d...; IDA. DR InterPro; IPR000679; Znf_GATA. DR Pfam; PF00320; GATA; 1. DR PRINTS; PR00619; GATAZNFINGER. DR SMART; SM00401; ZnF_GATA; 1. DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1. DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1. KW Transcription regulation; Activator; DNA-binding; Zinc-finger; KW Nuclear protein; Developmental protein. FT ZN_FING 319 343 GATA-TYPE. FT DOMAIN 52 55 POLY-ALA. FT DOMAIN 62 71 POLY-ALA. FT DOMAIN 81 86 POLY-GLN. FT DOMAIN 132 137 POLY-GLY. FT DOMAIN 206 215 POLY-ALA. FT DOMAIN 254 257 POLY-GLY. FT DOMAIN 439 445 POLY-GLN. FT DOMAIN 482 487 POLY-GLN. FT DOMAIN 539 545 POLY-ASN. FT DOMAIN 550 557 POLY-ASN. FT DOMAIN 578 585 POLY-SER. FT DOMAIN 602 614 POLY-ALA. FT DOMAIN 700 714 POLY-GLN. FT DOMAIN 739 744 POLY-GLN. SQ SEQUENCE 779 AA; 82109 MW; 7D4AD12A241E986D CRC64; MTPTLRRPAR QQLAEQLCLC WLVAYSDCQW HSVRHAVPQP NTSPSPAAAP SAAAATTSAT PAAATAAAAA ATSPQSTPAP QLQQQQSGAS GSAPLELLGA TAAAVAAATA AVNGHNSSLE DGYGSPRSSH SGGGGGGTLP AFQRIAYPNS GSVERYAPIT NYRGQNDTWF DPLSYATSSS GQAQLGVGVG AGVVSNVIRN GRAISAANAA AAAAADGTTG RVDPGTFLSA SASLSAMAAE SGGDFYKPNS FNVGGGGRSK ANTSGAASSY SCPGSNATSA ATSAVASGTA ATAATTLDEH VSRANSRRLS ASKRAGLSCS NCHTTHTSLW RRNPAGEPVC NACGLYYKLH SVPRPLTMKK DTIQKRKRKP KGTKSEKSKS KSKNALNAIM ESGSLVTNCH NVGVVLDSSQ MDVNDDMKPQ LDLKPYNSYS SQPQQQLPQY QQQQQLVMAD QHSSAASSPH SMGSTSLSPS AMSHQHQTHP HQQQQQQLCS GWTCRPTQTT KCRRSTCSSI SSSNRAACST HPAHPLHLQH PSPTHQLHNN NNNNNSSLFN NNNNNNNSSS NENNNKLIQK YLQAQQLSSS SNSDSTSDHQ LLAQLLPNSI TAAAAAAAAA AAAAIKTEAL SLTSQANCST ASAGLMVTST PTTASSTLSS LSHSNIISLQ NPYHQAGMTL CKPTRPSPPY YLTPEEDEQP ALIKMEEMDQ SQQQQQQQQH QQQQHGEIML SRSASLDEHY ELAAFQRHQQ QQQQPEQQTA SLLGQHEQHV TNYAMHKFGV DRETVVKME // ID SRYA_DROME STANDARD; PRT; 530 AA. AC P07666; Q9VAB4; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serendipity locus alpha protein. GN SRY-ALPHA OR SRY-A OR CG17957. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=86089101; PubMed=3935797; RA Vincent A., Colot H.V., Rosbash M.; RT "Sequence and structure of the serendipity locus of Drosophila RT melanogaster. A densely transcribed region including a blastoderm- RT specific gene."; RL J. Mol. Biol. 186:149-166(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP CHARACTERIZATION. RX MEDLINE=90346291; PubMed=2166703; RA Schweisguth F., Lepesant J.-A., Vincent A.; RT "The serendipity alpha gene encodes a membrane-associated protein RT required for the cellularization of the Drosophila embryo."; RL Genes Dev. 4:922-931(1990). CC -!- FUNCTION: REQUIRED FOR THE CELLULARIZATION OF THE EMBRYO. INVOLVED CC IN THE LOCALIZATION OF THE ACTIN FILAMENTS JUST PRIOR TO AND CC DURING PLASMA MEMBRANE INVAGINATION. SRY-ALPHA TOGETHER WITH NULLO CC AND BNK MAY PROVIDE AUXILIARY FUNCTIONS, BY ACTING BOTH TO CC STABILIZE A LARGE AND DYNAMIC MICROFILAMENT STRUCTURE AND REGULATE CC ITS FUNCTIONS. CC -!- SUBCELLULAR LOCATION: INNER MEMBRANE-ASSOCIATED AND CYTOPLASMIC. CC COLOCALIZES WITH THE STRUCTURAL TRANSITIONS IN THE MICROFILAMENT CC NETWORK DURING CELLULARIZATION. CC -!- TISSUE SPECIFICITY: BLASTODERM. CC -!- DEVELOPMENTAL STAGE: TRANSCRIPT LEVELS RISE STEADILY DURING CC SYNCTIAL STAGES TO REACH A PEAK IN EARLY CYCLE 14 AND THEN DECLINE CC RAPIDLY DURING CELLULARIZATION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03121; CAA26897.1; -. DR EMBL; AE003772; AAF56999.1; -. DR PIR; B23351; B23351. DR FlyBase; FBgn0003510; Sry-alpha. DR GO; GO:0005829; C:cytosol; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0007015; P:actin filament organization; IMP. DR InterPro; IPR008837; Serendipity_A. DR Pfam; PF05482; Serendipity_A; 1. KW Developmental protein. SQ SEQUENCE 530 AA; 59384 MW; EC576378256193FB CRC64; MEQLLAQLHT CSELIAEGYS STGNIGWLNE FCATFLDFAS DLKARLPEVA PSGANLDVET IFLCLTQVVT CITHLERTIS MEAPHMTRQH FLDRLDWCLR RLLVSLTQLE GNVTPVKNLE DHSFVELMDL ALDHLDDYME KLAQQRNNSL HILEESFTED TYQLASIVNH IVRHALAFAN VAIHSDKKAL TALCETLLAE CATFHEEAGE PNSGHRKLEA LSLERALYAL ESFLNEALLH LLFVSLIDLE NASVEKLKDA LQRDPAGAQE LISAFDTNMD RIQQIGVLAI AFSQDIKTKT IVRSCLASLE SLDACIVPAL QLPESTSSAH HAEVLQEHFN QELLIFRNVI HEIIDSCSLI NNYLDMLGER IHVQDKSHLK LIVQRGGVVV DHFRLPVNYS GLSEDGKRVH KDLILILREC QAVVNLDVPV DPKRIVKRLK ILYSVLAKLR DLICRDNLEP DSSVASEAQV PSSATRTFVR SSRSFGKRHR SFVKQTGNCS VFGPQDSLAE SGHSESDLIS FQITEILRLD // ID SRYB_DROME STANDARD; PRT; 351 AA. AC P07665; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serendipity locus beta protein. GN SRY-B OR SRY-BETA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=86089101; PubMed=3935797; RA Vincent A., Colot H.V., Rosbash M.; RT "Sequence and structure of the serendipity locus of Drosophila RT melanogaster. A densely transcribed region including a blastoderm- RT specific gene."; RL J. Mol. Biol. 186:149-166(1985). RN [2] RP DNA-BINDING SPECIFICITY. RX MEDLINE=91330876; PubMed=1868833; RA Payre F., Vincent A.; RT "Genomic targets of the serendipity beta and delta zinc finger RT proteins and their respective DNA recognition sites."; RL EMBO J. 10:2533-2541(1991). CC -!- FUNCTION: BINDS TO THE CONSENSUS DNA SEQUENCE 5'-YCAGAGATGCGCA-3'. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: ABUNDANT IN EARLY EMBRYOS AND PRESENT CC IN VERY LOW AMOUNTS AT EVERY STAGE OF THE FLY LIFE-CYCLE. CC -!- SIMILARITY: CONTAINS 6 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03121; CAA26896.1; -. DR PIR; A23351; A23351. DR HSSP; P08045; 1ZNF. DR TRANSFAC; T00769; -. DR FlyBase; FBgn0003511; Sry-beta. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 6. DR SMART; SM00355; ZnF_C2H2; 6. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. KW Developmental protein; Zinc-finger; Metal-binding; DNA-binding; KW Transcription regulation; Repeat; Nuclear protein. FT ZN_FING 166 190 C2H2-TYPE 1 (ATYPICAL). FT ZN_FING 196 218 C2H2-TYPE 2. FT ZN_FING 224 246 C2H2-TYPE 3. FT ZN_FING 252 274 C2H2-TYPE 4. FT ZN_FING 281 303 C2H2-TYPE 5. FT ZN_FING 310 332 C2H2-TYPE 6. SQ SEQUENCE 351 AA; 41239 MW; D3B404224238F855 CRC64; MSSTRPFCFV CGKEKSVGVF QLIEGTFKPI KDILKYFEKI INQRLELLPN SAACRDCLEY LFNYDRLVRN LSQVQRQIAD ALLGCRQVEG KAETKQQAAK RARVQVPAFK IVQATALKEP ERQPGEEDEC EEFMKEEMLD EEFQFSEPDD SMPSSEEEFF TETTEIPCHI CGEMFSSQEV LERHIKADTC QKSEQATCNV CGLKVKDDEV LDLHMNLHEG KTELECRYCD KKFSHKRNVL RHMEVHWDKK KYQCDKCGER FSLSWLMYNH LMRHDAEENA LICEVCHQQF KTKRTYKHHL RTHQTDRPRY PCPDCEKSFV DKYTLKVHKR VHQPVEKPES AEAKEATVTF F // ID SRYC_DROME STANDARD; PRT; 868 AA. AC P15619; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serendipity locus protein H-1 (Wings-down protein). GN SRY-C OR WDN. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89039875; PubMed=3141791; RA Vincent A., Kejzlarova-Lepesant J., Segalat L., Yanicostas C., RA Lepesant J.-A.; RT "sry h-1, a new Drosophila melanogaster multifingered protein gene RT showing maternal and zygotic expression."; RL Mol. Cell. Biol. 8:4459-4468(1988). CC -!- FUNCTION: THIS MATERNAL AND ZYGOTIC FINGER PROTEIN MAY BELONG TO CC A COMPLEX SET OF MULTIFINGERED PROTEINS WHICH PLAY AN IMPORTANT CC ROLE IN GENE ACTIVATION OR REGULATION AT EARLY EMBRYONIC STAGES CC THROUGH A MAXIMAL ACCUMULATION OF THEIR TRANSCRIPTS (OR PROTEIN CC PRODUCT) IN THE MATURE OOCYTE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: BLASTODERM SPECIFIC. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23391; AAA28487.1; -. DR PIR; A30817; A30817. DR TRANSFAC; T00768; -. DR FlyBase; FBgn0005642; wdn. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 7. DR ProDom; PD000003; Znf_C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 7. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. KW Developmental protein; Zinc-finger; Metal-binding; DNA-binding; KW Transcription regulation; Repeat; Nuclear protein. FT DOMAIN 52 85 SER/THR-RICH. FT DOMAIN 115 162 SER/THR-RICH. FT DOMAIN 141 213 PRO-RICH. FT DOMAIN 169 186 GLN-RICH. FT ZN_FING 268 292 C2H2-TYPE. FT ZN_FING 298 320 C2H2-TYPE. FT ZN_FING 330 351 C2H2-TYPE. FT ZN_FING 357 379 C2H2-TYPE. FT ZN_FING 385 407 C2H2-TYPE. FT ZN_FING 413 435 C2H2-TYPE. FT ZN_FING 441 463 C2H2-TYPE. FT ZN_FING 469 492 C2H2-TYPE. FT DOMAIN 521 531 POLY-ALA. FT DOMAIN 593 669 PRO-RICH. FT DOMAIN 632 647 GLN-RICH. SQ SEQUENCE 868 AA; 95360 MW; 0234DD17F0F2BF20 CRC64; MEGGKGEGKR MKEEAPSKKL PPKIYGGDAG TPTKAAHDEI LSSLLRINNF DSISSIKDES LDIDLSACVT ISSASLVNGN SLSSTDFWRV LDESAQNNTE LNLSSDVCRD DLAATSSSTL PSTLTSDNHS SSEFSVTFLR PEPPNAFTNS PFKKTSSSGT STPVKLSPEQ LHQQHQLQMP QSQLLQRKPK LPAATAVRLK VFKEEPPEEK HPPEQVVTKV EVCESELLPP SFTIFQQAKS AESVADRLAC RPAASETKPL EVDPAPLHKC LDCNGLLLET PDEVAKHEAA AHRLRLTYRC SECQREFELL AGLKKHLKTH RTEGRKDTWK KCPDCGKCLK LGSMWMHRKI HSDNKKYQCD ICGQKFVQKI NLTHHARIHS SEKPYECPEC QKRFQERSHL QRHQKYHAQT RSYRCEKCGK MYKTERCLKV HNLVHLEQRP FACTVCDKSF ISNSKLKQHS NIHTGMRPFK CNYCPRDFTN FPNWLKHTRR RHKVDHKTGE HLENIPSYCS KKSTTNKAQK AAAAAAAAAA ASSAVNPNEL SASSELKAKA NLTSTAAPAP AKQARKKKQP QQATLAALGI TLPAGTALQQ VHPVPLAQQH QQELTTVLVP LAPPAPKQTK AKRERKQLAP KQLQQKPQLL QQGQPQQSSL EPIPAVPQIK KEPVQTQGPF LDLHGLSLTS AEELIMEQAL EMEECGLYDA PNANNEMGTS DNAISDSAAA LHFQIKNELP DELLPDDDFL PCKPSDRLAC PSLESSPFSS PASMELTAVS CASSVAISTN ALPVRSGNYY LPAFTLNAHG KLSSTGNGVQ SVTTSLAQTP SVSMVNVPLL VRSNQMLPSV DTLLFTNQTG GSRFFAGKSA TAATPHLT // ID SRYD_DROME STANDARD; PRT; 430 AA. AC P07664; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Serendipity locus delta protein. GN SRY-D OR SRY-DELTA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=86089101; PubMed=3935797; RA Vincent A., Colot H.V., Rosbash M.; RT "Sequence and structure of the serendipity locus of Drosophila RT melanogaster. A densely transcribed region including a blastoderm- RT specific gene."; RL J. Mol. Biol. 186:149-166(1985). RN [2] RP SEQUENCE OF 338-430 FROM N.A. RX MEDLINE=84236096; PubMed=6329730; RA Vincent A., O'Connell P., Gray M.R., Rosbash M.; RT "Drosophila maternal and embryo mRNAs transcribed from a single RT transcription unit use alternate combinations of exons."; RL EMBO J. 3:1003-1013(1984). RN [3] RP NUCLEAR LOCALIZATION SIGNAL. RX MEDLINE=91184405; PubMed=1849091; RA Noselli S., Vincent A.; RT "A Drosophila nuclear localisation signal included in an 18 amino RT acid fragment from the serendipity delta zinc finger protein."; RL FEBS Lett. 280:167-170(1991). RN [4] RP DNA-BINDING SPECIFICITY. RX MEDLINE=91330876; PubMed=1868833; RA Payre F., Vincent A.; RT "Genomic targets of the serendipity beta and delta zinc finger RT proteins and their respective DNA recognition sites."; RL EMBO J. 10:2533-2541(1991). RN [5] RP CHARACTERIZATION. RX MEDLINE=97299663; PubMed=9154812; RA Payre F., Buono P., Vanzo N., Vincent A.; RT "Two types of zinc fingers are required for dimerization of the RT serendipity delta transcriptional activator."; RL Mol. Cell. Biol. 17:3137-3145(1997). CC -!- FUNCTION: TRANSCRIPTIONAL ACTIVATOR THAT CONTROLS BICOID GENE CC EXPRESSION DURING OOGENESIS. FOUND IN TRANSCRIPTIONALLY ACTIVE CC CELLS. BINDS TO SPECIFIC SITES ON POLYTENE CHROMOSOMES OF THIRD CC INSTAR LARVAE. BINDS TO THE CONSENSUS DNA SEQUENCE 5'- CC YTAGAGATGGRAA-3'. CC -!- SUBUNIT: BINDS DNA AS A HOMODIMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: FOUND IN OVARIES AND ABUNDANT IN EARLY CC EMBRYOS, ALSO FOUND IN VARIABLE AMOUNTS AT EVERY STAGE OF CC THE FLY LIFE CYCLE. CC -!- SIMILARITY: CONTAINS 7 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03121; CAA26898.1; -. DR EMBL; X00555; CAA25221.1; -. DR PIR; C23351; C23351. DR TRANSFAC; T00767; -. DR FlyBase; FBgn0003512; Sry-delta. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; IGI. DR GO; GO:0007292; P:female gamete generation; IGI. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 7. DR SMART; SM00355; ZnF_C2H2; 7. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. KW Developmental protein; Zinc-finger; Metal-binding; DNA-binding; KW Transcription regulation; Activator; Repeat; Nuclear protein. FT DOMAIN 149 161 ASP/GLU-RICH (ACIDIC). FT DOMAIN 186 192 NUCLEAR LOCALIZATION SIGNAL. FT ZN_FING 193 216 C2H2-TYPE 1. FT ZN_FING 222 244 C2H2-TYPE 2. FT ZN_FING 250 272 C2H2-TYPE 3. FT ZN_FING 278 300 C2H2-TYPE 4. FT ZN_FING 307 329 C2H2-TYPE 5. FT ZN_FING 336 358 C2H2-TYPE 6. FT ZN_FING 404 427 C2H2-TYPE 7. SQ SEQUENCE 430 AA; 49668 MW; B6ADCEF1E8B94086 CRC64; MDTCFFCGAV DLSDTGSSSS MRYETLSAKV PSSQKTVSLV LTHLANCIQT QLDLKPGARL CRCFQELSDY DTIMVNLMTT QKRLTTQLKG ALKSEFEVPE SGEDILVEEV EIPQSDVETD ADAEADALFV ELVKDQEESD TEIKREFVDE EEEEDDDDDD EFICEDVDVG DSEALYGKSS DGEDRPTKKR VKQECTTCGK VYNSWYQLQK HISEEHSKQP NHICPICGVI RRDEEYLELH MNLHEGKTEK QCRYCPKSFS RPVNTLRHMR SHWDKKKYQC EKCGLRFSQD NLLYNHRLRH EAEENPIICS ICNVSFKSRK TFNHHTLIHK ENRPRHYCSV CPKSFTERYT LKMHMKTHEG DVVYGVREEA PADEQQVVEE LHVDVDESEA AFTVIMSDND ENSGFCLICN TTFENKKELE HHLQFDHDVS // ID SSB_DROME STANDARD; PRT; 146 AA. AC P54622; Q9V3U4; DT 01-OCT-1996 (Rel. 34, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Single-stranded DNA-binding protein, mitochondrial precursor (Mt-SSB) DE (MtSSB) (Dm mtSSB) (Low power protein). GN MTSSB OR LOPO OR CG4337. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; RX MEDLINE=20250922; PubMed=10788480; RA Ruiz de Mena I., Lefai E., Garesse R., Kaguni L.S.; RT "Regulation of mitochondrial single-stranded DNA-binding protein gene RT expression links nuclear and mitochondrial DNA replication in RT Drosophila."; RL J. Biol. Chem. 275:13628-13636(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 4-146 FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Ovary; RX MEDLINE=94266149; PubMed=8206370; RA Stroumbakis N.D., Li Z., Tolias P.P.; RT "RNA- and single-stranded DNA-binding (SSB) proteins expressed during RT Drosophila melanogaster oogenesis: a homolog of bacterial and RT eukaryotic mitochondrial SSBs."; RL Gene 143:171-177(1994). RN [5] RP SEQUENCE OF 23-51, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MASS RP SPECTROMETRY. RX MEDLINE=95403346; PubMed=7673145; RA Thommes P., Farr C.L., Marton R.F., Kaguni L.S., Cotterill S.; RT "Mitochondrial single-stranded DNA-binding protein from Drosophila RT embryos. Physical and biochemical characterization."; RL J. Biol. Chem. 270:21137-21143(1995). RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=21191852; PubMed=11294889; RA Maier D., Farr C.L., Poeck B., Alahari A., Vogel M., Fischer S., RA Kaguni L.S., Schneuwly S.; RT "Mitochondrial single-stranded DNA-binding protein is required for RT mitochondrial DNA replication and development in Drosophila RT melanogaster."; RL Mol. Biol. Cell 12:821-830(2001). CC -!- FUNCTION: THIS PROTEIN BINDS PREFERENTIALLY AND COOPERATIVELY TO CC PYRIMIDINE RICH SS-DNA. REQUIRED FOR MITOCHONDRIAL DNA CC REPLICATION. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- TISSUE SPECIFICITY: UNIFORMLY DISTRIBUTED IN THE EARLY EMBRYO. CC HIGH LEVELS DETECTED IN THE ANTERIOR AND POSTERIOR MIDGUT CC PRIMORDIA OF STAGE 12 EMBRYOS. IN LARVAE, HIGH LEVELS WERE CC DETECTED IN PROLIFERATING TISSUES INCLUDING THE CNS AND DIGESTIVE CC TRACT. IN ADULTS, HIGHLY EXPRESSED IN THE CNS, DIGESTIVE TRACT AND CC OVARY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC LEVELS ARE HIGH DURING EMBRYOGENESIS AND IN THE LARVAE BUT CC DECREASE IN THE PUPAE BEFORE INCREASING AGAIN IN THE ADULT. CC -!- MASS SPECTROMETRY: MW=13845; MW_ERR=14; METHOD=MALDI; CC RANGE=23-146. CC -!- SIMILARITY: CONTAINS 1 SSB DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF181084; AAF16936.1; ALT_SEQ. DR EMBL; AE003712; AAF55287.2; -. DR EMBL; U00669; AAA20507.1; ALT_INIT. DR HSSP; Q04837; 3ULL. DR FlyBase; FBgn0010438; mtSSB. DR GO; GO:0000262; C:mitochondrial chromosome; IDA. DR GO; GO:0005739; C:mitochondrion; IDA. DR GO; GO:0003697; F:single-stranded DNA binding; IDA. DR GO; GO:0006264; P:mitochondrial DNA replication; IDA. DR GO; GO:0000002; P:mitochondrial genome maintenance; IDA. DR InterPro; IPR000424; SSB_protein. DR Pfam; PF00436; SSB; 1. DR TIGRFAMs; TIGR00621; ssb; 1. DR PROSITE; PS50935; SSB; 1. KW DNA-binding; DNA replication; Mitochondrion; Transit peptide. FT TRANSIT 1 22 MITOCHONDRION. FT CHAIN 23 146 SINGLE-STRANDED DNA-BINDING PROTEIN. FT DOMAIN 38 142 SSB. SQ SEQUENCE 146 AA; 16367 MW; AD505175C0555D48 CRC64; MQHTRRMLNP LLTGLRNLPA RGATTTTAAA PAKVEKTVNT VTILGRVGAD PQLRGSQEHP VVTFSVATHT NYKYENGDWA QRTDWHRVVV FKPNLRDTVL EYLKKGQRTM VQGKITYGEI TDQQGNQKTS TSIIADDVLF FRDANN // ID SSL_DROME STANDARD; PRT; 219 AA. AC Q24536; Q24540; Q9W163; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Suppressor-of-stellate-like protein (Suste-like protein) (Su(ste)- DE like). GN SSL OR CG13591. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Batumi; RX MEDLINE=97322366; PubMed=9177211; RA Kalmykova A.I., Shevelyov Y.Y., Dobritsa A.A., Gvozdev V.A.; RT "Acquisition and amplification of a testis-expressed autosomal gene, RT SSL, by the Drosophila Y chromosome."; RL Proc. Natl. Acad. Sci. U.S.A. 94:6297-6302(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE CASEIN KINASE 2 BETA CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L49382; AAB65817.1; -. DR EMBL; L42285; AAB65818.1; -. DR EMBL; AE003464; AAF47214.1; -. DR FlyBase; FBgn0015300; Ssl. DR GO; GO:0008605; F:protein kinase CK2, intrinsic regulator act...; IDA. DR InterPro; IPR000704; CAS_kinase_II. DR Pfam; PF01214; CK_II_beta; 1. DR PRINTS; PR00472; CASNKINASEII. DR ProDom; PD003829; CAS_kinase_II; 1. DR PROSITE; PS01101; CK2_BETA; 1. FT CONFLICT 143 143 N -> I (IN REF. 1; AAB65818). SQ SEQUENCE 219 AA; 25191 MW; 3F2494C8D1278CC3 CRC64; MSCPRSIEIP DGSWIDWFLG IKGHEFSCRV PNEYIQDKFN LTGLEFDSQT LEVVLDPEFD NEDWDCAEEK KLYGMIHARY IVSPRGIEDM RLKYERGDFG SCPRVFCKRQ KVLPVGLHDV WDKAQVKIYC PSCNNVYIPL PHNGMLDGAM FGTSFPHMFF MQLPSLIPSP PVEKYIPRIY GFQLHKKALM PPESAESPPI KVESSVSKSP SWLRNVPNF // ID SSRP_DROME STANDARD; PRT; 723 AA. AC Q05344; Q9W1J4; DT 01-OCT-1994 (Rel. 30, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Single-strand recognition protein (SSRP) (Chorion-factor 5). GN SSRP OR SSRP1 OR CF5 OR CG4817. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=93342017; PubMed=7688122; RA Hsu T., King D.L., Labonne C., Kafatos F.C.; RT "A Drosophila single-strand DNA/RNA-binding factor contains a high- RT mobility-group box and is enriched in the nucleolus."; RL Proc. Natl. Acad. Sci. U.S.A. 90:6488-6492(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93241947; PubMed=8479916; RA Bruhn S.L., Housman D.E., Lippard S.J.; RT "Isolation and characterization of cDNA clones encoding the RT Drosophila homolog of the HMG-box SSRP family that recognizes RT specific DNA structures."; RL Nucleic Acids Res. 21:1643-1646(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS TO SINGLE-STRANDED DNA AND RNA SEQUENCES, WITH CC HIGHEST AFFINITY FOR NUCLEOTIDES G AND U. CC -!- SUBCELLULAR LOCATION: NUCLEAR. PARTICULARLY ABUNDANT IN THE CC NUCLEOLUS. CC -!- TISSUE SPECIFICITY: EXPRESSED MOST ABUNDANTLY IN NURSE CELLS IN CC THE OVARY. CC -!- DEVELOPMENTAL STAGE: ABUNDANT THROUGHOUT OOGENESIS AND CC EMBRYOGENESIS, DECREASES DURING LARVAL STAGES AND INCREASES CC AGAIN IN PUPAE. CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -!- SIMILARITY: BELONGS TO THE SSRP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08825; AAA28914.1; -. DR EMBL; X68408; CAA48471.1; -. DR EMBL; AE003462; AAF47064.1; -. DR PIR; A48217; A48217. DR PIR; S33688; S33688. DR HSSP; Q05783; 1HMA. DR TRANSFAC; T01848; -. DR FlyBase; FBgn0010278; Ssrp. DR InterPro; IPR000910; HMG_12_box. DR InterPro; IPR000969; SSrcognition. DR Pfam; PF00505; HMG_box; 1. DR Pfam; PF03531; SSrecog; 1. DR PRINTS; PR00887; SSRCOGNITION. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW DNA-binding; RNA-binding; Nuclear protein. FT DNA_BIND 555 621 HMG BOX. FT CONFLICT 13 13 E -> Q (IN REF. 1). FT CONFLICT 33 33 K -> E (IN REF. 1). FT CONFLICT 212 212 G -> R (IN REF. 1). FT CONFLICT 428 428 M -> T (IN REF. 1). FT CONFLICT 498 498 V -> E (IN REF. 1). FT CONFLICT 504 504 D -> E (IN REF. 1). FT CONFLICT 573 573 I -> Y (IN REF. 1). SQ SEQUENCE 723 AA; 81532 MW; DE8017F75C6CA207 CRC64; MTDSLEYNDI NAEVRGVLCS GRLKMTEQNI IFKNTKTGKV EQISAEDIDL INSQKFVGTW GLRVFTKGGV LHRFTGFRDS EHEKLGKFIK AAYSQEMVEK EMCVKGWNWG TARFMGSVLS FDKESKTIFE VPLSHVSQCV TGKNEVTLEF HQNDDAPVGL LEMRFHIPAV ESAEEDPVDK FHQNVMSKAS VISASGESIA IFREIQILTP RGRYDIKIFS TFFQLHGKTF DYKIPMDSVL RLFMLPHKDS RQMFFVLSLD PPIKQGQTRY HYLVLLFAPD EETTIELPFS EAELRDKYEG KLEKEISGPV YEVMGKVMKV LIGRKITGPG NFIGHSGTAA VGCSFKAAAG YLYPLERGFI YIHKPPLHIR FEEISSVNFA RSGGSTRSFD FEVTLKNGTV HIFSSIEKEE YAKLFDYITQ KKLHVSNMGK DKSGYKDVDF GDSDNENEPD AYLARLKAEA REKEEDDDDG DSDEESTDED FKPNENESDV AEEYDSNVES DSDDDSDASG GGGDSDGAKK KKEKKSEKKE KKEKKHKEKE RTKKPSKKKK DSGKPKRATT AFMLWLNDTR ESIKRENPGI KVTEIAKKGG EMWKELKDKS KWEDAAAKDK QRYHDEMRNY KPEAGGDSDN EKGGKSSKKR KTEPSPSKKA NTSGSGFKSK EYISDDDSTS SDDEKDNEPA KKKSKPPSDG DAKKKKAKSE SEPEESEEDS NASDEDEEDE ASD // ID STAN_DROME STANDARD; PRT; 3579 AA. AC Q9V5N8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protocadherin-like wing polarity protein stan precursor (Starry night DE protein) (Flamingo protein). GN STAN OR FMI OR CG11895. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Embryo; RX MEDLINE=20025940; PubMed=10556066; RA Chae J.W., Kim M.-J., Goo J.H., Collier S., Gubb D., Charlton J., RA Adler P.N., Park W.J.; RT "The Drosophila tissue polarity gene starry night encodes a member of RT the protocadherin family."; RL Development 126:5421-5429(1999). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=99418630; PubMed=10490098; RA Usui T., Shima Y., Shimada Y., Hirano S., Burgess R.W., Schwarz T.L., RA Takeichi M., Uemura T.; RT "Flamingo, a seven-pass transmembrane cadherin, regulates planar cell RT polarity under the control of frizzled."; RL Cell 98:585-595(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: INVOLVED IN THE FZ SIGNALING PATHWAY THAT CONTROLS WING CC TISSUE POLARITY. ALSO MEDIATES HOMOPHILIC CELL ADHESION. MAY PLAY CC A ROLE IN INITIATING PREHAIR MORPHOGENESIS. MAY PLAY A CRITICAL CC ROLE IN TISSUE POLARITY AND IN FORMATION OF NORMAL DENDRITE CC FIELDS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: IN THE PUPAL WING, EXPRESSED AT RELATIVELY CC EVEN LEVELS IN ALL REGIONS. ABUNDANT IN 6-9 HOUR EMBRYOS. CC EXPRESSED AT HIGHER LEVELS IN PUPAE THAN LARVAE. CC -!- DEVELOPMENTAL STAGE: AT 12 HOURS AFTER PUPARIUM FORMATION (APF), CC EXPRESSED EVENLY AT CELL BOUNDARIES. BY 30 HOURS APF, EXPRESSION CC IS CONCENTRATED AT PROXIMAL AND DISTAL CELL BOUNDARIES WITH LITTLE CC OR NO EXPRESSION AT ANTERIOR AND POSTERIOR BOUNDARIES. WHEN CC PREHAIRS EMERGE AT 30-36 HOURS APF, EXPRESSION BECOMES EVENLY CC DISTRIBUTED AGAIN ALONG THE WHOLE CELL BOUNDARY. CC -!- SIMILARITY: BELONGS TO FAMILY 2 OF G-PROTEIN COUPLED RECEPTORS. CC -!- SIMILARITY: CONTAINS 8 CADHERIN DOMAINS. CC -!- SIMILARITY: CONTAINS 4 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 2 LAMININ G-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 1 GPS DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF172329; AAF02618.1; -. DR EMBL; AB028498; BAA84069.1; -. DR EMBL; AE003828; AAF58763.3; -. DR HSSP; P08709; 1BF9. DR FlyBase; FBgn0024836; stan. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008014; F:calcium-dependent cell adhesion molecule ac...; IMP. DR GO; GO:0005057; F:receptor signaling protein activity; IMP. DR GO; GO:0016358; P:dendrite morphogenesis; IEP. DR GO; GO:0007222; P:frizzled signaling pathway; IMP. DR GO; GO:0007367; P:segment polarity determination; IMP. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR000742; EGF_2. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR000832; GPCR_secretin. DR InterPro; IPR001879; hormn_receptor. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR000203; PKD_cys_rich. DR Pfam; PF00002; 7tm_2; 1. DR Pfam; PF00028; cadherin; 8. DR Pfam; PF00008; EGF; 3. DR Pfam; PF01825; GPS; 1. DR Pfam; PF02793; HRM; 1. DR Pfam; PF00053; laminin_EGF; 1. DR Pfam; PF00054; laminin_G; 1. DR PRINTS; PR00205; CADHERIN. DR PRINTS; PR00011; EGFLAMININ. DR PRINTS; PR00249; GPCRSECRETIN. DR SMART; SM00112; CA; 8. DR SMART; SM00179; EGF_CA; 1. DR SMART; SM00303; GPS; 1. DR SMART; SM00282; LamG; 2. DR PROSITE; PS00232; CADHERIN_1; 6. DR PROSITE; PS50268; CADHERIN_2; 8. DR PROSITE; PS00022; EGF_1; 4. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS50026; EGF_3; 3. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG. DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. DR PROSITE; PS50221; GPS; 1. DR PROSITE; PS50025; LAM_G_DOMAIN; 2. DR PROSITE; PS01248; LAMININ_TYPE_EGF; 1. KW Cell adhesion; Developmental protein; G-protein coupled receptor; KW Calcium-binding; Repeat; Signal; Transmembrane; EGF-like domain; KW Laminin EGF-like domain; Glycoprotein. FT SIGNAL 1 29 POTENTIAL. FT CHAIN 30 3579 PROTOCADHERIN-LIKE WING POLARITY PROTEIN FT STAN. FT DOMAIN 30 2816 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2817 2837 1 (POTENTIAL). FT DOMAIN 2838 2845 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 2846 2866 2 (POTENTIAL). FT DOMAIN 2867 2883 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2884 2904 3 (POTENTIAL). FT DOMAIN 2905 2919 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 2920 2940 4 (POTENTIAL). FT DOMAIN 2941 2959 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2960 2980 5 (POTENTIAL). FT DOMAIN 2981 3000 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 3001 3021 6 (POTENTIAL). FT DOMAIN 3022 3031 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 3032 3052 7 (POTENTIAL). FT DOMAIN 3053 3579 CYTOPLASMIC (POTENTIAL). FT DOMAIN 360 464 CADHERIN 1. FT DOMAIN 465 581 CADHERIN 2. FT DOMAIN 582 689 CADHERIN 3. FT DOMAIN 690 794 CADHERIN 4. FT DOMAIN 795 897 CADHERIN 5. FT DOMAIN 898 1007 CADHERIN 6. FT DOMAIN 1008 1113 CADHERIN 7. FT DOMAIN 1114 1220 CADHERIN 8. FT DOMAIN 1482 1518 EGF-LIKE 1 CALCIUM-BINDING. FT DOMAIN 1556 1753 LAMININ G-LIKE 1. FT DOMAIN 1756 1792 EGF-LIKE 2 CALCIUM-BINDING. FT DOMAIN 1796 1963 LAMININ G-LIKE 2. FT DOMAIN 1965 2000 EGF-LIKE 3 CALCIUM-BINDING. FT DOMAIN 2091 2126 EGF-LIKE 4 CALCIUM-BINDING. FT DOMAIN 2744 2802 GPS. FT DOMAIN 140 143 POLY-HIS. FT DOMAIN 155 159 POLY-ARG. FT DOMAIN 2567 2579 POLY-SER. FT DOMAIN 3460 3467 POLY-GLN. FT DISULFID 1486 1497 POTENTIAL. FT DISULFID 1491 1506 POTENTIAL. FT DISULFID 1508 1517 POTENTIAL. FT DISULFID 1760 1771 POTENTIAL. FT DISULFID 1765 1780 POTENTIAL. FT DISULFID 1782 1791 POTENTIAL. FT DISULFID 1969 1979 POTENTIAL. FT DISULFID 1973 1988 POTENTIAL. FT DISULFID 1990 1999 POTENTIAL. FT DISULFID 2092 2095 POTENTIAL. FT DISULFID 2097 2114 POTENTIAL. FT DISULFID 2116 2125 POTENTIAL. FT CARBOHYD 46 46 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 179 179 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 340 340 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 671 671 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 886 886 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1269 1269 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1374 1374 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1441 1441 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1650 1650 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1678 1678 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1747 1747 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1843 1843 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1975 1975 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2016 2016 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2028 2028 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2071 2071 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2088 2088 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2196 2196 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2320 2320 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 2784 2784 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 181 181 T -> S (IN REF. 1). FT CONFLICT 361 361 Q -> L (IN REF. 1). FT CONFLICT 395 401 MVSLLDS -> NGLTVGLP (IN REF. 2). FT CONFLICT 1968 1968 Q -> H (IN REF. 1). FT CONFLICT 2271 2271 G -> E (IN REF. 1). FT CONFLICT 2502 2502 R -> C (IN REF. 2). FT CONFLICT 2627 2627 D -> G (IN REF. 2). FT CONFLICT 2709 2709 T -> S (IN REF. 2). FT CONFLICT 2756 2756 Q -> R (IN REF. 2). FT CONFLICT 2901 2901 C -> Y (IN REF. 1). FT CONFLICT 3098 3098 L -> P (IN REF. 1). FT CONFLICT 3569 3579 ERNIDDDETTV -> DSEAEY (IN REF. 2). SQ SEQUENCE 3579 AA; 397139 MW; 4E801C493031FB19 CRC64; MQTREFPQRP LGLLLVLLVV LLQSSLIKSY LIIVHEDTPP GTVIFNASVY KLGSERHYKI NAHKSANFVH HLVSVNHKDG QIQLRKALKC DGIYYPNLFT FYVDSTSNRL RSIDYYSLPV RIFVSGHSCN EDRRIEQELH HHHYEEEDNT GYSKRRRRRS TQEMIQLNGN QLEEVFRQNS TEFRAGDLIF GDSFDNEMRH RILSRKRRAV GSPDPLHLQP ALHRRISDAK QWISETYASY AIHTTDKWNQ ICLRRSQFIN SLNAFLPRSV CQHCKVSFLD VNDERFAIEH QSRDLVASRD VCIAESMWKV SITFNIRCDR RDIVDSDHRL KIVYHHQEFN DTDIARRVRR ELRNQSPYFE QALYVASVLE EQPAGAAVTT VRARDPEDSP VVYSMVSLLD SRSQSLFKVD SRTGVVTTSA SLDRELMDVH YFRVVATDDS FPPRSGTTTL QVNVLDCNDH SPTFEAEQFE ASIREGATVG STVITLRATD QDIGKNAEIE YGIEAVTDGA GLAQDQEMPI FRIDSRSGVI STRSSLDRET SDSYHLLVTA ADLASAQSER RTATASVQVK VLDDNDNYPQ FSERTYTVQV PEDQWGGTED NTVAHIRATD ADQGNNAAIR YAIIGGNTQS QFSIDSMSGD VSLVKPLDYE SVRSYRLVIR AQDGGSPSRS NTTQLLVNVI DANDNAPRFY TSQFQESVLE NVPVGYNIIR VQAYDSDEGA NAEITYSISE RDDNFPLAVD PRTGWVQTIK PLDREEQGRF AFQVVAKDGG VPPKSASSSV VITVQDVNDN DPAFNPKYYE ANVGEDQPPG TPVTTVTATD PDEDSRLHYE ITTGNTRGRF AITSQNGRGL ITIAQSLDYK QEKRFLLTVA ATDSGGRSDT ATVHINITDA NNFAPIFENA PYSASVFEDA PVGTTVLVVS ATDSDVGVNA QITYSLNEES INGLGSPDPF SINPQTGAIV TNAPLDRETT SGYLLTVTAK DGGNPSLSDT TDVEIGVTDV NDNAPAFKSP LYQASILEDA LVGTSVIQVA ASDPDVGLNG RIKYLLSDRD IEDGSFVIDP TSGTIRTNKG LDRESVAVFH LTAIAVDKGS PPLSSTVEVQ IRLEDVNDSP PTFASDKITL YVPENSPVGS VVGEIHAHDP DEGVNAVVHY SIIGGDDSNA FSLVTRPGSE RAQLLTMTEL DYESTRKRFE LVVRAASPPL RNDAHIEILV TDVNDNAPVL RDFQVIFNNF RDHFPSGEIG RIPAFDADVS DKLHYRILSG NNANLLRLNS SSGGLVLSPQ LNTNVPKFAT MEVSVSDGIN EAKAIMQLSV RLITEDMLFN SVTVRLNEMT EEAFLSPLLN FFLDGLAAII PCPKEHIFVF SIQDDTDVSS RILNVSFSAR RPDVSHEEFY TPQYLQERVY LNRAILARLA TVEVLPFDDN LCVREPCLNF EECLTVLKFG NASEFIHSDT VLFRPIYPVN TFACSCPEGF TGSKEHYLCD TEVDLCYSDP CQNGGTCVRR EGGYTCVCPS THTGQNCETG VGHLRPCPSE TCEGGLSCLS NYPSSQPPPY TATCELRARA FGRNSFLTFE SLKQRHRFNL KLRFATVQEN GLLLYNGRYN ELHDFIALEI HEGHVSFSFS LGDHSERISV IQEAKVSDGK WHQVEVVYLN RSVTLVLDNC DTAIALSGQL GDRWSCANRT TLKLDKRCSL LTETCHRFLD LTGPLQVGGL PRIPAHFPVT NRDFVGCISD LRIDDRFVDL NSYVADNGTL AGCPQKAPLC QSEPCFNGGT CREGWGTYSC ECPEGYAGNS CQDNIPAPWR FSGDGSLSFN PLLRPIQLPW TTSFSLRTRQ KEAFLLQIQI GQNSSAAVCL RQGVLYYIFD GEPMYLAGAF LSDGEWHRVE IRWQQGSEIH FSVDYGQRSG SVPMSQKVQG LYVGKIVMGS PDGSIGAVPE ASPFEGCIQD VRIGAGQSVL SRPTIRENVE DGCESRAQCP DHCPNHSSCQ SSWDLSTCEC DSGYVGTDCA PICTVRPCAS GVCRANTSLP RGYDCECNSS SRHGDYCEKE LQQPCPGGWW GERVCGPCRC DLAQGYHPDC NKTTGQCYCK TNHYQPPNET ACLSCDCYSI GSFSGACNPL TGQCECREGV IGRRCDSCSN PYAEVTLSGC EVVYDACPRS FAGGVWWPRT PLGGVAIEGC PPPARGKGQR SCDVQSGSWN TPDMYNCTSE PFVELRRQLS QLEKLELELN SFVAIKMAEQ LRKACEAVDR RGASKDQKIS GNGRPNRRYK MESSFLLSNG GNVWSHELEM DYLSDELKFT HDRLYGADLL VTEGLLQELI NYELMQSGLN LSHSQDKYFI KNLVDAASVI LDRKYEAEWR RATELIQRGP DDLVDAFNKY LVVLARSQHD TYTSPFEIVQ PNMALGLDIV TTESLFGYEP EQLSEYHRSK YLKPNAFTTE SVVLPDTSGF LQHSARQRPV ISFPKYNNYI LDRRKFDQHT KVLVPLEMLG ITPPESDEIS QSGRRGSSHD HRAIVAYAQY KDVGQLLPDL YDETITRRWG VDVELATPIL SLQILVPSME REQETQRLEI PSRKIFSSSS PSSSSSSGST EQQFVEVFDV PKAPTSSSEQ QIEDIRITAH EIPPPVSSVE QQEASSDEDG EEREPHIRLN LDDIEFHGNS GEEVISPDSP EMLNPNYEGV SSTGSDEQPK GENEAVYRDR RLVKRQVEIT YPSEQMQQTE QVVYRSLGSP HLAQPIKLQM WLDVDSARFG PRSNPQCVRW NSFTNQWTRL GCQTEIPDFD GDFNPAAQQA ILVNCSCTHI SSYAVIVDVI DPEDIPEPSL LVQITSYSAF LVSLPLLLGV LLALALLRGQ QTNSNTIHQN IVLCVFCAEL LFFVGMQSRR QLLESEFPCK LTAICLHYFW LAAFAWTTVD CVHLYRMLTE MRDINHGPMG FYFAMGYGAP AIVVGLSVGV RAHEYGNSLF CWLSVYEPVV WWLVGPIAGM SVVNLLILFV SVKAAFTLKD HVLGFGNLRT LLWLSVVSLP LMGVMWVLAV LAASEHSQLL SLLLSGVVLL HALFCLIGYC IINKRVRENL QRTCLRCMGR KVPLLDSSMV VSNSSHNVNA AARPSNFLAS GYDTTTRRNI GISASSTTSR STAKTSSSPY SDGQLRQTST STSNYNSASD APSFLRGFES STTGRSRGGE EKPSRRQRKD SDSGSETDGR SLELASSHSS DDDESRTARS SGTHRSTAVS STPAYLPNIT EHVQATTPPE LNVVQSPQLF PSVNKPVYAP RWSSQLPDAY LQSPPNIGRW SQDTGSDNEH VHGQAKMTIS PNPLPNPDLT DTSYLQQHHN KINMPPSILE NIRDAREGYE DSLYGRRGEY PDKYGSYKPP SHYGSEKDYP GGGSGSQTIG HMRSFHPDAA YLSDNIYDKQ RTLGSGYLGA KSESPYLSKD RITPDIYGSR DGHYSLKRQP AYATDSLHSV HSLLKNDYHQ QQQQQQQHHL QDRLSEGSDK NGYHFPYTAE EDHLPARKLS HTQPPSLHGS QLMQPPGVGL VNDVNNPGLM GRHTLNGGSR HSSRASSPPS TMVAPMQPLG PLTSITDTER NIDDDETTV // ID STAR_DROME STANDARD; PRT; 597 AA. AC P42519; Q9VPW0; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Star protein. GN S OR CG4385. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95009505; PubMed=7924981; RA Kolodkin A.L., Pickup A.T., Lin D., Goodman C.S., Banerjee U.; RT "Characterization of Star and its interactions with sevenless and EGF RT receptor during photoreceptor cell development in Drosophila."; RL Development 120:1731-1745(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=21526628; PubMed=11672524; RA Lee J.R., Urban S., Garvey C.F., Freeman M.; RT "Regulated intracellular ligand transport and proteolysis control EGF RT signal activation in Drosophila."; RL Cell 107:161-171(2001). RN [4] RP REVIEW. RX MEDLINE=21650354; PubMed=11790319; RA Klaembt C.; RT "EGF receptor signalling: roles of Star and Rhomboid revealed."; RL Curr. Biol. 12:R21-R23(2002). CC -!- FUNCTION: INVOLVED IN EGF RECEPTOR SIGNALING. HAS AN EARLY ROLE CC IN PHOTORECEPTOR DEVELOPMENT. INTERACTS WITH THE RECEPTOR TORPEDO CC IN THE EYE. CC -!- SUBUNIT: INTERACTS WITH SPITZ VIA THE LUMENAL DOMAIN AND MEDIATES CC ITS TRANSPORT TO THE GOLGI. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM, GOLGI COMPLEX AND PLASMA MEMBRANE. CC -!- DEVELOPMENTAL STAGE: IN THE LARVAL EYE DISK, STAR IS EXPRESSED CC FIRST AT THE MORPHOGENETIC FURROW, THEN IN THE DEVELOPING R2, R5, CC AND R8 CELLS AS WELL AS IN THE POSTERIOR CLUSTERS OF THE DISK IN CC ADDITIONAL R CELLS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L31886; AAB04161.1; -. DR EMBL; AE003587; AAF51425.1; -. DR FlyBase; FBgn0003310; S. DR GO; GO:0005783; C:endoplasmic reticulum; IDA. DR GO; GO:0005794; C:Golgi apparatus; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0007174; P:EGF receptor ligand processing; IGI. DR GO; GO:0000042; P:protein-Golgi targeting; IGI. DR GO; GO:0042058; P:regulation of EGF receptor signaling pathway; IGI. KW Developmental protein; Vision; Transmembrane; Endoplasmic reticulum; KW Golgi stack. FT DOMAIN 1 279 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 280 300 POTENTIAL. FT DOMAIN 301 597 LUMENAL (POTENTIAL). FT DOMAIN 99 103 POLY-ASP. FT DOMAIN 163 166 POLY-GLY. FT DOMAIN 233 241 POLY-HIS. FT DOMAIN 249 261 POLY-GLY. FT DOMAIN 352 355 POLY-ALA. SQ SEQUENCE 597 AA; 65817 MW; 46B0A2F18B14486B CRC64; MSQQVFSAHP ALAVDQLQQA EQEEHNTSSN HHQQRSATQS RRHTKAAPKK FTLSRSCAGG GSGTLSGVHQ QVKPSPSNPA ISPECRKTLP VRTNYAAVDD DDDIECEDVD EVNFGQQEKE RERETRQPTK DCGTDETDHV QQRHKNTMTT SATAASRHHH QDGGGGDQSD LSSVISSPSV STVSSPLSTP TRLPQALQQQ LHCCQKSTGM ESRARTSPQQ IQHPHRQHHQ QQHHHHHHHH HLTAAGCTGG GGGGGGSGGS GSCKAKKLDP RLNPSPYRQL LPIALCLLSF AAVFATLIVY MDTTEIRHQQ FRLNMSRDYE LNGVAQDDPA LIDFLRQIHM GKYLGKASPK VAAAASVGVG PPPNSPRLAA AGSTFGSGNS SGSGADQLAH YVADLVGGKM NGAVIQSLSG PLAHLITAPW LSEQLNWMGV LVEPEPRWYF TLRKQNAQRA RMQVVHACVS PNTYPKEITI HNEDVRINSL HDEETSWFNS RVKCFPLYTI MLACERTEYD LLSLGVQGHE LEILQTLPFD KVKIDVISIH LLEDHEDVAD YVLDITRFLA GKSYKLQRKI GRNYFYQRLN ASASRTRKKD ILLLKTP // ID STAT_DROME STANDARD; PRT; 761 AA. AC Q24151; Q24181; Q8IN54; Q8SX55; Q9VDL8; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Signal transducer and transcription activator (Marelle protein) DE (d-STAT). GN STAT92E OR MARE OR MRL OR STAT OR CG4257. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM B). RC TISSUE=Embryo; RX MEDLINE=96190808; PubMed=8608595; RA Hou X.S., Melnick M.B., Perrimon N.; RT "Marelle acts downstream of the Drosophila HOP/JAK kinase and encodes RT a protein similar to the mammalian STATs."; RL Cell 84:411-419(1996). RN [2] RP SEQUENCE FROM N.A. (ISOFORM C). RC TISSUE=Embryo; RX MEDLINE=96190809; PubMed=8608596; RA Yan R., Small S., Desplan C., Dearolf C.R., Darnell J.E. Jr.; RT "Identification of a Stat gene that functions in Drosophila RT development."; RL Cell 84:421-430(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 267-761 FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: SIGNAL TRANSDUCTION AND ACTIVATION OF TRANSCRIPTION. CC PLAYS AN IMPORTANT ROLE IN THE SEGMENTAL PATTERN FORMATION IN THE CC EARLY EMBRYO BY ACTIVATING SPECIFIC STRIPES OF PAIR RULE GENE CC EXPRESSION. THE JANUS KINASE-STAT PATHWAY IS CONNECTED TO CC DROSOPHILA EARLY DEVELOPMENT. MUTANTS EXHIBIT ABERRANT EXPRESSION CC OF THE PAIR RULE GENE EVEN-SKIPPED AT THE CELLULAR BLASTODERM CC STAGE, LEADING TO LARVAL SEGMENTATION DEFECTS. CC -!- SUBUNIT: FORMS A HOMODIMER OR A HETERODIMER WITH A RELATED FAMILY CC MEMBER. CC -!- SUBCELLULAR LOCATION: NUCLEAR; TRANSLOCATED INTO THE NUCLEUS IN CC RESPONSE TO PHOSPHORYLATION (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; Synonyms=Long; CC IsoId=Q24151-1; Sequence=Displayed; CC Name=C; Synonyms=D, Short; CC IsoId=Q24151-2; Sequence=VSP_006290; CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYONIC, LARVAL, CC PUPAL, AND ADULT STAGES, WITH SOME DECREASE IN THE LATE EMBRYONIC CC STAGES. THE EXPRESSION IS UNIFORM IN UNFERTILIZED OR JUST CC FERTILIZED EGGS, SUGGESTING MATERNALLY DEPOSITED MRNA. AT CC BLASTODERM STAGE, EXPRESSION PATTERN SHOWS STRIPES, THAT ARE CC REMINISCENT OF MANY PAIR RULE GENES PATTERN. CC -!- PTM: TYROSINE PHOSPHORYLATED BY HOPSCOTCH. PHOSPHORYLATION IS CC REQUIRED FOR DNA-BINDING ACTIVITY AND DIMERIZATION. CC -!- SIMILARITY: BELONGS TO THE STAT FAMILY OF TRANSCRIPTION FACTORS. CC IN PARTICULAR TO MAMMALIAN STAT5 AND STAT6. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- CAUTION: REF.3 (AAN14351) SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC ERRONEOUS GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U40070; AAC46984.1; -. DR EMBL; U46688; AAB02195.1; -. DR EMBL; AE003731; AAF55773.2; -. DR EMBL; AE003731; AAN14351.2; ALT_SEQ. DR EMBL; AY094839; AAM11192.1; ALT_INIT. DR HSSP; P42227; 1BG1. DR FlyBase; FBgn0016917; Stat92E. DR GO; GO:0007350; P:blastoderm segmentation; IMP. DR GO; GO:0007298; P:border cell migration (sensu Insecta); IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0030097; P:hemopoiesis; NAS. DR GO; GO:0007538; P:primary sex determination; IMP. DR GO; GO:0019827; P:stem cell maintenance; IMP. DR GO; GO:0017145; P:stem cell renewal; IMP. DR GO; GO:0007476; P:wing morphogenesis; NAS. DR InterPro; IPR008967; P53-like. DR InterPro; IPR000980; SH2. DR InterPro; IPR001217; STAT. DR Pfam; PF00017; SH2; 1. DR Pfam; PF01017; STAT; 1. DR Pfam; PF02864; STAT_bind; 1. DR Pfam; PF02865; STAT_prot; 1. DR SMART; SM00252; SH2; 1. DR PROSITE; PS50001; SH2; 1. KW Transcription regulation; Activator; DNA-binding; Nuclear protein; KW SH2 domain; Phosphorylation; Alternative splicing; KW Developmental protein. FT DOMAIN 594 658 SH2. FT MOD_RES 711 711 PHOSPHORYLATION (BY JAK). FT VARSPLIC 699 705 Missing (in isoform C). FT /FTId=VSP_006290. FT CONFLICT 105 105 S -> T (IN REF. 2). FT CONFLICT 648 648 L -> H (IN REF. 2). SQ SEQUENCE 761 AA; 86414 MW; BF3A622A29899161 CRC64; MSLWKRISSH VDCEQRMAAY YEEKGMLELR LCLAPWIEDR IMSEQITPNT TDQLERVALK FNEDLQQKLL STRTASDQAL KFRVVELCAL IQRISAVELY THLRSGLQKE LQLVTEKSVA ATAGQSMPLN PYNMNNTPMV TGYMVDPSDL LAVSNSCNPP VVQGIGPIHN VQNTGIASPA LGMVTPKVEL YEVQHQIMQS LNEFGNCANA LKLLAQNYSY MLNSTSSPNA EAAYRSLIDE KAAIVLTMRR SFMYYESLHE MVIHELKNWR HQQAQAGNGA PFNEGSLDDI QRCFEMLESF IAHMLAAVKE LMRVRLVTEE PELTHLLEQV QNAQKNLVCS AFIVDKQPPQ VMKTNTRFAA SVRWLIGSQL GIHNNPPTVE CIIMSEIQSQ RFVTRNTQMD NSSLSGQSSG EIQNASSTME YQQNNHVFSA SFRNMQLKKI KRAEKKGTES VMDEKFALFF YTTTTVNDFQ IRVWTLSLPV VVIVHGNQEP QSWATITWDN AFAEIVRDPF MITDRVTWAQ LSVALNIKFG SCTGRSLTID NLDFLYEKLQ REERSEYITW NQFCKEPMPD RSFTFWEWFF AIMKLTKDHM LGMWKAGCIM GFINKTKAQT DLLRSVYGIG TFLLRFSDSE LGGVTIAYVN ENGLVTMLAP WTARDFQVLN LADRIRDLDV LCWLHPSDRN ASPVKRDVAF GEFYSKRQEP EPLVLDPVTG YVKSTLHVHV CRNGENGSTS GTPHHAQESM QLGNGDFGMA DFDTITNFEN F // ID STAU_DROME STANDARD; PRT; 1026 AA. AC P25159; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Maternal effect protein staufen. GN STAU. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91300552; PubMed=1712672; RA St Johnston D., Beuchle D., Nuesslein-Volhard C.; RT "Staufen, a gene required to localize maternal RNAs in the Drosophila RT egg."; RL Cell 66:51-63(1991). RN [2] RP STRUCTURE BY NMR OF 579-646. RX MEDLINE=95354674; PubMed=7628456; RA Bycroft M., Grunert S., Murzin A.G., Proctor M., St Johnston D.; RT "NMR solution structure of a dsRNA binding domain from Drosophila RT staufen protein reveals homology to the N-terminal domain of RT ribosomal protein S5."; RL EMBO J. 14:3563-3571(1995). RN [3] RP ERRATUM. RA Bycroft M., Grunert S., Murzin A.G., Proctor M., St Johnston D.; RL EMBO J. 14:4385-4385(1995). RN [4] RP CHARACTERIZATION OF DRBM DOMAINS. RX MEDLINE=20183617; PubMed=10716936; RA Micklem D.R., Adams J., Grunert S., St Johnston D.; RT "Distinct roles of two conserved Staufen domains in oskar mRNA RT localization and translation."; RL EMBO J. 19:1366-1377(2000). CC -!- FUNCTION: REQUIRED BOTH FOR THE LOCALIZATION OF MATERNAL CC DETERMINANTS TO THE POSTERIOR POLE OF THE DROSOPHILA EGG AND CC FOR BICOID RNA TO LOCALIZE CORRECTLY TO THE ANTERIOR POLE. CC OSKAR PROTEIN IS REQUIRED TO KEEP OSKAR RNA AND STAUFEN PROTEIN AT CC THE POSTERIOR POLE. CC -!- TISSUE SPECIFICITY: POLAR GRANULES AT THE POSTERIOR POLE OF THE CC OOCYTE, AND BY THE TIME THE EGG IS LAID, AT THE ANTERIOR POLE. CC -!- DOMAIN: CONTAINS A PROLINE-RICH DOMAIN. THE INSERTION OF THIS CC DOMAIN IN THE DRBM 2 DOMAIN IS REQUIRED FOR STAU-OSKAR MRNA CC LOCALIZATION. CC -!- SIMILARITY: CONTAINS 5 DRBM (DOUBLE-STRANDED RNA-BINDING) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M69111; AAA73062.1; -. DR PIR; A40315; A40315. DR PDB; 1EKZ; 21-AUG-00. DR PDB; 1STU; 31-JUL-95. DR FlyBase; FBgn0003520; stau. DR GO; GO:0045179; C:apical cortex; IDA. DR GO; GO:0003730; F:mRNA 3' UTR binding; IDA. DR GO; GO:0045450; P:bicoid mRNA localization; NAS. DR GO; GO:0045034; P:neuroblast cell division; NAS. DR GO; GO:0007316; P:pole plasm RNA localization; IMP. DR InterPro; IPR001159; DS_RBD. DR Pfam; PF00035; dsrm; 5. DR SMART; SM00358; DSRM; 4. DR PROSITE; PS50137; DS_RBD; 5. KW Developmental protein; RNA-binding; Repeat; 3D-structure. FT DOMAIN 311 378 DRBM 1. FT DOMAIN 398 557 DRBM 2 (ATYPICAL). FT DOMAIN 578 645 DRBM 3. FT DOMAIN 711 781 DRBM 4. FT DOMAIN 951 1018 DRBM 5. FT DOMAIN 3 77 GLN/HIS/PRO-RICH. FT DOMAIN 42 46 POLY-GLN. FT DOMAIN 47 51 POLY-PRO. FT DOMAIN 71 77 POLY-GLN. FT DOMAIN 451 455 POLY-PRO. FT HELIX 580 590 FT TURN 591 591 FT STRAND 595 598 FT STRAND 609 616 FT TURN 617 618 FT STRAND 619 627 FT TURN 628 629 FT HELIX 630 644 SQ SEQUENCE 1026 AA; 110347 MW; AE5B97624BBF7D0B CRC64; MQHNVHAARP APHIRAAHHH SHSHAHMHLH PGMEQHLGPS LQQQQQPPPP PQQPPHRDLH ARLNHHHLHA QQQQQQQTSS NQAAAVAAAG AAYHHGNINS NSGSNISSNS NQMQKIRQQH QHLSSSNGLL GNQPPGPPPQ AFNPLAGNPA ALAYNQLPPH PPHHMAAHLG SYAAPPPHYY MSQAKPAKYN HYGSNANSNS GSNNSNSNYA PKAILQNTYR NQKVVVPPVV QEVTPVPEPP VTTNNATTNS TSNSTVIASE PVTQEDTSQK PETRQEPASA DDHVSTGNID ATGALSNEDT SSSGRGGKDK TPMCLVNELA RYNKITHQYR LTEERGPAHC KTFTVTLMLG DEEYSADGFK IKKAQHLAAS KAIEETMYKH PPPKIRRSEE GGPMRTHITP TVELNALAMK LGQRTFYLLD PTQIPPTDSI VPPEFAGGHL LTAPGPGMPQ PPPPPAYALR QRLGNGFVPI PSQPMHPHFF HGPGQRPFPP KFPSRFALPP PLGAHVHHGP NGPFPSVPTP PSKITLFVGK QKFVGIGRTL QQAKHDAAAR ALQVLKTQAI SASEEALEDS MDEGDKKSPI SQVHEIGIKR NMTVHFKVLR EEGPAHMKNF ITACIVGSIV TEGEGNGKKV SKKRAAEKML VELQKLPPLT PTKQTPLKRI KVKTPGKSGA AAREGSVVSG TDGTMQTGKP ERRKRLNPPK DKLIDMDDAD NPITKLIQLQ QTRKEKEPIF ELIAKNGNET ARRREFVMEV SASGSTARGT GNSKKLAKRN AAQALFELLE AVQVTPTNET QSSEECCTSA TMSAVTAPAV EATAEGKVPM VATPVGPMPG ILILRQNKKP AKKRDQIVIV KSNVESKEEE ANKEVAVAAE ENSNNSANSG DSSNSSSGDS QATEAASESA LNTSTGSNTS GVSSNSSNVG ANTDGNNHAE SKNNTESSSN STSNTQSAGV HMKEQLLYLS KLLDFEVNFS DYPKGNHNEF LTIVTLSTHP PQICHGVGKS SEESQNDAAS NALKILSKLG LNNAMK // ID STC_DROME STANDARD; PRT; 1106 AA. AC P40798; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Shuttle craft protein. GN STC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS LONG AND SHORT). RC TISSUE=Ovary; RX MEDLINE=96104568; PubMed=8524296; RA Stroumbakis N.D., Li Z., Tolias P.P.; RT "A homolog of human transcription factor NF-X1 encoded by the RT Drosophila shuttle craft gene is required in the embryonic central RT nervous system."; RL Mol. Cell. Biol. 16:192-201(1996). CC -!- FUNCTION: PLAYS AN ESSENTIAL ROLE DURING THE LATE STAGES OF CC EMBRYONIC NEUROGENESIS. MAY EITHER FINE-TUNE THE GUIDANCE OR THE CC SPATIAL MAINTENANCE OF THE MIGRATING SNB AND IN NERVE ROOTS, WHICH CC ARE COMPOSED OF AXONS ORIGINATING FROM DISTINCT GROUPS OF MOTOR CC NEURONS AND MAY BE REQUIRED TO EITHER GUIDE OR MAINTAIN THE CC POSITION OF THESE NERVES ALONG A DIRECT AND STRAIGHT PATH TO THEIR CC ULTIMATE TARGETS IN PARTICULAR MUSCLE FIELDS. MAY PLAY A ROLE IN CC EGG CHAMBER DEVELOPMENT AND/OR MAY CONFER ESSENTIAL MATERNAL CC CONTRIBUTIONS TO THE EARLY EMBRYO. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P40798-1; Sequence=Displayed; CC Name=Short; CC IsoId=P40798-2; Sequence=VSP_005757; CC -!- TISSUE SPECIFICITY: OVARIES AND EMBRYONIC CENTRAL NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: MAJOR EXPRESSION IS SEEN IN THE OVARIES WHILE CC MODERATE LEVELS OF EXPRESSION ARE OBSERVED DURING EMBRYOGENESIS CC AND THROUGHOUT SUBSEQUENT STAGES OF FLY DEVELOPMENT. CC -!- SIMILARITY: TO YEAST YNL023C AND HUMAN NFX1. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U09306; AAB60255.1; -. DR PIR; T13938; T13938. DR TRANSFAC; T01688; -. DR FlyBase; FBgn0001978; stc. DR InterPro; IPR001374; R3H. DR InterPro; IPR000967; Znf_NFX1. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF01424; R3H; 1. DR Pfam; PF01422; zf-NF-X1; 8. DR SMART; SM00393; R3H; 1. DR SMART; SM00438; ZnF_NFX; 9. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW Transcription regulation; DNA-binding; Nuclear protein; Repeat; KW Alternative splicing; RNA-binding; Zinc-finger. FT DOMAIN 241 268 TANDEM REPEATS OF R-D. FT ZN_FING 386 433 RING-TYPE. FT DOMAIN 464 904 7 X APPROXIMATE REPEATS, CYS-RICH. FT REPEAT 464 500 1. FT REPEAT 517 554 2. FT REPEAT 575 614 3. FT REPEAT 634 675 4. FT REPEAT 723 762 5. FT REPEAT 834 871 6. FT REPEAT 875 904 7. FT VARSPLIC 109 115 Missing (in isoform Short). FT /FTId=VSP_005757. SQ SEQUENCE 1106 AA; 123261 MW; 8CE146DB37BB8D65 CRC64; MAEYWQQLTN GPGEAGPGNE SSAMVDCNGG HESAAVGGSC NRHSNNNYVN FNQFIMQHNL GGGAPSNATS TMQHPVGSSY TNFSLGGGGG AFGLNPPVAS ASTSHFANVS HQSPNFYSQA MIPTYQNGDG IARVTVTSSY GSVNPSNSNF SSFYTPFGNN PFDFSASKLQ ASAPEFVPNF AKLSLEETPA AATTNGNSTA SLETAINETR PRTLRAQEPA ERGANNQCSN HNYERERERE RDRDRDRERD RDRDRDRDRD RDRDRDRDSR PGNTRQQRRS DYRDDREDRY ERSDRRRPQK QQRYDNHRSN KRRDDWNRNR DRINGFPRAV DDLDTSNESA HPSPEKQSQL QQISPRRGPP LPPADNEKLS QREKLVRDIE QRRLECLVCV EAIKSHQPTW SCRNCYHMLH LKCTITWASS SKSEVGWRCP ACQNVLQDLP RDYLCFCGKL KNPPVSRTEL AHSCGEVCCR IEGCSHACTL LCHPGPCPPC QANVVRSCGC GRSTKTMQCA MKEEVLCGEI CDKLLNCGEH RCQAECHSGK CAACSEQVVQ QCHCGKQERK VPCTRESQDK RTYSCKDSCG QPLPCGHHKC KDSCHAGSCR PCKLSPEQIT SCPCGKIPVP AGQRSSCLDP IPTCEGICSR TLRCGKPAHP HQCGSKCHLG QCPPCPKQTG VKCRCGHMDQ MIKCRQLCNR ADDARCKRRC TKKRSCGKHK CNVECCIDID HDCPLPCNRT LSCGKHKCDQ PCHRGNCPPC YRSSFEELYC ECGAEVIYPP VPCGTKKPIC KLPSSRIHPC DHPPQHNCHS GPTCPPCMIF TTKLCHGNHD WRKTIPCSQP NFSCGMACGK PLPCGGHKCI KPCHEGPCQS AGEICRQSCT KPRPTCGHKC AAACHEGACP ETPCKELVEV QCECGNRKQN RSCQELAREH SRIATIQLAS SMAEMSRGNY MELSEILAPA KKSNKTLDCN DECRLLERNR RLAAALSSGN SDTKQKCLTK YSEFVRGFAK KNPALTKSVY ETLTDLVKLA KESKQRSRSH SFPTMNREKR QLVHELCEVF GIESVSYDKE PNRNVVATAH KDRCWFPATS IMEVLARESG QRRVPVPSNN AWGLKK // ID STEL_DROME STANDARD; PRT; 172 AA. AC P15021; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Stellate protein. GN STE. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Testis; RX MEDLINE=90169476; PubMed=1689686; RA Livak K.J.; RT "Detailed structure of the Drosophila melanogaster stellate genes and RT their transcripts."; RL Genetics 124:303-316(1990). CC -!- FUNCTION: RESPONSIBLE FOR THE APPEARANCE OF PROTEINACEOUS STAR- CC SHAPED CRYSTALS IN THE PRIMARY SPERMATOCYTES OF D.MELANOGASTER CC MALES LACKING A Y CHROMOSOME. CC -!- MISCELLANEOUS: THERE ARE MULTIPLE COPIES OF THE STELLATE GENE IN CC FRUIT FLY. CC -!- SIMILARITY: BELONGS TO THE CASEIN KINASE 2 BETA CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15899; CAA33906.1; -. DR PIR; S24397; S24397. DR FlyBase; FBgn0003523; Ste. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007283; P:spermatogenesis; IMP. DR InterPro; IPR000704; CAS_kinase_II. DR Pfam; PF01214; CK_II_beta; 1. DR PRINTS; PR00472; CASNKINASEII. DR ProDom; PD003829; CAS_kinase_II; 1. DR PROSITE; PS01101; CK2_BETA; 1. KW Testis; Multigene family. SQ SEQUENCE 172 AA; 19507 MW; C86304F591E76F8A CRC64; MSSSQNNNSS WIDWFLGIKG NQFLCRVPTD YVQDTFNQMG LEYFSEILDV ILKPVIDSSS GLLYGDEKKW YGMIHARYIR SERGLIAMHR KYLRGDFGSC PNISCDRQNT LPVGLSAVWG KSTVKIHCPR CKSNFHPKSD TQLDGAMFGP SFPDIFFSLL PNLTSPLDDP RT // ID STIL_DROME STANDARD; PRT; 321 AA. AC P92189; Q9V6D8; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Stand still protein. GN STIL OR CG8592. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Ovary; RX MEDLINE=97247728; PubMed=9093851; RA Pennetta G., Pauli D.; RT "stand still, a Drosophila gene involved in the female germline for RT proper survival, sex determination and differentiation."; RL Genetics 145:975-987(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTANTS RP STIL-1; STIL-2 AND STIL-4. RX MEDLINE=99203441; PubMed=10101125; RA Sahut-Barnola I., Pauli D.; RT "The Drosophila gene stand still encodes a germline chromatin- RT associated protein that controls the transcription of the ovarian RT tumor gene."; RL Development 126:1917-1926(1999). CC -!- FUNCTION: ESSENTIAL IN THE FEMALE GERMLINE FOR PROPER CC SURVIVAL, SEX DETERMINATION AND DIFFERENTIATION. PARTICIPATES IN CC THE TRANSCRIPTIONAL ACTIVATION OF OTU. DOES NOT REGULATE THE CC EXPRESSION OF OVO. CC -!- SUBCELLULAR LOCATION: NUCLEAR; ASSOCIATES WITH DECONDENSED CC CHROMATIN, INCLUDING SITES OF ACTIVE TRANSCRIPTION. CC -!- TISSUE SPECIFICITY: GERM CELLS SPECIFIC. EXPRESSED IN ALL GERM CC CELLS. DURING THE FIRST INSTAR LARVAE, IT IS EXPRESSED IN ALL GERM CC CELLS OF BOTH SEXES. IN THIRD INSTAR LARVAE, IT DECREASES IN MALE CC GERM CELLS WHILE IT REMAINS IN FEMALE GERM CELLS. IN ADULT OVARY, CC IT IS EXPRESSED IN CELLS OF THE GERMARIUM, INCLUDING THE STEM CC CELLS. IN THE EARLY PREVITELLOGENIC STAGES, IT IS HIGHLY EXPRESSED CC IN THE NURSE CELLS. DURING VITELLOGENESIS, IT IS NOT TRANSLOCATED CC INTO THE MATURING EGG. IN TESTES, IT IS ONLY EXPRESSED DURING SOME CC STEPS OF MALE GERMLINE DIFFERENTIATION. AT THE APEX TESTIS, IT IS CC EXPRESSED AT LOW LEVEL IN STEM CELLS AND DIVIDING SPERMATOGONIA, CC WHILE IN NEWLY FORMED 16-CELL CYSTS OF PRIMARY SPERMATOCYTES, IT CC IS TRANSIENTLY BUT STRONGLY EXPRESSED BEFORE VANISHING DURING CC SPERMATOCYTE GROWTH PHASE. CC -!- DEVELOPMENTAL STAGE: IN EMBRYOS, IT IS EXPRESSED FROM STAGE 11 IN CC THE GERM CELL SOON AFTER THEIR MIGRATION THROUGH THE MIDGUT CC EPITHELIUM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y10276; CAA71319.1; -. DR EMBL; Y10277; CAA71320.1; -. DR EMBL; AE003821; AAF58490.1; -. DR EMBL; AY075316; AAL68183.1; -. DR FlyBase; FBgn0003527; stil. KW Transcription regulation; Activator; Nuclear protein; Coiled coil. FT DOMAIN 74 103 COILED COIL (POTENTIAL). FT DOMAIN 147 167 COILED COIL (POTENTIAL). FT DOMAIN 272 292 COILED COIL (POTENTIAL). FT MUTAGEN 19 19 P->S: IN STIL-4; INDUCES FEMALE FT INFERTILITY DUE TO GERM OVARY DEFECTS. FT LOSS OF CHROMATIN ASSOCIATION. FT MUTAGEN 58 58 G->R: IN STIL-2; INDUCES FEMALE FT INFERTILITY DUE TO GERM OVARY DEFECTS. FT LOSS OF CHROMATIN ASSOCIATION. FT MUTAGEN 79 79 K->M: IN STIL-1; INDUCES FEMALE FT INFERTILITY DUE TO GERM OVARY DEFECTS. FT CONFLICT 216 216 L -> M (IN REF. 1). SQ SEQUENCE 321 AA; 35775 MW; 759D9DD97017DE77 CRC64; MSVNLDGSEE KMELKKHVPY ILNGELYRIE KQVGDNVTVK CCYCPPDRIY RGSVRSTGNF HMHIKRRHSS LLGKLHEMKV AALEERRDRI MKNRRFAKSR KKAPVAVAAT STAAQSDSGV FVDMQAAVPS GNESHELKIK TVFQRHKQEQ EGATRKLEDS TSDKANLPNI PKNLGIVVQN VSNISVETLP GGSTPASVSF LGRPVKPEQG SGPSFLADQP AAIDLSQVPP VQGESKSSGS LASSMEDVSM EYSRSQALSQ SLSMAHFLEH PQRDVLQRLE RSMAQISQEL HCRNRIEHNR MLLEAAKFKF LNPNFQFEPN L // ID STIM_DROME STANDARD; PRT; 570 AA. AC P83094; Q9VXL6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Stromal interaction molecule homolog precursor. GN STIM OR CG9126. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21356314; PubMed=11463338; RA Williams R.T., Manji S.S., Parker N.J., Hancock M., RA Van Stekelenburg L., Eid J.-P., Senior P.V., Kazenwadel J., RA Shandala T., Saint R., Smith P.J., Dziadek M.A.; RT "Identification and characterization of the STIM (stromal interaction RT molecule) gene family: coding for a novel class of transmembrane RT proteins."; RL Biochem. J. 357:673-685(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: POSSIBLE ADHESION MOLECULE (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CELL SURFACE CC (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 STERILE ALPHA MOTIF (SAM) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF328906; AAK82338.1; -. DR EMBL; AE003500; AAF48542.2; -. DR EMBL; AY069686; AAL39831.1; -. DR FlyBase; FBgn0045073; Stim. DR InterPro; IPR001660; SAM. DR Pfam; PF00536; SAM; 1. DR SMART; SM00454; SAM; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. KW Cell adhesion; Transmembrane; Coiled coil; Signal; Glycoprotein. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 570 STROMAL INTERACTION MOLECULE HOMOLOG. FT DOMAIN 24 294 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 295 312 POTENTIAL. FT DOMAIN 313 570 CYTOPLASMIC (POTENTIAL). FT DOMAIN 213 281 SAM. FT DOMAIN 26 95 HIS-RICH. FT DOMAIN 310 407 COILED COIL (POTENTIAL). FT DOMAIN 420 462 COILED COIL (POTENTIAL). FT CARBOHYD 212 212 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 570 AA; 64797 MW; B8DC7917F379D0B5 CRC64; MRKNTIWNYS LIFFCCVLKS ISTLDHGPHT VSVDSNRHNT QHQYKQNPNV ASQRHSSHES GQSLHNSQSE HVTHIAASHA GSGGEHSTHL AQNLHRSSYN LLSEAMSQAV SNEFSSMGSG SADGACAADD FDCYSGSVQD RFGMEAIASL HRQLDDDDNG NIDLSESDDF LREELKYDSG YEKRQKAFHF NDDMHISVKE LWEAWLRSEV HNWTIEQTTD WLAQSVQLPQ YVDLFKLHKV TGAALPRLAV NNLQYVGNVL GIKDPIHKQK ISLKAMDVVL FGPPRETGTR WKDYILVTLL LSAIIGCWYA YQQNKNAKRH LRRMAQDMEG LQRAEQSLQE MQKELERARM EQENVATEKL DLERRLKEAP TLSSSNSDLE VQQLKKEIEM LRNELSRAEF ELVDNCWSPP PQLQSWLQYT YELESKNHQK KRTSAEKQLQ SAREACEKLR KKRSSLVGAF VSTHGKSIDD VDRSIVEARN ALGDVTNELQ ERLHRWKQIE TCLGLNIVNN NGLPYLENVL YGRNGGLQSS MGMSSTKGSR ARITNSTEDL DDESIQGKLN FENFSLLATE // ID STLK_DROME STANDARD; PRT; 333 AA. AC P83098; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative serine/threonine-protein kinase STE20-like (EC 2.7.1.-). GN STLK OR CG40293. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). RN [2] RP CONCEPTUAL TRANSLATION. RA Manning G., Sudarsanam S., Plowman G.; RT "Prediction of novel protein kinases from the Drosophila genome RT project and EST sequences."; RL Unpublished observations (AUG-2001). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC STE20 SUBFAMILY. DR FlyBase; FBgn0046692; Stlk. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. KW Hypothetical protein; Transferase; Serine/threonine-protein kinase; KW ATP-binding. FT DOMAIN 10 298 PROTEIN KINASE. FT NP_BIND 16 24 ATP (BY SIMILARITY). FT BINDING 38 38 ATP (BY SIMILARITY). FT ACT_SITE 115 115 BY SIMILARITY. SQ SEQUENCE 333 AA; 38381 MW; 3C06F3F0872DEB8F CRC64; MMCSNNISDY KLLEILKNGM IGTVYKAEDI NNKCLAVKKV SMDQPMEKLT LLFNEVLTVR RLQHRNINTI VSCFLYKQYV YLTYKFMCFG NCEVLLKNVY TSGFPEVAIA LILKDVLSAL TYIHSEHYVH GSVRAKHILL SPRKAVLSNF SYCQSFISQG EKKTFIFGST VGIEKELYWT APEVLYQNLS GYTEKIDIYS IGITCCEMAN GFQPFKDTEL TYMYIEKVRG SLQVLLDKNS LLENQGSLSL EHTNKRIARD VIVNKSFSEN FHQFVELCLN KNPLSRWAAS KLMTHSFLKQ CRNTSLLDQL KDLGQKMSKF KRNERKYACT DNI // ID STNA_DROME STANDARD; PRT; 850 AA. AC Q24211; Q9W5M8; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Stoned A protein (StonedA) (Snt-A). GN STNA OR CG12500. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=CNS; RX MEDLINE=97001127; PubMed=8844157; RA Andrews J., Smith M., Merakovsky J., Coulson M., Hannan F., RA Kelly L.E.; RT "The stoned locus of Drosophila melanogaster produces a dicistronic RT transcript and encodes two distinct polypeptides."; RL Genetics 143:1699-1711(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=99042043; PubMed=9822725; RA Stimson D.T., Estes P.S., Smith M., Kelly L.E., Ramaswami M.; RT "A product of the Drosophila stoned locus regulates neurotransmitter RT release."; RL J. Neurosci. 18:9638-9649(1998). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX MEDLINE=99337940; PubMed=10407025; RA Fergestad T., Davis W.S., Broadie K.; RT "The stoned proteins regulate synaptic vesicle recycling in the RT presynaptic terminal."; RL J. Neurosci. 19:5847-5860(1999). RN [5] RP INTERACTION WITH SYT, AND MUTANT STN-TS2. RX MEDLINE=20524362; PubMed=11069931; RA Phillips A.M., Smith M., Ramaswami M., Kelly L.E.; RT "The products of the Drosophila stoned locus interact with synaptic RT vesicles via synaptotagmin."; RL J. Neurosci. 20:8254-8261(2000). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=21114085; PubMed=11160392; RA Fergestad T., Broadie K.; RT "Interaction of stoned and synaptotagmin in synaptic vesicle RT endocytosis."; RL J. Neurosci. 21:1218-1227(2001). RN [7] RP FUNCTION. RX MEDLINE=21212245; PubMed=11312288; RA Stimson D.T., Estes P.S., Rao S., Krishnan K.S., Kelly L.E., RA Ramaswami M.; RT "Drosophila stoned proteins regulate the rate and fidelity of synaptic RT vesicle internalization."; RL J. Neurosci. 21:3034-3044(2001). CC -!- FUNCTION: ADAPTER PROTEIN INVOLVED IN ENDOCYTIC RECYCLING OF CC SYNAPTIC VESICLES MEMBRANES. MAY ACT BY MEDIATING THE RETRIEVAL OF CC SYNAPTOTAGMIN PROTEIN SYT FROM THE PLASMA MEMBRANE, THEREBY CC FACILITATING THE INTERNALIZATION OF MULTIPLE SYNAPTIC VESICLES CC FROM THE PLASMA MEMBRANE. CC -!- SUBUNIT: INTERACTS WITH THE SECOND C2 DOMAIN OF SYT. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC; COLOCALIZES WITH SYNAPTIC CC VESICLE POOLS. COLOCALIZES WITH THE ENDOCYTIC NETWORK WITHIN CC SYNAPTIC BOUTONS. CC -!- DEVELOPMENTAL STAGE: PRESENT AT SYNAPTIC CONNECTIONS BOTH IN THE CC CNS AND IN NEUROMUSCULAR JUNCTIONS IN THE MATURE EMBRYO (20-22H) CC AND THROUGHOUT LARVAL DEVELOPMENT. IN THE THIRD INSTAR LARVA, IT CC IS EXPRESSED IN ALL SYNAPTIC BOUTONS TYPES, INCLUDING I, II AND CC III BOUTONS. CC -!- DOMAIN: THE ASP-PRO-PHE (DPF) MOTIFS, WHICH ARE FOUND IN MANY CC PRESYNATIC PROTEINS, ARE THOUGHT TO MEDIATE AN INTERACTION WITH CC ALPHA-ADAPTIN (BY SIMILARITY). CC -!- MISCELLANEOUS: STNB, WHICH IS INVOLVED IN THE SAME PATHWAY, IS CC DERIVED FROM THE SAME DICISTRONIC TRANSCRIPT THAT ENCODES THESE CC TWO DIFFERENT PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U54982; AAC16665.1; -. DR EMBL; AE003066; AAF45340.2; -. DR PIR; T13352; T13352. DR FlyBase; FBgn0016976; stnA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0008021; C:synaptic vesicle; IGI. KW Endocytosis; Synapse; Repeat. FT DOMAIN 26 290 INTERACTION WITH SYT. FT DOMAIN 9 17 POLY-LYS. FT DOMAIN 72 77 POLY-SER. FT DOMAIN 344 350 POLY-GLU. FT DOMAIN 431 434 POLY-PRO. FT SITE 224 226 DPF 1. FT SITE 461 463 DPF 2. FT SITE 535 537 DPF 3. FT SITE 666 668 DPF 4. FT SITE 755 757 DPF 5. FT SITE 823 825 DPF 6. FT MUTAGEN 35 35 K->M: IN STN-TS2; INDUCE BEHAVIORAL FT DEFECTS. HOMOZYGOUS ADULTS ARE VIABLE BUT FT EXHIBIT SLUGGISH AND UNCOORDINATED FT BEHAVIOR. FT CONFLICT 463 463 F -> L (IN REF. 1). SQ SEQUENCE 850 AA; 93108 MW; 2773741640B73757 CRC64; MLKLPKGLKK KKKKSKKDQE LFTEEELEQY KRDLKAKQEA AATKSDAGES DGASSDVEAH HEPVAFNSGL GSGSSSSILN AQQQLSDQNQ GAAGGDEEWA KFKALTSGVD SILHKTQDEL DRIKKESFYQ RLPSAAEKKK QKEEEAARLE AEQQEREKQR LGQIEAQRDK LAEAVVQLSE SEEEAGDYEA DDIFATDYIE AITSGELQLA VVPDSPVLAE DGPDPFDTAY AEKVIVGADR AKGNKKLVSL GAAVEVLSGR VDREHAVALA NPKRKLRKGI QNLLLSESIE LADSEAELLA ATSNAEPQHN LLDDLDEELS ESSVPIDLSV SLHLHLIKHK QPVEEEEELE QKGRENQLLN PDLSEFDSLK DEEDDEFAEL AAESLTKKEE VTVVSQVVLP VAQLPTEAFE AGSWAEFEEQ SGQEPGKPKR PPPPVRPPTG PHIVPGAIYV SEDEEENPED DPFNTNYAEQ VIKKTTVLEE DDDFDPRAEE HATEPPFLAA PQRDLLAGSA TDLSQVVPAP LAPTLSVDQE AEDFDPFDTS AVSALVQPKS TELRFLEREL LNYSGLDGVT LKHSLSDQDF DPRADQKEPA APQVKLEQKE TDFDTAQRKS SLSLNIQAKS VGFLVPASDL LGAGNELGAS KKPLTPYYAP SDNRLQERER EAEDVDPFDT SHVPEAKLSD IELKHIEKDL ISVPANLRHS LSDPDFDPRA PPTPVPAEVL LAVEENINIK VLTPAQDRKK LTNSGGSGKS EEDIDPFDTS IAANLQPGQT ELKLLENELL PETKTLVTDV LDVQSDAQEL GLGDKVLTPS THSRPSLPAQ DIDPFDTSIA ENLAPGEAEI KLLESELIER // ID STNB_DROME STANDARD; PRT; 1262 AA. AC Q24212; Q9W5J3; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Stoned B protein (StonedB) (Snt-B). GN STNB OR CG12473/CG40302. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=CNS; RX MEDLINE=97001127; PubMed=8844157; RA Andrews J., Smith M., Merakovsky J., Coulson M., Hannan F., RA Kelly L.E.; RT "The stoned locus of Drosophila melanogaster produces a dicistronic RT transcript and encodes two distinct polypeptides."; RL Genetics 143:1699-1711(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX MEDLINE=99337940; PubMed=10407025; RA Fergestad T., Davis W.S., Broadie K.; RT "The stoned proteins regulate synaptic vesicle recycling in the RT presynaptic terminal."; RL J. Neurosci. 19:5847-5860(1999). RN [4] RP INTERACTION WITH SYT. RX MEDLINE=20524362; PubMed=11069931; RA Phillips A.M., Smith M., Ramaswami M., Kelly L.E.; RT "The products of the Drosophila stoned locus interact with synaptic RT vesicles via synaptotagmin."; RL J. Neurosci. 20:8254-8261(2000). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=21114085; PubMed=11160392; RA Fergestad T., Broadie K.; RT "Interaction of stoned and synaptotagmin in synaptic vesicle RT endocytosis."; RL J. Neurosci. 21:1218-1227(2001). RN [6] RP FUNCTION. RX MEDLINE=21212245; PubMed=11312288; RA Stimson D.T., Estes P.S., Rao S., Krishnan K.S., Kelly L.E., RA Ramaswami M.; RT "Drosophila stoned proteins regulate the rate and fidelity of synaptic RT vesicle internalization."; RL J. Neurosci. 21:3034-3044(2001). RN [7] RP RNA EDITING. RX MEDLINE=22789647; PubMed=12907802; RA Hoopengardner B., Bhalla T., Staber C., Reenan R.; RT "Nervous system targets of RNA editing identified by comparative RT genomics."; RL Science 301:832-836(2003). CC -!- FUNCTION: ADAPTER PROTEIN INVOLVED IN ENDOCYTIC RECYCLING OF CC SYNAPTIC VESICLES MEMBRANES. MAY ACT BY MEDIATING THE RETRIEVAL OF CC SYNAPTOTAGMIN PROTEIN SYT FROM THE PLASMA MEMBRANE, THEREBY CC FACILITATING THE INTERNALIZATION OF MULTIPLE SYNAPTIC VESICLES CC FROM THE PLASMA MEMBRANE. CC -!- SUBUNIT: INTERACTS WITH THE SECOND C2 DOMAIN OF SYT. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC; COLOCALIZES WITH SYNAPTIC CC VESICLE POOLS. COLOCALIZES WITH THE ENDOCYTIC NETWORK WITHIN CC SYNAPTIC BOUTONS. CC -!- DEVELOPMENTAL STAGE: PRESENT AT SYNAPTIC CONNECTIONS BOTH IN THE CC CNS AND IN NEUROMUSCULAR JUNCTIONS IN THE MATURE EMBRYO (20-22H) CC AND THROUGHOUT LARVAL DEVELOPMENT. IN THE THIRD INSTAR LARVA, IT CC IS EXPRESSED IN ALL SYNAPTIC BOUTONS TYPES, INCLUDING I, II AND CC III BOUTONS. CC -!- DOMAIN: THE ASN-PRO-PHE (NPF) MOTIFS, WHICH ARE FOUND IN PROTEINS CC INVOLVED IN THE ENDOCYTIC PATHWAY, ARE KNOWN TO INTERACT WITH THE CC EH DOMAIN (BY SIMILARITY). CC -!- MISCELLANEOUS: STNA, WHICH IS INVOLVED IN THE SAME PATHWAY, IS CC DERIVED FROM THE SAME DICISTRONIC TRANSCRIPT THAT ENCODES THESE CC TWO DIFFERENT PROTEINS. CC -!- SIMILARITY: BELONGS TO THE STONED B FAMILY. CC -!- SIMILARITY: CONTAINS 1 SHD (STONIN HOMOLOGY) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 MHD (MU HOMOLOGY) DOMAIN. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U54982; AAC16666.1; -. DR EMBL; AE003200; AAF45320.1; ALT_SEQ. DR PIR; T13353; T13353. DR FlyBase; FBgn0016975; stnB. DR GO; GO:0030139; C:endocytic vesicle; IDA. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0008021; C:synaptic vesicle; IGI. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0008099; P:synaptic vesicle endocytosis; IMP. DR InterPro; IPR001392; Clathrn_med. DR Pfam; PF00928; Adap_comp_sub; 1. KW Endocytosis; Synapse; Repeat; RNA editing. FT DOMAIN 729 903 SHD. FT DOMAIN 847 1108 INTERACTION WITH SYT. FT DOMAIN 904 1218 MHD. FT DOMAIN 211 295 PRO-RICH. FT SITE 3 5 NPF 1. FT SITE 19 21 NPF 2. FT SITE 33 35 NPF 3. FT SITE 43 45 NPF 4. FT SITE 210 212 NPF 5. FT SITE 493 495 NPF 6. FT SITE 673 675 NPF 7. FT VARIANT 1186 1186 T -> A (partial, due to RNA editing). FT CONFLICT 117 117 A -> P (IN REF. 1). FT CONFLICT 1012 1012 L -> V (IN REF. 1). SQ SEQUENCE 1262 AA; 137768 MW; 2CE67046F8214C81 CRC64; MANPFLMDED LDGCDAAANP FLMQSEPEPS SDNPFMAATV ASNPFAFGAD DLELGAEPEA EATHDNDLDP AMSFFGTTIE AEDDTLSLKS GAEEEDEGKK PPQSQPQLQS HAHPHPAPPR PLVPPQSTQD LISTVSSQLD ETSSELLGRI PATRSPSPVS MRDLHSPSPT PDSGLADLLD VSVDSGSSAH TQGIEADLIS GVAGGVRLDN PFAVPTAVPN IQAAVPLPAT PIKQPPRPPP PRPAPPRPAP PGQAAPQRPP PPLAAVNPPP AAPEADDLLD MFGTTACKPA KPPPPKSKED ILSLFEQPHV PLSQPASKPD LLHDDLDETI GEGEPPEQEE PDTEQSNEIS SRDEPVFTSL LIRPDESTHD ITSQPQAATG LERQVNNMAA PSGTASTQRA TTPDIEITTV EDLPRSDDED EPEAMQEPET ETKPQIEPDT EPEIVSEHSP PTERLVTQAA LVDGELIAAE PEPEEMDTGL DFPLASSGQL SANPFASPDE EEPNFAPMPA AVANIFAVND PDSQMETPKA PSHTANIFAS DPDEFDAFSA KFDSVKKDNI SIMDGFGGSG AITPTGGDAW GGSAFGSTTI SANACGDTNS ADDGFGNDDD DFYAMQAPAR ADSVESVDKD FSVVIRPMAE ETSGVAPQLA PPPPPAVEVN QAQTTSLPGL TVNPFEDVSG FPAPGLPPTD GTAIKRTDSQ DTPQTPLYDE DVSQPLEEFP RLHYIGPGWE MQLRQPNKKK ITGQRFWKKI VVRLVVQNDV PVVQLLNQAG DKQPFQELPL QPSYSVSEIG AQQYDQFGKI FTMKLQYIFY KERPGVRPGQ VTKAERITNK LTKFAQYAIA GDYEGVKEFG SDLKKLGLPV EHAPQSSQLF KIGSMNYEDM KQFSVCIEEA LFKIPALRER ALTYKMEEVQ VTAVDEITVE QDFEGKILKQ IARVRLFFLA FLTGMPTIEL GVNDMWRQGK EVVGRHDIIP VATEEWIRLE AVEFHSVVNQ KEYERTRTIK FQPPDANYIE LLRFRVRPPK NRELPLQLKA TWCVSGNKVE LRADILVPGF TSRKLGQIPC EDVSVRFPIP ECWIYLFRVE KHFRYGSVKS AHRRTGKIKG IERILGAVDT LQESLIEVTS GQAKYEHHHR AIVWRCPRLP KEGQGAYTTH QLVCRMALTS YDQIPSELAP YAFVEFTMPA TQVSHTTVRS VSVQDSDGDE PPEKYVRYLA RHEYKVGIET THGESTNAYL AATRPIREEP PTTATKPTAS PVAPSDSDTD SN // ID STUB_DROME STANDARD; PRT; 786 AA. AC Q05319; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Serine proteinase stubble (EC 3.4.21.-) (Stubble-stubbloid protein). GN SB OR SB-SBD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93281671; PubMed=7685111; RA Appel L.F., Prout M., Abu-Shumays R., Hammonds A., Garbe J.C., RA Fristrom D., Fristrom J.; RT "The Drosophila Stubble-stubbloid gene encodes an apparent RT transmembrane serine protease required for epithelial RT morphogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 90:4937-4941(1993). CC -!- FUNCTION: HORMONE DEPENDENT PROTEASE REQUIRED FOR EPITHELIAL CC MORPHOGENESIS. HAS A DUAL FUNCTION, DETACHES IMAGINAL DISC CELLS CC FORM EXTRACELLULAR MATRICES THROUGH ITS EXTRACELLULAR PROTEOLYTIC CC DOMAIN AND TRANSMITS AN OUTSIDE-TO-INSIDE SIGNAL TO ITS CC INTRACELLULAR DOMAIN TO MODIFY THE CYTOSKELETON DURING CC MORPHOGENESIS. MAY BE ABLE TO ACTIVATE ITSELF. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. CC -!- INDUCTION: BY 20-HYDROXYECDYSONE (20HE). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-24 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L11451; AAA28918.1; -. DR PIR; A47547; A47547. DR HSSP; P00763; 1DPO. DR MEROPS; S01.225; -. DR FlyBase; FBgn0003319; Sb. DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; IMP. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; FALSE_NEG. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Transmembrane; Glycoprotein; Zymogen; KW Signal-anchor. FT CHAIN 1 542 NON-CATALYTIC CHAIN (POTENTIAL). FT CHAIN 543 786 CATALYTIC CHAIN (POTENTIAL). FT DOMAIN 1 58 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 59 80 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN). FT DOMAIN 81 786 EXTRACELLULAR (POTENTIAL). FT DOMAIN 543 786 SERINE PROTEASE. FT DOMAIN 267 276 POLY-SER. FT DOMAIN 287 298 POLY-GLN. FT DOMAIN 391 478 SER/THR-RICH. FT DOMAIN 412 422 POLY-THR. FT DOMAIN 471 478 POLY-SER. FT ACT_SITE 589 589 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 639 639 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 737 737 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 531 659 INTERCHAIN (BY SIMILARITY). FT DISULFID 574 590 BY SIMILARITY. FT DISULFID 703 722 BY SIMILARITY. FT DISULFID 733 762 BY SIMILARITY. FT CARBOHYD 177 177 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 671 671 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 786 AA; 85010 MW; CE3E755760B9DE4D CRC64; MKQPTLIRPR LRHRRSTPAA ATKMCPKRHW LVNNRAAGSR GSGGAAARSR RSLDQIVEVL VALIVVNCLA TAAAALITPP DSLESLGSLG IPSSSASSSE DDDDMSSGFY RIPHRLEGYP QLQQLQRGQN FKISPKPCSF GRVEGTCMFV WECIKSEGKH VGMCVDSFMF GSCCTHNYTD NIVLPQTAFS YTRPTKPLTL RPRPPAAPYK PMISGMTTIE RPHGAGTLVI RPSGPHHQGT LARPHPPPYQ SKPTTASDLH GSASHPSSSS SSSSSSNPNS IWHTSTQQQQ QQHQQNQQNH WQMTTEPSFI TKPRPTGWTK PGIVNLPMPA RPSKPSKPTK KPIVYDRSPP PPSSVPPSTS TSTTSTSLIW PAQTHPPQPH RPTRPQLSPG TSLAASSSSH WPSSTTSTTS STTSTTTTTT TTRRTTTPTT TTRRTTTNKP TRPYQRPTTA TSSSSTSTTS SKTPTTTRPI SSSSSSSSGI VTSSQRPTQP THRTPVLATS GIETNEISDS SIPDAGALGR VKTISAARSE CGVPTLARPE TRIVGGKSAA FGRWPWQVSV RRTSFFGFSS THRCGGALIN ENWIATAGHC VDDLLISQIR IRVGEYDFSH VQEQLPYIER GVAKKVVHPK YSFLTYEYDL ALVKLEQPLE FAPHVSPICL PETDSLLIGM NATVTGWGRL SEGGTLPSVL QEVSVPIVSN DNCKSMFMRA GRQEFIPDIF LCAGYETGGQ DSCQGDSGGP LQAKSQDGRF FLAGIISWGI GCAEANLPGV CTRISKFTPW ILEHVR // ID STXA_DROME STANDARD; PRT; 291 AA. AC Q24547; Q9TX14; Q9VCD7; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Syntaxin 1A (dSynt1). GN SYX1A OR SYX-1A OR CG31136/CG18615/CG5448. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=95136364; PubMed=7834751; RA Schulze K.L., Broadie K., Perin M.S., Bellen H.J.; RT "Genetic and electrophysiological studies of Drosophila syntaxin-1A RT demonstrate its role in nonneuronal secretion and RT neurotransmission."; RL Cell 80:311-320(1995). RN [2] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=95333891; PubMed=7609612; RA Cerezo J.R., Jimenez F., Moya F.; RT "Characterization and gene cloning of Drosophila syntaxin 1 (Dsynt1): RT the fruit fly homologue of rat syntaxin 1."; RL Brain Res. Mol. Brain Res. 29:245-252(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PLAYS A CRITICAL ROLE IN SEVERAL SECRETORY PROCESSES, CC INCLUDING CUTICLE SECRETION AND NEUROTRANSMITTER RELEASE, AND CC PROBABLY ASSISTS IN NEURONAL MEMBRANE MATURATION OR THE FINAL CC STAGES OF NEURONAL DIFFERENTIATION. ESSENTIAL FOR EMBRYONIC CC VIABILITY AND DEVELOPMENT. REQUIRED FOR COORDINATED PERISTALIC CC CONTRACTIONS. CC -!- SUBCELLULAR LOCATION: TYPE IV MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: PRIOR TO EMBRYONIC STAGE 12 EXPRESSION IS CC UBIQUITOUS, THEN IT BECOMES CONCENTRATED IN THE NEUROPIL. IN THIRD CC INSTAR LARVAE, EXPRESSION IS SEEN AT THE SYNAPTIC BOUTONS OF THE CC VENTRAL MUSCLES. IN ADULT BRAIN, EXPRESSION IS SEEN IN THE OPTIC CC LOBE NEUROPILS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE SYNTAXIN/EPIMORPHIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 T-SNARE COILED-COIL HOMOLOGY DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L37732; AAA75649.1; -. DR EMBL; AE003746; AAF56232.1; -. DR EMBL; AY061472; AAL29020.1; -. DR HSSP; P32851; 1BR0. DR FlyBase; FBgn0013343; Syx1A. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0005486; F:t-SNARE activity; NAS. DR GO; GO:0007349; P:cellularization; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localiz...; IMP. DR GO; GO:0016083; P:synaptic vesicle fusion; NAS. DR InterPro; IPR006012; Syntaxin. DR InterPro; IPR006011; Syntaxin_N. DR InterPro; IPR000727; T_SNARE. DR Pfam; PF05739; SNARE; 1. DR Pfam; PF00804; Syntaxin; 1. DR SMART; SM00503; SynN; 1. DR SMART; SM00397; t_SNARE; 1. DR PROSITE; PS00914; SYNTAXIN; 1. DR PROSITE; PS50192; T_SNARE; 1. KW Neurotransmitter transport; Coiled coil; Transmembrane. FT DOMAIN 1 268 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 269 289 ANCHOR FOR TYPE IV MEMBRANE PROTEIN FT (POTENTIAL). FT DOMAIN 290 291 VESICULAR (POTENTIAL). FT DOMAIN 33 117 COILED COIL (POTENTIAL). FT DOMAIN 195 257 T-SNARE COILED-COIL HOMOLOGY. FT CONFLICT 122 122 Q -> E (IN REF. 2). SQ SEQUENCE 291 AA; 33648 MW; BD0AB88ABC5DD7B3 CRC64; MTKDRLAALH AAQSDDEEET EVAVNVDGHD SYMDDFFAQV EEIRGMIDKV QDNVEEVKKK HSAILSAPQT DEKTKQELED LMADIKKNAN RVRGKLKGIE QNIEQEEQQN KSSADLRIRK TQHSTLSRKF VEVMTEYNRT QTDYRERCKG RIQRQLEITG RPTNDDELEK MLEEGNSSVF TQGIIMETQQ AKQTLADIEA RHQDIMKLET SIKELHDMFM DMAMLVESQG EMIDRIEYHV EHAMDYVQTA TQDTKKALKY QSKARRKKIM ILICLTVLGI LAASYVSSYF M // ID SU12_DROME STANDARD; PRT; 900 AA. AC Q9NJG9; Q8T9D8; Q9VW55; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polycomb protein Su(z)12 (Suppressor 12 of zeste protein). GN SU(Z)12 OR CG8013. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1), CHARACTERIZATION, AND MUTANT RP SU(Z)12-2. RX MEDLINE=21430867; PubMed=11546753; RA Birve A., Sengupta A.K., Beuchle D., Larsson J., Kennison J.A., RA Rasmuson-Lestander A., Mueller J.; RT "Su(z)12, a novel Drosophila Polycomb group gene that is conserved in RT vertebrates and plants."; RL Development 128:3371-3379(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP IDENTIFICATION IN A ESC/E(Z) COMPLEX WITH E(Z); CAF1 AND ESC, RP AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX. RX MEDLINE=22296673; PubMed=12408863; RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.; RT "Drosophila enhancer of Zeste/ESC complexes have a histone H3 RT methyltransferase activity that marks chromosomal Polycomb sites."; RL Cell 111:185-196(2002). RN [6] RP IDENTIFICATION IN A ESC/E(Z) COMPLEX WITH E(Z); CAF1 AND ESC, AND RP METHYLTRANSFERASE ACTIVITY OF THE COMPLEX. RX MEDLINE=22296674; PubMed=12408864; RA Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., RA Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.; RT "Histone methyltransferase activity of a Drosophila Polycomb group RT repressor complex."; RL Cell 111:197-208(2002). CC -!- FUNCTION: POLYCOMB GROUP (PCG) PROTEIN. PCG PROTEINS ACT BY CC FORMING MULTIPROTEIN COMPLEXES, WHICH ARE REQUIRED TO MAINTAIN THE CC TRANSCRIPTIONALLY REPRESSIVE STATE OF HOMEOTIC GENES THROUGHOUT CC DEVELOPMENT. PCG PROTEINS ARE NOT REQUIRED TO INITIATE REPRESSION, CC BUT TO MAINTAIN IT DURING LATER STAGES OF DEVELOPMENT. THEY CC PROBABLY ACT VIA THE METHYLATION OF HISTONES, RENDERING CHROMATIN CC HERITABLY CHANGED IN ITS EXPRESSIBILITY. COMPONENT OF THE ESC/E(Z) CC COMPLEX, WHICH METHYLATES LYS-9 AND LYS-27 RESIDUES OF HISTONE H3. CC DESPITE THE PRESENCE OF A ZINC-FINGER, IT DOES NOT BIND DIRECTLY CC TO DNA, THE ESC/E(Z) COMPLEX BEING PROBABLY RECRUITED TO DNA BY CC PHO. THE ESC/E(Z) COMPLEX IS NECESSARY BUT NOT SUFFICIENT TO CC RECRUIT A FUNCTIONAL PCG REPRESSIVE COMPLEX THAT REPRESSES TARGET CC GENES, SUGGESTING THAT THE RECRUITMENT OF THE DISTINCT PRC1 CC COMPLEX IS ALSO REQUIRED TO ALLOW A SUBSEQUENT REPRESSION. CC -!- SUBUNIT: COMPONENT OF THE ESC/E(Z) COMPLEX, COMPOSED OF ESC, E(Z), CC SU(Z)12, RPD3, CAF1 AND PROBABLY PHO. THIS COMPLEX IS DISTINCT CC FROM THE PRC1 COMPLEX, WHICH CONTAINS MANY OTHER PCG PROTEINS LIKE CC PC, PH, PSC, SU(Z)2. THE TWO COMPLEXES HOWEVER COOPERATE AND CC INTERACT TOGETHER DURING THE FIRST 3 HOURS OF DEVELOPMENT TO CC ESTABLISH PCG SILENCING. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=B; CC IsoId=Q9NJG9-1; Sequence=Displayed; CC Name=2; Synonyms=A; CC IsoId=Q9NJG9-2; Sequence=VSP_007033, VSP_007034; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE VEFS (VRN2-EMF2-FIS2-SU(Z)12) FAMILY. CC -!- SIMILARITY: CONTAINS 1 C2H2-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF149047; AAF73149.1; -. DR EMBL; AE003515; AAF49094.2; -. DR EMBL; AE003515; AAN11641.1; -. DR EMBL; AY069809; AAL39954.1; -. DR FlyBase; FBgn0020887; Su(z)12. DR GO; GO:0000790; C:nuclear chromatin; NAS. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0016458; P:gene silencing; NAS. DR GO; GO:0016481; P:negative regulation of transcription; NAS. DR InterPro; IPR007087; Znf_C2H2. DR SMART; SM00355; ZnF_C2H2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG. KW Transcription regulation; Repressor; Developmental protein; KW Nuclear protein; Metal-binding; Zinc; Zinc-finger; KW Alternative splicing. FT ZN_FING 411 434 C2H2-TYPE. FT DOMAIN 527 603 VEFS-BOX. FT DOMAIN 355 366 ASN-RICH. FT DOMAIN 699 879 SER-RICH. FT VARSPLIC 806 855 NTVLNKRQRYSDGSPGTGIGNGHGGGSGSGANRNKSNNHSL FT PATSNNASS -> VEQAADAPEVLTHSDNAVDVGIIDDECG FT GFGAVGVMNGVASPVANNCVGN (in isoform 2). FT /FTId=VSP_007033. FT VARSPLIC 856 900 Missing (in isoform 2). FT /FTId=VSP_007034. FT MUTAGEN 274 274 G->D: IN SU(Z)12-2; INDUCES LARVAL FT LETHALITY WHEN HOMOZYGOUS. SQ SEQUENCE 900 AA; 100104 MW; 53BA0D83C49EC92F CRC64; MAPAKKREKD SNPDGSAANG IIGLTHGAPD ASNAGSTVPP TAEGQVKLNG HQQEQELFLQ AFEKPTQIYR YLRNRHETNP IFLNRTLSYM KERMSRNNKK RISFQVNSML ESITQKSEAV SQNYLHVIYD SLHEKLPARL DNESGEDLLQ EQLLCEAGES VSVETTLYKI TRSKRKDSTL DFQELLSKCS QIVYNPKDRV GEHATISIPL QTMRPMGEQH TLYKLLFRIK VLSPSTCNDE NAETPPNKRS RPNEKMFGSE LILYEKSSGF ITEGEYEAML QPLNSTSIKS FSPKKCTWET MPDSYIPLSL TYDVYQQSPM LKFHLTLSNE QLPEMISAPE LQRYVQHLDA VAEMNYNNNN YNNNNNCSGL KNGSGGGNST VCKTTPEHIQ IVYNFMYSNN TRQQTEYTQE LNCPWCGLDC LRLYALLKHL KLCHARFNFT YQPAGSGARI DVTINDAYDG SYAGSPYDLA GPSGSSFART CGPVRRTSVT SLMVCRPRRQ KTCLDEFLEL DEDEISNQRS YITGHNRLYH HTETCLPVHP KELDIDSEGE SDPLWLRQKT IQMIDEFSDV NEGEKELMKL WNLHVMRHGF VGDCQLPIAC EMFLDAKGTE IVRKNLYRNF ILHMCSLFDY GLIAAETVYK TVQKLQGLLS KYAAGQELMQ RQREEQLKYW LDVGMHKKQE DPKTLKSPQK PAPPADQAST SSASTSGSGS GSSSMQPPKR MPAHLKRGSA ASSPGVQSKG TENGTNGSNS SSSNSKNVAK KSADQPLSTL ANTRERRSEY GQKRNVSGSR LAATPASKRK LSSKDNTVLN KRQRYSDGSP GTGIGNGHGG GSGSGANRNK SNNHSLPATS NNASSSSSNS KRAIARRRST SERTKASGST GGGAGGVRTR LSVPAKYERR // ID SUCA_DROME STANDARD; PRT; 324 AA. AC Q94522; Q9VZM4; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Succinyl-CoA ligase [GDP-forming] alpha-chain, mitochondrial precursor DE (EC 6.2.1.4) (Succinyl-CoA synthetase, alpha chain) (SCS-alpha). GN SCS-ALPHA OR CG1065. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 1-106 FROM N.A. RC TISSUE=Ovary; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., De Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). CC -!- CATALYTIC ACTIVITY: GTP + SUCCINATE + COA = GDP + SUCCINYL-COA + CC PHOSPHATE. CC -!- PATHWAY: SUBSTRATE LEVEL PHOSPHORYLATION STEP OF THE TRICARBOXYLIC CC ACID CYCLE. CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA CHAIN (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE SUCCINATE/MALATE COA LIGASE ALPHA CC SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003479; AAF47796.1; -. DR EMBL; Y09067; CAA70288.1; ALT_INIT. DR HSSP; P07459; 2SCU. DR FlyBase; FBgn0004888; Scs-alpha. DR InterPro; IPR003781; CoA_binding. DR InterPro; IPR005810; CoA_lig_alpha. DR InterPro; IPR005811; CoA_ligase. DR Pfam; PF02629; CoA_binding; 1. DR Pfam; PF00549; ligase-CoA; 1. DR PRINTS; PR01798; SCOASYNTHASE. DR TIGRFAMs; TIGR01019; sucCoAalpha; 1. DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1. DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1. KW Ligase; Glycolysis; Tricarboxylic acid cycle; Mitochondrion; KW GTP-binding; Transit peptide; Phosphorylation. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 324 SUCCINYL-COA LIGASE [GDP-FORMING] ALPHA- FT CHAIN. FT ACT_SITE 277 277 TELE-PHOSPHOHISTIDINE INTERMEDIATE FT (BY SIMILARITY). SQ SEQUENCE 324 AA; 34028 MW; 3C781229AA9FCCC6 CRC64; MRALLKVRDG FVAGVRCNSQ YNKTRGNLKL NGDSRVICQG FTGKQGTFHS QQALEYGTKL VGGISPKKGG TQHLGLPVFA SVAEAKKATD PHATVIYVPP PGAAAAIIEA LEAEIPLIVC ITEGVPQHDM VKVKHALISQ SKSRLVGPNC PGIIAPEQCK IGIMPGHIHK RGKIGVVSRS GTLTYEAVHQ TTEVGLGQTL CVGIGGDPFN GTDFIDCLEV FLKDPETKGI ILIGEIGGVA EEKAADYLTE YNSGIKAKPV VSFIAGVSAP PGRRMGHAGA IISGGKGGAN DKIAALEKAG VIVTRSPAKM GHELFKEMKR LELV // ID SUF_DROME STANDARD; PRT; 733 AA. AC P25991; Q9W5P7; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Suppressor of forked protein. GN SU(F) OR CG17170. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93170663; PubMed=8436295; RA Mitchelson A., Simonelig M., Williams C., O'Hare K.; RT "Homology with Saccharomyces cerevisiae RNA14 suggests that RT phenotypic suppression in Drosophila melanogaster by suppressor of RT forked occurs at the level of RNA stability."; RL Genes Dev. 7:241-249(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426071; PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002). CC -!- FUNCTION: ESSENTIAL PROTEIN, MAY PLAY A ROLE IN MRNA PRODUCTION CC OR STABILITY. CC -!- SUBUNIT: PROBABLY INTERACTS WITH AN RNA-BINDING PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: PRESENT THROUGHOUT DEVELOPMENT. MOST CC ABUNDANT IN EMBRYOS, PUPAE AND ADULT FEMALES. CC -!- SIMILARITY: CONTAINS 7 HAT REPEATS. CC -!- SIMILARITY: TO YEAST RNA14. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62679; CAA44551.1; -. DR PIR; A46389; A46389. DR TRANSFAC; T00773; -. DR FlyBase; FBgn0003559; su(f). DR InterPro; IPR003107; HAT. DR InterPro; IPR008847; Suf. DR InterPro; IPR008941; TPR-like. DR Pfam; PF05843; Suf; 1. DR SMART; SM00386; HAT; 10. KW Nuclear protein; Repeat. FT REPEAT 46 78 HAT 1. FT REPEAT 80 111 HAT 2. FT REPEAT 118 153 HAT 3. FT REPEAT 164 197 HAT 4. FT REPEAT 230 262 HAT 5. FT REPEAT 355 388 HAT 6. FT REPEAT 459 495 HAT 7. FT DOMAIN 580 716 PRO-RICH. SQ SEQUENCE 733 AA; 84458 MW; 5D395481C63FB432 CRC64; MSSARDLIKV DIEWGMERLV RAQQVVELRP YDIESWSVMI REAQTRPIHE VRSLYESLVN VFPTTARYWK LYIEMEMRSR YYERVEKLFQ RCLVKILNID LWKLYLTYVK ETKSGLSTHK EKMAQAYDFA LEKIGMDLHS FSIWQDYIYF LRGVEAVGNY AENQKITAVR RVYQKAVVTP IVGIEQLWKD YIAFEQNINP IISEKMSLER SKDYMNARRV AKELEYHTKG LNRNLPAVPP TLTKEEVKQV ELWKRFITYE KSNPLRTEDT ALVTRRVMFA TEQCLLVLTH HPAVWHQASQ FLDTSARVLT EKGDVQAAKI FADECANILE RSINGVLNRN ALLYFAYADF EEGRLKYEKV HTMYNKLLQL PDIDPTLVYV QYMKFARRAE GIKSARSIFK KAREDVRSRY HIFVAAALME YYCSKDKEIA FRIFELGLKR FGGSPEYVMC YIDYLSHLNE DNNTRVLFER VLSSGGLSPH KSVEVWNRFL EFESNIGDLS SIVKVERRRS AVFENLKEYE GKETAQLVDR YKFLDLYPCT STELKSIGYA ENVGIILNKV GGGAQSQNTG EVETDSEATP PLPRPDFSQM IPFKPRPCAH PGAHPLAGGV FPQPPALAAL CATLPPPNSF RGPFVSVELL FDIFMRLNLP DSAPQPNGDN ELSPKIFDLA KSVHWIVDTS TYTGVQHSVT AVPPRRRRLL PGGDDSDDEL QTAVPPSHDI YRLRQLKRFA KSN // ID SUHW_DROME STANDARD; PRT; 941 AA. AC P08970; Q9VFK9; DT 01-NOV-1988 (Rel. 09, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Suppressor of hairy wing protein. GN SU(HW) OR CG8573. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=89078995; PubMed=2462523; RA Parkhurst S.M., Harrison D.A., Remington M.P., Spana C., Kelley R.L., RA Coyne R.S., Corces V.G.; RT "The Drosophila su(Hw) gene, which controls the phenotypic effect of RT the gypsy transposable element, encodes a putative DNA-binding RT protein."; RL Genes Dev. 2:1205-1215(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP CHARACTERIZATION. RX MEDLINE=93178417; PubMed=8382607; RA Roseman R.R., Pirrotta V., Gelyer P.K.; RT "The su(Hw) protein insulates expression of the Drosophila RT melanogaster white gene from chromosomal position-effects."; RL EMBO J. 12:435-442(1993). RN [5] RP CHARACTERIZATION. RX MEDLINE=94010293; PubMed=7916729; RA Harrison D.A., Gdula D.A., Coyne R.S., Corces V.G.; RT "A leucine zipper domain of the suppressor of Hairy-wing protein RT mediates its repressive effect on enhancer function."; RL Genes Dev. 7:1966-1978(1993). CC -!- FUNCTION: SU(HW) CONTROLS THE PHENOTYPIC EFFECT OF THE GYPSY CC TRANSPOSABLE ELEMENT. BINDS SPECIFICALLY TO A REGION OF THE GIPSY CC ELEMENT LOCATED 3' OF THE 5'LTR. IT IS PROBABLY A TRANSCRIPTION CC FACTOR. COULD PLAY A ROLE IN THE ESTABLISHMENT OF CHROMATIN CC DOMAINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 12 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00228; CAA68371.1; -. DR EMBL; AE003704; AAF55043.1; -. DR EMBL; BT003273; AAO25030.1; -. DR PIR; S01909; S01909. DR HSSP; P07248; 2ADR. DR TRANSFAC; T00774; -. DR FlyBase; FBgn0003567; su(Hw). DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 12. DR SMART; SM00355; ZnF_C2H2; 12. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10. KW Transcription regulation; Zinc-finger; Metal-binding; DNA-binding; KW Repeat; Nuclear protein. FT DOMAIN 155 202 ASP/GLU-RICH (ACIDIC). FT ZN_FING 220 242 C2H2-TYPE 1 (ATYPICAL). FT ZN_FING 290 313 C2H2-TYPE 2. FT ZN_FING 319 341 C2H2-TYPE 3 (ATYPICAL). FT ZN_FING 348 366 C2H2-TYPE 4. FT ZN_FING 380 402 C2H2-TYPE 5. FT ZN_FING 413 435 C2H2-TYPE 6. FT ZN_FING 441 463 C2H2-TYPE 7. FT ZN_FING 469 491 C2H2-TYPE 8. FT ZN_FING 497 519 C2H2-TYPE 9. FT ZN_FING 523 545 C2H2-TYPE 10. FT ZN_FING 553 577 C2H2-TYPE 11. FT ZN_FING 596 619 C2H2-TYPE 12. FT CONFLICT 31 31 R -> K (IN REF. 1). FT CONFLICT 61 61 E -> G (IN REF. 1). FT CONFLICT 64 64 G -> D (IN REF. 1). FT CONFLICT 68 68 G -> E (IN REF. 1). FT CONFLICT 249 249 H -> R (IN REF. 1). FT CONFLICT 347 347 P -> S (IN REF. 1). FT CONFLICT 508 508 Q -> R (IN REF. 1). FT CONFLICT 667 667 G -> D (IN REF. 1). FT CONFLICT 875 875 E -> EDNE (IN REF. 1). FT CONFLICT 892 892 T -> K (IN REF. 1). FT CONFLICT 896 896 R -> K (IN REF. 1). FT CONFLICT 923 923 S -> T (IN REF. 1). SQ SEQUENCE 941 AA; 105779 MW; 60C6243AD088F961 CRC64; MSASKEGKEK KGKLLGVENI SPPKDKRPAT RMKLLNDVGA GEDSEASTTT TTSRTPSNKQ EKRGSVAGSR IKILNEEILG TPKTEKRGAT KSTAPAASTV KILNEKKTPS ATVTAVETTK IKTSPSKRKK MEHYVLQAVK SENTKADTTV TVVTEEDDTI DFILADDEEV VPGRIENNNG QEIVVTEDDE DLGEDGDEDG EDSSGKGNSS QTKIKEIVEH VCGKCYKTFR RVQSLKKHLE FCRYDSGYHL RKADMLKNLE KIEKDAVVME KKDICFCCSE SYDTFHLGHI NCPDCPKSFK TQTSYERHIF ITHSEFSDFP CSICNANLRS EALLALHEEQ HKSRGKPYAC KICGKDFTRS YHLKRHQKYS SCSSNETDTM SCKVCDRVFY RLDNLRSHLK QHLGTQVVKK PEYMCHTCKN CFYSLSTLNI HIRTHTGEKP FDCDLCDKKF SALVALKKHR RYHTGEKPYS CTVCNQAFAV KEVLNRHMKR HTGERPHKCD ECGKSFIQAT QLRTHSKTHI RPFPCEQCDE KFKTEKQLER HVKTHSRTKR PVFSCAECKR NFRTPALLKE HMDEGKHSPK QQRSSMRSAV KIMERTDCAI CDKNFDSSDT LRRHIRTVHE CDPDDIFGVE PHPSKRAKKD IESEEVVPVA LNTSAGSLIS SQTDGNGVVV REFLVDEGDG AAQTITLENE TYTILPLDGA IEGEQLTDEA GVKPEAKKEE AQVSPVVKKE QRKSLAASLA AAIADNLEES CSEDDFSGEI LTEEDIKLKE NVGKLIDMLV DPPILKKYGW PNAPEETVLC KVIENCGHDL TKGGENYAEL DYGSRMREYC KLLFTVVIHN DSIKSLLNNF PIDDVIEYVL GDEDQDEGGL DKDNESHSGD EEAVSVTGET KTNEIREKPE KKEVSAKSEK KEIVGKAVDK DNSEEVVREN KKKPVGEQEK A // ID SUH_DROME STANDARD; PRT; 594 AA. AC P28159; Q9TVK8; Q9TVY7; Q9TW34; Q9U8F9; Q9V446; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Suppressor of hairless protein (J kappa-recombination signal binding DE protein) (RBP-J kappa). GN SU(H) OR DRBP-JK OR CG3497. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Imaginal disks; RX MEDLINE=92315337; PubMed=1617730; RA Schweisguth F., Posakony J.W.; RT "Suppressor of Hairless, the Drosophila homolog of the mouse RT recombination signal-binding protein gene, controls sensory organ RT cell fates."; RL Cell 69:1199-1212(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 25-128 FROM N.A. RC STRAIN=LAMTO 3, LAMTO 4, LAMTO 5, LAMTO 12, LAMTO 13, LAMTP 18, RC LAMTO 19, LAMTO 21, LAMTO 27, LAMTO 28, LAMTO 31, LAMTO 33, LAMTO 35, RC LAMTO 37, LAMTO 101, LAMTO 106, LAMTO 111, LAMTO 120, LAMTO 124, and RC LAMTO 134; RX MEDLINE=99318836; PubMed=10388820; RA Depaulis F., Brazier L., Veuille M.; RT "Selective sweep at the Drosophila melanogaster Suppressor of RT Hairless locus and its association with the In(2L)t inversion RT polymorphism."; RL Genetics 152:1017-1024(1999). RN [6] RP SEQUENCE OF 44-594 FROM N.A. RC TISSUE=Embryo; RX MEDLINE=92078209; PubMed=1744127; RA Furukawa T., Kawaichi M., Matsunami N., Ryo H., Nishida Y., Honjo T.; RT "The Drosophila RBP-J kappa gene encodes the binding protein for the RT immunoglobulin J kappa recombination signal sequence."; RL J. Biol. Chem. 266:23334-23340(1991). RN [7] RP CHARACTERIZATION. RX MEDLINE=92315336; PubMed=1617729; RA Furukawa T., Maruyama S., Kawaichi M., Honjo T.; RT "The Drosophila homolog of the immunoglobulin recombination signal- RT binding protein regulates peripheral nervous system development."; RL Cell 69:1191-1197(1992). RN [8] RP FUNCTION, AND MUTAGENESIS OF TYR-315. RX MEDLINE=95113197; PubMed=7813798; RA Schweisguth F., Nero P., Posakony J.W.; RT "The sequence similarity of the Drosophila suppressor of hairless RT protein to the integrase domain has no functional significance in RT vivo."; RL Dev. Biol. 166:812-814(1994). RN [9] RP INTERACTION WITH HAIRLESS. RX MEDLINE=95047389; PubMed=7958912; RA Brou C., Logeat F., Lecourtois M., Vandekerckhove J., Kourilsky P., RA Schweisguth F., Israel A.; RT "Inhibition of the DNA-binding activity of Drosophila suppressor of RT hairless and of its human homolog, KBF2/RBP-J kappa, by direct RT protein-protein interaction with Drosophila hairless."; RL Genes Dev. 8:2491-2503(1994). RN [10] RP SUBCELLULAR LOCATION. RX MEDLINE=96232282; PubMed=8674407; RA Gho M., Lecourtois M., Geraud G., Posakony J.W., Schweisguth F.; RT "Subcellular localization of Suppressor of Hairless in Drosophila RT sense organ cells during Notch signalling."; RL Development 122:1673-1682(1996). RN [11] RP FUNCTION, AND DNA-BINDING. RX MEDLINE=20139426; PubMed=10673509; RA Morel V., Schweisguth F.; RT "Repression by suppressor of hairless and activation by Notch are RT required to define a single row of single-minded expressing cells in RT the Drosophila embryo."; RL Genes Dev. 14:377-388(2000). RN [12] RP FUNCTION. RX MEDLINE=22528965; PubMed=12642500; RA Koelzer S., Klein T.; RT "A Notch-independent function of Suppressor of Hairless during the RT development of the bristle sensory organ precursor cell of RT Drosophila."; RL Development 130:1973-1988(2003). CC -!- FUNCTION: TRANSCRIPTIONAL REGULATOR WICH PLAYS A CENTRAL ROLE IN CC NOTCH SIGNALING, A SIGNALING PATHWAY INVOLVED IN CELL-CELL CC COMMUNICATIONS THAT REGULATES A BROAD SPECTRUM OF CELL-FATE CC DETERMINATIONS. BINDS DIRECTLY THE 5'-GTGRGAR-3' DNA CONSENSUS CC SEQUENCE, WHICH IS PRESENT IN THE REGULATORY REGION OF SEVERAL CC GENES. REQUIRED FOR NEUROGENESIS IN IMAGINAL DISKS. ACTS AS A CC TRANSCRIPTIONAL REPRESSOR WHEN IT IS NOT ASSOCIATED WITH NOTCH CC PROTEINS. WHEN ASSOCIATED WITH SOME NOTCH PROTEIN, IT ACTS AS A CC TRANSCRIPTIONAL ACTIVATOR THAT ACTIVATES TRANSCRIPTION OF NOTCH CC TARGET GENES. SPECIFICALLY BINDS TO THE IMMUNOGLOBULIN KAPPA-TYPE CC J SEGMENT RECOMBINATION SIGNAL SEQUENCE. REQUIRED FOR CC TRANSCRIPTION OF SIM. ALSO FUNCTIONS INDEPENDENTLY OF NOTCH CC PATHWAY, IN THE DEVELOPMENT OF THE BRISTLE SENSORY ORGAN PRECURSOR CC CELL. CC -!- SUBUNIT: INTERACTS WITH ACTIVATED CLEAVED NOTCH. INTERACTS WITH CC HAIRLESS, THIS INTERACTION PREVENTING ITS DNA-BINDING ACTIVITY. CC -!- SUBCELLULAR LOCATION: NUCLEAR. IN IMAGINAL DISK, AT THE ONSET OF CC DIFFERENTIATION OF SOCKET CELL, IT IS ALSO PRESENT IN THE CC CYTOPLASM. CC -!- SIMILARITY: BELONGS TO THE SU(H) FAMILY. CC -!- SIMILARITY: CONTAINS 1 TIG DOMAIN. CC -!- CAUTION: DESPITE SOME SIMILARITY WITH THE "PHAGE" INTEGRASE CC FAMILY, REF.8 SHOWED THAT IT HAS NO RECOMBINASE ACTIVITY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M94383; AAA28919.1; -. DR EMBL; AE003411; AAF44914.1; -. DR EMBL; AE003646; AAF53434.1; -. DR EMBL; AY069091; AAL39236.1; -. DR EMBL; AF088255; AAD39698.1; -. DR EMBL; AF088256; AAD39699.1; -. DR EMBL; AF088257; AAD39700.1; -. DR EMBL; AF088258; AAD39701.1; -. DR EMBL; AF088259; AAD39702.1; -. DR EMBL; AF088260; AAD39703.1; -. DR EMBL; AF088261; AAD39704.1; -. DR EMBL; AF088262; AAD39705.1; -. DR EMBL; AF088263; AAD39706.1; -. DR EMBL; AF088264; AAD39707.1; -. DR EMBL; AF088265; AAD39708.1; -. DR EMBL; AF088266; AAD39709.1; -. DR EMBL; AF088267; AAD39710.1; -. DR EMBL; AF088268; AAD39711.1; -. DR EMBL; AF088269; AAD39712.1; -. DR EMBL; AF088270; AAD39713.1; -. DR EMBL; AF088271; AAD39714.1; -. DR EMBL; AF088272; AAD39715.1; -. DR EMBL; AF088273; AAD39716.1; -. DR EMBL; AF088274; AAD39717.1; -. DR EMBL; X58393; CAA41282.1; ALT_INIT. DR PIR; A42770; A42770. DR TRANSFAC; T01615; -. DR FlyBase; FBgn0004837; Su(H). DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0007219; P:N signaling pathway; IGI. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR002909; IPT_TIG. DR Pfam; PF01833; TIG; 1. KW Transcription regulation; Activator; Repressor; Developmental protein; KW Nuclear protein; DNA-binding; Repeat; Polymorphism. FT DNA_BIND 266 275 DNA BINDING MOTIF 1 (BY SIMILARITY). FT DNA_BIND 339 371 DNA BINDING MOTIF 2 (BY SIMILARITY). FT DOMAIN 429 519 TIG. FT DOMAIN 35 42 GLN-RICH. FT DOMAIN 58 88 GLN-RICH. FT DOMAIN 541 558 ASN-RICH. FT DOMAIN 569 576 GLN-RICH. FT VARIANT 80 82 MISSING (IN STRAINS LAMTO 3, LAMTO 4, FT LAMTO 12, LAMTO 18, LAMTO 19, LAMTO 21, FT LAMTO 31, LAMTO 35, LAMTO 101 AND LAMTO FT 111). FT VARIANT 81 82 MISSING (IN STRAINS LAMTO 13, LAMTO 37 FT AND LAMTO 134). FT VARIANT 82 82 MISSING (IN STRAIN LAMTO 124). FT MUTAGEN 315 315 Y->F: NO EFFECT. FT CONFLICT 116 117 ER -> DG (IN REF. 5). FT CONFLICT 492 492 V -> A (IN REF. 5). SQ SEQUENCE 594 AA; 66924 MW; 145144F336CD8F4C CRC64; MKSYSQFNLN AAAPPAIAYE TTVVNPNGSP LDPHQQQQQQ SQDMPHFGLP GPQPPSSQQQ QQQLQVHHQQ QQQQQQQQQQ QQHQQQMQMS LLPGPYRPHI EEKKLTRDAM EKYMRERNDM VIVILHAKVA QKSYGNEKRF FCPPPCIYLF GSGWRRRYEE MLQQGEGEQG AQLCAFIGIG SSDQDMQQLD LNGKQYCAAK TLFISDSDKR KHFMLSVKMF YGNGHDIGVF NSKRIKVISK PSKKKQSLKN ADLCIASGTN VALFNRLRSQ TVSTRYLHVE NGHFHASSTQ WGAFTIHLLD DNESESEEFQ VRDGYIHYGA TVKLVCSVTG MALPRLIIRK VDKQMALLEA DDPVSQLHKC AFYMKDTDRM YLCLSQEKII QFQATPCPKE PNKEMINDGA CWTIISTDKA EYQFYEGMGP VASPVTPVPI VNSLNLNGGG DVAMLELSGD NFTPHLQVWF GDVEAETMYR CTETLLCVVP EISQFRGEWL WVRQPTQVPI SLVRNDGIIY ATGLTFTYTP EPGPRPHCNT QAEDVMRARQ NNNNNNITSI SNNNNSNNAG SPAAGGGLQQ QQQQHQALPS ISEVQWNSHG SGLS // ID SUL1_DROME STANDARD; PRT; 1114 AA. AC Q9VEX0; Q8MRG1; Q9NIH6; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Extracellular sulfatase SULF-1 homolog precursor (EC 3.1.6.-) DE (DmSulf-1). GN SULF1 OR CG6725. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP SEQUENCE OF 104-1087 FROM N.A. RA Standiford D.M., Emerson C.P. Jr.; RT "Analysis of Drosophila melanogaster Sulf1 during development."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM AND GOLGI STACK. CC ALSO LOCALIZED ON THE CELL SURFACE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SULFATASE FAMILY. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS CC IN POSITIONS 242 AND 258. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003712; AAF55296.1; -. DR EMBL; AY119658; AAM50312.1; ALT_INIT. DR EMBL; AF211192; AAF32278.1; ALT_FRAME. DR FlyBase; FBgn0040271; Sulf1. DR GO; GO:0009986; C:cell surface; ISS. DR GO; GO:0005783; C:endoplasmic reticulum; ISS. DR GO; GO:0005795; C:Golgi stack; ISS. DR GO; GO:0018741; F:alkyl sulfatase activity; ISS. DR GO; GO:0008152; P:metabolism; ISS. DR InterPro; IPR000917; Sulfatase. DR Pfam; PF00884; Sulfatase; 1. DR PROSITE; PS00523; SULFATASE_1; 1. DR PROSITE; PS00149; SULFATASE_2; FALSE_NEG. KW Hydrolase; Signal; Glycoprotein; Endoplasmic reticulum; Golgi stack. FT SIGNAL 1 25 POTENTIAL. FT CHAIN 26 1114 EXTRACELLULAR SULFATASE SULF-1 HOMOLOG. FT MOD_RES 98 98 2-AMINO-3-OXOPROPIONIC ACID (BY FT SIMILARITY). FT CARBOHYD 122 122 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 159 159 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 181 181 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 208 208 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 251 251 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 447 447 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 683 683 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 713 713 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 743 743 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 817 817 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 945 945 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 955 955 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 974 974 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 104 105 SL -> TR (IN REF. 3). FT CONFLICT 655 655 E -> A (IN REF. 2). SQ SEQUENCE 1114 AA; 127302 MW; FC14DD0975B3A096 CRC64; MMRHSSLRLI IGGLILLLFV LNVFSKEQGS HSHKRSHSAK RFSRDSNSAR ERRPNIILIL TDDQDVELGS LNFMPRTLRL LRDGGAEFRH AYTTTPMCCP ARSSLLTGMY VHNHMVFTNN DNCSSPQWQA THETRSYATY LSNAGYRTGY FGKYLNKYNG SYIPPGWREW GGLIMNSKYY NYSINLNGQK IKHGFDYAKD YYPDLIANDS IAFLRSSKQQ NQRKPVLLTM SFPAPHGPED SAPQYSHLFF NVTTHHTPSY DHAPNPDKQW ILRVTEPMQP VHKRFTNLLM TKRLQTLQSV DVAVERVYNE LKELGELDNT YIVYTSDHGY HLGQFGLIKG KSFPFEFDVR VPFLIRGPGI QASKVVNEIV LNVDLAPTFL DMGGVPTPQH MDGRSILPLL LSRNRAVRDN WPDSFLIESS GRRETAEQIA ESRARLQIER RNMKLANSSL LEDFLEGAGE STTIVSSSST AATLMSSTAQ QPEDGEEEVE TDNEEDDVDG DGAMDSSAAA LEEDDLDDAA FEEGDEELDQ EFQQNNDLPL APYITKMMRL NSECSDPALL KNCLPGQKWK CVNEEGRWRK HKCKFHLQLE HQLAAMPRKQ YQRNCACFTP DGVVYTKIRA PSAGLHRVNK RTHNGPGRRR NKREVFHTEL PDEMEELLDL HQVVDQLVDH THRSKRDLPA SSNETIAQVI QQIQSTLEIL ELKFNEHELH ASNSSGNSYE RGEKYTKSGG HRCFVDATTA KVNCSNVIYD DEKTWRTSRT QIDMLIKLLK DKIGKLKEMK KQLRESNKQA LAAGRRNDNR RRNDQSVLDS GAGPEFNMSY FTEISSTPRS NVVGQTEVFQ GYGSASAFDS LEQTQSHRFT PRAECYCEPD VGENHADSKE MAREARRKLK EERQRKKERK RIKKARLEKE CLSEKMNCFS HDNQHWRTAP LWNDSPFCFC MNANNNTYSC LRTINGTHNF LYCEFTTGLI TFYNLTIDRF ETINRAAGLT PGERSHMHDA LDQLKSCRGR SCSIRRHQNH LEGGSSAPLL PINQVHRNNK RKHSPLAGAV GNYAFVGPRL DMEALPPIKR RKLSKYNRLT GSQQSHMKRR PWKQTPLQQS PRFLRTHSVT PAQA // ID SUR1_DROME STANDARD; PRT; 300 AA. AC Q9U4F3; Q8MSH4; Q9VRZ8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE SURF1-like protein. GN SURF1 OR CG9943. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20086449; PubMed=10622737; RA Poyau A., Buchet K., Godinot C.; RT "Sequence conservation from human to prokaryotes of Surf1, a protein RT involved in cytochrome c oxidase assembly, deficient in Leigh RT syndrome."; RL FEBS Lett. 462:416-420(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 99-300 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLY INVOLVED IN THE BIOGENESIS OF THE COX COMPLEX CC (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SURF1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF182954; AAF19610.1; -. DR EMBL; AE003560; AAF50632.2; -. DR EMBL; AY118815; AAM50675.1; ALT_INIT. DR FlyBase; FBgn0029117; Surf1. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS. DR GO; GO:0015232; F:heme transporter activity; ISS. DR GO; GO:0008535; P:cytochrome c oxidase biogenesis; ISS. DR InterPro; IPR002994; Surf1. DR Pfam; PF02104; SURF1; 1. DR ProDom; PD024360; Surf1; 1. DR PROSITE; PS50895; SURF1; 1. KW Transmembrane; Mitochondrion; Inner membrane. FT TRANSMEM 60 82 POTENTIAL. FT TRANSMEM 271 291 POTENTIAL. SQ SEQUENCE 300 AA; 34064 MW; 59C6969FA0E9A9C1 CRC64; MIRLGNQMCR QVAFNIQTVF RNPGTANNPR LITRKMTQQR PPVNWTTSIP NQAAKDKEKI APLGWFLLLI PATTFGLGCW QVKRKIWKEQ LIKDLNKQLS TAPVALPDDL TDLAQMEYRL VKIRGRFLHD KEMRLGPRSL IRPDGVETQG GLFSQRDSGN GYLIVTPFQL ADRDDIVLVN RGWVSRKQVE PETRPLGQQQ AEVELTAVVR KGEARPQFTP DHKGNVYLYR DLARMCAATG AAPVFLDAVY DPQTAAHAPI GGQTRVTLRN DHLSYLVTWF SLSAATSFLW YRQIVKRIPF // ID SUR4_DROME STANDARD; PRT; 270 AA. AC O18405; Q9VF84; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Surfeit locus protein 4 homolog. GN SURF4 OR SURF-4 OR CG6202. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96413309; PubMed=8816471; RA Armes N., Fried M.; RT "Surfeit locus gene homologs are widely distributed in invertebrate RT genomes."; RL Mol. Cell. Biol. 16:5591-5596(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. ENDOPLASMIC CC RETICULUM (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SURF4 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y14823; CAA75100.1; -. DR EMBL; AE003708; AAF55176.1; -. DR FlyBase; FBgn0019925; Surf4. DR InterPro; IPR002995; Surf4. DR Pfam; PF02077; SURF4; 1. DR ProDom; PD010195; Surf4; 1. DR PROSITE; PS01339; SURF4; 1. KW Transmembrane; Endoplasmic reticulum. FT TRANSMEM 65 85 POTENTIAL. FT TRANSMEM 93 113 POTENTIAL. FT TRANSMEM 115 135 POTENTIAL. FT TRANSMEM 178 198 POTENTIAL. FT TRANSMEM 206 226 POTENTIAL. FT TRANSMEM 243 263 POTENTIAL. FT SITE 267 268 ENDOPLASMIC RETICULUM RETRIEVAL MOTIF FT (POTENTIAL). SQ SEQUENCE 270 AA; 30545 MW; FEFA7D525A83C890 CRC64; MSIPNEYIAK TEDVAEQVIK RGKNVLPTVA RLCLIATFFE DGLRMYIQWN EQREYMDMSW GCGKFLATVF VLVNLLGQLG GCGMVMARFK VDIAVGLLFF IVVLQTVAYS ILWDFQFLLR NFALIGALLL VLAEARIEGR SLFAGVPSMG ENKPKNFMQL AGRILLAFMF ITLIRFELSV WQVIQDIIGS ILMVLVVLGY KTKLSALILV ALLTILNLYH NAWWTIPSYK PLRDFLKYDF FQTLSVIGGL LMIVSLGPGG VSMDEHKKKW // ID SUR6_DROME STANDARD; PRT; 324 AA. AC Q9VDS6; Q8MQW1; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Surfeit locus protein 6 homolog. GN SURF6 OR CG4510. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN A NUCLEOLAR FUNCTION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR; NUCLEOLAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SURF6 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003728; AAF55714.1; -. DR EMBL; AY122261; AAM52773.1; ALT_INIT. DR FlyBase; FBgn0038746; Surf6. DR GO; GO:0005730; C:nucleolus; NAS. DR GO; GO:0015232; F:heme transporter activity; NAS. DR GO; GO:0008535; P:cytochrome c oxidase biogenesis; NAS. DR InterPro; IPR007019; SURF6. DR Pfam; PF04935; SURF6; 1. KW Nuclear protein. SQ SEQUENCE 324 AA; 38135 MW; 436FB29440B0E12D CRC64; MTQAEIVKCL REEYEIEHNK DQKPEKEDLP AITKKFYQRV LELLTIHKVP YSKQEDEETY EEYLLSDTEE SGNKKKKQQG KLKNQDSDDE DVEARIASIK NKLRQKKGPT TERQQKRRES KKLKRSKGVQ KLLLSSAKNL KNENVKHQKL KNGVVKSEQE TEDSKEQIQP VKVQPVYNQE AKIVYSKVDF AANPGGKAKK SHQNPKEILK KLRDTKKHLT ELREQGETDK AAEIQTDIAW RNAFDKVEGK KVKDDTKLLQ KAIKKRRVEK KKSKTKWTER KQKVEHDKEK RQKKRQENLE KRSKDKKNRK LKTASKRGRI IPGY // ID SUS_DROME STANDARD; PRT; 1322 AA. AC P22293; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Suppressor of sable protein. GN SU(S). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=91117256; PubMed=1703632; RA Voelker R.A., Gibson W., Graves J.P., Sterling J.F., Eisenberg M.T.; RT "The Drosophila suppressor of sable gene encodes a polypeptide with RT regions similar to those of RNA-binding proteins."; RL Mol. Cell. Biol. 11:894-905(1991). RN [2] RP SEQUENCE OF 1-9 FROM N.A. RX MEDLINE=91169252; PubMed=1963868; RA Voelker R.A., Graves J.P., Gibson W., Eisenberg M.T.; RT "Mobile element insertions causing mutations in the Drosophila RT suppressor of sable locus occur in DNase I hypersensitive subregions RT of 5'-transcribed nontranslated sequences."; RL Genetics 126:1071-1082(1990). CC -!- FUNCTION: AFFECTS THE TRANSCRIPT LEVELS OF THOSE ALLELES THAT IT CC SUPPRESSES. MAY BE INVOLVED IN RNA METABOLISM. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: AT ALL STAGES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M57889; AAA28920.1; -. DR EMBL; X59364; CAA42010.1; -. DR FlyBase; FBgn0003575; su(s). DR InterPro; IPR000571; Znf_CCCH. DR Pfam; PF00642; zf-CCCH; 2. KW RNA-binding; Nuclear protein. FT DOMAIN 138 327 HIGHLY CHARGED DOMAIN. FT DOMAIN 446 474 GLN-RICH (OPA-REPEAT). FT DOMAIN 1087 1162 RNA-BINDING (BY SIMILARITY). SQ SEQUENCE 1322 AA; 143555 MW; D5F534EB5702EA08 CRC64; MSVALADEPL IDLEEDLEDG EIDDDEEDEQ QSSKIQVQKK TFVGDDDVQF VGVEAKNQND DEDVVYVGPS TDAVCLQNSN STKSKKPRPL EDDHASSIEL AIANALKKKG IEPPMPRMRS SNQDTSDQSL EGSGEGLATA NPLLQSTRSS RRRKRKKERE REQKKDKEQQ NRSRRDENDV SVVPGGVEDM DEYEMMNVRG GSPPPGGAAP PLSSCGQRFS GADWDMDDGS AATGAAGLGA GGGGGYNSHS SYDSYSDEET NGPGLMNQRR RTRRDNEKEH QRGVNNRKRR DRDRLEGGLA GSGSKRNRRD SGEGGGGGQE KMGGSNRVEP RKLELCKFYL MDCCAKRDKC SYMHKEFPCK YYYLGMDCYA GDDCLFYHGE PLSEQLRNVL LKHMETAPKE ILGDFKRISR DIAIVQMTRR HEQLCDQLNR ENTWNSIGCG LMGKRQDHQM QQQQQQLQHQ QLQQQQEQQQ TQQQAAADGG GCIPSLLDMV INPPLSENKR KSRWTEKMGA KAAAGAAGSS ERDSTSPDAK PLPPHLDLAN LSHVLSAENM AKLNKLGITN LEQMLQVPFG QLTEAGLTLV EIGEIQRKAE DAKPQTQAEL ESSTPPSKRE TEANNSNSKS NGLIMVDYTQ YLKDAHVSFS GNDPLDDDRD DDEQLIIDDG NDSTAEEDQQ PKKAKAPPAA THESSTEEAP LPSVFDLPSF MNNMLGQGSS ARQLLPASAN QENAHLPGGD QSTHKSAPIG GGTSTNVLGR ILFGDKQSDP EARAAFYRDI IRNPFKAHSG DGDVDSSNEN SNSNSHSLTP TPTPEPGSQS PKPEDHDQDM PELPVIAPAL PPTTPSLYVR RSMYDFDPVK EQEHGRQELL TEEKEQYQRD TDMRLPFEPM KHYMPATEID AAIFSHTPIR WQLHEVTIEE SSYAQIRASA LHKEQRELRD PRMRRILGLP ETPDNSGPLG SVPIMGPSSF SVDNIARCAT TIASPDLETA VRDSTPSSPP PSVVNLPSMS VPPPSMRVPP PNIQVEKPTV RTDPRRDPRR AVLQAPTKGA STANTTAPNA SGGSKQISEI RSLLQVSNWY NNLGTNNKIM VNQQLALVFT ELKKFHQLPN DAPKIFDVSF IVNNTTLQQI FAKLFIFVDD NGEVVQIPEE PNGNGAALGG GGDSGGGVGG GGGGGGVVLP NLSQPPPNLS QMLRLPPPNI RMLRMSGMMM QMGNVGPPFN QPPPRGGLMG MPPNGNGLNQ GVGNLGGLGQ LGINQGGGPV PNGNPFNPFG GNNGGGAGVM NNMNSMGNMG MGFNNFNNNG GRGGHFPGGG SGGNGNGNNR NQRGGNHRNR NI // ID SUUR_DROME STANDARD; PRT; 962 AA. AC Q9VTE2; Q9N6U5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Suppressor of Underreplication protein. GN SUUR OR SU(UR)ES OR CG7869. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=21898319; PubMed=11901119; RA Makunin I.V., Volkova E.I., Belyaeva E.S., Nabirochkina E.N., RA Pirrotta V., Zhimulev I.F.; RT "The Drosophila suppressor of underreplication protein binds to RT late-replicating regions of polytene chromosomes."; RL Genetics 160:1023-1034(2002). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP SUBCELLULAR LOCATION. RX MEDLINE=22530965; PubMed=12644953; RA Zhimulev I.F., Belyaeva E.S., Makunin I.V., Pirrotta V., Volkova E.I., RA Alekseyenko A.A., Andreyeva E.N., Makarevich G.F., Boldyreva L.V., RA Nanayev R.A., Demakova O.V.; RT "Influence of the SuUR gene on intercalary heterochromatin in RT Drosophila melanogaster polytene chromosomes."; RL Chromosoma 111:377-398(2003). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=22344761; PubMed=12456726; RA Zhimulev I.F., Belyaeva E.S., Semeshin V.F., Shloma V.V., RA Makunin I.V., Volkova E.I.; RT "Overexpression of the SuUR gene induces reversible modifications at RT pericentric, telomeric and intercalary heterochromatin of Drosophila RT melanogaster polytene chromosomes."; RL J. Cell Sci. 116:169-176(2003). CC -!- FUNCTION: REQUIRED FOR UNDERREPLICATION OF DNA, WHICH IS FOUND IN CC MANY LATE REPLICATING EUCHROMATIC REGIONS OF SALIVARY GLAND CC POLYTENE CHROMOSOMES. CONTROLS CHROMATIN ORGANIZATION IN POLYTENE CC CHROMOSOMES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. BINDS TO POLYTENE CHROMOSOMES FROM CC SALIVARY GLANDS; LOCALIZED AT LATE-REPLICATING INTERCALARY CC HETEROCHROMATIN AND PERICENTRIC HETEROCHROMATIN. COLOCALIZES WITH CC MANY POLYCOMB GROUP PROTEINS BINDING SITES ON POLYTENE CC CHROMOSOMES. CC -!- TISSUE SPECIFICITY: EXPRESSED THROUGHOUT DEVELOPMENT. WEAKLY CC EXPRESSED. EXPRESSED AT HIGHER LEVEL IN EMBRYOS AND ADULT FEMALES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ277592; CAB89187.1; -. DR EMBL; AE003546; AAF50110.3; -. DR EMBL; BT010066; AAQ22535.1; -. DR FlyBase; FBgn0025355; SuUR. DR InterPro; IPR000330; SNF2_N. DR Pfam; PF00176; SNF2_N; 1. KW Chromatin regulator; Nuclear protein; Developmental protein. SQ SEQUENCE 962 AA; 107624 MW; 5063FB88E875C4F9 CRC64; MYHFVSEQTP EVRLTDEALV TSHVTQYLKS FQLDAVRFVY DRLAKREFCI LNDESGLGKV ATVAALLSAL PPAKKTLVVL QNDEQLLTGW RFHLDTLTDL QVYIIQGVQD TTDSPHSVYL AKWSQLRSIG DLSRLKFDYI MVDNRGHSLN NSFCTSMLLK QFEGRVNVLI SSVDVTSDVR LLYNVLRLGG RLEHQYKSFA SFDRKFHLPD PKEVFSKRID LEEYYKQRGF LSEYIKDFRL RRFRHQFDKS LPLVAPEQYK HNLNLWLASK NSQSTISGSD VCSTIASIDN NPAQQNKTGL FEETDRLSEH SVDDVAMSPL IFEYSESDDE PLTVEPDADQ NPVLVVSSDD CEIVTPPSTP QNRTPSLNES PRTKSKKKFS KKTSPRKKAD LTDSEEDDEA TDNMPPRKRT RAATVHLTPK TRRLNVRILR VSLDTLSTPP PSRTTTAIVT PKTEPTARRK NLKKRTVSPV DVGRPATRGM QRLTRSAETK INSKYLKHRS LDDVKRSFPR RVKLEGNQTP RSSKQIVKQE PKSKVGQEKK QKTVDVPAQG TAKRKPGRPR KCQTKTEDLG KTKTKPNSKH LPPTPQVLSG SSLSSEYMQC AQRIPDNLDA IESPAFRVPF TPQQTPMLLT LPSTHNLLND SEVVSIPLYK DPVETVVINS SHDECSPQDP SQSRRTKALK RKRKPVTSVN SSFGGGLGLP PAKRSANKSP DLFSISSEHS QIPLAQPRPS SPFEGFKIFG SEVKQFQQQL AKVNISVPKK KRDRSCLDIL EQMFEPRQQQ SAKTSPKVLP TLPLTQKDDA ESTITQRRRT LLEDDFFEIT NNGQFGSRMR LNSSGEVSPV QPDQQSVRPS QANKITNYLI GSGITQERTQ PSNGNRNSIL ASLRKSPKSP KQGAKSTQAT KLTRWFGSVF GGGASQTSSV ESVSAPSTPV NSSTSAAACQ TRSARSGGAS GPTKRKRLEL FK // ID SUV3_DROME STANDARD; PRT; 1169 AA. AC P20193; DT 01-FEB-1991 (Rel. 17, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Suppressor of variegation protein 3-7. GN SUVAR(3)7. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95223788; PubMed=7708496; RA Cleard F., Matsarskaia M., Spierer P.; RT "The modifier of position-effect variegation Suvar(3)7 of Drosophila: RT there are two alternative transcripts and seven scattered zinc RT fingers, each preceded by a tryptophan box."; RL Nucleic Acids Res. 23:796-802(1995). RN [2] RP ERRATUM. RA Cleard F., Matsarskaia M., Spierer P.; RL Nucleic Acids Res. 23:3804-3804(1995). RN [3] RP SEQUENCE OF 255-1169 FROM N.A. RX MEDLINE=90190836; PubMed=2107402; RA Reuter G., Giarre M., Farah J., Gausz J., Spierer A., Spierer P.; RT "Dependence of position-effect variegation in Drosophila on dose of a RT gene encoding an unusual zinc-finger protein."; RL Nature 344:219-223(1990). RN [4] RP INTERACTION WITH SU(VAR)39. RX MEDLINE=21856321; PubMed=11867540; RA Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S., RA Jenuwein T., Dorn R., Reuter G.; RT "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation RT and heterochromatic gene silencing."; RL EMBO J. 21:1121-1131(2002). CC -!- FUNCTION: THIS PROTEIN IS A DOSE-LIMITING FACTOR IN POSITION- CC EFFECT VARIEGATION, THE INACTIVATION IN SOME CELLS OF A GENE CC TRANSLOCATED NEXT TO HETEROCHROMATIN. IT COULD PLAY A ROLE IN CC CHROMOSOME CONDENSATION. CC -!- SUBUNIT: INTERACTS WITH SU(VAR)39. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52187; CAA36434.1; -. DR PIR; S09151; S09151. DR FlyBase; FBgn0003598; Su(var)3-7. DR InterPro; IPR004210; BESS_motif. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF02944; BESS; 1. DR SMART; SM00355; ZnF_C2H2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. KW Zinc-finger; Nuclear protein; DNA-binding; Metal-binding; Repeat. FT ZN_FING 136 155 C2H2-TYPE. FT ZN_FING 238 262 C2H2-TYPE. FT ZN_FING 344 365 C2H2-TYPE. FT ZN_FING 406 431 C2H2-TYPE. FT ZN_FING 526 548 C2H2-TYPE. FT ZN_FING 656 680 C2H2-TYPE. FT ZN_FING 748 771 C2H2-TYPE. FT DOMAIN 844 1057 BINDS TO SU(VAR)39. FT DOMAIN 86 92 POLY-ASP. FT DOMAIN 589 592 POLY-GLU. FT DOMAIN 780 788 POLY-ALA. FT DOMAIN 1008 1011 POLY-ASN. FT DOMAIN 1113 1116 POLY-ASN. SQ SEQUENCE 1169 AA; 131110 MW; A2B9380941645328 CRC64; MRDDPCIEDI MDDEHAPLVA ELQSALNNPD DKQASEDPLL EDQEREPDAM STKTEPSSDA ESSHSYHDPM GLLERIEIHD PGDSQDDDDE DDESSNGGGV DGGMRRKMPR AQRWLLWMKR WPWILHEDSD GTLAFCLYCN ISINVNNRSR HIQQHNVSLS HQERECNYLA FKKSEEETRG AISSNEIKHE FGTKSYVAAM KQKRISETEA FNNFNWLRWL RWHPWLERSM PTGTIGTCRI CSVRMNVEFV YLRKRHETTK GHMEALRNLD SDKRSRKRKR SKSNSVTNSG GDEAEREKES EPEAGPEDAQ DTPVVMMNGD VDSGDDPGKW CALIPDTNPQ QCRCTLCNCT MAITSFLRHC KTRAHCHMLS TPAEKGSSDI RGIWAVFADM HPWLIADPED PSIGYCSVCR KRFMYGNSEI KRKNHEKSEK HTLALASAKA GIEVGSADGR GGDNMDEEEA AASDQAQSSQ TDDSEDNDDD NWSEIQKLGK GFAHKSSSEP RKATVRAGVR FYPWLCYSKD RKTQICKFCR VRFHNEAAKA RHELSARHVK LVKQFKMRQA KLHQGTNTQT KHNAQDDEES QEQDEEYGEE EEDAEEDSQS NFDLGTVQAR KTARADNKLF VKPIPATMKG KVMVWKGRFP WLSYKKNEQR GNYAWCKLCE VSLYLPSSKW ASKHQRTSRH IRLRIDRKRN GGNPLKTSNK NSGEISTVVA TASALASAEA RQKAAMAELQ AKYDWLDPDA NDENHCHCRV CDSRLPIKVF YLRQHDASRK HVENKERQRA NAAAAANAPS VSPTSTVDAE RQESGMDKES ENDMSVRSDG STAEPLAKRS RRSMEVRRII RALRDSMGKR QEERSQMDMA RNMICSSFDI VTRLRTLERE SVAHNESMAQ APPSVTVSPI KPPEPRHVMD LFFDSISPTM KSLPPDLAAE GKSKIMQLVC SLELRAMQRN ATTPTPATVS ASSKWPSSTT VTPVKTPPAP ISAPLASVDA DLHSSVVTTP HEYNNGQNNN NDKETVPKEP VTGASSAQVT INGSAKDLPE NIRRILTSNQ TQVTNRLETD SVRCVPVDKL TTQSRTNANG RLSQGGTSEA PSTPQADLSN GNTLAMIRQI RANNNNSSKI TVTNTPQMQQ PQQAQASITS STPIMRGGPS SNGCQITTFR TMVNHNRRP // ID SUV9_DROME STANDARD; PRT; 635 AA. AC P45975; Q9VFA6; DT 01-NOV-1995 (Rel. 32, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Histone-lysine N-methyltransferase, H3 lysine-9 specific (EC 2.1.1.43) DE (Histone H3-K9 methyltransferase) (H3-K9-HMTase) (Suppressor of DE variegation protein 3-9). GN SU(VAR)3-9 OR CG6476. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94349930; PubMed=7915232; RA Tschiersch B., Hofmann A., Krauss V., Dorn R., Korge G., Reuter G.; RT "The protein encoded by the Drosophila position-effect variegation RT suppressor gene Su(var)3-9 combines domains of antagonistic RT regulators of homeotic gene complexes."; RL EMBO J. 13:3822-3831(1994). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=Karsnas; RX MEDLINE=20519450; PubMed=11063691; RA Krauss V., Reuter G.; RT "Two genes become one: the genes encoding heterochromatin protein RT Su(var)3-9 and translation initiation factor subunit eIF-2gamma are RT joined to a dicistronic unit in holometabolic insects."; RL Genetics 156:1157-1167(2000). RN [3] RP REVISION TO 509. RA Schotta G., Ebert A., Lein S., Kubicek S., Krauss V., Jenuwein T., RA Reuter F.; RT "Histone H3-K9 methylation potential of Drosophila Su(var)3-9 mutants RT correlates with extent of gene silencing."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP INTERACTION WITH HDAC1. RX MEDLINE=21486105; PubMed=11571273; RA Czermin B., Schotta G., Huelsmann B.B., Brehm A., Becker P.B., RA Reuter G., Imhof A.; RT "Physical and functional association of SU(VAR)3-9 and HDAC1 in RT Drosophila."; RL EMBO Rep. 2:915-919(2001). RN [6] RP ENZYMATIC ACTIVITY, AND INTERACTION WITH SU(VAR)205 AND SU(VAR)3-7. RX MEDLINE=21856321; PubMed=11867540; RA Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S., RA Jenuwein T., Dorn R., Reuter G.; RT "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation RT and heterochromatic gene silencing."; RL EMBO J. 21:1121-1131(2002). CC -!- FUNCTION: MAJOR HISTONE METHYLTRANSFERASE. METHYLATES LYS-9 OF CC HISTONE H3. H3 LYS-9 METHYLATION REPRESENTS A SPECIFIC TAG FOR CC EPIGENETIC TRANSCRIPTIONAL REPRESSION BY RECRUITING SU(VAR)205/HP1 CC TO METHYLATED HISTONES. SEEMS TO BE INVOLVED IN HETEROCHROMATIC CC GENE SILENCING INCLUDING THE MODIFICATION OF POSITION-EFFECT- CC VARIEGATION. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE + HISTONE L-LYSINE = CC S-ADENOSYL-L-HOMOCYSTEINE + HISTONE N(6)-METHYL-L-LYSINE. CC -!- SUBUNIT: INTERACTS WITH SU(VAR)205 AND SU(VAR)3-7. PROBABLY CC ASSOCIATES WITH HDAC1. CC -!- SUBCELLULAR LOCATION: NUCLEAR; ASSOCIATES WITH CENTROMERIC CC HETEROCHROMATIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Isoforms A and B share the first 80 amino acid residues. CC Experimental confirmation may be lacking for some isoforms; CC Name=A; Synonyms=Su(var)3-9; CC IsoId=P45975-1; Sequence=Displayed; CC Name=B; Synonyms=eIF-2-gamma; CC IsoId=Q24208-1; Sequence=External; CC Name=C; CC IsoId=Q24208-2; Sequence=External; CC -!- SIMILARITY: BELONGS TO THE HISTONE-LYSINE METHYLTRANSFERASE CC FAMILY. SUVAR3-9 SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 CHROMO DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SET DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PRE-SET DOMAIN. CC -!- SIMILARITY: CONTAINS 1 POST-SET DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X80070; CAA56376.1; -. DR EMBL; AJ290956; CAB93768.2; -. DR EMBL; AE003708; AAF55154.1; -. DR PIR; S47004; S47004. DR FlyBase; FBgn0003600; Su(var)3-9. DR InterPro; IPR000953; Chromo. DR InterPro; IPR000795; EF_GTPbind. DR InterPro; IPR003616; PostSET. DR InterPro; IPR007728; Pre-SET. DR InterPro; IPR001214; SET. DR InterPro; IPR003606; Zn2-binding. DR Pfam; PF00385; chromo; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF05033; Pre-SET; 1. DR Pfam; PF00856; SET; 1. DR SMART; SM00298; CHROMO; 1. DR SMART; SM00508; PostSET; 1. DR SMART; SM00468; PreSET; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 1. DR PROSITE; PS50868; POST_SET; 1. DR PROSITE; PS50867; PRE_SET; 1. DR PROSITE; PS50280; SET; 1. KW Transferase; Methyltransferase; Chromatin regulator; Nuclear protein; KW Alternative splicing. FT DOMAIN 81 188 BINDS TO SU(VAR)205 AND SUVAR(3)7. FT DOMAIN 219 278 CHROMO. FT DOMAIN 410 474 PRE-SET. FT DOMAIN 476 607 SET. FT DOMAIN 619 635 POST-SET. FT CONFLICT 275 275 T -> I (IN REF. 4). FT CONFLICT 509 509 G -> E (IN REF. 1). FT CONFLICT 627 627 R -> A (IN REF. 4). SQ SEQUENCE 635 AA; 71903 MW; 4154A49F54B60E14 CRC64; MATAEAQIGV NRNLQKQDLS NLDVSKLTPL SPEVISRQAT INIGTIGHVA HGKSTVVKAI SGVQTVRFKN ELERNITIKL ERLSEKKIKN LLTSKQQRQQ YEIKQRSMLR HLAELRRHSR FRRLCTKPAS SSMPASTSSV DRRTTRRSTS QTSLSPSNSS GYGSVFGCEE HDVDKIPSLN GFAKLKRRRS SCVGAPTPNS KRSKNNMGVI AKRPPKGEYV VERIECVEMD QYQPVFFVKW LGYHDSENTW ESLANVADCA EMEKFVERHQ QLYETYIAKI TTELEKQLEA LPLMENITVA EVDAYEPLNL QIDLILLAQY RAAGSRSQRE PQKIGERALK SMQIKRAQFV RRKQLADLAL FEKRMNHVEK PSPPIRVENN IDLDTIDSNF MYIHDNIIGK DVPKPEAGIV GCKCTEDTEE CTASTKCCAR FAGELFAYER STRRLRLRPG SAIYECNSRC SCDSSCSNRL VQHGRQVPLV LFKTANGSGW GVRAATALRK GEFVCEYIGE IITSDEANER GKAYDDNGRT YLFDLDYNTA QDSEYTIDAA NYGNISHFIN HSCDPNLAVF PCWIEHLNVA LPHLVFFTLR PIKAGEELSF DYIRADNEDV PYENLSTAVR VECRCGRDNC RKVLF // ID SUWA_DROME STANDARD; PRT; 1042 AA. AC P12297; Q24543; DT 01-OCT-1989 (Rel. 12, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Suppressor of white apricot protein. GN SU(WA). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88166654; PubMed=2832151; RA Chou T.-B., Zachar Z., Bingham P.M.; RT "Developmental expression of a regulatory gene is programmed at the RT level of splicing."; RL EMBO J. 6:4095-4104(1987). RN [2] RP FUNCTION, AND ALTERNATIVE SPLICING. RX MEDLINE=88166655; PubMed=3443103; RA Zachar Z., Chou T.-B., Bingham P.M.; RT "Evidence that a regulatory gene autoregulates splicing of its RT transcript."; RL EMBO J. 6:4105-4111(1987). RN [3] RP CHARACTERIZATION OF RS DOMAIN. RX MEDLINE=92005712; PubMed=1655279; RA Li H., Bingham P.M.; RT "Arginine/serine-rich domains of the su(wa) and tra RNA processing RT regulators target proteins to a subnuclear compartment implicated in RT splicing."; RL Cell 67:335-342(1991). CC -!- FUNCTION: REGULATOR OF PRE-MRNA SPLICING (AND, POSSIBLY, OF OTHER CC RNA PROCESSING EVENTS). REGULATE ITS OWN EXPRESSION AT THE LEVEL CC OF RNA PROCESSING. CC -!- SUBCELLULAR LOCATION: NUCLEAR; SPECKLED SUBNUCLEAR COMPARTMENT. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P12297-1; Sequence=Displayed; CC Name=Short; CC IsoId=P12297-2; Sequence=VSP_004436; CC -!- DEVELOPMENTAL STAGE: THREE MRNAS ARE PRODUCED DURING DEVELOPMENT. CC THE SMALLEST OF THESE (3.5 KB RNA) IS THE MAJORITY SPECIES DURING CC PRECELLULAR BLASTODERM DEVELOPMENT AFTER WHICH ITS LEVELS DROP CC RAPIDLY, BUT PERSISTS AS A MINORITY SPECIES THROUGHOUT THE REST OF CC THE LIFE OF THE ORGANISM. THE LARGER TWO TRANSCRIPTS (4.4 AND 5.2 CC KB RNAS) FIRST APPEAR AROUND CELLULAR BLASTODERM AND LEVELS CC INCREASE SUBSTANTIALLY DURING NEXT FEW HOURS AND ARE THE CC PREPONDERANT RNA SPECIES THROUGHOUT THE REMAINDER OF THE LIFE OF CC THE ORGANISM. CC -!- DOMAIN: RS DOMAIN DIRECTS LOCALIZATION OF PROTEINS TO THE SPECKLED CC SUBNUCLEAR COMPARTMENT AND THE PURPOSE OF THIS LOCALIZATION IS TO CC ALLOW COLOCALIZATION AND CO-CONCENTRATION OF COMPONENTS OF THE CC SPLICING AND SPLICING REGULATORY MACHINERY TO PERMIT RELATIVELY CC HIGH RATES AND/OR EFFICIENCIES OF REACTION AND INTERACTON. CC -!- SIMILARITY: CONTAINS 2 SURP MOTIF REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06589; CAA29812.1; -. DR EMBL; X06589; CAA29813.1; -. DR PIR; S06028; S06028. DR FlyBase; FBgn0003638; su(w[a]). DR InterPro; IPR000061; Surp. DR Pfam; PF01805; Surp; 2. DR SMART; SM00648; SWAP; 2. DR PROSITE; PS50128; SURP; 2. KW Transcription regulation; RNA-binding; mRNA splicing; Repeat; KW Nuclear protein; Alternative splicing. FT DOMAIN 47 50 POLY-SER. FT DOMAIN 51 177 DRY CEEERYL MOTIF. FT REPEAT 313 355 SURP MOTIF 1. FT REPEAT 562 602 SURP MOTIF 2. FT DOMAIN 528 533 POLY-GLU. FT DOMAIN 640 643 POLY-ALA. FT DOMAIN 826 829 POLY-ASP. FT DOMAIN 829 964 ARG/SER-RICH (RS DOMAIN). FT DOMAIN 1035 1038 POLY-ARG. FT VARSPLIC 100 177 Missing (in isoform Short). FT /FTId=VSP_004436. SQ SEQUENCE 1042 AA; 114928 MW; E564006EE163C3B3 CRC64; MLPYNVRNAG GGSVGGILRR TGQGSGTGST ILGNGNSPGA LGAGKVSSSS LENHRQPPLE LLVFGYACKI FRDDEKAREM DHGKQLIPWM GDVNLKIDRL IIGTNPSNNY TINQYAHHCH KHTHTATYPP MSCPVRTTLP HTAAVKLLAE SDTYIYVGIV IDGIVIMALE DRACRYLYDV RGALCELAPH EAPPGGYGNR LEYLSAEEQR AEQLCEEERY LFLYNNEEEL RLRQEEDLKR LQQETSGGCF SQVGFQYDGQ SAASTSIGGS STATSQLSPN SEESELPFVL PYTLMMAPPL DMQLPETMKQ HAIIEKTARF IATQGAQMEI LIKAKQANNT QFDFLTQGGH LQPYYRHLLA AIKAAKFPPA PQTPLDQQNT DKEAPSADDH SEEVAGGRRN PNQVVITVPT IKYKPSANCA YTQLISKIKG VPLQAVLQED ESSNPGNSQH SGGTASPALS CRSEGHNSQG GEFTPVLLQY NGSTFTHEEE SSNREQQDDN DVNGGEPPQV ELLKNTSALA LAQNYSSESE EEEDQVQPEK EEEKKPEPVL TFPVPKDSLR HIIDKTATYV IKNGRQFEET LRTKSVDRFS FLLPANEYYP YYLYKVTGDV DAASKEEKTR KAAAVAAALM SKKGLSFGGA AAAVSGSNLD KAPVSFSIRA RDDQCPLQHT LPQEASDEET SSNAAGVEHV RPGMPDSVQR AIKQVETQLL ARTAGQKGNI TASPSCSSPQ KEQRQAEERV KDKLAQIARE KLNGMISREK QLQLERKRKA LAFLNQIKGE GAIVGSAVPV VGPNPPESAA GAATADSGDE SGDSVRSIPI TYFGPDDDDE VGEQRPEMRL IGSTQKDEED DDEEDGGDLE KYNLLNDDST NTFTSKPVLP PTAAPPPAAV LLSDDDDVQL VATTSTRSSS SRHLKTHRRS RSRSKNVRSS DSSPSSRESS RRRRQKSSRL SREPSSNPPR KSHHSSTQRK KTPKKRRRSK SRSRSKSIRR SRSISILRNN RRSRSRSPSC RNAEQRRQQD RRRTPTKKSH KRHKRRRRSS SP // ID SUZ2_DROME STANDARD; PRT; 1365 AA. AC P25172; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Suppressor 2 of zeste protein (Protein posterior sex combs). GN SU(Z)2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=91279476; PubMed=2057369; RA Brunk B.P., Adler P.N.; RT "The sequence of the Drosophila regulatory gene Suppressor two of RT zeste."; RL Nucleic Acids Res. 19:3149-3149(1991). CC -!- FUNCTION: REGULATES EXPRESSION OF THE HOMEOTIC SELECTOR GENES BY CC INFLUENCING HIGHER-ORDER CHROMATIN STRUCTURE THROUGH INTERACTION CC WITH OTHER PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56798; CAA40134.1; -. DR EMBL; X56799; CAA40135.1; -. DR PIR; S14871; S14871. DR FlyBase; FBgn0008654; Su(z)2. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Zinc-finger; Developmental protein; DNA-binding; Nuclear protein. FT ZN_FING 35 74 RING-TYPE. FT DOMAIN 623 628 POLY-GLN. FT DOMAIN 1077 1096 POLY-ASN. FT DOMAIN 1241 1251 POLY-SER. FT CONFLICT 603 603 MISSING (IN REF. 1; CAA40134). FT CONFLICT 785 785 K -> N (IN REF. 1; CAA40134). FT CONFLICT 831 831 A -> R (IN REF. 1; CAA40134). FT CONFLICT 965 965 MISSING (IN REF. 1; CAA40134). FT CONFLICT 1065 1065 D -> E (IN REF. 1; CAA40134). FT CONFLICT 1076 1076 MISSING (IN REF. 1; CAA40134). FT CONFLICT 1287 1287 A -> P (IN REF. 1; CAA40134). SQ SEQUENCE 1365 AA; 146058 MW; 7B4BA0F35B0FA683 CRC64; MHLQNTHNTM ESNAAMDATS PASRDVRQFH DLITCRLCRG YMIDPTTVDY CYHTYCRSCI LKHLLRAVYC PECKASGGKE INELNLKSDD TLRSLIYKLV PGLYQRECKE LADFKEQHDL VDEQTTDEPE FFTTTELISL SLEYHPAMLH QCGPGEVPPT IYLQCAAGLP VELLKRFLCS KYNIETDNGL VEVEVTYKDE VLPTNFTLMD VAYCYNWSRE SPMAFCYRIL LYDNEQTKND ENNLSRINQD IEPEHSVRRS KSAKSVTFAE DLESEIDSGS PRSKVRCKTP PKVSPSSKNK RLTSSKREAE PESPVSNFKS LRSNDMRYSD YAVSKVKSEP EQEQFLLPRE REQQPLEANT NIVVSIPPSQ LRKSYVDAED FELKTANRKG VGHLPKLKIE LNSMKSKLSM PLSAGPRLED TSCSSSCSAQ QLDLETYAKN IGLKPIEQPL QQSASNPDSK YSPNASPMSS CSSSTNGSSS SLGTADASTS TSTSSSHRKR KKKHSKEPKD ANGKRKKLHA EISSQTDGKM KVKITAKPNH KLDFKRSHSL ASGELDLQKL KLDSTSTSEA LNRTLGEEAR SINSLVVGGA PTPPPTPTAE PEQQQQQQQQ QQQPQQQQQQ QQQQQQQQFV VLPKIKDLTL PTSPPLPPSL FKAYTPSTTP TAPHTVAGGK PKQQQQQMPQ QPQAVLQQSM AKTNPAKPPL SSNNNRKPNS GHFAVPQAPT HRNMYHMQRY QSTPSSIASA ANKMPKRSMS LDESHPAKQA RLSQAQAMAS SYAAKLHMQT SNQAKSQAAA FLPNPQMRSY GLPDLGSKPT LPMLCPASSS SQVTITPRPR ATPSIYSFSE PNIHVPALEI VRLPVNKQSA GGKGLTMPPL SPPATSSARL MGPPAALPKH AGHGHGAAKR SCQMPTMPMP LPLPLPMPMT TIPAIVKSPP LSVALSGQRN NKGNSSNSNA YRTSPPALIN LRNTAAPQHS FPSKSSPKVE ANSKKSPPAA GCQGKTNGTA ALDKSKTSLR EFRPAVQSAV TATATTSVTT AAGAGAGAGT GTGTALAKDA DILDLSANPG RSNNDAKLAP NSPPAGNNNN NNNNNNNNNN NNNNNNSTSN SLEAALNKIK QNISANSNGG PSTTSGSNSN GTTNGDDLQN LHMLSESATA REKISIKAAS SGNGSGSTSS SSAKPKNANA LVRPQNASVR SIPNPSALAF RNQPAAASTA ASISKPLTVR AEEKPKVSTS NPGSLSPTNT SSSSSSSSSG SSGCSAATSP RAMTKKPTTI DQVAANLNIR AEAKAAALAE EAPPVLSSNA AKSPELAKTT TAVALRPEPK ETPITVSAAS TLLTIPSAVS SVSAVPETMA KPPVQIANAP VASSA // ID SWA_DROME STANDARD; PRT; 548 AA. AC P40688; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Swallow protein. GN SWA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92217243; PubMed=1806330; RA Chao Y.-C., Donahue K.M., Pokrywka N.J., Stephenson E.C.; RT "Sequence of swallow, a gene required for the localization of bicoid RT message in Drosophila eggs."; RL Dev. Genet. 12:333-341(1991). RN [2] RP SUBCELLULAR LOCATION. RX MEDLINE=94116446; PubMed=7507030; RA Hegde J., Stephenson E.C.; RT "Distribution of swallow protein in egg chambers and embryos of RT Drosophila melanogaster."; RL Development 119:457-470(1993). CC -!- FUNCTION: HAS A ROLE IN LOCALIZING BICOID MRNA AT THE ANTERIOR CC MARGIN OF THE OOCYTE DURING OOGENESIS, AND A POORLY CHARACTERIZED CC ROLE IN NUCLEAR DIVISIONS IN EARLY EMBRYOGENESIS. CC -!- SUBUNIT: MAY BE CONSTITUTED OF AN HOMO- OR HETERODIMER. CC -!- SUBCELLULAR LOCATION: UNIFORMLY DISTRIBUTED IN EGGS, BECOMES CC LOCALIZED TO THE NUCLEI DURING EARLY MITOTIC DIVISIONS IN EARLY CC EMBRYOGENESIS. SWALLOW ENTERS EACH NUCLEUS AT THE BEGINNING OF CC MITOSIS, OCCUPIES A POSITION COMPLEMENTARY TO THAT OF CONDENSED CC CHROMATIN, AND LEAVES EACH NUCLEUS AT THE END OF MITOSIS. CC -!- TISSUE SPECIFICITY: FOUND IN EARLY EMBRYOS AND IN OVARIES. NOT CC DETECTABLE IN MALES OR IN FEMALE BODIES EXCLUDING OVARIES. CC -!- DEVELOPMENTAL STAGE: PRESENT THROUGHOUT OOGENESIS AND AFTER CC FERTILIZATION. PRESENT ONLY IN 0-6 HOUR EMBRYOS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56023; CAA39500.1; -. DR PIR; S20806; S20806. DR FlyBase; FBgn0003655; swa. DR GO; GO:0045450; P:bicoid mRNA localization; NAS. DR GO; GO:0019094; P:pole plasm mRNA localization; IMP. DR InterPro; IPR000504; RNA_rec_mot. KW Developmental protein; Nuclear protein; Mitosis. SQ SEQUENCE 548 AA; 62070 MW; B8E0351C7B005159 CRC64; MSLQDESFPT DELFDQLNNL SSSGARNTWF AEHHKPAVFE RDTAPFLEIC YADPDFDADG DVANKSAKTC VSDPVGRDQE DEDDYDEDVD GDDHKLGCEK APLGSGRSSK AVSYQDIHSA YTKRRFQHVT SKVGQYIAEI QAQDQKRRNV KFAGFQRVNS MPESLTPTLQ QVYVHDGDFK VDKNCQTHSN SDSNYNSNSN NSSSSFDRLL AENESLQQKI NSLRVEAKRL QGFNEYVQER LDRKTDDFVK MKCNFETLRT ELSECQQKLR RQQDNSQHHF MYHIRSATSA KATQTDFLVD TIPASGNVLV TPHPLGDLTY NSSKGSIELA LLSVAPSARV AQNPVQVQRA IHPQSLDFSS VSTEADGSGS GEHRVETSSR ALVRRTPAPN NSETSQPSSN DSAIEVEAHE EERPSSRRQW EQQGELISPR QWGQHEGMYY FDKRNNRVIE VMGFNISQGR NQSHDTIHNQ SINDSQTRLL VHSMSMSHLE AHDHFRSKRT TLGSRMLRFL GPCVRCRNGD PLNRSNVTYK DGLPAMPEEE FVDQRNQR // ID SWS_DROME STANDARD; PRT; 1425 AA. AC Q9U969; Q9W3M0; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Swiss cheese protein. GN SWS OR CG2212. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, ALTERNATIVE SPLICING, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-648 AND RP GLY-95. RX MEDLINE=97442511; PubMed=9295388; RA Kretzschmar D., Hasan G., Sharma S., Heisenberg M., Benzer S.; RT "The swiss cheese mutant causes glial hyperwrapping and brain RT degeneration in Drosophila."; RL J. Neurosci. 17:7425-7432(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: MAY PLAY A ROLE IN THE SIGNALING MECHANISM BETWEEN CC NEURONS AND GLIA THAT REGULATES GLIA WRAPPING DURING DEVELOPMENT CC OF THE ADULT BRAIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9U969-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q9U969-2; Sequence=Not described; CC -!- TISSUE SPECIFICITY: BOTH ISOFORMS ARE EXPRESSED IN CORTICAL CELL CC BODIES OF ADULT BRAIN. CC -!- DEVELOPMENTAL STAGE: ISOFORM LONG IS EXPRESSED IN ALL CC DEVELOPMENTAL STAGES WITH HIGHEST LEVELS IN YOUNG EMBRYOS AND CC ADULTS. ISOFORM SHORT IS DETECTED ONLY IN ADULT HEAD. CC -!- SIMILARITY: BELONGS TO THE UPF0028 (SWS) FAMILY. CC -!- SIMILARITY: CONTAINS 3 CYCLIC NUCLEOTIDE-BINDING DOMAINS. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z97187; CAB51772.1; -. DR EMBL; AE003442; AAF46305.3; -. DR FlyBase; FBgn0003656; sws. DR InterPro; IPR000595; cNMP_binding. DR InterPro; IPR002641; Patatin. DR InterPro; IPR001423; UPF0028. DR Pfam; PF00027; cNMP_binding; 3. DR Pfam; PF01734; Patatin; 1. DR SMART; SM00100; cNMP; 3. DR PROSITE; PS50042; CNMP_BINDING_3; 3. DR PROSITE; PS01237; UPF0028; 1. KW Developmental protein; Repeat; Alternative splicing. FT NP_BIND 174 301 CNMP 1. FT NP_BIND 482 611 CNMP 2. FT NP_BIND 598 727 CNMP 3. FT MUTAGEN 648 648 G->R: IN ALLELE SWS-5; AGE-DEPENDENT FT NEURODEGENERATION. FT MUTAGEN 956 956 G->D: IN ALLELE SWS-4; AGE-DEPENDENT FT NEURODEGENERATION. FT CONFLICT 18 18 I -> T (IN REF. 1). FT CONFLICT 452 452 G -> P (IN REF. 1). FT CONFLICT 785 785 R -> H (IN REF. 1). FT CONFLICT 1377 1377 T -> N (IN REF. 1). SQ SEQUENCE 1425 AA; 160572 MW; A7FEE533B1C2B628 CRC64; MDVLEMLRAS ASGSYNTIFS DAWCQYVSKQ ITATVYMYFA LVMMSLLFIA WFLYFKRMAR LRLRDEIARS ISTVTNSSGD MRGLRFRKRD KMLFYGRRML RKMKNVSGQM YSSGKGYKRR AVMRFARRIL QLRRDNMPLE MRTVEPPAEY LEETIEGSDR VPPDALYMLQ SIRIFGHFEK PVFLRLCKHT QLLELMAGDY LFKITDPDDS VYIVQSGMIN VYISNADGST LSLKTVRKGE SVTSLLSFID VLSGNPSYYK TVTAKAIEKS VVIRLPMQAF EEVFQDNPDV MIRVIQVIMI RLQRVLFTAL RNYLGLNAEL VQNHMRYKSV STMSGPINSQ TSQSSRQAPN GPPMVISQMN LMQSAVSGTG SSGVSVTVTR PPSSPSRHSR EEHTLSDPNP NPDGSFHGTT NLFTEVHGDA PNADLFHQQQ QQHSVGNLST RRSSITLMAP DGSHSCLQTP GVTTSIDMRL VQSSAVDSLR KELGLSEEDS HIIEPFVELR ELEPNVTLIT EGNADDVCVW FVMTGTLAVY QSNQDATRAK QDKSDMLIHF VHPGEIVGGL AMLTGEASAY TIRSRSITRI AFIRRAAIYQ IMRQRPRIVL DLGNGVVRRL SPLVRQCDYA LDWIFLESGR AVYRQDESSD STYIVLSGRM RSVITHPGGK KEIVGEYGKG DLVGIVEMIT ETSRTTTVMA VRDSELAKLP EGLFNAIKLR YPIVVTKLIS FLSHRFLGSM QTRSGSGAPG APVEANPVTH KYSTVALVPI TDEVPMTPFT YELYHSLCAI GPVLRLTSDV VRKQLGSNIF EAANEYRLTS WLAQQEDRNI ITLYQCDSSL SAWTQRCMRQ ADVILIVGLG DRSHLVGKFE REIDRLAMRT QKELVLLYPE ASNAKPANTL SWLNARPWVT KHHHVLCVKR IFTRKSQYRI NDLYSRVLLS EPNMHSDFSR LARWLTGNSI GLVLGGGGAR GAAHIGMLKA IQEAGIPVDM VGGVSIGALM GALWCSERNI TTVTQKAREW SKKMTKWFLQ LLDLTYPITS MFSGREFNKT IHDTFGDVSI EDLWIPYFTL TTDITASCHR IHTNGSLWRY VRSSMSLSGY MPPLCDPKDG HLLLDGGYVN NLPADVMHNL GAAHIIAIDV GSQDDTDLTN YGDDLSGWWL LYKKWNPFTS PVKVPDLPDI QSRLAYVSCV RQLEEVKNSD YCEYIRPPID KYKTLAFGSF DEIRDVGYVF GKNYFESMAK AGRLGRFNQW FNKEPPKRVN HASLNEYTFI DLAQIVCRLP ETYAVNTAEL FSEDEDCDGY ISEPTTLNTD RRRIQVSRAG NSLSFSETEM DSDVELDLKL ERKTDKSTQS SPPSNSRSDM RGKEEARHMS NWHWGVKHKD ETGSGATEAT KTQTGQEQEL QQEQQDQGAT AEQLVDKDKE ENKENRSSPN NETKN // ID SX14_DROME STANDARD; PRT; 472 AA. AC P40656; Q9U1H4; Q9W1E2; Q9W1E3; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative transcription factor SOX-14. GN SOX14 OR CG17263/CG3090. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Cremazy F., Berta P., Girard F.; RT "Cloning of Sox14, a new Drosophila sox gene."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 198-251 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92310993; PubMed=1614875; RA Denny P., Swift S., Brand N., Dabhade N., Barton P., Ashworth A.; RT "A conserved family of genes related to the testis determining gene, RT SRY."; RL Nucleic Acids Res. 20:2887-2887(1992). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ252125; CAB64387.1; -. DR EMBL; AE003462; AAF47126.2; ALT_SEQ. DR EMBL; X65667; CAA46618.1; -. DR PIR; S22935; S22935. DR HSSP; P48436; 1SX9. DR FlyBase; FBgn0005612; Sox14. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW Transcription regulation; DNA-binding; Nuclear protein. FT DOMAIN 99 102 POLY-ALA. FT DNA_BIND 187 255 HMG BOX. FT DOMAIN 286 289 POLY-ASN. FT CONFLICT 102 110 APKTPKTPE -> STEDPQDPG (IN REF. 1). FT CONFLICT 114 115 MISSING (IN REF. 1). SQ SEQUENCE 472 AA; 51288 MW; 4CBF221890995D40 CRC64; MIAKPNQATT EPPLSLRPGT VPTVPATTPA RPATITIQRR HPAPKADSTP HTLPPFSPSP SPASSPSPAP AQTPGAQKTQ SQAAITHPAA VASPSAPVAA AAPKTPKTPE PRSTHTHTHT HSQHFSPPPR ESEMDGERSP SHSGHEMTLS MDGIDSSLVF GSARVPVNSS TPYSDATRTK KHSPGHIKRP MNAFMVWSQM ERRKICERTP DLHNAEISKE LGRRWQLLSK DDKQPYIIEA EKLRKLHMIE YPNYKYRPQK KQTRSPGSLK PNQDADGCEA RNDTTNNNNS LTTLAINGTT TAGRKSKRST STCQSGSASK RLRNDSGDTS SKPKYEVKME SAEQLNSADI ILPSADNLIS YQSSEYLPLS TLSNADCDEK LHSELSSGPL ESRENLSEVV NRFLPLFLGG NEDSQLGVSS LTQSQHNQSD PTAGLMDNIS DISPINDREE LTEEVMVPAL PGGESIERRA HP // ID SX15_DROME STANDARD; PRT; 784 AA. AC P40657; Q9U1J5; Q9V6Y8; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative transcription factor SOX-15 (Sox50E). GN SOX15 OR SOX50E OR CG8404. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Larva; RA Loh S.H.Y., Whitworth A., Russell S.; RT "Sox50E, a Drosophila Sox domain gene expressed in the proximal region RT of the wing imaginal disc."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 226-279 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92310993; PubMed=1614875; RA Denny P., Swift S., Brand N., Dabhade N., Barton P., Ashworth A.; RT "A conserved family of genes related to the testis determining gene, RT SRY."; RL Nucleic Acids Res. 20:2887-2887(1992). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 689. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ250955; CAB63944.1; ALT_FRAME. DR EMBL; AE003815; AAF58279.2; -. DR EMBL; X65668; CAA46619.1; -. DR PIR; S22936; S22936. DR HSSP; P48436; 1SX9. DR FlyBase; FBgn0005613; Sox15. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW Transcription regulation; DNA-binding; Nuclear protein. FT DOMAIN 131 134 POLY-GLY. FT DNA_BIND 215 283 HMG BOX. FT DOMAIN 731 735 POLY-HIS. FT CONFLICT 12 12 H -> R (IN REF. 1). SQ SEQUENCE 784 AA; 84871 MW; BEA3BF3FF25DC9AC CRC64; MEPSYDHEHP HHLLTNYNSK KYPHVSRTPE YSHSTGSDYP EHGGYLTDGR LMHESNSDAG IYHVRQGSEH SSPSLHSPAI QSSGYENEHL NEAVLAAHSH SHSPMPMVSS AYVGGGTASG SLINSNIPLL GGGGNSVLNK FLSHPHAGMV GGGTGQMEDC TSHSPIEAAS MWSYDYKGDL CAPNCGYLER HKPLPADLKY RPGGTQSKSA KESRIRRPMN AFMVWAKIER KKLADENPDL HNADLSKMLG KKWRSLTPQD RRPYVEEAER LRVIHMTEHP NYKYRPRRRK QSKLRAMQPG GKEQSESSPN PGTGGSKSNP KLATPPLATA SSSYTTPTDE STCNSTNQNH GQSTPGGLYE QPLKPTYSPS SVDCYSNADS TEQIESLAAN CPPALLNESS PTGGGYDNSL LLKKLTKPSP SRAAKSRQEK LAKSEEKNKG SQSQGQSQQG IYAATYPLAP TSVAVVAARG MYVTCNNRGL LDHGHSVKGT FYPPVSVSED DNSTSMRNSI SALQQHCNVV TSTPSSSGGT MPTSEMSSYT VSMADNCGNL RLSMNELSGN EYLPSANAYG MQYEDFLRYQ SNDMDYSTSA VEHKETTSDS ASGQKCLKYP DTNQNYDDYE AEAYSNAMLP ATAASYYTQL PYPPTSLAAF PLQLAVPFQQ TTSGAYGAQP IQSGYLHYGN YGGYEGMAQS QPQNQAPVHH QQASHSAPPS LSVPPNQTVT SNSAAISMQQ HHHHHFGPAP GMVGVGVGVG VGVGVGEMLF EQQQRKDDEI SNILAGVRKT CYSN // ID SXL_DROME STANDARD; PRT; 354 AA. AC P19339; P19340; Q26466; Q99141; Q9TYF5; Q9W3S6; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Sex-lethal protein. GN SXL OR SX1 OR CG33070/CG18350. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS MS3 AND CM1), FUNCTION, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Oregon-R; RX MEDLINE=89077532; PubMed=3144435; RA Bell L.R., Maine E.M., Schedl P., Cline T.W.; RT "Sex-lethal, a Drosophila sex determination switch gene, exhibits sex- RT specific RNA splicing and sequence similarity to RNA binding RT proteins."; RL Cell 55:1037-1046(1988). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS MS3; MS11 AND MS16), FUNCTION, AND RP DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=91260708; PubMed=1710769; RA Samuels M.E., Schedl P., Cline T.W.; RT "The complex set of late transcripts from the Drosophila sex RT determination gene sex-lethal encodes multiple related RT polypeptides."; RL Mol. Cell. Biol. 11:3584-3602(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM MS16). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE OF 1-26 FROM N.A. (ISOFORM 1), AND FUNCTION. RC TISSUE=Embryo; RX MEDLINE=92191272; PubMed=1547493; RA Keyes L.N., Cline T.W., Schedl P.; RT "The primary sex determination signal of Drosophila acts at the level RT of transcription."; RL Cell 68:933-943(1992). RN [7] RP SEQUENCE OF 1-41 FROM N.A. (ISOFORM FEMALE-SPECIFIC). RX MEDLINE=97132600; PubMed=8978052; RA Penalva L.O.F., Sakamoto H., Navarro-Sabate A., Sakashita E., RA Granadino B., Segarra C., Sanchez L.; RT "Regulation of the gene Sex-lethal: a comparative analysis of RT Drosophila melanogaster and Drosophila subobscura."; RL Genetics 144:1653-1664(1996). RN [8] RP CHARACTERIZATION. RX MEDLINE=93087158; PubMed=1454517; RA Sakamoto H., Inoue K., Higuchi I., Ono Y., Shimura Y.; RT "Control of Drosophila Sex-lethal pre-mRNA splicing by its own female- RT specific product."; RL Nucleic Acids Res. 20:5533-5540(1992). RN [9] RP STRUCTURE BY NMR OF 199-294. RX MEDLINE=95034815; PubMed=7524663; RA Lee A.L., Kanaar R., Rio D.C., Wemmer D.E.; RT "Resonance assignments and solution structure of the second RT RNA-binding domain of sex-lethal determined by multidimensional RT heteronuclear magnetic resonance."; RL Biochemistry 33:13775-13786(1994). RN [10] RP STRUCTURE BY NMR OF 122-209. RX MEDLINE=97446155; PubMed=9299339; RA Inoue M., Muto Y., Sakamoto H., Kigawa T., Takio K., Shimura Y., RA Yokoyama S.; RT "A characteristic arrangement of aromatic amino acid residues in the RT solution structure of the amino-terminal RNA-binding domain of RT Drosophila sex-lethal."; RL J. Mol. Biol. 272:82-94(1997). CC -!- FUNCTION: SEX DETERMINATION SWITCH PROTEIN WHICH CONTROLS SEXUAL CC DEVELOPMENT BY SEX-SPECIFIC SPLICING. REGULATES DOSAGE CC COMPENSATION IN FEMALES BY SUPPRESSING HYPERACTIVATION OF X-LINKED CC GENES. EXPRESSION OF THE EMBRYO-SPECIFIC ISOFORM IS UNDER THE CC CONTROL OF PRIMARY SEX-DETERMINING SIGNAL, WHICH DEPENDS ON THE CC RATIO OF X CHROMOSOMES RELATIVE TO AUTOSOMES (X:A RATIO). CC EXPRESSION OCCURS IN 2X:2A CELLS, BUT NOT IN X:2A CELLS. THE X:A CC RATIO SEEMS TO BE SIGNALED BY THE RELATIVE CONCENTRATION OF THE X- CC LINKED TRANSCRIPTION FACTORS SIS-A AND SIS-B. AS A RESULT, THE CC EMBRYO-SPECIFIC PRODUCT IS EXPRESSED EARLY ONLY IN FEMALE EMBRYOS CC AND SPECIFIES FEMALE-ADULT SPECIFIC SPLICING; IN THE MALE WHERE IT CC IS NOT EXPRESSED, THE DEFAULT SPLICING GIVES RISE TO A TRUNCATED CC NONFUNCTIONAL PROTEIN. THE FEMALE-SPECIFIC ISOFORM SPECIFIES THE CC SPLICING OF ITS OWN TRANSCRIPT, THEREBY INITIATING A POSITIVE CC AUTOREGULATORY FEEDBACK LOOP LEADING TO FEMALE DEVELOPMENT CC PATHWAY. THE FEMALE-SPECIFIC ISOFORM CONTROLS THE SEX-SPECIFIC CC SPLICING OF TRANSFORMER (TRA); ACTS AS A TRANSLATIONAL REPRESSOR CC FOR MALE-SPECIFIC LETHAL-2 (MSL-2) AND PREVENTS MALE-LESS (MLE), CC MSL-1 AND MSL-3 PROTEINS FROM ASSOCIATING WITH THE FEMALE X CC CHROMOSOME. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist; CC Name=MS3; Synonyms=A, CF1; CC IsoId=P19339-1; Sequence=Displayed; CC Name=1; CC IsoId=P19339-2; Sequence=VSP_005881; CC Name=CM1; CC IsoId=P19339-3; Sequence=VSP_005882, VSP_005884; CC Name=MS11; CC IsoId=P19339-4; Sequence=VSP_005883, VSP_005885; CC Name=MS16; CC IsoId=P19339-5; Sequence=VSP_005886; CC -!- TISSUE SPECIFICITY: EXPRESSED IN SOMATIC TISSUES, BUT NOT IN THE CC POLE CELLS, WHICH ARE THE PRECURSORS OF THE GERMLINE. CC -!- DEVELOPMENTAL STAGE: ISOFORM 1 IS EMBRYO-SPECIFIC. ISOFORM CM1 IS CC MALE-SPECIFIC. ISOFORMS MS3, MS11 AND MS16 ARE FEMALE SPECIFIC. CC ISOFORM 1 IS EXPRESSED FOR A BRIEF PERIOD DURING THE SYNCITIAL CC BLASTODERM STAGE. ISOFORM MS11 IS EXPRESSED IN 4-7 HOURS EMBRYO. CC -!- DOMAIN: THE GLY-ASN RICH DOMAIN IS REQUIRED FOR THE COOPERATIVE CC INTERACTION WITH RNA AND FOR REGULATING THE SPLICING ACTIVITY. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23635; AAA28885.1; -. DR EMBL; M23636; AAA28884.1; -. DR EMBL; M59447; AAA28922.1; -. DR EMBL; M59448; AAA28921.1; -. DR EMBL; AE003439; AAG22410.1; -. DR EMBL; AE003439; AAG22411.1; -. DR EMBL; BT003583; AAO39587.1; -. DR EMBL; S88324; AAB21845.1; -. DR EMBL; D84425; BAA20294.1; -. DR PIR; A31639; A31639. DR PIR; A39725; B31639. DR PDB; 1SXL; 30-SEP-94. DR PDB; 2SXL; 22-JUL-98. DR PDB; 1B7F; 10-APR-00. DR PDB; 3SXL; 27-APR-99. DR FlyBase; FBgn0003659; Sxl. DR GO; GO:0007549; P:dosage compensation; NAS. DR GO; GO:0030237; P:female sex determination; NAS. DR GO; GO:0046660; P:female sex differentiation; NAS. DR GO; GO:0018993; P:somatic sex determination; NAS. DR InterPro; IPR002343; Hud_Sxl_RNA. DR InterPro; IPR000504; RNA_rec_mot. DR InterPro; IPR006546; Sex_lethal_SF. DR Pfam; PF00076; rrm; 2. DR PRINTS; PR00961; HUDSXLRNA. DR SMART; SM00360; RRM; 2. DR TIGRFAMs; TIGR01659; sex-lethal; 1. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 1. KW Sexual differentiation; RNA-binding; Alternative splicing; Repeat; KW Transcription regulation; 3D-structure; Polymorphism. FT DOMAIN 125 203 RNA-BINDING (RRM) 1. FT DOMAIN 211 291 RNA-BINDING (RRM) 2. FT DOMAIN 1 32 GLY/ASN-RICH. FT DOMAIN 57 60 POLY-SER. FT DOMAIN 312 319 POLY-PRO. FT VARSPLIC 1 25 MYGNNNPGSNNNNGGYPPYGYNNKS -> MDFNFDTVTPCS FT TMCSYYNFKMA (in isoform 1). FT /FTId=VSP_005881. FT VARSPLIC 26 48 SGGRGFGMSHSLPSGMSRYAFSP -> RHIFFHSPERSSHH FT YHRKAKDTH (in isoform CM1). FT /FTId=VSP_005882. FT VARSPLIC 42 49 Missing (in isoform MS11). FT /FTId=VSP_005883. FT VARSPLIC 49 354 Missing (in isoform CM1). FT /FTId=VSP_005884. FT VARSPLIC 332 354 GRSIKSQQRFQNSHPYFDAKKFI -> DGAMEKLRSLFDAI FT CDAIFGLDSENFADLLDGLYRRKYHYPYL (in isoform FT MS11). FT /FTId=VSP_005885. FT VARSPLIC 332 354 GRSIKSQQRFQNSHPYFDAKKFI -> GENFADLLDGLYRR FT KYHYPYL (in isoform MS16). FT /FTId=VSP_005886. FT VARIANT 93 93 P -> S. FT VARIANT 96 96 S -> G. FT STRAND 127 129 FT HELIX 138 148 FT STRAND 153 156 FT STRAND 169 172 FT HELIX 178 186 FT TURN 187 188 FT STRAND 199 199 FT HELIX 203 207 FT STRAND 213 216 FT TURN 220 221 FT HELIX 224 231 FT STRAND 241 243 FT STRAND 254 257 FT HELIX 262 270 FT TURN 271 272 FT STRAND 285 285 FT STRAND 288 288 SQ SEQUENCE 354 AA; 38549 MW; 4E443D3BC88B134E CRC64; MYGNNNPGSN NNNGGYPPYG YNNKSSGGRG FGMSHSLPSG MSRYAFSPQD TEFSFPSSSS RRGYNDFPGC GGSGGNGGSA NNLGGGNMCH LPPMASNNSL NNLCGLSLGS GGSDDLMNDP RASNTNLIVN YLPQDMTDRE LYALFRAIGP INTCRIMRDY KTGYSFGYAF VDFTSEMDSQ RAIKVLNGIT VRNKRLKVSY ARPGGESIKD TNLYVTNLPR TITDDQLDTI FGKYGSIVQK NILRDKLTGR PRGVAFVRYN KREEAQEAIS ALNNVIPEGG SQPLSVRLAE EHGKAKAAHF MSQMGVVPAN VPPPPPQPPA HMAAAFNMMH RGRSIKSQQR FQNSHPYFDA KKFI // ID SY65_DROME STANDARD; PRT; 474 AA. AC P21521; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Synaptotagmin (p65). GN SYT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91093190; PubMed=1840599; RA Perin M.S., Johnston P.A., Oezcelik T., Jahn R., Francke U., RA Suedhof T.C.; RT "Structural and functional conservation of synaptotagmin (p65) in RT Drosophila and humans."; RL J. Biol. Chem. 266:615-622(1991). RN [2] RP INTERACTION WITH STNA AND STNB. RX MEDLINE=20524362; PubMed=11069931; RA Phillips A.M., Smith M., Ramaswami M., Kelly L.E.; RT "The products of the Drosophila stoned locus interact with synaptic RT vesicles via synaptotagmin."; RL J. Neurosci. 20:8254-8261(2000). RN [3] RP RNA EDITING. RX MEDLINE=22789647; PubMed=12907802; RA Hoopengardner B., Bhalla T., Staber C., Reenan R.; RT "Nervous system targets of RNA editing identified by comparative RT genomics."; RL Science 301:832-836(2003). CC -!- FUNCTION: MAY HAVE A REGULATORY ROLE IN THE MEMBRANE INTERACTIONS CC DURING TRAFFICKING OF SYNAPTIC VESICLES AT THE ACTIVE ZONE OF THE CC SYNAPSE. IT BINDS ACIDIC PHOSPHOLIPIDS WITH A SPECIFICITY THAT CC REQUIRES THE PRESENCE OF BOTH AN ACIDIC HEAD GROUP AND A DIACYL CC BACKBONE. CC -!- SUBUNIT: HOMODIMER OR HOMOTRIMER (POSSIBLE). INTERACTS WITH STNA CC AND STNB VIA ITS SECOND C2 DOMAIN. THIS INTERACTION MAY MEDIATE CC ITS RETRIEVAL FROM THE PLASMA MEMBRANE, THEREBY FACILITATING THE CC INTERNALIZATION OF MULTIPLE SYNAPTIC VESICLES FROM THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: SYNAPTIC VESICLES IN NEURONS. CC -!- SIMILARITY: CONTAINS 2 C2 DOMAINS. CC -!- SIMILARITY: BELONGS TO THE SYNAPTOTAGMIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M55048; AAA28925.1; -. DR PIR; B39052; BMFFSY. DR HSSP; P21707; 1BYN. DR FlyBase; FBgn0004242; syt. DR GO; GO:0030285; C:integral to synaptic vesicle membrane; NAS. DR GO; GO:0008345; P:larval locomotory behavior; IMP. DR GO; GO:0007269; P:neurotransmitter secretion; IMP. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localiz...; IMP. DR GO; GO:0016083; P:synaptic vesicle fusion; IMP. DR InterPro; IPR000008; C2. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR002149; LRI. DR Pfam; PF00168; C2; 2. DR SMART; SM00239; C2; 2. DR PROSITE; PS00499; C2_DOMAIN_1; 2. DR PROSITE; PS50004; C2_DOMAIN_2; 2. KW Transmembrane; Repeat; Synapse; RNA editing. FT DOMAIN 1 107 VESICULAR. FT TRANSMEM 108 134 POTENTIAL. FT DOMAIN 135 474 CYTOPLASMIC. FT DOMAIN 186 434 PHOSPHOLIPID BINDING (PROBABLE). FT DOMAIN 206 296 C2 DOMAIN 1. FT DOMAIN 339 430 C2 DOMAIN 2. FT VARIANT 367 367 I -> V (partial, due to RNA editing). FT VARIANT 379 379 K -> R (partial, due to RNA editing). FT VARIANT 383 383 V -> I (partial, due to RNA editing). FT VARIANT 405 405 M -> I (partial, due to RNA editing). SQ SEQUENCE 474 AA; 53278 MW; BF52A26EAF923F6F CRC64; MPPNAKSETD AKPEAEPAPA SEPAAELESV DQKLEETHHS KFREVDRQEQ EVLAEKAAEA ASQRIAQVES TTRSATTEAQ ESTTTAVPVI KKIEHVGEVV TEVIAERTGL PTWGVVAIII LVFLVVFGII FFCVRRFLKK RRTKDGKGKK GVDMKSVQLL GSAYKEKVQP DMEELTENAE EGDEEDKQSE QKLGRLNFKL EYDFNSNSLA VTVIQAEELP ALDMGGTSDP YVKVYLLPDK KKKFETKVHR KTLSPVFNET FTFKSLPYAD AMNKTLVFAI FDFDRFSKHD QIGEVKVPLC TIDLAQTIEE WRDLVSVEGE GGQEKLGDIC FSLRYVPTAG KLTVVILEAK NLKKMDVGGL SDPYVKIAIM QNGKRLKKKK TSVKKCTLNP YYNESFSFEV PFEQMQKICL VVTVVDYDRI GTSEPIGRCI LGCMGTGTEL RHWSDMLASP RRPIAQWHTL KDPEETDEIL KNMK // ID SYB_DROME STANDARD; PRT; 152 AA. AC P18489; DT 01-NOV-1990 (Rel. 16, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Synaptobrevin. GN SYB. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94010306; PubMed=8406010; RA Chin A.C., Burgess R.W., Wong B.R., Schwarz T.L., Scheller R.H.; RT "Differential expression of transcripts from syb, a Drosophila RT melanogaster gene encoding VAMP (synaptobrevin) that is abundant in RT non-neuronal cells."; RL Gene 131:175-181(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90180466; PubMed=2560644; RA Suedhof T.C., Baumert M., Perin M.S., Jahn R.; RT "A synaptic vesicle membrane protein is conserved from mammals to RT Drosophila."; RL Neuron 2:1475-1481(1989). CC -!- FUNCTION: UNKNOWN, BUT SYNAPTOBREVINS ARE PRESUMED TO BE INVOLVED CC IN TARGETING AND FUSION OF SYNAPTIC VESICLES WITH THE PRESYNAPTIC CC MEMBRANE AS WELL AS IN NEUROTRANSMITTER RELEASE. CC -!- SUBCELLULAR LOCATION: TYPE IV MEMBRANE PROTEIN. NEURONAL SYNAPTIC CC VESICLES. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=The ratio of isoform Syb-A to isoform Syb-B is highly CC regulated during development; CC Name=Syb-A; CC IsoId=P18489-1; Sequence=Displayed; CC Name=Syb-B; CC IsoId=P18489-2; Sequence=VSP_006327, VSP_006328; CC -!- TISSUE SPECIFICITY: NOT NERVOUS SYSTEM SPECIFIC; ABUNDANT IN CELLS CC OF THE GUT AND MALPIGHIAN TUBULES. CC -!- SIMILARITY: BELONGS TO THE SYNAPTOBREVIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 V-SNARE COILED-COIL HOMOLOGY DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L14270; AAA28924.1; -. DR EMBL; L14270; AAA28923.1; -. DR EMBL; X76200; -; NOT_ANNOTATED_CDS. DR PIR; JC1521; JC1521. DR PIR; JC1522; JC1522. DR FlyBase; FBgn0003660; Syb. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0008021; C:synaptic vesicle; NAS. DR GO; GO:0005485; F:v-SNARE activity; NAS. DR GO; GO:0007269; P:neurotransmitter secretion; NAS. DR GO; GO:0016083; P:synaptic vesicle fusion; NAS. DR InterPro; IPR001388; Synaptobrevin. DR Pfam; PF00957; synaptobrevin; 1. DR PRINTS; PR00219; SYNAPTOBREVN. DR ProDom; PD001229; Synaptobrevin; 1. DR PROSITE; PS00417; SYNAPTOBREVIN; 1. DR PROSITE; PS50892; V_SNARE; 1. KW Synapse; Synaptosome; Transmembrane; Coiled coil; KW Alternative splicing. FT DOMAIN 1 110 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 111 130 ANCHOR FOR TYPE IV MEMBRANE PROTEIN FT (POTENTIAL). FT DOMAIN 131 152 VESICULAR (POTENTIAL). FT DOMAIN 47 107 V-SNARE COILED-COIL HOMOLOGY. FT DOMAIN 1 31 ASN-RICH. FT VARSPLIC 130 132 VWP -> LFN (in isoform Syb-B). FT /FTId=VSP_006327. FT VARSPLIC 133 152 Missing (in isoform Syb-B). FT /FTId=VSP_006328. FT CONFLICT 93 93 S -> F (IN REF. 1). SQ SEQUENCE 152 AA; 16652 MW; FB5E7DF06D9DBF1C CRC64; MENNEAPSPS GSNNNDFPIL PPPPNANDNY NQFGDHQIRN NNAAQKKLQQ TQAKVDEVVG IMRVNVEKVL ERDQKLSELG ERADQLEQGA SQSEQQAGKL KRKQWWANMK MMIILGVIAV VLLIIVLVSV WPSSSDSGSG GGNKAITQAP PH // ID SYEP_DROME STANDARD; PRT; 1714 AA. AC P28668; Q9VCF5; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bifunctional aminoacyl-tRNA synthetase [Includes: Glutamyl-tRNA DE synthetase (EC 6.1.1.17) (Glutamate--tRNA ligase); Prolyl-tRNA DE synthetase (EC 6.1.1.15) (Proline--tRNA ligase)]. GN AATS-GLUPRO OR CG5394. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92097547; PubMed=1756734; RA Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.; RT "A component of the multisynthetase complex is a multifunctional RT aminoacyl-tRNA synthetase."; RL EMBO J. 10:4267-4277(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=97217441; PubMed=9063462; RA Cerini C., Semeriva M., Gratecos D.; RT "Evolution of the aminoacyl-tRNA synthetase family and the RT organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. RT Intron/exon structure of the gene, control of expression of the two RT mRNAs, selective advantage of the multienzyme complex."; RL Eur. J. Biochem. 244:176-185(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC DIPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- CATALYTIC ACTIVITY: ATP + L-PROLINE + TRNA(PRO) = AMP + CC DIPHOSPHATE + L-PROLYL-TRNA(PRO). CC -!- SUBUNIT: COMPONENT OF THE MULTISYNTHETASE COMPLEX WHICH IS CC COMPRISED OF A BIFUNCTIONAL GLUTAMYL-PROLYL-TRNA SYNTHETASE, THE CC MONOSPECIFIC ISOLEUCYL, LEUCYL, GLUTAMINYL, METHIONYL, LYSYL, CC ARGINYL, AND ASPARTYL-TRNA SYNTHETASES AS WELL AS THREE AUXILIARY CC PROTEINS, P18, P48 AND P43. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO CLASS-I CC AMINOACYL-TRNA SYNTHETASE FAMILY. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO CLASS-II CC AMINOACYL-TRNA SYNTHETASE FAMILY. CC -!- SIMILARITY: CONTAINS 6 WHEP-TRS DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74104; AAA28594.1; -. DR EMBL; U59923; AAC47469.1; -. DR EMBL; AE003745; AAF56211.1; -. DR PIR; S18644; S18644. DR HSSP; P00962; 1GTR. DR FlyBase; FBgn0005674; Aats-glupro. DR InterPro; IPR004526; GltX_arch. DR InterPro; IPR000924; Glu_tRNA-synt_1c. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004154; HGTP_anticodon. DR InterPro; IPR004499; ProS_fam_I. DR InterPro; IPR002314; tRNA-synt_2b. DR InterPro; IPR001412; tRNA-synt_I. DR InterPro; IPR002316; tRNA-synt_pro. DR InterPro; IPR006195; tRNA_ligase_II. DR InterPro; IPR000738; WHEP-TRS. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF00458; WHEP-TRS; 6. DR PRINTS; PR00987; TRNASYNTHGLU. DR PRINTS; PR01046; TRNASYNTHPRO. DR TIGRFAMs; TIGR00463; gltX_arch; 1. DR TIGRFAMs; TIGR00408; proS_fam_I; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR PROSITE; PS00762; WHEP_TRS; 6. KW Aminoacyl-tRNA synthetase; Protein biosynthesis; Ligase; ATP-binding; KW Multifunctional enzyme; Repeat. FT DOMAIN 170 754 GLUTAMYL-TRNA SYNTHETASE. FT DOMAIN 755 800 WHEP-TRS 1. FT DOMAIN 827 872 WHEP-TRS 2. FT DOMAIN 901 946 WHEP-TRS 3. FT DOMAIN 980 1025 WHEP-TRS 4. FT DOMAIN 1055 1100 WHEP-TRS 5. FT DOMAIN 1129 1173 WHEP-TRS 6. FT DOMAIN 1174 1180 POLY-GLY. FT DOMAIN 1207 1714 PROLYL-TRNA SYNTHETASE. FT SITE 209 220 "HIGH" REGION. FT SITE 438 442 "KMSKS" REGION. FT BINDING 441 441 ATP (BY SIMILARITY). FT CONFLICT 102 106 TSPLP -> DKSIA (IN REF. 3). FT CONFLICT 233 234 VC -> AF (IN REF. 3). FT CONFLICT 341 345 NTACA -> KYCVR (IN REF. 3). FT CONFLICT 583 583 K -> R (IN REF. 3). FT CONFLICT 692 692 L -> A (IN REF. 3). FT CONFLICT 753 753 T -> S (IN REF. 3). FT CONFLICT 802 802 T -> S (IN REF. 3). FT CONFLICT 873 873 P -> T (IN REF. 3). FT CONFLICT 887 887 G -> V (IN REF. 3). FT CONFLICT 1201 1201 P -> PA (IN REF. 3). FT CONFLICT 1461 1461 MISSING (IN REF. 3). FT CONFLICT 1587 1587 G -> V (IN REF. 3). SQ SEQUENCE 1714 AA; 189197 MW; 6FE8C58045E48A8C CRC64; MSIKLKANLN NPPISGLATA HLINGTVPVE IVWSKEETSL QFPDNRLLVC HSNNDVLRAL ARAAPDYKLY GETAIERTQI DHWLSFSLTC EDDISWALSF LTSPLPPVTY LVANKLTIAD FALFNEMHSR YEFLAAKGIP QHVQRWYDLI TAQPLIQKVL QSLPEDAKVK RSPQSSKEQT PAKTGERKQE GKFVDLPGAE MGKVVVRFPP EASGYLHIGH AKAALLNQYY ALVCQGTLIM RFDDTNPAKE TVEFENVILG DLEQLQIKPD VFTHTSNYFD LMLDYCVRLI KESKAYVDDT PPEQMKLERE QRVESANRSN SVEKNLSLWE EMVKGSEKGQ NTACAAKIDM SSPNGCMRDP TIYRCKNEPH PRTGTKYKVY PTYDFACPIV DAIENVTHTL RTTEYHDRDD QFYWFIDALK LRKPYIWSYS RLNMTNTVLS KRKLTWFVDS GLVDGWDDPR FPTVRGIIRR GMTVEGLKEF IIAQGSSKSV VFMNWDKIWA FNKKVIDPIA PRYTALEKEK RVIVNVAGAK VERIQVSVHP KDESLGKKTV LLGPRIYIDY VDAEALKEGE NATFINWGNI LIKKVNKDAS GNITSVDAAL NLENKDFKKT LKLTWLAVED DPSAYPPTFC VYFDNIISKA VLGKDEDFKQ FIGHKTRDEV PMLGDPELKK CKKGDIIQLQ RRGFFKVDVA YLPPSGYTNV PSPIVLFSIP DGHTKDVPTS GLKVNAPDAK ATKKASSPVS SSGQASELDS QITQQGDLVR DLKSKKAAKD QIDVAVKKLL ALKADYKSAT GKDWKPGQTS ATSAPVPAAS SSSANDAVSV NASIVKQGDL VRDLKGKKAS KPEIDAAVKT LLELKAQYKT LTGQDWKPGT VPPTAAPSAS AAPSVGGNDS VAQILSQITA QGDKVRELKS AKADKATVDA AVKTLLSLKA DYKAATGSDW KPGTTAPAPA AAPVKVKQEK NPDPASVLTV NTLLNKIAQQ GDKIRQLKSA KSEKSLVEAE VKLLLALKTD YKSLTGQEWK PGTVAPAPTT VNVIDLTGGD SGSDVGSVLS KIQAQGDKIR KLKSEKAAKN VIDPEVKTLL ALKGEYKTLS GKDWTPDAKS EPAVVKKEAS PVSMASPAKD ELTQEINAQG EKVRAAKGNK AAKEVIDAEV AKLLALKAKY KEVTGTDFPV AGRGGGGGGG SAKKAPKEAQ PKPAKPVKKE PADASGAVKK QTRLGLEATK EDNLPDWYSQ VITKGEMIEY YDVSGCYILR QWSFAIWKAI KTWFDAEITR MGVKECYFPI FVSKAVLEKE KTHIADFAPE VAWVTKSGDS DLAEPIAVRP TSETVMYPAY AKWVQSYRDL PIRLNQWNNV VRWEFKQPTP FLRTREFLWQ EGHTAFADKE EAAKEVLDIL DLYALVYTHL LAIPVVKGRK TEKEKFAGGD YTTTVEAFIS ASGRAIQGAT SHHLGQNFSK MFEIVYEDPE KTQQKKYVYQ NSWGITTRTI GVMIMVHADN QGLVLPPHVA CIQAIVVPCG ITVNTKDDER AQLLDACKAL EKRLVGGGVR CEGDYRDNYS PGWKFNHWEL KGVPLRLEVG PKDLKAQQLV AVRRDTGEKI TIPLADVEKK IPALLETIHE SMLNKAQEDM TSHTKKVTNW TDFCGFLEQK NILLAPFCGE ISCEDKIKAD SARGEEAEPG APAMGAKSLC IPFDQPAPIA ASDKCINPSC TNKPKFYTLF GRSY // ID SYN_DROME STANDARD; PRT; 980 AA. AC Q24546; Q24545; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Synapsin. GN SYN OR SYN1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS SYN-S AND SYN1-RT). RC STRAIN=Berlin; TISSUE=Head; RX MEDLINE=96209149; PubMed=8627354; RA Klagges B.R.E., Heimbeck G., Godenschwege T.A., Hofbauer A., RA Pflugfelder G.O., Reifegerste R., Reisch D., Schaupp M., Buchner S., RA Buchner E.; RT "Invertebrate synapsins: a single gene codes for several isoforms in RT Drosophila."; RL J. Neurosci. 16:3154-3165(1996). CC -!- SUBCELLULAR LOCATION: SYNAPSE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Syn1-RT; CC IsoId=Q24546-1; Sequence=Displayed; CC Name=Syn-S; CC IsoId=Q24546-2; Sequence=VSP_006324; CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED IN THE NERVOUS SYSTEM. CC -!- SIMILARITY: BELONGS TO THE SYNAPSIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95453; CAA64723.1; -. DR EMBL; X95453; CAA64722.1; -. DR HSSP; P17599; 1AUX. DR FlyBase; FBgn0004575; Syn. DR InterPro; IPR001359; Synapsin. DR Pfam; PF02078; Synapsin; 1. DR Pfam; PF02750; Synapsin_C; 1. DR PRINTS; PR01368; SYNAPSIN. DR PROSITE; PS00415; SYNAPSIN_1; FALSE_NEG. DR PROSITE; PS00416; SYNAPSIN_2; FALSE_NEG. KW Synapse; Neurone; Alternative splicing. FT DOMAIN 2 7 POLY-PRO. FT DOMAIN 668 680 POLY-SER. FT DOMAIN 692 695 POLY-PRO. FT DOMAIN 698 703 POLY-PRO. FT VARSPLIC 539 980 Missing (in isoform Syn-S). FT /FTId=VSP_006324. SQ SEQUENCE 980 AA; 102799 MW; E6037A2A4804F944 CRC64; MPPPPAPGQP AGAAPELSLS FGAGKTPATA APAPPRGVSA PTSPAKSREG LLQRVQSLTG AARDQGASIL GAAVQSATQR APAFSKDKYF TLLVLDDQNT DWSKYFRGRR LHGDFDIRGE QAEFRDITVV SSADTGPVVT MAAYRSGTRV ARSFRPDFVL IRQPPRDGSS DYRSTILGLK YGGVPSINSL HSIYQFQDKP WVFSHLLQLQ RRLGRDGFPL IEQTFFPNPR DLFQFTKFPS VLKAGHCHGG VATARLENQS ALQDAAGLVS GAGNDSHCYC TIEPYIDAKF SVHIQKIGNN YKAFMRKSIT GNWKTNQGSA MLEQITLTEK YKSWVDEISE LFGGMEVCGL SVVVAKDGRE YIISACNSTF ALIGDTQEED RRQIADLVSG RMQNVCRPSM AQTGPGKLPS RSSVSSRAES PTDEGVAPTP PLPAGPRPAP MGGPPPIPER TSPAVGSIGR LSSRSSISEV PEEPSSSGPS TVGGVRRDSQ TSQSSTISSS VSRAGQRPPQ TQNSVVEDAE DTMKNLRKTF AGIFGDMEIA NKKRGRTASE TSSGSGPGSV PSSAGPGSGF SSSFLGKQFS FAGKGEGVIS TQPTQRPSEE PPAIPTTASS AVRPESSVSV SDSRNTDTLT ERAGAGYQPV TNYEQQERVN PFDKEPSKSG SAASIHTSSS SSISSSSISS RINRNGNAIK SPPPPAGPPP PPPTNVTAVG SNANSSSGYR NSFSSSLSKD KTSYGNYGST TSVETITRMD TNTTNIGATA TEAGEASGVT AITNISNSDG IVAPTTGTIT TSVTTNDWRS AIGMRSASVY SAPAAVTTVL PGDTSGYDSN SIASQGEGLN NPSDLPSYTR PSYSRSESNA SKHSDLDVIF GDSKTTPASY GNGKYTRAAG SISDADMIFG GPPSNYKTDR FGASKSMSMT SGGVGSGNGS GSGLGGYKIY DGIQNAAFSD FSDSGSMSSI GSHTKRWSAS KEEDDELDLK // ID SYQ_DROME STANDARD; PRT; 778 AA. AC Q9Y105; Q9VBU3; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable glutaminyl-tRNA synthetase (EC 6.1.1.18) (Glutamine--tRNA DE ligase) (GlnRS). GN AATS-GLN OR BCDNA.GH11673 OR CG10506. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMINE + TRNA(GLN) = AMP + CC DIPHOSPHATE + L-GLUTAMINYL-TRNA(GLN). CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF145668; AAD38643.1; -. DR EMBL; AE003751; AAF56434.2; -. DR HSSP; P00962; 1GTR. DR FlyBase; FBgn0027090; Aats-gln. DR InterPro; IPR004514; GlnS. DR InterPro; IPR000924; Glu_tRNA-synt_1c. DR InterPro; IPR001412; tRNA-synt_I. DR InterPro; IPR007639; tRNA_synt_1c_R1. DR InterPro; IPR007638; tRNA_synt_1c_R2. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR Pfam; PF04558; tRNA_synt_1c_R1; 1. DR Pfam; PF04557; tRNA_synt_1c_R2; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR TIGRFAMs; TIGR00440; glnS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. KW Aminoacyl-tRNA synthetase; Protein biosynthesis; Ligase; ATP-binding. FT SITE 273 283 "HIGH" REGION. FT SITE 496 500 "KMSKS" REGION. FT BINDING 499 499 ATP (BY SIMILARITY). SQ SEQUENCE 778 AA; 87508 MW; 748509EC93E5E43A CRC64; MAGDDLIAKF QALGMSEQKA KETLKNANVT KNLQLSLAAA GSATLSDGTG MLIYHMATKL KPQTADHLPL LVRYIVEHKL DNTQRVDAAL EYLLKCGQSL NANIDLQALE KECGVGVVVT PEQIERTVQA KIKASYKEAL LEQRYHFNSF KILQDVRGEL KWADAKSVKA AIDVEIFDLL GPKTEADLKP QTKANDKPKA AKPKAEVTPA AQTAEAASDG ATTISELMKT KVHFHAPGEN FKADGYVVTE HTERLLKEHL ARTGGKVHTR FPPEPNGILH IGHAKAININ FGYAAAHDGV CYLRYDDTNP EKEEEKFFLA IKEMVEWLGY KPFKITYSSD NFQQLYEWAV VLINKGLAYV CHQKAEELKG FNPKPSPWRE RPIEESLRLF EDMKRGKIDE GAATLRMKVT LEEGKMDPVA YRIKFISHHR TGSDWCIYPT YDYTHCLCDS LEDITHSLCT KEFQSRRSSY YWLCNALGIY CPVQWEYGRL NMNYALVSKR KIAKLITEQI VHDWDDPRLF TLTALRRRGF PAEAINNFCA QMGVTGAQIA VDPAMLEAAV RDVLNVTAPR RLVVLEPLKV TIKNFPHAAP VQLEVPDFPQ NPQQGTHKIT LDKVIYIEQG DFKLEPEKGY RRLAPKQSVG LRHAGLVISV DEIVKDPATG QVVELICTSQ PAEQAEKPKA FVQWVSQPIQ LEVRLYEQLF KHKNPEDPNE VPGGFLSDIS EQSMSVVVAF ADRALNQAKV YDKFQFERIG FFSVDPDTSA NHLVFNRTVG LKEDAGKK // ID SYR_DROME STANDARD; PRT; 665 AA. AC Q9VXN4; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable arginyl-tRNA synthetase (EC 6.1.1.19) (Arginine--tRNA ligase) DE (ArgRS). GN AATS-ARG OR CG9020. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: ATP + L-ARGININE + TRNA(ARG) = AMP + CC DIPHOSPHATE + L-ARGINYL-TRNA(ARG). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003500; AAF48524.1; -. DR EMBL; AY070924; AAL48546.1; -. DR FlyBase; FBgn0027093; Aats-arg. DR InterPro; IPR001278; Arg_tRNA-synt_1c. DR InterPro; IPR005148; N. DR InterPro; IPR008909; tRNA-synt_1d_C. DR InterPro; IPR001412; tRNA-synt_I. DR Pfam; PF03485; N-Arg; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR Pfam; PF05746; tRNA-synt_1d_C; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR TIGRFAMs; TIGR00456; argS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. KW Aminoacyl-tRNA synthetase; Protein biosynthesis; Ligase; ATP-binding. FT SITE 205 216 "HIGH" REGION. SQ SEQUENCE 665 AA; 75576 MW; CCC31E337EBBDA54 CRC64; MSELNMELKK LRELELKTQG LAARIQTAKS GEQLDVDLVQ LQIENKKLKN RLFILKKSIA EESTAAGGDV SKPKESSSIT EHLESVFRQA IASAFPEFRD TPVIIAPVNS TSAKFGDYQC NNAMGLSKKL KEKGINKAPR DIATELKGHC PASPIIEKLE IAGAGFVNVF LSKDYASLAL SNLLRNGVKP PEVIKKRVLV DFSSPNIAKQ MHVGHLRSTI IGESLCRLLE FLQHDVIRIN HLGDWGTQFG MLIAHLEDRF PNYLNESPPI SDLQLFYKES KKRFDEDEEF KKRAYSRVVS LQKGVPNSIK AWELICNVSR KEFQTIYERL DISVKERGES FYQSRMLSVV EYLRGKGLLE VDEGREIMWP DDTKTGIPLT IVKSDGGFTY DTSDMAAIRH RLEEELCDWI IYVVDSGQST HFNTIFKAAE RSAILNPLSH RVDHVQFGVV LGEDGKKFKT RSGDTVKLSD LLDEGMKRSL QQLESRGRDK VLTPQELKDA QESLAYGCIK YSDLCHNRIS DYIFSFDKML EDRGNTAVYL LYTYTRICSI ARNSGEDFTN LPEILKKTNI VLDHEKEWKL AKTLLKLHDI LIKCSKELFL HFLCEFCFEV CTVFTEFYDS CYCIEKNKQG DIIGVNHSRI LLCEATAAVL RQCFYILGLK PVSKM // ID T2AA_DROME STANDARD; PRT; 366 AA. AC P52654; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Transcription initiation factor IIA alpha and beta chains (TFIIA DE p30 and p20 subunits) (dTFIIA-L). GN TFIIA-L. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Embryo; RX MEDLINE=94040743; PubMed=8224849; RA Yokomori K., Admon A., Goodrich J.A., Chen J.-L., Tjian R.; RT "Drosophila TFIIA-L is processed into two subunits that are RT associated with the TBP/TAF complex."; RL Genes Dev. 7:2235-2245(1993). CC -!- FUNCTION: TFIIA IS A COMPONENT OF THE TRANSCRIPTION MACHINERY OF CC RNA POLYMERASE II AND PLAYS AN IMPORTANT ROLE IN TRANSCRIPTIONAL CC ACTIVATION. INTERACTS WITH TBP (THE TATA-BINDING PROTEIN). CC -!- SUBUNIT: HETEROTRIMER OF AN ALPHA (P30), A BETA (P20) AND A GAMMA CC SUBUNIT (P14). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: THE ALPHA AND BETA SUBUNITS ARE POSTRANSLATIONALLY PRODUCED CC FROM THE PRECURSOR FORM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S66759; AAB28821.1; -. DR PIR; A49076; A49076. DR HSSP; P32773; 1YTF. DR TRANSFAC; T02225; -. DR FlyBase; FBgn0011289; TfIIA-L. DR InterPro; IPR004855; TFIIA. DR Pfam; PF03153; TFIIA; 1. KW Transcription regulation; Nuclear protein. SQ SEQUENCE 366 AA; 39240 MW; F000B1BEC90A08FD CRC64; MALCQTSVLK VYHAVIEDVI TNVRDGFLDE GVDEQVLQEM KQVWRNKLLA SKAVELSPDS GDGSHPPPIV ANNPKSHKAA NAKAKKAAAA TAVTSHQHIG GNSSMSSLVG LKSSAGMAAG SGIRNGLVPI KQEVNSQNPP PLHPTSGASM MQKQQQAASS GQGSIPIVAT LDPNRIMPVN ITLPSPAGSA SSESRVLTIQ VPASALQENQ LTQILTAHLI SSIMSLPTTL ASSVLQQHVN AALSSANHQK TLAAAKQLDG ALDSSDEDES EESDDNIDND DDDDLDKDDD EDAEHEDAAE EEPLNSEDDV TDEDSAEMFD TDNVIVCQYD KITRSRNKWK FYLKDGIMNM RGKDYVFQKS NGDAEW // ID T2AG_DROME STANDARD; PRT; 106 AA. AC P52656; Q9VCG7; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor IIA gamma chain (TFIIA P14 subunit) DE (TFIIA-14) (dTFIIA-S) (TFIIA-gamma). GN TFIIA-S OR CG5163. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 42-59. RC STRAIN=Oregon-R; RX MEDLINE=95047375; PubMed=7958898; RA Yokomori K., Zeidler M.P., Chen J.-L., Verrijzer C.P., Mlodzik M., RA Tjian R.; RT "Drosophila TFIIA directs cooperative DNA binding with TBP and RT mediates transcriptional activation."; RL Genes Dev. 8:2313-2323(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TFIIA IS A COMPONENT OF THE TRANSCRIPTION MACHINERY OF CC RNA POLYMERASE II AND PLAYS AN IMPORTANT ROLE IN TRANSCRIPTIONAL CC ACTIVATION. INTERACTS WITH TBP (THE TATA-BINDING PROTEIN). CC -!- SUBUNIT: HETEROTRIMER OF AN ALPHA (P30), A BETA (P20) AND A GAMMA CC SUBUNIT (P14). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: UBIQUITOUS. CC -!- SIMILARITY: BELONGS TO THE TFIIA-GAMMA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X83271; CAA58244.1; -. DR EMBL; AE003745; AAF56199.1; -. DR PIR; A54883; A55121. DR HSSP; P32774; 1YTF. DR TRANSFAC; T02226; -. DR FlyBase; FBgn0013347; TfIIA-S. DR InterPro; IPR003194; TFIIA_gamma. DR Pfam; PF02268; TFIIA_gamma; 1. DR Pfam; PF02751; TFIIA_gamma_C; 1. DR ProDom; PD009224; TFIIA_gamma; 1. KW Transcription regulation; Nuclear protein. SQ SEQUENCE 106 AA; 12193 MW; 978556B6AA8B31CA CRC64; MSYQLYRNTT LGNTLQESLD ELIQYGQITP GLAFKVLLQF DKSINNALNQ RVKARVTFKA GKLNTYRFCD NVWTLMLNDV EFREVHEIVK VDKVKIVACD GKSGEF // ID T2AH_DROME STANDARD; PRT; 107 AA. AC Q9W5B9; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor IIA gamma-2 chain (TFIIA-gamma-2). GN TFIIA-S-2 OR EG:BACR7A4.7 OR CG11639. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TFIIA IS A COMPONENT OF THE TRANSCRIPTION MACHINERY OF CC RNA POLYMERASE II AND PLAYS AN IMPORTANT ROLE IN TRANSCRIPTIONAL CC ACTIVATION. INTERACTS WITH TBP (THE TATA-BINDING PROTEIN) (BY CC SIMILARITY). CC -!- SUBUNIT: HETEROTRIMER OF AN ALPHA (P30), A BETA (P20) AND A GAMMA CC SUBUNIT (P14) (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TFIIA-GAMMA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003419; AAF45575.1; -. DR HSSP; P32774; 1YTF. DR FlyBase; FBgn0040338; TfIIA-S-2. DR InterPro; IPR003194; TFIIA_gamma. DR Pfam; PF02268; TFIIA_gamma; 1. DR Pfam; PF02751; TFIIA_gamma_C; 1. DR ProDom; PD009224; TFIIA_gamma; 1. KW Transcription regulation; Nuclear protein. SQ SEQUENCE 107 AA; 12273 MW; C6545CDDF3A65E44 CRC64; MNYQHYRATT LGRTLQDTLD EMMERGDITK KIANLVLLRY DKSISTALKD HGTSNMSFTA ERLETFRCCD NVWTLILKDA EFREDQHSLK VDVVKIVACL GTDNGNE // ID T2D1_DROME STANDARD; PRT; 2065 AA. AC P51123; O97068; Q86LF7; DT 01-OCT-1996 (Rel. 34, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor TFIID 230 kDa subunit (TAFII-230) DE (TAFII250) (TBP-associated factor 230 kDa) (p230). GN TAF1 OR TAF250 OR BG:DS00004.13 OR CG17603. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 63-75 AND 540-546. RX MEDLINE=93279463; PubMed=8504928; RA Kokubo T., Gong D.-W., Yamashita S., Horikoshi M., Roeder R.G., RA Nakatani Y.; RT "Drosophila 230-kD TFIID subunit, a functional homolog of the human RT cell cycle gene product, negatively regulates DNA binding of the TATA RT box-binding subunit of TFIID."; RL Genes Dev. 7:1033-1046(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RA Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., RA Palazzolo M.J.; RT "Complete sequence of the Antennapedia complex of Drosophila."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY PLAY AN ESSENTIAL ROLE IN TFIID ASSEMBLY BY CC INTERACTING WITH BOTH TBP AND OTHER TAF, AS WELL AS SERVING TO CC LINK THE CONTROL OF TRANSCRIPTION TO THE CELL CYCLE. ESSENTIAL FOR CC PROGRESSION OF THE G1 PHASE OF THE CELL CYCLE. POSSESSES DNA- CC BINDING ACTIVITY. IS A NEGATIVE REGULATOR OF THE TATA BOX-BINDING CC ACTIVITY OF TBP. CC -!- SUBUNIT: TF2D IS COMPOSED OF TBP AND A VARIETY OF TBP-ASSOCIATED CC FACTORS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 2 BROMODOMAINS. CC -!- SIMILARITY: CONTAINS 1 HMG BOX DOMAIN. CC -!- SIMILARITY: TO HUMAN TAFII-250 (CCG1). SOME TO S.POMBE TAFII-111 CC AND TO S.CEREVISIAE TAF145. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S61883; AAB26991.2; -. DR EMBL; AE001572; AAD19815.1; -. DR EMBL; AE003674; AAF54102.3; -. DR EMBL; BT004888; AAO47866.1; -. DR PDB; 1TBA; 16-AUG-99. DR TRANSFAC; T02119; -. DR FlyBase; FBgn0010355; Taf1. DR InterPro; IPR001487; Bromodomain. DR Pfam; PF00439; bromodomain; 2. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 2. DR PROSITE; PS50014; BROMODOMAIN_2; 2. KW Bromodomain; Nuclear protein; DNA-binding; Cell cycle; Repeat; KW Transcription regulation; Phosphorylation; 3D-structure. FT DNA_BIND 1244 1357 HMG BOX (POTENTIAL). FT DOMAIN 1442 1448 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 1487 1557 BROMODOMAIN 1. FT DOMAIN 1609 1679 BROMODOMAIN 2. FT DOMAIN 1992 2056 GLN-RICH. FT VARIANT 572 572 P -> S. FT CONFLICT 98 98 E -> G (IN REF. 1). FT CONFLICT 113 113 E -> EERE (IN REF. 1). FT CONFLICT 169 169 E -> D (IN REF. 5). FT CONFLICT 267 268 KR -> QS (IN REF. 1). FT CONFLICT 361 361 M -> I (IN REF. 1). FT CONFLICT 386 386 P -> Q (IN REF. 1). FT CONFLICT 656 657 KL -> NV (IN REF. 1). FT CONFLICT 762 762 F -> Y (IN REF. 1). FT CONFLICT 1088 1088 M -> I (IN REF. 5). FT CONFLICT 1462 1462 K -> E (IN REF. 5). FT CONFLICT 1680 1680 K -> E (IN REF. 5). FT CONFLICT 1870 1870 A -> AEEPIGEDDSQQVAEAMVQLSGVGGYYAQQQQ (IN FT REF. 5). SQ SEQUENCE 2065 AA; 232220 MW; 221BAAC465AB224A CRC64; MEMESDNSDD EGSIGNGLDL TGILFGNIDS EGRLLQDDDG EGRGGTGFDA ELRENIGSLS KLGLDSMLLE VIDLKEAEPP SDDEEEEDAR PSAVSASEGM SAFDALKAGV KREDGAVKAQ DDAIDYSDIT ELSEDCPRTP PEETSTYDDL EDAIPASKVE AKLTKDDKEL MPPPSAPMRS GSGGGIEEPA KSNDASSPSD DSKSTDSKDA DRKLDTPLAD ILPSKYQNVD VRELFPDFRP QKVLRFSRLF GPGKPTSLPQ IWRHVRKRRR KRNQSRDQKT TNTGGSDSPS DTEEPRKRGF SLHYAAEPTP AECMSDDEDK LLGDFNSEDV RPEGPDNGEN SDQKPKVADW RFGPAQIWYD MLEVPDSGEG FNYGFKTKAA STSSQPQLKD ERRVKSPEDD VEDPSIADDA FLMVSQLHWE DDVVWDGNDI KAKVLQKLNS KTNAAGWLPS SGSRTAGAFS QPGKPSMPVG SGSSKQGSGA SSKKAQQNAQ AKPAEAPDDT WYSLFPVENE ELIYYKWEDE VIWDAQQVSK VPKPKVLTLD PNDENIILGI PDDIDPSKIN KSTGPPPKIK IPHPHVKKSK ILLGKAGVIN VLAEDTPPPP PKSPDRDPFN ISNDTYYTPK TEPTLRLKVG GNLIQHSTPV VELRAPFVPT HMGPMKLRAF HRPPLKKYSH GPMAQSIPHP VFPLLKTIAK KAKQREVERI ASGGGDVFFM RNPEDLSGRD GDIVLAEFCE EHPPLINQVG MCSKIKNYYK RKAEKDSGPQ DFVYGEVAFA HTSPFLGILH PGQCIQAIEN NMYRAPIYPH KMAHNDFLVI RTRNNYWIRS VNSIYTVGQE CPLYEVPGPN SKRANNFTRD FLQVFIYRLF WKSRDNPRRI RMDDIKQAFP AHSESSIRKR LKQCADFKRT GMDSNWWVIK PEFRLPSEEE IRAMVSPEQC CAYFSMIAAE QRLKDAGYGE KFLFAPQEDD DEEAQLKLDD EVKVAPWNTT RAYIQAMRGK CLLQLSGPAD PTGCGEGFSY VRVPNKPTQT KEEQESQPKR SVTGTDADLR RLPLQRAKEL LRQFKVPEEE IKKLSRWEVI DVVRTLSTEK AKAGEEGMDK FSRGNRFSIA EHQERYKEEC QRIFDLQNRV LASSEVLSTD EAESSASEES DLEELGKNLE NMLSNKKTST QLSREREELE RQELLRQLDE EHGGPSGSGG AKGAKGKDDP GQQMLATNNQ GRILRITRTF RGNDGKEYTR VETVRRQPVI DAYIKIRTTK DEQFIKQFAT LDEQQKEEMK REKRRIQEQL RRIKRNQERE RLAQLAQNQK LQPGGMPTSL GDPKSSGGHS HKERDSGYKE VSPSRKKFKL KPDLKLKCGA CGQVGHMRTN KACPLYSGMQ SSLSQSNPSL ADDFDEQSEK EMTMDDDDLV NVDGTKVTLS SKILKRHGGD DGKRRSGSSS GFTLKVPRDA MGKKKRRVGG DLHCDYLQRH NKTANRRRTD PVVVLSSILE IIHNELRSMP DVSPFLFPVS AKKVPDYYRV VTKPMDLQTM REYIRQRRYT SREMFLEDLK QIVDNSLIYN GPQSAYTLAA QRMFSSCFEL LAEREDKLMR LEKAINPLLD DDDQVALSFI FDKLHSQIKQ LPESWPFLKP VNKKQVKDYY TVIKRPMDLE TIGKNIEAHR YHSRAEYLAD IELIATNCEQ YNGSDTRYTK FSKKILEYAQ TQLIEFSEHC GQLENNIAKT QERARENAPE FDEAWGNDDY NFDRGSRASS PGDDYIDVEG HGGHASSSNS IHRSMGAEAG SSHTAPAVRK PAPPGPGEVK RGRGRPRKQR DPVEEDLQCS TDDEDDDEEE DFQEVSEDEN NAASILDQGE RINAPADAMD GMFDPKNIKT EIDLEAHQMA DESMDVDPNY DPSDFLAMHK QRQSLGEPSS LQGAFTNFLS HEQDDNGPYN PAEASTSAAS GADLGMDASM AMQMAPEMPV NTMNNGMGID DDLDISESDE EDDGSRVRIK KEVFDDGDYA LQHQQMGQAA SQSQIYMVDS SNEPTTLDYQ QPPQLDFQQV QEMEQLQHQV MPPMQSEQLQ QQQTPQGDND YAWTF // ID T2D2_DROME STANDARD; PRT; 1221 AA. AC Q24325; Q8SZR7; Q9VT64; DT 01-NOV-1997 (Rel. 35, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor TFIID 150 kDa subunit (TAFII-150) DE (TAFII150). GN TAF2 OR TAF150 OR CG6711. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Embryo; RX MEDLINE=94233377; PubMed=8178153; RA Verrijzer C.P., Yokomori K., Chen J.-L., Tjian R.; RT "Drosophila TAFII150: similarity to yeast gene TSM-1 and specific RT binding to core promoter DNA."; RL Science 264:933-941(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TAFS ARE COMPONENTS OF THE TRANSCRIPTION FACTOR IID CC (TFIID) COMPLEX THAT ARE ESSENTIAL FOR MEDIATING REGULATION OF RNA CC POLYMERASE TRANSCRIPTION. TAFII-150 IS AN ESSENTIAL SUBUNIT WHICH CC INTERACTS DIRECTLY WITH TBP AND TAFII-250 AND BINDS TO CORE CC PROMOTOR DNA. CC -!- SUBUNIT: TFIID IS COMPOSED OF TATA BINDING PROTEIN (TBP) AND A CC NUMBER OF TBP-ASSOCIATED FACTORS (TAFS). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: TO YEAST TAFII-150 (TSM1). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X79243; CAA55830.1; -. DR EMBL; AE003550; AAF50190.2; -. DR EMBL; AY070564; AAL48035.1; -. DR PIR; A54063; A54063. DR MEROPS; M01.UNW; -. DR TRANSFAC; T02120; -. DR FlyBase; FBgn0011836; Taf2. DR InterPro; IPR001930; Peptidase_M1. DR Pfam; PF01433; Peptidase_M1; 1. KW Transcription regulation; Nuclear protein. FT DOMAIN 845 1213 BINDS TO TBP AND TAFII-250. FT DOMAIN 1138 1183 HIGHLY CHARGED. FT CONFLICT 53 53 R -> S (IN REF. 1). FT CONFLICT 88 88 H -> P (IN REF. 1). FT CONFLICT 1175 1221 DKDKERKDKDKRDPHISRLQARETATPDTLSSEDSSNSNSL FT PPMNLN -> ERKDKDKRDPHISRLQAARQPLRTLSARRTV FT ATAIACRP (IN REF. 1). SQ SEQUENCE 1221 AA; 139498 MW; C2DC066826B1AF6E CRC64; METQPEVPEV PLRPFKLAHQ VVSLTGISFE RRSIIGVVEL TIVPNSENLR LIRLNAKQLR IYSVVLNDVC QADFTYFDPF QNICYKEHKS RALEVYSKHH LTAAQYTDPD VNNGELLIQV PPEGYSMIQE GQGLRIRIEF SLENPKCGVH FVIPPASTDE ETQMNSSHMF TNCYENSSRL WFPCVDSFAD PCTWRLEFTV DKNMTAVSCG ELLEVIMTPD LRKKTFHYSV STPVCAPNIA LAVGQFEIYV DPHMHEVTHF CLPGLLPLLK NTVRYLHEAF EFYEETLSTR YPFSCYKQVF VDELDTDISA YATMSIASVN LLHSIAIIDQ TYISRTFMSR AVAEQFFGCF ITSHHWSDTW LAKGIAEYLC GLYSRKCFGN NEYRAWVQSE LARVVRYEEQ YGGIILDCSQ PPAPLPVSGT NQSAASSKQQ EIVHYFPIKS LHTVSPKYVE AMRRKAHFVI RMLENRIGQE LLIQVFNKQL ALASSAATTK IGAGLWSQLL ISTNIFIKAI FTVTGKDMSV FMDQWVRTGG HAKFSLTSVF NRKRNTIELE IRQDYVNQRG IRKYNGPLMV QLQELDGTFK HTLQIESTLV KSDITCHSKS RRNKKKKIPL CTGEEVDMDL SAMDDSPVLW IRLDPEMILL RDLIIEQPDF QWQYQLRHER DVTAQFQAIQ ALQKYPTNAT RLALTDTIES ERCFYQVRCE AAHSLTKVAN QMVASWSGPP AMLNIFRKFF GSFSAPHIIK LNNFSNFQLY FLQKAIPVAM AGLRTSHGIC PPEVMRFLFD LFKYNENSRN HYTDAYYRAA LVEALGETLT PVVSVAIHGT QITTDSLSTD AKLVLDEVTR LLNMEKHLPS YKYMVSVSCL KVIRKLQKFG HLPSLPHIYR SYAEYGIYLD LRIAAMECLV DFVKVDGRSE DLEHLITLLE TDPDPAARHA LAQLLIDNPP FTRESRSRLD KPNLVDRLWF SINRLPYDTK LRCDIVDLYY ALYGTKRPNC LQAGENQSFY KDLMKDNNSS VGSVTGSFKK TSDSKSHLPT PTNTLDNEPQ ERQKPAMVTI KRTATEAFEV GDEIIKLERS EEITVLDEPV NVQAYDSETK VNALQADEEA RDTHQAAKRL KNEMYAEDDN SSTMLDVGDS TRYESSHEEG KLKSGDGGLK KKKKKEKKKH KHKHKHRHSK DKDKDKDKER KDKDKRDPHI SRLQARETAT PDTLSSEDSS NSNSLPPMNL N // ID T2D3_DROME STANDARD; PRT; 921 AA. AC P47825; P49845; Q8T9E0; Q9VUY7; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor TFIID 110 kDa subunit (P110) DE (TAFII-110) (110 kDa TBP-associated factor). GN TAF4 OR TAF110 OR CG5444. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM LONG), AND SEQUENCE OF 519-540; 597-616 RP AND 857-874. RC TISSUE=Embryo; RX MEDLINE=93145326; PubMed=7678780; RA Hoey T., Weinzierl R.O.J., Gill G., Chen J.-L., Dynlacht B.D., RA Tjian R.; RT "Molecular cloning and functional analysis of Drosophila TAF110 RT reveal properties expected of coactivators."; RL Cell 72:247-260(1993). RN [2] RP SEQUENCE FROM N.A. (ISOFORM LONG), AND SEQUENCE OF 398-406; 520-540 RP AND 860-877. RC TISSUE=Embryo; RX MEDLINE=93317591; PubMed=8327460; RA Kokubo T., Gong D.-W., Roeder R.G., Horikoshi M., Nakatani Y.; RT "The Drosophila 110-kDa transcription factor TFIID subunit directly RT interacts with the N-terminal region of the 230-kDa subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5896-5900(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TFIID IS A MULTIMERIC PROTEIN COMPLEX THAT PLAYS A CC CENTRAL ROLE IN MEDIATING PROMOTER RESPONSES TO VARIOUS ACTIVATORS CC AND REPRESSORS. MAY FUNCTION AS A COACTIVATOR BY SERVING AS A SITE CC OF PROTEIN-PROTEIN CONTACT BETWEEN ACTIVATORS LIKE SP1 (OR BTD) CC AND TFIID COMPLEX. CC -!- SUBUNIT: TFIID IS COMPOSED OF TATA BINDING PROTEIN (TBP) AND A CC NUMBER OF TBP-ASSOCIATED FACTORS (TAFS). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P47825-1; Sequence=Displayed; CC Name=Short; CC IsoId=P47825-2; Sequence=VSP_004441; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO THE TAF2C FAMILY. CC -!- SIMILARITY: CONTAINS 1 TAFH/NHR1 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L06861; -; NOT_ANNOTATED_CDS. DR EMBL; S63550; AAB27433.1; -. DR EMBL; AE003528; AAF49536.1; -. DR EMBL; AY069807; AAL39952.1; -. DR PIR; A48184; A48184. DR TRANSFAC; T02121; -. DR FlyBase; FBgn0010280; Taf4. DR GO; GO:0005669; C:transcription factor TFIID complex; IPI. DR GO; GO:0016251; F:general RNA polymerase II transcription fac...; IPI. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IPI. DR GO; GO:0006367; P:transcription initiation from Pol II promoter; IPI. DR InterPro; IPR007900; TAF4. DR InterPro; IPR003894; TAF_hom. DR Pfam; PF05236; TAF4; 1. DR SMART; SM00549; TAFH; 1. KW Transcription regulation; Nuclear protein; Alternative splicing. FT DOMAIN 293 383 TAFH/NHR1. FT DOMAIN 66 82 POLY-GLN. FT DOMAIN 108 111 POLY-GLN. FT DOMAIN 259 265 POLY-GLN. FT VARSPLIC 138 207 Missing (in isoform Short). FT /FTId=VSP_004441. FT CONFLICT 114 114 V -> M (IN REF. 4). SQ SEQUENCE 921 AA; 99338 MW; 27E6852859872767 CRC64; MNTSQTAAGN RITFTSQPLP NGTISIAGNP GAVISTAQLP NTTTIKTIQA GIGGQHQGLQ QVHHVQQQQQ SQQQQQQQQQ TQSAGQPLLN SMLPAGVVVG MRQQAPSQQQ QKNVPTNPLS RVVINSHMAG VRPQSPSITL STLNTGQTPA LLVKTDNGFQ LLRVGTTTGP PTVTQTITNT SNNSNTTSTT NHPTTTQIRL QTVPAAASMT NTTATSNIIV NSVASSGYAN SSQPPHLTQL NAQAPQLPQI TQIQTIPAQQ SQQQQVNNVS SAGGTATAVS STTAATTTQQ GNTKEKCRKF LANLIELSTR EPKPVEKNVR TLIQELVNAN VEPEEFCDRL ERLLNASPQP CLIGFLKKSL PLLRQALYTK ELVIEGIKPP PQHVLGLAGL SQQLPKIQAQ IRPIGPSQTT TIGQTQVRMI TPNALGTPRP TIGHTTISKQ PPNIRLPTAP RLVNTGGIRT QIPSLQVPGQ ANIVQIRGPQ HAQLQRTGSV QIRATTRPPN SVPTANKLTA VKVGQTQIKA ITPSLHPPSL AAISGGPPPT PTLSVLSTLN SASTTTLPIP SLPTVHLPPE ALRAREQMQN SLNHNSNHFD AKLVEIKAPS LHPPHMERIN ASLTPIGAKT MARPPPAINK AIGKKKRDAM EMDAKLNTSS GGAASAANSF FQQSSMSSMY GDDDINDVAA MGGVNLAEES QRILGCTENI GTQIRSCKDE VFLNLPSLQA RIRAITSEAG LDEPSQDVAV LISHACQERL KNIVEKLAVI AEHRIDVIKL DPRYEPAKDV RGQIKFLEEL DKAEQKRHEE LEREMLLRAA KSRSRVEDPE QAKMKARAKE MQRAEMEELR QRDANLTALQ AIGPRKKLKL DGETVSSGAG SSGGGVLSSS GSAPTTLRPR IKRVNLRDML FYMEQEREFC RSSMLFKTYL K // ID T2D4_DROME STANDARD; PRT; 704 AA. AC P49846; Q9V5R1; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor TFIID 85 kDa subunit (P85) (TAFII-80). GN TAF5 OR TAF80 OR CG7704. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 105-120; 272-280 AND 365-374. RC TISSUE=Embryo; RX MEDLINE=94067146; PubMed=8247000; RA Kokubo T., Gong D.-W., Yamashita S., Takada R., Roeder R.G., RA Horikoshi M., Nakatani Y.; RT "Molecular cloning, expression, and characterization of the RT Drosophila 85-kilodalton TFIID subunit."; RL Mol. Cell. Biol. 13:7859-7863(1993). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Embryo; RX MEDLINE=93247643; PubMed=8483503; RA Dynlacht B.D., Weinzierl R.O.J., Admon A., Tjian R.; RT "The dTAFII80 subunit of Drosophila TFIID contains beta-transducin RT repeats."; RL Nature 363:176-179(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TFIID IS A MULTIMERIC PROTEIN COMPLEX THAT PLAYS A CC CENTRAL ROLE IN MEDIATING PROMOTER RESPONSES TO VARIOUS ACTIVATORS CC AND REPRESSORS. TAFII-80 INTERACTS DIRECTLY WIH TBP AND TAFII-110. CC MAY PLAY A ROLE IN HELPING TO ANCHOR TAFII-110 WITHIN THE TFIID CC COMPLEX. MAY BE INVOLVED IN TRANSDUCING SIGNALS FROM VARIOUS CC TRANSCRIPTIONAL REGULATORS TO THE RNA POLYMERASE II TRANSCRIPTION CC MACHINERY. CC -!- SUBUNIT: TFIID IS COMPOSED OF TATA BINDING PROTEIN (TBP) AND A CC NUMBER OF TBP-ASSOCIATED FACTORS (TAFS). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 6 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U06460; AAC46481.1; -. DR EMBL; AE003828; AAF58737.1; -. DR EMBL; AY051960; AAK93384.1; -. DR PIR; S33263; S33263. DR TRANSFAC; T02122; -. DR FlyBase; FBgn0010356; Taf5. DR InterPro; IPR007582; TFIID_WDA. DR InterPro; IPR001680; WD40. DR Pfam; PF04494; TFIID_WDA; 1. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 4. DR SMART; SM00320; WD40; 6. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. KW Transcription regulation; Nuclear protein; Repeat; WD repeat. FT REPEAT 376 405 WD 1. FT REPEAT 448 478 WD 2. FT REPEAT 490 520 WD 3. FT REPEAT 532 562 WD 4. FT REPEAT 574 604 WD 5. FT REPEAT 616 646 WD 6. FT CONFLICT 410 411 KL -> NV (IN REF. 2). SQ SEQUENCE 704 AA; 79324 MW; F4E2F12534501EF6 CRC64; MSLEVSNING GNGTQLSHDK RELLCLLKLI KKYQLKSTEE LLCQEANVSS VELSEISESD VQQVLGAVLG AGDANRERKH VQSPAQGHKQ SAVTEANAAE ELAKFIDDDS FDAQHYEQAY KELRTFVEDS LDIYKHELSM VLYPILVQIY FKILASGLRE KAKEFIEKYK CDLDGYYIEG LFNLLLLSKP EELLENDLVV AMEQDKFVIR MSRDSHSLFK RHIQDRRQEV VADIVSKYLH FDTYEGMARN KLQCVATAGS HLGEAKRQDN KMRVYYGLLK EVDFQTLTTP APAPEEEDDD PDAPDRPKKK KPKKDPLLSK KSKSDPNAPS IDRIPLPELK DSDKLLKLKA LREASKRLAL SKDQLPSAVF YTVLNSHQGV TCAEISDDST MLACGFGDSS VRIWSLTPAK LRTLKDADSL RELDKESADI NVRMLDDRSG EVTRSLMGHT GPVYRCAFAP EMNLLLSCSE DSTIRLWSLL TWSCVVTYRG HVYPVWDVRF APHGYYFVSC SYDKTARLWA TDSNQALRVF VGHLSDVDCV QFHPNSNYVA TGSSDRTVRL WDNMTGQSVR LMTGHKGSVS SLAFSACGRY LASGSVDHNI IIWDLSNGSL VTTLLRHTST VTTITFSRDG TVLAAAGLDN NLTLWDFHKV TEDYISNHIT VSHHQDENDE DVYLMRTFPS KNSPFVSLHF TRRNLLMCVG LFKS // ID T2D5_DROME STANDARD; PRT; 606 AA. AC P49847; Q961B6; Q9VW16; DT 01-OCT-1996 (Rel. 34, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor TFIID 62 kDa subunit (p62) (TAFII-60). GN TAF6 OR TAF60 OR CG32211/CG9348. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 3-606 FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=94150630; PubMed=7545910; RA Kokubo T., Gong D.-W., Wootton J.C., Horikoshi M., Roeder R.G., RA Nakatani Y.; RT "Molecular cloning of Drosophila TFIID subunits."; RL Nature 367:484-487(1994). RN [5] RP SEQUENCE OF 7-606 FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=Oregon-R; RX MEDLINE=94085406; PubMed=8262073; RA Weinzierl R.O., Ruppert S., Dynlacht B.D., Tanese N., Tjian R.; RT "Cloning and expression of Drosophila TAFII60 and human TAFII70 RT reveal conserved interactions with other subunits of TFIID."; RL EMBO J. 12:5303-5309(1993). CC -!- FUNCTION: TFIID IS A MULTIMERIC PROTEIN COMPLEX THAT PLAYS A CC CENTRAL ROLE IN MEDIATING PROMOTER RESPONSES TO VARIOUS ACTIVATORS CC AND REPRESSORS. BINDS TIGHTLY TO TAFII-250 AND ALSO DIRECTLY CC INTERACTS WITH TAFII-40. CC -!- SUBUNIT: TFIID IS COMPOSED OF TATA BINDING PROTEIN (TBP) AND A CC NUMBER OF TBP-ASSOCIATED FACTORS (TAFS). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE TAF2E FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003516; AAF49139.2; -. DR EMBL; AY051702; AAK93126.1; -. DR EMBL; U06459; AAC46480.1; ALT_INIT. DR EMBL; L25443; AAA16536.1; ALT_INIT. DR TRANSFAC; T02124; -. DR FlyBase; FBgn0010417; Taf6. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR004823; TFIID_TAF. DR Pfam; PF02969; TAF; 1. KW Transcription regulation; Nuclear protein. FT CONFLICT 3 3 G -> K (IN REF. 4). FT CONFLICT 101 101 F -> L (IN REF. 5). FT CONFLICT 582 582 D -> E (IN REF. 4 AND 5). SQ SEQUENCE 606 AA; 65654 MW; 9D93C3496A23C0A3 CRC64; MSGKPSKPSS PSSSMLYGSS ISAESMKVIA ESIGVGSLSD DAAKELAEDV SIKLKRIVQD AAKFMNHAKR QKLSVRDIDM SLKVRNVEPQ YGFVAKDFIP FRFASGGGRE LHFTEDKEID LGEITSTNSV KIPLDLTLRS HWFVVEGVQP TVPENPPPLS KDSQLLDSVN PVIKMDQGLN KDAAGKPTTG KIHKLKNVET IHVKQLATHE LSVEQQLYYK EITEACVGSD EPRRGEALQS LGSDPGLHEM LPRMCTFIAE GVKVNVVQNN LALLIYLMRM VRALLDNPSL FLEKYLHELI PSVMTCIVSK QLCMRPELDN HWALRDFASR LMAQICKNFN TLTNNLQTRV TRIFSKALQN DKTHLSSLYG SIAGLSELGG EVIKVFIIPR LKFISERIEP HLLGTSISNT DKTAAGHIRA MLQKCCPPIL RQMRSAPDTA EDYKNDFGFL GPSLCQAVVK VRNAPASSIV TLSSNTINTA PITSAAQTAT TIGRVSMPTT QRQGSPGVSS LPQIRAIQAN QPAQKFVIVT QNSPQQGQAK VVRRGSSPHS VVLSAASNAA SASNSNSSSS GSLLAAAQRS SDNVCVIAGS EAPAVDGITV QSFRAS // ID T2D6_DROME STANDARD; PRT; 479 AA. AC Q9VHY5; O76207; Q8T087; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable transcription initiation factor TFIID 55 kDa subunit (TAFII- DE 55) (TAFII55). GN TAF7 OR TAF55 OR ANON-84EC OR CG2670. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=98267192; PubMed=9601978; RA Clark D.V., Sabl J.F., Henikoff S.; RT "Repetitive arrays containing a housekeeping gene promoter have RT altered polytene chromosome morphology in Drosophila."; RL Chromosoma 107:96-104(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 23-479 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TAFS ARE COMPONENTS OF THE TRANSCRIPTION FACTOR IID CC (TFIID) COMPLEX THAT ARE ESSENTIAL FOR MEDIATING REGULATION OF RNA CC POLYMERASE TRANSCRIPTION (BY SIMILARITY). CC -!- SUBUNIT: TFIID IS COMPOSED OF TATA BINDING PROTEIN (TBP) AND A CC NUMBER OF TBP-ASSOCIATED FACTORS (TAFS). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE TAF2F FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF017096; AAC39086.1; -. DR EMBL; AE003676; AAF54162.1; -. DR EMBL; AY069482; AAL39627.1; -. DR FlyBase; FBgn0024909; Taf7. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0003700; F:transcription factor activity; NAS. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS. DR InterPro; IPR006751; TAFII55_N. DR Pfam; PF04658; TAFII55_N; 1. KW Hypothetical protein; Transcription regulation; Nuclear protein. FT DOMAIN 407 453 GLN-RICH. FT CONFLICT 269 269 V -> A (IN REF. 3). FT CONFLICT 348 348 V -> G (IN REF. 1). FT CONFLICT 475 479 NMLES -> ICWTLKIQI (IN REF. 1). SQ SEQUENCE 479 AA; 55064 MW; F6B945E4AD207441 CRC64; MPSLAVPHLT PISNEHLVSS KEVVFFWKNR IEMFEKKSDK VKQAEHKARD DGVELESQFI MRVPKELADT VHEAINAGTI KDRLTIQLDP DLRYGEVRID DQILYTKLVD LPTVVESYKT IDNKSFYKSA DICQILICKE EREDETEKES PNKNKKKDPN KVDKKYLFPH GITPPCKNVR KRRFRKTLKK KNVEAPEIEK EVKHLLRIDN EAVRVDYEII NEEDKPMDEL EQSDIKPYND ADDDLQDEST MHASEKTIME MSSQRHLQVE SDDDEASNFP SHRAPNMGVA VHDIFGEEVS STDDEDEPDR GNNTMQRRVM EESSRLSADD SRMSDFFGAS GSNTGAGVVK MEQNVFSKSM FGHEASSPKL SAAGSSSNLA APSGFYDSQM LAKREEFENM EFIDEPQPQY TQQQVQQKIN QLTRQIRELK AQQVQKSTEI ASIQNATLKQ RMQETLDNLY TQVIERELEL KDFENMLES // ID T2D7_DROME STANDARD; PRT; 278 AA. AC Q27272; Q9VX16; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor TFIID 42 kDa subunit (TAFII-42) DE (TAFII40) (p42) (Enhancer of yellow 1 protein). GN E(Y)1 OR TAF40 OR CG6474. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94150630; PubMed=7545910; RA Kokubo T., Gong D.W., Wootton J.C., Horikoshi M., Roeder R.G., RA Nakatani Y.; RT "Molecular cloning of Drosophila TFIID subunits."; RL Nature 367:484-487(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=94037099; PubMed=8221891; RA Goodrich J.A., Hoey T., Thut C.J., Admon A., Tjian R.; RT "Drosophila TAFII40 interacts with both a VP16 activation domain and RT the basal transcription factor TFIIB."; RL Cell 75:519-530(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TAFS ARE COMPONENTS OF THE TRANSCRIPTION FACTOR IID CC (TFIID) COMPLEX THAT ARE ESSENTIAL FOR MEDIATING REGULATION OF RNA CC POLYMERASE TRANSCRIPTION (BY SIMILARITY). CC -!- SUBUNIT: TFIID IS COMPOSED OF TATA BINDING PROTEIN (TBP) AND A CC NUMBER OF TBP-ASSOCIATED FACTORS (TAFS). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE TAF2G FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U06458; AAC47347.1; -. DR EMBL; L29540; AAA28488.1; -. DR EMBL; AE003506; AAF48767.1; -. DR PIR; A49067; A49067. DR TRANSFAC; T02125; -. DR FlyBase; FBgn0000617; e(y)1. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR003162; TFIID-31. DR Pfam; PF02291; TFIID-31; 1. DR ProDom; PD011023; TFIID-31; 1. KW Transcription regulation; Nuclear protein. FT DOMAIN 190 197 POLY-THR. FT DOMAIN 202 209 POLY-GLY. FT DOMAIN 250 256 POLY-GLY. FT DOMAIN 267 274 POLY-GLU (ACIDIC). SQ SEQUENCE 278 AA; 29314 MW; 0EA442C80467001F CRC64; MSAEKSDKAK ISAQIKHVPK DAQVIMSILK ELNVQEYEPR VVNQLLEFTF RYVTCILDDA KVYANHARKK TIDLDDVRLA TEVTLDKSFT GPLERHVLAK VADVRNSMPL PPIKPHCGLR LPPDRYCLTG VNYKLRATNQ PKKMTKSAVE GRPLKTVVKP VSSANGPKRP HSVVAKQQVV TIPKPVIKFT TTTTTKTVGS SGGSGGGGGQ EVKSESTGAG GDLKMEVDSD AAAVGSIAGA SGSGAGSASG GGGGGGSSGV GVAVKREREE EEFEFVTN // ID T2D9_DROME STANDARD; PRT; 196 AA. AC P49906; Q9VL90; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor TFIID 28 kDa subunit beta DE (p28-beta) (TAFII30 beta). GN TAF11 OR TAF30-BETA OR CG4079. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94102540; PubMed=8276241; RA Yokomori K., Chen J.L., Admon A., Zhou S., Tjian R.; RT "Molecular cloning and characterization of dTAFII30 alpha and RT dTAFII30 beta: two small subunits of Drosophila TFIID."; RL Genes Dev. 7:2587-2597(1993). RN [2] RP SEQUENCE FROM N.A. RA Nakatani Y.; RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TFIID IS A MULTIMERIC PROTEIN COMPLEX THAT PLAYS A CC CENTRAL ROLE IN MEDIATING PROMOTER RESPONSES TO VARIOUS ACTIVATORS CC AND REPRESSORS. CC -!- SUBUNIT: TFIID IS COMPOSED OF TATA BINDING PROTEIN (TBP) AND A CC NUMBER OF TBP-ASSOCIATED FACTORS (TAFS). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE TAF2I FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S67660; AAB29541.1; -. DR EMBL; U06457; AAB19245.1; -. DR EMBL; AE003626; AAF52806.1; -. DR PIR; B49453; B49453. DR TRANSFAC; T02131; -. DR FlyBase; FBgn0011291; Taf11. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR006809; TAFII28. DR Pfam; PF04719; TAFII28; 1. KW Transcription regulation; Nuclear protein. FT DOMAIN 80 87 POLY-GLU. SQ SEQUENCE 196 AA; 22091 MW; E852855E3F598AC9 CRC64; MDEILFPTQQ KSNSLSDGDD VDLKFFQSAS GERKDSDTSD PGNDADRDGK DADGDNDNKN TDGDGDSGEP AHKKLKTKKE LEEEERERMQ VLVSNFTEEQ LDRYEMYRRS AFPKAAVKRL MQTITGCSVS QNVVIAMSGI AKVFVGEVVE EALDVMEAQG ESGALQPKFI REAVRRLRTK DRMPIGRYQQ PYFRLN // ID T2DA_DROME STANDARD; PRT; 196 AA. AC P49905; Q26339; Q9VGK0; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor TFIID 28 kDa subunit alpha/22 kDa DE subunit (p28-alpha/p22) (TAFII30 alpha). GN TAF12 OR TAF30-ALPHA OR CG17358. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 147-173. RX MEDLINE=94150630; PubMed=7545910; RA Kokubo T., Gong D.-W., Wootton J.C., Horikoshi M., Roeder R.G., RA Nakatani Y.; RT "Molecular cloning of Drosophila TFIID subunits."; RL Nature 367:484-487(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94102540; PubMed=8276241; RA Yokomori K., Chen J.L., Admon A., Zhou S., Tjian R.; RT "Molecular cloning and characterization of dTAFII30 alpha and RT dTAFII30 beta: two small subunits of Drosophila TFIID."; RL Genes Dev. 7:2587-2597(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TFIID IS A MULTIMERIC PROTEIN COMPLEX THAT PLAYS A CC CENTRAL ROLE IN MEDIATING PROMOTER RESPONSES TO VARIOUS ACTIVATORS CC AND REPRESSORS. CC -!- SUBUNIT: TFIID IS COMPOSED OF TATA BINDING PROTEIN (TBP) AND A CC NUMBER OF TBP-ASSOCIATED FACTORS (TAFS). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; CC Comment=2 isoforms, 28 kDa (shown here) and 22 kDa, are produced CC by alternative initiation; CC -!- SIMILARITY: BELONGS TO THE TAF2J FAMILY. ALSO SIMILAR TO HISTONES CC H2B AND H3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U06456; AAB19244.1; -. DR EMBL; U06450; AAC46479.1; -. DR EMBL; S67741; AAB29540.1; -. DR EMBL; AE003692; AAF54677.1; -. DR EMBL; AY061435; AAL28983.1; -. DR PIR; A49453; A49453. DR PIR; S42222; S42222. DR TRANSFAC; T02126; -. DR FlyBase; FBgn0011290; Taf12. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR003228; TFIID_sub. DR Pfam; PF03847; TFIID_A; 1. DR ProDom; PD012998; TFIID_sub; 1. KW Transcription regulation; Nuclear protein; Alternative initiation. FT CHAIN 1 196 TRANSCRIPTION INITIATION FACTOR TFIID, FT ISOFORM 28 KDA. FT CHAIN 37 196 TRANSCRIPTION INITIATION FACTOR TFIID, FT ISOFORM 22 KDA. FT INIT_MET 37 37 FOR ISOFORM 22 KDA. FT CONFLICT 15 15 E -> R (IN REF. 2). FT CONFLICT 127 127 E -> R (IN REF. 2). SQ SEQUENCE 196 AA; 21523 MW; 9D6AE98FB9AEC1EC CRC64; MSDLFTTFDS NGVAEHHLHH NHNSTSSASG LLHDPPMASP SQHSPMTNNS NSSSQNGGPV SGLGTGTGPI SGGSKSSNHT SSAAGSENTP MLTKPRLTEL VREVDTTTQL DEDVEELLLQ IIDDFVEDTV KSTSAFAKHR KSNKIEVRDV QLHFERKYNM WIPGFGTDEL RPYKRAAVTE AHKQRLALIR KTIKKY // ID T2FA_DROME STANDARD; PRT; 577 AA. AC Q05913; Q9VI19; DT 01-FEB-1994 (Rel. 28, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) DE (Transcription factor 5, large chain) (TF5A). GN TFIIF-ALPHA OR CG10281. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93219133; PubMed=8464745; RA Gong D.-W., Horikoshi M., Nakatani Y.; RT "Analysis of cDNA encoding Drosophila transcription initiation factor RT TFIIF alpha (RAP74)."; RL Nucleic Acids Res. 21:1492-1492(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93219101; PubMed=8464716; RA Kephart D., Price M.P., Burton Z.F., Finkelstein A., RA Greenblalt J., Price D.H.; RT "Cloning of a Drosophila cDNA with sequence similarity to human RT transcription factor RAP74."; RL Nucleic Acids Res. 21:1319-1319(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION. RX MEDLINE=94230464; PubMed=8175788; RA Kephart D., Wang B.Q., Burton Z.F., Price D.H.; RT "Functional analysis of Drosophila factor 5 (TFIIF), a general RT transcription factor."; RL J. Biol. Chem. 269:13536-13543(1994). CC -!- FUNCTION: TFIIF IS A GENERAL TRANSCRIPTION INITIATION FACTOR THAT CC BINDS TO RNA POLYMERASE II AND HELPS TO RECRUIT IT TO THE CC INITIATION COMPLEX IN COLLABORATION WITH TFIIB. IT PROMOTES CC TRANSCRIPTION ELONGATION. CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: TO OTHER TRANSCRIPTION FACTOR IIF, ALPHA SUBUNIT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L10331; -; NOT_ANNOTATED_CDS. DR EMBL; X66982; CAA47391.1; -. DR EMBL; AE003675; AAF54125.1; -. DR EMBL; AY051733; AAK93157.1; -. DR PIR; S30237; S30237. DR TRANSFAC; T02173; -. DR FlyBase; FBgn0010282; TfIIF-alpha. DR InterPro; IPR008851; TFIIF-alpha. DR Pfam; PF05793; TFIIF-alpha; 1. KW Transcription regulation; DNA-binding; Nuclear protein. FT CONFLICT 20 20 A -> R (IN REF. 1). FT CONFLICT 76 76 E -> G (IN REF. 1). FT CONFLICT 528 528 P -> A (IN REF. 1). SQ SEQUENCE 577 AA; 64466 MW; 1E3DF88E3C833761 CRC64; MSSASKSTPS AASGSSTSAA AAAAASVASG SASSSANVQE FKIRVPKMPK KHHVMRFNAT LNVDFAQWRN VKLERENNMK EFRGMEEDQP KFGAGSEYNR DQREEARRKK FGIIARKYRP EAQPWILKVG GKTGKKFKGI REGGVGENAA FYVFTHAPDG AIEAYPLTEW YNFQPIQRYK SLSAEEAEQE FGRRKKVMNY FSLMLRKRLR GDEEEEQDPE EAKLIKAATK KSKELKITDM DEWIDSEDES DSEDEEDKKK KEQEDSDDGK AKGKGKKGAD KKKKKRDVDD EAFEESDDGD EEGREMDYDT SSSEDEPDPE AKVDKDMKGV AEEDALRKLL TSDEEEDDEK KSDESDKEDA DGEKKKKDKG KDEVSKDKKK KKPTKDDKKG KSNGSGDSST DFSSDSTDSE DDLSNGPPKK KVVVKDKDKE KEKEKESAAS SKVIASSSNA NKSRSATPTL STDASKRKMN SLPSDLTASD TSNSPTSTPA KRPKNEISTS LPTSFSGGKV EDYGITEEAV RRYLKRKPLT ATELLTKFKN KKTPVSSDRL VETMTKILKK INPVKHTIQG KMYLWIK // ID T2FB_DROME STANDARD; PRT; 277 AA. AC P41900; Q9VGX4; DT 01-NOV-1995 (Rel. 32, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor IIF, beta subunit (TFIIF-beta). GN TFIIF-BETA OR TFIIF30 OR CG6538. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95319928; PubMed=7596813; RA Gong D.-W., Mortin M.A., Horikoshi M., Nakatani Y.; RT "Molecular cloning of cDNA encoding the small subunit of Drosophila RT transcription initiation factor TFIIF."; RL Nucleic Acids Res. 23:1882-1886(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Frank D.J., Tyree C.M., Kadonaga J.T.; RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TFIIF IS A GENERAL TRANSCRIPTION INITIATION FACTOR THAT CC BINDS TO RNA POLYMERASE II AND HELPS TO RECRUIT IT TO THE CC INITIATION COMPLEX IN COLLABORATION WITH TFIIB. IT PROMOTES CC TRANSCRIPTION ELONGATION. THIS SUBUNIT SHOWS ATP-DEPENDENT CC DNA-HELICASE ACTIVITY (BY SIMILARITY). CC -!- SUBUNIT: HETERODIMER OF AN ALPHA AND A BETA SUBUNIT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: REGIONS OF SIMILARITIES WITH PROKARYOTIC SIGMA CC FACTORS IN THE REGION THAT BINDS RNA POLYMERASE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U25188; AAA86888.1; -. DR EMBL; U02461; AAA81888.1; -. DR EMBL; AE003688; AAF54548.1; -. DR PIR; S57336; S57336. DR HSSP; P13984; 2BBY. DR TRANSFAC; T02174; -. DR FlyBase; FBgn0010421; TfIIF-beta. DR GO; GO:0005674; C:transcription factor TFIIF complex; NAS. DR GO; GO:0016251; F:general RNA polymerase II transcription fac...; NAS. DR InterPro; IPR003196; TFIIF_beta. DR Pfam; PF02270; TFIIF_beta; 1. KW Transcription regulation; DNA-binding; Helicase; ATP-binding; KW Nuclear protein. FT NP_BIND 43 50 ATP (BY SIMILARITY). FT CONFLICT 97 117 VFSHMAPSDGKENSTTSAAQP -> YSRTWHRPMARRTRLP FT RRHS (IN REF. 2). SQ SEQUENCE 277 AA; 32107 MW; ED128DE2815D21CA CRC64; MSKEDKEKTQ IIDKDLDLSN AGRGVWLVKV PKYIAQKWEK APTNMDVGKL RINKTPGQKA QVSLSLTPAV LALDPEEKIP TEHILDVSQV TKQTLGVFSH MAPSDGKENS TTSAAQPDNE KLYMEGRIVQ KLECRPIADN CYMKLKLESI RKASEPQRRV QPIDKIVQNF KPVKDHAHNI EYRERKKAEG KKARDDKNAV MDMLFHAFEK HQYYNIKDLV KITNQPISYL KEILKDVCDY NMKNPHKNMW ELKKEYRHYK TEEKKEEEHK SGSSDSE // ID TAKT_DROME STANDARD; PRT; 249 AA. AC Q9VBV3; Q8MR66; Q9VBV2; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Takeout protein precursor. GN TO OR CG11853. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=20414702; PubMed=10958689; RA So W.V., Sarov-Blat L., Kotarski C.K., McDonald M.J., Allada R., RA Rosbash M.; RT "takeout, a novel Drosophila gene under circadian clock RT transcriptional regulation."; RL Mol. Cell. Biol. 20:6935-6944(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=Canton-S; RX MEDLINE=20348740; PubMed=10892651; RA Sarov-Blat L., So W.V., Liu L., Rosbash M.; RT "The Drosophila takeout gene is a novel molecular link between RT circadian rhythms and feeding behavior."; RL Cell 101:647-656(2000). RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=Canton-S; RX MEDLINE=22323098; PubMed=12435630; RA Dauwalder B., Tsujimoto S., Moss J., Mattox W.; RT "The Drosophila takeout gene is regulated by the somatic sex- RT determination pathway and affects male courtship behavior."; RL Genes Dev. 16:2879-2892(2002). CC -!- FUNCTION: PARTICIPATES IN A NOVEL CIRCADIAN OUTPUT PATHWAY THAT CC CONVEYS TEMPORAL AND FOOD STATUS INFORMATION TO FEEDING-RELEVANT CC METABOLISMS AND ACTIVITIES. INVOLVED IN MALE COURTSHIP BEHAVIOR. CC IN THE BRAIN-ASSOCIATED FAT BODY, TRANSCRIPTION IS ENHANCED BY THE CC DSX AND FRU MALE-SPECIFIC ISOFORMS AND REPRESSED BY THE DSX CC FEMALE-SPECIFIC ISOFORM. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: EXPRESSION IS LARGELY RESTRICTED TO HEAD, WITH CC LIMITED EXPRESSION DETECTABLE IN CARDIA AND CROP. IN ENTRAINED CC INDIVIDUALS, EXPRESSION IS OBSERVED IN THE BRAIN CORTEX (REGION CC BETWEEN OPTIC LOBE AND CENTRAL COMPLEX), PHOTORECEPTORS AND CC ANTENNAE. IN ASYNCHRONOUS INDIVIDUALS, EXPRESSION IS SEEN IN THIRD CC ANTENNAL SEGMENT AND MALE-SPECIFIC EXPRESSION IS SEEN IN THE CC BRAIN-ASSOCIATED FAT BODY. CC -!- INDUCTION: STARVATION AND CIRCADIAN CLOCK. IN THE HEADS OF CC ENTRAINED FLIES, LEVELS FLUCTUATE DAILY AND THE CYCLE PHASE IS CC DELAYED WITH RESPECT TO PER AND TIM. CYCLING APPEARS TO BE LINKED CC TO THE ENDOGENOUS CLOCK RATHER THAN LIGHT CC STIMULI. CC -!- SIMILARITY: BELONGS TO THE TO FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF261748; AAF79960.1; -. DR EMBL; AE003751; AAF56425.2; -. DR EMBL; AY122096; AAM52608.1; ALT_INIT. DR FlyBase; FBgn0039298; to. DR GO; GO:0009267; P:cellular response to starvation; IEP. DR GO; GO:0007623; P:circadian rhythm; IEP. DR GO; GO:0007631; P:feeding behavior; NAS. DR GO; GO:0008049; P:male courtship behavior; IGI. DR InterPro; IPR004272; Odorant_binding. DR Pfam; PF03027; DUF233; 1. DR SMART; SM00700; JHBP; 1. KW Behavior; Biological rhythms; Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 249 TAKEOUT PROTEIN. SQ SEQUENCE 249 AA; 27343 MW; CC3C8634310D5061 CRC64; MFAIAFAVVL CLLVSVDAKF PEDPKPCKYG DGECIMKLCN TLFSENSAEG DPGLNLMQLD PLKVDRMVIS QGESSSPVGI TLTFTDNLLY GIKDQRIVKV KGFGRDLTAK HEVKIVTKTF SLVGPYNIQG KVLILPISGT GQSNMTMVNV RAIVSFSGKP LVKNGETYLD VTDLKITMKP ESSHYHFSNL FNGDKALGDN MNVFLNENSE AIYKETAKAI DRSFGKLYLG VVKGVFSKLP YAKFFADES // ID TAL1_DROME STANDARD; PRT; 320 AA. AC Q9W1G0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable transaldolase (EC 2.2.1.2). GN TAL OR CG2827. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TRANSALDOLASE IS IMPORTANT FOR THE BALANCE OF CC METABOLITES IN THE PENTOSE-PHOSPHATE PATHWAY (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: SEDOHEPTULOSE 7-PHOSPHATE + D-GLYCERALDEHYDE CC 3-PHOSPHATE = D-ERYTHROSE 4-PHOSPHATE + D-FRUCTOSE 6-PHOSPHATE. CC -!- PATHWAY: PENTOSE PHOSPHATE PATHWAY; NONOXIDATIVE PART. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE TRANSALDOLASE FAMILY. SUBFAMILY 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003462; AAF47106.1; -. DR EMBL; AY118920; AAM50780.1; -. DR HSSP; P30148; 1ONR. DR FlyBase; FBgn0023477; Tal. DR InterPro; IPR001585; Transaldolase. DR InterPro; IPR004730; Transaldolase_AB. DR Pfam; PF00923; Transaldolase; 1. DR TIGRFAMs; TIGR00874; talAB; 1. DR PROSITE; PS01054; TRANSALDOLASE_1; 1. DR PROSITE; PS00958; TRANSALDOLASE_2; 1. KW Transferase; Pentose shunt. FT ACT_SITE 140 140 BY SIMILARITY. SQ SEQUENCE 320 AA; 35460 MW; 3D9D81129D2DA43F CRC64; MSVLQELKKI TTIVADTGDF EAINIYKPTD ATTNPSLILS ASSMERYQPL VQKAVEYAKG KKGSVSEQVA EAMDYLCVLF GTEILKVVPG RVSTEIDARL SFDTKKSVEK ALKLIALYKS LGVDKERILI KLASTWEGIK AAEILENEHG VHCNLTLLFS FAQAVACAEA GVTLISPFVG RILDWYVANT DTKKFEALKD PGVISVTNIY NYYKKFGYKT LVMGASFRNV GEIKALAGCD LLTISPALLK ELENETESVV TYLSVSNAKL QDIEKITVDE SRFRWLLNED AMATDKLSEG IRKFAVDTVK LENLIKTYLK // ID TAN_DROME STANDARD; PRT; 299 AA. AC Q8T0D4; Q9NHW6; Q9VRT0; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tantalus protein. GN TAN OR CG6586. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH ASX. RC TISSUE=Embryo; RX MEDLINE=21290825; PubMed=11397012; RA Dietrich B.H., Moore J., Kyba M., dosSantos G., McCloskey F., RA Milne T.A., Brock H.W., Krause H.M.; RT "Tantalus, a novel ASX-interacting protein with tissue-specific RT functions."; RL Dev. Biol. 234:441-453(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: POTENTIAL COFACTOR INVOLVED IN SENSORY ORGAN CC DEVELOPMENT. DESPITE ITS INTERACTION WITH THE POLYCOMB GROUP CC PROTEIN ASX, IT DOES NOT REGULATE THE EXPRESSION OF HOMEOTIC CC GENES. CC -!- SUBUNIT: BINDS TO DNA IN VITRO. INTERACTS DIRECTLY WITH ASX. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. IN EMBRYOS, IT IS CC PREDOMINANTLY CYTOPLASMIC. IN THIRD INSTAR LARVAE, IT IS CC PREDOMINANTLY NUCLEAR OR CYTOPLASMIC DEPENDING ON TISSUES. CC COLOCALIZES WITH ASX ON MANY BINDING SITES ON POLYTENE CC CHROMOSOMES, BUT DOES NOT BIND TO HOMEOTIC GENES LOCI. CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED IN PRECELLULARIZED CC EMBRYOS. THEN IT DECREASES AT CELLULAR BLASTODERM TO INCREASE CC AGAIN DURING GERM BAND EXTENTION. DURING GERM BAND EXTENTION, IT CC IS HIGHLY EXPRESSED IN SOMATIC AND VISCERAL MESODERM. CC UBIQUITOUSLY EXPRESSED IN IMAGINAL DISKS. IN OVARY, IT IS CC EXPRESSED FROM STAGE 10. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF218585; AAF26736.1; -. DR EMBL; AE003564; AAF50710.2; -. DR EMBL; AY069394; AAL39539.1; -. DR FlyBase; FBgn0028980; tan. KW DNA-binding; Developmental protein. FT CONFLICT 63 63 H -> Q (IN REF. 1). SQ SEQUENCE 299 AA; 33765 MW; D087870EC0B16233 CRC64; MDNIVYDFAK ITFQAKDNRS PTTNSNLSWQ LNQMALSDME EMQDTSEPIA PPESDDNVSS ESHDSDDVDS QLSRCEDNDD DSDCISGSSR RSSTFGARAG VARRRMPARV SKDNFNRICS AIMKPIKKKQ RKELNTNAQT LKSIEKIYTS RRMKKFTPTN LETIFEEPSD ENAADAEDDS EECSISSQVK VVKVWGRKLR RAISFSDGLN KNKILSKRRR QKVKKTFGKR FALKKISMTE FHDRLNKSFD SAMLEGDDAE AGGSAEAVNI PKTSMTMEDI QLPTMSSQHQ FLMQPAGFE // ID TAP_DROME STANDARD; PRT; 398 AA. AC O16867; P91640; Q9VVF9; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Basic helix-loop-helix neural transcription factor TAP (Protein DE biparous). GN TAP OR BPS OR CG7659. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97115720; PubMed=8954743; RA Bush A.B., Hiromi Y.H., Cole M.D.; RT "Biparous: a novel bHLH gene expressed in neuronal and glial RT precursors in Drosophila."; RL Dev. Biol. 180:759-772(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=97354289; PubMed=9210583; RA Gautier P., Ledent V., Massaer M., Dambly-Chaudiere C., Ghysen A.; RT "tap, a Drosophila bHLH gene expressed in chemosensory organs."; RL Gene 191:15-21(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP CHARACTERIZATION. RC STRAIN=Oregon-R; RX MEDLINE=98211586; PubMed=9551861; RA Ledent V., Gaillard F., Gautier P., Ghysen A., Dambly-Chaudiere C.; RT "Expression and function of tap in the gustatory and olfactory organs RT of Drosophila."; RL Int. J. Dev. Biol. 42:163-170(1998). CC -!- FUNCTION: MAY PLAY A ROLE IN THE SPECIFICATION OF THE SUGAR- CC SENSITIVE ADULT GUSTATORY NEURON AND AFFECT THE RESPONSE TO SUGAR CC AND SALT. REGULATED BY POXN. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF022883; AAC80572.1; -. DR EMBL; X95845; CAA65103.1; -. DR EMBL; AE003524; AAF49352.1; -. DR FlyBase; FBgn0015550; tap. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW DNA-binding; Nuclear protein; Transcription regulation; Neurogenesis; KW Developmental protein; Differentiation. FT DNA_BIND 155 166 BASIC DOMAIN. FT DOMAIN 167 207 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 18 23 POLY-ASP. FT DOMAIN 308 312 POLY-GLN. SQ SEQUENCE 398 AA; 44850 MW; 54FF558483B18258 CRC64; MAACYNAYSA GSQSFEFDED DDDASFDSGY EKSFETEAQL SSRRRLDFGT PPTPAIPQPY SGGTWDAVPL SSPPAGFVGL LDTSSNHSTR SGRTLVEHLN SRATNGVFDP PLTSTPVKSP EDPNAPRPKR KYAVGKNRVT RSRSPTQVVK IKRFRRMKAN DRERNRMHNL NDALEKLRVT LPSLPEETKL TKIEILRFAH NYIFALEQVL ESGGSINLDL EKLQNFTLSG ERITKELFDA LFVNPQPYPL FGRMFPYGQG MAPLAQHQTA PASHAEQPPA MGGFQHGMDY PQQPPGFDFT GSMRFYHQQQ QQPHQPHHLQ PNPQQESSPQ QFSQEKYDLF RGSFDAAANL HSTNLDSGIH QQSSFYSQTP PWKDYPEDQA HVHPVPHQHS YKNFAPQV // ID TBA1_DROME STANDARD; PRT; 450 AA. AC P06603; Q9VI59; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tubulin alpha-1 chain. GN ALPHA-TUB84B OR TUBA84B OR CG1913. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87041478; PubMed=3095837; RA Theurkauf W.E., Baum H., Bo J., Wensink P.C.; RT "Tissue-specific and constitutive alpha-tubulin genes of Drosophila RT melanogaster code for structurally distinct proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8477-8481(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. IT CC BINDS TWO MOLES OF GTP, ONE AT AN EXCHANGEABLE SITE ON THE BETA CC CHAIN AND ONE AT A NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN. CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M14643; AAA28985.1; -. DR EMBL; AE003672; AAF54067.1; -. DR PIR; A26488; A26488. DR FlyBase; FBgn0003884; alpha-Tub84B. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (POTENTIAL). FT SITE 450 450 INVOLVED IN POLYMERIZATION. SQ SEQUENCE 450 AA; 49908 MW; E4521F429F5045D2 CRC64; MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TVGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD RIRKLADQCT GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGMDSG DGEGEGAEEY // ID TBA2_DROME STANDARD; PRT; 449 AA. AC P06604; Q9VH86; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tubulin alpha-2 chain. GN ALPHA-TUB85E OR TUBA85E OR CG9476. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87041478; PubMed=3095837; RA Theurkauf W.E., Baum H., Bo J., Wensink P.C.; RT "Tissue-specific and constitutive alpha-tubulin genes of Drosophila RT melanogaster code for structurally distinct proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8477-8481(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 65-79 AND 86-95. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. IT CC BINDS TWO MOLES OF GTP, ONE AT AN EXCHANGEABLE SITE ON THE BETA CC CHAIN AND ONE AT A NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN. CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M14644; AAA28986.1; -. DR EMBL; AE003684; AAF54433.1; -. DR PIR; B26488; B26488. DR FlyBase; FBgn0003886; alpha-Tub85E. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (POTENTIAL). FT SITE 449 449 INVOLVED IN POLYMERIZATION. SQ SEQUENCE 449 AA; 49966 MW; 61BBF5AF92308AB6 CRC64; MRECISVHIG QAGVQIGNAC WELYCLEHGI QPDGHMPSDK TVGGGDDSFS TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDVVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYMNLNRL IGQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISVEK AYHEQLTVAE ITNACFEPAN QMVKCDPRRG KYMACCMLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFAE AREDLAALEK DYEEVGIDST TELGEDEEY // ID TBA3_DROME STANDARD; PRT; 450 AA. AC P06605; Q9VIB8; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tubulin alpha-3 chain. GN ALPHA-TUB84D OR TUBA84D OR CG2512. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87041478; PubMed=3095837; RA Theurkauf W.E., Baum H., Bo J., Wensink P.C.; RT "Tissue-specific and constitutive alpha-tubulin genes of Drosophila RT melanogaster code for structurally distinct proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8477-8481(1986). RN [2] RP REVISIONS. RA Wensink P.C.; RL Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. IT CC BINDS TWO MOLES OF GTP, ONE AT AN EXCHANGEABLE SITE ON THE BETA CC CHAIN AND ONE AT A NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN. CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M14645; AAA28987.1; -. DR EMBL; AE003671; AAF54007.1; -. DR PIR; C26488; C26488. DR FlyBase; FBgn0003885; alpha-Tub84D. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (POTENTIAL). FT SITE 450 450 INVOLVED IN POLYMERIZATION. SQ SEQUENCE 450 AA; 49890 MW; 4C55DCA1D734D5CC CRC64; MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TVGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD RIRKLADQCT GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFA VYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKVDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGMDSG DGEGEGAEEY // ID TBA4_DROME STANDARD; PRT; 462 AA. AC P06606; Q9VT30; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tubulin alpha-4 chain. GN ALPHA-TUB67C OR TUBA67C OR CG8308. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87041478; PubMed=3095837; RA Theurkauf W.E., Baum H., Bo J., Wensink P.C.; RT "Tissue-specific and constitutive alpha-tubulin genes of Drosophila RT melanogaster code for structurally distinct proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8477-8481(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. IT CC BINDS TWO MOLES OF GTP, ONE AT AN EXCHANGEABLE SITE ON THE BETA CC CHAIN AND ONE AT A NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN. CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M14646; AAA28988.1; -. DR EMBL; AE003551; AAF50226.2; -. DR FlyBase; FBgn0004236; alpha-Tub67C. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 153 159 GTP (POTENTIAL). SQ SEQUENCE 462 AA; 51180 MW; 08B7AEF53E1B7592 CRC64; MREVVSIQIG QCGIQIGNAC WELYLLEHGI NLDGSLKTKE ELTASGSSAS VGHDTSANDA RTFFTETGNG KQVPRSIFVD LEPTVIDDVR NGCMRELYHP EQLISGKEDA ANNYARGRYS IGKEVIDRVT SRLQKIAEQC DSLQGFLIFH SLGGGTGSGF TSLLVERLST DYSKKCKLDF AVYPSPKVST AVVEPYNALL TTHSTMDHSD CVFMVDNEAI YDICNNSLGV DRPAYRNLNR LIAQIVSSTT ASLRFSGSMN VDLNEFQTNL VPFPRIHFPL VAYAPLMSAE RSAHEQHAIT TLTNACFESS NMMVKCDPRA GKFMACCMLY RGDVVPKDVN AAVSAIKSKR HIQFVDWCPT GFKIGINYEK PAFVPDGDLA KTSRACCMLS NTTAISVAFS NLSYKFDLMF KKRAFVHWYV GEGMEEGEFT EARENIAVLE RDFEEVGLDN AEEGGDEDFD EF // ID TBB1_DROME STANDARD; PRT; 447 AA. AC Q24560; Q9V8V4; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tubulin beta-1 chain. GN BETA-TUB56D OR CG9277. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88054313; PubMed=3119300; RA Michiels F., Falkenburg D., Mueller A.M., Hinz U., Otto U., RA Bellmann R., Glaetzer K.H., Brand R., Bialojan S., Renkawitz-Pohl R.; RT "Testis-specific beta 2 tubulins are identical in Drosophila RT melanogaster and D. hydei but differ from the ubiquitous beta 1 RT tubulin."; RL Chromosoma 95:387-395(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. IT CC BINDS TWO MOLES OF GTP, ONE AT AN EXCHANGEABLE SITE ON THE BETA CC CHAIN AND ONE AT A NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN (BY CC SIMILARITY). CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M20419; AAA28989.1; -. DR EMBL; AE003796; AAF57555.1; -. DR FlyBase; FBgn0003887; beta-Tub56D. DR GO; GO:0045298; C:tubulin; ISS. DR GO; GO:0005525; F:GTP binding; ISS. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IC. DR GO; GO:0007017; P:microtubule-based process; ISS. DR InterPro; IPR002453; Beta_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 140 146 GTP (POTENTIAL). FT CONFLICT 35 35 A -> T (IN REF. 1). FT CONFLICT 163 163 I -> S (IN REF. 1). SQ SEQUENCE 447 AA; 50147 MW; 9E6F66C5C96731DB CRC64; MREIVHIQAG QCGNQIGAKF WEIISDEHGI DATGAYHGDS DLQLERINVY YNEASGGKYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTYSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGVTTCL RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNIQNKNSSY FVEWIPNNVK TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQEATA DEDAEFEEEQ EAEVDEN // ID TBB2_DROME STANDARD; PRT; 446 AA. AC P08840; P22247; Q9VHE1; DT 01-NOV-1988 (Rel. 09, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tubulin beta-2 chain. GN BETA-TUB85D OR TUBB85D OR CG9359. OS Drosophila melanogaster (Fruit fly), and OS Drosophila hydei (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7224; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster, and D.hydei; RX MEDLINE=88054313; PubMed=3119300; RA Michiels F., Falkenburg D., Mueller A.M., Hinz U., Otto U., RA Bellmann R., Glaetzer K.H., Brand R., Bialojan S., RA Renkawitz-Pohl R.; RT "Testis-specific beta 2 tubulins are identical in Drosophila RT melanogaster and D. hydei but differ from the ubiquitous beta 1 RT tubulin."; RL Chromosoma 95:387-395(1987). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 47-58 AND 104-121. RC SPECIES=D.melanogaster; STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. IT CC BINDS TWO MOLES OF GTP, ONE AT AN EXCHANGEABLE SITE ON THE BETA CC CHAIN AND ONE AT A NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN. CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS. CC -!- TISSUE SPECIFICITY: TESTIS SPECIFIC. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M20420; AAA28991.1; -. DR EMBL; M20421; AAA28992.1; -. DR EMBL; AE003682; AAF54373.1; -. DR FlyBase; FBgn0003889; beta-Tub85D. DR FlyBase; FBgn0012356; Dhyd\beta-Tub85D. DR GO; GO:0045298; C:tubulin; ISS. DR GO; GO:0005525; F:GTP binding; ISS. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IC. DR GO; GO:0007017; P:microtubule-based process; ISS. DR InterPro; IPR002453; Beta_tubulin. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR InterPro; IPR008280; Tub_FtsZ_C. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 140 146 GTP (POTENTIAL). FT CONFLICT 135 135 L -> S (IN REF. 1). SQ SEQUENCE 446 AA; 49870 MW; E11495E67158E358 CRC64; MREIVHIQAG QCGNQIGGKF WEVISDEHCI DATGTYYGDS DLQLERINVY YNEATGAKYV PRAILVDLEP GTMDSVRSGA FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV RKESEGCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNIQNKNSSF FVEWIPNNCK TAVCDIPPRG LKMSATFIGN STAIQELFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQEATA DEEGEFDEDE EGGGDE // ID TBB3_DROME STANDARD; PRT; 454 AA. AC P08841; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tubulin beta-3 chain. GN BETA-TUB60D OR TUBB60C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87257938; PubMed=3037352; RA Rudolph J.E., Kimble M., Hoyle H.D., Subler M.A., Raff E.C.; RT "Three Drosophila beta-tubulin sequences: a developmentally regulated RT isoform (beta 3), the testis-specific isoform (beta 2), and an RT assembly-defective mutation of the testis-specific isoform (B2t8) RT reveal both an ancient divergence in metazoan isotypes and structural RT constraints for beta-tubulin function."; RL Mol. Cell. Biol. 7:2231-2242(1987). RN [2] RP SEQUENCE OF 15-21 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93170162; PubMed=1363225; RA Hinz U., Wolk A., Renkawitz-Pohl R.; RT "Ultrabithorax is a regulator of beta 3 tubulin expression in the RT Drosophila visceral mesoderm."; RL Development 116:543-554(1992). RN [3] RP SEQUENCE OF 20-44 FROM N.A. RX MEDLINE=93250859; PubMed=8485515; RA Tourmente S., Chapel S., Dreau D., Drake M.E., Bruhat A., RA Couderc J.L., Dastugue B.; RT "Enhancer and silencer elements within the first intron mediate the RT transcriptional regulation of the beta 3 tubulin gene by 20- RT hydroxyecdysone in Drosophila Kc cells."; RL Insect Biochem. Mol. Biol. 23:137-143(1993). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. IT CC BINDS TWO MOLES OF GTP, ONE AT AN EXCHANGEABLE SITE ON THE BETA CC CHAIN AND ONE AT A NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN. CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS. CC -!- MISCELLANEOUS: BETA-3 IS A DEVELOPMENTALLY REGULATED ISOFORM. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22335; AAA28993.1; -. DR EMBL; M22341; AAA28993.1; JOINED. DR EMBL; X68393; CAA48459.1; -. DR EMBL; S60740; AAD13917.1; -. DR PIR; B27810; B27810. DR PIR; S33567; S33567. DR FlyBase; FBgn0003888; beta-Tub60D. DR GO; GO:0005874; C:microtubule; IDA. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0007627; P:larval behavior (sensu Insecta); IMP. DR GO; GO:0009416; P:response to light; IMP. DR InterPro; IPR002453; Beta_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 146 152 GTP (POTENTIAL). SQ SEQUENCE 454 AA; 50900 MW; 457C471788547787 CRC64; MREIVHLQAG QCGNQIGAKF WEIISEEHGI DSNGIYVGDS DLQLERVSVY YNEASAVTRS SGGKYVPRAI LLDLEPGTME SVRSGPYGQL FRPDNFVYGQ SGAGNNWAKG HYTEGAELVD NVLDVVRKEC ENCDCLQGFQ LTHSLGGGTG SGMGTLLISK IREEYPDRIM NTYSVVPSPK VSDTVVEPYN ATLSIHQLVE NTDETYCIDN EALYDICFRT LKVSNPSYGD LNHLVSLTMS GVTTCLRFPG QLNADLRKLA VNMVPFPRLH FFMPGFAPLT SRGSQQYRAL TVPELTQQMF DAKNMMAACD PRHGRYLTVA AVFRGRMSMK EVDEQMLAVQ NKNSSYFVEW IPNNVKTAVC DIPPRGLKMS STFIGNTTAI QELFKRISEQ FSAMFRRKAF LHWYTGEGMD EMEFTEAESN MNDLVSEYQQ YQEATADDEF DPEVNQEEVE GDCI // ID TBG1_DROME STANDARD; PRT; 475 AA. AC P23257; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin gamma-1 chain (Gamma-1 tubulin). GN TUBG1 OR TUBG OR TUBG23C OR TUB23C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91249388; PubMed=1904010; RA Zheng Y., Jung M.K., Oakley B.R.; RT "Gamma-tubulin is present in Drosophila melanogaster and Homo sapiens RT and is associated with the centrosome."; RL Cell 65:817-823(1991). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. GAMMA CC TUBULIN IS FOUND AT MICROTUBULE ORGANIZING CENTERS (MTOC) SUCH AS CC THE SPINDLE POLES OR THE CENTROSOME, SUGGESTING THAT IT IS CC INVOLVED IN THE MINUS-END NUCLEATION OF MICROTUBULE ASSEMBLY. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M61765; AAA28597.1; -. DR PIR; B39527; UBFFG. DR FlyBase; FBgn0004176; gamma-Tub23C. DR GO; GO:0008275; C:gamma-tubulin small complex; IPI. DR GO; GO:0019001; F:guanyl nucleotide binding; IDA. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (POTENTIAL). SQ SEQUENCE 475 AA; 53311 MW; B1DF97014BEE5362 CRC64; MPSEIITLQL GQCGNQIGFE FWKRLCLEHG ISPSGVLEDF ANDGLDRKDV FFYQADDDHY IPRAVLLDLE PRVINTIMGS VYSKLYNPEN VYLSKHGGGA GNNWASGYSQ GEKLQEEVFD IIDREADGSD SLEGFILCHS IAGGTGSGMG SFIMERLADR YPKKLIQTFS VFPNQDEISD VVVQPYNSML TLKRLTTAAD SVVVLDNTAL NRIACDRLHI QNPSFSQINN LVSTIMSVST TTLRYPSYMN NNLIGLTAPL IPTPQLHFLM TGYTPLTSDS DIHTQQLVNV RKTTVLDVMR RLLQPKNMMV STGPDKSNHH CYISILNIIQ GEVDPTQVHK SLQRIRDRKM AQFIPWGPTS IQVALSRSSP YVQSNHRVSG LMLANHTSIC SLFERALNQY DNVRKRGAFL DQFRREDIFK DDLNELDESR ETVDCLVQEY EAATREDYMQ FSVKRGNGPV DSKSEDSRSV TSAGS // ID TBG2_DROME STANDARD; PRT; 457 AA. AC P42271; DT 01-NOV-1995 (Rel. 32, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin gamma-2 chain (Gamma-2 tubulin). GN TUBG2 OR TUBG37C OR TUB37CD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=97278854; PubMed=9133431; RA Wilson P.G., Zheng Y., Oakley C.E., Oakley B.R., Borisy G.G., RA Fuller M.T.; RT "Differential expression of two gamma-tubulin isoforms during RT gametogenesis and development in Drosophila."; RL Dev. Biol. 184:207-221(1997). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. GAMMA CC TUBULIN IS FOUND AT MICROTUBULE ORGANIZING CENTERS (MTOC) SUCH AS CC THE SPINDLE POLES OR THE CENTROSOME, SUGGESTING THAT IT IS CC INVOLVED IN THE MINUS-END NUCLEATION OF MICROTUBULE ASSEMBLY. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M76765; AAB52553.1; -. DR PIR; T08419; T08419. DR FlyBase; FBgn0010097; gamma-Tub37C. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (POTENTIAL). SQ SEQUENCE 457 AA; 51266 MW; E0CC99794DEED181 CRC64; MPSEIITLQL GQCGNQIGFE FWKRLCLEHG ISPDGVLEDF ATDGQDRKDV FFYQADDNHY IPRAVLIDLE PRVINNIMTS PYSKLYNQEN VFLSKHGGGA GNNWASGFSQ GEKVQEEVFD ILDREADGSD SLEGFVLCHS IAGGTGSGMG SYVLERLSER FPKKLIQTYS VFPNQDEISD VVVQPYNSIL TLKRLTKCAD SVVVLDNTAL NRIATERLHI QTPTFTQINN LVSTIMSLST TTLRYPSYMN NNLIGLTASL IPTPQLHFLM TGYTPLMSDC EAKTSVRKTT VLDVMRRLLQ PKNMMVSALT DKQSRQCFVS ILNIIQGEVD PSQVHKSLQR IRERKLANFI PWGPASIQVA LPRSSPYVQS AHKVSGLMMA NHTGISSLFK RALAQYDKLR KRNAFLDNFR RESMFQDDLT ELDIARDTVD CLVQEYEAAT QIDYPQWSPA VEASKAG // ID TBP_DROME STANDARD; PRT; 353 AA. AC P20227; Q9W2D8; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE TATA-box binding protein (TATA-box factor) (TATA binding factor) (TATA DE sequence-binding protein) (Transcription initiation factor TFIID TBP DE subunit). GN TBP OR TFIID OR BTF1 OR CG9874. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90304877; PubMed=2194666; RA Hoey T., Dynlacht B.D., Peterson M.G., Pugh B.F., Tjian R.; RT "Isolation and characterization of the Drosophila gene encoding the RT TATA box binding protein, TFIID."; RL Cell 61:1179-1186(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91067664; PubMed=2123550; RA Muhich M., Iida C.T., Horikoshi M., Roeder R.G., Parker C.S.; RT "cDNA clone encoding Drosophila transcription factor TFIID."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9148-9152(1990). RN [3] RP SEQUENCE FROM N.A. RA Lira-Devito L.M., Burke T.W., Kadonaga J.T.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Lee K., Oh Y., Yoon J., Cho N., Baek K.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GENERAL TRANSCRIPTION FACTOR THAT FUNCTIONS AT THE CC CORE OF THE DNA-BINDING MULTIPROTEIN FACTOR TFIID. BINDING OF CC TFIID TO THE TATA BOX IS THE INITIAL TRANSCRIPTIONAL STEP OF THE CC PRE-INITIATION COMPLEX (PIC), PLAYING A ROLE IN THE ACTIVATION OF CC EUKARYOTIC GENES TRANSCRIBED BY RNA POLYMERASE II. CC -!- SUBUNIT: BELONGS TO THE TFIID COMPLEX TOGETHER WITH THE TBP- CC ASSOCIATED FACTORS (TAFS). BINDS DNA AS MONOMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE TBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M38388; AAA28926.1; -. DR EMBL; M38082; AAA28931.1; -. DR EMBL; U11718; AAA68629.1; -. DR EMBL; U35147; AAA79092.1; -. DR EMBL; AE003454; AAF46754.1; -. DR PIR; A35615; A35615. DR HSSP; P20226; 1CDW. DR TRANSFAC; T00797; -. DR FlyBase; FBgn0003687; Tbp. DR InterPro; IPR000814; TFIID. DR Pfam; PF00352; TBP; 2. DR PRINTS; PR00686; TIFACTORIID. DR PROSITE; PS00351; TFIID; 2. KW Transcription; Nuclear protein; DNA-binding; Repeat. FT DOMAIN 54 61 POLY-GLN. FT DOMAIN 94 103 POLY-GLN. FT REPEAT 179 255 1. FT REPEAT 269 346 2. FT CONFLICT 101 101 Q -> QQ (IN REF. 4). FT CONFLICT 146 146 G -> A (IN REF. 4). SQ SEQUENCE 353 AA; 38451 MW; 7B079BC01BAF69BC CRC64; MDQMLSPNFS IPSIGTPLHQ MEADQQIVAN PVYHPPAVSQ PDSLMPAPGS SSVQHQQQQQ QSDASGGSGL FGHEPSLPLA HKQMQSYQPS ASYQQQQQQQ QLQSQAPGGG GSTPQSMMQP QTPQSMMAHM MPMSERSVGG SGAGGGGDAL SNIHQTMGPS TPMTPATPGS ADPGIVPQLQ NIVSTVNLCC KLDLKKIALH ARNAEYNPKR FAAVIMRIRE PRTTALIFSS GKMVCTGAKS EDDSRLAARK YARIIQKLGF PAKFLDFKIQ NMVGSCDVKF PIRLEGLVLT HCNFSSYEPE LFPGLIYRMV RPRIVLLIFV SGKVVLTGAK VRQEIYDAFD KIFPILKKFK KQS // ID TCP4_DROME STANDARD; PRT; 110 AA. AC Q9VLR5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative RNA polymerase II transcriptional coactivator. GN SSB-C31A OR CG8396. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GENERAL COACTIVATOR THAT FUNCTIONS COOPERATIVELY WITH CC TAFS AND MEDIATES FUNCTIONAL INTERACTIONS BETWEEN UPSTREAM CC ACTIVATORS AND THE GENERAL TRANSCRIPTIONAL MACHINERY. BINDS CC SINGLE-STRANDED DNA (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TRANSCRIPTIONAL COACTIVATOR PC4 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003620; AAF52619.1; -. DR HSSP; P53999; 1PCF. DR FlyBase; FBgn0015299; Ssb-c31a. DR InterPro; IPR003173; PC4. DR InterPro; IPR009044; ssDNA_bind_regul. DR Pfam; PF02229; PC4; 1. KW Hypothetical protein; Transcription; Transcription regulation; KW Activator; Nuclear protein; DNA-binding. SQ SEQUENCE 110 AA; 12189 MW; 03EF363E88CB32E0 CRC64; MPKTKKKDSS SDSDSGPDDR IKPASKKAKE SDAPNSDPKD SGENGATSWT LEGLRQVRIN EFRGRKSVDI REFYDKGGQI LPGKKGISLS LIQWKKLLEV AEEVTRAIEN // ID TCPA_DROME STANDARD; PRT; 557 AA. AC P12613; Q9VCZ6; DT 01-OCT-1989 (Rel. 12, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE T-complex protein 1, alpha subunit (TCP-1-alpha) (CCT-alpha). GN CCT-1 OR TCP-1 OR CG5374. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89121509; PubMed=3146529; RA Ursic D., Ganetzky B.; RT "A Drosophila melanogaster gene encodes a protein homologous to the RT mouse t complex polypeptide 1."; RL Gene 68:267-274(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MOLECULAR CHAPERONE; ASSIST THE FOLDING OF PROTEINS UPON CC ATP HYDROLYSIS. KNOWN TO PLAY A ROLE, IN VITRO, IN THE FOLDING OF CC ACTIN AND TUBULIN. CC -!- SUBUNIT: HETERO-OLIGOMERIC COMPLEX OF ABOUT 850 TO 900 KDA THAT CC FORMS TWO STACKED RINGS, 12 TO 16 NM IN DIAMETER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE TCP-1 CHAPERONIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M21159; AAA28927.1; -. DR EMBL; AE003739; AAF56009.1; -. DR PIR; JT0367; JT0367. DR HSSP; P48424; 1A6D. DR FlyBase; FBgn0003676; T-cp1. DR InterPro; IPR002194; Chaperonin_TCP-1. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR008950; GroEL-ATPase. DR Pfam; PF00118; cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR PRINTS; PR00304; TCOMPLEXTCP1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. KW Chaperone; ATP-binding; Multigene family. FT CONFLICT 17 19 GAS -> RRI (IN REF. 1). FT CONFLICT 192 192 A -> V (IN REF. 1). FT CONFLICT 198 198 I -> V (IN REF. 1). FT CONFLICT 240 240 L -> H (IN REF. 1). FT CONFLICT 413 413 A -> R (IN REF. 1). SQ SEQUENCE 557 AA; 59556 MW; 6F4A28237456F3A2 CRC64; MSTLASPLSI AGTRQSGASV RTQNVMAALS ISNIVKSSLG PVGLDKMLVD DIGDVTVTND GATILRLLEV EHPAAKVLVE LAQLQDEEVG DGTTSVVILA AELLKNADEL VKQKIHPTSI ISGYRIACKE ACKYISEHLT APVDELGRDS LINIAKTSMS SKIIGADAEF FSAMVVDAAQ SVKITDPRGQ AAYSIKAINV LKAHGKSARE SVLIPGYALN CTIASQQMPK KIVNAKIACL DFSLQKTKMK MGVQVLINDP DKLEAIRARE LDITKERINM ILGTGVNVVL VSGGVDDLCM KYFVEAGAMA VRRVKKSDLK IIAKATGAAF ITSLTNMDGE ESFDASMVGE AAEVAQERIC DDELILIKGT KARAAASIIL RGPNDFYCDE MERSVHDALC VVKRVLESKK VVAGGGCVEA ALSIYLENFA TSLASREQLA IAEFAKSLLV IPKTLSVNAA KDATDLVAKL RSYHNSSQTK PERSDLKWTG LDLIEGVVRD NKKAGVLEPA MSKIKSLKFA TEAAITILRI DDMIKLNPED KSGKSYADAC AAGELDG // ID TCPG_DROME STANDARD; PRT; 544 AA. AC P48605; Q9VER9; DT 01-FEB-1996 (Rel. 33, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE T-complex protein 1, gamma subunit (TCP-1-gamma) (CCT-gamma). GN CCT-GAMMA OR CCT-3 OR CCTG OR CG8977. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D., RA Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96257223; PubMed=8666276; RA Walkley N.A., Malik A.N.; RT "Drosophila melanogaster P1 genomic clone DS05563 contains the RT chaperonin-encoding gene Cctg."; RL Gene 171:221-223(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MOLECULAR CHAPERONE; ASSIST THE FOLDING OF PROTEINS UPON CC ATP HYDROLYSIS. KNOWN TO PLAY A ROLE, IN VITRO, IN THE FOLDING OF CC ACTIN AND TUBULIN. CC -!- SUBUNIT: HETERO-OLIGOMERIC COMPLEX OF ABOUT 850 TO 900 KDA THAT CC FORMS TWO STACKED RINGS, 12 TO 16 NM IN DIAMETER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE TCP-1 CHAPERONIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U31961; AAA84416.1; -. DR EMBL; X95602; CAA64860.1; -. DR EMBL; AE003714; AAF55350.1; -. DR HSSP; P48424; 1A6D. DR FlyBase; FBgn0015019; Cct-gamma. DR InterPro; IPR002194; Chaperonin_TCP-1. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR008950; GroEL-ATPase. DR Pfam; PF00118; cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR PRINTS; PR00304; TCOMPLEXTCP1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. KW Chaperone; ATP-binding; Multigene family. FT CONFLICT 12 12 S -> SD (IN REF. 2). FT CONFLICT 35 47 MISSING (IN REF. 1). SQ SEQUENCE 544 AA; 59394 MW; DD5E635809B322C2 CRC64; MFGGQQPILV LSQNTKRESG RKVQLENIQA GKAIADVIRT CLGPQAMLKM LMDPMGGIVM TNDGNAILRE ITVQHPAAKS MIEIARTQDE EVGDGTTSVI VLAGEMLAAA EPFLQQQIHP TVIIRAYREA LEDIVGHLQS QLSIQLDVKD KAKMADVVKA CVGTKFIGKW SDLAVKIALD AVETVTLSEN GRLEVDIKRY AKVEKIPGGA IEESCVLKGV MINKDVTHPK MRRLIENPRI VLLDCSLEYK KGESQTNVEI IGEQDFTRML QIEEEFVQRI CADIIAVKPD LVFTEKGVSD LAQHYLLKAG ITAIRRLRKT DNLRIARACG ATIVNRTEEL TEKDVGTGAG LFEVKKIGDE YFTFVTECKE PKACTILLRG ASKDILNETE RNLQDALHVA RNLVLEPRLV AGGGAVEMAA SQLLTRKQVK GPYTAVAHAL EIIPRTLAQN CGANTIRALT ALRAKHASHT GDGVCAWGID GESGEIVDMN VKNIWEPLAV KLQTYKTAVE TAILLLRIDD IVSGSKKRGG NEPTNPAAMA QGQE // ID TDP_DROME STANDARD; PRT; 377 AA. AC Q24318; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription factor dp. GN DP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye imaginal disk; RX MEDLINE=94294381; PubMed=8022787; RA Dynlacht B.D., Brook A., Dembski M., Yenush L., Dyson N.; RT "DNA-binding and trans-activation properties of Drosophila E2F and DP RT proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6359-6363(1994). CC -!- FUNCTION: CAN STIMULATE E2F-DEPENDENT TRANSCRIPTION. CC -!- SUBUNIT: HETERODIMER OF E2F AND DP. COOPERATE TO GIVE SEQUENCE- CC SPECIFIC DNA BINDING AND OPTIMAL TRANS-ACTIVATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE E2F/DP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X79708; CAA56147.2; ALT_INIT. DR PIR; B55745; B55745. DR HSSP; Q14188; 1CF7. DR TRANSFAC; T01550; -. DR FlyBase; FBgn0011763; Dp. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0008069; P:dorsal/ventral axis determination, follicul...; IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0045850; P:positive regulation of nurse cell apoptosis; IMP. DR GO; GO:0000074; P:regulation of cell cycle; IMP. DR InterPro; IPR003316; E2F_TDP. DR Pfam; PF02319; E2F_TDP; 1. KW Transcription regulation; DNA-binding; Nuclear protein. FT DOMAIN 81 88 POLY-SER. SQ SEQUENCE 377 AA; 42683 MW; 868F180D242C3DDC CRC64; MGAFSQMGSQ GQFIRLQDNG LSIPKTEAGT TYTTVSAQKT SGAGSGHYDL PLKGDRYVKF TPNPIKMKSK LHAIQSNSLH SMSASSSSVQ RKRKPDKAGK GLRHFSMKVC EKVEEKGKTT YNEVADDLVS EEMKNNAYDN NCDQKNIRRR VYDALNVLMA INVISKDKKE IRWIGLPANS TETFLALEEE NCQRRERIKQ KNEMLREMIM QHVAFKGLVE RNKRNESQGV VPSPNASIQL PFIIVNTHKS TKINCSVTND KSEYIFKFDK TFEMHDDIEV LKRMGFLLGL DKGECTPENI ERVKSWVPPN LAKYVEAYGT GKTGENMYES DDEDNEFNGY LESANESQGF AQHSAQHTTD GEFKLEMDDD ELDDDID // ID TERM_DROME STANDARD; PRT; 428 AA. AC P11455; Q9VVQ3; DT 01-OCT-1989 (Rel. 12, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Terminus protein. GN TERM OR TER OR CG4216. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88055884; PubMed=3334721; RA Baldarelli R.M., Mahoney P.A., Salas F., Gustavson E., Boyer P.D., RA Chang M.-F., Roark M., Lengyel J.A.; RT "Transcripts of the Drosophila blastoderm-specific locus, terminus, RT are concentrated posteriorly and encode a potential DNA-binding RT finger."; RL Dev. Biol. 125:85-95(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM THE CELLULAR BLASTODERM STAGE CC ON, MOST DURING GASTRULATION AND IS NO LONGER DETECTED BY THE END CC OF GERM BAND EXTENSION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19140; AAA28928.1; -. DR EMBL; AE003520; AAF49257.1; -. DR PIR; A43741; A43741. DR FlyBase; FBgn0003683; term. DR InterPro; IPR007087; Znf_C2H2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; UNKNOWN_1. KW DNA-binding; Zinc-finger; Developmental protein. FT ZN_FING 325 346 C3H-TYPE. FT CONFLICT 144 144 A -> V (IN REF. 1). SQ SEQUENCE 428 AA; 49165 MW; F545653F738AE434 CRC64; MFDEPIISSF VFTNEETTQT FHHQWFSQGQ LHECATCYSS IDADEPPSQH WLRGGEASQG LHLTKQQQAV MDIIEARQIE TFFFCDESSK DKLEHFMGET CARGIPELLR WMFQNNTVAV EFNLACYVNA MDQVLIFQSG SLRADHHYDV DESVGVVYEM LMQRIENYLN CSSEYGMAEC SITRLKVQVK RIRVEADGQS ADSSVFALPL QLQEEEGLTA TTGCSTSEAE LASLRSAYLK HFRECNGYFP PNMRVNLYGL QQCKTTKELY VVPYHISETL QQLPNKNFLI LNNIMGQFQR LHELSTPVNS IERDQTSSPL KDLHCRRCRT QFSRRSKLHI HQKLRCGQDF SVDSMHADIV EIYEQCLPIS RSVFQHACYG ITKPKTMMRK GQFVPIECDW RSESSVKVQH GPCVVISNAQ HNSPCKFY // ID TF2B_DROME STANDARD; PRT; 315 AA. AC P29052; Q9VKV7; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transcription initiation factor IIB (General transcription factor DE TFIIB). GN TFIIB OR CG5193. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92212925; PubMed=1557390; RA Yamashita S., Wada K., Horikoshi M., Gong D.W., Kokubo T., RA Hisatake K., Yokotani N., Malik S., Roeder R.G., Nakatani Y.; RT "Isolation and characterization of a cDNA encoding Drosophila RT transcription factor TFIIB."; RL Proc. Natl. Acad. Sci. U.S.A. 89:2839-2843(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92354915; PubMed=1644295; RA Wampler S.L., Kadonaga J.T.; RT "Functional analysis of Drosophila transcription factor IIB."; RL Genes Dev. 6:1542-1552(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Lira-Devito L.M., Kadonaga J.T.; RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Yoon J., Oh Y., Lee K., Baek K.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GENERAL FACTOR THAT PLAYS A MAJOR ROLE IN THE ACTIVATION CC OF EUKARYOTIC GENES TRANSCRIBED BY RNA POLYMERASE II. CC -!- COFACTOR: BINDS 1 ZINC ION PER SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: ASSOCIATES WITH TFIID-IIA (DA COMPLEX) TO FORM TFIID- CC IIA-IIB (DAB-COMPLEX) WHICH IS THEN RECOGNIZED BY POLYMERASE II. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE TFIIB FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M88164; AAA28930.1; -. DR EMBL; M91081; AAA28929.1; -. DR EMBL; U02879; AAA68626.1; -. DR EMBL; U35148; AAA79093.1; -. DR EMBL; AE003628; AAF52951.1; -. DR PIR; A42695; A42695. DR HSSP; Q00403; 1TFB. DR TRANSFAC; T02158; -. DR FlyBase; FBgn0004915; TfIIB. DR InterPro; IPR006670; Cyclin. DR InterPro; IPR000812; TFIIB_euk. DR Pfam; PF00382; transcript_fac2; 2. DR PRINTS; PR00685; TIFACTORIIB. DR SMART; SM00385; CYCLIN; 2. DR PROSITE; PS00782; TFIIB; 2. KW Transcription regulation; Nuclear protein; Repeat; Zinc-finger; KW Metal-binding; Zinc. FT ZN_FING 14 36 ZN-RIBBON TFIIB-TYPE. FT REPEAT 123 199 1. FT REPEAT 217 293 2. FT METAL 14 14 ZINC (BY SIMILARITY). FT METAL 17 17 ZINC (BY SIMILARITY). FT METAL 33 33 ZINC (BY SIMILARITY). FT METAL 36 36 ZINC (BY SIMILARITY). SQ SEQUENCE 315 AA; 34369 MW; AA5803F7B94BB1F4 CRC64; MASTSRLDNN KVCCYAHPES PLIEDYRAGD MICSECGLVV GDRVIDVGSE WRTFSNEKSG VDPSRVGGPE NPLLSGGDLS TIIGPGTGSA SFDAFGAPKY QNRRTMSSSD RSLISAFKEI SSMADRINLP KTIVDRANNL FKQVHDGKNL KGRSNDAKAS ACLYIACRQE GVPRTFKEIC AVSKISKKEI GRCFKLTLKA LETSVDLITT ADFMCRFCAN LDLPNMVQRA ATHIAKKAVE MDIVPGRSPI SVAAAAIYMA SQASEHKRSQ KEIGDIAGVA DVTIRQSYKL MYPHAAKLFP EDFKFTTPID QLPQM // ID TFH1_DROME STANDARD; PRT; 585 AA. AC Q960E8; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE TFIIH basal transcription factor complex subunit 1. GN TFB1 OR CG8151. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPONENT OF THE CORE-TFIIH BASAL TRANSCRIPTION FACTOR CC INVOLVED IN NUCLEOTIDE EXCISION REPAIR (NER) OF DNA AND, WHEN CC COMPLEXED TO CAK, IN RNA TRANSCRIPTION BY RNA POLYMERASE II (BY CC SIMILARITY). CC -!- SUBUNIT: ONE OF THE SIX SUBUNITS FORMING THE CORE-TFIIH BASAL CC TRANSCRIPTION FACTOR (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 2 BSD DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003815; AAM71000.1; -. DR EMBL; AY052097; AAK93521.1; -. DR FlyBase; FBgn0033929; Tfb1. DR InterPro; IPR005607; BSD. DR Pfam; PF03909; BSD; 2. DR PROSITE; PS50858; BSD; 2. KW Transcription regulation; DNA repair; Nuclear protein; Repeat. FT DOMAIN 104 159 BSD 1. FT DOMAIN 180 232 BSD 2. SQ SEQUENCE 585 AA; 66339 MW; 629BE277BC6AF6C0 CRC64; MTTSSEDVLL QMGEVRYKKG DGTLYVMNER VAWMAEHRDT VTVSHRYADI KTQKISPEGK PKVQLQVVLH DGNTSTFHFV NRQGQAAMLA DRDKVKELLQ QLLPNFKRKV DKDLEDKNRI LVENPNLLQL YKDLVITKVL TSDEFWATHA KDHALKKMGR SQEIGVSGAF LADIKPQTDG CNGLKYNLTS DVIHCIFKTY PAVKRKHFEN VPAKMSEAEF WTKFFQSHYF HRDRLTAGTK DIFTECGKID DQALKAAVQQ GAGDPLLDLK KFEDVPLEEG FGSVAGDRNV VNSGNIVHQN MIKRFNQHSI MVLKTCANVT SAPSTMTNGT NNANGPVSQS AYTNGMNGKG QATATATKSS SDQVDKDEPQ SKKQRLMEKI HYVDLGDPIL EGDDSANGEK AKSKHFELSK VERYLNGPVQ NSMYDNHNDP MSLEEVQYKL VRNSESWLNR NVQRTFICSK AAVNALGELS PGGSMMRGFQ EQSAGQLVPN DFQRELRHLY LSLSELLKHF WSCFPPTSEE LETKLQRMHE TLQRFKMAKL VPFENRAMHE LSPLRSSLTQ HLNQLLRTAN SKFATWKERK LRNTR // ID TFS2_DROME STANDARD; PRT; 313 AA. AC P20232; Q9V3M8; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Transcription elongation factor S-II (RNA polymerase II elongation DE factor DMS-II) (TFIIS). GN TFIIS OR DMSII OR CG3710. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91057107; PubMed=2243775; RA Marshall T.K., Guo H., Price D.H.; RT "Drosophila RNA polymerase II elongation factor DmS-II has homology RT to mouse S-II and sequence similarity to yeast PPR2."; RL Nucleic Acids Res. 18:6293-6298(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95290504; PubMed=7772609; RA Oh Y., Yoon J., Baek K.; RT "Isolation and characterization of the gene encoding the Drosophila RT melanogaster transcriptional elongation factor, TFIIS."; RL Biochim. Biophys. Acta 1262:99-103(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: NECESSARY FOR EFFICIENT RNA POLYMERASE II TRANSCRIPTION CC ELONGATION PAST TEMPLATE-ENCODED ARRESTING SITES. THE ARRESTING CC SITES IN DNA HAVE THE PROPERTY OF TRAPPING A CERTAIN FRACTION OF CC ELONGATING RNA POLYMERASES THAT PASS THROUGH, RESULTING IN LOCKED CC TERNARY COMPLEXES. CLEAVAGE OF THE NASCENT TRANSCRIPT BY S-II CC ALLOWS THE RESUMPTION OF ELONGATION FROM THE NEW 3'TERMINUS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: S-II BINDS TO RNA-POLYMERASE II IN THE ABSENCE OF CC TRANSCRIPTION. CC -!- SIMILARITY: BELONGS TO THE TFS-II FAMILY. CC -!- SIMILARITY: CONTAINS 1 RIBBON-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53670; CAA37710.1; -. DR EMBL; L26091; AAA92864.2; ALT_SEQ. DR EMBL; AE003412; AAF44916.1; ALT_SEQ. DR EMBL; AE003646; AAF53436.1; -. DR EMBL; AY051843; AAK93267.1; -. DR PIR; S55899; S55899. DR HSSP; P23193; 1TFI. DR FlyBase; FBgn0010422; TfIIS. DR InterPro; IPR001222; TFIIS. DR InterPro; IPR003618; TFS2_centre. DR InterPro; IPR003617; TFS2_N. DR InterPro; IPR006289; TFSII. DR Pfam; PF01096; TFIIS; 1. DR SMART; SM00510; TFS2M; 1. DR SMART; SM00509; TFS2N; 1. DR SMART; SM00440; ZnF_C2C2; 1. DR TIGRFAMs; TIGR01385; TFSII; 1. DR PROSITE; PS00466; TFIIS; 1. KW Transcription regulation; Zinc-finger; DNA-binding; Nuclear protein. FT DOMAIN 122 128 POLY-SER. FT ZN_FING 275 306 ZN-RIBBON. SQ SEQUENCE 313 AA; 34300 MW; 9DC7D99D71BD3DA3 CRC64; MSVEEEVFRI QKKMSKMASD GTGQDQALDL LKALQTLNIN LDILTKTRIG MTVNELRKSS KDDEVIALAK TLIKNWKRFL ASPAPTTPNN SSAKEGSSNN SSASKSTSAA KSSSSISGKD KSSSSSSSKD KEKKGSTSSS QTSFPSGGMT DAVRIKCREM LATALKIGEV PEGCGEPEEM AAELEDAIYS EFNNTDMKYK NRIRSRVANL KDPKNPGLRG NFMCGAVTAK QLAKMTPEEM ASDEMKKLRE KFVKEAINDA QLATVQGTKT DLLKCAKCKK RNCTYNQLQT RSADEPMTTF VMCNECGNRW KFC // ID TFZ_DROME STANDARD; PRT; 378 AA. AC Q9V6G5; Q8ML32; Q8SZ79; Q9U9U8; Q9V6G4; DT 28-FEB-2003 (Rel. 41, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tafazzin homolog. GN TAFAZZIN OR CG8766. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Canton-S; RA Benevolenskaya E.V., Frolov M.V., Birchler J.A.; RT "Drosophila homolog of the human G4.5 gene encoding tafazzin RT proteins."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 1-39 FROM N.A. (ISOFORM A). RC STRAIN=Canton-S; RX MEDLINE=20556141; PubMed=11102369; RA Frolov M.V., Benevolenskaya E.V., Birchler J.A.; RT "The oxen gene of Drosophila encodes a homolog of subunit 9 of yeast RT ubiquinol-cytochrome c oxidoreductase complex: evidence for RT modulation of gene expression in response to mitochondrial activity."; RL Genetics 156:1727-1736(2000). CC -!- SUBCELLULAR LOCATION: ISOFORMS WITH HYDROPHOBIC N-TERMINUS ARE CC THOUGHT TO BE MEMBRANE ANCHORED (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=Q9V6G5-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9V6G5-2; Sequence=VSP_004450; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q9V6G5-3; Sequence=VSP_007017; CC Note=No experimental confirmation available; CC -!- DOMAIN: THE HYDROPHILIC DOMAIN MAY SERVE AS AN EXPOSED LOOP CC INTERACTING WITH OTHER PROTEINS (BY SIMILARITY). CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT AT POSITION 117. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF148684; AAD48409.1; ALT_FRAME. DR EMBL; AE003821; AAF58461.2; -. DR EMBL; AE003821; AAF58462.3; -. DR EMBL; AE003821; AAM68652.2; -. DR EMBL; AY071059; AAL48681.1; -. DR EMBL; AF017783; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0026619; tafazzin. DR GO; GO:0016021; C:integral to membrane; NAS. DR InterPro; IPR002123; Acyltransferase. DR InterPro; IPR000872; Tafazzin. DR Pfam; PF01553; Acyltransferase; 1. DR PRINTS; PR00979; TAFAZZIN. DR SMART; SM00563; PlsC; 1. KW Alternative splicing; Transmembrane. FT TRANSMEM 138 158 POTENTIAL. FT DOMAIN 243 283 HYDROPHILIC (BY SIMILARITY). FT VARSPLIC 1 41 MFMVVCSNLRRPGHVGAASAARNINWLISEGYTPPIRAMAR FT -> M (in isoform C). FT /FTId=VSP_007017. FT VARSPLIC 1 100 Missing (in isoform B). FT /FTId=VSP_004450. SQ SEQUENCE 378 AA; 43016 MW; 88690B6E2731FFB9 CRC64; MFMVVCSNLR RPGHVGAASA ARNINWLISE GYTPPIRAMA RPYVQAPEAR PVPDERYPGS QQDRKDIATQ TVRSSKPKDL RPPSPPTPSQ TLNSSSLPPP MSDQDADPSL DVPTGVAMPY NIDWIFPRLR NPSKFWYVVS QFVVSAVGIF SKVVLMFLNK PRVYNRERLI QLITKRPKGI PLVTVSNHYS CFDDPGLWGC LPLGIVCNTY KIRWSMAAHD ICFTNKLHSL FFMFGKCIPV VRGIGVYQDA INLCIEKAAL GHWIHVFPEG KVNMDKEELR LKWGVGRIIY ESPKIPIILP MWHEGMDDLL PNVEPYVIQR GKQVTLNVGQ PLDLNDFILD LKKRQVPEPT ARKLITDKIQ EAFRDLRAET EKLHRERN // ID THI1_DROME STANDARD; PRT; 107 AA. AC P47938; Q8MSC0; Q9W4D5; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Thioredoxin 1 (DmTrx-1) (Deadhead protein). GN DHD OR TRX-1 OR CG4193. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=94274010; PubMed=7516301; RA Salz H.K., Flickinger T.W., Mittendorf E., Pellicena-Palle A., RA Petschek J.P., Albrecht E.B.; RT "The Drosophila maternal effect locus deadhead encodes a thioredoxin RT homolog required for female meiosis and early embryonic RT development."; RL Genetics 136:1075-1086(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-31 AND CYS-34. RX MEDLINE=97260068; PubMed=9106167; RA Pellicena-Palle A., Stitzinger S.M., Salz H.K.; RT "The function of the Drosophila thioredoxin homologue encoded by the RT deadhead gene is redox-dependent and blocks the initiation of RT development but not DNA synthesis."; RL Mech. Dev. 62:61-65(1997). RN [5] RP FUNCTION. RX MEDLINE=22001321; PubMed=11877442; RA Bauer H., Kanzok S.M., Schirmer R.H.; RT "Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin RT peroxidase-1 from Drosophila melanogaster: isolation and RT characterization of a second thioredoxin in D. melanogaster and RT evidence for distinct biological functions of Trx-1 and Trx-2."; RL J. Biol. Chem. 277:17457-17463(2002). CC -!- FUNCTION: PARTICIPATES IN VARIOUS REDOX REACTIONS THROUGH THE CC REVERSIBLE OXIDATION OF ITS ACTIVE CENTER DITHIOL TO A DISULFIDE CC AND CATALYZES DITHIOL-DISULFIDE EXCHANGE REACTIONS. AS A REDUCING CC SUBSTRATE OF PEROXIREDOXIN 1, THIOREDOXIN 2 IS PREFERRED OVER CC THIOREDOXIN 1. REQUIRED FOR FEMALE MEIOSIS AND EARLY EMBRYONIC CC DEVELOPMENT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY. CC -!- SIMILARITY: BELONGS TO THE THIOREDOXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L27072; AAA28937.1; -. DR EMBL; AE003433; AAF46019.1; -. DR EMBL; AY118929; AAM50789.1; ALT_SEQ. DR PIR; S47867; S47867. DR HSSP; P10599; 1ERV. DR FlyBase; FBgn0011761; dhd. DR GO; GO:0030508; F:thiol-disulfide exchange intermediate activity; IDA. DR InterPro; IPR006662; Thiored. DR InterPro; IPR006663; Thioredox_dom2. DR Pfam; PF00085; thiored; 1. DR PRINTS; PR00421; THIOREDOXIN. DR PROSITE; PS00194; THIOREDOXIN; 1. KW Redox-active center; Electron transport. FT DISULFID 31 34 REDOX-ACTIVE. FT MUTAGEN 31 31 C->S: LOSS OF FUNCTION. FT MUTAGEN 34 34 C->S: LOSS OF FUNCTION. SQ SEQUENCE 107 AA; 12384 MW; 6A716FD55690C53B CRC64; MASVRTMNDY HKRIEAADDK LIVLDFYATW CGPCKEMEST VKSLARKYSS KAVVLKIDVD KFEELTERYK VRSMPTFVFL RQNRRLASFA GADEHKLTNM MAKLVKA // ID THI2_DROME STANDARD; PRT; 114 AA. AC Q9V429; Q95SW4; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Thioredoxin 2 (DmTrx-2). GN TRX-2 OR CG31884/CG3864. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RA Seong K., Horiuchi N., Aigaki T.; RT "Charaterization of Drosophila thioredoxin."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX MEDLINE=22001321; PubMed=11877442; RA Bauer H., Kanzok S.M., Schirmer R.H.; RT "Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin RT peroxidase-1 from Drosophila melanogaster: isolation and RT characterization of a second thioredoxin in D. melanogaster and RT evidence for distinct biological functions of Trx-1 and Trx-2."; RL J. Biol. Chem. 277:17457-17463(2002). CC -!- FUNCTION: PARTICIPATES IN VARIOUS REDOX REACTIONS THROUGH THE CC REVERSIBLE OXIDATION OF ITS ACTIVE CENTER DITHIOL TO A DISULFIDE CC AND CATALYZES DITHIOL-DISULFIDE EXCHANGE REACTIONS. AS A REDUCING CC SUBSTRATE OF PEROXIREDOXIN 1, THIOREDOXIN 2 IS PREFERRED OVER CC THIOREDOXIN 1. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9V429-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q9V429-2; Sequence=VSP_006423; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: LARVAL STAGES. CC -!- SIMILARITY: BELONGS TO THE THIOREDOXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF220362; AAF37263.1; -. DR EMBL; AE003625; AAN10700.1; -. DR EMBL; AY060458; AAL25497.1; -. DR HSSP; P10599; 1ERV. DR FlyBase; FBgn0040070; Trx-2. DR GO; GO:0030508; F:thiol-disulfide exchange intermediate activity; IDA. DR GO; GO:0045454; P:cell redox homeostasis; IDA. DR InterPro; IPR006662; Thiored. DR InterPro; IPR006663; Thioredox_dom2. DR InterPro; IPR005746; Thioredoxin. DR Pfam; PF00085; thiored; 1. DR PRINTS; PR00421; THIOREDOXIN. DR TIGRFAMs; TIGR01068; thioredoxin; 1. DR PROSITE; PS00194; THIOREDOXIN; 1. KW Redox-active center; Electron transport; Alternative splicing. FT DISULFID 40 43 REDOX-ACTIVE (BY SIMILARITY). FT VARSPLIC 1 16 MMILLRDSTNLHFHLQ -> MVYQVKDK (in isoform FT Short). FT /FTId=VSP_006423. SQ SEQUENCE 114 AA; 12696 MW; D67E87151114C4CE CRC64; MMILLRDSTN LHFHLQADLD GQLTKASGKL VVLDFFATWC GPCKMISPKL VELSTQFADN VVVLKVDVDE CEDIAMEYNI SSMPTFVFLK NGVKVEEFAG ANAKRLEDVI KANI // ID THR_DROME STANDARD; PRT; 1209 AA. AC P42286; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Three rows protein. GN THR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S, and Oregon-R; RX MEDLINE=94138073; PubMed=8305737; RA D'Andrea R.J., Stratmann R., Lehner C.F., John U.P., Saint R.; RT "The three rows gene of Drosophila melanogaster encodes a novel RT protein that is required for chromosome disjunction during mitosis."; RL Mol. Biol. Cell 4:1161-1174(1993). CC -!- FUNCTION: REQUIRED SPECIFICALLY FOR CHROMOSOME DISJUNCTION DURING CC ALL MITOSES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03276; AAB60210.1; -. DR EMBL; S69585; AAB29824.1; -. DR PIR; A49440; A49440. DR FlyBase; FBgn0003701; thr. DR GO; GO:0007422; P:peripheral nervous system development; IMP. KW Mitosis. FT VARIANT 222 222 S -> T (IN OREGON-R). FT VARIANT 257 257 R -> K (IN OREGON-R). FT VARIANT 258 258 A -> T (IN OREGON-R). FT VARIANT 757 757 P -> L (IN OREGON-R). SQ SEQUENCE 1209 AA; 137847 MW; B4349FA66AA6E7F0 CRC64; MTQRQISLCA TLLVQLNESL FGKRSRSFFK SLSFLPSESL AKMFNALLML LASSTSSNLA NLFPECLSLT LALVQIDMFS PQSNQQMSLQ LLRMSKELFR QESNLCYALQ LMYYYIKLIF VREPTGDFKR TYIDLSSKFQ HFFEHKVASH AKEQWLADFL VAIQLLQVLI HQSNSKLQSP FQIFWQQFDG ESSPEIYTAH FQLLQTCASL AVNITRSPLG CSCSHEACKS VRRHCILAYG LCALDAYINW KPAAEQRANV SPHKPLLGVV KYSMDVAKTM KCLGPTSVEI IKLVRQLTYV ADQVTCPEQM SVLLPLLEPL QKLRPLVADQ DMSSLLRRLF KASSHCGDSN IACRIQASYL ASITNPARLR SQVCLYYHNL GKKGTEIKRC VYEWHESTPL PFPLTPDQKK QLYDTDFFAL LHYLRSPSTA HMESLIRCRT SDYHLVLLAR QMRKDDSISK KCIEVHDKLR QQRSLSRMDN LCLGHASVGL LLDALEAQKT KVSTKEITEN MFEELLLSKN LWQMNIQREQ RLVNYASEAI SAFSNFFDRA DQEPLSANET SIDWEALIDD AIATANALSS MGYQSEEDDA WLLLLRMGRL LEDRFTYLRA LNHFLSQNEV SSRLNLKLGE EVEVAEELLD DLWPQLKNGK FFKRQQTTVM LCFCHLASYY ARMECYSHAQ LLLLHVEQLR EEFPERQGKS DIVLLTLQTV RFRIGYQQRK PTNCRLPTPL RQLDILLDNV RSFCNLSSLD GGSLQLPLST LVRESTESSA NRLSERLSFS NIALHLVLQS GLALRAIEVF LAWLWTNLQM ESFDKAQSKL RLIEHCLGIK QLNPTSRPEK EAIKDVAISD LASNMHLLQL VEPIRKQQLL NMASPNLLKM RPHSPNPQLD LDRYITLDVA PANLRENSQL QCLYFVTGCL HARLRFLQRN SEQLEEFYGR AHNWMQEKPP MSSALYPMLH AQQLYHLNYL RFARKHVEAI STAQLGLKMR SRAVDINFEY NFLAQLKTAQ LELKPVGQDK PQVKILRRAL VFNHSPEDKK RTATGSVSAV KNTASKVKQS AKKAPRFRIY EELELRPPSA TSCSSSGGSG TENTPPSDHV DLNACQAIEI SDDDDSPLVS TKKTQPKSRE KAKPKATSKA CKVLTLDNSL EIVETPTITT STRSTRARLR QPVETPKTAT LSSKRTRRQV LEAQAPETES ISTRTRHRH // ID TID_DROME STANDARD; PRT; 520 AA. AC Q27237; O02528; O02529; O02549; Q24554; Q27259; Q8T9A7; Q9W1K7; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tumorous imaginal discs protein, mitochondrial precursor DE (Lethal(2)tumorous imaginal discs protein) (TID56) (TID50). GN L(2)TID OR CG5504. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Oregon-R, Harvich, bIf, and apxo; RX MEDLINE=98038975; PubMed=9373138; RA Kurzik-Dumke U., Kaymer M., Gundacker D., Debes A., Labitzke K.; RT "Gene within gene configuration and expression of the Drosophila RT melanogaster genes lethal(2) neighbour of tid [l(2)not] and lethal(2) RT relative of tid."; RL Gene 200:45-58(1997). RN [2] RP SEQUENCE FROM N.A. (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=95277995; PubMed=7758246; RA Kurzik-Dumke U., Gundacker D., Rentrop M., Gateff E.; RT "Tumor suppression in Drosophila is causally related to the function RT of the lethal(2) tumorous imaginal discs gene, a dnaJ homolog."; RL Dev. Genet. 16:64-76(1995). RN [3] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Oregon-2; RA Gundacker S., Neubhuer M., Kurzik-Dumke U.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [7] RP CHARACTERIZATION. RX MEDLINE=98244577; PubMed=9585178; RA Kurzik-Dumke U., Debes A., Kaymer M., Dienes P.; RT "Mitochondrial localization and temporal expression of the Drosophila RT melanogaster DnaJ homologous tumor suppressor Tid50."; RL Cell Stress Chaperones 3:12-27(1998). CC -!- FUNCTION: MAY ACT AS A TUMOR SUPPRESSOR IN LARVAL IMAGINAL DISKS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL OUTER MEMBRANE-ASSOCIATED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q27237-1; Sequence=Displayed; CC Name=B; CC IsoId=Q27237-2; Sequence=VSP_008308, VSP_008309; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED THROUGHOUT EMBRYONIC CC DEVELOPMENT. IN LARVAE, EXPRESSION IS SEEN IN SENSORY ORGANS, CC GOPPLET CELLS, GONADS, IMAGINAL DISKS, PROVENTRICULUS, FAT BODY, CC HEMATOPOIETIC ORGAN, MIDGUT, MALPIGHIAN TUBULES AND RING GLAND. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT DEVELOPMENT, HIGHEST CC EXPRESSION IN FIRST AND SECOND INSTAR LARVAE AND ADULTS. CC -!- MISCELLANEOUS: IN STRAINS HARVICH AND APXO, THERE ARE 2 IDENTICAL CC GENES WHICH CODE FOR L(2)TID PROTEIN. CC -!- SIMILARITY: CONTAINS 1 J DOMAIN. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95241; CAA64528.1; -. DR EMBL; X95242; CAA64531.1; -. DR EMBL; X95247; CAA64536.1; -. DR EMBL; X95249; CAA64538.1; -. DR EMBL; X95251; CAA64540.1; -. DR EMBL; Y10074; CAA71163.1; -. DR EMBL; Y10074; CAA71164.1; -. DR EMBL; X77822; CAA54837.1; -. DR EMBL; X98094; CAA66720.1; -. DR EMBL; AE003461; AAF47051.2; ALT_SEQ. DR EMBL; AY069853; AAL39998.1; -. DR PIR; S42091; S42091. DR HSSP; P08622; 1XBL. DR FlyBase; FBgn0002174; l(2)tid. DR GO; GO:0005739; C:mitochondrion; IDA. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001305; DnaJ_CXXCXGXG. DR InterPro; IPR001623; DnaJ_N. DR InterPro; IPR008971; HSP40_DnaJ_pep. DR InterPro; IPR003095; Hsp_DnaJ. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR Pfam; PF00684; DnaJ_CXXCXGXG; 1. DR PRINTS; PR00625; DNAJPROTEIN. DR SMART; SM00271; DnaJ; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS00637; DNAJ_CXXCXGXG; FALSE_NEG. KW Developmental protein; Chaperone; Mitochondrion; Outer membrane; KW Repeat; Transit peptide; Zinc; Metal-binding; Polymorphism; KW Alternative splicing. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 520 TUMOROUS IMAGINAL DISCS PROTEIN. FT DOMAIN 65 130 J-DOMAIN. FT REPEAT 227 234 CXXCXGXG MOTIF (APPROXIMATE). FT REPEAT 244 251 CXXCXGXG MOTIF. FT REPEAT 266 273 CXXCXGXG MOTIF (APPROXIMATE). FT REPEAT 280 287 CXXCXGXG MOTIF. FT METAL 227 227 ZINC 1 (BY SIMILARITY). FT METAL 230 230 ZINC 1 (BY SIMILARITY). FT METAL 244 244 ZINC 2 (BY SIMILARITY). FT METAL 247 247 ZINC 2 (BY SIMILARITY). FT METAL 266 266 ZINC 2 (BY SIMILARITY). FT METAL 269 269 ZINC 2 (BY SIMILARITY). FT METAL 280 280 ZINC 1 (BY SIMILARITY). FT METAL 283 283 ZINC 1 (BY SIMILARITY). FT VARSPLIC 446 447 AG -> SE (in isoform B). FT /FTId=VSP_008308. FT VARSPLIC 448 520 Missing (in isoform B). FT /FTId=VSP_008309. FT VARIANT 28 28 T -> A (in strain apxo). FT VARIANT 47 48 Missing (in strains Oregon-2 and Oregon- FT R). FT VARIANT 222 222 N -> I (in strain apxo). FT VARIANT 286 287 Missing (in strain apxo). FT VARIANT 415 415 A -> D (in strain apxo). FT VARIANT 478 478 E -> K (in strains bIf and Berkeley). FT VARIANT 489 489 K -> E (IN STRAINS bIf and Berkeley). FT CONFLICT 286 286 K -> M (IN REF. 1, 2, 3; CAA64528 AND 6). FT CONFLICT 341 341 A -> V (IN REF. 1, 2, 3; CAA64528 AND 6). SQ SEQUENCE 520 AA; 56137 MW; 1904B878F386FB1A CRC64; MMISCKKLFV FRQLPAVRRC LAAAAFSTPR ATSYRILSSA GSGSTRADAP QVRRLHTTRD LLAKDYYATL GVAKNANGKD IKKAYYQLAK KYHPDTNKED PDAGRKFQEV SEAYEVLSDE QKRREYDTYG QTAENIGRQG GGFPGGGAGG FGPEGFSQSW QFRSSIDPEE LFRKIFGEGN FRTNSFDDFA DSKFGFGQAQ EMVMDLTFAQ AARGVNKDVN VNVVDQCPKC AGTKCEPGTK PGRCQYCNGT GFETVSTGPF VMRSTCRYCQ GTRQHIKYPC SECEGKGRTV QRRKVTVPVP AGIENGQTVR MQVGSKELFV TFRVERSDYF RREGADVHTD AAISLAQAVL GGTVRVQGVY EDQWINVEPG TSSHHKIMLR GKGLKRVNAH GHGDHYVHVK ITVPSAKKLD KKRLALIEAY AELEEDTPGQ IHGIANRKDG SKQATAGASE EPGAGAAAKA SAAAAGSGAS KPGPGAEESE GKDQWTDNKK TKAKEGGGSG SGQGDGGGGG FISKIKSMFN // ID TIMP_DROME STANDARD; PRT; 210 AA. AC Q9VH14; O96747; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tissue inhibitor of metalloproteases precursor. GN TIMP OR CG6281. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=99216424; PubMed=10198170; RA Pohar N., Godenschwege T.A., Buchner E.; RT "Invertebrate tissue inhibitor of metalloproteinase: structure and RT nested gene organization within the synapsin locus is conserved from RT Drosophila to human."; RL Genomics 57:293-296(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COMPLEXES WITH METALLOPROTEINASES AND IRREVERSIBLY CC INACTIVATES THEM (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: SECRETED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE TIMP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ010067; CAA08989.1; -. DR EMBL; AE003686; AAF54507.1; -. DR EMBL; AY069211; AAL39356.1; -. DR FlyBase; FBgn0025879; Timp. DR GO; GO:0005576; C:extracellular; ISS. DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS. DR InterPro; IPR001820; TIMP. DR InterPro; IPR008993; TIMP_like. DR Pfam; PF00965; TIMP; 1. DR SMART; SM00206; NTR; 1. DR PROSITE; PS00288; TIMP; FALSE_NEG. KW Metalloprotease inhibitor; Signal. FT SIGNAL 1 27 POTENTIAL. FT CHAIN 28 210 TISSUE INHIBITOR OF METALLOPROTEASES. FT DISULFID 28 96 BY SIMILARITY. FT DISULFID 30 118 BY SIMILARITY. FT DISULFID 145 195 BY SIMILARITY. FT DISULFID 150 155 BY SIMILARITY. FT CONFLICT 76 76 S -> P (IN REF. 1). SQ SEQUENCE 210 AA; 23980 MW; E7F4A7845CB69BD0 CRC64; MDLRKHLGLL TLLLVAVFAF YGRPADACSC MPSHPQTHFA QADYVVQLRV LRKSDTIEPG RTTYKVHIKR TYKATSEARR MLRDGRLSTP QDDAMCGINL DLGKVYIVAG RMPTLNICSY YKEYTRMTIT ERHGFSGGYA KATNCTVTPC FGERCFKGRN YADTCKWSPF GKCETNYSAC MPHKVQTVNG VISRCRWRRT QLYRKCMSNP // ID TIM_DROME STANDARD; PRT; 1421 AA. AC P49021; O44380; Q8I037; Q95U67; Q9VQR6; Q9VQR7; DT 01-FEB-1996 (Rel. 33, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Timeless protein. GN TIM OR CG3234. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=96055118; PubMed=7481771; RA Myers M.P., Wager-Smith K., Wesley C.S., Young M.W., Sehgal A.; RT "Positional cloning and sequence analysis of the Drosophila clock RT gene, timeless."; RL Science 270:805-808(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORM B). RX MEDLINE=98033379; PubMed=9365248; RA Myers M.P., Rothenfluh A., Chang M., Young M.W.; RT "Comparison of chromosomal DNA composing timeless in Drosophila RT melanogaster and D. virilis suggests a new conserved structure for the RT TIMELESS protein."; RL Nucleic Acids Res. 25:4710-4714(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 8-53 FROM N.A., AND ALTERNATIVE INITIATION. RC STRAIN=Canton-S, CO-TG14, CO-TG20, PERS, PER+, and PER01; RX MEDLINE=97169240; PubMed=9016581; RA Rosato E., Trevisan A., Sandrelli F., Zordan M., Kyriacou C.P., RA Costa R.; RT "Conceptual translation of timeless reveals alternative initiating RT methionines in Drosophila."; RL Nucleic Acids Res. 25:455-458(1997). RN [6] RP SEQUENCE OF 57-1421 FROM N.A. (ISOFORM C). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [7] RP SEQUENCE OF 243-303 FROM N.A. RX MEDLINE=98186271; PubMed=9504927; RA Ousley A., Zafarullah K., Chen Y., Emerson M., Hickman L., Sehgal A.; RT "Conserved regions of the timeless (tim) clock gene in Drosophila RT analyzed through phylogenetic and functional studies."; RL Genetics 148:815-825(1998). RN [8] RP INTERACTION WITH PER. RX MEDLINE=96055120; PubMed=7481773; RA Gekakis N., Saez L., Delahaye-Brown A.M., Myers M.P., Sehgal A., RA Young M.W., Weitz C.J.; RT "Isolation of timeless by PER protein interaction: defective RT interaction between timeless protein and long-period mutant PERL."; RL Science 270:811-815(1995). CC -!- FUNCTION: REQUIRED FOR THE PRODUCTION OF CIRCADIAN RHYTHMS. THE CC BIOLOGICAL CYCLE DEPENDS ON THE RHYTHMIC FORMATION AND NUCLEAR CC LOCALIZATION OF THE TIM-PER COMPLEX. LIGHT INDUCES THE DEGRADATION CC OF TIM, WHICH PROMOTES ELIMINATION OF PER. NUCLEAR ACTIVITY OF THE CC HETERODIMER COORDINATIVELY REGULATES PER AND TIM TRANSCRIPTION CC THROUGH A NEGATIVE FEEDBACK LOOP. BEHAVES AS A NEGATIVE ELEMENT IN CC CIRCADIAN TRANSCRIPTIONAL LOOP. DOES NOT APPEAR TO BIND DNA, CC SUGGESTING INDIRECT TRANSCRIPTIONAL INHIBITION. CC -!- SUBUNIT: FORMS A HETERODIMER WITH PERIOD (PER); THE COMPLEX THEN CC TRANSLOCATES INTO THE NUCLEUS. CC -!- SUBCELLULAR LOCATION: NUCLEAR AT SPECIFIC PERIODS OF THE DAY. CC FIRST ACCUMULATES IN THE PERINUCLEAR REGION ABOUT ONE HOUR BEFORE CC TRANSLOCATION INTO THE NUCLEUS. INTERACTION WITH PER IS REQUIRED CC FOR NUCLEAR LOCALIZATION. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=B; CC IsoId=P49021-1; Sequence=Displayed; CC Note=An additional isoform is produced by alternative initiation CC at Met-24 of isoform B in strains with a premature STOP codon CC shortly after Met-1; CC Name=A; CC IsoId=P49021-2; Sequence=VSP_004457; CC Note=Apparently not implicated in circadian rhythms causing a CC long-period phenotype and arrhythmia; CC Name=C; CC IsoId=P49021-3; Sequence=VSP_007693, VSP_007694; CC Note=No experimental confirmation available; CC Event=Alternative initiation; CC Comment=2 isoforms are produced by alternative initiation at CC Met-1 and Met-24 of isoform B in strains with a premature STOP CC codon shortly after the Met-1; CC -!- TISSUE SPECIFICITY: ISOFORM B IS EXPRESSED IN THE HEAD. CC -!- PTM: PHOSPHORYLATED WITH A CIRCADIAN RHYTHMICITY. CC -!- POLYMORPHISM: A POLYMORPHISM IDENTIFIED IN SOME STRAINS GENERATES CC A PREMATURE STOP CODON SHORTLY AFTER MET-1; IN THIS CASE MET-24 IS CC THE START SITE. CC -!- SIMILARITY: CONTAINS 1 PAS (PER-ARNT-SIM) DIMERIZATION DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37018; AAC46920.1; -. DR EMBL; AF032401; AAB94890.1; ALT_INIT. DR EMBL; AF032400; AAB94890.1; JOINED. DR EMBL; AE003579; AAF51097.1; -. DR EMBL; AE003579; AAF51098.3; ALT_INIT. DR EMBL; AE003579; AAN10372.2; -. DR EMBL; Y09930; -; NOT_ANNOTATED_CDS. DR EMBL; Y09931; -; NOT_ANNOTATED_CDS. DR EMBL; Y09932; -; NOT_ANNOTATED_CDS. DR EMBL; Y09933; -; NOT_ANNOTATED_CDS. DR EMBL; Y09934; -; NOT_ANNOTATED_CDS. DR EMBL; Y09935; -; NOT_ANNOTATED_CDS. DR EMBL; AY058278; AAL13507.1; -. DR EMBL; BT001424; AAN71179.1; -. DR EMBL; AF038501; AAB94929.1; -. DR FlyBase; FBgn0014396; tim. DR GO; GO:0005737; C:cytoplasm; NAS. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0008062; P:eclosion rhythm; NAS. DR GO; GO:0045475; P:locomotor rhythm; NAS. DR GO; GO:0007617; P:mating behavior; IMP. DR GO; GO:0000122; P:negative regulation of transcription from P...; NAS. DR GO; GO:0006606; P:protein-nucleus import; NAS. DR GO; GO:0045187; P:regulation of sleep; IMP. DR InterPro; IPR006906; Timeless. DR Pfam; PF04821; TIMELESS; 1. KW Biological rhythms; Nuclear protein; Repeat; Phosphorylation; KW Alternative initiation; Alternative splicing; Polymorphism. FT CHAIN 1 1421 TIMELESS PROTEIN, ISOFORM B. FT CHAIN 24 1421 TIMELESS PROTEIN, ISOFORM IN STRAINS WITH FT A PREMATURE STOP CODON. FT INIT_MET 24 24 FOR ISOFORM IN STRAINS WITH A PREMATURE FT STOP CODON SHORTLY AFTER THE MET-1. FT REPEAT 536 610 PAS-1. FT REPEAT 747 946 PAS-2. FT DOMAIN 260 291 NECESSARY FOR NORMAL CIRCADIAN RHYTHM. FT DOMAIN 383 412 ASP/GLU-RICH (ACIDIC). FT DOMAIN 573 583 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 184 187 POLY-LEU. FT DOMAIN 405 412 POLY-GLU. FT DOMAIN 455 460 POLY-PRO. FT DOMAIN 1309 1312 POLY-SER. FT DOMAIN 1333 1336 POLY-GLY. FT VARSPLIC 260 291 Missing (in isoform A). FT /FTId=VSP_004457. FT VARSPLIC 914 914 C -> W (in isoform C). FT /FTId=VSP_007693. FT VARSPLIC 915 1421 Missing (in isoform C). FT /FTId=VSP_007694. FT CONFLICT 1256 1256 V -> I (IN REF. 4). SQ SEQUENCE 1421 AA; 159200 MW; 12C24FF4E0833966 CRC64; MSRVRQLHNH IWNNQNFDKV KSVMDWLLAT PQLYSAFSSL GCLEGDTYVV NPNALAILEE INYKLTYEDQ TLRTFRRAIG FGQNVRSDLI PLLENAKDDA VLESVIRILV NLTVPVECLF SVDVMYRTDV GRHTIFELNK LLYTSKEAFT EARSTKSVVE YMKHILESDP KLSPHKCDQI NNCLLLLRNI LHIPETHAHC VMPMMQSMPH GISMQNTILW NLFIQSIDKL LLYLMTCPQR AFWGVTMVQL IALIYKDQHV STLQKLLSLW FEASLSESSE DNESNTSPPK QGSGDSSPML TSDPTSDSSD NGSNGRGMGG GMREGTAATL QEVSRKGQEY QNAMARVPAD KPDGSEEASD MTGNDSEQPG SPEQSQPAGE SMDDGDYEDQ RHRQLNEHGE EDEDEDEVEE EEYLQLGPAS EPLNLTQQPA DKVNNTTNPT SSAPQGCLGN EPFKPPPPLP VRASTSAHAQ MQKFNESSYA SHVSAVKLGQ KSPHAGQLQL TKGKCCPQKR ECPSSQSELS DCGYGTQVEN QESISTSSND DDGPQGKPQH QKPPCNTKPR NKPRTIMSPM DKKELRRKKL VKRSKSSLIN MKGLVQHTPT DDDISNLLKE FTVDFLLKGY SYLVEELHMQ LLSNAKVPID TSHFFWLVTY FLKFAAQLEL DMEHIDTILT YDVLSYLTYE GVSLCEQLEL NARQEGSDLK PYLRRMHLVV TAIREFLQAI DTYNKVTHLN EDDKAHLRQL QLQISEMSDL RCLFVLLLRR FNPSIHSKQY LQDLVVTNHI LLLILDSSAK LGGCQTIRLS EHITQFATLE VMHYYGILLE DFNNNGEFVN DCIFTMMHHI GGDLGQIGVL FQPIILKTYS RIWEADYELC DDWSDLIEYV IHKFMNTPPK SPLTIPTTSL TEMTKEHNQE HTVCSWSQEE MDTLYWYYVQ SKKNNDIVGK IVKLFSNNGN KLKTRISIIQ QLLQQDIITL LEYDDLMKFE DAEYQRTLLT TPTSATTESG IEIKECAYGK PSDDVQILLD LIIKENKAQH LLWLQRILIE CCFVKLTLRS GLKVPEGDHI MEPVAYHCIC KQKSIPVVQW NNEQSTTMLY QPFVLLLHKL GIQLPADAGS IFARIPDYWT PETMYGLAKK LGPLDKLNLK FDASELEDAT ASSPSRYHHT GPRNSLSSVS SLDVDLGDTE ELALIPEVDA AVEKAHAMAS TPSPSEIFAV PKTKHCNSII RYTPDPTPPV PNWLQLVMRS KCNHRTGPSG DPSDCVGSSS TTVDDEGFGK SISAATSQAA STSMSTVNPT TTLSLNMLNT FMGSHNENSS SSGCGGTVSS LSMVALMSTG AAGGGGNTSG LEMDVDASMK SSFERLEVNG SHFSRANNLD QEYSAMVASV YEKEKELNSD NVSLASDLTR MYVSDEDDRL ERTEIRVPHY H // ID TIN1_DROME STANDARD; PRT; 167 AA. AC Q9W0Y1; Q95T30; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Troponin C-akin-1 protein. GN TINA-1 OR CG2803. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 6-167 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [3] RP TISSUE SPECIFICITY. RX MEDLINE=22283639; PubMed=12397110; RA Lovato T.L., Nguyen T.P., Molina M.R., Cripps R.M.; RT "The Hox gene abdominal-A specifies heart cell fate in the Drosophila RT dorsal vessel."; RL Development 129:5019-5027(2002). CC -!- TISSUE SPECIFICITY: IN EMBRYOS, EXPRESSION IS SEEN IN HEART CELLS CC OF THE DORSAL VESSEL AND HINDGUT VISCERAL MESODERM. CC -!- SIMILARITY: BELONGS TO THE UPF0131 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003465; AAF47298.1; -. DR EMBL; AY060353; AAL25392.1; ALT_INIT. DR FlyBase; FBgn0035083; Tina-1. DR InterPro; IPR005347; UPF0131. DR Pfam; PF03674; UPF0131; 1. SQ SEQUENCE 167 AA; 19056 MW; 8FCDE6E575950F5F CRC64; MGQAKKVSSA LSKLFVYGAL KYGQPSNSIL ASSGNGFAKF WCKATTTQKL PLVIATRYNI PFLLNKPGVG YYVTGEIYEV DDRMLNSLDN LEDCEEIYTR EMHDMNIGVG EGTVPCWVYL LQKYPENLLS LRYLSSYENS TTHPYIMRHR RTHKHPAQDD LTYEAQN // ID TIPE_DROME STANDARD; PRT; 452 AA. AC P48613; Q9VZG6; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE TipE protein (Temperature-induced paralytic E). GN TIPE OR CG1232. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=96016095; PubMed=7553842; RA Feng G., Deak P., Chopra M., Hall L.M.; RT "Cloning and functional analysis of TipE, a novel membrane protein RT that enhances Drosophila para sodium channel function."; RL Cell 82:1001-1011(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ENHANCES PARA SODIUM CHANNEL FUNCTION. REQUIRED DURING CC PUPAL DEVELOPMENT TO RESCUE ADULT PARALYSIS AND ALSO PROTECTS CC ADULT FLYS AGAINST HEAT-INDUCED LETHALITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: PREFERENTIALLY EXPRESSED IN THE CENTRAL CC NERVOUS SYSTEM OF DEVELOPING EMBRYOS. THE LONGER TIPE FORMS CC ARE FOUND PREDOMINANTLY IN HEADS AND LEGS, THE SHORT FORM IN CC THE BODY REGION. CC -!- DEVELOPMENTAL STAGE: EXPRESSED WEAKLY IN MIDDLE TO LATE EMBRYOS, CC ABSENT IN LARVAE AND IS MOST ABUNDANTLY EXPRESSED IN MIDDLE TO CC LATE PUPAL STAGES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U27561; AAC48307.1; -. DR EMBL; AE003480; AAF47857.1; -. DR EMBL; AY060317; AAL25356.1; -. DR PIR; A57217; A57217. DR FlyBase; FBgn0003710; tipE. DR GO; GO:0005886; C:plasma membrane; IDA. DR GO; GO:0006814; P:sodium ion transport; NAS. KW Transmembrane; Glycoprotein. FT DOMAIN 1 20 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 21 41 POTENTIAL. FT DOMAIN 42 274 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 275 295 POTENTIAL. FT DOMAIN 296 452 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 72 72 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 102 102 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 108 108 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 212 212 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 237 237 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 452 AA; 50190 MW; 1E81443B5E9ACF24 CRC64; MGDEQDKRTG KEKLLFYTTA FFILLGTFSL FAFLFLVPFV IEPAFTTIFM QFEEVPALCE TYDTEIYYGA KNCSWSSCRE GCTKDIYTCT QIRVNYRLNL YNFTDEFNFT EYHINLKEAE RILPPVKRTD RYERALRSDY EYDNLGGGTG LDIDLGAGRM EQLNFGDADG SNGYLIEDSE DTRGLSASGT LISDERRPFD EISELNEGLM GNRSMYYYVG ARLFPNVKGC GYPPMLNCTI WLKRYTKIGM KFPCYYSKVD PSLVISDLDY WQNTLNLVYS MAIPIPSFII SVIYLTYAYF KIYNEDEETA PLDKNAEDMD IDDIDAVDDS DGAVLADNVA GSQIINMDST TNDSCLEGVL PNGGPGMTAS ISQGGSVTTP GPYIAQSPAG SQMTPNSEIN SFGHQLKVQM ADELSRDSLE NGAISTSNSV QGNLSKTMTT SISTPPGPTA AV // ID TIPT_DROME STANDARD; PRT; 1024 AA. AC Q9U3V5; Q95SG6; Q9V9P4; DT 10-OCT-2003 (Rel. 42, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Tiptop protein. GN TIPTOP OR CG12630. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Fasano L., Nhouyvanisvong M., Caubit X., Kerridge S., Jacq B., RA Vola C.; RT "Teashirt-related paralog."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE OF 1-18 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE MALPIGHIAN TUBULES AND CC STOMATOGASTRIC NERVOUS SYSTEM. CC -!- SIMILARITY: CONTAINS 4 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF219383; AAF23183.1; ALT_INIT. DR EMBL; AE003782; AAF57242.2; ALT_INIT. DR EMBL; AY060807; AAL28355.1; ALT_SEQ. DR FlyBase; FBgn0028979; tiptop. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 4. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. KW Transcription regulation; Zinc-finger; Metal-binding; Repeat; KW DNA-binding; Nuclear protein. FT ZN_FING 317 341 C2H2-TYPE 1. FT ZN_FING 426 450 C2H2-TYPE 2. FT ZN_FING 499 523 C2H2-TYPE 3. FT ZN_FING 926 949 C2H2-TYPE 4. SQ SEQUENCE 1024 AA; 108363 MW; 93888A08467C4F5C CRC64; MMLHEAVMLE IYRQALSASE LTSPRCQSRD SNTSAGAGAG MADVRCPSNE SHCSANDRLT PAATPTLTPT EATISPNSVG LPLTATLPPA AAVALLPPQS AAMAAYLAAA QQNHLLLTNP LAAAASLVQH ATQQAVVEGE VESPALDFSR KRPKSHGDDD QEEDQEQDQE QEQEQEPDHD VQCDNGPLDL SVSTGKRQES VSPPARKIPR SISADYKSPL PPGSWMPPIN PYLAAVAAKT GGLGYSKLAP SEASKALEKM TEMSRLETSP TAARSLGATS SVGAGVPAGA SSNSGGRHSA WQSHWLNKGA DTAKDVFKCV WCKQSFSTLA NLTAHMKETQ HCGVQIPSPL PTGGVGTPSA PPPTRLATSA SNSACSSSSS STSSSSNSSK SELNMLIKET MPLPRKLVRG QDVWLGKGAE QTRQILKCMW CGQSFRSLAE MTSHMQETQH YTNIISQEQI ISWKSGDERE RPTNTGVPST STAAPSSPSC TAPSVSAVLT CKVCDQAFGS LKELSTHMAQ KSHYKESPAP SASPPAAGTG NPKRGRQNRN EKRKKSLPVR KLLELERSGS NSSLDSALKP LRDFAAATKI TCEKCGSKIE TALFVEHIRK CLGESIPIPP RRSNAGVDRL PSPSLGLGAE KPPSVLNALE QLIEKSFESR TSRTMTHGGY SEAGTPLGAS ILKRLGIEDS SDYTKPLMDA QAMHLLRSSF ASRDRSASES SSASRVESSY TPDRQQATPH KSPDTPAPPP PPPPTIKAEP LEAEPLVGCD REGCSPRQQI QVKKEFSMEA CRESPRSVSK SPAPQTERSP PDNGSLLALN SMFDQLSGVE NSGNNNSGHC FNNNNSCSSV SAQKPKAHPL AALQKLCETT DPPSTGLRSA SSAGSSTASA TLPSANGNDL VAFSWACNEA VLSASNGGSA GDSSIIKCSY CDTPFASKGA YRHHLSKVHF VKDAGEDSPR LKSPAVQSPR SMPLASPRRS ASRSPATGSQ QPPPSPTISP YDESPQSKFL KYTELAKQLS SKNA // ID TIS1_DROME STANDARD; PRT; 437 AA. AC P47980; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE TIS11 protein (dTIS11). GN TIS11 OR TISCC1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95022644; PubMed=7936658; RA Ma Q., Wadleigh D., Chi T., Herschman H.; RT "The Drosophila TIS11 homologue encodes a developmentally controlled RT gene."; RL Oncogene 9:3329-3334(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=95129868; PubMed=7828883; RA Warbrick E., Glover D.; RT "A Drosophila melanogaster homolog of the TIS11 family of immediate RT early genes that can rescue a cdr1 cdc25 mutant strain of fission RT yeast."; RL Gene 151:243-246(1994). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 2 C3H1-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13397; AAA62666.1; -. DR EMBL; X81194; CAA57066.1; -. DR FlyBase; FBgn0011837; Tis11. DR InterPro; IPR000571; Znf_CCCH. DR Pfam; PF00642; zf-CCCH; 2. DR SMART; SM00356; ZnF_C3H1; 2. KW Nuclear protein; Repeat; Metal-binding; Zinc-finger; DNA-binding. FT ZN_FING 142 161 C3H1-TYPE 1. FT ZN_FING 180 199 C3H1-TYPE 2. FT DOMAIN 82 96 POLY-GLN. FT DOMAIN 242 252 POLY-SER. FT DOMAIN 253 259 POLY-GLY. FT DOMAIN 263 266 POLY-ASN. FT CONFLICT 15 15 S -> A (IN REF. 2). FT CONFLICT 96 98 QPP -> PA (IN REF. 2). SQ SEQUENCE 437 AA; 47320 MW; A28C55DA84DABA2F CRC64; MSADILQKSR EQDDSHYFER GDISKYVTMN DHLGDFDCNE VRKEIRMLLA HGANLDQQHQ QQPHRHHGGL TRTISQPAQL IQQQQQQHQQ QQQQQQPPVA SLVTITENLG NMNLHRKLER TQSEPLPPQQ PMNTSRYKTE LCRPFEEAGE CKYGEKCQFA HGSHELRNVH RHPKYKTEYC RTFHSVGFCP YGPRCHFVHN ADEARAQQAA QAAKSSTQSQ SQSQQSSSQN FSPKSNQSSN QSSNSSSSSS SSGGGGGGGN SINNNNGSQF YLPLSPPLSM STGSDRESPT GSLSLSPTNS LTSFPFHDAL QHGYLASNGA KSNSSASSTS SASGMGLGMS MGIGQGMIIG QGLGMGHHGP ATPPESPNVP ISPVHTPPPY DVVVSGSGAG NNSVGSKQLL QKSVSTPMQQ EDTPRLPVFN RLSSGVEAYQ QQSNLGL // ID TKR_DROME STANDARD; PRT; 753 AA. AC P14083; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Protein TKR. GN TKR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88112827; PubMed=3428600; RA Haller J., Cote S., Broenner G., Jaeckle H.; RT "Dorsal and neural expression of a tyrosine kinase-related Drosophila RT gene during embryonic development."; RL Genes Dev. 1:862-867(1987). CC -!- FUNCTION: POSSIBLE REGULATORY ROLE DURING DEVELOPMENT. CC -!- CAUTION: WAS ORIGINALLY THOUGHT TO BE A KINASE ON THE BASIS OF CC WEAK AND NON-SIGNIFICATIVE SIMILARITIES. DR PIR; A27041; A27041. DR FlyBase; FBgn0003715; Tkr. DR InterPro; IPR007889; HTH_psq. DR Pfam; PF05225; HTH_psq; 1. FT DOMAIN 143 151 POLY-ASP. FT DOMAIN 153 157 POLY-GLU. FT DOMAIN 174 183 POLY-ALA. FT DOMAIN 221 224 POLY-ASN. FT DOMAIN 297 306 POLY-ALA. FT DOMAIN 325 332 POLY-ALA. FT DOMAIN 709 712 POLY-ALA. SQ SEQUENCE 753 AA; 81021 MW; F98D3272A7DDBE5E CRC64; MPSARLFGNA SSAIAALGLR RKREQESDRD LESDQELGGS SPMPRRKQAR PRRRSGHVPH DFTLNKTDAE SLQTVIKHEL LERAERDQEE APDRDNSQGE AEKISSSPAK TLVERAKEQK SMKQEGSNQP SSLNENHHQL ELDDEDDDDQ DHEEEEEQDI EELIHTTNEL RRQAAAAAAN AAAMSPNPSP CLSDGPEDLC TTKKGKELIS GPSSSADCES NNNNSSKLQD NNQRIMLSLK DIRQLNANPN PTAIHTPTSC SGGNNGLLTF PPPGLRPPGL PDSPPCHMEA LEAQMHAAAA AAVAAAGSGE HPFHHMEHEM EMSLAAAAAA AAMHQREPRD PRDGRDHNAF ASNLLGPMGM PPFGGHNGGH PGNSGPGNGC PGQAAHERLE EMSNRLSKEL GKEFGKEFGK EFGPAPSMSL QGPFNAPDGP PHPPSPLPFP GMSSAMTLTP PHMFGLDSPL GLFPPGIDPG KLYNPLMEMS DPRDMPGGPP PFLKKKMPRP KGQHSAPRGG PPRSWTNTEL TEALQHVWNK KMTTSQASRI FGIPYNSLLM YVRGKYGKSL KLEQLRKDCI SGPPIEMLQM GIGGGSGGST KNEKSKERKE KEKDKNSMSS NGSGGSANSQ GGAPTSGSGP MQHSGELGPM GQLDLDLGLP LGPPGGPRSN SSEPDLLSAP NALFNPFNPQ GFYPDFSGGF PGLPLSMLNL LPPAERHHAA AAMHHLGVRW MRTASLLDRS SPLPWTKTTQ VLEYRSRWST VGR // ID TLD_DROME STANDARD; PRT; 1057 AA. AC P25723; Q9VC46; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dorsal-ventral patterning tolloid protein precursor (EC 3.4.24.-). GN TLD OR CG6868. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92034970; PubMed=1840509; RA Shimell M.J., Ferguson E.L., Childs S.R., O'Connor M.B.; RT "The Drosophila dorsal-ventral patterning gene tolloid is related to RT human bone morphogenetic protein 1."; RL Cell 67:469-481(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95324373; PubMed=7600963; RA Finelli A.L., Bossie C.A., Xie T., Padgett R.W.; RT "Mutational analysis of the Drosophila tolloid gene, a human BMP-1 RT homolog."; RL Development 120:861-870(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR NORMAL DORSAL DEVELOPMENT. TLD MAY INTERACT CC PHYSICALLY WITH DPP-C PROTEIN. CC -!- MISCELLANEOUS: MUTATIONS IN TLD GENE LEAD TO A PARTIAL CC TRANSFORMATION OF DORSAL ECTODERM INTO VENTRAL ECTODERM. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M12A. CC -!- SIMILARITY: CONTAINS 2 EGF-LIKE DOMAINS. CC -!- SIMILARITY: CONTAINS 5 CUB DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M76976; AAA28491.1; -. DR EMBL; U04239; AAC46482.1; -. DR EMBL; AE003749; AAF56329.1; -. DR PIR; A39288; A39288. DR HSSP; P00742; 1HCG. DR MEROPS; M12.010; -. DR FlyBase; FBgn0003719; tld. DR GO; GO:0004222; F:metalloendopeptidase activity; NAS. DR GO; GO:0007378; P:amnioserosa formation; NAS. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR000859; CUB. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR006026; Peptidase_M. DR InterPro; IPR001506; Peptidase_M12A. DR Pfam; PF01400; Astacin; 1. DR Pfam; PF00431; CUB; 5. DR Pfam; PF00008; EGF; 2. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00042; CUB; 5. DR SMART; SM00179; EGF_CA; 2. DR SMART; SM00235; ZnMc; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 2. DR PROSITE; PS01180; CUB; 5. DR PROSITE; PS00022; EGF_1; FALSE_NEG. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS01187; EGF_CA; 2. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW Developmental protein; Hydrolase; Metalloprotease; Zinc; Glycoprotein; KW EGF-like domain; Calcium; Signal; Repeat; Zymogen. FT SIGNAL 1 27 POTENTIAL. FT PROPEP 28 126 POTENTIAL. FT CHAIN 127 1057 DORSAL-VENTRAL PATTERNING TOLLOID FT PROTEIN. FT DOMAIN 127 329 METALLOPROTEASE. FT DOMAIN 330 467 CUB 1. FT DOMAIN 468 580 CUB 2. FT DOMAIN 581 621 EGF-LIKE 1, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 624 742 CUB 3. FT DOMAIN 743 783 EGF-LIKE 2, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 787 899 CUB 4. FT DOMAIN 900 1016 CUB 5. FT METAL 221 221 ZINC (CATALYTIC) (BY SIMILARITY). FT ACT_SITE 222 222 BY SIMILARITY. FT METAL 225 225 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 231 231 ZINC (CATALYTIC) (BY SIMILARITY). FT SITE 235 237 CELL ATTACHMENT SITE (POTENTIAL). FT SITE 315 317 CELL ATTACHMENT SITE (POTENTIAL). FT DISULFID 330 380 BY SIMILARITY. FT DISULFID 407 429 BY SIMILARITY. FT DISULFID 468 495 BY SIMILARITY. FT DISULFID 522 544 BY SIMILARITY. FT DISULFID 585 596 BY SIMILARITY. FT DISULFID 592 605 BY SIMILARITY. FT DISULFID 607 620 BY SIMILARITY. FT DISULFID 624 652 BY SIMILARITY. FT DISULFID 683 706 BY SIMILARITY. FT DISULFID 747 758 BY SIMILARITY. FT DISULFID 754 767 BY SIMILARITY. FT DISULFID 769 782 BY SIMILARITY. FT DISULFID 787 813 BY SIMILARITY. FT DISULFID 840 862 BY SIMILARITY. FT DISULFID 900 930 BY SIMILARITY. FT DISULFID 957 979 BY SIMILARITY. FT CARBOHYD 166 166 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 431 431 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 533 533 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 634 634 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 667 667 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 781 781 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 854 854 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 908 908 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1057 AA; 120575 MW; 76F4B5AEB7996FBA CRC64; MKAKLVVLSV GALWMMMFFL VDYAEGRRLS QLPESECDFD FKEQPEDFFG ILDSSLVPPK EPKDDIYQLK TTRQHSGRRR KQSHKSQNKA ALRLPPPFLW TDDAVDVLQH SHSPTLNGQP IQRRRRAVTV RKERTWDYGV IPYEIDTIFS GAHKALFKQA MRHWENFTCI KFVERDPNLH ANYIYFTVKN CGCCSFLGKN GNGRQPISIG RNCEKFGIII HELGHTIGFH HEHARGDRDK HIVINKGNIM RGQEYNFDVL SPEEVDLPLL PYDLNSIMHY AKNSFSKSPY LDTITPIGIP PGTHLELGQR KRLSRGDIVQ ANLLYKCASC GRTYQQNSGH IVSPHFIYSG NGVLSEFEGS GDAGEDPSAE SEFDASLTNC EWRITATNGE KVILHLQQLH LMSSDDCTQD YLEIRDGYWH KSPLVRRICG NVSGEVITTQ TSRMLLNYVN RNAAKGYRGF KARFEVVCGG DLKLTKDQSI DSPNYPMDYM PDKECVWRIT APDNHQVALK FQSFELEKHD GCAYDFVEIR DGNHSDSRLI GRFCGDKLPP NIKTRSNQMY IRFVSDSSVQ KLGFSAALML DVDECKFTDH GCQHLCINTL GSYQCGCRAG YELQANGKTC EDACGGVVDA TKSNGSLYSP SYPDVYPNSK QCVWEVVAPP NHAVFLNFSH FDLEGTRFHY TKCNYDYLII YSKMRDNRLK KIGIYCGHEL PPVVNSEQSI LRLEFYSDRT VQRSGFVAKF VIDVDECSMN NGGCQHRCRN TFGSYQCSCR NGYTLAENGH NCTETRCKFE ITTSYGVLQS PNYPEDYPRN IYCYWHFQTV LGHRIQLTFH DFEVESHQEC IYDYVAIYDG RSENSSTLGI YCGGREPYAV IASTNEMFMV LATDAGLQRK GFKATFVSEC GGYLRATNHS QTFYSHPRYG SRPYKRNMYC DWRIQADPES SVKIRFLHFE IEYSERCDYD YLEITEEGYS MNTIHGRFCG KHKPPIIISN SDTLLLRFQT DESNSLRGFA ISFMAVDPPE DSVGEDFDAV TPFPGYLKSM YSSETGSDHL LPPSRLI // ID TLL_DROME STANDARD; PRT; 452 AA. AC P18102; Q9VA33; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tailless protein. GN TLL OR NR2E2 OR CG1378. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90304905; PubMed=2364433; RA Pignoni F., Baldarelli R.M., Steingrimsson E., Diaz R.J., RA Patapoutian A., Merriam J.R., Lengyel J.A.; RT "The Drosophila gene tailless is expressed at the embryonic termini RT and is a member of the steroid receptor superfamily."; RL Cell 62:151-163(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93157371; PubMed=8430097; RA Liaw G.-J., Steingrimsson E., Pignoni F., Courey A.J., Lengyel J.A.; RT "Characterization of downstream elements in a Raf-1 pathway."; RL Proc. Natl. Acad. Sci. U.S.A. 90:858-862(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP FUNCTION. RX MEDLINE=99287803; PubMed=10357938; RA Daniel A., Dumstrei K., Lengyel J.A., Hartenstein V.; RT "The control of cell fate in the embryonic visual system by atonal, RT tailless and EGFR signaling."; RL Development 126:2945-2954(1999). CC -!- FUNCTION: ORPHAN RECEPTOR THAT BINDS DNA AS A MONOMER TO HORMONE CC RESPONSE ELEMENTS (HRE) CONTAINING AN EXTENDED CORE MOTIF HALF- CC SITE SEQUENCE 5'-AAGTCA-3' IN WHICH THE 5' FLANKING NUCLEOTIDES CC PARTICIPATE IN DETERMINING RECEPTOR SPECIFICITY. THIS RECEPTOR CC BINDS TO THE CONSENSUS SEQUENCE [AG][AG]AAGTCAA. PLAYS A KEY ROLE CC IN THE ESTABLISHMENT OF NONMETAMERIC DOMAINS AT THE ANTERIOR AND CC POSTERIOR POLES OF THE EMBRYO. IT MAY ALSO PLAY A ROLE IN THE CC NERVOUS SYSTEM. THE MATERNAL TERMINAL PATHWAY ACTIVATES THE TLL CC GENE IN THE TERMINI; TLL ACTIVITY THEN REPRESSES SEGMENTATION AND CC ACTIVATES TERMINAL-SPECIFIC GENES IN THESE DOMAINS. INVOLVED IN CC THE REGULATION OF EARLY EYE DEVELOPMENT. IN THE EMBRYONIC VISUAL CC SYSTEM ANLAGE DRIVES CELLS TO OPTIC LOBE AS OPPOSED TO BOLWIG'S CC ORGAN FATE. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: BRAIN AND PERIPHERAL NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: DURING STAGE 10 FOUND IN THE ANTERIOR PART OF CC THE VISUAL SYSTEM THAT LATER GIVES RISE TO THE ANTERIOR LIP OF THE CC OPTIC LOBE. AT STAGE 12 ALSO FOUND IN THE POSTERIOR LIP OF THE CC OPTIC LOBE. IN THIRD LARVAL INSTAR EXPRESSED IN THE OPTIC LOBE OF CC THE LARVAL BRAIN AND IN THE EYE ANTENNAL DISK, BOTH IN ANTENNAL CC AND EYE PORTION. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR2 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M34639; AAA28936.1; -. DR EMBL; AF019362; AAB71371.1; -. DR EMBL; AE003775; AAF57091.1; -. DR PIR; A35602; A35602. DR HSSP; P10826; 1HRA. DR TRANSFAC; T00789; -. DR FlyBase; FBgn0003720; tll. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR GO; GO:0007369; P:gastrulation; NAS. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR GO; GO:0006351; P:transcription, DNA-dependent; NAS. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Activator; Repressor; Developmental protein. FT DNA_BIND 34 101 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 34 54 C4-TYPE. FT ZN_FING 70 96 C4-TYPE. FT DOMAIN 244 389 LIGAND-BINDING (BY SIMILARITY). FT DOMAIN 262 265 POLY-LEU. SQ SEQUENCE 452 AA; 50549 MW; A4ABEFFDE993A37C CRC64; MQSSEGSPDM MDQKYNSVRL SPAASSRILY HVPCKVCRDH SSGKHYGIYA CDGCAGFFKR SIRRSRQYVC KSQKQGLCVV DKTHRNQCRA CRLRKCFEVG MNKDAVQHER GPRNSTLRRH MAMYKDAMMG AGEMPQIPAE ILMNTAALTG FPGVPMPMPG LPQRAGHHPA HMAAFQPPPS AAAVLDLSVP RVPHHPVHQG HHGFFSPTAA YMNALATRAL PPTPPLMAAE HIKETAAEHL FKNVNWIKSV RAFTELPMPD QLLLLEESWK EFFILAMAQY LMPMNFAQLL FVYESENANR EIMGMVTREV HAFQEVLNQL CHLNIDSTEY ECLRAISLFR KSPPSASSTE DLANSSILTG SGSPNSSASA ESRGLLESGK VAAMHNDARS ALHNYIQRTH PSQPMRFQTL LGVVQLMHKV SSFTIEELFF RKTIGDITIV RLISDMYSQR KI // ID TLR1_DROME STANDARD; PRT; 504 AA. AC P30974; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tachykinin-like peptides receptor 86C (NKD). GN TAKR86C OR NKD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=92112776; PubMed=1370464; RA Monnier D., Colas J.-F., Rosay P., Hen R., Borrelli E., Maroteaux L.; RT "NKD, a developmentally regulated tachykinin receptor in Drosophila."; RL J. Biol. Chem. 267:1298-1302(1992). RN [2] RP SEQUENCE OF 1-60 FROM N.A. RX MEDLINE=96028533; PubMed=7547478; RA Rosay P., Colas J.F., Maroteaux L.; RT "Dual organisation of the Drosophila neuropeptide receptor NKD gene RT promoter."; RL Mech. Dev. 51:329-339(1995). CC -!- FUNCTION: MAY PLAY A ROLE IN NEUROGENESIS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CENTRAL NERVOUS SYSTEM, AS WELL AS IN SUBSETS CC OF NEURONS IN EACH SEGMENT OF THE DEVELOPING VENTRAL GANGLIA. CC -!- DEVELOPMENTAL STAGE: DURING THE DEVELOPMENT AND IN THE ADULT. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC HIGHEST TO OTHER TACHYKININS RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77168; AAA28722.1; -. DR EMBL; S80427; AAB35334.2; -. DR HSSP; P02699; 1BOJ. DR FlyBase; FBgn0004841; Takr86C. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein. FT DOMAIN 1 84 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 85 108 1 (POTENTIAL). FT DOMAIN 109 118 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 119 143 2 (POTENTIAL). FT DOMAIN 144 155 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 156 179 3 (POTENTIAL). FT DOMAIN 180 199 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 200 224 4 (POTENTIAL). FT DOMAIN 225 250 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 251 275 5 (POTENTIAL). FT DOMAIN 276 308 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 309 330 6 (POTENTIAL). FT DOMAIN 331 343 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 344 367 7 (POTENTIAL). FT DOMAIN 368 504 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 12 12 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 28 28 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 36 36 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 504 AA; 57781 MW; 33F3D814376A1AC5 CRC64; MSEIVDTELL VNCTILAVRR FELNSIVNTT LLGSLNRTEV VSLLSSIIDN RDNLESINEA KDFLTECLFP SPTRPYELPW EQKTIWAIIF GLMMFVAIAG NGIVLWIVTG HRSMRTVTNY FLLNLSIADL LMSSLNCVFN FIFMLNSDWP FGSIYCTINN FVANVTVSTS VFTLVAISFD RYIAIVDPLK RRTSRRKVRI ILVLIWALSC VLSAPCLLYS SIMTKQYYNG KSRTVCFMMW PDGRYPTSMA DYAYNLIILV LTTGIPMIVM LICYSLMGRV PGGSRSIGEN TDRQMESMKS KRKVVRMFIA IVSIFAICWL PYHLFFIYAY HNNQVASTKY VQHMYLGFYW LAMSNAMVNP LIYYWMNKRF RMYFQRIICC CCVGLTRHRF DSPKSRLTNK NSSNRHTRAE TKSQWKRSTM ETQIQQAPVT SSCREQRSAQ QQQPPGSGTN RAAVECIMER PADGSSSPLC LSINNSIGER QRVKIKYISC DEDNNPVELS PKQM // ID TLR2_DROME STANDARD; PRT; 519 AA. AC P30975; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tachykinin-like peptides receptor 99D (dTKR). GN TAKR99D. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92007772; PubMed=1717263; RA Li X.-J., Wolfgang W., Wu Y.-N., North R.A., Forte M.; RT "Cloning, heterologous expression and developmental regulation of a RT Drosophila receptor for tachykinin-like peptides."; RL EMBO J. 10:3221-3229(1991). CC -!- FUNCTION: PROBABLE RECEPTOR FOR TACHYKININ-LIKE PEPTIDES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC HIGHEST TO OTHER TACHYKININS RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62711; CAA44595.1; -. DR PIR; S17783; S17783. DR FlyBase; FBgn0004622; Takr99D. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; Lipoprotein; KW Palmitate. FT DOMAIN 1 100 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 101 123 1 (POTENTIAL). FT DOMAIN 124 134 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 135 155 2 (POTENTIAL). FT DOMAIN 156 175 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 176 197 3 (POTENTIAL). FT DOMAIN 198 217 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 218 238 4 (POTENTIAL). FT DOMAIN 239 270 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 271 292 5 (POTENTIAL). FT DOMAIN 293 324 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 325 346 6 (POTENTIAL). FT DOMAIN 347 361 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 362 384 7 (POTENTIAL). FT DOMAIN 385 519 CYTOPLASMIC (POTENTIAL). FT DOMAIN 471 481 GLY/SER-RICH. FT CARBOHYD 3 3 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 19 19 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 22 22 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 61 61 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 174 254 BY SIMILARITY. FT LIPID 399 399 S-palmitoyl cysteine (Potential). SQ SEQUENCE 519 AA; 58480 MW; CACC5175F0BE476B CRC64; MENRSDFEAD DYGDISWSNW SNWSTPAGVL FSAMSSVLSA SNHTPCRTLA RSSPYPPVSF NHSQTLSTDQ PAVGDVEDAA EDAAASMETG SFAFVVPWWR QVLWSILFGG MVIVATGGNL IVVWIVMTTK RMRTVTNYFI VNLSIADAMV SSLNVTFNYY YMLDSDWPFG EFYCKLSQFI AMLSICASVF TLMAISIDRY VAIIRPLQPR MSKRCNLAIA AVIWLASTLI SCPMMIIYRT EEVPVRGLSN RTVCYPEWPD GPTNHSTMES LYNILIIILT YFLPIVSMTV TYSRVGIELW GSKTIGECTP RQVENVRSKR RVVKMMIVVV LIFAICWLPF HSYFIITSCY PAITEAPFIQ ELYLAIYWLA MSNSMYNPII YCWMNSRFRY GFKMVFRWCL FVRVGTEPFS RRENLTSRYS CSGSPDHNRI KRNDTQKSIL YTCPSSPKSH RISHSGTGRS ATLRNSLPAE SLSSGGSGGG GHRKRLSYQQ EMQQRWSGPN SATAVTNSSS TANTTQLLS // ID TOLL_DROME STANDARD; PRT; 1097 AA. AC P08953; Q9VBB8; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Toll protein precursor. GN TL OR CG5490. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88135760; PubMed=2449285; RA Hashimoto C., Hudson K.L., Anderson K.V.; RT "The Toll gene of Drosophila, required for dorsal-ventral embryonic RT polarity, appears to encode a transmembrane protein."; RL Cell 52:269-279(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=91092252; PubMed=2124970; RA Keith F.J., Gay N.J.; RT "The Drosophila membrane receptor Toll can function to promote RT cellular adhesion."; RL EMBO J. 9:4299-4306(1990). CC -!- FUNCTION: REQUIRED FOR DORSAL-VENTRAL EMBRYONIC POLARITY. MAY CC FUNCTION AS A MEMBRANE RECEPTOR. PROMOTES HETEROPHILIC CELLULAR CC ADHESION. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE TOLL-LIKE RECEPTOR FAMILY. CC -!- SIMILARITY: CONTAINS 21 LEUCINE-RICH (LRR) REPEATS. CC -!- SIMILARITY: CONTAINS 1 TIR DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19969; AAA28941.1; -. DR EMBL; AE003758; AAF56624.1; -. DR PIR; A29943; A29943. DR HSSP; O60603; 1FYW. DR FlyBase; FBgn0003717; Tl. DR GO; GO:0004888; F:transmembrane receptor activity; NAS. DR GO; GO:0006963; P:antibacterial polypeptide induction; IMP. DR GO; GO:0006966; P:antifungal humoral response (sensu Inverteb...; IMP. DR GO; GO:0006967; P:antifungal polypeptide induction; IMP. DR GO; GO:0009950; P:dorsal/ventral axis specification; NAS. DR GO; GO:0008063; P:Tl signaling pathway; NAS. DR InterPro; IPR004075; IL1_receptor1. DR InterPro; IPR001611; LRR. DR InterPro; IPR000483; LRR_Cterm. DR InterPro; IPR000372; LRR_Nterm. DR InterPro; IPR003591; LRR_typ. DR InterPro; IPR000157; TIR. DR Pfam; PF00560; LRR; 11. DR Pfam; PF01463; LRRCT; 2. DR Pfam; PF01462; LRRNT; 1. DR Pfam; PF01582; TIR; 1. DR PRINTS; PR01537; INTRLKN1R1F. DR PRINTS; PR00019; LEURICHRPT. DR SMART; SM00369; LRR_TYP; 3. DR SMART; SM00082; LRRCT; 2. DR SMART; SM00013; LRRNT; 1. DR SMART; SM00255; TIR; 1. DR PROSITE; PS50104; TIR; 1. KW Developmental protein; Transmembrane; Glycoprotein; Repeat; KW Cell adhesion; Leucine-rich repeat; Signal. FT SIGNAL 1 27 POTENTIAL. FT CHAIN 28 1097 TOLL PROTEIN. FT DOMAIN 28 807 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 808 828 POTENTIAL. FT DOMAIN 829 1097 CYTOPLASMIC (POTENTIAL). FT REPEAT 149 172 LRR 1. FT REPEAT 174 195 LRR 2. FT REPEAT 196 219 LRR 3. FT REPEAT 221 243 LRR 4. FT REPEAT 245 267 LRR 5. FT REPEAT 268 291 LRR 6. FT REPEAT 293 317 LRR 7. FT REPEAT 319 340 LRR 8. FT REPEAT 341 364 LRR 9. FT REPEAT 365 388 LRR 10. FT REPEAT 390 412 LRR 11. FT REPEAT 413 436 LRR 12. FT REPEAT 438 459 LRR 13. FT REPEAT 472 495 LRR 14. FT REPEAT 496 521 LRR 15. FT REPEAT 523 546 LRR 16. FT REPEAT 550 574 LRR 17. FT REPEAT 667 690 LRR 18. FT REPEAT 692 713 LRR 19. FT REPEAT 714 736 LRR 20. FT REPEAT 785 807 LRR 21. FT DOMAIN 857 996 TIR. FT CARBOHYD 80 80 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 140 140 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 175 175 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 235 235 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 270 270 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 275 275 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 346 346 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 391 391 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 482 482 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 508 508 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 528 528 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 654 654 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 677 677 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 702 702 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 715 715 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 730 730 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 738 738 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1097 AA; 124655 MW; D1BFC42245E3EABE CRC64; MSRLKAASEL ALLVIILQLL QWPGSEASFG RDACSEMSID GLCQCAPIMS EYEIICPANA ENPTFRLTIQ PKDYVQIMCN LTDTTDYQQL PKKLRIGEVD RVQMRRCMLP GHTPIASILD YLGIVSPTTL IFESDNLGMN ITRQHLDRLH GLKRFRFTTR RLTHIPANLL TDMRNLSHLE LRANIEEMPS HLFDDLENLE SIEFGSNKLR QMPRGIFGKM PKLKQLNLWS NQLHNLTKHD FEGATSVLGI DIHDNGIEQL PHDVFAHLTN VTDINLSANL FRSLPQGLFD HNKHLNEVRL MNNRVPLATL PSRLFANQPE LQILRLRAEL QSLPGDLFEH STQITNISLG DNLLKTLPAT LLEHQVNLLS LDLSNNRLTH LPDSLFAHTT NLTDLRLEDN LLTGISGDIF SNLGNLVTLV MSRNRLRTID SRAFVSTNGL RHLHLDHNDI DLQQPLLDIM LQTQINSPFG YMHGLLTLNL RNNSIIFVYN DWKNTMLQLR ELDLSYNNIS SLGYEDLAFL SQNRLHVNMT HNKIRRIALP EDVHLGEGYN NNLVHVDLND NPLVCDCTIL WFIQLVRGVH KPQYSRQFKL RTDRLVCSQP NVLEGTPVRQ IEPQTLICPL DFSDDPRERK CPRGCNCHVR TYDKALVINC HSGNLTHVPR LPNLHKNMQL MELHLENNTL LRLPSANTPG YESVTSLHLA GNNLTSIDVD QLPTNLTHLD ISWNHLQMLN ATVLGFLNRT MKWRSVKLSG NPWMCDCTAK PLLLFTQDNF ERIGDRNEMM CVNAEMPTRM VELSTNDICP AEKGVFIALA VVIALTGLLA GFTAALYYKF QTEIKIWLYA HNLLLWFVTE EDLDKDKKFD AFISYSHKDQ SFIEDYLVPQ LEHGPQKFQL CVHERDWLVG GHIPENIMRS VADSRRTIIV LSQNFIKSEW ARLEFRAAHR SALNEGRSRI IVIIYSDIGD VEKLDEELKA YLKMNTYLKW GDPWFWDKLR FALPHRRPVG NIGNGALIKT ALKGSTDDKL ELIKPSPVTP PLTTPPAEAT KNPLVAQLNG VTPHQAIMIA NGKNGLTNLY TPNGKSHGNG HINGAFIINT NAKQSDV // ID TOP1_DROME STANDARD; PRT; 972 AA. AC P30189; Q9VXW6; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA topoisomerase I (EC 5.99.1.2). GN TOP1 OR CG6146. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93117086; PubMed=1335568; RA Hsieh T.-S., Brown S.D., Huang P., Fostel J.; RT "Isolation and characterization of a gene encoding DNA topoisomerase RT I in Drosophila melanogaster."; RL Nucleic Acids Res. 20:6177-6182(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96354910; PubMed=8769417; RA Zhang C.X., Lee M.P., Chen A.D., Brown S.D., Hsieh T.-S.; RT "Isolation and characterization of a Drosophila gene essential for RT early embryonic development and formation of cortical cleavage RT furrows."; RL J. Cell Biol. 134:923-934(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CC CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. CC -!- CATALYTIC ACTIVITY: ATP-INDEPENDENT BREAKAGE OF SINGLE-STRANDED CC DNA, FOLLOWED BY PASSAGE AND REJOINING. CC -!- MISCELLANEOUS: EUKARYOTIC TOPOISOMERASE I AND II CAN RELAX BOTH CC NEGATIVE AND POSITIVE SUPERCOILS, WHEREAS PROKARYOTIC ENZYMES CC RELAX ONLY NEGATIVE SUPERCOILS. CC -!- MISCELLANEOUS: WHEN A TOPOISOMERASE TRANSIENTLY BREAKS A DNA CC BACKBONE BOND, IT SIMULTANEOUSLY FORMS A PROTEIN-DNA LINK, IN CC WHICH A TYROSYL OXYGEN IN THE ENZYME IS JOINED TO A DNA PHOSPHORUS CC AT ONE END OF THE ENZYME-SEVERED DNA STRAND. CC -!- SIMILARITY: BELONGS TO THE EUKARYOTIC TYPE I TOPOISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74557; AAA28951.1; -. DR EMBL; U80064; AAC24158.1; -. DR EMBL; AE003498; AAF48440.1; -. DR PIR; S35521; S35521. DR HSSP; P11387; 1A35. DR FlyBase; FBgn0004924; Top1. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0009795; P:embryonic morphogenesis; IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0002168; P:larval development (sensu Insecta); IMP. DR InterPro; IPR001631; Topismerse_I. DR InterPro; IPR008336; Topoisomer_I_N. DR Pfam; PF02919; Topoisomer_I_N; 1. DR Pfam; PF01028; Topoisomerase_I; 1. DR PRINTS; PR00416; EUTPISMRASEI. DR SMART; SM00435; TOPEUc; 1. DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1. KW Isomerase; Topoisomerase; DNA-binding. FT DOMAIN 32 39 POLY-HIS. FT DOMAIN 40 198 SER-RICH. FT ACT_SITE 930 930 DNA CLEAVAGE (BY SIMILARITY). FT CONFLICT 40 40 S -> H (IN REF. 3). FT CONFLICT 46 46 S -> SSS (IN REF. 3). FT CONFLICT 201 201 H -> Q (IN REF. 3). SQ SEQUENCE 972 AA; 111688 MW; 3764B8BDEEFA30CD CRC64; MSGDVAAENS IHIQNGGSCE VVQSNGVTTN GHGHHHHHHS SSSSSSKHKS SSKDKHRDRE REHKSSNSSS SSKEHKSSSR DKDRHKSSSS SSKHRDKDKE RDGSSNSHRS GSSSSHKDKD GSSSSKHKSS SGHHKRSSKD KERRDKDKDR GSSSSSRHKS SSSSRDKERS SSSHKSSSSS SSSKSKHSSS RHSSSSSSKD HPSYDGVFVK PEPVSQQLMH SGSVDAFQMQ QLGSYEAAAA GTNFNGNGNV AGANYKNGYE ESIVDIKKEE ESFNNLSQAS SCDYSMSQFR ADEPPFVVKH EQSYAEEDST MNYNDHDDDA DEMNDDEEDV PLAMRKRKQE ATDRPDGGMD NDDDDDIPLL ARKKVKKEKI KKESKEKSKK RVKEEPSDDY GNVKPKKKKM KKEPEPAVSP GKRQKAKAKV EEEEVWRWWE EEKRADGVKW STLEHKGPVF APRYERVPRN VRFYYDGKPL ELSEETEEAA TFYAKMLNHD YCTKEVFNNN FFKDFRKSMT PREREIIKDF RKCNFQEMFN YFQAESEKRK AASKEEKLIK KNENEALMKE FGFCMIDGHK EKIGNFRLEP PGLFRGRGEH PKMGMIKRRI QASDVSINCG KDSKVPSPPP GSRWKEVRHD NTVTWLASWI ENVQGQVKYI MLNPSSKLKG EKDHIKYETA RRLDKVIDKI RATYRDEWKS KEMRVRQRAV ALYFIDKLAL RAGNEKDEDQ ADTVGCCSLR VEHVQLHKEL NGKENVVVFD FPGKDSIRYY NEVEVEKRVF KNLELFMEHK KEGDDLFDRL NTQVLNEHLK ELMEGLTAKV FRTYNASKTL QSQLDLLTDP SATVPEKLLA YNRANRAVAI LCNHQRSVPK SHEKSMENLK EKIKAKREAI EKCESEYHSR DEKKGKQLER LRDQLKKLEL QETDRDENKT IALGTSKLNY LDPRISVAWC KKHDVPIEKI FNKTQRTKFL WAVHMADENY RF // ID TOP2_DROME STANDARD; PRT; 1447 AA. AC P15348; Q9VIW2; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA topoisomerase II (EC 5.99.1.3). GN TOP2 OR CG10223. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89178626; PubMed=2538621; RA Wyckoff E., Natalie D., Nolan J.M., Lee M., Hsieh T.-S.; RT "Structure of the Drosophila DNA topoisomerase II gene. Nucleotide RT sequence and homology among topoisomerases II."; RL J. Mol. Biol. 205:1-13(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: CONTROL OF TOPOLOGICAL STATES OF DNA BY TRANSIENT CC BREAKAGE AND SUBSEQUENT REJOINING OF DNA STRANDS. TOPOISOMERASE II CC MAKES DOUBLE-STRAND BREAKS. CC -!- CATALYTIC ACTIVITY: ATP-DEPENDENT BREAKAGE, PASSAGE AND REJOINING CC OF DOUBLE-STRANDED DNA. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: EUKARYOTIC TOPOISOMERASE I AND II CAN RELAX BOTH CC NEGATIVE AND POSITIVE SUPERCOILS, WHEREAS PROKARYOTIC ENZYMES CC RELAX ONLY NEGATIVE SUPERCOILS. CC -!- SIMILARITY: BELONGS TO THE TYPE II TOPOISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61209; CAA43523.1; -. DR EMBL; AE003663; AAF53802.2; -. DR PIR; S02160; S02160. DR HSSP; P06786; 1BGW. DR FlyBase; FBgn0003732; Top2. DR GO; GO:0008623; C:chromatin accessibility complex; IDA. DR GO; GO:0005626; C:insoluble fraction; IDA. DR GO; GO:0005710; C:metaphase chromosome; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0005625; C:soluble fraction; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0003918; F:DNA topoisomerase type II activity; IDA. DR GO; GO:0003723; F:RNA binding; IDA. DR InterPro; IPR003594; ATPbind_ATPase. DR InterPro; IPR003957; CBFA_NFYB_topis. DR InterPro; IPR001241; DNA_topoisoII. DR InterPro; IPR002205; DNA_topoisoIV. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00521; DNA_topoisoIV; 1. DR Pfam; PF02518; HATPase_c; 1. DR PRINTS; PR00615; CCAATSUBUNTA. DR PRINTS; PR00418; TPI2FAMILY. DR ProDom; PD000742; DNA_topoisoIV; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SMART; SM00434; TOP4c; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. KW Isomerase; Topoisomerase; DNA-binding; ATP-binding; Nuclear protein. FT NP_BIND 142 147 ATP (POTENTIAL). FT ACT_SITE 785 785 DNA CLEAVAGE (BY SIMILARITY). SQ SEQUENCE 1447 AA; 164394 MW; 63B5D2814AD06419 CRC64; MENGNKALSI EQMYQKKSQL EHILLRPDSY IGSVEFTKEL MWVYDNSQNR MVQKEISFVP GLYKIFDEIL VNAADNKQRD KSMNTIKIDI DPERNMVSVW NNGQGIPVTM HKEQKMYVPT MIFGHLLTSS NYNDDEKKVT GGRNGYGAKL CNIFSTSFTV ETATREYKKS FKQTWGNNMG KASDVQIKDF NGTDYTRITF SPDLAKFKMD RLDEDIVALM SRRAYDVAAS SKGVSVFLNG NKLGVRNFKD YIDLHIKNTD DDSGPPIKIV HEVANERWEV ACCPSDRGFQ QVSFVNSIAT YKGGRHVDHV VDNLIKQLLE VLKKKNKGGI NIKPFQVRNH LWVFVNCLIE NPTFDSQTKE NMTLQQKGFG SKCTLSEKFI NNMSKSGIVE SVLAWAKFKA QNDIAKTGGR KSSKIKGIPK LEDANEAGGK NSIKCTLILT EGDSAKSLAV SGLGVIGRDL YGVFPLRGKL LNVREANFKQ LSENAEINNL CKIIGLQYKK KYLTEDDLKT LRYGKVMIMT DQDQDGSHIK GLLINFIHTN WPELLRLPFL EEFITPIVKA TKKNEELSFY SLPEFEEWKN DTANHHTYNI KYYKGLGTST SKEAKEYFQD MDRHRILFKY DGSVDDESIV MAFSKKHIES RKVWLTNHMD EVKRRKELGL PERYLYTKGT KSITYADFIN LELVLFSNAD NERSIPSLVD GLKPGQRKVM FTCFKRNDKR EVKVAQLSGS VAEMSAYHHG EVSLQMTIVN LAQNFVGANN INLLEPRGQF GTRLSGGKDC ASARYIFTIM SPLTRLIYHP LDDPLLDYQV DDGQKIEPLW YLPIIPMVLV NGAEGIGTGW STKISNYNPR EIMKNLRKMI NGQEPSVMHP WYKNFLGRME YVSDGRYIQT GNIQILSGNR LEISELPVGV WTQNYKENVL EPLSNGTEKV KGIISEYREY HTDTTVRFVI SFAPGEFERI HAEEGGFYRV FKLTTTLSTN QMHAFDQNNC LRRFPTAIDI LKEYYKLRRE YYARRRDFLV GQLTAQADRL SDQARFILEK CEKKLVVENK QRKAMCDELL KRGYRPDPVK EWQRRIKMED AEQADEEDEE EEEAAPSVSS KAKKEKEVDP EKAFKKLTDV KKFDYLLGMS MWMLTEEKKN ELLKQRDTKL SELESLRKKT PEMLWLDDLD ALESKLNEVE EKERAEEQGI NLKTAKALKG QKSASAKGRK VKSMGGGAGA GDVFPDPDGE PVEFKITEEI IKKMAAAAKV AQAAKEPKKP KEPKEPKVKK EPKGKQIKAE PDASGDEVDE FDAMVEGGSK TSPKAKKAVV KKEPGEKKPR QKKENGGGLK QSKIDFSKAK AKKSDDDVEE VTPRAERPGR RQASKKIDYS SLFSDEEEDG GNVGSDDDGN ASDDDSPKRP AKRGREDESS GGAKKKAPPK KRRAVIESDD DDIEIDEDDD DDSDFNC // ID TORS_DROME STANDARD; PRT; 340 AA. AC O77277; Q8T037; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Torsin-like protein precursor. GN TORP4A OR EG:84H4.1 OR CG3024. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Chou J., Gusella J.F.; RT "A Drosophila homolog of human torsinA, gene responsible for primary RT torsion dystornia."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: MAY SERVE AS A MOLECULAR CHAPERONE ASSISTING IN THE CC PROPER FOLDING OF SECRETED AND/OR MEMBRANE PROTEINS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CLPA/CLPB FAMILY. TORSIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF236156; AAF60321.1; ALT_INIT. DR EMBL; AE003431; AAF45969.2; -. DR EMBL; AL031766; CAA21132.1; ALT_INIT. DR EMBL; AY069592; AAL39737.1; -. DR FlyBase; FBgn0025615; torp4a. DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS. DR GO; GO:0005524; F:ATP binding; ISS. DR GO; GO:0003754; F:chaperone activity; ISS. DR GO; GO:0006457; P:protein folding; ISS. KW Chaperone; Endoplasmic reticulum; ATP-binding; Signal; Glycoprotein. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 340 TORSIN-LIKE PROTEIN. FT NP_BIND 108 115 ATP (POTENTIAL). FT CARBOHYD 96 96 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 311 311 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 340 AA; 38170 MW; 942F05D3C2ACE7A8 CRC64; MMSFPRMLSL CLSVLVILPL PLQSVDPLTI GAVGAVALGA YFKEHTYCRF AECCDDRNIP ARIDELERSL ERTLIGQHIV RQHIVPALKA HIASGNKSRK PLVISFHGQP GTGKNFVAEQ IADAMYLKGS RSNYVTKYLG QADFPKESEV SNYRVKINNA VRDTLRSCPR SLFIFDEVDK MPSGVFDQLT SLVDYNAFVD GTDNTKAIFI FLSNTAGSHI ASHLGSVMKN GRLREDTRLS DFEPLLRKAA YNMDGGMKKT TMIESHVIDH FIPFLPMEKA HVIKCLEAEL LRWRRDPKQA NNQKIIEDII NSSISYDRTH SLFAISGCKT LEKKVAMAIY // ID TOR_DROME STANDARD; PRT; 923 AA. AC P18475; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tyrosine-protein kinase receptor torso precursor (EC 2.7.1.112). GN TOR. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89181943; PubMed=2927509; RA Sprenger F., Stevens L.M., Nuesslein-Volhard C.; RT "The Drosophila gene torso encodes a putative receptor tyrosine RT kinase."; RL Nature 338:478-483(1989). RN [2] RP CHARACTERIZATION. RX MEDLINE=93140754; PubMed=8423783; RA Sprenger F., Torsoclair M.M., Morrison D.K.; RT "Biochemical analysis of torso and D-raf during Drosophila RT embryogenesis: implications for terminal signal transduction."; RL Mol. Cell. Biol. 13:1163-1172(1993). CC -!- FUNCTION: PROBABLE RECEPTOR WITH TYROSINE-PROTEIN KINASE ACTIVITY. CC REQUIRED FOR DETERMINATION OF ANTERIOR AND POSTERIOR TERMINAL CC STRUCTURES IN THE DROSOPHILA EMBRYO. THE LIGAND OF TORSO SEEMS TO CC BE TSL. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED THROUGHOUT THE EMBRYO BUT IS CC ACTIVATED SPECIFICALLY AT THE POLES. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15150; CAA33247.1; -. DR PIR; S03900; S03900. DR HSSP; P11362; 1FGK. DR FlyBase; FBgn0003733; tor. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0030381; P:eggshell pattern formation (sensu Insecta); IMP. DR GO; GO:0007362; P:terminal region determination; IMP. DR InterPro; IPR003961; FN_III. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00060; FN3; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Developmental protein; Receptor; Glycoprotein; KW Tyrosine-protein kinase; ATP-binding; Transferase; Phosphorylation; KW Transmembrane; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 923 TYROSINE-PROTEIN KINASE RECEPTOR TORSO. FT DOMAIN 21 399 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 400 420 POTENTIAL. FT DOMAIN 421 923 CYTOPLASMIC (POTENTIAL). FT DOMAIN 475 874 PROTEIN KINASE. FT NP_BIND 481 489 ATP (BY SIMILARITY). FT BINDING 502 502 ATP (BY SIMILARITY). FT ACT_SITE 741 741 BY SIMILARITY. FT CARBOHYD 37 37 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 63 63 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 107 107 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 142 142 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 146 146 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 287 287 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 298 298 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 314 314 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 326 326 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 342 342 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 348 348 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 377 377 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 923 AA; 105163 MW; FB25881F5757CF41 CRC64; MLIFYAKYAF IFWFFVGSNQ GEMLLMDKIS HDKTLLNVTA CTQNCLEKGQ MDFRSCLKDC RINGTFPGAL RKVQENYQMN MICRTESEIV FQIDWVQHSR GTEPAPNATY IIRVDAVKDD NKETTLYLSD DNFLILPGLE SNSTHNITAL AMHGDGSYSL IAKDQTFATL IRGYQPSKMG AVNLLRFVPQ PDDLHHIAAE IEWKPSAESN CYFDMVSYST NSVNMDEPLE VQFRDRKKLY RHTVDNLEFD KQYHVGVRTV NIMNRLESDL QWLPIAVPSC LDWYPYNYTL CPPHKPENLT VTQKQYLPNI LALNITWARP RYLPDNYTLH IFDLFKGGTE LNYTLDQNRS HFYVPKITVL GSHFEVHLVA QSAGGKNVSG LTLDKVPRGV LLSEGNMVKL VLFIIVPICC ILMLCSLTFC RRNRSEVQAL QMDAKDAKAS EFHLSLMDSS GLLVTLSANE SLEVMDELEV EPHSVLLQDV LGEGAFGLVR RGVYKKRQVA VKLLKDEPND EDVYAFKCEI QMLKAVGKHP NIVGIVGYST RFSNQMMLLI EYCSLGSLQN FLREEWKFRQ EQNAIGLKKN LEQNVDNRRF NRLPRNSIHD RIEDINNSML STVEEESESD QTHSSRCETY TLTRITNAAD NKGYGLEDIE NIGGSYIPKT AEAPKDQPKR KLKPQPKKDS KQDFKSDNKK RIFENKEYFD CLDSSDTKPR IPLKYADLLD IAQQVAVGME FLAQNKVVHR DLAARNVLIS VDRSIKIADF GLSRDVYHEN VYRKSGGSGK LPIKWLALES LTHQVYTSQS DVWSFGVLLY EITTLGGMPY PSVSPSDLLQ LLRQGHRMKR PEGCTQEMFS LMESCWSSVP SHRPTFSALK HRLGGMILAT NDVPERLKQL QAATESKLKS CDGLNSKVEQ VPCEEELYLE PLN // ID TP3A_DROME STANDARD; PRT; 1250 AA. AC Q9NG98; Q9VIV1; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA topoisomerase III alpha (EC 5.99.1.2). GN TOP3-ALPHA OR CG10123. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Plank J.L., Reineke J.C., Wilson T.M., Hsieh T.-S.; RT "Drosophila melanogaster topoisomerase III alpha."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: WEAKLY RELAXES NEGATIVE SUPERCOILS AND DISPLAYS A CC DISTINCT PREFERENCE FOR BINDING SINGLE-STRANDED DNA. CC -!- CATALYTIC ACTIVITY: ATP-INDEPENDENT BREAKAGE OF SINGLE-STRANDED CC DNA, FOLLOWED BY PASSAGE AND REJOINING. CC -!- MISCELLANEOUS: WHEN A TOPOISOMERASE TRANSIENTLY BREAKS A DNA CC BACKBONE BOND, IT SIMULTANEOUSLY FORMS A PROTEIN-DNA LINK, IN CC WHICH A TYROSYL OXYGEN IN THE ENZYME IS JOINED TO A DNA PHOSPHORUS CC AT ONE END OF THE ENZYME-SEVERED DNA STRAND (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PROKARYOTIC TYPE I/III TOPOISOMERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF255733; AAF71288.1; -. DR EMBL; AE003663; AAF53813.2; -. DR FlyBase; FBgn0040268; Top3-alpha. DR InterPro; IPR000380; DNA_tpisomrase. DR InterPro; IPR003601; DNAtopI_ATP_bind. DR InterPro; IPR003602; DNAtopI_DNA_bind. DR InterPro; IPR006171; Toprim_dom. DR InterPro; IPR006154; Toprim_sub. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 1. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. KW Isomerase; Topoisomerase; DNA-binding. FT ACT_SITE 356 356 DNA CLEAVAGE (BY SIMILARITY). FT CONFLICT 111 111 K -> E (IN REF. 1). SQ SEQUENCE 1250 AA; 136136 MW; 108E4AC18EA5677A CRC64; MKAVLTCFRP VVASHRRYCA NPGQAMKYLN VAEKNDAAKT IAGLLSNGAA QRREGYSVYN KVFDFEAPVR GQNAKMVMTS VSGHMMQLAF QVSYKNWRTV DPRSLFDAPV KKGVGSDYEP IKRTLEREVR GCQGLIIWTD CDREGENIGY EIIDVCRAIK PNISVYRATF SEITTVAVRR ALQQLGQPDK RQSDAVDVRT ELDLRTGAAI TRFQTMRLQR LFPEKIADKL ISYGSCQIPT LGFVAERYKE IEAFVSEPFW KIKVLHTIDD LTVEFNWARN RLFDKEACEN YLLLCLAEPD PRALVESVTV KPKHKWRPTP LDTVEMEKLG SRKLKLSAKE TMTIAEKLYT KGFISYPRTE TNQFSKEFAL APLVEMQTGH RDWGAFAQRV IEWGPNPRNG NKSDQAHPPI HPTKLAENLQ GNEARVYELV VRHFLACVSK DAVGSETLVH IDIAGEKFTA NGLVIHERNY LDVYVYDKWS AKQIHHYENG QRFEPTEVSL HEGATTAPPL LTEADLIALM EKHGIGTDAT HAEHINTIKE RGYIGVLDKG FLVPGVIGMG LYEGYDAMEL ALAKPQLRAE FELDLKLICQ GQKDPKVVLT EQIAKYKQAY QQITDKITAM DAKISARINE TPAANSAVQE GADGSAPSHG IIQSIFQCPK CNEAPLALKP KKNQQGWYIG CNNFPDCKNA VWLPTECKDA SVLDECCPTC GDGYRMLKFR LSTPYYRGVF GTPSGWYKTC LPCDNLFRTT FNINLDSVKK VGGIVGEVRG GGGGPGPGPG GGGSGRGAGS GGWSSGPGGG GSGGGGGSGG WGSGTGGGGS GGWGSGTGGG GLGGGKGKKP GGESKKSATK KPPNEPKPKK TKEPKAAPNK KTSSKSSGSI RSFFTSAAPT NSASNGLDEF FDSNDGFEDA MLAAAESVES SSQPKTISMV PLDDDIAAAF AADDDAEFEA LVNGGTMPTE SNGDQQLDKS LSEWIKEQDK ADERPMLWGT RERASLGTAA PTPPPKPAAK RPRWDSVERD STPPSSVPES ETVLCTGCQQ PARQNTVRKN GPNLGRLYYK CPKPDECNFF QWADEPPSSA KSKNSTGSAP QSTTSWGSNR VVTLPSIQQS NSQRGQSSMR SNSSSTVTIT QTKTKQQERN TATPGDGEEV MCNCGQLASQ LTVRKDGPNQ GRPFYACPTR EKSCGFFKWG DEDQNQGASS TSWGSANRNP PGRSQPTAIT SDGPKTRRCG LCRKEGHTRN KCPRKDEFDM // ID TP3B_DROME STANDARD; PRT; 875 AA. AC O96651; Q9W416; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA topoisomerase III beta (EC 5.99.1.2). GN TOP3-BETA OR TOP3 OR CG3458. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=20102653; PubMed=10636841; RA Wilson T.M., Chen A.D., Hsieh T.-S.; RT "Cloning and characterization of Drosophila topoisomerase IIIbeta. RT Relaxation of hypernegatively supercoiled DNA."; RL J. Biol. Chem. 275:1533-1540(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: WEAKLY RELAXES NEGATIVE SUPERCOILS AND DISPLAYS A CC DISTINCT PREFERENCE FOR BINDING SINGLE-STRANDED DNA. CC -!- CATALYTIC ACTIVITY: ATP-INDEPENDENT BREAKAGE OF SINGLE-STRANDED CC DNA, FOLLOWED BY PASSAGE AND REJOINING. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING THE FIRST 6 HOURS OF CC EMBRYONIC DEVELOPMENT, LEVELS DECLINE DURING LARVAL AND PUPAL CC STAGES TO INCREASE AGAIN DURING ADULTHOOD. CC -!- MISCELLANEOUS: WHEN A TOPOISOMERASE TRANSIENTLY BREAKS A DNA CC BACKBONE BOND, IT SIMULTANEOUSLY FORMS A PROTEIN-DNA LINK, IN CC WHICH A TYROSYL OXYGEN IN THE ENZYME IS JOINED TO A DNA PHOSPHORUS CC AT ONE END OF THE ENZYME-SEVERED DNA STRAND (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PROKARYOTIC TYPE I/III TOPOISOMERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF099909; AAD13219.1; -. DR EMBL; AE003437; AAF46144.1; -. DR FlyBase; FBgn0026015; Top3-beta. DR InterPro; IPR003601; DNAtopI_ATP_bind. DR InterPro; IPR003602; DNAtopI_DNA_bind. DR InterPro; IPR000380; DNA_tpisomrase. DR InterPro; IPR006171; Toprim_dom. DR InterPro; IPR006154; Toprim_sub. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. KW Isomerase; Topoisomerase; DNA-binding. FT ACT_SITE 332 332 DNA CLEAVAGE (BY SIMILARITY). FT DOMAIN 819 859 GLY-RICH. FT CONFLICT 747 747 V -> M (IN REF. 1). SQ SEQUENCE 875 AA; 96973 MW; 3A26520C10AB6057 CRC64; MKSVLMVAEK PSLAASLAGI LSNGRCTAKR GTGNGCSTHE WTGNFRNEGS VHFRMTSVCG HVMSLDFNKK YNCWDKVDPI QLFGCATEKK ETNPKQNMRK FLAHEARGCD YLVLWLDCDK EGENICFEVM DAVKHVINNV YSDQVTYRAH FSAITEKDIK KAMETLGHPN ENEAKSVDAR QELDLRIGCA FTRFQTKFFQ DRYGDLDSSL ISYGPCQTPT LGFCVKRHDD IQTFKPESFW HLQLLAGQPE VTLEWARGRV FKKDIAIMLL NRVKEHKKAT VESVASKEAY KSKPQALNTV ELMRICSSGL GIGPFQAMQI AERLYTQGYI SYPRTETNQY PTNFDLPAVL HVLKPSADFG EEARSILGDI QTPRKGKDAG DHPPITPMKL GNRSDFDRDT WRVYEFICRH FMGTVSRDLK YRVTTAKLSV GMETFSCTAS VLIDAGFTKV MTWSAFGKDE PQPPFVQGTQ VAINDVRLIE SQTGPPDYLT ESELITLMEE HGIGTDASIP VHINNICQRN YVHIENGRKL MPTTLGIVLV HGYQKIDPEL VLPTMRTEVE RMLTLIAQGS ANFQDVLRHA IKIFKLKFMY FVKNIDSMDA LFEVSFSPLA ESGKAHSRCG KCRRYMKYIQ TKPARLHCSH CDETYALPIG NVKVYREFKC PLDDFDLLAF STGVKGRSYP FCPYCYNHPP FSDMPHLGGC NTCTNANCPH SLNTLGISSC VECPTGVLVL DCTLAPTWKL GCNRCDVIIN CFKGATKITV EEAKCQECGA QQVNVVYKSD KSKFKDGSEE KSGCIFCSAD FSHLVEKHRA VASRPVRSGG GFRGGKAGRG GGGMGGAAFG SGGAVTAGGG PNAGGGVRGS RVAKDKMGQL ASYFV // ID TPC1_DROME STANDARD; PRT; 154 AA. AC P47947; Q9V9E1; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Troponin C, isoform 1. GN TPNC41C OR TNC41C OR CG2981. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95071221; PubMed=7980384; RA Fyrberg C., Parker H., Hutchison B., Fyrberg E.A.; RT "Drosophila melanogaster genes encoding three troponin-C isoforms and RT a calmodulin-related protein."; RL Biochem. Genet. 32:119-135(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: PRESENT ONLY IN ADULT MUSCLES. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76043; CAA53628.1; -. DR EMBL; AE003788; AAF57350.1; -. DR HSSP; P02588; 1PON. DR FlyBase; FBgn0013348; TpnC41C. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 4. DR ProDom; PD000012; EF-hand; 2. DR PROSITE; PS00018; EF_HAND; 2. KW Muscle protein; Calcium-binding; Multigene family. FT DOMAIN 24 35 ANCESTRAL CALCIUM SITE 1 (POTENTIAL). FT CA_BIND 57 68 EF-HAND 2 (POTENTIAL). FT DOMAIN 97 108 ANCESTRAL CALCIUM SITE 3 (POTENTIAL). FT CA_BIND 133 144 EF-HAND 4 (POTENTIAL). FT CONFLICT 84 84 A -> R (IN REF. 1). FT CONFLICT 154 154 MISSING (IN REF. 1). SQ SEQUENCE 154 AA; 17156 MW; 614C087F529FB508 CRC64; MSDELTKEQT ALLRNAFNAF DPEKNGYINT AMVGTILSML GHQLDDATLA DIIAEVDEDG SGQIEFEEFT TLAARFLVEE DAEAMMAELK EAFRLYDKEG NGYITTGVLR EILRELDDKL TNDDLDMMIE EIDSDGSGTV DFDEFMEVMT GGDD // ID TPC2_DROME STANDARD; PRT; 155 AA. AC P47948; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Troponin C, isoform 2. GN TPNC47D OR TNC47D. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95071221; PubMed=7980384; RA Fyrberg C., Parker H., Hutchison B., Fyrberg E.A.; RT "Drosophila melanogaster genes encoding three troponin-C isoforms and RT a calmodulin-related protein."; RL Biochem. Genet. 32:119-135(1994). CC -!- TISSUE SPECIFICITY: ACCUMULATES ALMOST EXCLUSIVELY IN LARVAL CC MUSCLES. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76044; CAA53629.1; -. DR PIR; S38877; S38877. DR HSSP; P02593; 1CDM. DR FlyBase; FBgn0010423; TpnC47D. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 4. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 3. DR PROSITE; PS00018; EF_HAND; 2. KW Muscle protein; Calcium-binding; Multigene family. FT DOMAIN 27 38 ANCESTRAL CALCIUM SITE 1 (POTENTIAL). FT CA_BIND 60 71 EF-HAND 2 (POTENTIAL). FT DOMAIN 100 111 ANCESTRAL CALCIUM SITE 3 (POTENTIAL). FT CA_BIND 136 147 EF-HAND 4 (POTENTIAL). SQ SEQUENCE 155 AA; 17895 MW; 7831DD9AD0205F23 CRC64; MDNIDEDLTP EQIAVLQKAF NSFDHQKTGS IPTEMVADIL RLMGQPFDRQ ILDELMHEVD EDKSGRLEFE EFVQLAAKFI VEEDDEAMQK DVREAFRLYD KQGNGYIPTS CLKEILKELD DQLTEQELDI MIEEIDSDGS GTVDFDEFME MMTGE // ID TPC3_DROME STANDARD; PRT; 155 AA. AC P47949; Q9VVE1; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Troponin C, isoform 3. GN TPNC73F OR TNC73F OR CG7930. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95071221; PubMed=7980384; RA Fyrberg C., Parker H., Hutchison B., Fyrberg E.A.; RT "Drosophila melanogaster genes encoding three troponin-C isoforms and RT a calmodulin-related protein."; RL Biochem. Genet. 32:119-135(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: PRESENT IN BOTH LARVAL AND ADULT MUSCLES. CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76042; CAA53627.1; -. DR EMBL; AE003525; AAF49371.1; -. DR PIR; S38878; S38878. DR HSSP; P02593; 1CDM. DR FlyBase; FBgn0010424; TpnC73F. DR InterPro; IPR003299; Calflagin. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 4. DR PRINTS; PR01362; CALFLAGIN. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 3. DR PROSITE; PS00018; EF_HAND; 2. KW Muscle protein; Calcium-binding; Multigene family. FT DOMAIN 27 38 ANCESTRAL CALCIUM SITE 1 (POTENTIAL). FT CA_BIND 60 71 EF-HAND 2 (POTENTIAL). FT DOMAIN 100 111 ANCESTRAL CALCIUM SITE 3 (POTENTIAL). FT CA_BIND 136 147 EF-HAND 4 (POTENTIAL). FT CONFLICT 93 93 R -> A (IN REF. 1). SQ SEQUENCE 155 AA; 17696 MW; F45FCF78438C4D0B CRC64; MSSVDEDLTP EQIAVLQKAF NSFDHQKTGS IPTEMVADIL RLMGQPFDKK ILEELIEEVD EDKSGRLEFG EFVQLAAKFI VEEDAEAMQK ELREAFRLYD KQGNGFIPTT CLKEILKELD DQLTEQELDI MIEEIDSDGS GTVDFDEFME MMTGE // ID TPIS_DROME STANDARD; PRT; 247 AA. AC P29613; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Triosephosphate isomerase (EC 5.3.1.1) (TIM). GN TPI. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92079900; PubMed=1720860; RA Shaw-Lee R.L., Lissemore J.L., Sullivan D.T.; RT "Structure and expression of the triose phosphate isomerase (Tpi) RT gene of Drosophila melanogaster."; RL Mol. Gen. Genet. 230:225-229(1991). RN [2] RP SEQUENCE OF 158-170. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE = GLYCERONE CC PHOSPHATE. CC -!- PATHWAY: PLAYS AN IMPORTANT ROLE IN SEVERAL METABOLIC PATHWAYS. CC -!- SUBUNIT: HOMODIMER. CC -!- SIMILARITY: BELONGS TO THE TRIOSEPHOSPHATE ISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57576; CAA40804.1; -. DR PIR; S18604; S18604. DR HSSP; P00940; 1TPH. DR FlyBase; FBgn0003738; Tpi. DR InterPro; IPR000652; Triophos_ismrse. DR Pfam; PF00121; TIM; 1. DR ProDom; PD001005; Triophos_ismrse; 1. DR TIGRFAMs; TIGR00419; tim; 1. DR PROSITE; PS00171; TIM; 1. KW Isomerase; Glycolysis; Gluconeogenesis; Fatty acid biosynthesis; KW Pentose shunt. FT ACT_SITE 94 94 BY SIMILARITY. FT ACT_SITE 164 164 BY SIMILARITY. SQ SEQUENCE 247 AA; 26579 MW; F6BBB0269A95D6DE CRC64; MSRKFCVGGN WKMNGDQKSI AEIAKTLSSA ALDPNTEVVI GCPAIYLMYA RNLLPCELGL AGQNAYKVAK GAFTGEISPA MLKDIGADWV ILGHSERRAI FGESDALIAE KAEHALAEGL KVIACIGETL EEREAGKTNE VVARQMCAYA QKIKDWKNVV VAYEPVWAIG TGKTATPDQA QEVHASLRQW LSDNISKEVS ASLRIQYGGS VTAANAKELA KKPDIDGFLV GGASLKPEFL DIINARQ // ID TPM1_DROME STANDARD; PRT; 285 AA. AC P06754; P09492; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tropomyosin 1, muscle/non-muscle/9A isoforms (Tropomyosin II) DE (Cytoskeletal tropomyosin). GN TM1 OR TMII. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM MUSCLE). RX MEDLINE=87106815; PubMed=3803921; RA Hanke P.D., Storti R.V.; RT "Nucleotide sequence of a cDNA clone encoding a Drosophila muscle RT tropomyosin II isoform."; RL Gene 45:211-214(1986). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS MUSCLE AND 9A). RC STRAIN=Oregon-R; TISSUE=Pupae; RX MEDLINE=87064486; PubMed=3097506; RA Karlik C.C., Fyrberg E.A.; RT "Two Drosophila melanogaster tropomyosin genes: structural and RT functional aspects."; RL Mol. Cell. Biol. 6:1965-1973(1986). RN [3] RP SEQUENCE FROM N.A. (ISOFORM NON-MUSCLE). RC TISSUE=Embryo, and Pupae; RX MEDLINE=88087013; PubMed=3693358; RA Hanke P.D., Lepinske H.M., Storti R.V.; RT "Characterization of a Drosophila cDNA clone that encodes a 252-amino RT acid non-muscle tropomyosin isoform."; RL J. Biol. Chem. 262:17370-17373(1987). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC; ISOFORM 9A. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist; CC Name=Muscle; Synonyms=9D; CC IsoId=P06754-1; Sequence=Displayed; CC Name=Non-muscle; Synonyms=Cytoskeletal; CC IsoId=P06754-2; Sequence=VSP_006617, VSP_006618, VSP_006619, CC VSP_006620, VSP_006621, VSP_006622; CC Name=9A; CC IsoId=P06754-3; Sequence=VSP_006622; CC Name=33; Synonyms=9C; CC IsoId=P49455-1; Sequence=External; CC Name=34; Synonyms=9B; CC IsoId=P49455-2; Sequence=External; CC -!- DEVELOPMENTAL STAGE: ISOFORM 9A IS EXPRESSED BOTH MATERNALLY AND CC ZYGOTICALLY DURING EMBRYOGENESIS AND MID PUPAL STAGES. MUSCLE CC ISOFORM IS EXPRESSED AT LATE EMBRYOGENESIS THROUGH TO ADULTHOOD, CC HIGHEST EXPRESSION LEVEL BEING LATE EMBRYO AND EARLY LARVAL CC STAGES. CC -!- DOMAIN: THE MOLECULE IS IN A COILED COIL STRUCTURE. THE SEQUENCE CC EXHIBITS A PROMINENT SEVEN-RESIDUES PERIODICITY. CC -!- SIMILARITY: BELONGS TO THE TROPOMYOSIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M15466; AAA28975.1; -. DR EMBL; L00363; AAA28966.1; -. DR EMBL; M12840; AAA28966.1; JOINED. DR EMBL; L00355; AAA28966.1; JOINED. DR EMBL; L00356; AAA28966.1; JOINED. DR EMBL; L00357; AAA28966.1; JOINED. DR EMBL; L00358; AAA28966.1; JOINED. DR EMBL; L00359; AAA28966.1; JOINED. DR EMBL; L00360; AAA28966.1; JOINED. DR EMBL; L00362; AAA28966.1; JOINED. DR EMBL; M13023; AAA28969.1; -. DR EMBL; M12840; AAA28969.1; JOINED. DR EMBL; L00355; AAA28969.1; JOINED. DR EMBL; L00356; AAA28969.1; JOINED. DR EMBL; L00357; AAA28969.1; JOINED. DR EMBL; L00358; AAA28969.1; JOINED. DR EMBL; L00359; AAA28969.1; JOINED. DR EMBL; L00360; AAA28969.1; JOINED. DR EMBL; L00362; AAA28969.1; JOINED. DR EMBL; J03502; AAA28972.1; -. DR PIR; A25561; A25561. DR HSSP; P23370; 1RIS. DR FlyBase; FBgn0003721; Tm1. DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP. DR InterPro; IPR000533; Tropomyosin. DR Pfam; PF00261; Tropomyosin; 1. DR PRINTS; PR00194; TROPOMYOSIN. DR PROSITE; PS00326; TROPOMYOSIN; 1. KW Muscle protein; Cytoskeleton; Actin-binding; Coiled coil; KW Alternative splicing; Multigene family. FT DOMAIN 14 277 COILED COIL (POTENTIAL). FT VARSPLIC 1 32 Missing (in isoform Non-muscle). FT /FTId=VSP_006617. FT VARSPLIC 33 80 NTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEE FT KNKALQN -> MTTRLPQGTLLDVLKKKMRQTKEEMEKYKD FT ECEEFHKRLQLEVVRREE (in isoform FT Non-muscle). FT /FTId=VSP_006618. FT VARSPLIC 134 154 ALADEERMDALENQLKEARFL -> TNMEDDKVALLENQLA FT QAKLI (in isoform Non-muscle). FT /FTId=VSP_006619. FT VARSPLIC 170 188 AMVEADLERAEERAEQGEN -> VLMEQDLERSEEKVELSE FT S (in isoform Non-muscle). FT /FTId=VSP_006620. FT VARSPLIC 214 231 SNQREEEYKNQIKTLNTR -> ATQKEETFETQIKVLDHS FT (in isoform Non-muscle). FT /FTId=VSP_006621. FT VARSPLIC 261 285 VLEKERYKDIGDDLDTAFVELILKE -> LNVRGKNKLLQE FT EMEATLHDIQNM (in isoform 9A and FT Non-muscle isoform). FT /FTId=VSP_006622. FT CONFLICT 106 114 LGSATAKLS -> SASAIQLAA (IN REF. 2). FT CONFLICT 119 119 A -> S (IN REF. 2). FT CONFLICT 126 126 A -> I (IN REF. 3). FT CONFLICT 129 129 I -> A (IN REF. 3). FT CONFLICT 163 163 D -> E (IN REF. 3). FT CONFLICT 183 183 A -> AMVEADLERAEERA (IN REF. 2). FT CONFLICT 199 199 V -> L (IN REF. 2). FT CONFLICT 214 214 S -> A (IN REF. 2). SQ SEQUENCE 285 AA; 32761 MW; 87AA353E34633901 CRC64; MDAIKKKMQA MKVDKDGALE RALVCEQEAR DANTRAEKAE EEARQLQKKI QTVENELDQT QEALTLVTGK LEEKNKALQN AESEVAALNR RIQLLEEDLE RSEERLGSAT AKLSEASQAA DESERARKIL ENRALADEER MDALENQLKE ARFLAEEADK KYDEVARKLA MVEADLERAE ERAEQGENKI VELEEELRVV GNNLKSLEVS EEKSNQREEE YKNQIKTLNT RLKEAEARAE FAERSVQKLQ KEVDRLEDDL VLEKERYKDI GDDLDTAFVE LILKE // ID TPM2_DROME STANDARD; PRT; 284 AA. AC P09491; P09490; Q24408; Q24427; Q24428; Q8SZ65; Q9VF95; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tropomyosin 2 (Tropomyosin I). GN TM2 OR TMI OR CG4843. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS EMBRYONIC AND THORACIC). RC TISSUE=Embryo, Larva, and Pupae; RX MEDLINE=84205681; PubMed=6202423; RA Karlik C.C., Mahaffey J.W., Coutu M.D., Fyrberg E.A.; RT "Organization of contractile protein genes within the 88F subdivision RT of the D. melanogaster third chromosome."; RL Cell 37:469-481(1984). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS EMBRYONIC AND THORACIC). RX MEDLINE=86085920; PubMed=3079761; RA Basi G.S., Storti R.V.; RT "Structure and DNA sequence of the tropomyosin I gene from Drosophila RT melanogaster."; RL J. Biol. Chem. 261:817-827(1986). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM EMBRYONIC). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 258-284 FROM N.A. (ISOFORM EMBRYONIC). RX MEDLINE=85215579; PubMed=4000944; RA Boardman M., Basi G.S., Storti R.V.; RT "Multiple polyadenylation sites in a Drosophila tropomyosin gene are RT used to generate functional mRNAs."; RL Nucleic Acids Res. 13:1763-1776(1985). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Thoracic; Synonyms=127, t; CC IsoId=P09491-1; Sequence=Displayed; CC Name=Embryonic; Synonyms=129, A, B, e; CC IsoId=P09491-2; Sequence=VSP_006616; CC -!- DOMAIN: THE MOLECULE IS IN A COILED COIL STRUCTURE. THE SEQUENCE CC EXHIBITS A PROMINENT SEVEN-RESIDUES PERIODICITY. CC -!- SIMILARITY: BELONGS TO THE TROPOMYOSIN FAMILY. CC -!- CAUTION: REF.6 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K02622; AAA28970.1; -. DR EMBL; K02623; AAA28971.1; -. DR EMBL; K02622; AAA28971.1; JOINED. DR EMBL; K03277; AAA28973.1; -. DR EMBL; K03277; AAA28974.1; -. DR EMBL; AE003708; AAN13652.1; -. DR EMBL; AY071087; AAL48709.1; -. DR EMBL; X02220; CAA26142.1; ALT_SEQ. DR PIR; A25624; A25624. DR PIR; B25624; B25624. DR FlyBase; FBgn0004117; Tm2. DR InterPro; IPR000533; Tropomyosin. DR Pfam; PF00261; Tropomyosin; 1. DR PRINTS; PR00194; TROPOMYOSIN. DR PROSITE; PS00326; TROPOMYOSIN; 1. KW Muscle protein; Coiled coil; Repeat; Alternative splicing; KW Multigene family. FT VARSPLIC 259 284 RLFNEKEKYKAICDDLDQTFAELTGY -> ELGINKDRYKS FT LADEMDSTFAELAGY (in isoform Embryonic). FT /FTId=VSP_006616. FT CONFLICT 11 11 M -> V (IN REF. 1). FT CONFLICT 88 88 Q -> L (IN REF. 1). FT CONFLICT 95 95 I -> T (IN REF. 1). FT CONFLICT 255 255 R -> D (IN REF. 1). SQ SEQUENCE 284 AA; 32981 MW; 07AD03FDD304EA5F CRC64; MDAIKKKMQA MKLEKDNAID KADTCENQAK DANSRADKLN EEVRDLEKKF VQVEIDLVTA KEQLEKANTE LEEKEKLLTA TESEVATQNR KVQQIEEDLE KSEERSTTAQ QKLLEATQSA DENNRMCKVL ENRSQQDEER MDQLTNQLKE ARMLAEDADT KSDEVSRKLA FVEDELEVAE DRVRSGESKI MELEEELKVV GNSLKSLEVS EEKANQRVEE FKREMKTLSI KLKEAEQRAE HAEKQVKRLQ KEVDRLEDRL FNEKEKYKAI CDDLDQTFAE LTGY // ID TPM4_DROME STANDARD; PRT; 518 AA. AC P49455; P49456; Q24425; Q24426; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tropomyosin 1, isoforms 33/34 (Tropomyosin II). GN TM1 OR TMII. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 33 AND 34). RC TISSUE=Embryo, and Pupae; RX MEDLINE=89127197; PubMed=2851721; RA Hanke P.D., Storti R.V.; RT "The Drosophila melanogaster tropomyosin II gene produces multiple RT proteins by use of alternative tissue-specific promoters and RT alternative splicing."; RL Mol. Cell. Biol. 8:3591-3602(1988). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 33 AND 34). RC STRAIN=Oregon-R; TISSUE=Pupae; RX MEDLINE=87064486; PubMed=3097506; RA Karlik C.C., Fyrberg E.A.; RT "Two Drosophila melanogaster tropomyosin genes: structural and RT functional aspects."; RL Mol. Cell. Biol. 6:1965-1973(1986). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist; CC Name=33; Synonyms=9C; CC IsoId=P49455-1; Sequence=Displayed; CC Name=Muscle; Synonyms=9D; CC IsoId=P06754-1; Sequence=External; CC Name=Non-muscle; Synonyms=Cytoskeletal; CC IsoId=P06754-2; Sequence=External; CC Name=9A; CC IsoId=P06754-3; Sequence=External; CC Name=34; Synonyms=9B; CC IsoId=P49455-2; Sequence=VSP_006623, VSP_006624, VSP_006625; CC -!- TISSUE SPECIFICITY: BOTH ISOFORMS ARE ONLY EXPRESSED IN INDIRECT CC FLIGHT MUSCLES. CC -!- DEVELOPMENTAL STAGE: BOTH ISOFORMS ARE EXPRESSED DURING PUPAL AND CC ADULT STAGES. CC -!- DOMAIN: THE MOLECULE IS IN A COILED COIL STRUCTURE. THE SEQUENCE CC EXHIBITS A PROMINENT SEVEN-RESIDUES PERIODICITY. CC -!- SIMILARITY: BELONGS TO THE TROPOMYOSIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76208; CAA53800.1; -. DR EMBL; X76208; CAA53801.1; -. DR EMBL; K02620; AAA28967.1; ALT_SEQ. DR EMBL; L00355; AAA28967.1; JOINED. DR EMBL; L00356; AAA28967.1; JOINED. DR EMBL; L00357; AAA28967.1; JOINED. DR EMBL; L00358; AAA28967.1; JOINED. DR EMBL; L00359; AAA28967.1; JOINED. DR EMBL; L00360; AAA28967.1; JOINED. DR EMBL; L00362; AAA28967.1; JOINED. DR EMBL; M12840; AAA28967.1; JOINED. DR EMBL; K02621; AAA28968.1; -. DR EMBL; M12840; AAA28968.1; JOINED. DR EMBL; L00355; AAA28968.1; JOINED. DR EMBL; L00356; AAA28968.1; JOINED. DR EMBL; L00357; AAA28968.1; JOINED. DR EMBL; L00358; AAA28968.1; JOINED. DR EMBL; L00359; AAA28968.1; JOINED. DR EMBL; L00360; AAA28968.1; JOINED. DR EMBL; L00362; AAA28968.1; JOINED. DR FlyBase; FBgn0003721; Tm1. DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP. DR InterPro; IPR000533; Tropomyosin. DR Pfam; PF00261; Tropomyosin; 1. DR PRINTS; PR00194; TROPOMYOSIN. DR PROSITE; PS00326; TROPOMYOSIN; 1. KW Muscle protein; Cytoskeleton; Actin-binding; Coiled coil; KW Alternative splicing; Multigene family. FT DOMAIN 14 267 COILED COIL (POTENTIAL). FT DOMAIN 287 518 ALA/PRO-RICH. FT VARSPLIC 259 293 DLIVEKERYCMIGDSLDEAFVDLIKGLEPFWNPRN -> EM FT IKEIEHYALVGDQLDWTFVEMMGMPPFYNERY (in FT isoform 34). FT /FTId=VSP_006623. FT VARSPLIC 300 367 KLPTPTPEELAAMEEARAAAEAAAAAEAEAAEAAAAAGEAG FT ADGAPAAPGEEKAPAKEPTPPKEPTPP -> ELTEEEKAAL FT EAAAIAEKARAEELAALGEEAGAEAGEGGAPAEGAAPGEPG FT AATEPGVEAPPAEPERIPT (in isoform 34). FT /FTId=VSP_006624. FT VARSPLIC 391 518 KNYEPPPPGSEPEPVPAAEGEAAPAAEGAAPPAEGAAPPAE FT GAVPPADGAAPPAEGAAPAAEGAAPPADGAAPPAEAAAAPA FT DAAAPAAEAAPAEAPAAEATAAEAPPAEAAPAEAAPAAAEG FT EAPPA -> RNAEPGDFAPPAEAAPAEGAPPAEGAPAAEGA FT APAEGAPAAEGAPPAEGAPAPAPAEGEAAPPAPAAEGDAAA FT APPPPPAEGEAAPAPAEGEAPPAPPAEAAPAAEAPPA (in FT isoform 34). FT /FTId=VSP_006625. FT CONFLICT 106 114 LGSATAKLS -> SASAIQLAA (IN REF. 2). FT CONFLICT 119 119 A -> S (IN REF. 2). FT CONFLICT 183 183 A -> AMVEADLERAEERA (IN REF. 2). FT CONFLICT 199 199 V -> L (IN REF. 2). FT CONFLICT 503 503 P -> A (IN REF. 2; AAA28968). SQ SEQUENCE 518 AA; 54558 MW; 153D0872CF9DB6EA CRC64; MDAIKKKMQA MKVDKDGALE RALVCEQEAR DANTRAEKAE EEARQLQKKI QTVENELDQT QEALTLVTGK LEEKNKALQN AESEVAALNR RIQLLEEDLE RSEERLGSAT AKLSEASQAA DESERARKIL ENRALADEER MDALENQLKE ARFLAEEADK KYDEVARKLA MVEADLERAE ERAEQGENKI VELEEELRVV GNNLKSLEVS EEKANQREEE YKNQIKTLNT RLKEAEARAE FAERSVQKLQ KEVDRLEDDL IVEKERYCMI GDSLDEAFVD LIKGLEPFWN PRNPKPPTPK LPTPTPEELA AMEEARAAAE AAAAAEAEAA EAAAAAGEAG ADGAPAAPGE EKAPAKEPTP PKEPTPPPPP PPPFEYSIDL PPEGAEVPYV KNYEPPPPGS EPEPVPAAEG EAAPAAEGAA PPAEGAAPPA EGAVPPADGA APPAEGAAPA AEGAAPPADG AAPPAEAAAA PADAAAPAAE AAPAEAPAAE ATAAEAPPAE AAPAEAAPAA AEGEAPPA // ID TRA2_DROME STANDARD; PRT; 264 AA. AC P19018; Q9V734; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transformer-2 sex-determining protein. GN TRA2 OR TRA-2 OR CG10128. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RX MEDLINE=89077531; PubMed=3144434; RA Amrein H., Gorman M., Noethiger R.; RT "The sex-determining gene tra-2 of Drosophila encodes a putative RNA RT binding protein."; RL Cell 55:1025-1035(1988). RN [2] RP ERRATUM. RA Amrein H., Gorman M., Noethiger R.; RL Cell 58:420-420(1989). RN [3] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=91006062; PubMed=2120049; RA Amrein H., Maniatis T., Noethiger R.; RT "Alternatively spliced transcripts of the sex-determining gene tra-2 RT of Drosophila encode functional proteins of different size."; RL EMBO J. 9:3619-3629(1990). RN [4] RP SEQUENCE FROM N.A., FUNCTION, AND ALTERNATIVE SPLICING. RC TISSUE=Imaginal disks; RX MEDLINE=90337316; PubMed=2116360; RA Mattox W., Palmer M.J., Baker B.S.; RT "Alternative splicing of the sex determination gene transformer-2 is RT sex-specific in the germ line but not in the soma."; RL Genes Dev. 4:789-805(1990). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [7] RP SEQUENCE FROM N.A. (ISOFORM TMAJ). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [8] RP SEQUENCE OF 9-264 FROM N.A., AND FUNCTION. RX MEDLINE=89168430; PubMed=2493992; RA Goralski T.J., Edstroem J.-E., Baker B.S.; RT "The sex determination locus transformer-2 of Drosophila encodes a RT polypeptide with similarity to RNA binding proteins."; RL Cell 56:1011-1018(1989). RN [9] RP IDENTIFICATION OF A TRA-2 BINDING SITE IN PRE-MRNA. RX MEDLINE=91235294; PubMed=1674449; RA Hedley M.L., Maniatis T.; RT "Sex-specific splicing and polyadenylation of dsx pre-mRNA requires a RT sequence that binds specifically to tra-2 protein in vitro."; RL Cell 65:579-586(1991). RN [10] RP INTERACTION WITH SR PROTEINS IN THE ENHANCER COMPLEX. RX MEDLINE=93327418; PubMed=8334698; RA Tian M., Maniatis T.; RT "A splicing enhancer complex controls alternative splicing of RT doublesex pre-mRNA."; RL Cell 74:105-114(1993). RN [11] RP CHARACTERIZATION OF STRUCTURAL DOMAINS, AND MUTAGENESIS. RX MEDLINE=94170373; PubMed=8124712; RA Amrein H., Hedley M.L., Maniatis T.; RT "The role of specific protein-RNA and protein-protein interactions in RT positive and negative control of pre-mRNA splicing by Transformer 2."; RL Cell 76:735-746(1994). RN [12] RP IDENTIFICATION OF A PURINE-RICH ENHANCER IN THE ENHANCER COMPLEX. RX MEDLINE=95172379; PubMed=7867927; RA Lynch K.W., Maniatis T.; RT "Synergistic interactions between two distinct elements of a regulated RT splicing enhancer."; RL Genes Dev. 9:284-293(1995). CC -!- FUNCTION: REQUIRED FOR FEMALE SEX DETERMINATION IN SOMATIC CELLS CC AND FOR SPERMATOGENESIS IN MALE GERM CELLS. POSITIVE REGULATOR OF CC FEMALE-SPECIFIC SPLICING AND/OR POLYADENYLATION OF DOUBLESEX(DSX) CC PRE-MRNA. SPLICING REQUIRES AN ENHANCER COMPLEX, DSXRE (DSX REPEAT CC ELEMENT: WHICH CONTAINS SIX COPIES OF A 13-NUCLEOTIDE REPEAT AND A CC PURINE-RICH ENHANCER (PRE)). DSXRE IS FORMED THROUGH COOPERATIVE CC INTERACTIONS BETWEEN TRA, TRA2 AND THE SR PROTEINS, AND THESE CC INTERACTIONS REQUIRE BOTH THE REPEAT SEQUENCES AND PRE. PRE IS CC REQUIRED FOR SPECIFIC BINDING OF TRA2 TO THE DSXRE. PROTEIN-RNA CC AND PROTEIN-PROTEIN INTERACTIONS ARE INVOLVED IN TRA-2 DEPENDENT CC ACTIVATION AND REPRESSION OF ALTERNATIVE SPLICING. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Tmaj; Synonyms=Major, A; CC IsoId=P19018-1; Sequence=Displayed; CC Name=Tmin; Synonyms=Minor, B; CC IsoId=P19018-2; Sequence=VSP_005901; CC Name=MsTmaj; Synonyms=C; CC IsoId=P19018-3; Sequence=VSP_005900; CC Name=MsTmin; Synonyms=D; CC IsoId=P19018-4; Sequence=VSP_005902; CC -!- TISSUE SPECIFICITY: ISOFORMS TMAJ AND TMIN ARE EXPRESSED IN MALES CC AND FEMALES. ISOFORMS MSTMAJ AND MSTMIN ARE PRESENT ONLY IN MALE CC GERM CELLS. CC -!- DOMAIN: THE RS2 (ARG/SER-RICH DOMAIN 2) AND RNP-CS CC (RIBONUCLEOPROTEIN CONSENSUS SEQUENCE) DOMAINS ARE REQUIRED FOR CC BOTH MALE STERILITY AND FEMALE-SPECIFIC DSX SPLICING BUT THE RS1 CC DOMAIN IS DISPENSABLE. CC -!- PTM: EXTENSIVELY PHOSPHORYLATED ON SERINE RESIDUES IN THE RS CC DOMAIN (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -!- SIMILARITY: BELONGS TO THE SR FAMILY OF SPLICING FACTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23633; AAA28953.1; -. DR EMBL; X57484; CAA40722.1; -. DR EMBL; M30939; AAA28954.1; -. DR EMBL; M30939; AAA28955.1; -. DR EMBL; M30939; AAA28956.1; -. DR EMBL; M30939; AAA28957.1; -. DR EMBL; M76381; AAA69686.1; -. DR EMBL; AE003814; AAF58232.2; -. DR EMBL; AE003814; AAM68558.1; -. DR EMBL; AE003814; AAM68559.1; -. DR EMBL; AE003814; AAM68560.1; -. DR EMBL; AY058768; AAL13997.1; -. DR EMBL; J03155; AAA62771.1; -. DR PIR; A32373; A32373. DR PIR; D35846; D35846. DR PIR; S12003; A31638. DR FlyBase; FBgn0003742; tra2. DR GO; GO:0003723; F:RNA binding; NAS. DR GO; GO:0030237; P:female sex determination; IMP. DR GO; GO:0000003; P:reproduction; IMP. DR GO; GO:0000245; P:spliceosome assembly; NAS. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; 1. KW Sexual differentiation; Spermatogenesis; RNA-binding; mRNA splicing; KW Alternative splicing; Phosphorylation. FT DOMAIN 21 90 ARG/SER-RICH (RS1 DOMAIN). FT DOMAIN 97 175 RNA-BINDING (RRM). FT DOMAIN 176 196 LINKER. FT DOMAIN 197 264 ARG/SER-RICH (RS2 DOMAIN). FT VARSPLIC 1 85 Missing (in isoform MsTmaj). FT /FTId=VSP_005900. FT VARSPLIC 2 39 Missing (in isoform Tmin). FT /FTId=VSP_005901. FT VARSPLIC 134 264 TQRSRGFCFIYFEKLSDARAAKDSCSGIEVDGRRIRVDFSI FT TQRAHTPTPGVYLGRQPRGKAPRSFSPRRGRRVYHDRSASP FT YDNYRDRYDYRNDRYDRNLRRSPSRNRYTRNRSYSRSRSPQ FT LRRTSSRY -> INP (in isoform MsTmin). FT /FTId=VSP_005902. FT MUTAGEN 11 82 MISSING: IN D2; GREATLY REDUCED FEMALE- FT SPECIFIC DSX SPLICING. FT MUTAGEN 49 82 MISSING: IN D1; GREATLY REDUCED FEMALE- FT SPECIFIC DSX SPLICING, RETAINS MALE FT FERTILITY. FT MUTAGEN 113 123 MISSING: IN A36; LOSS OF FEMALE-SPECIFIC FT DSX SPLICING; AND MALE FERTILITY. FT MUTAGEN 138 138 R->L: IN PM1; LOSS OF FEMALE-SPECIFIC DSX FT SPLICING; AND MALE FERTILITY. FT MUTAGEN 140 140 F->A: IN PM2; NO FEMALE-SPECIFIC DSX FT SPLICING; SOME LOW MALE FERTILITY. FT MUTAGEN 151 151 A->V: IN TS1; LITTLE FEMALE-SPECIFIC DSX FT SPLICING, LOSS OF MALE FERTILITY AND FT TEMPERATURE-SENSITIVE PHENOTYPE. FT MUTAGEN 172 264 MISSING: IN D5; LOSS OF FEMALE-SPECIFIC FT DSX SPLICING AND MALE FERTILITY. FT MUTAGEN 173 173 S->F: IN A15, LOSS OF FEMALE-SPECIFIC DSX FT SPLICING AND MALE FERTILITY. FT MUTAGEN 173 173 S->A: IN PM3; GREATLY REDUCED FEMALE- FT SPECIFIC DSX SPLICING, RETAINS MALE FT FERTILITY AND TEMPERATURE-SENSITIVE FT PHENOTYPE. FT MUTAGEN 173 173 S->T: IN PM4; LOSS OF FEMALE-SPECIFIC DSX FT SPLICING, RETAINS MALE FERTILITY AND FT TEMPERATURE-SENSITIVE PHENOTYPE. FT MUTAGEN 181 181 P->S: IN TS2; TEMPERATURE-SENSITIVE FT PHENOTYPE. FT MUTAGEN 205 264 MISSING: IN D4; LOSS OF FEMALE-SPECIFIC FT DSX SPLICING, GREATLY REDUCED MALE FT FERTILITY. FT MUTAGEN 236 264 MISSING: IN D3; GREATLY REDUCED FEMALE- FT SPECIFIC DSX SPLICING, RETAINS MALE FT FERTILITY. SQ SEQUENCE 264 AA; 31031 MW; 3BECBD694B0817B3 CRC64; MDREPLSSGR LHCSARYKHK RSASSSSAGT TSSGHKDRRS DYDYCGSRRH QRSSSRRRSR SRSSSESPPP EPRHRSGRSS RDRERMHKSR EHPQASRCIG VFGLNTNTSQ HKVRELFNKY GPIERIQMVI DAQTQRSRGF CFIYFEKLSD ARAAKDSCSG IEVDGRRIRV DFSITQRAHT PTPGVYLGRQ PRGKAPRSFS PRRGRRVYHD RSASPYDNYR DRYDYRNDRY DRNLRRSPSR NRYTRNRSYS RSRSPQLRRT SSRY // ID TRE1_DROME STANDARD; PRT; 392 AA. AC Q9NDM2; Q95NV3; Q95NV9; Q9NKZ6; Q9W498; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Gustatory receptor Trehalose 1 (Trehalose receptor 1). GN TRE1 OR CG3171. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Labial palps; RX MEDLINE=20342437; PubMed=10884225; RA Ishimoto H., Matsumoto A., Tanimura T.; RT "Molecular identification of a taste receptor gene for trehalose in RT Drosophila."; RL Science 289:116-119(2000). RN [2] RP SEQUENCE FROM N.A., FUNCTION, AND VARIANTS. RC STRAIN=HG84, Shanghai, Singapore, Tananarive, w cv, and w cx; RX MEDLINE=21450540; PubMed=11566105; RA Ueno K., Ohta M., Morita H., Mikuni Y., Nakajima S., Yamamoto K., RA Isono K.; RT "Trehalose sensitivity in Drosophila correlates with mutations in and RT expression of the gustatory receptor gene Gr5a."; RL Curr. Biol. 11:1451-1455(2001). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TASTE RECEPTOR SENSITIVE TO TREHALOSE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED UBIQUITOUSLY IN ADULT TISSUES. CC HIGHEST EXPRESSION LEVELS ARE SEEN IN TASTE SENSORY CELLS OF THE CC LABELLAR CHEMOSENSORY NEURONS AND TARSI. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYO TO ADULT CC STAGES. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB034204; BAA95353.1; -. DR EMBL; AB042625; BAA96500.1; -. DR EMBL; AB066613; BAB68237.1; -. DR EMBL; AB066614; BAB68238.1; -. DR EMBL; AB066615; BAB68239.1; -. DR EMBL; AB066616; BAB68240.1; -. DR EMBL; AB066617; BAB68241.1; -. DR EMBL; AB066618; BAB68242.1; -. DR EMBL; AE003435; AAF46059.2; -. DR EMBL; AY070980; AAL48602.1; -. DR FlyBase; FBgn0046687; Tre1. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008527; F:taste receptor activity; IMP. DR GO; GO:0001582; P:sweet taste perception; IMP. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Receptor; G-protein coupled receptor; Transmembrane; Glycoprotein; KW Polymorphism; Multigene family. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 60 1 (POTENTIAL). FT DOMAIN 61 73 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 74 94 2 (POTENTIAL). FT DOMAIN 95 110 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 111 131 3 (POTENTIAL). FT DOMAIN 132 156 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 157 177 4 (POTENTIAL). FT DOMAIN 178 202 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 203 223 5 (POTENTIAL). FT DOMAIN 224 268 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 269 289 6 (POTENTIAL). FT DOMAIN 290 302 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 303 323 7 (POTENTIAL). FT DOMAIN 324 392 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 298 298 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 7 7 M -> MDMGMGM (IN STRAINS HG84, SINGAPORE FT AND W CV). FT VARIANT 12 12 F -> I (IN STRAINS HG84, SINGAPORE FT AND W CV). FT VARIANT 348 348 L -> M (IN STRAINS SHANGHAI AND FT TANANARIVE). FT CONFLICT 226 226 L -> P (IN REF. 1). SQ SEQUENCE 392 AA; 43843 MW; 41A58C69479BBFDA CRC64; MDQDMGMATG YFQDADMQMD EPAAATQSIY PHSATLFAAI SACVFVTIGV LGNLITLLAL LKSPTIREHA TTAFVISLSI SDLLFCSFSL PLTAVRFFQE SWTFGTTLCK IFPVIFYGNV AVSLLSMVGI TLNRYILIAC HSRYSQIYKP KFITLQLLFV WAVSFLLLLP PILGIWGEMG LDEATFSCTI LKKEGRSIKK TLFVIGFLLP CLVIIVSYSC IYITVLHQKK KIRNHDNFQI AAAKGSSSSG GGSYMTTTCT RKAREDNRLT VMMVTIFLCF LVCFLPLMLA NVVDDERNTS YPWLHIIASV MAWASSVINP IIYAASNRNY RVAYYKIFAL LKFWGEPLSP MPSRNYHQSK NSKELSGVIR STPLFHAVQK NSINQMCQTY SV // ID TREA_DROME STANDARD; PRT; 596 AA. AC Q9W2M2; Q961P0; Q9W2M1; Q9W2M3; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trehalase precursor (EC 3.2.1.28) (Alpha,alpha-trehalase) DE (Alpha,alpha-trehalose glucohydrolase). GN TREH OR CG9364. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: ALPHA,ALPHA-TREHALOSE + H(2)O = 2 D-GLUCOSE. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=C, F; CC IsoId=Q9W2M2-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; Synonyms=A, D; CC IsoId=Q9W2M2-2; Sequence=VSP_007735; CC Note=No experimental confirmation available; CC -!- SIMILARITY: BELONGS TO FAMILY 37 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003452; AAM68194.1; -. DR EMBL; AE003452; AAF46667.2; -. DR EMBL; AY051466; AAK92890.1; -. DR FlyBase; FBgn0003748; Treh. DR GO; GO:0046658; C:extrinsic to plasma membrane, GPI-anchored; ISS. DR GO; GO:0004555; F:alpha,alpha-trehalase activity; ISS. DR GO; GO:0005991; P:trehalose metabolism; ISS. DR InterPro; IPR001661; Glyco_hydro_37. DR Pfam; PF01204; Trehalase; 1. DR PRINTS; PR00744; GLHYDRLASE37. DR PROSITE; PS00927; TREHALASE_1; 1. DR PROSITE; PS00928; TREHALASE_2; FALSE_NEG. KW Hydrolase; Glycosidase; Glycoprotein; Signal; Alternative splicing. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 596 TREHALASE. FT CARBOHYD 288 288 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 293 293 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 359 359 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 451 451 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 516 516 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 53 MFKLPTISLLLVSWSCLVALSQAKTYSLPDLTTDYNNAIPV FT DEEEAQDPFASC -> MASPANPSSNHKMNGNG (in FT isoform 2). FT /FTId=VSP_007735. SQ SEQUENCE 596 AA; 67689 MW; 600D03B2087929EC CRC64; MFKLPTISLL LVSWSCLVAL SQAKTYSLPD LTTDYNNAIP VDEEEAQDPF ASCKIYCEGN LLHTIQTAVP KLFADSKTFV DMKLNNSPDK TLEDFNAMME AKNQTPSSED LKQFVDKYFS APGTELEKWT PTDWKENPSF LDLISDPDLK QWGVELNSIW KDLGRKMKDE VSKNPEYYSI IPVPNPVIVP GGRFIEFYYW DSYWIIRGLL YSQMFDTARG MIENFFSIVN RFGFIPNGGR VYYHGRSQPP LLTGMVKSYV DFTNDDKFAI DALDTLEHEF EFFVNNHNVT VKNHSLCVYR DSSSGPRPES YREDVETGEE FPTDEAKELH YSELKAGAES GMDFSSRWFI SPTGTNDGNR SALSTTSIVP VDLNAYLYWN AKLIAEFHSK AGNTKKVTEY ETKAEKLLLG IQEVLWNEEA GVWLDYDMIN QKPRDYYTPT NLSPLWVKAF NISESEKISA SVMAYIERNK LDSFPGGVPN TLSYTGEQWD APNVWAPMQY ILVEGLNNLN TPEAKNMSLK WATRWVKTNF AAFSKDRHMY EKYNADEFGV GGGGGEYEVQ TGFGWSNGVI IEWLSKHGRD ISIGSGCGCL AGEKRQ // ID TRFP_DROME STANDARD; PRT; 252 AA. AC P91641; Q9VLT4; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trf-proximal protein (Transcription mediator-related protein). GN TRFP OR TMR OR CG18780/CG18267. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RA Crowley T.E.; RT "Mutations near the Trf cluster cause a premeiotic defect in the RT Drosophila male germ line."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY REGULATE TRANSCRIPTION OF CLASS II GENES THROUGH CC ASSOCIATION WITH THE RNA POLYMERASE II-SRB COMPLEX (BY CC SIMILARITY). CC -!- SUBUNIT: COMPONENT OF AN RNA POLYMERASE II-SRB COMPLEX (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y10975; CAA71871.1; -. DR EMBL; AE003619; AAF52599.2; -. DR EMBL; BT003473; AAO39476.1; -. DR FlyBase; FBgn0013531; Trfp. KW Transcription regulation; Nuclear protein. FT CONFLICT 220 220 H -> Q (IN REF. 1). SQ SEQUENCE 252 AA; 27862 MW; 608AB5A43DAC52F5 CRC64; MGVTILQPYP LPEGKSGAHI IDQLSKRLLA LGATHAGQFL VDCETFISTP QPHNGAPGRA VHVLHNSEYP ASTFSIIDNG TGKQVAIVAD NIFDLLMLKM TNTFTSKKQT KIESRGARFE YGDFVIKLGS VTMMEHFKGI LIEIEYKSCV ILAYCWEMIR EMLQGFLGIA VNKDFPSYFA PQTIMTAMGQ QQLHAKHNDI FEPMDTVKQY LEQFTNYRKH VTLMGGMGSG PGSQQVGPNV HMSPAVAGLH RS // ID TRF_DROME STANDARD; PRT; 224 AA. AC Q27896; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE TBP-related factor. GN TRF OR CG7562. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Testis; RX MEDLINE=93156846; PubMed=8429912; RA Crowley T.E., Hoey T., Liu J.-K., Jan Y.N., Jan L.Y., Tjian R.; RT "A new factor related to TATA-binding protein has highly restricted RT expression patterns in Drosophila."; RL Nature 361:557-561(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ACTS AS A TRANSCRIPTION FACTOR. BINDS TO THE TATA BOX CC PROMOTER ELEMENT WHICH LIES CLOSE TO THE POSITION OF TRANSCRIPTION CC INITIATION. CC -!- FUNCTION: MAY BE ESSENTIAL FOR EMBRYONIC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: PRIMARY SPERMATOCYTES IN THE ADULT TESTIS AND CC IN A SUBSET OF CELLS IN THE DORSAL MEDIAL REGION OF THE EMBRYONIC CC CNS. CC -!- SIMILARITY: BELONGS TO THE TBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X70837; CAA50185.1; -. DR EMBL; X70838; CAA50186.1; -. DR EMBL; AE003619; AAF52600.1; -. DR EMBL; AY128483; AAM75076.1; -. DR PIR; S37740; S37740. DR HSSP; P20226; 1TGH. DR FlyBase; FBgn0010287; Trf. DR GO; GO:0005669; C:transcription factor TFIID complex; ISS. DR GO; GO:0016251; F:general RNA polymerase II transcription fac...; ISS. DR GO; GO:0006367; P:transcription initiation from Pol II promoter; ISS. DR InterPro; IPR000814; TFIID. DR Pfam; PF00352; TBP; 2. DR PRINTS; PR00686; TIFACTORIID. DR PROSITE; PS00351; TFIID; 2. KW Transcription regulation; DNA-binding; Nuclear protein; Repeat. FT REPEAT 51 127 1. FT REPEAT 141 218 2. SQ SEQUENCE 224 AA; 25455 MW; CA619BE4BA726460 CRC64; MQFHFKVADA ERDRDNVAAT SNAAANPHAA LQPQQPVALV EPKDAQHEIR LQNIVATFSV NCELDLKAIN SRTRNSEYSP KRFRGVIMRM HSPRCTALIF RTGKVICTGA RNEIEADIGS RKFARILQKL GFPVKFMEYK LQNIVATVDL RFPIRLENLN HVHGQFSSYE PEMFPGLIYR MVKPRIVLLI FVNGKVVFTG AKSRKDIMDC LEAISPILLS FRKT // ID TRH_DROME STANDARD; PRT; 958 AA. AC Q24119; Q24165; Q8SX13; Q9W0Q7; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trachealess protein. GN TRH OR CG6883. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3). RC TISSUE=Embryo; RX MEDLINE=96136712; PubMed=8557198; RA Wilk R., Weizman I., Shilo B.-Z.; RT "Trachealess encodes a bHLH-PAS protein that is an inducer of RT tracheal cell fates in Drosophila."; RL Genes Dev. 10:93-102(1996). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RC TISSUE=Embryo; RX MEDLINE=96136713; PubMed=8557189; RA Isaac D.D., Andrew D.J.; RT "Tubulogenesis in Drosophila: a requirement for the trachealess gene RT product."; RL Genes Dev. 10:103-117(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 77-958 FROM N.A. (ISOFORM 1). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: TRANSCRIPTION FACTOR, MASTER REGULATOR OF TRACHEAL CELL CC FATES IN THE EMBRYO, NECESSARY FOR THE DEVELOPMENT OF THE SALIVARY CC GLAND DUCT AND THE POSTERIOR SPIRACLES. IT MAY INDUCE A GENERAL CC FATE OF BRANCHED TUBULAR STRUCTURES OF EPITHELIAL ORIGIN. TGO/TRH CC HETERODIMERS ARE INVOLVED IN THE CONTROL OF BREATHLESS EXPRESSION. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. HETERODIMER WITH TGO. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=1; Synonyms=A; CC IsoId=Q24119-1; Sequence=Displayed; CC Name=2; CC IsoId=Q24119-2; Sequence=VSP_002161; CC Name=3; CC IsoId=Q24119-3; Sequence=VSP_002162; CC -!- TISSUE SPECIFICITY: TRACHEA, SALIVARY GLAND DUCTS, POSTERIOR CC SPIRACLES (FILZKOEPER PRIMORDIA) AND A SUBSET OF CELLS IN THE CNS. CC -!- DEVELOPMENTAL STAGE: DURING EMBRYOGENESIS, FIRST DETECTED IN THE CC TRACHEAL PLACODES AT STAGE 8, AND EXPRESSION CONTINUES THROUGHOUT CC EMBRYONIC AND LARVAL DEVELOPMENT. IN THE DEVELOPING SALIVARY CC GLAND, EXPRESSION IS OBSERVED IN THE ENTIRE GLAND AT STAGE 9 AND CC BY STAGE 12, EXPRESSION IS CONFINED TO THE SALIVARY DUCTS. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -!- SIMILARITY: CONTAINS 2 PAS (PER-ARNT-SIM) DIMERIZATION DOMAINS. CC -!- SIMILARITY: CONTAINS 1 PAS-ASSOCIATED C-TERMINAL (PAC) DOMAIN. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS CC IN POSITIONS 22 AND 34. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U33427; AAA96257.1; ALT_INIT. DR EMBL; U42699; AAA96754.1; ALT_FRAME. DR EMBL; AE003468; AAF47386.1; -. DR EMBL; AY094911; AAM11264.1; ALT_INIT. DR FlyBase; FBgn0003749; trh. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; ISS. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; ISS. DR GO; GO:0007431; P:salivary gland development; IMP. DR GO; GO:0007424; P:tracheal system development (sensu Insecta); IMP. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS_domain. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00989; PAS; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR PROSITE; PS50888; HLH; 1. DR PROSITE; PS50112; PAS; 2. KW Developmental protein; Nuclear protein; Transcription regulation; KW Repeat; DNA-binding; Alternative splicing. FT DNA_BIND 86 99 BASIC DOMAIN. FT DOMAIN 100 140 HELIX-LOOP-HELIX MOTIF. FT DOMAIN 174 244 PAS 1. FT DOMAIN 391 461 PAS 2. FT DOMAIN 465 508 PAC. FT DOMAIN 629 636 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 154 157 POLY-SER. FT DOMAIN 244 250 POLY-GLY. FT DOMAIN 251 254 POLY-SER. FT DOMAIN 255 264 POLY-GLY. FT DOMAIN 722 728 POLY-GLN. FT VARSPLIC 281 286 Missing (in isoform 2). FT /FTId=VSP_002161. FT VARSPLIC 328 356 Missing (in isoform 3). FT /FTId=VSP_002162. FT CONFLICT 78 78 P -> A (IN REF. 1). FT CONFLICT 250 250 G -> GG (IN REF. 2). FT CONFLICT 703 703 A -> T (IN REF. 1). FT CONFLICT 708 708 A -> P (IN REF. 1). FT CONFLICT 829 829 A -> V (IN REF. 1). SQ SEQUENCE 958 AA; 102241 MW; 8F9CF758F1370541 CRC64; MLPYQAAVAM DYAGYQRQPT PGHPGSHMAT MGSLGMPAVP FTHSWMVPTQ DLCAMPPYNK MTGHQQPPGA GMHAQQQPLE PGILELRKEK SRDAARSRRG KENYEFYELA KMLPLPAAIT SQLDKASIIR LTISYLKLRD FSGHGDPPWT REASSSSKLK SAAIRRSPAV DLFEQHQGTH ILQSLDGFAL AVAADGRFLY ISETVSIYLG LSQVEMTGSS IFDYIHQADH SEIADQLGLS LTSGGGGGGG SSSSGGGGGG AGGGMASPTS GASDDGSGTH GTNNPDVAAS MTQASTSGYK GYDRSFCVRM KSTLTKRGCH FKSSGYRASD ATSNCNNGNN ASNNAKNVKN PGSNYSVVLL LCKLRPQYTF SHSRKSQPPL LGMVALAIAL PPPSVHEIRL ECDMFVTRVN FDLRVAHCEP RVSDLLDYSP EDLVNKSLYS LCHAEDANRL RKSHSDLIEK GQVLTGYYRL MNKSGGYTWL QTCATVVCST KNADEQNIIC VNYVISNREN ENMILDCCQL EPSPDSIKHE EGLGNDKSSG SPGGDASGEG NSHLSAGDMK LNSPKTDSEG HSHRGRGRSA AASHGSSMNS LTMIKDSPTP LGVEIDSGVL PTTVATPVPA ATPPVQSTKR KRKTKASQHA EDQGQEQVIS EQPLPKLPTM EQRDQQPRSR LPSIVDEQPS SAADSAVKDL EQAMSKHLPS PAAVVSVAPP NTDFSADSLL KQQQQQQQLD PNEKSSTIQW IGTPYQQPPA PMPATALLRQ LYANRESVIR ATARQTPTGV GPGVFYGDQQ TGPLPTPPGS ESSYENQYLQ LHSAASGGHP GGQKTSADAF TNLVSTYGGY HSSIDYHNAM TPPSSVSPRD SNQPGKAAPV LASNGGYDYA PDPLRGQYAT SSGDVVPATL PLKPQASYTA TMHPSGSTTT EGGVTYSNLD QPQYFAPHSS FHLYHKGSPA SGWYSTPS // ID TRI_DROME STANDARD; PRT; 268 AA. AC P36188; Q9VWY1; Q9VWY2; Q9VWY3; Q9VWY4; DT 01-JUN-1994 (Rel. 29, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Troponin I (TNI) (Wings apart-A protein) (Heldup protein). GN WUPA OR HDP OR TNI OR CG7178. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 2 AND 9), AND FUNCTION. RC STRAIN=Canton-S; TISSUE=Embryo, and Larva; RX MEDLINE=91115093; PubMed=1899228; RA Barbas J.A., Galceran J., Krah-Jentgens I., de la Pompa J.L., RA Canal I., Pongs O., Ferrus A.; RT "Troponin I is encoded in the haplolethal region of the Shaker gene RT complex of Drosophila."; RL Genes Dev. 5:132-140(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 6). RC STRAIN=Oregon-R; TISSUE=Pupae; RX MEDLINE=91340840; PubMed=1908472; RA Beall C.J., Fyrberg E.; RT "Muscle abnormalities in Drosophila melanogaster heldup mutants are RT caused by missing or aberrant troponin-I isoforms."; RL J. Cell Biol. 114:941-951(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. (ISOFORM 8). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=93180788; PubMed=7680094; RA Barbas J.A., Galceran J., Torroja L., Prado A., Ferrus A.; RT "Abnormal muscle development in the heldup3 mutant of Drosophila RT melanogaster is caused by a splicing defect affecting selected RT troponin I isoforms."; RL Mol. Cell. Biol. 13:1433-1439(1993). CC -!- FUNCTION: TROPONIN I IS THE ATPASE INHIBITORY SUBUNIT OF TROPONIN CC IN THE THIN FILAMENT REGULATORY COMPLEX. INVOLVED IN THE CC DEVELOPMENT AND MAINTENANCE OF MUSCLE AND NERVOUS SYSTEM. MAY ALSO CC BE INVOLVED IN THE CYTOSKELETAL APPARATUS. CC -!- SUBUNIT: BINDS TO ACTIN AND TROPOMYOSIN. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Comment=Exon 3 is either present or absent, exon 6 has 4 CC mutually exclusive forms (6a1, 6a2, 6b1 and 6b2) and C-terminal CC exons 9 and 10 are mutually exclusive; CC Name=10; Synonyms=G; CC IsoId=P36188-1; Sequence=Displayed; CC Name=1; CC IsoId=P36188-2; Sequence=VSP_006626, VSP_006627, VSP_006630; CC Name=2; Synonyms=A; CC IsoId=P36188-3; Sequence=VSP_006626, VSP_006627; CC Name=3; CC IsoId=P36188-4; Sequence=VSP_006626, VSP_006628, VSP_006630; CC Name=4; Synonyms=B; CC IsoId=P36188-5; Sequence=VSP_006626, VSP_006628; CC Name=5; CC IsoId=P36188-6; Sequence=VSP_006626, VSP_006630; CC Name=6; Synonyms=C, F; CC IsoId=P36188-7; Sequence=VSP_006626; CC Name=7; CC IsoId=P36188-8; Sequence=VSP_006626, VSP_006629, VSP_006630; CC Name=8; Synonyms=D, E; CC IsoId=P36188-9; Sequence=VSP_006626, VSP_006629; CC Name=9; CC IsoId=P36188-10; Sequence=VSP_006630; CC -!- TISSUE SPECIFICITY: ALL ISOFORMS ARE EXPRESSED IN SOMATIC MUSCLE. CC ISOFORMS CONTAINING EXON 6A1 (ISOFORMS 1 AND 2) ARE EXPRESSED IN CC ALL MUSCLES BUT HIGHEST EXPRESSION IS IN ABDOMINAL MUSCLE AND CC SPLANCHNIC MUSCLE OF THE GUT. ISOFORMS CONTAINING EXON 6B1 CC (ISOFORMS 5, 6, 9 AND 10) ARE HIGHLY EXPRESSED IN THE TERGAL CC DEPRESSOR OF TROCHANTER (TDT) MUSCLE. CC -!- DEVELOPMENTAL STAGE: ISOFORMS CONTAINING EXON 3 (ISOFORM 9 AND CC ISOFORM 10) ARE EXPRESSED IN ADULTS. ISOFORMS CONTAINING EXON 6A1 CC (ISOFORMS 1 AND 2) ARE EXPRESSED AT ALL DEVELOPMENTAL STAGES. CC ISOFORMS CONTAINING EXON 6A2 (ISOFORMS 3 AND 4) ARE WEAKLY CC EXPRESSED IN EMBRYOS AND LARVAE AND VERY WEAKLY IN ADULTS. CC ISOFORMS CONTAINING EXON 6B1 (ISOFORMS 5, 6, 9 AND 10) ARE WEAKLY CC EXPRESSED IN LARVA AND INCREASE DURING METAMORPHOSIS. ISOFORMS CC CONTAINING EXON 6B2 (ISOFORMS 7 AND 8) ARE WEAKLY EXPRESSED IN CC EMBRYOS AND LARVAE AND AT A HIGHER LEVEL IN ADULTS. CC -!- SIMILARITY: BELONGS TO THE TROPONIN I FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58188; CAA41171.1; -. DR EMBL; X59376; CAA42020.1; -. DR EMBL; AE003507; AAF48802.2; -. DR EMBL; AE003507; AAF48803.2; -. DR EMBL; AE003507; AAF48804.2; -. DR EMBL; AE003507; AAF48805.2; -. DR EMBL; AE003507; AAN09458.1; -. DR EMBL; AY122145; AAM52657.1; -. DR PIR; A40547; A40547. DR PIR; B38594; B38594. DR FlyBase; FBgn0004028; wupA. DR GO; GO:0005861; C:troponin complex; NAS. DR GO; GO:0003779; F:actin binding; NAS. DR GO; GO:0007517; P:muscle development; IMP. DR GO; GO:0007399; P:neurogenesis; IMP. DR InterPro; IPR001978; Troponin. DR Pfam; PF00992; Troponin; 1. KW Muscle protein; Actin-binding; Acetylation; Methylation; KW Alternative splicing. FT INIT_MET 0 0 BY SIMILARITY. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT MOD_RES 200 200 METHYLATION (TRI-) (BY SIMILARITY). FT MOD_RES 204 204 METHYLATION (TRI-) (BY SIMILARITY). FT DOMAIN 161 170 TROPONIN T-INTERACTION (BY SIMILARITY). FT DOMAIN 188 201 ACTIN-BINDING (BY SIMILARITY). FT VARSPLIC 5 65 Missing (in isoform 1, isoform 2, isoform FT 3, isoform 4, isoform 5, isoform 6, FT isoform 7 and isoform 8). FT /FTId=VSP_006626. FT VARSPLIC 150 182 GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> DTLK FT SLIKQHYDRINKLEDQKYDLEYVVKRKDV (in isoform FT 1 and isoform 2). FT /FTId=VSP_006627. FT VARSPLIC 150 182 GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> DTIQ FT SVCKDYHSKILKLESEKYDFEYDVARKDY (in isoform FT 3 and isoform 4). FT /FTId=VSP_006628. FT VARSPLIC 150 182 GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> AELQ FT TICKQYWQRVYSLEGDKFDLEHVQKVKAQ (in isoform FT 7 and isoform 8). FT /FTId=VSP_006629. FT VARSPLIC 248 268 PDWSKGKPGDAKVKEEVEAEA -> IKDAAVLNKAKK (in FT isoform 1, isoform 3, isoform 5, isoform FT 7 and isoform 9). FT /FTId=VSP_006630. SQ SEQUENCE 268 AA; 29950 MW; 16C121C96200906F CRC64; ADDEKKAAAP AAAPAAAAKP AAPAAAPAAN GKAAPAANGK AAPAAAAAPA GPPKDPNDPK VKAEEAKKAK QAEIERKRAE VRKRMEEASK AKKAKKGFMT PERKKKLRLL LRKKAAEELK KEQERKAAER RRIIEERCGS PRNLSDASEG ELQEICEEYY ERMYICEGQK WDLEYEVRKK DWEINDLNAQ VNDLRGKFVK PALKKVSKYE NKFAKLQKKA AEFNFRNQLK VVKKKEFTLE EEEKEKKPDW SKGKPGDAKV KEEVEAEA // ID TRLC_DROME STANDARD; PRT; 264 AA. AC P36951; Q9W2W4; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transient receptor potential locus C protein precursor (GIP-like DE protein). GN GIP OR CG2227. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88042982; PubMed=3118483; RA Wong F., Yuh Z., Schaefer E.L., Roop B.C., Ally A.H.; RT "Overlapping transcription units in the transient receptor potential RT locus of Drosophila melanogaster."; RL Somat. Cell Mol. Genet. 13:661-669(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: BELONGS TO THE HYI FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18635; AAA28978.1; -. DR EMBL; AE003450; AAF46573.1; -. DR PIR; S29144; S29144. DR FlyBase; FBgn0011770; Gip. KW Signal. FT SIGNAL 1 14 POTENTIAL. FT CHAIN 15 264 TRANSIENT RECEPTOR POTENTIAL LOCUS C FT PROTEIN. SQ SEQUENCE 264 AA; 29093 MW; D469EAF11DF629B7 CRC64; MALKFAANLN FLFTERATSI AERIRLAHQN GFRAVEIPYP EGETSDVVSA VKETGVVVSL VNLAFDKSDD QLRFGSTSVP GSEKLFRSQL DATIDFARQV NCGKIHLTAG LFKGGQESDY TKTYTANLKI AADSLRASKM IGVIEPINKY AVPGYYMNSY SKAAGILADV AADNIQLLAD LYHLQHLHGN VSKTLEEYKA LIGHFQIAQV PHRHEPDVSG ELDYGFVFKA LQEFGYDGWI GCEYKPKTTT VEGLGWVSKL GYTL // ID TRPL_DROME STANDARD; PRT; 1124 AA. AC P48994; Q9V5B2; DT 01-FEB-1996 (Rel. 33, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transient-receptor-potential like protein. GN TRPL OR CG18345/CG1694. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=92232293; PubMed=1314616; RA Phillips A.M., Bull A.L., Kelly L.E.; RT "Identification of a Drosophila gene encoding a calmodulin-binding RT protein with homology to the trp phototransduction gene."; RL Neuron 8:631-642(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS CALMODULIN. SUGGESTED TO MEDIATE CALCIUM ENTRY. CC SEEMS TO FORM A LIGHT-SENSITIVE CALCIUM PERMEANT CHANNEL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN THE RHABDOMERIC CC MEMBRANES OF THE PHOTORECEPTOR CELLS. CC -!- SIMILARITY: BELONGS TO THE TRANSIENT RECEPTOR FAMILY. STRPC CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 ANK REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M88185; AAA28979.1; -. DR EMBL; AE003832; AAM68793.1; -. DR PIR; JH0588; JH0588. DR FlyBase; FBgn0005614; trpl. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0015075; F:ion transporter activity; NAS. DR GO; GO:0015279; F:store-operated calcium channel activity; NAS. DR GO; GO:0006811; P:ion transport; NAS. DR GO; GO:0009628; P:response to abiotic stimulus; IMP. DR InterPro; IPR002110; ANK. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR002153; Trans_receptor. DR InterPro; IPR004729; Trp_CaChannel. DR Pfam; PF00023; ank; 2. DR Pfam; PF00520; ion_trans; 1. DR PRINTS; PR01097; TRNSRECEPTRP. DR SMART; SM00248; ANK; 2. DR TIGRFAMs; TIGR00870; trp; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. KW Ionic channel; Transmembrane; Ion transport; Calcium channel; KW Calmodulin-binding; Vision; ANK repeat; Repeat. FT DOMAIN 1 340 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 341 361 POTENTIAL. FT DOMAIN 362 373 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 374 394 POTENTIAL. FT DOMAIN 395 431 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 432 452 POTENTIAL. FT DOMAIN 453 512 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 513 533 POTENTIAL. FT DOMAIN 534 548 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 549 569 POTENTIAL. FT DOMAIN 570 645 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 646 666 POTENTIAL. FT DOMAIN 667 1124 CYTOPLASMIC (POTENTIAL). FT REPEAT 78 107 ANK 1. FT REPEAT 152 181 ANK 2. FT DOMAIN 710 727 CALMODULIN-BINDING (POTENTIAL). FT DOMAIN 809 825 CALMODULIN-BINDING (POTENTIAL). FT CONFLICT 228 229 II -> SS (IN REF. 1). SQ SEQUENCE 1124 AA; 127749 MW; AF6323BA27626583 CRC64; MGRKKKLPTG VSSGVSHASS APKSVGGCCV PLGLPQPLLL EEKKFLLAVE RGDMPNVRRI LQKALRHQHI NINCMDPLGR RALTLAIDNE NLEMVELLVV MGVETKDALL HAINAEFVEA VELLLEHEEL IYKEGEPYSW QKVDINTAMF APDITPLMLA AHKNNFEILR ILLDRGAAVP VPHDIRCGCE ECVRLTAEDS LRHSLSRVNI YRALCSPSLI CLTSNDPIIT AFQLSWELRN LALTEQECKS EYMDLRRQCQ KFAVDLLDQT RTSNELAIIL NYDPQMSSYE PGDRMSLTRL VQAISYKQKK FVAHSNIQQL LSSIWYDGLP GFRRKSIVDK VICIAQVAVL FPLYCLIYMC APNCRTGQLM RKPFMKFLIH ASSYLFFLFI LILVSQRADD DFVRIFGTTR MKKELAEQEL RQRGQTPSKL ELIVVMYVIG FVWEEVQEIF AVGMKSYLRN MWNFIDFLRN SLYVSVMCLR AFAYIQQATE IARDPQMAYI PREKWHDFDP QLIAEGLFAA ANVFSALKLV HLFSINPHLG PLQISLGRMV IDIVKFFFIY TLVLFAFACG LNQLLWYFAA LEKSKCYVLP GGEADWGSHG DSCMKWRRFG NLFESSQSLF WASFGMVGLD DFELSGIKSY TRFWGLLMFG SYSVINVIVL LNLLIAMMSN SYAMIDEHSD TEWKFARTKL WMSYFEDSAT LPPPFNVLPS VKWVIRIFRK SSKTIDRQRS KKRKEQEQFS EYDNIMRSLV WRYVAAMHRK FENNPVSEDD INEVKSEINT MRYEMLEIFE NSGMDVSSAN KKERQPRPRR IKVWERRLMK GFQVAPVQNG CELDAFGNVN GQGEMQEIKV ESIPSKPAKE TAKERFQRVA RTVLLQSTTH KWNVVLRAAK DSQIGRCTKN ERKSLQNLGR AIEEAKRLIM LNPGCPSGRE SPIRIEFEDE KTSTLLELLN QISAEISDSE KPKIRPIWRP PLKTVPARAM AANNTRSLTA PELKISRKSS PAPTPTPTPG VSHTALSQFR NRELPLCPSK LIANSAPSAP TAPPKKSAPT APTPTYKPTT HAPFSVEGGN RENTRASDGV RSDNSNFDIH VVDLDEKGGH LGRDNVSDIS SIASTSPQRP KHRN // ID TRP_DROME STANDARD; PRT; 1275 AA. AC P19334; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Transient receptor potential protein. GN TRP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90180449; PubMed=2516726; RA Montell C., Rubin G.M.; RT "Molecular characterization of the Drosophila trp locus: a putative RT integral membrane protein required for phototransduction."; RL Neuron 2:1313-1323(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90148782; PubMed=2482778; RA Wong F., Schaefer E.L., Roop B.C., Lamendola J.N., Johnson-Seaton D., RA Shao D.; RT "Proper function of the Drosophila trp gene product during pupal RT development is important for normal visual transduction in the RT adult."; RL Neuron 3:81-94(1989). RN [3] RP SEQUENCE OF 1126-1275 FROM N.A. RX MEDLINE=88042982; PubMed=3118483; RA Wong F., Yuh Z.T., Schaefer E.L., Roop B.C., Ally A.H.; RT "Overlapping transcription units in the transient receptor potential RT locus of Drosophila melanogaster."; RL Somat. Cell Mol. Genet. 13:661-669(1987). CC -!- FUNCTION: REQUIRED FOR PHOTOTRANSDUCTION. SUGGESTED TO MEDIATE CC CALCIUM ENTRY. SEEMS TO FORM A LIGHT-SENSITIVE CALCIUM PERMEANT CC CHANNEL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN THE RHABDOMERIC CC MEMBRANES OF THE PHOTORECEPTOR CELLS. CC -!- SIMILARITY: BELONGS TO THE TRANSIENT RECEPTOR FAMILY. STRPC CC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 ANK REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M34394; AAA28976.1; -. DR EMBL; M21306; AAA56928.1; -. DR EMBL; M18634; AAA28977.1; -. DR FlyBase; FBgn0003861; trp. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0015279; F:store-operated calcium channel activity; NAS. DR GO; GO:0008377; P:light-induced release of calcium, from inte...; IDA. DR GO; GO:0009416; P:response to light; IMP. DR InterPro; IPR002110; ANK. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR002153; Trans_receptor. DR InterPro; IPR004729; Trp_CaChannel. DR Pfam; PF00023; ank; 2. DR Pfam; PF00520; ion_trans; 1. DR PRINTS; PR01097; TRNSRECEPTRP. DR SMART; SM00248; ANK; 2. DR TIGRFAMs; TIGR00870; trp; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. KW Ionic channel; Transmembrane; Ion transport; Calcium channel; KW Vision; ANK repeat; Repeat. FT DOMAIN 1 366 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 367 387 POTENTIAL. FT DOMAIN 388 390 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 391 411 POTENTIAL. FT DOMAIN 412 418 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 419 439 POTENTIAL. FT DOMAIN 440 450 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 451 471 POTENTIAL. FT DOMAIN 472 507 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 508 528 POTENTIAL. FT DOMAIN 529 541 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 542 562 POTENTIAL. FT DOMAIN 563 638 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 639 659 POTENTIAL. FT DOMAIN 660 1275 EXTRACELLULAR (POTENTIAL). FT REPEAT 69 98 ANK 1. FT REPEAT 143 172 ANK 2. FT CONFLICT 285 288 GQRQ -> ASSE (IN REF. 2). FT CONFLICT 326 329 RRKQ -> PQE (IN REF. 2). FT CONFLICT 365 374 KPFVKFITHS -> NPLSSSSRTP (IN REF. 2). FT CONFLICT 785 785 S -> N (IN REF. 2). SQ SEQUENCE 1275 AA; 142589 MW; 91CFCDD9896989B1 CRC64; MGSNTESDAE KALGSRLDYD LMMAEEYILS DVEKNFILSC ERGDLPGVKK ILEEYQGTDK FNINCTDPMN RSALISAIEN ENFDLMVILL EHNIEVGDAL LHAISEEYVE AVEELLQWEE TNHKEGQPYS WEAVDRSKST FTVDITPLIL AAHRNNYEIL KILLDRGATL PMPHDVKCGC DECVTSQTTD SLRHSQSRIN AYRALSASSL IALSSRDPVL TVFQLSWELK RLQAMESEFR AEYTEMRQMV QDFGTSLLDH ARTSMELEVM LNFNHEPSHD IWCLGQRQTL ERLKLAIRYK QKTFVAHPNV QQLLAAIWYD GLPGFRRKQA SQQLMDVVKL GCSFPIYSLK YILAPDSEGA KFMRKPFVKF ITHSCSYMFF LMLLGAASLR VVQITFELLA FPWMLTMLED WRKHERGSLP GPIELAIITY IMALIFEELK SLYSDGLFEY IMDLWNIVDY ISNMFYVTWI LCRATAWVIV HRDLWFRGID PYFPREHWHP FDPMLLSEGA FAAGMVFSYL KLVHIFSINP HLGPLQVSLG RMIIDIIKFF FIYTLVLFAF GCGLNQLLWY YAELEKNKCY HLHPDVADFD DQEKACTIWR RFSNLFETSQ SLFWASFGLV DLVSFDLAGI KSFTRFWALL MFGSYSVINI IVLLNMLIAM MSNSYQIISE RADTEWKFAR SQLWMSYFED GGTIPPPFNL CPNMKMLRKT LGRKRPSRTK SFMRKSMERA QTLHDKVMKL LVRRYITAEQ RRRDDYGITE DDIIEVRQDI SSLRFELLEI FTNNSWDVPD IEKKSQGVAR TTKGKVMERR ILKDFQIGFV ENLKQEMSES ESGRDIFSSL AKVIGRKKTQ KGDKDWNAIA RKNTFASDPI GSKRSSMQRH SQRSLRRKII EQANEGLQMN QTQLIEFNPN LGDVTRATRV AYVKFMRKKM AADEVSLADD EGAPNGEGEK KPLDASGSKK SITSGGTGGG ASMLAAAALR ASVKNVDEKS GADGKPGTMG KPTDDKKPGD DKDKQQPPKD SKPSAGGPKP GDQKPTPGAG APKPQAAGTI SKPGESQKKD APAPPTKPGD TKPAAPKPGE SAKPEAAAKK EESSKTEASK PAATNGAAKS AAPSAPSDAK PDSKLKPGAA GAPEATKATN GASKPDEKKS GPEEPKKAAG DSKPGDDAKD KDKKPGDDKD KKPGDDKDKK PADNNDKKPA DDKDKKPGDD KDKKPGDDKD KKPSDDKDKK PADDKDKKPA AAPLKPAIKV GQSSAAAGGE RGKSTVTGRM ISGWL // ID TRSF_DROME STANDARD; PRT; 197 AA. AC P11596; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Female-specific transformer protein. GN TRA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND FUNCTION. RX MEDLINE=87301717; PubMed=2441872; RA Boggs R.T., Gregor P., Idriss S., Belote J.M., McKeown M.; RT "Regulation of sexual differentiation in D. melanogaster via RT alternative splicing of RNA from the transformer gene."; RL Cell 50:739-747(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94283902; PubMed=8013913; RA Walthour C.S., Schaeffer S.W.; RT "Molecular population genetics of sex determination genes: the RT transformer gene of Drosophila melanogaster."; RL Genetics 136:1367-1372(1994). RN [3] RP CHARACTERIZATION OF RS DOMAIN. RX MEDLINE=92005712; PubMed=1655279; RA Li H., Bingham P.M.; RT "Arginine/serine-rich domains of the su(wa) and tra RNA processing RT regulators target proteins to a subnuclear compartment implicated in RT splicing."; RL Cell 67:335-342(1991). RN [4] RP INTERACTION WITH SR PROTEINS IN ENHANCER COMPLEX. RX MEDLINE=93327418; PubMed=8334698; RA Tian M., Maniatis T.; RT "A splicing enhancer complex controls alternative splicing of RT doublesex pre-mRNA."; RL Cell 74:105-114(1993). CC -!- FUNCTION: MEMBER OF THE REGULATORY PATHWAY CONTROLLING FEMALE CC SOMATIC SEXUAL DIFFERENTIATION, REGULATED BY SXL. ACTIVATES CC DSX FEMALE-SPECIFIC SPLICING BY PROMOTING THE FORMATION OF A CC SPLICING ENHANCER COMPLEX WHICH CONSISTS OF TRA, TRA2 AND SR CC PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR; SPECKLED SUBNUCLEAR COMPARTMENT. CC -!- DOMAIN: RS DOMAIN DIRECTS LOCALIZATION OF PROTEINS TO THE SPECKLED CC SUBNUCLEAR COMPARTMENT AND THE PURPOSE OF THIS LOCALIZATION IS TO CC ALLOW COLOCALIZATION AND CO-CONCENTRATION OF COMPONENTS OF THE CC SPLICING AND SPLICING REGULATORY MACHINERY TO PERMIT RELATIVELY CC HIGH RATES AND/OR EFFICIENCIES OF REACTION AND INTERACTION. CC -!- MISCELLANEOUS: THE SEXUAL REGULATION OF TRA OCCURS THROUGH A CC MECHANISM OF SEX-SPECIFIC ALTERNATIVE RNA SPLICING. THE NON-SEX- CC SPECIFIC RNA EXPRESSED IN MALES IS NOT TRANSLATED. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-3 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19465; AAA75341.1; -. DR EMBL; L19466; AAA75342.1; -. DR EMBL; L19467; AAA28958.1; -. DR EMBL; L19468; AAA28959.1; -. DR EMBL; L19469; AAA28960.1; -. DR EMBL; L19470; AAA28961.1; -. DR EMBL; L19618; AAA28962.1; -. DR EMBL; L19619; AAA28963.1; -. DR EMBL; L19620; AAA28964.1; -. DR EMBL; M17478; AAB59226.1; -. DR EMBL; L19464; AAA75340.1; -. DR PIR; A29648; A29648. DR FlyBase; FBgn0003741; tra. DR GO; GO:0018993; P:somatic sex determination; NAS. DR GO; GO:0000245; P:spliceosome assembly; NAS. KW Nuclear protein; Sexual differentiation. FT DOMAIN 15 125 ARG/SER-RICH (RS DOMAIN). SQ SEQUENCE 197 AA; 24134 MW; 10C0B7A6F0C1AF81 CRC64; MKMDADSSGT QHRDSRGSRS RSRREREYHG RSSERDSRKK EHKIPYFADE VREQDRLRRL RQRAHQSTRR TRSRSRSQSS IRESRHRRHR QRSRSRNRSR SRSSERKRRQ RSRSRSSERR RRQRSPHRYN PPPKIINYYV QVPPQDFYGM SGMQQSFGYQ RLPRPPPFPP APYRYRQRPP FIGVPRFGYR NAGRPPY // ID TRT_DROME STANDARD; PRT; 396 AA. AC P19351; DT 01-NOV-1990 (Rel. 16, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Troponin T, skeletal muscle (Upheld protein) (Intended thorax DE protein). GN UP OR INT. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Asynchronous muscle; RX MEDLINE=89141761; PubMed=2852258; RA Bullard B., Leonard K., Larkins A., Butcher G., Karlik C., RA Fyrberg E.A.; RT "Troponin of asynchronous flight muscle."; RL J. Mol. Biol. 204:621-637(1988). RN [2] RP REVISIONS, SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=91080155; PubMed=2124273; RA Fryberg E.A., Fryberg C.C., Beall C., Saville D.L.; RT "Drosophila melanogaster troponin-T mutations engender three distinct RT syndromes of myofibrillar abnormalities."; RL J. Mol. Biol. 216:657-675(1990). CC -!- FUNCTION: TROPONIN T IS THE TROPOMYOSIN-BINDING SUBUNIT OF CC TROPONIN, THE THIN FILAMENT REGULATORY COMPLEX WHICH CONFERS CC CALCIUM-SENSITIVITY TO STRIATED MUSCLE ACTOMYOSIN ATPASE ACTIVITY. CC -!- DISEASE: MUTATIONS IN TROPONIN-T ENGENDER THREE DISTINCT SYNDROMES CC OF MYOFIBRILLAR ABNORMALITIES. CC -!- SIMILARITY: BELONGS TO THE TROPONIN T FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54504; CAA38366.1; -. DR PIR; S13251; S13251. DR FlyBase; FBgn0004169; up. DR InterPro; IPR001978; Troponin. DR Pfam; PF00992; Troponin; 1. KW Muscle protein. FT DOMAIN 341 396 ASP/GLU-RICH (HIGHLY ACIDIC). SQ SEQUENCE 396 AA; 47333 MW; 3CAAA8AAA8943C23 CRC64; MSDDEEYTSE EEEVVEETRE ETKPPQTPAE GEGDPEFIKR QDQKRSDLDD QLKEYITEWR KQRSKEEDEL KKLKEKQAKR KVTRAEEEQK MAQRKKEEEE RRVREAEEKK QREIEEKAMR LEEAEKKRQA MLQAMKDKDK KGPNFTIAKK DAGVLGLSSA AMERNKTKEQ LEEEKKISLS FRIKPLAIEG FAEAKLREKA QELWELIVKL ETEKYDLEER QKRQDYDLKE LKERQKQQLR HKALKKGLDP EALTGKYPPK IQVASKYERR VDTRSYDDKK KLFEGGWDEI SKDSNEKIWN EKKEQYTGRQ KSKLPKWFGE RPGKKAGEPE TPEGEEDAKA DEDIVEDDEE VEEEVVEEED EEDEEDEEEE EEEEEEEEEE EEEEEEEEEE EEEEEE // ID TRUN_DROME STANDARD; PRT; 226 AA. AC Q24155; Q9VL09; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trunk protein precursor. GN TRK OR CG5619. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96033803; PubMed=7590233; RA Casanova J., Furriols M., McCormick C.A., Struhl G.; RT "Similarities between trunk and spatzle, putative extracellular RT ligands specifying body pattern in Drosophila."; RL Genes Dev. 9:2539-2544(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR ACTIVITY OF THE TOR RECEPTOR, COULD BE CC A LIGAND OF TOR. INVOLVED IN SPECIFYING TERMINAL BODY PATTERN. CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U41064; AAC46953.1; -. DR EMBL; AE003628; AAF52896.1; ALT_INIT. DR FlyBase; FBgn0003751; trk. DR GO; GO:0008358; P:maternal determination of anterior/posterio...; NAS. DR GO; GO:0007362; P:terminal region determination; IMP. KW Developmental protein; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 226 TRUNK PROTEIN. SQ SEQUENCE 226 AA; 26348 MW; 2CF1B5049C63521B CRC64; MKSQSELAIV LTWLAVLGTA QDDADYCAEL STQSLAKILG QAFNPRYMSI DPPGEPEEKS YHLGYKRSSY ELPFYADSDA ISVSHFPAWE TNHFALVEKK KEAPRSKSLR TRSAFMDRVG HPRIDGFKQR PWECSSKINW IDLGLNYFPR YIRSIECIAR KCWYDHFNCK PKSFTIKVLR RKTGSCIRIN DKLILITAEK FENDYTQLWI WEEIAVNFCC ECVMLY // ID TRX1_DROME STANDARD; PRT; 596 AA. AC P91938; Q961E3; Q9W3H2; Q9W3H3; DT 01-NOV-1997 (Rel. 35, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Thioredoxin reductase 1, mitochondrial precursor (EC 1.8.1.9) (TrxR- DE 1). GN TRXR-1 OR GR OR CG2151. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RX MEDLINE=97209518; PubMed=9056265; RA Candas M., Sohal R.S., Radyuk S.N., Klichko V.I., Orr W.C.; RT "Molecular organization of the glutathione reductase gene in RT Drosophila melanogaster."; RL Arch. Biochem. Biophys. 339:323-334(1997). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS A AND D), FUNCTION, AND MUTAGENESIS OF RP CYS-594 AND CYS-595. RX MEDLINE=21108315; PubMed=11158675; RA Kanzok S.M., Fechner A., Bauer H., Ulschmid J.K., Muller H.M., RA Botella-Munoz J., Schneuwly S., Schirmer R., Becker K.; RT "Substitution of the thioredoxin system for glutathione reductase in RT Drosophila melanogaster."; RL Science 291:643-646(2001). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE OF 1-447 FROM N.A. (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=21417178; PubMed=11525742; RA Missirlis F., Phillips J.P., Jackle H.; RT "Cooperative action of antioxidant defense systems in Drosophila."; RL Curr. Biol. 11:1272-1277(2001). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX MEDLINE=21909553; PubMed=11796729; RA Missirlis F., Ulschmid J.K., Hirosawa-Takamori M., Groenke S., RA Schaefer U., Becker K., Phillips J.P., Jaeckle H.; RT "Mitochondrial and cytoplasmic thioredoxin reductase variants encoded RT by a single Drosophila gene are both essential for viability."; RL J. Biol. Chem. 277:11521-11526(2002). RN [8] RP ENZYME ACTIVITY. RX MEDLINE=22001321; PubMed=11877442; RA Bauer H., Kanzok S.M., Schirmer R.H.; RT "Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin RT peroxidase-1 from Drosophila melanogaster: isolation and RT characterization of a second thioredoxin in D.melanogaster and RT evidence for distinct biological functions of Trx-1 and Trx-2."; RL J. Biol. Chem. 277:17457-17463(2002). CC -!- FUNCTION: THIOREDOXIN SYSTEM IS A MAJOR PLAYER IN GLUTATHIONE CC METABOLISM, DUE TO THE DEMONSTRATED ABSENCE OF A GLUTATHIONE CC REDUCTASE. FUNCTIONALLY INTERACTS WITH THE SOD/CAT REACTIVE CC OXIDATION SPECIES (ROS) DEFENSE SYSTEM AND THEREBY HAS A ROLE IN CC PREADULT DEVELOPMENT AND LIFE SPAN. LACK OF A GLUTATHIONE CC REDUCTASE SUGGESTS ANTIOXIDANT DEFENSE IN DROSOPHILA, AND PROBABLY CC IN RELATED INSECTS, DIFFERS FUNDAMENTALLY FROM THAT IN OTHER CC ORGANISMS. CC -!- CATALYTIC ACTIVITY: THIOREDOXIN + NADP(+) = THIOREDOXIN DISULFIDE CC + NADPH. CC -!- COFACTOR: BINDS 1 FAD PER SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (ISOFORM B); CYTOPLASMIC CC (ISOFORM A). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=B; Synonyms=Mito; CC IsoId=P91938-1; Sequence=Displayed; CC Note=Can partially substitute for the cytoplasmic enzyme CC activity. Isoform D is produced by alternative initiation at CC Met-106 of isoform B; CC Name=A; Synonyms=Cyto; CC IsoId=P91938-2; Sequence=VSP_005572, VSP_005574; CC Note=Unable to compensate for the loss of the mitochondrial CC enzyme activity; CC Name=C; CC IsoId=P91938-3; Sequence=VSP_005571, VSP_005573; CC Event=Alternative initiation; CC Comment=2 isoforms, B (shown here) and D, are produced by CC alternative initiation at Met-1 and Met-106; CC -!- TISSUE SPECIFICITY: DURING EMBRYOGENESIS, EXPRESSION IS SEEN IN CC GERM CELL PROGENITORS, DEVELOPING MIDGUT, HINDGUT AND CC PROVENTRICULUS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY CC DURING ALL STAGES OF DEVELOPMENT, HIGHEST EXPRESSION DURING ADULT CC STAGES. CC -!- MISCELLANEOUS: THE ACTIVE SITE IS A REDOX-ACTIVE DISULFIDE BOND. CC -!- MISCELLANEOUS: OPTIMUM PH IS 7.1 (FOR ISOFORM A AND ISOFORM B). CC -!- SIMILARITY: BELONGS TO THE CLASS-I OF PYRIDINE NUCLEOTIDE- CC DISULFIDE OXIDOREDUCTASE FAMILY. CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT TO BE A GLUTHATIONE CC REDUCTASE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U81995; AAB48441.1; -. DR EMBL; AF301145; AAG25640.1; -. DR EMBL; AF301144; AAG25639.1; -. DR EMBL; AE003443; AAF46354.1; -. DR EMBL; AE003443; AAF46355.2; -. DR EMBL; AE003443; AAN09228.1; -. DR EMBL; AY051643; AAK93067.1; ALT_TERM. DR HSSP; P06715; 1GES. DR FlyBase; FBgn0020653; Trxr-1. DR GO; GO:0005739; C:mitochondrion; IDA. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA. DR GO; GO:0006125; P:thioredoxin pathway; IMP. DR InterPro; IPR001327; FAD_pyr_redox. DR InterPro; IPR000815; Hg_reductase. DR InterPro; IPR000205; NAD_BS. DR InterPro; IPR001100; Pyr_redox. DR InterPro; IPR004099; pyr_redox_dim. DR InterPro; IPR006338; Reduct_Se. DR Pfam; PF00070; pyr_redox; 1. DR Pfam; PF02852; pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00945; HGRDTASE. DR PRINTS; PR00411; PNDRDTASEI. DR ProDom; PD000139; FAD_pyr_redox; 1. DR TIGRFAMs; TIGR01438; TGR; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. KW Redox-active center; Oxidoreductase; NADP; Flavoprotein; FAD; KW Mitochondrion; Transit peptide; Alternative initiation; KW Alternative splicing. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 596 THIOREDOXIN REDUCTASE 1, ISOFORM B. FT CHAIN 106 596 THIOREDOXIN REDUCTASE 1, ISOFORM D. FT INIT_MET 106 106 FOR ISOFORM D. FT NP_BIND 144 162 FAD (ADP PART) (BY SIMILARITY). FT DISULFID 162 167 REDOX-ACTIVE (BY SIMILARITY). FT ACT_SITE 569 569 BY SIMILARITY. FT VARSPLIC 1 88 Missing (in isoform C). FT /FTId=VSP_005571. FT VARSPLIC 1 105 Missing (in isoform A). FT /FTId=VSP_005572. FT VARSPLIC 89 110 QHPHCDRAAMYAQPVRKMSTKG -> MLKYMICAIVVGAKK FT STSSKYN (in isoform C). FT /FTId=VSP_005573. FT VARSPLIC 106 110 MSTKG -> MAPVQ (in isoform A). FT /FTId=VSP_005574. FT MUTAGEN 594 594 C->S: LOSS OF TRX REDUCTION. FT MUTAGEN 595 595 C->S: LOSS OF TRX REDUCTION. FT CONFLICT 88 88 F -> L (IN REF. 5). FT CONFLICT 134 134 V -> S (IN REF. 1). FT CONFLICT 151 151 MISSING (IN REF. 1). FT CONFLICT 189 190 MISSING (IN REF. 1). FT CONFLICT 195 195 E -> D (IN REF. 1 AND 5). FT CONFLICT 203 207 KLVQS -> RLCAV (IN REF. 1). FT CONFLICT 213 216 KSVN -> SRH (IN REF. 1). FT CONFLICT 220 220 R -> V (IN REF. 1). FT CONFLICT 239 247 DSHTLLAKL -> TRTHCCPSM (IN REF. 1). FT CONFLICT 264 264 MISSING (IN REF. 1). FT CONFLICT 276 280 VEYGI -> AEIGT (IN REF. 1). FT CONFLICT 292 292 MISSING (IN REF. 1). FT CONFLICT 317 318 EP -> G (IN REF. 1). FT CONFLICT 351 386 RKTVPLSVEKQDDGKLLVKYKNVETGEEAEDVYDTV -> A FT DVDRCREADDAAAREYRLTQIRFTTSHHR (IN REF. FT 1). FT CONFLICT 379 379 A -> S (IN REF. 5). FT CONFLICT 396 398 VDD -> CDS (IN REF. 1). FT CONFLICT 403 406 NAGV -> MPAL (IN REF. 1). FT CONFLICT 424 425 AN -> PH (IN REF. 1). FT CONFLICT 455 455 Y -> F (IN REF. 1). FT CONFLICT 461 461 R -> S (IN REF. 1). FT CONFLICT 473 483 TPLEYACVGLS -> SWSTSASGLA (IN REF. 1). FT CONFLICT 488 495 VKQFGADE -> SSSSEPR (IN REF. 1). FT CONFLICT 559 560 IN -> L (IN REF. 1). FT CONFLICT 583 583 K -> KP (IN REF. 1). SQ SEQUENCE 596 AA; 64322 MW; 8DA6FC08CF6A7292 CRC64; MNLCNSRFSV TFVRQCSTIL TSPSAGIIQN RGSLTTKVPH WISSSLSCAH HTFQRTMNLT GQRGSRDSTG ATGGNAPAGS GAGAPPPFQH PHCDRAAMYA QPVRKMSTKG GSYDYDLIVI GGGSAGLACA KEAVLNGARV ACLDFVKPTP TLGTKWGVGG TCVNVGCIPK KLMHQASLLG EAVHEAAAYG WNVDEKIKPD WHKLVQSVQN HIKSVNWVTR VDLRDKKVEY INGLGSFVDS HTLLAKLKSG ERTITAQTFV IAVGGRPRYP DIPGAVEYGI TSDDLFSLDR EPGKTLVVGA GYIGLECAGF LKGLGYEPTV MVRSIVLRGF DQQMAELVAA SMEERGIPFL RKTVPLSVEK QDDGKLLVKY KNVETGEEAE DVYDTVLWAI GRKGLVDDLN LPNAGVTVQK DKIPVDSQEA TNVANIYAVG DIIYGKPELT PVAVLAGRLL ARRLYGGSTQ RMDYKDVATT VFTPLEYACV GLSEEDAVKQ FGADEIEVFH GYYKPTEFFI PQKSVRYCYL KAVAERHGDQ RVYGLHYIGP VAGEVIQGFA AALKSGLTIN TLINTVGIHP TTAEEFTRLA ITKRSGLDPT PASCCS // ID TRX2_DROME STANDARD; PRT; 516 AA. AC Q9VNT5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Thioredoxin reductase 2, mitochondrial precursor (EC 1.8.1.9) (TrxR- DE 2). GN TRXR-2 OR CG11401. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Kanzok S., Becker K., Schirmer R.H.; RT "Drosophila melanogaster thioredoxin reductase 2."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: THIOREDOXIN SYSTEM IS A MAJOR PLAYER IN GLUTATHIONE CC METABOLISM, DUE TO THE DEMONSTRATED ABSENCE OF A GLUTATHIONE CC REDUCTASE. FUNCTIONALLY INTERACTS WITH THE SOD/CAT REACTIVE CC OXIDATION SPECIES (ROS) DEFENSE SYSTEM AND THEREBY HAS A ROLE IN CC PREADULT DEVELOPMENT AND LIFE SPAN. LACK OF A GLUTATHIONE CC REDUCTASE SUGGESTS ANTIOXIDANT DEFENSE IN DROSOPHILA, AND PROBABLY CC IN RELATED INSECTS, DIFFERS FUNDAMENTALLY FROM THAT IN OTHER CC ORGANISMS. CC -!- CATALYTIC ACTIVITY: THIOREDOXIN + NADP(+) = THIOREDOXIN DISULFIDE CC + NADPH. CC -!- COFACTOR: BINDS 1 FAD PER SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- MISCELLANEOUS: THE ACTIVE SITE IS A REDOX-ACTIVE DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE CLASS-I OF PYRIDINE NUCLEOTIDE- CC DISULFIDE OXIDOREDUCTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF236866; AAF64152.1; -. DR EMBL; AE003598; AAF51835.1; -. DR EMBL; AY121613; AAM51940.1; -. DR HSSP; P06715; 1GES. DR FlyBase; FBgn0037170; Trxr-2. DR GO; GO:0005739; C:mitochondrion; ISS. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISS. DR GO; GO:0006125; P:thioredoxin pathway; ISS. DR InterPro; IPR001327; FAD_pyr_redox. DR InterPro; IPR000815; Hg_reductase. DR InterPro; IPR000205; NAD_BS. DR InterPro; IPR001100; Pyr_redox. DR InterPro; IPR004099; pyr_redox_dim. DR InterPro; IPR006338; Reduct_Se. DR Pfam; PF00070; pyr_redox; 1. DR Pfam; PF02852; pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00945; HGRDTASE. DR PRINTS; PR00411; PNDRDTASEI. DR ProDom; PD000139; FAD_pyr_redox; 1. DR TIGRFAMs; TIGR01438; TGR; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. KW Redox-active center; Oxidoreductase; NADP; Flavoprotein; FAD; KW Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 516 THIOREDOXIN REDUCTASE 2. FT NP_BIND 62 79 FAD (ADP PART) (BY SIMILARITY). FT DISULFID 79 84 REDOX-ACTIVE (BY SIMILARITY). FT ACT_SITE 489 489 BY SIMILARITY. SQ SEQUENCE 516 AA; 56276 MW; D82A89CBF6A4B7E8 CRC64; MSTIKFLRSS THNALRSSLG WCRLAASRPR YDYDLVVLGG GSAGLACAKE AAGCGARVLC FDYVKPTPVG TKWGIGGTCV NVGCIPKKLM HQASLLGEAV HEAVAYGWNV DDTNIRPDWR KLVRSVQNHI KSVNWVTRVD LRDKKVEYVN SMATFRDSHT IEYVAMPGAE HRQVTSEYVV VAVGGRPRYP DIPGAVELGI TSDDIFSYER EPGRTLVVGA GYVGLECACF LKGLGYEPTV MVRSIVLRGF DRQMSELLAA MMTERGIPFL GTTIPKAVER QADGRLLVRY RNTTTQMDGS DVFDTVLWAI GRKGLIEDLN LDAAGVKTHD DKIVVDAAEA TSVPHIFAVG DIIYGRPELT PVAILSGRLL ARRLFAGSTQ LMDYADVATT VFTPLEYSCV GMSEETAIEL RGADNIEVFH GYYKPTEFFI PQKSVRHCYL KAVAEVSGDQ KILGLHYIGP VAGEVIQGFA AALKTGLTVK TLLNTVGIHP TTAEEFTRLS ITKRSGRDPT PASCCS // ID TRX_DROME STANDARD; PRT; 3726 AA. AC P20659; Q27255; Q27327; DT 01-FEB-1991 (Rel. 17, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Trithorax protein. GN TRX. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90192757; PubMed=2107543; RA Mazo A.M., Huang D.-H., Mozer B.A., Dawid I.B.; RT "The trithorax gene, a trans-acting regulator of the bithorax complex RT in Drosophila, encodes a protein with zinc-binding domains."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2112-2116(1990). RN [2] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND CHARACTERIZATION. RX MEDLINE=95009521; PubMed=7924996; RA Sedkov Y., Tillib S., Mizrokhi L., Mazo A.; RT "The bithorax complex is regulated by trithorax earlier during RT Drosophila embryogenesis than is the Antennapedia complex, correlating RT with a bithorax-like expression pattern of distinct early trithorax RT transcripts."; RL Development 120:1907-1917(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=96100387; PubMed=8555104; RA Tillib S., Sedkov Y., Mizrokhi L., Mazo A.; RT "Conservation of structure and expression of the trithorax gene RT between Drosophila virilis and Drosophila melanogaster."; RL Mech. Dev. 53:113-122(1995). RN [4] RP CHARACTERIZATION. RX MEDLINE=95047388; PubMed=7958911; RA Kuzin B., Tillib S., Sedkov Y., Mizrokhi L., Mazo A.; RT "The Drosophila trithorax gene encodes a chromosomal protein and RT directly regulates the region-specific homeotic gene fork head."; RL Genes Dev. 8:2478-2490(1994). CC -!- FUNCTION: FUNCTIONS IN SEGMENT DETERMINATION THROUGH INTERACTION CC WITH GENES OF BITHORAX (BX-C) AND ANTENNAPEDIA (ANT-X) COMPLEXES. CC IT CAN BEHAVE AS AN ACTIVATOR OF BX-C. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P20659-1; Sequence=Displayed; CC Name=Short; CC IsoId=P20659-2; Sequence=VSP_006665; CC -!- MISCELLANEOUS: THIS PROTEIN HAS BEEN EXPERIMENTALLY SHOWN TO BIND CC ZINC. CC -!- SIMILARITY: BELONGS TO THE TRX/MLL FAMILY. CC -!- SIMILARITY: CONTAINS 1 SET DOMAIN. CC -!- SIMILARITY: CONTAINS 5 PHD-TYPE ZINC FINGERS. CC -!- SIMILARITY: CONTAINS 1 POST-SET DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M31617; AAA29025.1; -. DR EMBL; Z50152; CAA90514.1; -. DR EMBL; Z50152; CAA90513.1; -. DR EMBL; Z31725; CAA83516.1; -. DR EMBL; Z31725; CAA83515.1; -. DR PIR; A35085; A35085. DR HSSP; P20393; 1A6Y. DR TRANSFAC; T00850; -. DR FlyBase; FBgn0003862; trx. DR InterPro; IPR003889; FYrich_C. DR InterPro; IPR003888; FYrich_N. DR InterPro; IPR003616; PostSET. DR InterPro; IPR001214; SET. DR InterPro; IPR001965; Znf_PHD. DR Pfam; PF00628; PHD; 3. DR Pfam; PF00856; SET; 1. DR SMART; SM00542; FYRC; 1. DR SMART; SM00541; FYRN; 1. DR SMART; SM00249; PHD; 5. DR SMART; SM00508; PostSET; 2. DR SMART; SM00317; SET; 1. DR PROSITE; PS50868; POST_SET; 1. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS01359; ZF_PHD_1; 4. DR PROSITE; PS50016; ZF_PHD_2; 3. KW Transcription regulation; Zinc-finger; Metal-binding; DNA-binding; KW Nuclear protein; Developmental protein; Activator; KW Alternative splicing. FT ZN_FING 1266 1347 PHD-TYPE 1. FT ZN_FING 1348 1393 PHD-TYPE 2. FT ZN_FING 1421 1482 PHD-TYPE 3. FT ZN_FING 1734 1793 PHD-TYPE 4 (ATYPICAL). FT ZN_FING 1794 1844 PHD-TYPE 5 (ATYPICAL). FT DOMAIN 3587 3708 SET. FT DOMAIN 3710 3726 POST-SET. FT DOMAIN 512 516 POLY-SER. FT DOMAIN 565 570 POLY-ASP. FT DOMAIN 661 664 POLY-SER. FT DOMAIN 905 910 POLY-SER. FT DOMAIN 1576 1582 POLY-GLN. FT DOMAIN 2298 3027 GLN-RICH. FT DOMAIN 3032 3040 POLY-SER. FT DOMAIN 3181 3184 POLY-GLN. FT DOMAIN 3220 3225 POLY-GLU. FT VARSPLIC 1 368 Missing (in isoform Short). FT /FTId=VSP_006665. FT CONFLICT 2025 2025 P -> PWLTSPLKFLGLSTHGGLLLWLLLGVVVRLKQGG FT (IN REF. 1). FT CONFLICT 2341 2341 R -> S (IN REF. 1). FT CONFLICT 2392 2392 G -> S (IN REF. 1). SQ SEQUENCE 3726 AA; 400575 MW; D2756E50763D1CF5 CRC64; MGRSKFPGKP SKSINRKRIS VLQLEDDAAN PAEPQQPAPE SQQPSGSGSG SSAAREKGNN CDNDEDDNAP GGASISGNTA SSSAGSGNSG NGSSSGSSTG SGSSGSGSTN GGSVNGGTHH KSAANLDKEA VTKDQNGDGD KTRGNVSSAP SGKLSAAASG KALSKSSRTF SASTSVTSSG RSSGSSPDGN SGASSDGASS GISCGKSTAK STEASSGKLA KTTGAGTCSS AKSSKASSLE QLVKQQPLVS GACLKALFVA TPATSTGLAC ALVSPGGSSQ GGTFPISAAL LRARKNSNKK FKKLNLARGE VMLPSTSKLK QLNSPVVDNP SPSPPILSGS TPSVEGGIGV GGVVSPGEDA ALKRVLTEMP NEVARDPSPS SCTAAANGAA SGKGSASNGP PAMASSGDGS SPKSGADTGP STSSTTAKQK KTVTFRNVLE TSDDKSVVKR FYNPDIRIPI VSIMKKDSLN RPLNYSRGGE CIVRPSILSK ILNKNSNIDK LNSLKFRSAG ASSSSSNQES RSSSNVFGLS RAFGAPMDED DEGGVTFRRN DSPEDQNNAE DDEMDDDDDD EEAEEDDQNE DDNDEAASEK SAETEKSAGA DERDPDEKQL VMDSHFVLPK RSTRSSRIIK PNKRLLEEGA ISTKKPLSLG DSKGKNVFGT SSSSAGSTAS TFSASTNLKL GKETFFNFGT LKPNSSAAGI FVLRQPRLQF QADNQQATFA APKACPTSPS AIPKPANSLA TSSFGSLAST NSSTVTPTPS ACSICSAVVS SKEVTQARKY GVVACDVCRK FFSKMTKKSI SANSSTANTS SGSQQYLQCK GNEGSPCSIH SAKSQLKNFK KFYKDRCTAC WLKKCMISFQ LPAAHRSRLS AILPPGMRGE AAAREEKSAE LLSPTGSLRF TSTASSSSPS VVASTSVKWK SSGDSTSALT SIKPNPLAEN NVTFGSTPLL RPAILENPLF LKISNAADQK LAAAEAISPS LTKKNSKQEK EKVKESEQSE KLLSPTQAGT KKSGAAEAQV EEVQPQKEEA PQTSTTTQPS ASNGASHGVP QAELAGETNA TGDTLKRQRI DLPGPRVKHV CRSASIVLGQ PLATFGEDQQ PEDAADMQQE IAAPVPSAIM EPSPEKPTHI VTDENDNCAS CKTSPVGDES KPSKSSGSAQ AEVKKATALG KEGTASAAGG SSAKVTTRNA AVASNLIVAA SKKQRNGDIA TSSSVTQSSN QTQGRKTKEH RQQRTLISID FWENYDPAEV CQTGFGLIVT ETVAQRALCF LCGSTGLDPL IFCACCCEPY HQYCVQDEYN LKHGSFEDTT LMGSLLETTV NASTGPSSSL NQLTQRLNWL CPRCTVCYTC NMSSGSKVKC QKCQKNYHST CLGTSKRLLG ADRPLICVNC LKCKSCSTTK VSKFVGNLPM CTGCFKLRKK GNFCPICQRC YDDNDFDLKM MECGDCGQWV HSKCEGLSDE QYNLLSTLPE SIEFICKKCA RRNESSKIKA EEWRQAVMEE FKASLYSVLK LLSKSRQACA LLKLSPRKNV RCTCGASSNQ GKLQPKALQF SSGSDNGLGS DGESQNSDDV YEFKDQQQQQ QQRNANMNKP RVKPLPCSCQ QHISHSQSFS LVDIKQKIAG NSYVSLEEFN YDMSQVIQQS NCDELDIAYK ELLSEQFPWF QNETKACTDA LEEDMFESCS GGNYEDLQDA GGVSASVYNE HSTSQAESRS GVLDIPLEEV DDFGSCGIKM RLDTRMCLFC RKSGEGLSGE EARLLYCGHD CWVHTNCAMW SAEVFEEIDG SLQNVHSAVA RGRMIKCTVC GNRGATVGCN VRSCGEHYHY PCARSIDCAF LTDKSMYCPA HAKNGNALKA NGSPSVTYES NFEVSRPVYV ELDRKRKKLI EPARVQFHIG SLEVRQLGAI VPRFSDSYEA VVPINFLCSR LYWSSKEPWK IVEYTVRTTI QNSSSTLTAL DVGRNYTVDH TNPNSKEVQL GMAQIARWHT SLARSEFLEN GGTDWSGEFP NPNSCVPPDQ NTEEEPQQQA DLLPPELKDA IFEDLPHELL DGISMLDIFL YDDKTDLFAI SEQSKDGTQA MTSNQAQNQN QQAGGANSVS ICDEDTRNSN TSLGNGWPAS NPVEDAMLSA ARNSSQVQML KTLAWPKLDG NSAMATAIKR RKLSKNLAEG VFLTLSSQQR NKKEMATVAG VSRRQSISET SVEGVATTSG SVRSKSFTWS AAKRYFEKSE GREEAAKMRI MQMDGVDDSI TEFRIISGDG NLSTAQFSGQ VKCDRCQCTY RNYDAFQRHL PSCSPTMSSN ETESDVSGQG MTNNATQISA ESLNELQKQL LANAGGLNYL QSATSFPQVQ RLGSLGQFGL QGLQQLQLQP QSLGNGFFLS QPNPATQANT DDLQIYANSL QGLAANLGGG FTLAQPTVTA PAQPQLIAVS TNPDGTQQFI QIPQTMQATT TPTATYQTLQ ATNTDKKIML PLTAAGKPLK TVATKAAQQA AVKQRQLKSG HQVKPIQAKL QPHPQQHQQQ QQTQVQQPIT VMGQNLLQPQ LLFQSSTQTQ APQIILPQAQ PQNIISFVTG DGSQGQPLQY ISIPTAGEYK PQPQPTATPT FLTTAPGAGA TYLQTDASGN LVLTTTPSNS GLQMLTAQSL QAQPQVIGTL IQPQTIQLGG GADGNQPGSN QQPLILGGTG GGSSGLEFAT TSPQVILATQ PMYYGLETIV QNTVMSSQQF VSTAMPGMLS QNASFSATTT QVFQASKIEP IVDLPAGYVV LNNTGDASSA GTFLNAASVL QQQTQDDTTT QILQNANFQF QSVPTSSGAS TSMDYTSPVM VTAKIPPVTQ IKRTNAQAKA AGISGVGKVP PQPQVVNKVL PTSIVTQQSQ VQVKNSNLKQ SQVKGKAASG TGTTCGAPPS IASKPLQKKT NMIRPIHKLE VKPKVMKPTP KVQNQNHSLL QQQQQQQPQL QQQIPAVVVN QVPKVTISQQ RIPAQTQQQQ LQQAQMIHIP QQQQPLQQQQ VQVQPSMPII TLAEAPVVQS QFVMEPQALE QQELANRVQH FSTSSSSSSS NCSLPTNVVN PMQQQAPSTT SSSTTRPTNR VLPMQQRQEP APLSNECPVV SSPTPPKPVE QPIIHQMTSA SVSKCYAQKS TLPSPVYEAE LKVSSVLESI VPDVTMDAIL EEQPVTQSIY TEGLYEKNSP GESKTEQLLL QQQQREQLNQ QLVNNGYLLD KHTFQVEPMD TDVYREEDLE EEEDEDDDFS LKMRTSACND HEMSDSEEPA VKDKISKILD NLTNDDCADS IATATTMEVD ASAGYQQMVE DVLATTAAQS APTEEFEGAL ETAAVEAAAT YINEMADAHV LDLKQLQNGV ELELRRRKEE QRTVSQEQEQ SKAAIVPTAA APEPPQPIQE PKKMTGPHLL YEIQSEDGFT YKSSSITEIW EKVFEAVQVA RRAHGLTPLP EGPLADMGGI QMIGLKTNAL KYLIEQLPGV EKCSKYTPKY HKRNGNVSTA ANGAHGGNLG GSSASAALSV SGGDSHGLLD YGSDQDELEE NAYDCARCEP YSNRSEYDMF SWLASRHRKQ PIQVFVQPSD NELVPRRGTG SNLPMAMKYR TLKETYKDYV GVFRSHIHGR GLYCTKDIEA GEMVIEYAGE LIRSTLTDKR ERYYDSRGIG CYMFKIDDNL VVDATMRGNA ARFINHCCEP NCYSKVVDIL GHKHIIIFAV RRIVQGEELT YDYKFPFEDE KIPCSCGSKR CRKYLN // ID TRYA_DROME STANDARD; PRT; 256 AA. AC P04814; Q9V5Y2; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin alpha precursor (EC 3.4.21.4). GN ALPHA-TRY OR TRY-ALPHA OR CG18444. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86041859; PubMed=2414727; RA Davis C.A., Riddell D.C., Higgins M.J., Holden J.J.A., White B.N.; RT "A gene family in Drosophila melanogaster coding for trypsin-like RT enzymes."; RL Nucleic Acids Res. 13:6605-6619(1985). RN [2] RP SEQUENCE FROM N.A. RA Magoulas C., Hickey D.A.; RL Submitted (XXX-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Wang S., Magoulas C., Hickey D.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: SYNTHESIZED IN THE MIDGUT OF BOTH LARVAE AND CC ADULTS, PRIMARILY IN THE VENTRICULUS AND GASTRIC CAECA. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02989; CAA26732.1; -. DR EMBL; M96372; AAA28982.1; -. DR EMBL; U04853; AAA17453.1; -. DR EMBL; AE003826; AAF58659.1; -. DR PIR; A23493; TRFF. DR HSSP; P00763; 1DPO. DR MEROPS; S01.112; -. DR FlyBase; FBgn0003863; alpha-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 22 PROBABLE. FT PROPEP 23 30 ACTIVATION PEPTIDE. FT CHAIN 31 256 TRYPSIN ALPHA. FT ACT_SITE 71 71 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 116 116 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 210 210 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 56 72 BY SIMILARITY. FT DISULFID 180 197 BY SIMILARITY. FT DISULFID 206 230 BY SIMILARITY. FT SITE 204 204 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 256 AA; 26041 MW; 8B5634992F2E7C63 CRC64; MLKIVILLSA VVCALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSI YSANIIVTAA HCLQSVSASV LQVRAGSTYW SSGGVVAKVS SFKNHEGYNA NTMVNDIAVI RLSSSLSFSS SIKAISLATY NPANGASAAV SGWGTQSSGS SSIPSQLQYV NVNIVSQSQC ASSTYGYGSQ IRNTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA DVAVLRSWVV STANSI // ID TRYB_DROME STANDARD; PRT; 253 AA. AC P35004; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin beta precursor (EC 3.4.21.4). GN BETA-TRY. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Magoulas C., Hickey D.A.; RL Submitted (XXX-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Wang S., Magoulas C., Hickey D.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96372; AAA28980.1; -. DR EMBL; U04853; AAA17451.1; -. DR HSSP; P00763; 1DPO. DR MEROPS; S01.112; -. DR FlyBase; FBgn0010357; beta-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 22 PROBABLE. FT PROPEP 23 30 ACTIVATION PEPTIDE. FT CHAIN 31 253 TRYPSIN BETA. FT ACT_SITE 71 71 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 116 116 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 210 210 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 56 72 BY SIMILARITY. FT DISULFID 180 197 BY SIMILARITY. FT DISULFID 206 230 BY SIMILARITY. FT SITE 204 204 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 253 AA; 25704 MW; E505375C8200144E CRC64; MLKFLILLSA VACALGGTIP EGLLPQLDGR IVGGTATTIS SFPWQISLQR SGRHSCGGSI YSARVIVTAA HCLQSVSASS LQIRGGSSYW SSGGVVAKVS SFKNHEGYNA NTMTSDIAVL NLSSSLSFSS TIKAIGLASS NTANGAAASV SGWGTESSGS SSIPSQLRYV NVNIVSQSRC SSSSYGYGNQ IKSSMICAFA SGKDSCQGDS GGPLVSGGVL VGVVSWGYGC AAANYPGVYA DVAALRSWVI NNA // ID TRYD_DROME STANDARD; PRT; 253 AA. AC P42276; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin delta precursor (EC 3.4.21.4). GN DELTA-TRY. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Wang S., Magoulas C., Hickey D.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04853; AAA17449.1; -. DR HSSP; P00763; 1DPO. DR MEROPS; S01.112; -. DR FlyBase; FBgn0010358; delta-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 22 PROBABLE. FT PROPEP 23 30 ACTIVATION PEPTIDE. FT CHAIN 31 253 TRYPSIN DELTA. FT ACT_SITE 71 71 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 116 116 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 210 210 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 56 72 BY SIMILARITY. FT DISULFID 180 197 BY SIMILARITY. FT DISULFID 206 230 BY SIMILARITY. FT SITE 204 204 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 253 AA; 25710 MW; 72182C992B5DA77F CRC64; MLKFVILLSA VACALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSI YSSNVIVTAA HCLQSVSASV LQIRAGSSYW SSGGVTFSVS SFKNHEGYNA NTMVNDIVII KINGALTFSS TIKAIGLASS NPANGAAGSV SGWGTLSYGS SSIPSQLQYV NVNIVSQSQC ASSTYGYGSQ IRSTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYS DVAALRSWVI SNA // ID TRYE_DROME STANDARD; PRT; 256 AA. AC P35005; Q9V5Y1; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin epsilon precursor (EC 3.4.21.4). GN EPSILON-TRY OR TRY-EPSILON OR CG18681. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Magoulas C., Hickey D.A.; RL Submitted (XXX-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Wang S., Magoulas C., Hickey D.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96372; AAA28981.1; -. DR EMBL; U04853; AAA17452.1; -. DR EMBL; AE003826; AAF58660.1; -. DR HSSP; P00763; 1DPO. DR MEROPS; S01.112; -. DR FlyBase; FBgn0010425; epsilon-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 22 PROBABLE. FT PROPEP 23 30 ACTIVATION PEPTIDE. FT CHAIN 31 256 TRYPSIN EPSILON. FT ACT_SITE 71 71 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 116 116 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 210 210 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 56 72 BY SIMILARITY. FT DISULFID 180 197 BY SIMILARITY. FT DISULFID 206 230 BY SIMILARITY. FT SITE 204 204 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 256 AA; 27810 MW; CB8B276430F8616D CRC64; MLKFAVLLSV LACALAGTIP DGLLPQLDGR IVGGYETSID AHPYQVSLQR YGSHFCGGSI YSHDIVITAA HCLQSIEAKD LKIRVGSTYW RSGGSVHSVR SFRNHEGYNS RTMVNDIAII RIESDLSFRS SIREIRIADS NPREGATAVV SGWGTTESGG STIPDHLLAV DLEIIDVSRC RSDEFGYGKK IKDTMLCAYA PHKDACQGDS GGPLVSGDRL VGVVSWGYGC GDVRYPGVYA DVAHFHEWIE RTAEEV // ID TRYG_DROME STANDARD; PRT; 253 AA. AC P42277; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin gamma precursor (EC 3.4.21.4). GN GAMMA-TRY. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Wang S., Magoulas C., Hickey D.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04853; AAA17450.1; -. DR HSSP; P00763; 1DPO. DR MEROPS; S01.112; -. DR FlyBase; FBgn0010359; gamma-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 22 PROBABLE. FT PROPEP 23 30 ACTIVATION PEPTIDE. FT CHAIN 31 253 TRYPSIN GAMMA. FT ACT_SITE 71 71 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 116 116 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 210 210 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 56 72 BY SIMILARITY. FT DISULFID 180 197 BY SIMILARITY. FT DISULFID 206 230 BY SIMILARITY. FT SITE 204 204 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 253 AA; 25694 MW; 72182C992B4B7D7F CRC64; MLKFVILLSA VACALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSI YSSNVIVTAA HCLQSVSASV LQIRAGSSYW SSGGVTFSVS SFKNHEGYNA NTMVNDIVII KINGALTFSS TIKAIGLASS NPANGAAGSV SGWGTLSYGS SSIPSQLQYV NVNIVSQSQC ASSTYGYGSQ IRSTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA DVAALRSWVI SNA // ID TRYI_DROME STANDARD; PRT; 252 AA. AC P52905; Q9V5Y6; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin iota precursor (EC 3.4.21.4). GN IOTA-TRY OR TRY-IOTA OR CG7754. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Gao L., Wang S., Hickey D.A.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04853; AAA84377.1; -. DR EMBL; AE003826; AAF58655.1; -. DR HSSP; P00763; 1DPO. DR MEROPS; S01.112; -. DR FlyBase; FBgn0015001; iota-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 19 POTENTIAL. FT PROPEP 20 27 ACTIVATION PEPTIDE. FT CHAIN 28 252 TRYPSIN IOTA. FT ACT_SITE 68 68 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 113 113 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 206 206 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 53 69 BY SIMILARITY. FT DISULFID 175 193 BY SIMILARITY. FT DISULFID 202 226 BY SIMILARITY. FT SITE 200 200 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 252 AA; 26612 MW; 044DEDA4700910C2 CRC64; MAVYGIVATV LVLLLLGDAS DVEATGRIIG GSDQLIRNAP WQVSIQISAR HECGGVIYSK EIIITAGHCL HERSVTLMKV RVGAQNHNYG GTLVPVAAYK VHEQFDSRFL HYDIAVLRLS TPLTFGLSTR AINLASTSPS GGTTVTVTGW GHTDNGALSD SLQKAQLQII DRGECASQKF GYGADFVGEE TICAASTDAD ACTGDSGGPL VASSQLVGIV SWGYRCADDN YPGVYADVAI LRPWIVKAAN AI // ID TRYT_DROME STANDARD; PRT; 262 AA. AC P42278; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin theta precursor (EC 3.4.21.4). GN THETA-TRY. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Wang S., Magoulas C., Hickey D.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04853; AAA17454.1; -. DR HSSP; P00761; 1EPT. DR MEROPS; S01.112; -. DR FlyBase; FBgn0011555; theta-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 19 PROBABLE. FT PROPEP 20 34 ACTIVATION PEPTIDE. FT CHAIN 35 262 TRYPSIN THETA. FT ACT_SITE 76 76 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 121 121 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 216 216 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 61 77 BY SIMILARITY. FT DISULFID 186 203 BY SIMILARITY. FT DISULFID 212 236 BY SIMILARITY. FT SITE 210 210 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 262 AA; 28342 MW; 43D451B9A93059FC CRC64; MHRLVVLLVC LAVGSACAGT VGVSNGDPFE REGRIVGGED TTIGGDPYQV SLQTKSGSHF CGGSLINEDT VVTAAHCLVG RKVSKVFVRL GSTLYNEGGI VVAVRELAYN EDYNSKTMEY DVGILKLDEK VKETENIRYI ELATETPPTG TTAVVTGWGS KCYFWCMTLP KTLQEVYVNI VDWKTCASDE YKYGEIIYDS MVCAYEKKKD ACQGDSGGPL AVGNTLVGIV SWGYACASNL LPGVYSDVPA LRKWILNASE TL // ID TRYU_DROME STANDARD; PRT; 262 AA. AC P42279; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin eta precursor (EC 3.4.21.4). GN ETA-TRY. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Wang S., Magoulas C., Hickey D.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04853; AAA17455.1; -. DR HSSP; P00763; 1DPO. DR MEROPS; S01.112; -. DR FlyBase; FBgn0011554; eta-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; FALSE_NEG. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 22 POTENTIAL. FT PROPEP 23 27 ACTIVATION PEPTIDE. FT CHAIN 28 262 TRYPSIN ETA. FT ACT_SITE 74 74 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 120 120 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 215 215 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 62 75 BY SIMILARITY. FT DISULFID 185 200 BY SIMILARITY. FT DISULFID 211 235 BY SIMILARITY. FT SITE 209 209 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 262 AA; 28145 MW; 7BA241F68D335126 CRC64; MNKVILRVLA VLFLLGIYAV SAQPDGRIVG GADTSSYYTK YVVQLRRRSS SSSSYAQTCG GCILDAVTIA TAAHCVYNRE AENFLVVSGD DSRGGMYGVV VRVSQLIPHE LYNSSTMDND IALVVVDPPL PLDSFSTMEA IVIASEQPPV GVQATISGWG YTKENGLSSD QLQQVKVPIV DSEKCQEAYY WRPISEGMLC AGLSEGGKDA CQGDSGGPLV VANKLAGIVS WGEGCARPNY PGVYANVAYY KDWIAKQRTS YV // ID TRYZ_DROME STANDARD; PRT; 280 AA. AC P42280; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Trypsin zeta precursor (EC 3.4.21.4). GN ZETA-TRY. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Wang S., Magoulas C., Hickey D.A.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-|-XAA, LYS-|-XAA. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04853; AAA17456.1; -. DR HSSP; P00763; 1DPO. DR MEROPS; S01.112; -. DR FlyBase; FBgn0011556; zeta-Try. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Zymogen; Signal; Multigene family. FT SIGNAL 1 22 PROBABLE. FT PROPEP 23 38 ACTIVATION PEPTIDE. FT CHAIN 39 280 TRYPSIN ZETA. FT ACT_SITE 87 87 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 134 134 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 234 234 CHARGE RELAY SYSTEM (BY SIMILARITY). FT DISULFID 72 88 BY SIMILARITY. FT DISULFID 198 218 BY SIMILARITY. FT DISULFID 230 254 BY SIMILARITY. FT SITE 228 228 REQUIRED FOR SPECIFICITY (BY SIMILARITY). SQ SEQUENCE 280 AA; 29598 MW; 6255F1CCEAE823CB CRC64; MSSSWIVGLL AFLVSLVALT QGLPLLEDLD EKSVPDGRIV GGYATDIAQV PYQISLRYKG ITTPENPFRH RCGGSIFNET TIVTAGHCVI GTVASQYKVV AGTNFQTGSD GVITNVKEIV MHEGYYSGAA YNNDIAILFV DPPLALNNFT IKGIKLASEQ PIEGTVSKVS GWGTTSPGGY SSNQLLAVDV PIVSNELCDQ DYEDFGDETY RITSAMLCAG KPGVGGADAC QGDSGGPLAV RDELYGVVSW GNSCALPNYP GVYANVAYLR PWIDAVLAGL // ID TSG_DROME STANDARD; PRT; 249 AA. AC P54356; Q9VYR6; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Twisted gastrulation protein precursor. GN TSG OR CG1502. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Embryo; RX MEDLINE=95047309; PubMed=7958834; RA Mason E.D., Konrad K.D., Webb C.D., Marsh J.L.; RT "Dorsal midline fate in Drosophila embryos requires twisted RT gastrulation, a gene encoding a secreted protein related to human RT connective tissue growth factor."; RL Genes Dev. 8:1489-1501(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: SPECIFY THE FATE OF DORSAL CELLS IN DROSOPHILA EMBRYOS. CC MUTATIONS OF TSG ONLY AFFECT THE FATE OF A NARROW STRIP OF DORSAL CC MIDLINE CELLS AND DO NOT AFFECT DORSAL ECTODERM CELLS. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: FIRST APPEARS IN STAGE 4 EMBRYOS, EXPRESSED IN CC TWO DOMAINS: A BROAD MID-DORSAL SADDLE AND AN ANTERIOR CAP, CC EXPRESSION BETWEEN THE DOMAINS IS CONTINUOUS ACROSS THE DORSAL CC MIDLINE. AT STAGE 5, EXPRESSION IS REFINED INTO 4 GRADED STRIPES CC IN THE MID-DORSAL REGION AND A PAIRED DOMAIN IN THE ANTERIOR CC REGION. DURING STAGES 7 AND 8, ANTERIOR EXPRESSION FADES AND THE CC MID DORSAL STRIPES ARE LOCATED BETWEEN THE ANTERIOR AND POSTERIOR CC TRANSVERSE FURROW (ATF AND PTF). EXPRESSING CELLS BECOME CC INCORPORATED INTO THE DEEPENING PTF. CC -!- DEVELOPMENTAL STAGE: GASTRULATING EMBRYO. CC -!- SIMILARITY: SOME, TO THE CEF-10/CYR61/CTFG/FISP-12/NOV PROTEIN CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U09808; AAC24234.1; -. DR EMBL; AE003487; AAF48123.1; -. DR PIR; A53836; A53836. DR FlyBase; FBgn0003865; tsg. DR GO; GO:0005576; C:extracellular; IPI. DR GO; GO:0008201; F:heparin binding; IPI. DR GO; GO:0017015; P:regulation of TGFbeta receptor signaling pa...; IMP. DR GO; GO:0007362; P:terminal region determination; IGI. DR GO; GO:0008293; P:torso signaling pathway; IGI. DR InterPro; IPR006761; Tsg. DR Pfam; PF04668; Tsg; 1. KW Developmental protein; Glycoprotein; Signal. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 249 TWISTED GASTRULATION PROTEIN. FT CARBOHYD 199 199 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 249 AA; 27220 MW; 313EE6A406E4B86D CRC64; MQLLCYFVIL FVGIAPWSSL ANDDGCNEVV CGSVVSKCLI TQSCQCKLND CHCCKDCLNC LGELYIECCG CLDMCPKHKD VLPSLTPRSE IGDIEGVPEL FDTLTAEDDE GWSTIRFSMR AGFKQRVQGG ASGDAGNGNG NGNAGSAGVT LCTVIYVNSC IRANKCRQQC ESMGASSYRW FHDGCCECVG ENCLNYGINE SRCRGCPEDQ DQLLTADTVP AEAEQDLERF FGNEEIEDEW GYGEEDEFS // ID TSH_DROME STANDARD; PRT; 993 AA. AC P22265; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Teashirt protein. GN TSH. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91098655; PubMed=1846092; RA Fasano L., Roeder L., Core N., Alexandre E., Vola C., Jacq B., RA Kerridge S.; RT "The gene teashirt is required for the development of Drosophila RT embryonic trunk segments and encodes a protein with widely spaced RT zinc finger motifs."; RL Cell 64:63-79(1991). RN [2] RP POSSIBLE FUNCTION. RX MEDLINE=93083418; PubMed=1360402; RA Roeder L., Vola C., Kerridge S.; RT "The role of the teashirt gene in trunk segmental identity in RT Drosophila."; RL Development 115:1017-1033(1992). RN [3] RP POSSIBLE FUNCTION. RX MEDLINE=95009555; PubMed=7925029; RA de Zulueta P., Alexandre E., Jacq B., Kerridge S.; RT "Homeotic complex and teashirt genes co-operate to establish trunk RT segmental identities in Drosophila."; RL Development 120:2287-2296(1994). CC -!- FUNCTION: REQUIRED FOR THE DEVELOPMENT OF DROSOPHILA EMBRYONIC CC TRUNK SEGMENTS. REPRESS THE EXPRESSION OF HEAD HOMEOTIC GENES. CC NECESSARY, IN COMBINATION WITH SCR, FOR THE FORMATION OF THE CC PROTHORACIC SEGMENT. MAY BE INVOLVED IN CHROMATIN STRUCTURE FOR CC MODULATION OF TRANSCRIPTION. NEGATIVELY CONTROL THE EXPRESSION OF CC MOD AND POSITIVELY THAT OF DLL AND OF ITS OWN EXPRESSION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED EXCLUSIVELY IN THE TRUNK (FROM PS3 CC TO PS13). CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYONIC, LARVAL AND CC ADULT DEVELOPMENT. NOT MATERNALLY EXPRESSED. CC -!- SIMILARITY: CONTAINS 3 C2H2-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M57496; AAA28983.1; -. DR PIR; A38437; A38437. DR TRANSFAC; T00805; -. DR FlyBase; FBgn0003866; tsh. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 3. DR SMART; SM00355; ZnF_C2H2; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. KW Wnt signaling pathway; Developmental protein; KW Transcription regulation; Repressor; Activator; Zinc-finger; KW Metal-binding; Repeat; DNA-binding; Nuclear protein. FT DOMAIN 104 136 ALA-RICH. FT DOMAIN 175 183 ASP/GLU-RICH (ACIDIC). FT ZN_FING 354 378 C2H2-TYPE 1. FT ZN_FING 466 490 C2H2-TYPE 2. FT ZN_FING 533 557 C2H2-TYPE 3. FT DOMAIN 104 107 POLY-ALA. FT DOMAIN 115 122 POLY-ALA. FT DOMAIN 175 180 POLY-GLU. FT DOMAIN 401 407 POLY-PRO. FT DOMAIN 830 834 POLY-ASN. SQ SEQUENCE 993 AA; 106206 MW; 2DF9C6774F68B6D1 CRC64; MLHEALMLEI YRQALNAGAL PTARPRSTES ANSSERCPSH DSNSSEHGGG AGSGGVGHRL DAAALSTGVM PGEGPTTLHS SFPAVPQSLP SQPPSMEAYL HMVAAAAQQY GFPLAAAAAA GAGPRLPLPL ANEAAAPFKL PPQASPTASS NNSEALDFRT NLYGRAESAE PPASEGEEEE FDDGANNPLD LSVGTRKRGH ESEPQLGHIQ VKKMFKSDSP PANSVASPSA SQLLPGVNPY LAAVAAANIF RAGQFPDWNS KNDLVVDPLE KMSDIVKGGA SGMGTKEKMH SSKATTPQAA SQPPKSPVQP TPNQNSESGG GSGGGAAGSG AVTKARHNIW QSHWQNKGVA SSVFRCVWCK QSFPTLEALT THMKDSKHCG VNVPPFGNLP SNNPQPQHHH PTPPPPPQNH NLRKHSSGSA SNHSPSANVK NAFQYRGDPP TPLPRKLVRG QNVWLGKGVE QAMQILKCMR CGESFRSLGE MTKHMQETQH YTNILSQEQS ISIKSGNANA NSDAKESHNS LSSEESRTLS AVLTCKVCDK AFNSLGDLSN HMAKNNHYAE PLLQSAGARK RPAPKKREKS LPVRKLLEMK GGSGTTQEDH SNEKTSVQGK PGLGPGGGDK NDAALFAERM RQYITGVKAP EEIAKVAAAQ LLAKNKSPEL VEQKNGGQQR LRASSVLSAI EQMFTTSFDT PPRHASLPAS SPSNSSTKNT SPVASSILKR LGIDETVDYN KPLIDTNDPY YQHYRYTSSE RSGSECSAEA RPRLDAPTPE KQQQGGGHDE ESSKPAIKQE REAESKPVKM EIKSEFVDEP NEAEETSKME AAVVNGSATN NNNNIVERSS PKTPSSAASP QTRLLPPRSP AESQRSVTPK SPASSHKSYD GSSEGTKKFP SDSLNALSSM FDSLGSSGAG ANSRAKLAGR SCCWRIRISR EPHRRGELLG GLATILREEG EDRLSPRAET KRETESFALF SLFRAKRIFN IFWFVSALPS PRT // ID TSL_DROME STANDARD; PRT; 356 AA. AC P40689; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Torso-like protein precursor. GN TSL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=94150705; PubMed=8107870; RA Martin J.-R., Raibaud A., Ollo R.; RT "Terminal pattern elements in Drosophila embryo induced by the torso- RT like protein."; RL Nature 367:741-745(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94102536; PubMed=8276237; RA Savant-Bhonsale S., Montell D.J.; RT "Torso-like encodes the localized determinant of Drosophila terminal RT pattern formation."; RL Genes Dev. 7:2548-2555(1993). CC -!- FUNCTION: PROBABLE LIGAND THAT BINDS TO THE TORSO RECEPTOR. CC IMPLICATED IN A RECEPTOR TYROSINE KINASE SIGNALLING PATHWAY THAT CC SPECIFIES TERMINAL CELL FATE. CC -!- TISSUE SPECIFICITY: RESTRICTED TO SPECIALIZED CATEGORIES OF CC FOLLICLE CELLS LOCALIZED AT THE POLES OF THE EGG CHAMBER. CC -!- DEVELOPMENTAL STAGE: AT EARLY BLASTODERM STAGE, FORMS A CC SYMMETRICAL CONCENTRATION GRADIENT AT THE POLES ON THE SURFACE OF CC THE DEVITELLINIZED EMBRYO. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z30342; CAA82998.1; -. DR EMBL; X75614; CAA53285.1; -. DR PIR; S42388; S42388. DR FlyBase; FBgn0003867; tsl. DR InterPro; IPR001862; MAC_perforin. DR SMART; SM00457; MACPF; 1. KW Developmental protein; Glycoprotein; Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 356 TORSO-LIKE PROTEIN. FT CARBOHYD 74 74 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 141 141 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 190 190 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 225 225 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 267 267 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 296 296 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 1 5 MLSDA -> MR (IN REF. 2). FT CONFLICT 87 87 P -> L (IN REF. 2). SQ SEQUENCE 356 AA; 41440 MW; 0200FD23C17DB20F CRC64; MLSDASWPGL FWLLTLALLA DGGRRESQLR IGKAINIFLR YGYLGISMRV IPLNDNSEPD RWVFKEPTKN IYRNLSGLAE SHEDTTPGIF HGDFHMEFCE NRRQLFQAYF RDFSIERMDK PWEAFTGGWF PDNAAKKLGI NTSFIQGDYS YVLVRVVRFR ETGRLNAEIP VHQPLEPDVR SRMDQLQIGN ITSAVRFMED VGTHYVNSYT TGNSLYQVFV YSRKNYSMIK ERIKSKGLNG LSKLDLYNYF APWFAAHLGQ IRSASANATV ERWARRKLQY EYYVVKYVTL LKLHGNSTLL RSLDSLLGND AILQLDLKSL KPIFREEPEK ESWYHEVLDN NVKLWELNMP QSHPTR // ID TTKA_DROME STANDARD; PRT; 813 AA. AC P42282; Q24313; DT 01-NOV-1995 (Rel. 32, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tramtrack protein, alpha isoform (Tramtrack p88) (Fushi tarazu DE repressor protein). GN TTK OR FTZ-F2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93279467; PubMed=8504931; RA Xiong W.C., Montell C.; RT "Tramtrack is a transcriptional repressor required for cell fate RT determination in the Drosophila eye."; RL Genes Dev. 7:1085-1096(1993). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Embryo; RX MEDLINE=92191990; PubMed=1372245; RA Read D., Manley J.L.; RT "Alternatively spliced transcripts of the Drosophila tramtrack gene RT encode zinc finger proteins with distinct DNA binding RT specificities."; RL EMBO J. 11:1035-1044(1992). CC -!- FUNCTION: BINDS TO A NUMBER OF SITES IN THE TRANSCRIPTIONAL CC REGULATORY REGION OF FTZ. ISOFORM ALPHA IS REQUIRED TO REPRESS CC GENES THAT PROMOTE THE R7 CELL FATE. PROBABLE REPRESSOR OF THE CC TRANSCRIPTION OF THE SEGMENTATION GENES FTZ, EVE, H, ODD, RUN, AND CC EN. MAY BIND TO THE REGION AGGGC/TGG. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Alpha; Synonyms=p88; CC IsoId=P42282-1; Sequence=Displayed; CC Name=Beta; Synonyms=p59; CC IsoId=P17789-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 2 C2H2-TYPE ZINC FINGERS. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-3 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X71626; CAA50633.1; -. DR EMBL; Z11723; CAA77785.1; -. DR EMBL; Z11723; CAA77786.1; ALT_INIT. DR PIR; S36018; S36018. DR TRANSFAC; T00844; -. DR FlyBase; FBgn0003870; ttk. DR GO; GO:0005700; C:polytene chromosome; IDA. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR InterPro; IPR000637; AT_hook. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00384; AT_hook; 1. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. KW Transcription regulation; Zinc-finger; Metal-binding; DNA-binding; KW Nuclear protein; Alternative splicing. FT DOMAIN 33 98 BTB. FT ZN_FING 610 638 C2H2-TYPE 1. FT ZN_FING 646 669 C2H2-TYPE 2. FT CONFLICT 186 186 L -> V (IN REF. 2). FT CONFLICT 358 358 R -> P (IN REF. 2). FT CONFLICT 524 524 Q -> E (IN REF. 2). SQ SEQUENCE 813 AA; 88441 MW; 54E721DB4928DF38 CRC64; MKMASQRFCL RWNNHQSNLL SVFDQLLHAE TFTDVTLAVE GQHLKAHKMV LSACSPYFNT LFVSHPEKHP IVILKDVPYS DMKSLLDFMY RGEVSVDQER LTAFLRVAES LRIKGLTEVN DDKPSPAAAA AGAGATGSES TATTPQLQRI QPYLVPQRNR SQAGGLLASA ANAGNTPTLP VQPSLLSSAL MPKRKRGRPR KLSGSSNGTG NDYDDFDREN MMNDSSDLGN GKMCNESYSG NDDGSDDNQP NAGHTDDLNE SRDSLPSKRS KNSKDHRVVS HHEDNSTSVT PTKATPELSQ RLFGSSSTTI SATAPGGSST GPSETISLLE ISDERESAPV HLPTILGLKI RAINTTTRAQ QGSPQTPTKS KPKIRQATGS NNSNSLLKQQ LRGGAKDPEV PPATRITGAV TPNAALNAEE QSKEMPKKNQ DEVNACIGLH SLANAAEQQA AQVASTGNLH HQLLLHMAAN NSMLNTTDYY QQQQQESPSS AGQFMDDDLE LLSLNDQQDK SDEPDHEMVT LADQNAGLPG YQGNEAEATP AQEDSPAAET ATAPPPAPRS GKKGAKRPIQ RRRVRRKAQS TLDDQAEHLT EMSVRGLDLF RYASVVEGVY RCTECAKENM QKTFKNKYSF QRHAFLYHEG KHRKVFPCPV CSKEFSRPDK MKNHLKMTHE NFTPPKDIGA FSPLKYLISA AAAGDMHATI YQQQQDHYHR QLAEQLEQQN ASFDSRDSSL ILPDVKMEHA EDQDAEQEAE LSDGGYDASN PAAAAAAMLS LQQDVIIKDE IQISPSPSPT PPASCAVAEG KSLALASTAQ TAT // ID TTKB_DROME STANDARD; PRT; 643 AA. AC P17789; Q9V9V3; DT 01-AUG-1990 (Rel. 15, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tramtrack protein, beta isoform (Tramtrack p69) (Fushi tarazu DE repressor protein). GN TTK OR FTZ-F2 OR CG1856. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=90107945; PubMed=2104801; RA Harrison S.D., Travers A.A.; RT "The tramtrack gene encodes a Drosophila finger protein that RT interacts with the ftz transcriptional regulatory region and shows a RT novel embryonic expression pattern."; RL EMBO J. 9:207-216(1990). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RA Brown J.L., Sonoda S., Ueda H., Scott M.P., Wu C.; RT "Repression of the Drosophila fushi tarazu (ftz) segmentation gene."; RL Submitted (XXX-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=93279467; PubMed=8504931; RA Xiong W.C., Montell C.; RT "Tramtrack is a transcriptional repressor required for cell fate RT determination in the Drosophila eye."; RL Genes Dev. 7:1085-1096(1993). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP DNA-BINDING STUDIES. RX MEDLINE=92349422; PubMed=1640455; RA Fairall L., Harrison S.D., Travers A.A., Rhodes D.; RT "Sequence-specific DNA binding by a two zinc-finger peptide from the RT Drosophila melanogaster Tramtrack protein."; RL J. Mol. Biol. 226:349-366(1992). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 499-561. RX MEDLINE=94067350; PubMed=8247159; RA Fairall L., Schwabe J.W.R., Chapman L., Finch J.T., Rhodes D.; RT "The crystal structure of a two zinc-finger peptide reveals an RT extension to the rules for zinc-finger/DNA recognition."; RL Nature 366:483-487(1993). CC -!- FUNCTION: BINDS TO A NUMBER OF SITES IN THE TRANSCRIPTIONAL CC REGULATORY REGION OF FTZ. ISOFORM BETA IS REQUIRED TO REPRESS CC INAPPROPRIATE SEGMENTATION GENE TRANSCRIPTION AND REPRESS GENES CC INCOMPATIBLE WITH DEVELOPMENT OF PHOTORECEPTOR CELL FATES. CC PROBABLE REPRESSOR OF THE TRANSCRIPTION OF THE SEGMENTATION GENES CC FTZ, EVE, H, ODD, RUN, AND EN. MAY BIND TO THE REGION AGGGC/TGG. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Beta; Synonyms=p59; CC IsoId=P17789-1; Sequence=Displayed; CC Name=Alpha; Synonyms=p88; CC IsoId=P42282-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT EMBRYOGENESIS. EXPRESSED CC IN YOLK NUCLEI DURING THE FAST PHASE OF GERMBAND ELONGATION. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 2 C2H2-TYPE ZINC FINGERS. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-3 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17121; CAA34981.1; ALT_INIT. DR EMBL; M62856; AAA28544.1; ALT_INIT. DR EMBL; X71627; CAA50634.1; -. DR EMBL; AE003779; AAF57181.1; -. DR PIR; S36017; S36017. DR PDB; 2DRP; 31-AUG-94. DR TRANSFAC; T00843; -. DR FlyBase; FBgn0003870; ttk. DR GO; GO:0005700; C:polytene chromosome; IDA. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR InterPro; IPR000637; AT_hook. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00384; AT_hook; 1. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. KW Transcription regulation; Zinc-finger; Metal-binding; DNA-binding; KW Nuclear protein; 3D-structure; Alternative splicing. FT DOMAIN 33 98 BTB. FT ZN_FING 508 531 C2H2-TYPE 1. FT ZN_FING 538 561 C2H2-TYPE 2. FT CONFLICT 255 255 T -> M (IN REF. 2). FT CONFLICT 281 281 H -> Q (IN REF. 2). FT CONFLICT 501 501 T -> I (IN REF. 2). SQ SEQUENCE 643 AA; 68770 MW; 98DAEA1A5E97DC59 CRC64; MKMASQRFCL RWNNHQSNLL SVFDQLLHAE TFTDVTLAVE GQHLKAHKMV LSACSPYFNT LFVSHPEKHP IVILKDVPYS DMKSLLDFMY RGEVSVDQER LTAFLRVAES LRIKGLTEVN DDKPSPAAAA AGAGATGSES TATTPQLQRI QPYLVPQRNR SQAGGLLASA ANAGNTPTLP VQPSLLSSAL MPKRKRGRPR KLSGSSNGTG NDYDDFDREN MMNDSSDLGN GKMCNESYSG NDDGSDDNQP NAGHTDDLNE SRDSLPSKRS KNSKDHRVVS HHEDNSTSDG NDSDGEGLDT SYMEPQLMLD EYDEPVEFKY NPLTDNSSPT QDHTDGSHLN EQARQQAFLI AAQRKHQVET AAAAAASGIK LNIIGMAAGG AQVKSMVSIP KLTPIGKVNA ASTPLVSPAG SFSTATVKPR VQKRPKLGKQ NGDVKPAVFS SQEYLDIYNS NDGFKLKAAG LSGSTPNLSA GLGTPSVKTK LNLSSNVGEG EAEGSVRDYC TKEGEHTYRC KVCSRVYTHI SNFCRHYVTS HKRNVKVYPC PFCFKEFTRK DNMTAHVKII HKIENPSTAL ATVAAANLAG QPLGVSGAST PPPPDLSGQN SNQSLPATSN ALSTSSSSST SSSSGSLGPL TTSAPPAPAA AAQ // ID TUBE_DROME STANDARD; PRT; 462 AA. AC P22812; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tube protein. GN TUBE. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91126085; PubMed=1899484; RA Letsou A., Alexander S., Orth K., Wasserman S.A.; RT "Genetic and molecular characterization of tube, a Drosophila gene RT maternally required for embryonic dorsoventral polarity."; RL Proc. Natl. Acad. Sci. U.S.A. 88:810-814(1991). RN [2] RP DOMAINS. RX MEDLINE=94074544; PubMed=8253071; RA Letsou A., Alexander S., Wasserman S.A.; RT "Domain mapping of tube, a protein essential for dorsoventral RT patterning of the Drosophila embryo."; RL EMBO J. 12:3449-3458(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 23-175 IN COMPLEX WITH RP PELLE. RX MEDLINE=20055599; PubMed=10589682; RA Xiao T., Towb P., Wasserman S.A., Sprang S.R.; RT "Three-dimensional structure of a complex between the death domains RT of Pelle and Tube."; RL Cell 99:545-555(1999). CC -!- FUNCTION: REQUIRED FOR THE DETERMINATION OF EMBRYONIC DORSOVENTRAL CC POLARITY. IS INVOLVED IN TRANSDUCTION OF INFORMATION REGULATING CC NUCLEAR IMPORT OF DORSAL PROTEIN. CC -!- SUBUNIT: INTERACTS WITH PELLE THROUGH THEIR RESPECTIVE N-TERMINAL CC DEATH DOMAINS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: MATERNAL AND ZYGOTIC GENE PRODUCT. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MAXIMALLY EARLY IN EMBRYOGENESIS, CC AND IN LATE LARVAL DEVELOPMENT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59501; AAA28994.1; -. DR PIR; A37862; A33170. DR PDB; 1D2Z; 29-NOV-99. DR FlyBase; FBgn0003882; tub. DR GO; GO:0005737; C:cytoplasm; NAS. DR GO; GO:0006966; P:antifungal humoral response (sensu Inverteb...; IMP. DR GO; GO:0009950; P:dorsal/ventral axis specification; NAS. DR GO; GO:0008063; P:Tl signaling pathway; NAS. DR InterPro; IPR000488; Death. DR Pfam; PF00531; death; 1. DR SMART; SM00005; DEATH; 1. KW Developmental protein; Repeat; Embryo; Transducer; 3D-structure. FT DOMAIN 262 460 5 X APPROXIMATE REPEATS. FT REPEAT 262 269 1. FT REPEAT 286 293 2. FT REPEAT 319 326 3. FT REPEAT 356 363 4. FT REPEAT 453 460 5. FT DOMAIN 388 401 ASP/GLU-RICH (ACIDIC). FT TURN 29 30 FT STRAND 32 32 FT HELIX 33 35 FT HELIX 38 49 FT HELIX 50 52 FT TURN 53 53 FT HELIX 54 60 FT STRAND 62 62 FT HELIX 67 71 FT TURN 73 74 FT HELIX 78 81 FT HELIX 82 84 FT STRAND 86 86 FT HELIX 90 102 FT TURN 105 106 FT HELIX 109 118 FT TURN 119 119 FT TURN 123 124 FT STRAND 128 128 FT HELIX 129 138 FT TURN 139 140 FT HELIX 142 151 FT TURN 152 153 FT TURN 165 166 FT STRAND 171 171 SQ SEQUENCE 462 AA; 49757 MW; C894CB3C5EBFF749 CRC64; MAYGWNGCGM GVQVNGSNGA IGLSSKYSRN TELRRVEDND IYRLAKILDE NSCWRKLMSI IPKGMDVQAC SGAGCLNFPA EIKKGFKYTA QDVFQIDEAA NRLPPDQSKS QMMIDEWKTS GKLNERPTVG VLLQLLVQAE LFSAADFVAL DFLNESTPAR PVDGPGALIS LELLEEEMEV DNEGLSLKYQ SSTATLGADA QGSVGLNLDN FEKDIVRRDK SVPQPSGNTP PIAPPRRQQR STTNSNFATL TGTGTTSTTI PNVPNLTILN PSEQIQEPVL QPRPMNIPDL SILISNSGDL RATVSDNPSN RTSSTDPPNI PRITLLIDNS GDVNSRPNHA PAKASTATTP TASSNNLPMI SALNISKGSK ETLRPESRSS SSSLSKDDDD DNDGEEDGEE EYPDAFLPNL SNSEQQSSNN DSSLTTVTGT SGDNSFELTN DSSSTSNDDY ACNIPDLSEL QQ // ID TUD_DROME STANDARD; PRT; 2515 AA. AC P25823; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Maternal tudor protein. GN TUD. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92038995; PubMed=1936993; RA Golumbeski G.S., Bardsley A., Tax F., Boswell R.E.; RT "Tudor, a posterior-group gene of Drosophila melanogaster, encodes a RT novel protein and an mRNA localized during mid-oogenesis."; RL Genes Dev. 5:2060-2070(1991). CC -!- FUNCTION: REQUIRED DURING OOGENESIS FOR THE FORMATION OF CC PRIMORDIAL GERM CELLS AND FOR NORMAL ABDOMINAL SEGMENTATION. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT THE LIFE CYCLE. CC -!- MISCELLANEOUS: THE TUD MRNA ACCUMULATES WITHIN THE POSTERIOR CC REGION OF THE DEVELOPING OOCYTE DURING THE EARLY TO MIDDLE STAGES CC OF OOGENESIS. CC -!- SIMILARITY: CONTAINS 9 TUDOR DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62420; CAA44286.1; -. DR PIR; A41519; A41519. DR HSSP; Q16637; 1G5V. DR FlyBase; FBgn0003891; tud. DR GO; GO:0019090; P:mitochondrial rRNA, mitochondrial export; IMP. DR GO; GO:0007315; P:pole plasm assembly; IMP. DR InterPro; IPR008191; Maternal_tudor. DR InterPro; IPR002999; Tudor. DR Pfam; PF00567; TUDOR; 10. DR SMART; SM00333; TUDOR; 10. DR PROSITE; PS50304; TUDOR; 9. KW Developmental protein; Repeat. FT DOMAIN 455 513 TUDOR 1. FT DOMAIN 641 696 TUDOR 2. FT DOMAIN 1062 1122 TUDOR 3. FT DOMAIN 1355 1414 TUDOR 4. FT DOMAIN 1662 1718 TUDOR 5. FT DOMAIN 1839 1898 TUDOR 6. FT DOMAIN 2023 2082 TUDOR 7. FT DOMAIN 2211 2269 TUDOR 8. FT DOMAIN 2392 2451 TUDOR 9. SQ SEQUENCE 2515 AA; 285236 MW; 683C100AD308BADA CRC64; MNGQARIALP SKVDLYITHV DHVGPYLKVY GHVNRDAASL ISERIRNLLP TCFAIEPSWS VERQQALLIP GTFCIFKNIN GPAPGDVEYR RIRVVSADLE GQSMRAEIDF VDFGYNRTVD SHDLMFPKQP KLLQNIPLHC FQYIVLGICS EWDQTDLAEV RRLVVNQIVK ITVEPTQICD QKFASLRWKD FELNEFLVQQ KQIGVSVDKQ LMMDHCKKLW KDNPQSPVTE YNNNSIHNSK TPMEIAREQL AVRQSLAARL DAQRSVQVTP SRPLNADAPD YTPKHLPLVN VTNVQVQMPG LNNTQKPVFV STNPYNRANY QPAVPAAQPY VPKANPRSQY TYYNVRMNKP INAMPPPAGP HVPIQHFNQQ ANNVSLSYVP ARFTPPPTPS IAQHQIPIPA FRTTSLTVGL TYDVVISYVE NGPYLFWVHL KSSDHDLSTM MGQIERTKLK ALAQAPELGT ACVARFSEDG HLYRAMVCAV YAQRYRVVYV DYGNSELLSA SDLFQIPPEL LEIKPFAFRF ALAGTKEIEP IDDSMKRIFK KSAIYRNFEL TVQAPESVGS MQTCHLNQNG TNMLELLRQL KNSRQSYKKA EQLENDDAVE IRFIDSPSNF YVQKVANIGK FEQLMDEMFS YYNATREFPD QLILGAPCIV KCDQEWYRAE ILRVDDSVIV RHVDFGYEQN VKRHLIGHIA EKHLEMPRQA IKCCLKGFEN SELSEDKITD QFEMLAEESN IRRRTFSVRI FRIEPDGLNV VNLLAKNLNV MKKLYKLSMP FEQYLSLEKG QFNANNTRAE SVISSELNKS HILNSTSIGE TENRLQEQEK EQQQKKVDVR QQQLAVEIPQ AVKSVSGSKN STDWDKRSST SAGSKDSKRQ QQQQIQRIDR HLDFSCETQS TGSYSSGMSS PRKGNRQQNG RTPIQSPRHN EKQEAKKNAR FSNSESPRRS RDGQQGNQRS QNAPQGYAQK PQRQKSTLDG NISSKRSSGV GSDIASSSSE SVAAAKPEKY VSLDKPYALQ EMKTPSKEAA SLSWWLSPFQ FYIVPKSVSA KYDNIMRDMR EFYRQKQHQP LQLKVGSTVV VRQRKDNAIL RATVTACNHM MRKYRVFCVD TGSLITVTSE DIWQLEQRFA DPPCMAHRCS FHSVVTNYDP LYIVDRMETF VPVNAKVDCE FVSKEKSNQG SNTSSTCSYT VNIFVNGASL RDMLVKAEFL TEVAPEIRVN LLAGQQIRGK FTSIRDMTSF KVQFDYGNNV NFLCTYDDAK FVKSNPNLAR RFKEFYEGKS FALNVKNVCE NNIVHLRPVM PLFMEDRRSF ICPYPVVLSS FQALVVYTAK PYRVYVQPQA IVPSMQTLLD NMYEHYKAKG DSLKKFDVGQ ICAVRSSDGN WYRARISGKD SNAACFEVFY IDYGNTEEIK RDDIKALDAK FYEHASGFAV EINLPIGRPS NDTKLKARIS EILEEKVVTI KSIEVRRSHL IADVILENNQ SVIDLLKAEK LVPGKDLDYM RKQMEKGKSR TYEYIETVDL TLDEEEDKGR KETVSKSGSA NASPKKKQHN DKDREPKKSK PAEPARTVAP QPVALKTPSP VPAEPAPVPK PATPVPEVVE VPEINPTVRE AAAESKQAPA QEDPYKDLDC VVLSHCDNPA QFYVHPIDQL SKLNQLHENL QIVSPSLPQL MNVVNGADCV SMYSVDKCWY RAKIIDAELM VLLFIDYGNT DCVSDATDIK ESMWSHIEPF CLPCALPIRP KGTADWVDAA NGIFNESYSK VPRLEYLTQG DHITTSYVNM YIDGEDVAKK LIADGFARPL EYLASGCSCY ISHVNGICDF FIQLERDSKA LELIELYLRK KDTLKPLEGF EKGLIVAALF EDDELWYRAQ LQKELPDSRY EVLFIDYGNT STTSKCLMLS EEIASLPSLS KKCSLQLPDA YISWSPEAEA KFAELTGEGE LVFTTQLLKP GQDHVTIDLL LDGENIIDRL LPLCQRKEPK EASKESLAVT TKAIITHVEN TSRIYLQFSE KDSLMDIICE KLNGSKLQPK TEKAAVDDMC VVQFADDLEF YRSRILEVLE DDQYKVILID YGNTTVVDKL YELPQEFTLI KPVAEICSME PSAIFEKNKA LTLTTFDALL DSCKGVVAVE FVNKSASPPV VRLTTKDKRS LKIYEHLQKL VQAELKLIQK RNENSECIIS YGNSPKSFYV QMKHNSADLD LIVKTLQSLK KEKLKKLIDP TTNSNGVCYS QEDACYYRCS IKSVLDPSQG FEVFLLDYGN TLVVPEVWQL PQEIEPIPSL ALHCQLSKIP MDVSDEKLEE AFAALLEQHF GELYEITTQP NEDETKPLIA ELRINYKDFV QELVSTVTGV QKPLEAELHN CVVVQFDGPM SFYVQMESDV PALEQMTDKL LDAEQDLPAF SDLKEGALCV AQFPEDEVFY RAQIRKVLDD GKCEVHFIDF GNNAVTQQFR QLPEELAKPA RYSRHCELDA STISKCDAAL LQSFIDTRFS ETFQVEILAT KGTGTHVVRL FYQSKNISEK LQECQ // ID TWIN_DROME STANDARD; PRT; 426 AA. AC Q03019; Q9V454; DT 01-JUL-1993 (Rel. 26, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cdc25-like protein phosphatase twine (EC 3.1.3.48). GN TWE OR CG4965. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92298395; PubMed=1606618; RA Alphey L.S., Jimenez J., White-Cooper H., Dawson I., Nurse P., RA Glover D.M.; RT "Twine, a cdc25 homolog that functions in the male and female RT germline of Drosophila."; RL Cell 69:977-988(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SEQUENCE OF 32-426 FROM N.A. RX MEDLINE=93161947; PubMed=1286615; RA Courtot C., Fankhauser C., Simanis V., Lehner C.F.; RT "The Drosophila cdc25 homolog twine is required for meiosis."; RL Development 116:405-416(1992). CC -!- FUNCTION: REQUIRED DURING MEIOSIS. REGULATES THE TRANSITION FROM CC THE EXTENDED G2 PHASE TO THE ONSET OF THE FIRST MEIOTIC DIVISION. CC -!- CATALYTIC ACTIVITY: PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN CC TYROSINE + PHOSPHATE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN DEVELOPING MALE AND FEMALE GERM CC CELLS. CC -!- SIMILARITY: BELONGS TO THE MPI PHOSPHATASE FAMILY. CC -!- SIMILARITY: CONTAINS 1 RHODANESE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M94158; AAA28413.1; -. DR EMBL; AE003650; AAF53508.1; -. DR EMBL; AY061266; AAL28814.1; -. DR EMBL; X69018; CAA48783.1; -. DR EMBL; AE003415; AAF44991.1; -. DR PIR; A41910; A41910. DR HSSP; P30305; 1QB0. DR FlyBase; FBgn0002673; twe. DR GO; GO:0009795; P:embryonic morphogenesis; IMP. DR GO; GO:0007140; P:male meiosis; IMP. DR GO; GO:0007348; P:regulation of syncytial blastoderm mitotic ...; IMP. DR GO; GO:0007283; P:spermatogenesis; IMP. DR InterPro; IPR000751; MPI_Phosphatase. DR InterPro; IPR001763; Rhodanese-like. DR Pfam; PF00581; Rhodanese; 1. DR PRINTS; PR00716; MPIPHPHTASE. DR SMART; SM00450; RHOD; 1. DR PROSITE; PS50206; RHODANESE_3; 1. KW Cell division; Meiosis; Hydrolase. FT DOMAIN 265 371 RHODANESE. FT ACT_SITE 318 318 BY SIMILARITY. FT CONFLICT 48 48 L -> M (IN REF. 5). SQ SEQUENCE 426 AA; 48320 MW; 0F8626692B683D08 CRC64; MASKRLMLDV EEEDDESGAC GQENFDPHDA DMEYQAKRRK SAVQETPLQW MLKRHIPAST TVLSPITELS QNMNGARLDG TPKSTQRIPA NRTLNNFNSL SSRTLGSFSS SCSSYESGNS LDDEYMDMFE MESAENHNLE LPDDLEVLLS GQLKSESNLE EMSNKKGSLR RCLSMYPSEQ PEEAVQEPDQ ETNMPMKKMQ RKTLSMNDAE IMRALGDEPE LIGDLSKPCT LPCLATGIRH RDLKTISSDT LARLIQGEFD EQLGSQGGYE IIDCRYPYEF LGGHIRGAKN LYTRGQIQEA FPTLTSNQEN RRIYVFHCEF SSERGPKLLR YLRSNDRSQH THNYPALDYP ELYILHNGYK EFFGLYSQLC QPSQYVPMLA PAHNDEFRYF RAKTKSWQCG EGGDSGIGGG GSRGLRKSRS RLLYAE // ID TWST_DROME STANDARD; PRT; 490 AA. AC P10627; Q9W1W1; DT 01-JUL-1989 (Rel. 11, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Twist protein. GN TWI OR CG2956. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=88329004; PubMed=3416836; RA Thisse B., Stoetzel C., Gorostiza-Thisse C., Perrin-Schmitt F.; RT "Sequence of the twist gene and nuclear localization of its protein RT in endomesodermal cells of early Drosophila embryos."; RL EMBO J. 7:2175-2183(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: TWIST IS INVOLVED IN THE ESTABLISHMENT OF GERM LAYERS CC IN DROSOPHILA EMBRYOS. CC -!- SUBUNIT: EFFICIENT DNA BINDING REQUIRES DIMERIZATION WITH ANOTHER CC BHLH PROTEIN. HOMODIMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: MESODERMAL GERM LAYER. CC -!- SIMILARITY: CONTAINS 1 BASIC HELIX-LOOP-HELIX (BHLH) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12506; CAA31024.1; -. DR EMBL; X14569; CAA32707.1; -. DR EMBL; AE003459; AAF46941.1; -. DR PIR; S00995; S00995. DR HSSP; P25912; 1AN2. DR TRANSFAC; T01517; -. DR FlyBase; FBgn0003900; twi. DR GO; GO:0016563; F:transcriptional activator activity; NAS. DR GO; GO:0007499; P:ectoderm/mesoderm interaction; NAS. DR GO; GO:0007369; P:gastrulation; NAS. DR GO; GO:0045944; P:positive regulation of transcription from P...; NAS. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Differentiation; Developmental protein; Nuclear protein; DNA-binding; KW Transcription regulation. FT DOMAIN 48 70 GLN/HIS-RICH. FT DOMAIN 178 189 GLN-RICH. FT DOMAIN 244 263 GLN-RICH. FT DNA_BIND 362 374 BASIC DOMAIN. FT DOMAIN 375 414 HELIX-LOOP-HELIX MOTIF. FT CONFLICT 44 44 Q -> H (IN REF. 1). FT CONFLICT 112 112 T -> A (IN REF. 1). FT CONFLICT 251 251 L -> Q (IN REF. 1). FT CONFLICT 453 453 A -> G (IN REF. 1; CAA31024). SQ SEQUENCE 490 AA; 54422 MW; AEB0D4D4EEE97DB7 CRC64; MMSARSVSPK VLLDISYKPT LPNIMELQNN VIKLIQVEQQ AYMQSGYQLQ HQQQHLHSHQ HHQQHHQQQH AQYAPLPSEY AAYGITELED TDYNIPSNEV LSTSSNQSAQ STSLELNNNN TSSNTNSSGN NPSGFDGQAS SGSSWNEHGK RARSSGDYDC QTGGSLVMQP EHKKLIHQQQ QQQQQHQQQI YVDYLPTTVD EVASAQSCPG VQSTCTSPQS HFDFPDEELP EHKAQVFLPL YNNQQQQSQQ LQQQQPHQQS HAQMHFQNAY RQSFEGYEPA NSLNGSAYSS SDRDDMEYAR HNALSSVSDL NGGVMSPACL ADDGSAGSLL DGSDAGGKAF RKPRRRLKRK PSKTEETDEF SNQRVMANVR ERQRTQSLND AFKSLQQIIP TLPSDKLSKI QTLKLATRYI DFLCRMLSSS DISLLKALEA QGSPSAYGSA SSLLSAAANG AEADLKCLRK ANGAPIIPPE KLSYLFGVWR MEGDAQHQKA // ID TY3H_DROME STANDARD; PRT; 579 AA. AC P18459; Q24000; Q8SY95; DT 01-NOV-1990 (Rel. 16, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tyrosine 3-monooxygenase (EC 1.14.16.2) (Tyrosine 3-hydroxylase) (TH) DE (Protein Pale). GN PLE OR TH OR CG10118. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS NEURONAL AND HYPODERMAL). RX MEDLINE=90166583; PubMed=2483109; RA Neckameyer W.S., Quinn W.G.; RT "Isolation and characterization of the gene for Drosophila tyrosine RT hydroxylase."; RL Neuron 2:1167-1175(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM NEURONAL). RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PLAYS AN IMPORTANT ROLE IN THE PHYSIOLOGY OF ADRENERGIC CC NEURONES. CC -!- CATALYTIC ACTIVITY: L-TYROSINE + TETRAHYDROPTERIDINE + O(2) = 3,4- CC DIHYDROXY-L-PHENYLALANINE + DIHYDROPTERIDINE + H(2)O. CC -!- COFACTOR: FERROUS ION. CC -!- PATHWAY: CATECHOLAMINE BIOSYNTHESIS; FIRST STEP. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Neuronal; CC IsoId=P18459-1; Sequence=Displayed; CC Name=Hypodermal; CC IsoId=P18459-2; Sequence=VSP_000545; CC -!- SIMILARITY: BELONGS TO THE BIOPTERIN-DEPENDENT AROMATIC AMINO ACID CC HYDROXYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U14395; AAA62876.1; -. DR EMBL; U14395; AAA62877.1; -. DR EMBL; X76209; CAA53802.1; -. DR EMBL; AE003561; AAN12080.1; -. DR EMBL; AE003561; AAF50648.1; -. DR EMBL; AY071698; AAL49320.1; -. DR PIR; A55369; A55369. DR HSSP; P04177; 1TOH. DR FlyBase; FBgn0005626; ple. DR GO; GO:0004511; F:tyrosine 3-monooxygenase activity; NAS. DR GO; GO:0006584; P:catecholamine metabolism; NAS. DR GO; GO:0007619; P:courtship behavior; NAS. DR InterPro; IPR001273; Aaa_hydroxylase. DR InterPro; IPR005962; Tyr_3_monox. DR Pfam; PF00351; biopterin_H; 1. DR PRINTS; PR00372; FYWHYDRXLASE. DR ProDom; PD002559; Aaa_hydroxylase; 1. DR TIGRFAMs; TIGR01269; Tyr_3_monoox; 1. DR PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1. KW Catecholamine biosynthesis; Oxidoreductase; Monooxygenase; Iron; KW Neurotransmitter biosynthesis; Alternative splicing. FT METAL 409 409 IRON (BY SIMILARITY). FT METAL 414 414 IRON (BY SIMILARITY). FT METAL 454 454 IRON (BY SIMILARITY). FT VARSPLIC 60 130 Missing (in isoform Hypodermal). FT /FTId=VSP_000545. FT CONFLICT 264 264 P -> L (IN REF. 3). SQ SEQUENCE 579 AA; 65995 MW; 416CF26E04087E85 CRC64; MMAVAAAQKN REMFAIKKSY SIENGYPSRR RSLVDDARFE TLVVKQTKQT VLEEARSKAN DDSLEDCIVQ AQEHIPSEQD VELQDEHANL ENLPLEEYVP VEEDVEFESV EQEQSESQSQ EPEGNQQPTK NDYGLTEDEI LLANAASESS DAEAAMQSAA LVVRLKEGIS SLGRILKAIE TFHGTVQHVE SRQSRVEGVD HDVLIKLDMT RGNLLQLIRS LRQSGSFSSM NLMADNNLNV KAPWFPKHAS ELDNCNHLMT KYEPDLDMNH PGFADKVYRQ RRKEIAEIAF AYKYGDPIPF IDYSDVEVKT WRSVFKTVQD LAPKHACAEY RAAFQKLQDE QIFVETRLPQ LQEMSDFLRK NTGFSLRPAA GLLTARDFLA SLAFRIFQST QYVRHVNSPY HTPEPDSIHE LLGHMPLLAD PSFAQFSQEI GLASLGASDE EIEKLSTVYW FTVEFGLCKE HGQIKAYGAG LLSSYGELLH AISDKCEHRA FEPASTAVQP YQDQEYQPIY YVAESFEDAK DKFRRWVSTM SRPFEVRFNP HTERVEVLDS VDKLETLVHQ MNTEILHLTN AISKLRRPF // ID TYDP_DROME STANDARD; PRT; 580 AA. AC Q9VQM4; Q9NFM9; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Probable tyrosyl-DNA phosphodiesterase (EC 3.1.4.-) (Tyr-DNA DE phosphodiesterase) (Glaikit protein). GN TDP1 OR GKT OR CG8825 OR CG8826. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=20400110; PubMed=10940635; RA Dunlop J., Corominas M., Serras F.; RT "The novel gene glaikit, is expressed during neurogenesis in the RT Drosophila melanogaster embryo."; RL Mech. Dev. 96:133-136(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: INVOLVED IN REPAIRING COVALENT TOPOISOMERASE I-DNA CC COMPLEXES. TO MODULATE THE TOPOLOGICAL CHANGES INDUCED DURING DNA CC REPLICATION AND TRANSCRIPTION, TOPOISOMERASE I TRANSIENTLY BREAKS CC A DNA STRAND AND FORMS A COVALENT LINKAGE BETWEEN THE ACTIVE-SITE CC TYROSINE AND THE 3'PHOSPHATE OF THE BROKEN DNA STRAND. THE STRAND CC IS SUBSEQUENTLY RE-LIGATED BY NUCLEOPHILIC ATTACK OF THE CC 5'HYDROXYL ON THIS PHOSPHODIESTER BOND. UNDER CERTAIN CONDITIONS, CC NUCLEOPHILIC ATTACK OF THE 5'HYDROXYL DOES NOT OCCUR AND THE CC TOPOISOMERASE I FORMS A STALLED COVALENT COMPLEX WITH THE DNA. CC EFFICIENT REPAIR OF THESE STALLED COMPLEXES REQUIRES AN ENZYME CC THAT CATALYZES THE HYDROLYSIS OF THE PHOSPHODIESTER BOND BETWEEN CC THE TYROSINE RESIDUE AND THE DNA 3'PHOSPHATE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CATALYZES THE HYDROLYSIS OF A PHOSPHODIESTER CC BOND BETWEEN A TYROSINE RESIDUE AND A DNA 3'PHOSPHATE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE DELAMINATING NEUROBLASTS OF CC THE EMBRYONIC CENTRAL NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: AT THE EARLIEST STAGES OF EMBRYONIC CC DEVELOPMENT THE EXPRESSION IS UBIQUITOUS, BUT BY THE TIME THE CC NEUROBLASTS ARE DELAMINATING, THE EXPRESSION BECAME RESTRICTED TO CC NEUROBLASTS AND A FEW GANGLION MOTHER CELLS. CC -!- SIMILARITY: BELONGS TO THE PHOSPHOLIPASE D FAMILY. CC -!- SIMILARITY: CONTAINS 2 PLD PHOSPHODIESTERASE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ277122; CAB86488.1; -. DR EMBL; AE003580; AAF51141.1; -. DR EMBL; AY051884; AAK93308.1; -. DR FlyBase; FBgn0031506; Tdp1. KW Hydrolase; DNA repair; Repeat; Nuclear protein. FT DOMAIN 87 94 POLY-SER. FT DOMAIN 243 274 PLD PHOSPHODIESTERASE 1. FT DOMAIN 483 507 PLD PHOSPHODIESTERASE 2. FT ACT_SITE 248 248 NUCLEOPHILE IN THE FIRST STEP OF THE FT CATALYTIC REACTION. FT CONFLICT 214 214 L -> V (IN REF. 1). FT CONFLICT 300 300 G -> R (IN REF. 1). FT CONFLICT 310 310 L -> R (IN REF. 1). FT CONFLICT 327 327 A -> P (IN REF. 1). FT CONFLICT 407 407 L -> P (IN REF. 1). FT CONFLICT 455 455 K -> N (IN REF. 1). SQ SEQUENCE 580 AA; 64193 MW; 14EC03C1E993BE87 CRC64; MKECPYGEKC YRKNPIHFGE FSHAHLDAIY AKGNESGDYE IPANYSSEMI HTQLKLLEKL FPKQATNKEQ EAHSSSSKPA VTAPVASGSS SSGSLDTNPS GSSASGPAAS QDTSNLAKKQ KLNAKNIRDY IPVVIEKGGM AKKLERAAPY NMFLTAITDS KPTHSEPLSI TLQEILDESL GEIESTVQIN FMVDIGWLLG HYYFAGILDK PLLLLYGDES PELLSIGKFK QQVTAIRVKM PTPFATSHTK MMFLGYSDGS MRVVISTANL YEDDWHNRTQ GLWISPKLPA LPVDADTGAG ESLTGFKQDL MLYLVEYKIS QLQPWIARIR NSDFSAINVF FLGSVPGGHR EGSVRGHPWG HARLASLLAK HAAPIDDRIP VVCQSSSIGS LGANVQAWIQ QDFVNSLKKD STPVGKLRQM PPFKMIYPSY GNVAGSHDGM LGGGCLPYGK NTNDKQPWLK DYLQQWKSSD RFRSRAMPHI KSYTRFNLED QSVYWFVLTS ANLSKAAWGC FNKNSNIQPC LRIANYEAGV LFLPRFVTGE DTFPLGNNRD GVPAFPLPYD VPLTPYAPDD KPFLMDYLQG // ID TYSY_DROME STANDARD; PRT; 321 AA. AC O76511; Q9VQJ3; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Thymidylate synthase (EC 2.1.1.45) (TS) (TSase). GN TS OR CG3181. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Tsoi S.C.M., Huang S.M., Sander M.; RT "Genomic organization of the Drosophlia 23C genetic interval: RT identification of 3 genes in the 10Kb region surrounding the RRP1 RT gene."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: 5,10-METHYLENETETRAHYDROFOLATE + DUMP = CC DIHYDROFOLATE + DTMP. CC -!- PATHWAY: DEOXYRIBONUCLEOTIDE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE THYMIDYLATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF073994; AAC27622.1; -. DR EMBL; AE003581; AAF51176.1; -. DR HSSP; P04818; 1HW4. DR FlyBase; FBgn0024920; Ts. DR InterPro; IPR000398; Thymidylat_synth. DR Pfam; PF00303; thymidylat_synt; 1. DR PRINTS; PR00108; THYMDSNTHASE. DR ProDom; PD001180; Thymidylat_synt; 1. DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1. KW Transferase; Methyltransferase; Nucleotide biosynthesis. FT ACT_SITE 201 201 BY SIMILARITY. FT CONFLICT 193 193 I -> M (IN REF. 1). SQ SEQUENCE 321 AA; 36657 MW; DCBC920153990CFE CRC64; MVLTPTKDGP DQESMPLPAD NGESPSKQQA PVNRDEMHYL DLLRHIIANG EQRMDRTEVG TLSVFGSQMR FDMRNSFPLL TTKRVFFRAV AEELLWFVAG KTDAKLLQAK NVHIWDGNSS REFLDKMGFT GRAVGDLGPV YGFQWRHFGA QYGTCDDDYS GKGIDQLRQV IDTIRNNPSD RRIIMSAWNP LDIPKMALPP CHCLAQFYVS EKRGELSCQL YQRSADMGLG VPFNIASYAL LTHMIAHVTG LKPGDFVHTM GDTHVYLNHV EPLKEQLERT PRPFPKLIIK RQVQDIEDFR FEDFQIVDYN PHPKIQMDMA V // ID U119_DROME STANDARD; PRT; 265 AA. AC Q9XYQ2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Unc-119 protein homolog (DmUNC-119). GN UNC-119 OR CG1659. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20316624; PubMed=10858820; RA Maduro M.F., Gordon M., Jacobs R., Pilgrim D.B.; RT "The UNC-119 family of neural proteins is functionally conserved RT between humans, Drosophila and C. elegans."; RL J. Neurogenet. 13:191-212(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- TISSUE SPECIFICITY: EXPRESSED IN NERVOUS SYSTEM. CC -!- SIMILARITY: BELONGS TO THE PDE6D / UNC119 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF119102; AAD30967.1; -. DR EMBL; AE003440; AAF46250.1; -. DR FlyBase; FBgn0025549; unc-119. DR InterPro; IPR008015; GMP_PDE_delta. DR InterPro; IPR007110; Ig-like. DR Pfam; PF05351; GMP_PDE_delta; 1. SQ SEQUENCE 265 AA; 28412 MW; 6C183CBCF5F2B95E CRC64; MSVVGKQLNP VQSSGAGAVT TSSSAAAGSS SSNSGVEANG GSGGSSGAAA AGAGASGDAK RPAESSSVTP DEVLHLTKIT DDYLCSANAN VFEIDFTRFK IRDLESGAVL FEIAKPPSEQ YPEGLSSDET MLAAAEKLSL DDTADPNAGR YVRYQFTPAF LNLKTVGATV EFTVGSQPLN NFRMIERHFF RDRLLKTFDF EFGFCFPFSK NTVEHIYEFP NLPPDLVAEM ISSPFETRSD SFYFVGNRLV MHNKADYAYD GGNIV // ID U2AF_DROME STANDARD; PRT; 416 AA. AC Q24562; Q9VXH2; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Splicing factor U2AF 50 kDa subunit (U2 auxiliary factor 50 kDa DE subunit) (U2 snRNP auxiliary factor large subunit). GN U2AF50 OR CG9998. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SB2040; TISSUE=Embryo; RX MEDLINE=94024011; PubMed=7692602; RA Kanaar R., Roche S.E., Beall E.L., Green M.R., Rio D.C.; RT "The conserved pre-mRNA splicing factor U2AF from Drosophila: RT requirement for viability."; RL Science 262:569-573(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: NECESSARY FOR THE SPLICING OF PRE-MRNA. BINDS TO THE CC POLYPYRIMIDINE TRACT OF INTRONS EARLY DURING SPLICEOSOME ASSEMBLY CC (BY SIMILARITY). CC -!- SUBUNIT: FORMS A HETERODIMER WITH THE U2AF SMALL SUBUNIT. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: PRESENT THROUGHOUT DEVELOPMENT. CC -!- SIMILARITY: CONTAINS 3 RNA RECOGNITION MOTIF (RRM) DOMAINS. CC -!- SIMILARITY: BELONGS TO THE SR FAMILY OF SPLICING FACTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L23404; AAA03548.1; -. DR EMBL; AE003502; AAF48596.1; -. DR EMBL; AY069320; AAL39465.1; -. DR PIR; A48249; A48249. DR HSSP; P26368; 2U2F. DR FlyBase; FBgn0005411; U2af50. DR GO; GO:0008248; F:pre-mRNA splicing factor activity; IMP. DR InterPro; IPR000504; RNA_rec_mot. DR InterPro; IPR006529; U2AF_lg. DR Pfam; PF00076; rrm; 3. DR SMART; SM00360; RRM; 2. DR TIGRFAMs; TIGR01642; U2AF_lg; 1. DR PROSITE; PS50102; RRM; 3. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Nuclear protein; RNA-binding; mRNA splicing; Repeat. FT DOMAIN 6 41 ARG/SER-RICH (RS DOMAIN). FT DOMAIN 93 175 RNA-BINDING (RRM) 1. FT DOMAIN 207 285 RNA-BINDING (RRM) 2. FT DOMAIN 318 408 RNA-BINDING (RRM) 3. SQ SEQUENCE 416 AA; 46655 MW; 541F1544E276DFFE CRC64; MGYDDRERDR ERRRHRSRSR DRHRERSRDR RHHRNSRRKP SLYWDVPPPG FEHITPMQYK AMQASGQIPA SVVPDTPQTA VPVVGSTITR QARRLYVGNI PFGVTEEEMM EFFNQQMHLV GLAQAAGSPV LACQINLDKN FAFLEFRSID ETTQAMAFDG INLKGQSLKI RRPHDYQPMP GITDTPAIKP AVVSSGVIST VVPDSPHKIF IGGLPNYLND DQVKELLLSF GKLRAFNLVK DAATGLSKGY AFCEYVDLSI TDQSIAGLNG MQLGDKKLIV QRASVGAKNA QNAANTTQSV MLQVPGLSNV VTSGPPTEVL CLLNMVTPDE LRDEEEYEDI LEDIKEECTK YGVVRSVEIP RPIEGVEVPG CGKVFVEFNS VLDCQKAQQA LTGRKFSDRV VVTSYFDPDK YHRREF // ID U2AG_DROME STANDARD; PRT; 264 AA. AC Q94535; Q9VPN4; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Splicing factor U2af 38 kDa subunit (U2 auxiliary factor 38 kDa DE subunit) (U2 snRNP auxiliary factor small subunit). GN U2AF38 OR CG3582. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Embryo; RX MEDLINE=96413646; PubMed=8816800; RA Rudner D.Z., Kanaar R., Breger K.S., Rio D.C.; RT "Mutations in the small subunit of the Drosophila U2AF splicing RT factor cause lethality and developmental defects."; RL Proc. Natl. Acad. Sci. U.S.A. 93:10333-10337(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: NECESSARY FOR THE SPLICING OF PRE-MRNA. BINDS TO THE CC POLYPYRIMIDINE TRACT OF INTRONS EARLY DURING SPLICEOSOME ASSEMBLY CC (BY SIMILARITY). CC -!- SUBUNIT: ASSOCIATES WITH A 65 KDA PROTEIN (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE SR FAMILY OF SPLICING FACTORS. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -!- SIMILARITY: CONTAINS 2 C3H1-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U67066; AAB17271.1; -. DR EMBL; AE003590; AAF51512.1; -. DR EMBL; AY058537; AAL13766.1; -. DR PIR; JC6125; JC6125. DR FlyBase; FBgn0017457; U2af38. DR GO; GO:0008248; F:pre-mRNA splicing factor activity; IMP. DR InterPro; IPR000504; RNA_rec_mot. DR InterPro; IPR000571; Znf_CCCH. DR Pfam; PF00076; rrm; 1. DR Pfam; PF00642; zf-CCCH; 2. DR SMART; SM00360; RRM; 1. DR SMART; SM00356; ZnF_C3H1; 2. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Nuclear protein; RNA-binding; mRNA splicing; Zinc-finger; Repeat. FT DOMAIN 44 149 RNA-BINDING (RRM). FT DOMAIN 180 213 ARG/SER-RICH (RS DOMAIN). FT DOMAIN 190 197 POLY-ARG. FT DOMAIN 252 262 POLY-GLY. FT CONFLICT 66 66 H -> D (IN REF. 1). SQ SEQUENCE 264 AA; 29877 MW; 577285FB66FDB2F5 CRC64; MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRIHNKP TFSQTVLLQN LYVNPQNSAK SADGSHLVAN VSDEEMQEHY DNFFEDVFVE CEDKYGEIEE MNVCDNLGDH LVGNVYIKFR NEADAEKAAN DLNNRWFGGR PVYSELSPVT DFREACCRQY EMGECTRSGF CNFMHLKPIS RELRRYLYSR RRRARSRSRS PGRRRGSRSR SRSPGRRGGG RGDGVGGGNY LNNERDNMRG NDRGNDRDRR KGGGGGGGGG GGRY // ID UBC1_DROME STANDARD; PRT; 147 AA. AC P25867; Q9VFG6; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin-conjugating enzyme E2-17 kDa (EC 6.3.2.19) DE (Ubiquitin-protein ligase) (Ubiquitin carrier protein) (Effete DE protein). GN EFF OR UBCD1 OR CG7425. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-P2; RX MEDLINE=92155178; PubMed=1310935; RA Treier M., Seufert W., Jentsch S.; RT "Drosophila UbcD1 encodes a highly conserved ubiquitin-conjugating RT enzyme involved in selective protein degradation."; RL EMBO J. 11:367-372(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 1-11 FROM N.A., AND FUNCTION. RX MEDLINE=97260538; PubMed=9106658; RA Cenci G., Rawson R.B., Belloni G., Castrillon D.H., Tudor M., RA Petrucci R., Goldberg M.L., Wasserman S.A., Gatti M.; RT "UbcD1, a Drosophila ubiquitin-conjugating enzyme required for proper RT telomere behavior."; RL Genes Dev. 11:863-875(1997). CC -!- FUNCTION: CATALYZES THE COVALENT ATTACHMENT OF UBIQUITIN TO OTHER CC PROTEINS. MEDIATES THE SELECTIVE DEGRADATION OF SHORT-LIVED AND CC ABNORMAL PROTEINS. REQUIRED FOR PROPER TELOMERE BEHAVIOR DURING CC CELL DIVISIONS AND POSSIBLY FOR UBIQUITINATION OF PROTEINS CC INVOLVED IN POSTMEIOTIC STAGES OF SPERMATOGENESIS. DELETION CC MUTATIONS ARE LETHAL IN HOMOZYGOTES. CC -!- CATALYTIC ACTIVITY: ATP + UBIQUITIN + PROTEIN LYSINE = AMP + CC DIPHOSPHATE + PROTEIN N-UBIQUITYLLYSINE. CC -!- PATHWAY: UBIQUITIN CONJUGATION; SECOND STEP. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN- CC THIOLESTER FORMATION. CC -!- SIMILARITY: BELONGS TO THE UBIQUITIN-CONJUGATING ENZYME FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62575; CAA44453.1; -. DR EMBL; AE003706; AAF55093.1; -. DR EMBL; AY060304; AAL25343.1; -. DR EMBL; U68298; AAB39622.1; -. DR PIR; S19157; S19157. DR HSSP; P15731; 1QCQ. DR FlyBase; FBgn0011217; eff. DR GO; GO:0004840; F:ubiquitin conjugating enzyme activity; IGI. DR GO; GO:0007001; P:chromosome organization and biogenesis (sen...; IMP. DR GO; GO:0007140; P:male meiosis; IMP. DR GO; GO:0007067; P:mitosis; IMP. DR GO; GO:0006512; P:ubiquitin cycle; IGI. DR InterPro; IPR000608; UBQ_conjugat. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. KW Ubl conjugation pathway; Ligase; Meiosis; Cell cycle; Cell division; KW Multigene family. FT BINDING 85 85 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 147 AA; 16678 MW; 82E0CE24F925E2EE CRC64; MALKRINKEL QDLGRDPPAQ CSAGPVGDDL FHWQATIMGP PDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNELARE WTRKYAM // ID UBC2_DROME STANDARD; PRT; 232 AA. AC P52485; Q9VKQ4; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin-conjugating enzyme E2-24 kDa (EC 6.3.2.19) DE (Ubiquitin-protein ligase) (Ubiquitin carrier protein). GN UBCD2 OR CG6720. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DP CN BW; RX MEDLINE=96162026; PubMed=8576256; RA Matuschewski K., Hauser H.P., Treier M., Jentsch S.; RT "Identification of a novel family of ubiquitin-conjugating enzymes RT with distinct amino-terminal extensions."; RL J. Biol. Chem. 271:2789-2794(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYZES THE COVALENT ATTACHMENT OF UBIQUITIN TO OTHER CC PROTEINS. CC -!- CATALYTIC ACTIVITY: ATP + UBIQUITIN + PROTEIN LYSINE = AMP + CC DIPHOSPHATE + PROTEIN N-UBIQUITYLLYSINE. CC -!- PATHWAY: UBIQUITIN CONJUGATION; SECOND STEP. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN- CC THIOLESTER FORMATION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE UBIQUITIN-CONJUGATING ENZYME FAMILY. CC STRONGEST, TO HUMAN UBCH6. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X92663; CAA63351.1; -. DR EMBL; AE003629; AAF53008.1; -. DR HSSP; P15731; 1QCQ. DR FlyBase; FBgn0015320; UbcD2. DR GO; GO:0004840; F:ubiquitin conjugating enzyme activity; IGI. DR InterPro; IPR000608; UBQ_conjugat. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. KW Ubl conjugation pathway; Ligase; Multigene family. FT BINDING 170 170 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 232 AA; 24435 MW; DE71AFD8EB618C86 CRC64; MSSTPAAGSA AEVATSSATS NAPSAPSTTA SNVSNTSQPT TAGTPQARGG RGSNANGGAS GSNAGGGDEP RKEAKTTPRI SRALGTSAKR IQKELAEITL DPPPNCSAGP KGDNLYEWVS TILGPPGSVY EGGVFFLDIH FSPEYPFKPP KVTFRTRIYH CNINSQGVIC LDILKDNWSP ALTISKVLLS ICSLLTDCNP ADPLVGSIAT QYLQNREEHD RIARLWTKRY AT // ID UBC3_DROME STANDARD; PRT; 151 AA. AC P35128; Q9VY67; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin-conjugating enzyme E2-17 kDa (EC 6.3.2.19) DE (Ubiquitin-protein ligase) (Ubiquitin carrier protein) (Bendless DE protein). GN BEN OR UBCD3 OR CG18319. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93357019; PubMed=8394720; RA Muralidhar M., Thomas J.B.; RT "The Drosophila bendless gene encodes a neural protein related to RT ubiquitin-conjugating enzymes."; RL Neuron 11:253-266(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94238376; PubMed=8182464; RA Oh C.E., McMahon R., Benzer S., Tanouye M.A.; RT "Bendless, a Drosophila gene affecting neuronal connectivity, encodes RT a ubiquitin-conjugating enzyme homolog."; RL J. Neurosci. 14:3166-3179(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYZES THE COVALENT ATTACHMENT OF UBIQUITIN TO OTHER CC PROTEINS. CC -!- CATALYTIC ACTIVITY: ATP + UBIQUITIN + PROTEIN LYSINE = AMP + CC DIPHOSPHATE + PROTEIN N-UBIQUITYLLYSINE. CC -!- PATHWAY: UBIQUITIN CONJUGATION; SECOND STEP. CC -!- MISCELLANEOUS: MUTANTS IN THIS GENE EXHIBIT SEVERAL, LARGELY CC NEURONAL DEFECTS INCLUDING LESIONS AFFECTING THE NEURONAL CC CONNECTIVITY OF THE GIANT FIBER WITH THE "JUMPING MUSCLE", AND THE CC AXONS OF PHOTORECEPTOR CELLS R7 AND R8 FAIL TO MAKE THE PROPER CC RIGHT-ANGLE TURN INTO THE MEDULLA (HENCE THE TERM "BENDLESS"). CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN- CC THIOLESTER FORMATION. CC -!- SIMILARITY: BELONGS TO THE UBIQUITIN-CONJUGATING ENZYME FAMILY. CC STRONGEST, TO YEAST UBC13 AND TO UBC5. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L20126; AAA28392.1; -. DR EMBL; S70118; AAB30753.1; -. DR EMBL; AE003494; AAF48338.1; -. DR PIR; S35793; S35793. DR HSSP; P15731; 1QCQ. DR FlyBase; FBgn0000173; ben. DR GO; GO:0007412; P:axon target recognition; IMP. DR GO; GO:0007629; P:flight behavior; IMP. DR GO; GO:0007630; P:jump response; IMP. DR GO; GO:0008594; P:photoreceptor cell morphogenesis (sensu Dro...; IMP. DR InterPro; IPR000608; UBQ_conjugat. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. KW Ubl conjugation pathway; Ligase; Multigene family. FT BINDING 87 87 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 151 AA; 17236 MW; 1D096E72A7AEA420 CRC64; MSSLPRRIIK ETQRLMQEPV PGINAIPDEN NARYFHVIVT GPNDSPFEGG VFKLELFLPE DYPMSAPKVR FITKIYHPNI DRLGRICLDV LKDKWSPALQ IRTILLSIQA LLSAPNPDDP LANDVAELWK VNEAEAIRNA REWTQKYAVE D // ID UBC4_DROME STANDARD; PRT; 199 AA. AC P52486; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin-conjugating enzyme E2-22 kDa (EC 6.3.2.19) DE (Ubiquitin-protein ligase) (Ubiquitin carrier protein). GN UBCD4. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Kirby R.J.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CATALYZES THE COVALENT ATTACHMENT OF UBIQUITIN TO OTHER CC PROTEINS. CC -!- CATALYTIC ACTIVITY: ATP + UBIQUITIN + PROTEIN LYSINE = AMP + CC DIPHOSPHATE + PROTEIN N-UBIQUITYLLYSINE. CC -!- PATHWAY: UBIQUITIN CONJUGATION; SECOND STEP. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN- CC THIOLESTER FORMATION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE UBIQUITIN-CONJUGATING ENZYME FAMILY. CC STRONGEST, TO YEAST UBC1. CC -!- SIMILARITY: CONTAINS 1 UBA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X92838; CAA63424.1; -. DR HSSP; P15731; 1QCQ. DR FlyBase; FBgn0015321; UbcD4. DR InterPro; IPR000449; UBA_domain. DR InterPro; IPR000608; UBQ_conjugat. DR Pfam; PF00627; UBA; 1. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00165; UBA; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS50030; UBA; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. KW Ubl conjugation pathway; Ligase; Multigene family. FT DOMAIN 161 199 UBA. FT BINDING 92 92 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 199 AA; 22391 MW; 720CA9595FC0C08F CRC64; MANMAVSRIK REFKEVMRSE EIVQCSIKIE LVNGQLTELR GEIAGPPDTP YEGGKFVLEI KVPETYPFNP PKARFITRIW HPNISSVTGA ICLDILKDNW AAAMTLRTVL LSLQALLAAA EPDDPQDAVV AYQFKDKYDL FLLTAKHWTN AYAGGPHTFP DCDSKIQRLR DMGIDEHEAR AVLSKENWNL EKATEGLFS // ID UBC6_DROME STANDARD; PRT; 151 AA. AC P25153; Q9VN70; DT 01-MAY-1992 (Rel. 22, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin-conjugating enzyme E2-17 kDa (EC 6.3.2.19) DE (Ubiquitin-protein ligase) (Ubiquitin carrier protein). GN UBCD6 OR DHR6 OR CG2013. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91219466; PubMed=1902572; RA Koken M.H.M., Reynolds P., Bootsma D., Hoeijmakers J.H.J., Prakash S., RA Prakash L.; RT "Dhr6, a Drosophila homolog of the yeast DNA-repair gene RAD6."; RL Proc. Natl. Acad. Sci. U.S.A. 88:3832-3836(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYZES THE COVALENT ATTACHMENT OF UBIQUITIN TO OTHER CC PROTEINS. REQUIRED FOR POSTREPLICATION REPAIR OF UV-DAMAGED DNA. CC -!- CATALYTIC ACTIVITY: ATP + UBIQUITIN + PROTEIN LYSINE = AMP + CC DIPHOSPHATE + PROTEIN N-UBIQUITYLLYSINE. CC -!- PATHWAY: UBIQUITIN CONJUGATION; SECOND STEP. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN- CC THIOLESTER FORMATION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE UBIQUITIN-CONJUGATING ENZYME FAMILY. CC STRONGEST, TO YEAST RAD6. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63792; AAA28308.1; -. DR EMBL; M64435; AAA28309.1; -. DR EMBL; M63791; AAA28309.1; JOINED. DR EMBL; AE003604; AAF52079.1; -. DR PIR; A39392; A39392. DR HSSP; P25865; 2AAK. DR FlyBase; FBgn0004436; UbcD6. DR GO; GO:0006281; P:DNA repair; IGI. DR InterPro; IPR000608; UBQ_conjugat. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. KW Ubl conjugation pathway; Ligase; DNA repair; Nuclear protein; KW Multigene family. FT BINDING 88 88 UBIQUITIN (BY SIMILARITY). FT CONFLICT 99 99 T -> R (IN REF. 1). SQ SEQUENCE 151 AA; 17152 MW; CC4B35992E4A9220 CRC64; MSTPARRRLM RDFKRLQEDP PTGVSGAPTD NNIMIWNAVI FGPHDTPFED GTFKLTIEFT EEYPNKPPTV RFVSKVFHPN VYADGGICLD ILQNRWSPTY DVSAILTSIQ SLLSDPNPNS PANSTAAQLY KENRREYEKR VKACVEQSFI D // ID UBC7_DROME STANDARD; PRT; 153 AA. AC P52487; Q9VIB4; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin-conjugating enzyme E2-18 kDa (EC 6.3.2.19) DE (Ubiquitin-protein ligase) (Ubiquitin carrier protein). GN UBC84D OR CG12799. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96359183; PubMed=8703090; RA Robin C., Russell R.J., Medveczky K.M., Oakeshott J.G.; RT "Duplication and divergence of the genes of the alpha-esterase RT cluster of Drosophila melanogaster."; RL J. Mol. Evol. 43:241-252(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYZES THE COVALENT ATTACHMENT OF UBIQUITIN TO OTHER CC PROTEINS (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + UBIQUITIN + PROTEIN LYSINE = AMP + CC DIPHOSPHATE + PROTEIN N-UBIQUITYLLYSINE. CC -!- PATHWAY: UBIQUITIN CONJUGATION; SECOND STEP. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN- CC THIOLESTER FORMATION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE UBIQUITIN-CONJUGATING ENZYME FAMILY. CC STRONGEST, TO HUMAN UBC7. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U51051; AAB01150.1; -. DR EMBL; AE003671; AAF54011.1; -. DR HSSP; P15731; 1QCQ. DR FlyBase; FBgn0017456; Ubc84D. DR InterPro; IPR000608; UBQ_conjugat. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. KW Ubl conjugation pathway; Ligase. FT BINDING 86 86 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 153 AA; 17746 MW; 14464662FA7D2EA9 CRC64; MAATRRLTRE LSDLVEAKMS TLRNIESSDE SLLMWTGLLV PEKAPYNKGA FRIEINFPPQ YPFMPPKILF KTKIYHPNVD EKGEVCLPII STDNWKPTTR TEQVLQALVA IVHNPEPEHP LRSDLAEEFV REHKKFMKTA EEFTKKNAEK RPE // ID UBIQ_DROME STANDARD; PRT; 76 AA. AC Q9VZL4; Q9VKW6; Q9VQX7; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin. GN (RPL40 OR CG2960) AND (RPS27A OR UBI-F80 OR UBI-F OR CG5271) AND GN (UBI-P63E OR UBI-M OR CG11624). OS Drosophila melanogaster (Fruit fly), OS Ceratitis capitata (Mediterranean fruit fly), OS Spodoptera frugiperda (Fall armyworm), and OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7213, 7108, 7130; RN [1] RP SEQUENCE FROM N.A. (UBI-P63E). RC SPECIES=D.melanogaster; RA Arribas C., Sampedro J., Izquierdo M.; RT "The ubiquitin genes in D. melanogaster: transcription and RT polymorphism."; RL Biochim. Biophys. Acta 868:119-127(1986). RN [2] RP SEQUENCE FROM N.A. (RPS27A AND UBI-P63E). RC SPECIES=D.melanogaster; RX MEDLINE=89096844; PubMed=2463465; RA Lee H., Simon J.A., Lis J.T.; RT "Structure and expression of ubiquitin genes of Drosophila RT melanogaster."; RL Mol. Cell. Biol. 8:4727-4735(1988). RN [3] RP SEQUENCE FROM N.A. (RPL40). RC SPECIES=D.melanogaster; STRAIN=Canton-S; TISSUE=Larva; RX MEDLINE=90326530; PubMed=2165256; RA Cabrera y Poch H.L., Arribas C., Izquierdo M.; RT "Sequence of a Drosophila cDNA encoding a ubiquitin gene fusion to a RT 52-aa ribosomal protein tail."; RL Nucleic Acids Res. 18:3994-3994(1990). RN [4] RP SEQUENCE FROM N.A. (RPL40). RC SPECIES=D.melanogaster; STRAIN=Canton-S; RX MEDLINE=92392292; PubMed=1381584; RA Cabrera H.L., Barrio R., Arribas C.; RT "Structure and expression of the Drosophila ubiquitin-52-amino-acid RT fusion-protein gene."; RL Biochem. J. 286:281-288(1992). RN [5] RP SEQUENCE FROM N.A. (RPS27A). RC SPECIES=D.melanogaster; STRAIN=Canton-S; RX MEDLINE=94347108; PubMed=8068011; RA Barrio R., del Arco A., Cabrera H., Arribas C.; RT "Structure and expression of the Drosophila ubiquitin-80-amino-acid RT fusion-protein gene."; RL Biochem. J. 302:237-244(1994). RN [6] RP SEQUENCE FROM N.A. (RPL40; RPS27A AND UBI-P63E). RC SPECIES=D.melanogaster; STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [7] RP SEQUENCE OF 1-74. RC SPECIES=C.capitata; RX MEDLINE=82265683; PubMed=6286647; RA Gavilanes J.G., Gonzalez de Buitrago G., Perez-Castells R., RA Rodriguez R.; RT "Isolation, characterization, and amino acid sequence of a ubiquitin- RT like protein from insect eggs."; RL J. Biol. Chem. 257:10267-10270(1982). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=S.frugiperda; RX MEDLINE=90115886; PubMed=2153300; RA Guarino L.A.; RT "Identification of a viral gene encoding a ubiquitin-like protein."; RL Proc. Natl. Acad. Sci. U.S.A. 87:409-413(1990). RN [9] RP SEQUENCE FROM N.A. RC SPECIES=M.sexta; RX MEDLINE=91000673; PubMed=2169771; RA Schwartz L.M., Myer A., Kosz L., Engelstein M., Maier C.; RT "Activation of polyubiquitin gene expression during developmentally RT programmed cell death."; RL Neuron 5:411-419(1990). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=M.sexta; TISSUE=Pupae; RX MEDLINE=91045065; PubMed=1700368; RA Bishoff S.T., Schwartz L.M.; RT "Characterization of a ubiquitin-fusion gene from the tobacco RT hawkmoth, Manduca sexta."; RL Nucleic Acids Res. 18:6039-6043(1990). CC -!- FUNCTION: INVOLVED IN THE ATP-DEPENDENT SELECTIVE DEGRADATION OF CC CELLULAR PROTEINS, THE MAINTENANCE OF CHROMATIN STRUCTURE, THE CC REGULATION OF GENE EXPRESSION, THE STRESS RESPONSE, AND RIBOSOME CC BIOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. CC -!- MISCELLANEOUS: UBIQUITIN IS SYNTHESIZED AS A POLYUBIQUITIN CC PRECURSOR WITH EXACT HEAD TO TAIL REPEATS, THE NUMBER OF REPEATS CC DIFFERS BETWEEN SPECIES (UP TO 12 IN XENOPUS). IN SOME SPECIES CC THERE IS A FINAL AMINO-ACID AFTER THE LAST REPEAT. SOME UBIQUITIN CC GENES CONTAIN A SINGLE COPY OF UBIQUITIN FUSED TO A RIBOSOMAL CC PROTEIN (EITHER L40 OR S27A). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33013; AAA28999.1; -. DR EMBL; M33015; AAA29001.1; -. DR EMBL; M33122; AAA29007.1; -. DR EMBL; M22428; AAA28997.1; ALT_TERM. DR EMBL; M22536; AAA28998.1; ALT_TERM. DR EMBL; X53059; CAA37227.1; ALT_TERM. DR EMBL; X59943; CAA42568.1; ALT_TERM. DR EMBL; X69119; CAA48871.1; -. DR EMBL; AE003479; AAG22241.2; ALT_TERM. DR EMBL; AE003577; AAF51034.1; ALT_TERM. DR EMBL; AE003628; AAF52941.1; ALT_TERM. DR EMBL; M30306; AAA29989.1; ALT_SEQ. DR EMBL; X53524; CAA37599.1; ALT_TERM. DR PIR; A26087; A26087. DR PIR; B34813; UQUYSF. DR PIR; JH0302; JH0302. DR PIR; S13136; UQWO7A. DR FlyBase; FBgn0003941; RpL40. DR FlyBase; FBgn0003942; RpS27A. DR FlyBase; FBgn0003943; Ubi-p63E. DR GO; GO:0005842; C:cytosolic large ribosomal subunit (sensu Eu...; IDA. DR GO; GO:0009408; P:response to heat; IEP. DR InterPro; IPR000626; Ubiquitin. DR Pfam; PF00240; ubiquitin; 1. DR PRINTS; PR00348; UBIQUITIN. DR SMART; SM00213; UBQ; 1. DR PROSITE; PS00299; UBIQUITIN_1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. KW Nuclear protein; Polyprotein. FT SITE 48 48 NECESSARY FOR BRANCHED-CHAIN FT MULTIUBIQUITIN ADDUCTS. FT BINDING 54 54 ACTIVATING ENZYME. FT SITE 68 68 ESSENTIAL FOR FUNCTION. FT BINDING 72 72 ACTIVATING ENZYME. FT BINDING 76 76 ACCEPTOR PROTEINS. SQ SEQUENCE 76 AA; 8565 MW; C42A35397FFD9B52 CRC64; MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG // ID UBL_DROME STANDARD; PRT; 227 AA. AC P35122; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Ubiquitin DE thiolesterase). GN UCH. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=93246063; PubMed=7683284; RA Zhang N., Wilkinson K., Bownes M.; RT "Cloning and analysis of expression of a ubiquitin carboxyl terminal RT hydrolase expressed during oogenesis in Drosophila melanogaster."; RL Dev. Biol. 157:214-223(1993). CC -!- FUNCTION: UBIQUITIN-PROTEIN HYDROLASE IS INVOLVED BOTH IN THE CC PROCESSING OF UBIQUITIN PRECURSORS AND OF UBIQUINATED PROTEINS. CC THIS ENZYME IS A THIOL PROTEASE THAT RECOGNIZE AND HYDROLYZE CC A PEPTIDE BOND AT THE C-TERMINAL GLYCINE OF UBIQUITIN. CC -!- CATALYTIC ACTIVITY: UBIQUITIN C-TERMINAL THIOLESTER + H(2)O = CC UBIQUITIN + A THIOL. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING OOGENESIS. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C12. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69678; CAA49358.1; -. DR EMBL; X69679; CAA49359.1; -. DR PIR; S33956; S33956. DR HSSP; P15374; 1UCH. DR MEROPS; C12.UPW; -. DR FlyBase; FBgn0010288; Uch. DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IDA. DR GO; GO:0016579; P:protein deubiquitination; IDA. DR InterPro; IPR001578; Peptidase_C12. DR Pfam; PF01088; Peptidase_C12; 1. DR PRINTS; PR00707; UBCTHYDRLASE. DR ProDom; PD350662; UCH_1; 1. DR PROSITE; PS00140; UCH_1; 1. KW Ubl conjugation pathway; Hydrolase; Thiol protease. FT ACT_SITE 93 93 BY SIMILARITY. FT ACT_SITE 164 164 BY SIMILARITY. FT ACT_SITE 179 179 BY SIMILARITY. FT DOMAIN 38 55 UBIQUITIN BINDING 1 (POTENTIAL). FT DOMAIN 173 181 UBIQUITIN BINDING 2 (POTENTIAL). SQ SEQUENCE 227 AA; 25894 MW; 55AED76F8BCC6DC4 CRC64; MLTWTPLESN PEVLTKYIHK LAVSPAWSVT DVIGLEDDTL EWIPRPVKAF ILLFPCSETY EKHRTEEHDR IKEVEEQHPE DLFYMRQFTH NACGTVALIH SVANNKEVDI DRGVLKDFLE KTASLSPEER GRALEKDEKF TADHEALAQE GQTNAANHEK VIHHFIALVN KEGTLYELDG RKSFPIKHGP TSEETFVKDA AKVCKEFMAR DPNEVRFTVL ALTAAQQ // ID UBPE_DROME STANDARD; PRT; 898 AA. AC Q24574; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Ubiquitin carboxyl-terminal hydrolase 64E (EC 3.1.2.15) (Ubiquitin DE thiolesterase 64E) (Ubiquitin-specific processing protease 64E) DE (Deubiquitinating enzyme 64E). GN UBP64E OR D-UBP-64E. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96413323; PubMed=8816485; RA Henchoz S., de Rubertis F., Pauli D., Spierer P.; RT "The dose of a putative ubiquitin-specific protease affects position- RT effect variegation in Drosophila melanogaster."; RL Mol. Cell. Biol. 16:5717-5725(1996). CC -!- FUNCTION: HAS AN EFFECT ON POSITION-EFFECT VARIEGATION. CC -!- CATALYTIC ACTIVITY: UBIQUITIN C-TERMINAL THIOLESTER + H(2)O = CC UBIQUITIN + A THIOL. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C19. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99211; CAA67601.1; -. DR MEROPS; C19.UPW; -. DR FlyBase; FBgn0016756; Ubp64E. DR InterPro; IPR001394; Peptidase_C19. DR Pfam; PF00443; UCH; 1. DR PROSITE; PS00972; UCH_2_1; 1. DR PROSITE; PS00973; UCH_2_2; 1. DR PROSITE; PS50235; UCH_2_3; 1. KW Ubl conjugation pathway; Hydrolase; Thiol protease; Nuclear protein. FT ACT_SITE 64 64 BY SIMILARITY. FT ACT_SITE 371 371 BY SIMILARITY. FT ACT_SITE 379 379 BY SIMILARITY. FT DOMAIN 633 638 POLY-SER. SQ SEQUENCE 898 AA; 101492 MW; 11070D8E144B0878 CRC64; MVRTRLCQTS IVASMEAMSC EHGRESTQRV RTSCPRPPQK LRQRQGRRAW SRGYVGLVNQ AMTCYLNSLL QALFMTPEFR NALYRWEFDN DNEAKKSYQL QKLFLNLQTS PKAAVETTDL TRSFGWDSTE AWQQHDIQEL CRVMFDALEH KFKNTKQANL ISNLYEGKMN AYVKCLGCNT EKNDCEDTFL DIPLPVRPFG SSSAYGSIEE ALRAFVQPET LDGNNQYLCE KCKKKCDAHK GLHFKSFPYI LTLHLKRFDF DYQTMHRIKL NDRVTFPQTL NLNTFINRSG NSGEQNSQLN GTVDDCSTAD SGSAMEDDNL SSGVVTTASS SQHENDLNDE DEGIDMSSST SKSAKQGSGP YLYELFAIMI HSGSASGGHY YAYIKDFDNN EWFCFNDQNV TSITQEDIQR SFGGPNGSYY SSAYTSSTNA YMLMYRQVDA KRNELVAKVR DFPEHIKTLL PKLHSEEETR VSRLGRHITV TDLALPDLYK PRVYFYNPSL KKMKITRVYV SQSFNINLVL MSAYEMLNVE QFAPLSRCRL VAYNSSMDTI IQSLESCTDP ALTELRAANY SLDFLLEYRA EDQEFEVYRE RHYLVCVKVD LSTMAMDGPL VTQQGERKPH VLRAIALRCT LASSSSYSHG ARHGAKAFVS YDPHPTRRPC NISRTWPTPQ FKSITYFYLN VPNTDAATLE MLGVPTVESV ECASGGDVVD AAMMNGVAPG HMSSSNDYDW RRYKRDLVEP MSQPSPSHGH ESNSEDSSLS DGDRTLVETD NMAHRGGGDS QVSSTSHSPQ LSSPEDEAAS HDAMMRVHAY CNGNGSYAAA DVVDPLLLPT STNHFFYRHK GRVRGCGWHR FQSGHQSDEE AQLRTRTRAY KLLVGTHMRM GAFKKHHRAA DPSARRPL // ID UCRX_DROME STANDARD; PRT; 55 AA. AC Q9XY35; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquinol-cytochrome C reductase complex 6.3 kDa protein (EC 1.10.2.2) DE (Complex III subunit X) (Oxen protein). GN OX OR QCR10 OR QCR9 OR CG8764. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Benevolenskaya E.V., Frolov M.V., Birchler J.A.; RT "The oxen gene is a modifier of gene expression in Drosophila."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THIS IS A COMPONENT OF THE UBIQUINOL-CYTOCHROME C CC REDUCTASE COMPLEX (COMPLEX III OR CYTOCHROME B-C1 COMPLEX), WHICH CC IS PART OF THE MITOCHONDRIAL RESPIRATORY CHAIN. THIS SUBUNIT CC INTERACTS WITH CYTOCHROME C1 (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: QH(2) + 2 FERRICYTOCHROME C = Q + 2 CC FERROCYTOCHROME C. CC -!- SUBUNIT: BC1 COMPLEX CONTAINS 11 SUBUNITS; 3 RESPIRATORY SUBUNITS CC (CYTOCHROME B, CYTOCHROME C1, RIESKE PROTEIN), 2 CORE PROTEINS AND CC 6 LOW-MOLECULAR WEIGHT PROTEINS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL INNER MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE UQCRX/QCR9 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF017783; AAD28637.1; -. DR EMBL; AE003821; AAF58459.1; -. DR FlyBase; FBgn0011227; ox. DR InterPro; IPR008027; UCR_UQCRX_QCR9. DR Pfam; PF05365; UCR_UQCRX_QCR9; 1. KW Mitochondrion; Inner membrane; Electron transport; Respiratory chain; KW Oxidoreductase. SQ SEQUENCE 55 AA; 6294 MW; A4A172E460818247 CRC64; MKVIYNTLFK RTSTYAVAII ASAFFFERAL DVTSVAIFEG INKGKLWKDI KGKYE // ID UFD1_DROME STANDARD; PRT; 316 AA. AC Q9VTF9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin fusion degradation protein 1 homolog (UB fusion protein 1). GN UFD1-LIKE OR UFD1L OR CG6233. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RX MEDLINE=21328890; PubMed=11435701; RA Ratti A., Amati F., Bozzali M., Conti E., Sangiuolo F., Berloco M., RA Palumbo G., Botta A., Pizzutti A., Novelli G., Dallapiccola B.; RT "Cloning and molecular characterization of three ubiquitin fusion RT degradation 1 (Ufd1) ortholog genes from Xenopus laevis, Gallus gallus RT and Drosophila melanogaster."; RL Cytogenet. Cell Genet. 92:279-282(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: FUNCTIONS AT A POST-UBIQUITATION STEP IN THE UBIQUITIN CC FUSION DEGRADATION (UFD) PATHWAY (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM EARLY EMBRYOS THROUGH TO CC ADULTHOOD. CC -!- SIMILARITY: BELONGS TO THE UFD1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF228282; AAK00730.1; -. DR EMBL; AF228283; AAK00731.1; -. DR EMBL; AE003546; AAF50090.1; -. DR EMBL; AY060735; AAL28283.1; -. DR FlyBase; FBgn0036136; Ufd1-like. DR InterPro; IPR009010; Asp_decarb_fold. DR InterPro; IPR004854; UFD1. DR Pfam; PF03152; UFD1; 1. KW Ubl conjugation pathway. SQ SEQUENCE 316 AA; 34791 MW; B7C1EA88CCA5CDA3 CRC64; MFHFSGFNMM FPEGRNFHAN YKCFSVSMLP GNERTDVEKG GKIIMPPSAL DTLTRLNVEY PMLFKLTNVK KSRSSHAGVL EFVADEGKCY LPHWMMENLL LGEGDILNIE SVSLPVATFS KFQPHSTDFL DITNPKAVLE NALRNFACLT RGDVIAIKYN KKVYELCVLE TKPGNAVSII ECDMNVEFEA PVGYKDHSET QASGSGQQGA AGTVGGEIAG ATNAILEEVV ETFKGSGVRL DGKKKKESQL ETPVVKKVLA RGVPDYDFQF GLIRFDRNIR PISDRSQEDD AVAGNADASD AESFHGTGFS MKKTRK // ID UGDH_DROME STANDARD; PRT; 476 AA. AC O02373; O02647; Q9VRZ9; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE UDP-glucose 6-dehydrogenase (EC 1.1.1.22) (UDP-Glc dehydrogenase) DE (UDP-GlcDH) (UDPGDH) (Sugarless protein). GN SGL OR KIWI OR SKA OR CG10072. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97359976; PubMed=9217004; RA Binari R.C., Staveley B.E., Johnson W.A., Godavarti R., RA Sasisekharan R., Manoukian A.S.; RT "Genetic evidence that heparin-like glycosaminoglycans are involved in RT wingless signaling."; RL Development 124:2623-2632(1997). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=98000096; PubMed=9342049; RA Haecker U., Lin X., Perrimon N.; RT "The Drosophila sugarless gene modulates Wingless signaling and RT encodes an enzyme involved in polysaccharide biosynthesis."; RL Development 124:3565-3573(1997). RN [3] RP SEQUENCE FROM N.A. RA Haerry T., Heslip T., Marsh J.L., O'Connor M.B.; RT "Defects in glucuronate biosynthesis disrupt Wingless signaling in RT Drosophila."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Benevolenskaya E.V., Frolov M.V., Birchler J.A.; RT "Mutation in the Drosophila gene encoding UDP-glucose dehydrogenase RT affects expression of unlinked genes."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: UDP-GLUCOSE + 2 NAD(+) + H(2)O = UDP- CC GLUCURONATE + 2 NADH. CC -!- PATHWAY: BIOSYNTHESIS OF GLYCOSAMINOGLYCANS; HYALURONAN, CC CHONDROITIN SULFATE, AND HEPARAN SULFATE. CC -!- SIMILARITY: BELONGS TO THE UDP-GLUCOSE/GDP-MANNOSE DEHYDROGENASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF007870; AAB63208.1; -. DR EMBL; AF000570; AAB58714.1; -. DR EMBL; AF009013; AAB63462.1; -. DR EMBL; AF001310; AAC97125.1; -. DR EMBL; AF001312; AAC97126.1; -. DR EMBL; AF001311; AAC97126.1; JOINED. DR EMBL; AE003560; AAF50631.1; -. DR EMBL; AY052137; AAK93561.1; -. DR FlyBase; FBgn0010851; sgl. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR001732; UDPG_MGDP_dh. DR Pfam; PF00984; UDPG_MGDP_dh; 1. DR Pfam; PF03720; UDPG_MGDP_dh_C; 1. DR Pfam; PF03721; UDPG_MGDP_dh_N; 1. KW Oxidoreductase; NAD. FT NP_BIND 2 19 NAD (POTENTIAL). FT ACT_SITE 272 272 BY SIMILARITY. FT CONFLICT 59 59 K -> R (IN REF. 3). SQ SEQUENCE 476 AA; 52874 MW; 1450B9A0C802BBE7 CRC64; MKVCCIGAGY VGGPTCAVMA LKCPDIVITL VDKSSERIAQ WNSDKLPIYE PGLDEVVKKC RNVNLFFSTD IETAIKEADL IFISVNTPTK TCGNGKGRAA DLKYVESAAR MIAEIAQSNK IVVEKSTVPV RAAESIMHIL RANQKPGIHY DILSNPEFLA EGTAINDLLN ADRVLIGGEE TPEGHQAVEK LSWIYEHWIP KQNILTTNTW SSELSKLAAN AFLAQRISSI NSLSAVCEAT GADVSEVARA VGLDSRIGSK FLQASVGFGG SCFQKDILNL IYICENLNLP EVAAYWQQVI DMNEYQKRRF SQKIIESLFN TVSDKRIAIL GFAFKKNTGD TRETAAITVC QTLLEEGAAL DIYDPKVEPE QIIDDLTHPS VTESPEKVKK AVQIHSDPYS AVRATHALVI CTEWDEFVDL DFKRIYQSMM KPAYIFDGRK ILDHERLQQI GFHVQTIGKK YQRTGLLRSW GIVPQL // ID UGGG_DROME STANDARD; PRT; 1548 AA. AC Q09332; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE UDP-glucose:glycoprotein glucosyltransferase precursor (EC 2.4.1.-) DE (UDP--Glc:glycoprotein glucosyltransferase) (dUGT). GN UGT OR UGGG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 23-37. RC TISSUE=Embryo; RX MEDLINE=95246722; PubMed=7729408; RA Parker C.G., Fessler L.I., Nelson R.E., Fessler J.H.; RT "Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence RT and characterization of an enzyme that distinguishes between RT denatured and native proteins."; RL EMBO J. 14:1294-1303(1995). CC -!- FUNCTION: SELECTIVELY REGLUCOSYLATES UNFOLDED GLYCOPROTEINS, THUS CC PROVIDING QUALITY CONTROL FOR PROTEIN TRANSPORT OUT OF THE ER. CC UNFOLDED, DENATURED GLYCOPROTEINS ARE SUBSTANTIALLY BETTER CC SUBSTRATES FOR GLUCOSYLATION BY THIS ENZYME THAN ARE THE CC CORRESPONDING NATIVE PROTEINS. THIS PROTEIN AND TRANSIENT CC GLUCOSYLATION MAY BE INVOLVED IN MONITORING AND/OR ASSISTING THE CC FOLDING AND ASSEMBLY OF NEWLY MADE GLYCOPROTEINS, IN ORDER TO CC IDENTIFY GLYCOPROTEINS THAT NEED ASSISTANCE IN FOLDING FROM CC CHAPERONES. CC -!- COFACTOR: REQUIRES CALCIUM AND MANGANESE IONS FOR ACTIVITY. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN. CC -!- DEVELOPMENTAL STAGE: IS PRESENT AT LOW BUT DETECTABLE LEVELS IN CC THE EARLIEST EMBRYOS, INCREASING AT 6-8 HRS WITH A MAXIMUM AT 10- CC 12 HRS. LEVELS DECREASE THEREAFTER AND ARE NOT DETECTED IN 18-20 CC HRS EMBRYOS AND FIRST INSTAR LARVAE BUT IS DETECTED AGAIN AT CC SECOND INSTAR TO PUPATION. CC -!- SIMILARITY: BELONGS TO THE GLYCOSYLTRANSFERASE FAMILY 8. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U20554; AAA85850.1; -. DR PIR; S54723; S54723. DR FlyBase; FBgn0014075; Ugt. DR GO; GO:0005635; C:nuclear membrane; IDA. DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA. DR InterPro; IPR002495; Glyco_trans_8. DR Pfam; PF01501; Glyco_transf_8; 1. KW Signal; Transferase; Glycosyltransferase; Endoplasmic reticulum; KW Glycoprotein. FT SIGNAL 1 22 FT CHAIN 23 1548 UDP-GLUCOSE:GLYCOPROTEIN FT GLUCOSYLTRANSFERASE. FT CARBOHYD 181 181 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 266 266 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 864 864 N-LINKED (GLCNAC...) (POTENTIAL). FT SITE 1545 1548 PREVENT SECRETION FROM ER (POTENTIAL). SQ SEQUENCE 1548 AA; 174465 MW; 95D6849961622DB6 CRC64; MLRAVALCVS VVLIALYTPT SGESSQSYPI TTLINAKWTQ TPLYLEIAEY LADEQAGLFW DYVSGVTKLD TVLNEYDTES QQYNAALELV KSHVSSPQLP LLRLVVSMHS LTPRIQTHFQ LAEELRSSGS CQSFTFAQVG SELACSFNEL QKKLEVPLAK DSLDAPVVTY SFDHIFPGSE NNTRTVVLYG DLGSSQFRTY HKLLEKEANA GRIRYILRHQ LAKKDKRPVR LSGYGVELHL KSTEYKSQDD APKPEAGSTS DEDLANESDV QGFDFKVLKQ KHPTLKRALD QLRQRLLQGN DEIAQLKAWE FQDLGLQAAA AIAEIQGDET LQILQYTAHN FPMLARTLLA HKVTDGLRAE VKHNTEAFGR SLNVAPPDGA LFINGLFFDA DTMDLYSLIE TLRSEMRVLE SLHSNNVRGS LASSLLALDL TASSKKEFAI DIRDTAVQWV NDIENDVQYR RWPSSVMDLL RPTFPGMLRN IRKNVFNLVL VVDALQPTAR SVIKLSESFV IHQAPIRLGL VFDARDANED NLADYVAITC AYNYVSQKKD ARAALSFLTD IYAAVGETKV VTKKDIVKQL TKEFTSLSFA KAEEFLEEDS TYDYGRELAA EFIQRLGFGD KEQPQALLNG VPMPSNVVTA DSDFEEAIFT EIMTHTSNLQ KAVYKGELTD NDVAIDYLMN QPHVMPRLNQ RILSQEDVKY LDINGVAYKN LGNVGVLNRL SNRDMTATLM DNLKYFGGKK STELIGRTSL QFLTIWVFAD LETDQGRDLL THALDYVQSG ESVRVAFIPN TESSSASSRR NLNRLVWAAM QSLPPTQATE QVLKWLKKPK EKIEIPTQLE DILGSTELHL KMLRVYSQRV LGLNKSQRLV IGNGRLYGPL SSDESFDSAD FALLARFSSL QYSDKVRQVL KESAQDVNEE FNSDTLLKLY ASLLPRQTKT RFKLPTDLKT DHSVVKLPPK QEKLPHFDVA AVLDPASRAA QKLTPILILL RQVLNCQLNL YLIPVPQHSD MPVKNFYRYV VEPEVQFEAN GGRSDGPLAK FSGLPANPLL TQQLQVPENW LVEAVRAVYD LDNIKLTDIG GPVHSEFDLE YLLLEGHCFD AASGAPPRGL QLVLGTQSQP TLVDTIVMAN LGYFQLKANP GAWSLRLREG KSADIYAISH IEGTNTHHSA GSSEVQVLIT SLRSHVVKLR VSKKPGMQQA ELLSDDNEQA AQSGMWNSIA SSFGGGSANQ AASDEDTETI NIFSVASGHL YERLLRIMMV SLLKHTKSPV KFWFLKNYLS PQFTDFLPHM ASEYNFQYEL VQYKWPRWLH QQTEKQRTIW GYKILFLDVL FPLNVRKIIF VDADAIVRTD IKELYDMDLG GAPYAYTPFC DSRKEMEGFR FWKQGYWRSH LMGRRYHISA LYVVDLKRFR KIAAGDRLRG QYQALSQDPN SLSNLDQDLP NNMIHQVAIK SLPDDWLWCQ TWCSDSNFKT AKVIDLCNNP QTKEAKLTAA QRIVPEWKDY DAELKTLMSR IEDHENSHSR DSAVDDSVDD SVEVTTVTPS HEPKHGEL // ID UNK_DROME STANDARD; PRT; 599 AA. AC Q86B79; Q24580; Q960U9; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Unkempt protein. GN UNK OR CG4620. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=92354890; PubMed=1339381; RA Mohler J., Weiss N., Murli S., Mohammadi S., Vani K., Vasilakis G., RA Song C.H., Epstein A., Kuang T., English J., Cherdak D.; RT "The embryonically active gene, unkempt, of Drosophila encodes a RT Cys3His finger protein."; RL Genetics 131:377-388(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 3-599 FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: ESSENTIAL FOR LATE LARVAL/EARLY PUPAL DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: UBIQUITOUS IN MOST SOMATIC TISSUES FROM CC SYNCYTIAL EMBRYO THROUGH TO EMBRYO STAGE 15. EXPRESSION BECOMES CC RESTRICTED PREDOMINANTLY TO THE CNS AT STAGES 16 AND 17. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND CC ZYGOTICALLY. CC -!- MISCELLANEOUS: MUTANTS HAVE AN 'UNKEMPT' APPEARANCE: SMALL ROUGH CC EYES, HELD OUT WINGS AND CROSSED SCUTELLAR BRISTLES. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -!- SIMILARITY: CONTAINS 4 C3H1-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11527; CAA77616.1; ALT_INIT. DR EMBL; AE003742; AAO41593.1; -. DR EMBL; AY051832; AAK93256.1; ALT_INIT. DR PIR; S42526; S42526. DR FlyBase; FBgn0004395; unk. DR InterPro; IPR000571; Znf_CCCH. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00642; zf-CCCH; 4. DR SMART; SM00356; ZnF_C3H1; 4. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW Developmental protein; DNA-binding; Zinc; Metal-binding; Zinc-finger; KW Repeat. FT DOMAIN 77 97 C3H1-TYPE 1. FT DOMAIN 200 217 C3H1-TYPE 2. FT DOMAIN 236 261 C3H1-TYPE 3. FT DOMAIN 278 297 C3H1-TYPE 4. FT ZN_FING 556 591 RING-TYPE. SQ SEQUENCE 599 AA; 68442 MW; 4BCBD702FF6C9846 CRC64; MLANETNKLL LSSQQEKPNH YTYLKEFRVE QCQSFLQHKC NQHRPFVCFN WHFQNQRRRR PVRKRDGTFN YSADNYCTKY DETTGICPEG DECPYLHRTA GDTERRYHLR YYKTCMCVHD TDSRGYCVKN GLHCAFAHGM QDQRPPVYDI KELETLQNAE STLDSTNALN ALDKERNLMN EDPKWQDTNY VLANYKTEPC KRPPRLCRQG YACPQYHNSK DKRRSPRKYK YRSTPCPNVK HGEEWGEPGN CEAGDNCQYC HTRTEQQFHP EIYKSTKCND VQQAGYCPRS VFCAFAHVEP CSMDDPRENS LSASLANTSL LTRSSAPINI PNTTLSNSIN DFNSGSFAVN IPSSSLTYSP TNHANLFNVD AFNYGGSNKL SNSLSATQND SSLFFPSRII SPGFGDGLSI SPSVRISELN TIRDDINSSS VGNSLFENTL NTAKNAFSLQ SLQSQNNSDL GRITNELLTK NAQIHKLNGR FEDMACKLKI AELHRDKAKQ EAQEWKERYD LAQIQLNLPA ELRDLSIQKL KQLQSKLRTD LEEVDKVLYL ENAKKCMKCE ENNRTVTLEP CNHLSICNTC AESVTECPYC QVPVITTHT // ID URIC_DROME STANDARD; PRT; 352 AA. AC P16163; Q9VLX4; DT 01-APR-1990 (Rel. 14, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN URO OR UO OR CG7171. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=Canton-S; TISSUE=Salivary gland; RX MEDLINE=90377201; PubMed=2118989; RA Wallrath L.L., Burnett J.B., Friedman T.B.; RT "Molecular characterization of the Drosophila melanogaster urate RT oxidase gene, an ecdysone-repressible gene expressed only in the RT Malpighian tubules."; RL Mol. Cell. Biol. 10:5114-5127(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYZES THE OXIDATION OF URIC ACID TO 5- CC HYDROXYISOURATE WHICH SPONTANEOUSLY DECOMPOSE TO FORM ALLANTOIN. CC -!- CATALYTIC ACTIVITY: URATE + O(2) = 5-HYDROXYISOURATE + H(2)O(2). CC -!- ENZYME REGULATION: REPRESSED BY 20-HYDROXYECDYSONE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: MALPIGHIAN TUBULES. CC -!- DEVELOPMENTAL STAGE: THIRD INSTAR LARVAE AND ADULT. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51940; CAA36203.1; -. DR EMBL; AE003618; AAF52555.1; -. DR PIR; A35920; A35920. DR HSSP; Q00511; 1UOX. DR FlyBase; FBgn0003961; Uro. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 2. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 350 352 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 114 114 R -> K (IN REF. 1). SQ SEQUENCE 352 AA; 40062 MW; 1D0E00F8AD0FC96F CRC64; MFATPLRQPA AANHQTPKNS AGMDEHGKPY QYEITDHGYG KDAVKVLHVS RNGPVHAIQE FEVGTHLKLY SKKDYYQGNN SDIVATDSQK NTVYLLAKKH GIESPEKFAL LLARHFINKY SHVEEAHVHV EAYPWQRVCQ EETRTNVNGK CENGVQGNCD FSSIDNRSLH NHAFIFTPTA LHYCDVVIRR TDPKQTVITG IKGLRVLKTT QSSFVNFVND EFRSLPDQYD RIFSTVVDCS WEYSDTENLD FLRAWQTVKN IIIRNFAGDP QVGVSSPSVQ HTLYLSERQV LDVLPQVSVI SMTMPNKHYF NFDTKPFQKI APGDNNEVFI PVDKPHGTIY AQLARKNINS HL // ID US74_DROME STANDARD; PRT; 373 AA. AC Q95YI5; Q9VVG8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE UDP-sugar transporter UST74c (Fringe connection protein). GN FRC OR UST74C OR CG3874. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21424745; PubMed=11533661; RA Goto S., Taniguchi M., Muraoka M., Toyoda H., Sado Y., Kawakita M., RA Hayashi S.; RT "UDP-sugar transporter implicated in glycosylation and processing of RT Notch."; RL Nat. Cell Biol. 3:816-822(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN THE IMPORT OF UDP-SUGARS FROM THE CYTOPLASM CC INTO THE GOLGI LUMEN. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. GOLGI. CC -!- SIMILARITY: BELONGS TO THE NUCLEOTIDE SUGAR TRANSPORTER FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB062677; BAB62105.1; -. DR EMBL; AE003524; AAF49343.1; -. DR FlyBase; FBgn0042641; frc. KW Transport; Sugar transport; Transmembrane; Golgi stack. FT TRANSMEM 89 111 POTENTIAL. FT TRANSMEM 131 153 POTENTIAL. FT TRANSMEM 174 196 POTENTIAL. FT TRANSMEM 206 225 POTENTIAL. FT TRANSMEM 238 260 POTENTIAL. FT TRANSMEM 275 297 POTENTIAL. FT TRANSMEM 302 324 POTENTIAL. FT TRANSMEM 329 351 POTENTIAL. FT CONFLICT 269 269 E -> G (IN REF. 1). FT CONFLICT 275 275 V -> L (IN REF. 1). SQ SEQUENCE 373 AA; 41182 MW; 53DDFF6DA6A76AA5 CRC64; MSMSRGGNTT LDLQPLLAES DVGNRELEEK MGGSADRSSL LDGSGSKELS HREREDSALF VKKIGSALFY GLSSFMITVV NKTVLTSYHF PSFLFLSLGQ LTASIVVLGM GKRLKLVNFP PLQRNTFAKI FPLPLIFLGN MMFGLGGTKT LSLPMFAALR RFSILMTMLL ELKILGLRPS NAVQVSVYAM IGGALLAASD DLSFNMRGYI YVMITNALTA SNGVYVKKKL DTSEIGKYGL MYYNSLFMFL PALALNYVTG NLDQALNFEQ WNDSVFVVQF LLSCVMGFIL SYSTILCTQF NSALTTTIVG CLKNICVTYL GMFIGGDYVF SWLNCIGINI SVLASLLYTY VTFRRKRAPD KQDHLPSTRG ENV // ID USP_DROME STANDARD; PRT; 508 AA. AC P20153; Q9W535; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ultraspiracle protein (XR2C) (Chorion factor 1). GN USP OR NR2B4 OR CF1 OR EG:22E5.1 OR CG4380. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Larva; RX MEDLINE=90384571; PubMed=2169594; RA Oro A.E., McKeown M., Evans R.M.; RT "Relationship between the product of the Drosophila ultraspiracle RT locus and the vertebrate retinoid X receptor."; RL Nature 347:298-301(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=90332404; PubMed=2165589; RA Henrich V.C., Sliter T.J., Lubahn D.B., Macintyre A., Gilbert L.I.; RT "A steroid/thyroid hormone receptor superfamily member in Drosophila RT melanogaster that shares extensive sequence similarity with a RT mammalian homologue."; RL Nucleic Acids Res. 18:4143-4148(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 15-294 FROM N.A. RC TISSUE=Ovary; RX MEDLINE=91007257; PubMed=2120114; RA Shea M.J., King D.L., Conboy M.J., Mariani B.D., Kafatos F.C.; RT "Proteins that bind to Drosophila chorion cis-regulatory elements: a RT new C2H2 zinc finger protein and a C2C2 steroid receptor-like RT component."; RL Genes Dev. 4:1128-1140(1990). RN [6] RP SUBUNITS. RX MEDLINE=94067348; PubMed=8247157; RA Yao T.-P., Froman B.M., Jiang Z., Cherbas L., Chen J.-D., RA McKeown M.M., Cherbas P., Evans R.M.; RT "Functional ecdysone receptor is the product of EcR and Ultraspiracle RT genes."; RL Nature 366:476-479(1993). CC -!- FUNCTION: RECEPTOR FOR ECDYSONE. MAY BE AN IMPORTANT MODULATOR OF CC INSECT METAMORPHOSIS. PLAYS AN IMPORTANT PART IN EMBRYONIC AND CC POST-EMBRYONIC DEVELOPMENT. BINDS TO ECDYSONE RESPONSE ELEMENTS CC (ECRES) SUCH AS IN THE PROMOTER REGION OF S15 CHORION GENE. CC -!- SUBUNIT: HETERODIMER OF USP AND ECR. ONLY THE HETERODIMER IS CC CAPABLE OF HIGH-AFFINITY BINDING TO ECDYSONE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DOMAIN: COMPOSED OF THREE DOMAINS: A MODULATING N-TERMINAL DOMAIN, CC A DNA-BINDING DOMAIN AND A C-TERMINAL STEROID-BINDING DOMAIN. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTOR FAMILY. NR2 CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53417; CAA37496.1; -. DR EMBL; X52591; CAA36827.1; -. DR EMBL; AL031765; CAA21122.1; -. DR EMBL; AE003422; AAF45707.1; -. DR EMBL; X53379; CAA37459.1; -. DR PIR; A35872; A35872. DR PIR; T13737; T13737. DR PDB; 1HG4; 23-FEB-01. DR TRANSFAC; T00117; -. DR FlyBase; FBgn0003964; usp. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0004884; F:ecdysteroid hormone receptor activity; IDA. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS. DR GO; GO:0016322; P:neuronal remodeling; IMP. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Stdhrmn_receptor. DR InterPro; IPR008946; Str_ncl_receptor. DR InterPro; IPR001628; Znf_C4steroid. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; 3D-structure. FT DOMAIN 1 103 MODULATING (BY SIMILARITY). FT DNA_BIND 104 169 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 104 124 C4-TYPE. FT ZN_FING 140 164 C4-TYPE. FT DOMAIN 170 223 HINGE. FT DOMAIN 224 508 LIGAND-BINDING (BY SIMILARITY). FT CONFLICT 213 213 G -> E (IN REF. 2). FT CONFLICT 339 339 MISSING (IN REF. 2). SQ SEQUENCE 508 AA; 55244 MW; 58BA37A9FD9EBE80 CRC64; MDNCDQDASF RLSHIKEEVK PDISQLNDSN NSSFSPKAES PVPFMQAMSM VHVLPGSNSA SSNNNSAGDA QMAQAPNSAG GSAAAAVQQQ YPPNHPLSGS KHLCSICGDR ASGKHYGVYS CEGCKGFFKR TVRKDLTYAC RENRNCIIDK RQRNRCQYCR YQKCLTCGMK REAVQEERQR GARNAAGRLS ASGGGSSGPG SVGGSSSQGG GGGGGVSGGM GSGNGSDDFM TNSVSRDFSI ERIIEAEQRA ETQCGDRALT FLRVGPYSTV QPDYKGAVSA LCQVVNKQLF QMVEYARMMP HFAQVPLDDQ VILLKAAWIE LLIANVAWCS IVSLDDGGAG GGGGGLGHDG SFERRSPGLQ PQQLFLNQSF SYHRNSAIKA GVSAIFDRIL SELSVKMKRL NLDRRELSCL KAIILYNPDI RGIKSRAEIE MCREKVYACL DEHCRLEHPG DDGRFAQLLL RLPALRSISL KCQDHLFLFR ITSDRPLEEL FLEQLEAPPP PGLAMKLE // ID UZIP_DROME STANDARD; PRT; 488 AA. AC P10379; Q960B4; Q9W0W7; DT 01-MAR-1989 (Rel. 10, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Unzipped protein precursor (Zipper protein). GN UZIP OR ZIP OR CG3533. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88296414; PubMed=3402433; RA Zhao D.-B., Code S., Jaehnig F., Haller J., Jaeckle H.; RT "Zipper encodes a putative integral membrane protein required for RT normal axon patterning during Drosophila neurogenesis."; RL EMBO J. 7:1115-1119(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR NORMAL AXON PATTERNING DURING NEUROGENESIS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07450; CAA30332.1; -. DR EMBL; AE003465; AAF47312.2; -. DR EMBL; AY052139; AAK93563.1; -. DR PIR; S00483; EPFF. DR FlyBase; FBgn0004055; uzip. KW Differentiation; Neurogenesis; Transmembrane; Signal. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 488 UNZIPPED PROTEIN. FT DOMAIN 22 465 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 466 486 POTENTIAL. FT DOMAIN 487 488 CYTOPLASMIC (POTENTIAL). FT DOMAIN 380 400 SER/THR-RICH. FT CARBOHYD 35 35 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 232 232 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 317 317 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 374 374 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 448 448 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 488 488 L -> SVDEIELWTQYRV (IN REF. 1). SQ SEQUENCE 488 AA; 54308 MW; 5B4E93D9012A2BE7 CRC64; MTSNSCLISL GLLLVLIQIL APAKAAEHSV FTHKNASSVL GQLVTSSTLV WESYDPKDAT QLQFAVEGGK YVTEDEHYPM YVCRVPIDGI QVSGHTEKIL QRHVCLAAHY KHGKYDNFDV LMNKGHLGKV GWRHWRKFDA GVPVGAIRIG DDSYIGRHRA PSQPNKDGVV THWGADFNLG HLEPVGLGKI RVIEAEREKY YDDGEVLVET EPFRYELRDI KLDRLRTDIQ ENMTELVTRK LENLEDKYST VETILSYTFN YNQYWGSHEG VARGLPTKIF EKDEAVPAEI NWALKHTEKR SENKAVHTKL WPGTAINVTL RGNYVTLEAP YSGKLFAFYY GSDESVSRKI SAEVRKSYLK EVKLEFSPVY WIENGTLVPT TTTTTTTSTS TTTHATTTST NEPTPINEPP LVHMKDNGVQ HSGPDTLEKT LHDSPSSNEL NSHEAPENMS SDPGKDVALA GFGVNAAGST FIAGSALLTL LLTIFLSL // ID V0D1_DROME STANDARD; PRT; 350 AA. AC Q9W4P5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase subunit d 1 (EC 3.6.3.14) (V-ATPase d subunit 1) DE (Vacuolar proton pump d subunit 1) (V-ATPase 39 KDa subunit 1). GN VHAAC39 OR CG2934. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: SUBUNIT OF THE INTEGRAL MEMBRANE V0 COMPLEX OF VACUOLAR CC ATPASE. VACUOLAR ATPASE IS RESPONSIBLE FOR ACIDIFYING A VARIETY OF CC INTRACELLULAR COMPARTMENTS IN EUKARYOTIC CELLS, THUS PROVIDING CC MOST OF THE ENERGY REQUIRED FOR TRANSPORT PROCESSES IN THE CC VACUOLAR SYSTEM. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (COMPONENTS A TO H) ATTACHED TO CC AN INTEGRAL MEMBRANE V0 PROTON PORE COMPLEX (COMPONENTS: A, C, C', CC C'' AND D). CC -!- SIMILARITY: BELONGS TO THE V-ATPASE V0D/AC39 SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003429; AAF45902.1; -. DR FlyBase; FBgn0028665; VhaAC39. DR InterPro; IPR002843; ATPsynt_AC39sub. DR Pfam; PF01992; vATP-synt_AC39; 1. KW Hydrolase; ATP synthesis; Hydrogen ion transport. SQ SEQUENCE 350 AA; 39851 MW; 3BF8B899A29ED02F CRC64; MNSSGFMFNI DNGYLEGLCR GFKCGILKQA DYLNLVQCET LEDLKLHLQG TDYGSFLANE PSPLSVSVID DKLREKLVIE FQHMRNHAVE PLSNFLDFIT YGYMIDNIIL LITGTLHQRP ISELIPKCHP LGSFEQMEAI HVASTPAELY NAVLVDTPLA PFFVDCISEQ DLDEMNIEII RNTLYKAYLE AFYNFCKNMG GATADVMCEI LAFEADRRAI IITINSFGTE LSKDDRAKLY PNCGKMYPDG LAALARADDY EQVKTVAEYY AEYAALFDGS GNNPGDKTLE DKFFEHEVKL DVYAFLQQFH FGVFYAYLKL KEQECRNIVW IAECVAQKHR AKIDNYIPIF // ID VAA1_DROME STANDARD; PRT; 614 AA. AC P48602; Q9V3M7; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase catalytic subunit A isoform 1 (EC 3.6.3.14) (V- DE ATPase A subunit 1) (Vacuolar proton pump alpha subunit 1) (V-ATPase DE 69 kDa subunit 1). GN VHA68-1 OR VHA68 OR VHAA1 OR VHAA OR CG12403. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=97202737; PubMed=9050231; RA Dow J.A.T., Davies S.A., Guo Y., Graham S., Finbow M.E., Kaiser K.; RT "Molecular genetic analysis of V-ATPase function in Drosophila RT melanogaster."; RL J. Exp. Biol. 200:237-245(1997). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Head; RA Guo Y., Dow J.A.T., Kaiser K.; RT "Molecular characterization and mutagenesis of the genes encoding two RT differentially expressed isoforms of the V-ATPase A-subunit in RT Drosophila melanogaster."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYTIC SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF CC VACUOLAR ATPASE. V-ATPASE VACUOLAR ATPASE IS RESPONSIBLE FOR CC ACIDIFYING A VARIETY OF INTRACELLULAR COMPARTMENTS IN EUKARYOTIC CC CELLS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (MAIN COMPONENTS: SUBUNITS A, B, CC C, D, E, AND F) ATTACHED TO AN INTEGRAL MEMBRANE V0 PROTON PORE CC COMPLEX (MAIN COMPONENT: THE PROTEOLIPID PROTEIN). CC -!- SIMILARITY: BELONGS TO THE ATPASE ALPHA/BETA CHAINS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U19745; AAA61761.2; -. DR EMBL; AF185049; AAF00515.1; -. DR EMBL; AE003638; AAF53236.1; -. DR FlyBase; FBgn0020368; Vha68-1. DR InterPro; IPR005725; ATP_synthV_A. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR009005; F1_ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; Hydrogen ion transport; Hydrolase; ATP-binding. FT NP_BIND 247 254 ATP (POTENTIAL). SQ SEQUENCE 614 AA; 68375 MW; 9E3B340722041542 CRC64; MSNLRKFKDE ERESEYGRVY AVSGPVVTAE AMSGSAMYEL VRVGYYELVG EIIRLEGDMA TIQVYEETSG VTVGDPVLRT GKPLSVELGP GIMGSIFDGI QRPLRDIGVM TNSIYIPKGV NTTALSRSEM WEFNPLNVRV GSHITGGDLY GVVHENTLVK QRMIVAPRAK GTVRYIAPAG NYNLEDIVLE TEFDGEITKH TMLQVWPVRQ PRPVTEKLPA NHPLFTGQRV LDSLFPCVQG GTTAIPGAFG CGKTVISQAL SKYSNSDVII YVGCGERGNE MSEVLRDFPE LTCEIDGVTE SIMKRTALVA NTSNMPVAAR EASIYTGITL SEYFRDMGYN VAMMADSTSR WAEALREISG RLAEMPADSG YPAYLGARLA TFYERAGRVK CLGNPEREGS VSIVGAVSPP GGDFSDPVTS ATLGIVQVFW GLDKKLAQRK HFPSINWLIS YSKYMRALDE YYDKNYPEFV PLRTKVKEIL QEEEDLSEIV QLVGKASLAE TDKVTLEVAK LLKDDFLQQN SYSPYDRVCP FYKTVGMLRN IMAFYETARH AVESTAQSDN KITWNTIRES MGGIMYQLSS MKFKDPVKDG EQKIKADYDQ LYEDLQQAFR NLED // ID VAA2_DROME STANDARD; PRT; 614 AA. AC Q27331; Q9VK48; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase catalytic subunit A isoform 2 (EC 3.6.3.14) (V- DE ATPase A subunit 2) (Vacuolar proton pump alpha subunit 2) (V-ATPase DE 69 kDa subunit 2). GN VHA68-2 OR VHAA2 OR CG3762. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R, and Canton-S; RX MEDLINE=97202737; PubMed=9050231; RA Dow J.A.T., Davies S.A., Guo Y., Graham S., Finbow M.E., Kaiser K.; RT "Molecular genetic analysis of V-ATPase function in Drosophila RT melanogaster."; RL J. Exp. Biol. 200:237-245(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYTIC SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF CC VACUOLAR ATPASE. V-ATPASE VACUOLAR ATPASE IS RESPONSIBLE FOR CC ACIDIFYING A VARIETY OF INTRACELLULAR COMPARTMENTS IN EUKARYOTIC CC CELLS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (MAIN COMPONENTS: SUBUNITS A, B, CC C, D, E, AND F) ATTACHED TO AN INTEGRAL MEMBRANE V0 PROTON PORE CC COMPLEX (MAIN COMPONENT: THE PROTEOLIPID PROTEIN). CC -!- SIMILARITY: BELONGS TO THE ATPASE ALPHA/BETA CHAINS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U59146; AAB02270.1; -. DR EMBL; U59147; AAB02271.1; -. DR EMBL; AE003638; AAF53231.1; -. DR FlyBase; FBgn0020367; Vha68-2. DR InterPro; IPR005725; ATP_synthV_A. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR009005; F1_ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; Hydrogen ion transport; Hydrolase; ATP-binding; KW Multigene family. FT NP_BIND 247 254 ATP (POTENTIAL). FT CONFLICT 210 212 HHA -> QPR (IN REF. 2). FT CONFLICT 367 367 R -> A (IN REF. 2). SQ SEQUENCE 614 AA; 68350 MW; 6B9FB730D0FAE803 CRC64; MSNLKRFDDE ERESKYGRVF AVSGPVVTAE AMSGSAMYEL VRVGYYELVG EIIRLEGDMA TIQVYEETSG VTVGDPVLRT GKPLSVELGP GIMGSIFDGI QRPLKDINEL TESIYIPKGV NVPSLSRVAS WEFNPLNVKV GSHITGGDLY GLVHENTLVK HKMIVNPRAK GTVRYIAPSG NYKVDDVVLE TEFDGEITKH TMLQVWPVRH HAPVTEKLPA NHPLLTGQRV LDSLFPCVQG GTTAIPGAFG CGKTVISQAL SKYSNSDVII YVGCGERGNE MSEVLRDFPE LSVEIDGVTE SIMKRTALVA NTSNMPVAAR EASIYTGITL SEYFRDMGYN VSMMADSTSR WAEALREISG RLAEMPRDSG YPAYLGARLA SFYERAGRVK CLGNPEREGS VSIVGAVSPP GGDFSDPVTS ATLGIVQVFW GLDKKLAQRK HFPSINWLIS YSKYMRALDD FYDKNFPEFV PLRTKVKEIL QEEEDLSEIV QLVGKASLAE TDKITLEVAK LLKDDFLQQN SYSSYDRFCP FYKTVGMLRN IIDFYDMARH SVESTAQSEN KITWNVIREA MGNIMYQLSS MKFKDPVKDG EAKIKADFEQ LHEDLQQAFR NLED // ID VAD1_DROME STANDARD; PRT; 246 AA. AC Q9V7D2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Vacuolar ATP synthase subunit D 1 (EC 3.6.3.14) (V-ATPase D subunit 1) DE (Vacuolar proton pump D subunit 1) (dV-ATPase D). GN VHA36 OR CG8186. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Farkas R., Kucharova S., Mechler B.M.; RT "Cloning of Drosophila vacuolar ATPase subunit D."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF VACUOLAR ATPASE. CC V-ATPASE IS RESPONSIBLE FOR ACIDIFYING A VARIETY OF INTRACELLULAR CC COMPARTMENTS IN EUKARYOTIC CELLS, THUS PROVIDING MOST OF THE CC ENERGY REQUIRED FOR TRANSPORT PROCESSES IN THE VACUOLAR SYSTEM (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (COMPONENTS A TO H) ATTACHED TO CC AN INTEGRAL MEMBRANE V0 PROTON PORE COMPLEX (COMPONENTS: A, C, C', CC C'' AND D) (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE V-ATPASE D SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF218238; AAG13186.1; -. DR EMBL; AE003810; AAF58126.1; -. DR EMBL; AY069116; AAL39261.1; -. DR FlyBase; FBgn0022097; Vha36. DR InterPro; IPR002699; ATPsynt_Dsub. DR Pfam; PF01813; ATP-synt_D; 1. DR ProDom; PD004122; ATPsynt_Dsub; 1. DR TIGRFAMs; TIGR00309; V_ATPase_subD; 1. KW Hydrolase; ATP synthesis; Hydrogen ion transport. SQ SEQUENCE 246 AA; 27627 MW; 38B281E251C29590 CRC64; MSGKDRLPIF PSRGAQMLMK ARLAGAQKGH GLLKKKADAL QMRFRLILGK IIETKTLMGD VMKEAAFSLA EAKFTSGDIN QVVLQNVTKA QIKIRTKKDN VAGVTLPVFE SYQDGSDTYE LAGLARGGQQ LAKLKKNYQS AVKLLVELAS LQTSFVTLDE VIKITNRRVN AIEHVIIPRI DRTLAYIISE LDELEREEFY RLKKIQDKKR EARIKADAKK AELLQQGIDV RQQANILDEG DDDVLF // ID VAF1_DROME STANDARD; PRT; 124 AA. AC Q24583; Q9V7E2; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase subunit F (EC 3.6.3.14) (V-ATPase F subunit) DE (Vacuolar proton pump F subunit) (V-ATPase 14 kDa subunit). GN VHA14 OR CG8210. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=96269411; PubMed=8682310; RA Guo Y., Kaiser K., Wieczorek H., Dow J.A.T.; RT "The Drosophila melanogaster gene vha14 encoding a 14-kDa F-subunit RT of the vacuolar ATPase."; RL Gene 172:239-243(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF VACUOLAR ATPASE CC ESSENTIAL FOR ASSEMBLY OR CATALYTIC FUNCTION. V-ATPASE IS CC RESPONSIBLE FOR ACIDIFYING A VARIETY OF INTRACELLULAR COMPARTMENTS CC IN EUKARYOTIC CELLS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (COMPONENTS A TO H) ATTACHED TO CC AN INTEGRAL MEMBRANE V0 PROTON PORE COMPLEX (COMPONENTS: A, C, C', CC C'' AND D). CC -!- SIMILARITY: BELONGS TO THE V-ATPASE F SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z26918; CAA81541.1; -. DR EMBL; AE003810; AAF58115.1; -. DR PIR; JC4849; JC4849. DR FlyBase; FBgn0010426; Vha14. DR InterPro; IPR005772; ATPsynt_F_euk. DR InterPro; IPR008218; ATPsynt_Fsub. DR Pfam; PF01990; ATP-synt_F; 1. DR ProDom; PD003811; ATPsynt_F_euk; 1. DR TIGRFAMs; TIGR01101; V_ATP_synt_F; 1. KW Hydrolase; ATP synthesis; Hydrogen ion transport. SQ SEQUENCE 124 AA; 13850 MW; 1D8DC23808090A96 CRC64; MALHSAIKGK LISVIGDEDT CVGFLLGGVG EINKNRHPNF MVVDKNTAVS ELEDCFKRFL KRDDIDIILI NQNCAELIRH VIDAHTSPVP AVLEIPSKDH PYDASKDSIL RRARGMFNPE DLVR // ID VASA_DROME STANDARD; PRT; 661 AA. AC P09052; Q24582; Q9V3Q8; DT 01-NOV-1988 (Rel. 09, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vasa protein (Antigen Mab46F11). GN VAS OR BG:DS00929.14 OR CG3506. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89014721; PubMed=3140040; RA Lasko P.F., Ashburner M.; RT "The product of the Drosophila gene vasa is very similar to RT eukaryotic initiation factor-4A."; RL Nature 335:611-617(1988). RN [2] RP REVISIONS. RA Lasko P.F.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=89028669; PubMed=3052853; RA Hay B., Jan L.Y., Jan Y.N.; RT "A protein component of Drosophila polar granules is encoded by vasa RT and has extensive sequence similarity to ATP-dependent helicases."; RL Cell 55:577-587(1988). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., RA Moshrefi A., Palazzolo M., Reese M.G., Spradling A.C., Tsang G., RA Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE VASA PROTEIN IS REQUIRED ONLY IN THE FEMALE GERM CC LINE. IT IS IMPORTANT FOR OOCYTE FORMATION AND IN THE CC SPECIFICATION OF THE POSTERIOR STRUCTURES OF THE EMBRYO. CC -!- DEVELOPMENTAL STAGE: MATERNALLY EXPRESSED (DURING OOGENESIS). CC FUNCTION DURING EARLY EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE DEAD BOX HELICASE FAMILY. CC DDX4/VASA SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12945; CAA31405.1; -. DR EMBL; X12946; CAA31405.1; JOINED. DR EMBL; M23560; AAA29013.1; -. DR EMBL; AE003412; AAF44917.1; -. DR EMBL; AE003646; AAF53438.1; -. DR PIR; A58768; A58768. DR HSSP; Q58083; 1HV8. DR FlyBase; FBgn0003970; vas. DR GO; GO:0018994; C:polar granule; IDA. DR GO; GO:0046843; P:dorsal appendage formation; IMP. DR GO; GO:0007292; P:female gamete generation; IMP. DR GO; GO:0007316; P:pole plasm RNA localization; IMP. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. KW Developmental protein; Hydrolase; ATP-binding; Repeat; Helicase. FT NP_BIND 289 296 ATP (BY SIMILARITY). FT SITE 399 402 DEAD BOX. FT DOMAIN 93 127 5 X 7 AA TANDEM REPEATS OF [FS]-R-G-G- FT [EQ]-G-G. FT REPEAT 93 99 1. FT REPEAT 100 106 2. FT REPEAT 107 113 3. FT REPEAT 114 120 4. FT REPEAT 121 127 5. FT CONFLICT 35 35 A -> R (IN REF. 3). FT CONFLICT 153 165 MISSING (IN REF. 3). FT CONFLICT 192 192 V -> A (IN REF. 1 AND 3). FT CONFLICT 265 265 Y -> F (IN REF. 1). FT CONFLICT 322 322 V -> C (IN REF. 3). FT CONFLICT 452 452 F -> S (IN REF. 1). FT CONFLICT 582 582 R -> C (IN REF. 1). FT CONFLICT 594 594 D -> H (IN REF. 3). SQ SEQUENCE 661 AA; 72331 MW; 8617C25CCB3130B9 CRC64; MSDDWDDEPI VDTRGARGGD WSDDEDTAKS FSGEAEGDGV GGSGGEGGGY QGGNRDVFGR IGGGRGGGAG GYRGGNRDGG GFHGGRREGE RDFRGGEGGF RGGQGGSRGG QGGSRGGQGG FRGGEGGFRG RLYENEDGDE RRGRLDREER GGERRGRLDR EERGGERGER GDGGFARRRR NEDDINNNNN IVEDVERKRE FYIPPEPSND AIEIFSSGIA SGIHFSKYNN IPVKVTGSDV PQPIQHFTSA DLRDIIIDNV NKSGYKIPTP IQKCSIPVIS SGRDLMACAQ TGSGKTAAFL LPILSKLLED PHELELGRPQ VVIVSPTREL AIQIFNEARK FAFESYLKIG IVYGGTSFRH QNECITRGCH VVIATPGRLL DFVDRTFITF EDTRFVVLDE ADRMLDMGFS EDMRRIMTHV TMRPEHQTLM FSATFPEEIQ RMAGEFLKNY VFVAIGIVGG ACSDVKQTIY EVNKYAKRSK LIEILSEQAD GTIVFVETKR GADFLASFLS EKEFPTTSIH GDRLQSQREQ ALRDFKNGSM KVLIATSVAS RGLDIKNIKH VINYDMPSKI DDYVHRIGRT GRVGNNGRAT SFFDPEKDRA IAADLVKILE GSGQTVPDFL RTCGAGGDGG YSNQNFGGVD VRGRGNYVGD ATNVEEEEQW D // ID VATB_DROME STANDARD; PRT; 490 AA. AC P31409; Q9VG52; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase subunit B (EC 3.6.3.14) (V-ATPase B subunit) DE (Vacuolar proton pump B subunit) (V-ATPase 57 kDa subunit). GN VHA55 OR CG17369. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=EYA; TISSUE=Head; RX MEDLINE=97094810; PubMed=8940044; RA Davies S.A., Kelly D.C., Goodwin S.F., Yang S., Sozen M.A., RA Kaiser K., Dow J.A.T.; RT "Analysis and inactivation of vha55, the gene encoding the vacuolar RT ATPase B-subunit in Drosophila melanogaster reveals a larval lethal RT phenotype."; RL J. Biol. Chem. 271:30677-30684(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: NONCATALYTIC SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF CC VACUOLAR ATPASE. V-ATPASE IS RESPONSIBLE FOR ACIDIFYING A VARIETY CC OF INTRACELLULAR COMPARTMENTS IN EUKARYOTIC CELLS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (MAIN COMPONENTS: SUBUNITS A, B, CC C, D, E, AND F) ATTACHED TO AN INTEGRAL MEMBRANE V0 PROTON PORE CC COMPLEX (MAIN COMPONENT: THE PROTEOLIPID PROTEIN). CC -!- SIMILARITY: BELONGS TO THE ATPASE ALPHA/BETA CHAINS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67839; CAA48034.1; -. DR EMBL; AE003696; AAF54837.1; -. DR EMBL; AY051623; AAK93047.1; -. DR PIR; S25167; S25167. DR FlyBase; FBgn0005671; Vha55. DR InterPro; IPR005723; ATP_synthV_B. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW Hydrolase; ATP synthesis; Hydrogen ion transport. SQ SEQUENCE 490 AA; 54549 MW; 89651BE1B5A53618 CRC64; MNAQQAQREH VLAVSRDFIS QPRLTYKTVS GVNGPLVILD EVKFPKFAEI VQLRLADGTV RSGQVLEVSG SKAVVQVFEG TSGIDAKNTL CEFTGDILRT PVSEDMLGRV FNGSGKPIDK GPPILAEDFL DIQGQPINPW SRIYPEEMIQ TGISAIDVMN SIARGQKIPI FSAAGLPHNE IAAQICRQAG LVKLPGKSVL DDHTDNFAIV FAAMGVNMET ARFFKQDFEE NGSMENVCLF LNLANDPTIE RIITPRLALT AAEFLAYQCE KHVLVILTDM SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PVNVLPSLSR LMKSAIGEGM TRKDHSDVSN QLYACYAIGK DVQAMKAVVG EEALTPDDLL YLEFLTKFEK NFISQGNYEN RTVFESLDIG WQLLRIFPKE MLKRIPASIL AEFYPRDSRH // ID VATC_DROME STANDARD; PRT; 714 AA. AC Q9V7N5; O18365; Q869C0; Q95RY7; Q9V7N6; Q9V7N7; DT 16-OCT-2001 (Rel. 40, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Vacuolar ATP synthase subunit C (EC 3.6.3.14) (V-ATPase C subunit) DE (Vacuolar proton pump C subunit). GN VHA44 OR L(2)06072 OR CG8048. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A), AND TISSUE SPECIFICITY. RC TISSUE=CNS, and Larval ring gland; RX MEDLINE=98250685; PubMed=9584098; RA Harvie P.D., Filippova M., Bryant P.J.; RT "Genes expressed in the ring gland, the major endocrine organ of RT Drosophila melanogaster."; RL Genetics 149:217-231(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF VACUOLAR ATPASE. CC SUBUNIT C IS NECESSARY FOR THE ASSEMBLY OF THE CATALYTIC SECTOR OF CC THE ENZYME AND IS LIKELY TO HAVE A SPECIFIC FUNCTION IN ITS CC CATALYTIC ACTIVITY. V-ATPASE IS RESPONSIBLE FOR ACIDIFYING A CC VARIETY OF INTRACELLULAR COMPARTMENTS IN EUKARYOTIC CELLS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (COMPONENTS A TO H) ATTACHED TO AN CC INTEGRAL MEMBRANE V0 PROTON PORE COMPLEX (COMPONENTS: A, C, C', CC C'' AND D). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=D; CC IsoId=Q9V7N5-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=A; Synonyms=B; CC IsoId=Q9V7N5-2; Sequence=VSP_000440; CC Name=C; CC IsoId=Q9V7N5-3; Sequence=VSP_008707, VSP_000441; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: IN LARVAE, EXPRESSED IN THE RING GLAND, CNS, CC IMAGINAL DISKS AND LYMPH GLAND. CC -!- SIMILARITY: BELONGS TO THE V-ATPASE C SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF006655; AAB62571.1; -. DR EMBL; AE003807; AAF58013.3; -. DR EMBL; AE003807; AAF58012.1; -. DR EMBL; AE003807; AAM68515.1; -. DR EMBL; AY061038; AAL28586.1; -. DR EMBL; AY102676; AAM27505.1; -. DR FlyBase; FBgn0020611; Vha44. DR GO; GO:0000221; C:hydrogen-transporting ATPase V1 domain; ISS. DR GO; GO:0015992; P:proton transport; ISS. DR InterPro; IPR004907; V-ATPase_C. DR Pfam; PF03223; V-ATPase_C; 1. KW Hydrolase; ATP synthesis; Hydrogen ion transport; KW Alternative splicing. FT VARSPLIC 97 422 Missing (in isoform A). FT /FTId=VSP_000440. FT VARSPLIC 151 151 G -> A (in isoform C). FT /FTId=VSP_008707. FT VARSPLIC 152 423 Missing (in isoform C). FT /FTId=VSP_000441. FT CONFLICT 593 593 T -> P (IN REF. 1). SQ SEQUENCE 714 AA; 78856 MW; 96C9FA90460101EF CRC64; MMSEYWIISA PGDKTCQQTY DTMNNLTSKQ HNLCNNYKFH IPDLKVGTLD QLVGLSDDLG KLDTYVEQIT RKVANYLGEV LEDQRDKLHE NLMANNSPGP PDDSMPCRHH QRIKHLSLRH QRKHQHTHHQ NKPQHYHHHH HHHQLPQDLK GKSAATCSPA TPPAPASAPP HLPPACACDV LAPGSLTGGS LTNLSTSHEP EPEFDVCPCD ECFACAPPST SATASTLLAD ECYSQTASSM LSATRCALST VAAIATGSGL GNGPSTSAAA AAAASNSSGG GGGGGPASCS TLCSSAYFST SAPTTSSSVH SSMSRSNSKR LNNNTCSINN NKLSFRSGSH VSQLHLATQQ PQHHHSHPHQ QPHTNPLQSP VQKSMSEDEG DASNAHEDGE TDEDPKSPHS VQSDLSDAFD WWFNKPKRNS KKTELPQYLT RFQWDMAKYP IKQSLRNIAD IISKQIGQID GDLKTKSQAY NNLKGNLQNL EKKKTGSLLT RNLADLVKKE HFILDSEYLT TLLVIVPKVM ANDWLTNYEK ITDMIVPRSS QLIQEDADYC LFNVTLFKKV AEEFKLHARE RKFIVRDFVY NEEELAAGKN EMTKLMTDKK KQFGPLVRWL KVNFSEAFCA LIHVKALRVF VESVLRYGLP VNFQAILIEP NKKSVKRLRD VLNQLYGHLD GASAGGAVSS ADNVDIPGLG FGQSEYFPYV FYKVNIDMVE QAKV // ID VATE_DROME STANDARD; PRT; 226 AA. AC P54611; Q9V3K4; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase subunit E (EC 3.6.3.14) (V-ATPase E subunit) DE (Vacuolar proton pump E subunit) (V-ATPase 28 kDa subunit). GN VHA26 OR CG1088. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=96350394; PubMed=8765087; RA Guo Y., Wang Z., Carter A., Kaiser K., Dow J.A.T.; RT "Characterisation of vha26, the Drosophila gene for a 26 kDa RT E-subunit of the vacuolar ATPase."; RL Biochim. Biophys. Acta 1283:4-9(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). CC -!- FUNCTION: SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF VACUOLAR ATPASE CC ESSENTIAL FOR ASSEMBLY OR CATALYTIC FUNCTION. V-ATPASE IS CC RESPONSIBLE FOR ACIDIFYING A VARIETY OF INTRACELLULAR COMPARTMENTS CC IN EUKARYOTIC CELLS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (COMPONENTS A TO H) ATTACHED TO CC AN INTEGRAL MEMBRANE V0 PROTON PORE COMPLEX (COMPONENTS: A, C, C', CC C'' AND D) (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE V-ATPASE E SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U38951; AAB09739.1; -. DR EMBL; U38198; AAB09738.1; -. DR EMBL; AE003602; AAF51997.1; -. DR EMBL; AF145618; AAD38593.1; -. DR FlyBase; FBgn0015324; Vha26. DR InterPro; IPR002842; ATPsynt_Esub. DR Pfam; PF01991; vATP-synt_E; 1. KW Hydrolase; ATP synthesis; Hydrogen ion transport. SQ SEQUENCE 226 AA; 26082 MW; AF3CFAC426AF4EC2 CRC64; MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQQQR LKIMEYYEKK EKQVELQKKI QSSNMLNQAR LKVLKVREDH VSSVLDDARK RLGEVTKNQS EYETVLTKLI VQGLFQIMEP KVILRCREVD VPLVRNVLPA AVEQYKAQIN QNVELFIDEK DFLSADTCGG VELLALNGRI KVPNTLESRL DLISQQLVPE IRNALFGRNV NRKFTD // ID VATG_DROME STANDARD; PRT; 117 AA. AC Q9XZH6; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase subunit G (EC 3.6.3.14) (V-ATPase G subunit) DE (Vacuolar proton pump G subunit) (V-ATPase 13 kDa subunit). GN VHA13 OR CG6213. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Dow J.A.T.; RT "The Drosophila vha13 gene encodes a G-subunit of the VATPase."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CATALYTIC SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF CC VACUOLAR ATPASE. V-ATPASE VACUOLAR ATPASE IS RESPONSIBLE FOR CC ACIDIFYING A VARIETY OF INTRACELLULAR COMPARTMENTS IN EUKARYOTIC CC CELLS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (COMPONENTS A TO H) ATTACHED TO CC AN INTEGRAL MEMBRANE V0 PROTON PORE COMPLEX (COMPONENTS: A, C, C', CC C'' AND D). CC -!- SIMILARITY: BELONGS TO THE V-ATPASE G SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF143200; AAD32690.1; -. DR EMBL; AE003727; AAF55686.1; -. DR FlyBase; FBgn0026753; Vha13. DR InterPro; IPR005124; V-ATPase_G. DR Pfam; PF03179; V-ATPase_G; 1. DR TIGRFAMs; TIGR01147; V_ATP_synt_G; 1. KW Hydrolase; ATP synthesis; Hydrogen ion transport. SQ SEQUENCE 117 AA; 13625 MW; 66152EEA4422A0C8 CRC64; MASQTQGIQQ LLAAEKKAAE KVAEARKRKA RRLKQAKDEA TEEIEKFRQE RERAFKEFEA KHMGSREGVA AKIDADIRVK LADMDRAIQT RKDPFILEIL QYVYNISPEV HKNYNHK // ID VATH_DROME STANDARD; PRT; 392 AA. AC Q9V3J1; Q9VJJ2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase subunit H (EC 3.6.3.14) (V-ATPase H subunit) DE (Vacuolar proton pump H subunit) (Vacuolar proton pump subunit SFD). GN VHASFD OR CG17332. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Westhoff M.A., Dow J.A.T.; RT "Characterization of vhaSFD, the gene encoding a SFD subunit of the RT Drosophila V-ATPAse."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: SUBUNIT OF THE PERIPHERAL V1 COMPLEX OF VACUOLAR ATPASE. CC SUBUNIT H ACTIVATE ATPASE ACTIVITY OF THE ENZYME AND COUPLE ATPASE CC ACTIVITY TO PROTON FLOW. VACUOLAR ATPASE IS RESPONSIBLE FOR CC ACIDIFYING A VARIETY OF INTRACELLULAR COMPARTMENTS IN EUKARYOTIC CC CELLS, THUS PROVIDING MOST OF THE ENERGY REQUIRED FOR TRANSPORT CC PROCESSES IN THE VACUOLAR SYSTEM (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (COMPONENTS A TO H) ATTACHED TO CC AN INTEGRAL MEMBRANE V0 PROTON PORE COMPLEX (COMPONENTS: A, C, C', CC C'' AND D). CC -!- SIMILARITY: BELONGS TO THE V-ATPASE H SUBUNIT FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF159457; AAD47254.1; -. DR EMBL; AE003652; AAF53555.2; ALT_SEQ. DR EMBL; AE003652; AAF53556.2; ALT_SEQ. DR FlyBase; FBgn0027779; VhaSFD. DR InterPro; IPR008938; ARM. DR InterPro; IPR004908; V-ATPase_H. DR Pfam; PF03224; V-ATPase_H; 1. KW Hydrolase; ATP synthesis; Hydrogen ion transport. SQ SEQUENCE 392 AA; 45159 MW; B7F6E1BB712F4305 CRC64; MIAATSVLQQ QAADIRTRTI NWASYMQSQM ISEEDYKAIS ALDKSRASFL AQNSSQVVKT LLNLVSHLSK DSTIQYILVL LDDLLQEDRS RVDLFHDTAG KLKQCIWGPF LNLLNRQDGF IVNMSSRILA KFACWGHETM PKSDLNFYLQ FLKDQLASNN NEYIQSVARC LQMMLRVDEY RFAFVGVDGI STLIRILSTR VNFQVQYQLI FCLWVLTFNP LLAAKMNKFS VIPILADILS DCAKEKVTRI ILAVFRNLIE KPEDSSVAKD HCIAMVQCKV LKQLSILEQR RFDDEDITAD VEYLSEKLQN SVQDLSSFDE YATEVRSGRL EWSPVHKSAK FWRENAQRLN EKNYELLRIL VHLLETSKDA IILSVACFDI GEYVRHYPRG KQ // ID VATL_DROME STANDARD; PRT; 159 AA. AC P23380; Q9V9D2; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vacuolar ATP synthase 16 kDa proteolipid subunit (EC 3.6.3.14) DE (Ductin) (VHA16K). GN VHA16 OR VHA OR CG3161. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91067485; PubMed=2147478; RA Meagher L., McLean P., Finbow M.E.; RT "Sequence of a cDNA from Drosophila coding for the 16 kD proteolipid RT component of the vacuolar H(+)-ATPase."; RL Nucleic Acids Res. 18:6712-6712(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=95074257; PubMed=7983150; RA Finbow M.E., Goodwin S.F., Meagher L., Lane N.J., Keen J., RA Findlay J.B.C., Kaiser K.; RT "Evidence that the 16 kDa proteolipid (subunit c) of the vacuolar RT H(+)- ATPase and ductin from gap junctions are the same polypeptide RT in Drosophila and Manduca: molecular cloning of the Vha16k gene from RT Drosophila."; RL J. Cell Sci. 107:1817-1824(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: PROTON-CONDUCTING PORE FORMING SUBUNIT OF THE MEMBRANE CC INTEGRAL V0 COMPLEX OF VACUOLAR ATPASE. V-ATPASE IS RESPONSIBLE CC FOR ACIDIFYING A VARIETY OF INTRACELLULAR COMPARTMENTS IN CC EUKARYOTIC CELLS. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(IN) = ADP + PHOSPHATE + CC H(+)(OUT). CC -!- SUBUNIT: V-ATPASE IS AN HETEROMULTIMERIC ENZYME COMPOSED OF A CC PERIPHERAL CATALYTIC V1 COMPLEX (MAIN COMPONENTS: SUBUNITS A, B, CC C, D, E, AND F) ATTACHED TO AN INTEGRAL MEMBRANE V0 PROTON PORE CC COMPLEX (MAIN COMPONENT: THE PROTEOLIPID PROTEIN; WHICH IS PRESENT CC AS A HEXAMER THAT FORMS THE PROTON-CONDUCTING PORE). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. VACUOLAR. CC -!- MISCELLANEOUS: THIS SUBUNIT BINDS DICYCLOHEXYLCARBODIIMIDE (DCDD) CC WHICH INHIBITS THE ATPASE. CC -!- SIMILARITY: BELONGS TO THE V-ATPASE PROTEOLIPID SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55979; CAA39449.1; -. DR EMBL; X77936; CAA54908.1; -. DR EMBL; AE003789; AAF57361.1; -. DR PIR; S42878; S42878. DR FlyBase; FBgn0004145; Vha16. DR InterPro; IPR002379; ATPase_Csub. DR InterPro; IPR000245; Vac_ATPsynt_Csub. DR Pfam; PF00137; ATP-synt_C; 2. DR PRINTS; PR00122; VACATPASE. DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1. KW Hydrolase; Hydrogen ion transport; ATP synthesis; Transmembrane. FT DOMAIN 1 12 LUMENAL (POTENTIAL). FT TRANSMEM 13 35 POTENTIAL. FT DOMAIN 36 57 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 58 78 POTENTIAL. FT DOMAIN 79 96 LUMENAL (POTENTIAL). FT TRANSMEM 97 118 POTENTIAL. FT DOMAIN 119 130 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 131 156 POTENTIAL. FT DOMAIN 157 159 LUMENAL (POTENTIAL). FT BINDING 143 143 DICYCLOHEXYLCARBODIIMIDE (POTENTIAL). SQ SEQUENCE 159 AA; 16267 MW; 9F147F8D72C72123 CRC64; MSSEVSSDNP IYGPFFGVMG AASAIIFSAL GAAYGTAKSG TGIAAMSVMR PELIMKSIIP VVMAGIIAIY GLVVAVLIAG ALEEPSKYSL YRGFIHLGAG LAVGFSGLAA GFAIGIVGDA GVRGTAQQPR LFVGMILILI FAEVLGLYGL IVAIYLYTK // ID VAT_DROME STANDARD; PRT; 578 AA. AC O17444; Q9VE42; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vesicular acetylcholine transporter (VAChT). GN VACHT OR CG32848/CG12345. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=98112815; PubMed=9446576; RA Kitamoto T., Wang W., Salvaterra P.M.; RT "Structure and organization of the Drosophila cholinergic locus."; RL J. Biol. Chem. 273:2706-2713(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: INVOLVED IN ACETYLCHOLINE TRANSPORT INTO SYNAPTIC CC VESICLES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE MAJOR FACILITATOR (MFS) SUPERFAMILY. CC VESICULAR TRANSPORTER FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF030197; AAB86609.1; -. DR EMBL; AE003723; AAF55587.2; -. DR FlyBase; FBgn0015323; VAChT. DR InterPro; IPR004734; Drug_resist. DR InterPro; IPR007114; MFS. DR InterPro; IPR005828; Sub_transporter. DR Pfam; PF00083; sugar_tr; 1. DR TIGRFAMs; TIGR00880; 2_A_01_02; 1. DR PROSITE; PS50850; MFS; 1. KW Transport; Neurotransmitter transport; Transmembrane; Glycoprotein. FT DOMAIN 1 32 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 33 53 POTENTIAL. FT DOMAIN 54 98 VESICULAR LUMEN (POTENTIAL). FT TRANSMEM 99 119 POTENTIAL. FT DOMAIN 120 125 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 126 146 POTENTIAL. FT DOMAIN 147 154 VESICULAR LUMEN (POTENTIAL). FT TRANSMEM 155 175 POTENTIAL. FT DOMAIN 176 187 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 188 208 POTENTIAL. FT DOMAIN 209 215 VESICULAR LUMEN (POTENTIAL). FT TRANSMEM 216 236 POTENTIAL. FT DOMAIN 237 263 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 264 284 POTENTIAL. FT DOMAIN 285 299 VESICULAR LUMEN (POTENTIAL). FT TRANSMEM 300 320 POTENTIAL. FT DOMAIN 321 330 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 331 351 POTENTIAL. FT DOMAIN 352 355 VESICULAR LUMEN (POTENTIAL). FT TRANSMEM 356 376 POTENTIAL. FT DOMAIN 377 387 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 388 408 POTENTIAL. FT DOMAIN 409 413 VESICULAR LUMEN (POTENTIAL). FT TRANSMEM 414 434 POTENTIAL. FT DOMAIN 435 578 CYTOPLASMIC (POTENTIAL). FT DOMAIN 509 513 POLY-GLN. FT DOMAIN 549 563 POLY-GLN. FT CARBOHYD 78 78 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 293 293 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 97 97 T -> S (IN REF. 1). FT CONFLICT 160 160 A -> V (IN REF. 1). FT CONFLICT 272 272 L -> M (IN REF. 1). SQ SEQUENCE 578 AA; 64313 MW; 4E73402CB934E4B5 CRC64; MASFQIPVIN LEVREVKDIV WEKIQEPVNQ RRLILVIVSI ALLLDNMLYM VIVPIIPDYL REIGSFDDGP TPPPLRDNIT GKIIPVHHDH HGQDSATGIL FASKAIVQLM VNPFSGGLID KIGYDLPMMI GLTIMFFSTA VFACGSSYSV LFFARSLQGA GSAFADTAGL AMIADRFTEE NERSQALGIA LAFISFGCLV APPFGGALYQ FAGKEVPFLI LALVCLLDGL MLLLVMKPVK EAMKQSKDVQ DQVIPIWRLL MDPYIAVCAG ALTMSNVALA FLEPTISLWM EDNMTTDNWK IGMVWLPAFF PHVLGVVITV KMARKYPQHQ WLMAAGGLAL EGFSCFIIPF CSGYKMLMLP ICVICFGIAL IDTALLPTLG YLVDVRYVSV YGSIYAIADI SYSIAYAVGP IIAGGVVEAI GFTALNFLIA FSNLAYVPVL RKLRNIYDFK PFENEANILM QDPPNKEYQT YVMHDQKPVE GGVKNHLEYG QQYQQEQETN LDDQQYEYQQ QQQGYQQGYQ QDQGYQPGYQ EQGGSYAPQG QPRVANPFQQ QQQQQQQQQQ QVQSRGPAAP ANPFRQGF // ID VAV_DROME STANDARD; PRT; 793 AA. AC Q9NHV9; Q8T061; Q9VWJ5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vav protein (DroVav). GN VAV OR CG7893. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=20245449; PubMed=10781813; RA Dekel I., Russek N., Jones T., Mortin M.A., Katzav S.; RT "Identification of the Drosophila melanogaster homologue of the RT mammalian signal transducer protein, Vav."; RL FEBS Lett. 472:99-104(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: COUPLES TYROSINE KINASE SIGNALS WITH THE ACTIVATION OF CC THE RHO/RAC GTPASES. PROBABLY PLAYS A PIVOTAL ROLE AS A SIGNAL CC TRANSDUCER PROTEIN DURING FRUIT FLY DEVELOPMENT. CC -!- TISSUE SPECIFICITY: UBIQUITOUS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED BOTH MATERNALLY AND ZYGOTICALLY IN CC ALL STAGES OF DEVELOPMENT. CC -!- PTM: PHOSPHORYLATED ON TYROSINE RESIDUES. CC -!- SIMILARITY: CONTAINS 1 CALPONIN-HOMOLOGY (CH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 DBL-HOMOLOGY (DH) DOMAIN. CC -!- SIMILARITY: CONTAINS 1 PH DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 ZINC-DEPENDENT PHORBOL-ESTER AND DAG CC BINDING DOMAIN. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF218780; AAF28765.1; -. DR EMBL; AE003511; AAF48943.2; ALT_SEQ. DR EMBL; AY069536; AAL39681.1; -. DR FlyBase; FBgn0040068; vav. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS. DR GO; GO:0005100; F:Rho GTPase activator activity; ISS. DR GO; GO:0007266; P:Rho protein signal transduction; ISS. DR InterPro; IPR001715; Calponin-like. DR InterPro; IPR003247; CH_type. DR InterPro; IPR002219; DAG_PE-bind. DR InterPro; IPR001849; PH. DR InterPro; IPR000219; RhoGEF. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3. DR Pfam; PF00307; CH; 1. DR Pfam; PF00130; DAG_PE-bind; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00621; RhoGEF; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3; 1. DR PRINTS; PR00401; SH2DOMAIN. DR ProDom; PD001527; CH_type; 1. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00033; CH; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00325; RhoGEF; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 1. DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW Phorbol-ester binding; Zinc; SH2 domain; SH3 domain; KW Guanine-nucleotide releasing factor; Repeat; Phosphorylation. FT DOMAIN 18 136 CH. FT DOMAIN 216 396 DH. FT DOMAIN 432 541 PH. FT DOMAIN 553 601 PHORBOL-ESTER AND DAG BINDING. FT DOMAIN 622 726 SH2. FT DOMAIN 726 788 SH3. FT CONFLICT 53 53 T -> M (IN REF. 1). FT CONFLICT 148 148 F -> L (IN REF. 1). FT CONFLICT 372 372 L -> M (IN REF. 1). FT CONFLICT 503 503 R -> E (IN REF. 1). FT CONFLICT 645 664 LLRVRPQGPSTAHETMYALS -> PVASSSAGPIHCPRDDV FT CAY (IN REF. 1). FT CONFLICT 739 739 P -> Q (IN REF. 1). SQ SEQUENCE 793 AA; 91355 MW; 1031929FE4FB8BF3 CRC64; MASSSSSNSF GGVAGVNGDL WRECVAWLTR CKVIPPDHKA AQPDAEIRIL AMTLRDGVLL CNLVIHLDPS SLDPREFNRK PQMAQFLCSK NIKLFLDVCH NNFGIRDADL FEPTMLYDLT NFHRVLITLS KLSQCRKVQQ LHPDLIGFNL QLSPTERSHS DEAIYKDLHS TTTDNIACNG TGYDHTNTKE EEVYQDLCAL HRTSRSQTAS STSFEQRDYV IRELIDTESN YLDVLTALKT KFMGPLERHL NQDELRLIFP RIRELVDIHT KFLDKLRESL TPNAKVKMAQ VFLDFREPFL IYGEFCSLLL GAIDYLADVC KKNQIIDQLV QKCERDYNVG KLQLRDILSV PMQRILKYHL LLDKLVKETS PLHDDYRSLE RAKEAMIDVS QYINEVKRDS DHLVIIQKVK DSICDIHLLQ NGNGSDLLQY GRLLLDGELH IKAHEDQKTK LRYAFVFDKI LIMVKALHIK TGDMQYTYRD SHNLADYRVE QSHSRRTIGR DTRFKYQLLL ARKSGKTAFT LYLKSEHERD KWRKALTEAM ESLEPPGCQS TDHKMEIYTF DAPTTCRHCS KFLKGRIHQG YRCKVCQISV HKGCISSTGR CKQNPVSVPP PVCDRQLSEF NWFAGNMDRE TAAHRLENRR IGTYLLRVRP QGPSTAHETM YALSLKTDDN VIKHMKINQE NSGDSMLYCL SSRRHFKTIV ELVSYYERND LGENFAGLNQ SLQWPYKEVI ATALYDYEPK AGSNQLQLRT DCQVLVIGKD GDSKGWWRGK IGDTVGYFPK EYVQEQKLAS EEL // ID VEIN_DROME STANDARD; PRT; 623 AA. AC Q94918; Q9VRQ3; DT 16-OCT-2001 (Rel. 40, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vein protein precursor (Epidermal growth factor-like protein) DE (Defective dorsal discs protein). GN VN OR DDD OR CG10491. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC TISSUE=Embryo, and Imaginal disks; RX MEDLINE=96421972; PubMed=8824589; RA Schnepp B.C., Grumbling G.B., Donaldson T.D., Simcox A.A.; RT "Vein is a novel component in the Drosophila epidermal growth factor RT receptor pathway with similarity to the neuregulins."; RL Genes Dev. 10:2302-2313(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: LIGAND FOR THE EGFR RECEPTOR. SEEMS TO PLAY A ROLE IN CC THE GLOBAL PROLIFERATION OF WING DISC CELLS AND THE LARVAL CC PATTERNING. SHOWS A STRONG SYNERGISTIC GENETIC INTERACTION WITH CC SPI, SUGGESTING A MOLECULAR INTERDEPENDENCE. REQUIRED FOR THE CC DEVELOPMENT OF INTERVEINS CELLS. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q94918-1; Sequence=Displayed; CC Name=2; CC IsoId=Q94918-2; Sequence=VSP_001419; CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN BLASTODERM EMBRYOS IN TWO CC VENTROLATERAL STRIPES THAT ARE BROUGHT TO THE MIDLINE AS CC GASTRULATION PROCEEDS. IN THE GERM-BAND RETRACTION STAGE, CC EXPRESSION IS SEEN IN THE CNS AND EPIDERMIS. AT LATE BLASTODERM, CC EXPRESSION IS LOCALIZED IN THE ANLAGEN OF THE AMNIOSEROSA. CC EXPRESSION IN THE HEAD, CYPEOLABRUM, MAXILLARY AND LABIAL LOBES, CC AND AROUND THE STOMODEUM THROUGHOUT EMBRYO DEVELOPMENT. IN LATE CC EMBRYOS, EXPRESSION DECAYS IN ALL ECTODERMAL CELLS AND APPEARS IN CC THE SEGMENTAL MUSCLES AND THE GUT WALL. IN THE LARVA, EXPRESSION CC OCCURS IN THE DORSAL METATHORACIC DISC, THE EYE-ANTENNAL DISC AND CC THE VENTRAL THORACIC DISC. FOUND IN THE INTERVEIN IN THE PUPA. CC -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN. CC -!- SIMILARITY: CONTAINS 1 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U67935; AAC47293.1; -. DR EMBL; AE003564; AAF50739.2; -. DR FlyBase; FBgn0003984; vn. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0005154; F:epidermal growth factor receptor binding; IMP. DR GO; GO:0007173; P:EGF receptor signaling pathway; IMP. DR GO; GO:0007477; P:notum morphogenesis; IMP. DR GO; GO:0045742; P:positive regulation of EGF receptor signali...; NAS. DR GO; GO:0007476; P:wing morphogenesis; IMP. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006210; IEGF. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR Pfam; PF00008; EGF; 1. DR Pfam; PF00047; ig; 1. DR SMART; SM00181; EGF; 1. DR SMART; SM00408; IGc2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; FALSE_NEG. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50835; IG_LIKE; 1. KW EGF-like domain; Glycoprotein; Immunoglobulin domain; Growth factor; KW Developmental protein; Alternative splicing; Signal. FT SIGNAL 1 40 POTENTIAL. FT CHAIN 41 623 VEIN PROTEIN. FT DOMAIN 457 542 IG-LIKE C2-TYPE. FT DOMAIN 561 599 EGF-LIKE. FT DOMAIN 43 53 POLY-GLN. FT DOMAIN 87 96 POLY-SER. FT DOMAIN 138 314 GLN-RICH. FT DISULFID 478 531 BY SIMILARITY. FT CARBOHYD 76 76 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 252 252 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 350 350 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 381 381 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 424 424 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 449 449 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 521 521 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 574 574 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 609 623 FVAIYGQIHTLNNDY -> SSPESCKNYQGGYY (in FT isoform 2). FT /FTId=VSP_001419. FT CONFLICT 149 149 MISSING (IN REF. 1). FT CONFLICT 220 220 S -> T (IN REF. 1). FT CONFLICT 494 494 E -> D (IN REF. 1). SQ SEQUENCE 623 AA; 71697 MW; AFD2724D5C1F56C8 CRC64; MYAQHLRKWS LKTKKQLMPL ILLIISYMLL LNTCVLSSSA TTQQQQQQQQ QQQHLPRLWE GSAEESSYYI PLSSDNGSGS SESSAESGSS SSRSSSNNID NNILSRLLSL NSNSLSSRSN VKLKPATVFD AGSSTPAQQE QHVAAVPEQQ QQQQQQQQSM QKVPNTLINS QIYNLLYNGM PSEAASSKMR RHIQPSQLPH QPESRAQLPS NYSSRPAVRS YLIESYEMPE SMLEDRSPEQ AARSRRDGSN TNGSRQQQRT GHRQQLQQDK RDHRRQRQDQ QKEQRQQQQQ RQHKSGNKHQ QQQQQRRKHQ RKHQRYNRYC SARDPAQLAF AAPTVFQGVF KSMSADRRVN FSATMKVEKV YKQQHDLQLP TLVRLQFALS NSSGECDIYR ERLMPRGMLR SGNDLQQASD ISYMMFVQQT NPGNFTILGQ PMRVTHLVVE AVETAVSENY TQNAEVTKIF SKPSKAIIKH GKKLRIVCEV SGQPPPKVTW FKDEKSINRK RNIYQFKHHK RRSELIVRSF NSSSDAGRYE CRAKNKASKA IAKRRIMIKA SPVHFPTDRS ASGIPCNFDY CFHNGTCRMI PDINEVYCRC PTEYFGNRCE NKWPDSRYFV AIYGQIHTLN NDY // ID VERM_DROME STANDARD; PRT; 379 AA. AC P20351; Q9VZ50; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Tryptophan 2,3-dioxygenase (EC 1.13.11.11) (Tryptophan pyrrolase) DE (Vermilion protein). GN V OR CG5163. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90205819; PubMed=2108317; RA Searles L.L., Ruth R.S., Pret A.-M., Fridell R.A., Ali A.J.; RT "Structure and transcription of the Drosophila melanogaster vermilion RT gene and several mutant alleles."; RL Mol. Cell. Biol. 10:1423-1431(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: DURING LARVAL LIFE CONTROLS THE LEVEL OF POTENTIALLY CC HARMFUL FREE TRYPTOPHAN IN THE HEMOLYMPH BY CONVERTING IT TO CC KYNURENINE, AND DURING ADULT DEVELOPMENT THE SAME REACTION IS THE CC FIRST STEP IN THE OMMOCHROME BIOSYNTHETIC PATHWAY. CC -!- CATALYTIC ACTIVITY: L-TRYPTOPHAN + O(2) = L-FORMYLKYNURENINE. CC -!- PATHWAY: BROWN EYE PIGMENT BIOSYNTHESIS; FIRST STEP. CC -!- DEVELOPMENTAL STAGE: HIGH IN LATE LARVAE AND IN ADULT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M34147; AAA29014.1; -. DR EMBL; AE003484; AAF47978.1; -. DR EMBL; AY051478; AAK92902.1; -. DR PIR; A34780; A34780. DR FlyBase; FBgn0003965; v. DR GO; GO:0006727; P:ommochrome biosynthesis; IMP. DR InterPro; IPR004981; Trp_dioxygenase. DR Pfam; PF03301; Trp_dioxygenase; 1. KW Oxidoreductase; Dioxygenase. SQ SEQUENCE 379 AA; 44421 MW; E9E4C1B1C86D687F CRC64; MSCPYAGNGN DHDDSAVPLT TEVGKIYGEY LMLDKLLDAQ CMLSEEDKRP VHDEHLFIIT HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT PLDFMDFRKY LAPASGFQSL QFRLIENKLG VLTEQRVRYN QKYSDVFSDE EARNSIRNSE KDPSLLELVQ RWLERTPGLE ESGFNFWAKF QESVDRFLEA QVQSAMEEPV EKAKNYRLMD IEKRREVYRS IFDPAVHDAL VRRGDRRFSH RALQGAIMIT FYRDEPRFSQ PHQLLTLLMD IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFLDL FNLSTFLIPR EAIPPLDETI RKKLINKSV // ID VG_DROME STANDARD; PRT; 453 AA. AC Q26366; Q9V6H9; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vestigial protein. GN VG OR CG3830. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92090727; PubMed=1752439; RA Williams J.A., Bell J.B., Carroll S.B.; RT "Control of Drosophila wing and haltere development by the nuclear RT vestigial gene product."; RL Genes Dev. 5:2481-2495(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: INVOLVED IN DETERMINING WHICH THORACIC IMAGINAL DISK CC CELLS WILL FORM WINGS AND HALTERES, PERHAPS BY INTERACTING WITH CC OTHER NUCLEAR REGULATORY PROTEINS. LOSS OF VESTIGIAL FUNCTION CC SELECTIVELY ELIMINATES WING AND HALTERE FORMATION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S72379; AAB20671.1; -. DR EMBL; AE003820; AAF58444.1; -. DR PIR; A41640; A41640. DR FlyBase; FBgn0003975; vg. DR GO; GO:0008587; P:wing margin morphogenesis; NAS. DR InterPro; IPR006627; DUF_TDU. DR SMART; SM00711; TDU; 1. KW Nuclear protein; Developmental protein. FT DOMAIN 69 79 POLY-ALA. FT DOMAIN 83 91 POLY-ALA. FT DOMAIN 98 110 POLY-GLY. FT DOMAIN 228 231 POLY-GLY. FT DOMAIN 267 272 POLY-GLY. SQ SEQUENCE 453 AA; 46327 MW; E65D18E6FE4D9B28 CRC64; MAVSCPEVMY GAYYPYLYGR AGTSRSFYQY ERFNQDLYSS SGVNLAASSS ASGSSHSPCS PILPPSVSAN AAAAVAAAAH NSAAAAVAVA ANQASSSGGI GGGGLGGLGG LGGGPASGLL GSNVVPGSSS VGSVGLGMSP VLSGAAGHSL HSSHRTHAHS LAHAHTHPHS HTHTHTHQTK EEDLIVPRSE AEARLVGSQQ HQHHNESSCS SGPDSPRHAH SHSHPLHGGG GATGGPSSAG GTGSGGGDGG GTGAIPKNLP ALETPMGSGG GGLAGSGQGQ AQYLSASCVV FTNYSGDTAS QVDEHFSRAL NYNNKDSKES SSPMSNRNFP PSFWNSNYVH PIPAPTHHQV SDLYGTATDT GYATDPWVPH AAHYGSYAHA AHAHAAHAHA YHHNMAQYGS LLRLPQQYAS HGSRLHHDQQ TAHALEYSSY PTMAGLEAQV AQVQESSKDL YWF // ID VIT1_DROME STANDARD; PRT; 439 AA. AC P02843; Q9W2Y9; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vitellogenin I precursor (Yolk protein 1). GN YP1 OR CG2985. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82105554; PubMed=6275360; RA Hung M.-C., Wensink P.C.; RT "The sequence of the Drosophila melanogaster gene for yolk protein RT 1."; RL Nucleic Acids Res. 9:6407-6419(1981). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=82059495; PubMed=6272212; RA Hovemann B., Galler R., Walldorf U., Kupper H., Bautz E.K.F.; RT "Vitellogenin in Drosophila melanogaster: sequence of the yolk RT protein I gene and its flanking regions."; RL Nucleic Acids Res. 9:4721-4734(1981). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 1-54 FROM N.A. RX MEDLINE=82221407; PubMed=6806773; RA Hovemann B., Galler R.; RT "Vitellogenin in Drosophila melanogaster: a comparison of the YPI and RT YPII genes and their transcription products."; RL Nucleic Acids Res. 10:2261-2274(1982). CC -!- FUNCTION: VITELLOGENIN IS THE MAJOR YOLK PROTEIN OF EGGS WHERE CC IT IS USED AS A FOOD SOURCE DURING EMBRYOGENESIS. CC -!- TISSUE SPECIFICITY: SYNTHESIZED IN THE FAT BODY AND OVARIAN CC FOLLICLE CELLS AND ACCUMULATE IN THE OOCYTE. CC -!- INDUCTION: BY BETA-ECDYSONE; IN MALES. CC -!- SIMILARITY: PARTIAL, TO LIPASES. STRONG TO OTHER VITTELOGENINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00248; CAA23502.1; -. DR EMBL; X01524; CAA25709.1; -. DR EMBL; AE003449; AAF46548.1; -. DR PIR; A93744; VJFF1. DR FlyBase; FBgn0004045; Yp1. DR GO; GO:0007548; P:sex differentiation; NAS. DR InterPro; IPR000734; Lipase. DR Pfam; PF00151; lipase; 1. KW Yolk; Signal. FT SIGNAL 1 20 FT CHAIN 21 439 VITELLOGENIN I. SQ SEQUENCE 439 AA; 48711 MW; DF8A02080D69C522 CRC64; MNPMRVLSLL ACLAVAALAK PNGRMDNSVN QALKPSQWLS GSQLEAIPAL DDFTIERLEN MNLERGAELL QQVYHLSQIH HNVEPNYVPS GIQVYVPKPN GDKTVAPLNE MIQRLKQKQN FGEDEVTIIV TGLPQTSETV KKATRKLVQA YMQRYNLQQQ RQHGKNGNQD YQDQSNEQRK NQRTSSEEDY SEEVKNAKTQ SGDIIVIDLG SKLNTYERYA MLDIEKTGAK IGKWIVQMVN ELDMPFDTIH LIGQNVGAHV AGAAAQEFTR LTGHKLRRVT GLDPSKIVAK SKNTLTGLAR GDAEFVDAIH TSVYGMGTPI RSGDVDFYPN GPAAGVPGAS NVVEAAMRAT RYFAESVRPG NERSFPAVPA NSLQQYKQND GFGKRAYMGI DTAHDLEGDY ILQVNPKSPF GRNAPAQKQS SYHGVHQAWN TNQDSKDYQ // ID VIT2_DROME STANDARD; PRT; 442 AA. AC P02844; Q9W2Z0; DT 21-JUL-1986 (Rel. 01, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vitellogenin II precursor (Yolk protein 2). GN YP2 OR CG2979. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=83189120; PubMed=6405043; RA Hung M.-C., Wensink P.C.; RT "Sequence and structure conservation in yolk proteins and their RT genes."; RL J. Mol. Biol. 164:481-492(1983). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP SEQUENCE OF 1-59 FROM N.A. RX MEDLINE=82221407; PubMed=6806773; RA Hovemann B., Galler R.; RT "Vitellogenin in Drosophila melanogaster: a comparison of the YPI and RT YPII genes and their transcription products."; RL Nucleic Acids Res. 10:2261-2274(1982). RN [5] RP SEQUENCE OF 168-176, AND SULFATION. RX MEDLINE=89008370; PubMed=3139663; RA Baeuerle P.A., Lottspeich F., Huttner W.B.; RT "Purification of yolk protein 2 of Drosophila melanogaster and RT identification of its site of tyrosine sulfation."; RL J. Biol. Chem. 263:14925-14929(1988). CC -!- FUNCTION: VITELLOGENIN IS THE MAJOR YOLK PROTEIN OF EGGS WHERE IT CC IS USED AS A FOOD SOURCE DURING EMBRYOGENESIS. CC -!- TISSUE SPECIFICITY: SYNTHESIZED IN THE FAT BODY AND OVARIAN CC FOLLICLE CELLS AND ACCUMULATE IN THE OOCYTE. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING LATE PUPAL DEVELOPMENT AND CC IN ADULT FEMALES BETWEEN DAYS 1-3. CC -!- INDUCTION: BY BETA-ECDYSONE; IN MALES. CC -!- SIMILARITY: PARTIAL, TO LIPASES. STRONG TO OTHER VITTELOGENINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003449; AAF46547.1; -. DR EMBL; AY061042; AAL28590.1; -. DR EMBL; X01524; CAA25710.1; -. DR PIR; A03333; VJFF2. DR FlyBase; FBgn0005391; Yp2. DR GO; GO:0007548; P:sex differentiation; NAS. DR InterPro; IPR000734; Lipase. DR Pfam; PF00151; lipase; 1. KW Yolk; Signal; Sulfation. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 442 VITELLOGENIN II. FT MOD_RES 172 172 SULFATION. FT CONFLICT 68 68 L -> M (IN REF. 1). SQ SEQUENCE 442 AA; 49660 MW; 7DBD384E37E84F14 CRC64; MNPLRTLCVM ACLLAVAMGN PQSGNRSGRR SNSLDNVEQP SNWVNPREVE ELPNLKEVTL KKLQEMSLEE GATLLDKLYH LSQFNHVFKP DYTPEPSQIR GYIVGERGQK IEFNLNTLVE KVKRQQKFGD DEVTIFIQGL PETNTQVQKA TRKLVQAYQQ RYNLQPYETT DYSNEEQSQR SSSEEQQTQR RKQNGEQDDT KTGDLIVIQL GNAIEDFEQY ATLNIERLGE IIGNRLVELT NTVNVPQEII HLIGSGPAAH VAGVAGRQFT RQTGHKLRRI TALDPTKIYG KPEERLTGLA RGDADFVDAI HTSAYGMGTS QRLANVDFFP NGPSTGVPGA DNVVEATMRA TRYFAESVRP GNERNFPSVA ASSYQEYKQN KGYGKRGYMG IATDFDLQGD YILQVNSKSP FGRSTPAQKQ TGYHQVHQPW RQSSSNQGSR RQ // ID VIT3_DROME STANDARD; PRT; 420 AA. AC P06607; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Vitellogenin III precursor (Yolk protein 3). GN YP3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=87305580; PubMed=3114046; RA Garabedian M.J., Shirras A.D., Bownes M., Wensink P.C.; RT "The nucleotide sequence of the gene coding for Drosophila RT melanogaster yolk protein 3."; RL Gene 55:1-8(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87146365; PubMed=3029679; RA Yan Y.L., Kunert C.J., Postlethwait J.H.; RT "Sequence homologies among the three yolk polypeptide (Yp) genes in RT Drosophila melanogaster."; RL Nucleic Acids Res. 15:67-85(1987). RN [3] RP SEQUENCE FROM N.A. (MUTANT YP3S1). RX MEDLINE=91360094; PubMed=1909425; RA Liddell S., Bownes M.; RT "Characterization, molecular cloning and sequencing of YP3s1, a RT fertile yolk protein 3 mutant in Drosophila."; RL Mol. Gen. Genet. 228:81-88(1991). CC -!- FUNCTION: VITELLOGENIN IS THE MAJOR YOLK PROTEIN OF EGGS WHERE IT CC IS USED AS A FOOD SOURCE DURING EMBRYOGENESIS. CC -!- TISSUE SPECIFICITY: SYNTHESIZED IN THE FAT BODY AND OVARIAN CC FOLLICLE CELLS AND ACCUMULATE IN THE OOCYTE. CC -!- INDUCTION: BY BETA-ECDYSONE; IN MALES. CC -!- MISCELLANEOUS: THE MUTANT YP3-S1 IS SYNTHESIZED IN THE FAT BODY, CC BUT NOT SECRETED, PROBABLY DUE TO THE AMINO ACID MUTATION IN THE CC SIGNAL PEPTIDE. CC -!- SIMILARITY: PARTIAL, TO LIPASES. STRONG TO OTHER VITTELOGENINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M15898; AAA29024.1; -. DR EMBL; X04754; CAA28451.1; -. DR PIR; A25876; A25876. DR FlyBase; FBgn0004047; Yp3. DR GO; GO:0007548; P:sex differentiation; NAS. DR InterPro; IPR000734; Lipase. DR Pfam; PF00151; lipase; 1. KW Yolk; Signal. FT SIGNAL 1 19 FT CHAIN 20 420 VITELLOGENIN III. FT VARIANT 10 10 A -> D (IN MUTANT YP3S1). SQ SEQUENCE 420 AA; 46101 MW; 5457C49CAC933B26 CRC64; MMSLRICLLA TCLLVAAHAS KDASNDRLKP TKWLTATELE NVPSLNDITW ERLENQPLEQ GAKVIEKIYH VGQIKHDLTP SFVPSPSNVP VWIIKSNGQK VECKLNNYVE TAKAQPGFGE DEVTIVLTGL PKTSPAQQKA MRRLIQAYVQ KYNLQQLQKN AQEQQQQLKS SDYDYTSSEE AADQWKSAKA ASGDLIIIDL GSTLTNFKRY AMLDVLNTGA MIGQTLIDLT NKGVPQEIIH LIGQGISAHV AGAAGNKYTA QTGHKLRRIT GLDPAKVLSK RPQILGGLSR GDADFVDAIH TSTFAMGTPI RCGDVDFYPN GPSTGVPGSE NVIEAVARAT RYFAESVRPG SERNFPAVPA NSLKQYKEQD GFGKRAYMGL QIDYDLRGDY ILEVNAKSPF GQRSPAHKQA AYHGMHHAQN // ID VNL1_DROME STANDARD; PRT; 558 AA. AC Q9NFP1; Q9W431; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vanin-like protein 1 precursor. GN CG32754/CG3648. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99432008; PubMed=10501839; RA Granjeaud S., Naquet P., Galland F.; RT "An ESTs description of the new Vanin gene family conserved from fly RT to human."; RL Immunogenetics 49:964-972(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: PROBABLE HYDROLASE. CC -!- TISSUE SPECIFICITY: EXPRESSED IN LARVAE AND EARLY PUPAE. CC -!- SIMILARITY: BELONGS TO THE CN HYDROLASE FAMILY. BTD/VNN SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 CN HYDROLASE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ276261; CAB77020.1; -. DR EMBL; AE003436; AAN09161.1; -. DR EMBL; AY052034; AAK93458.1; -. DR FlyBase; FBgn0040069; vanin-like. DR GO; GO:0019898; C:extrinsic to membrane; NAS. DR GO; GO:0016787; F:hydrolase activity; NAS. DR InterPro; IPR003010; Ntlse/CNhydtse. DR Pfam; PF00795; CN_hydrolase; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. KW Hydrolase; Signal; Glycoprotein. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 558 VANIN-LIKE PROTEIN 1. FT DOMAIN 33 344 CN HYDROLASE. FT CARBOHYD 65 65 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 103 103 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 120 120 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 128 128 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 180 180 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 354 354 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 379 379 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 558 AA; 62341 MW; 7920621923BB7779 CRC64; MSNTWWWLSV VLLILGLMPG MSQQAALAES DYYTAGVVEF KQSILSLSAW SDSLAGYVEI INSENASATD IIVFPESTLN SAGSTTFVPN PEDQINPCLS DPNATYYEEF LVTLSCAARN ASKYIVINLT EKQKCEDIPE DTRPCASNGL NVFNTNVVFD RQGVVVSRYR KVHLYGEAKN STFLPELITF ETDFGVTFGH FICFDILFYT PAHQLIVEQG ITDFVYPAMW FSQLPFLTAV QTQQGWAYAN DVNLLASGAS RPSIGNSGSG IYHGRSGTLT SVMRQDSGER AIYVAQVPKY TRSRSLKKRA KRSLQEIQTR QVASSSSFYM KRDYVENYES ELLKLDEGTS GAINRTICQG SFCCNFDIAW RSLGTATENG SYYSYRLGTY DGWRNENNVD ANYIRNCALF TCSGDSIDDC GKLLPTEGEL QQSRVTFTRL AIGVTYPESR EFLLFPDTLQ DSLLPLEPSQ FEWSQRKPTE DSYVQEVRFA LKETQELSNL LTFGIYGNYY DNECTFGVGT EEEQLACGYR SGSPGLRILG GWLAMPLIIL AIARTMSS // ID VP28_DROME STANDARD; PRT; 210 AA. AC Q9V359; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE VPS28 protein homolog. GN VPS28 OR L(2)K16503 OR CG12770. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- SIMILARITY: BELONGS TO THE VPS28 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003838; AAF59143.1; -. DR EMBL; AY060620; AAL28168.1; -. DR FlyBase; FBgn0021814; Vps28. DR InterPro; IPR007143; VPS28. DR Pfam; PF03997; VPS28; 1. KW Hypothetical protein; Transport; Protein transport. SQ SEQUENCE 210 AA; 24512 MW; 843DB9820ADE9D96 CRC64; MQEQSPELYE EVKLFRNARE REKYDNMADL YAIINTIQQL EKAYIRDCIT PQEYTAACSK YLVQYKVAFK QVQCDEFPSV ETFVKKFRLD CPAALERIRE DRPITIRDDK GNTSKCIAEI VSLFITIMDK LRLQINTMDA LQPDVKDLAD NMNRLSLIPE DFDAKLKVEK WLGSLNEMQA SDELSEGQVR QFLFDLESAY ADFNKLLHSQ // ID VTU1_DROME STANDARD; PRT; 141 AA. AC P11449; Q9VMK4; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vitelline membrane protein Vm26Aa precursor (Protein TU-2) (Protein DE SV17.5). GN VM26AA OR VM26A.1 OR CG9048. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88055846; PubMed=3119397; RA Burke T., Waring G.L., Popodi E., Minoo P.; RT "Characterization and sequence of follicle cell genes selectively RT expressed during vitelline membrane formation in Drosophila."; RL Dev. Biol. 124:441-450(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94123988; PubMed=8293994; RA Scherer L.J., Harris D.H., White M.K., Steel L.S., Jin J., RA Petri W.H.; RT "Comparative analysis of the sequence and structure of two Drosophila RT melanogaster genes encoding vitelline membrane proteins."; RL Gene 136:121-127(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 71-108 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=89065296; PubMed=3143615; RA Scherer L.J., Harris D.H., Petri W.H.; RT "Drosophila vitelline membrane genes contain a 114 base pair region RT of highly conserved coding sequence."; RL Dev. Biol. 130:786-788(1988). CC -!- FUNCTION: MAJOR EARLY EGGSHELL PROTEIN. CC -!- TISSUE SPECIFICITY: FOLLICLE CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING VITELLINE MEMBRANE CC BIOSYNTHESIS. CC -!- SIMILARITY: A 38 AMINO ACIDS REGION (VM DOMAIN) IS CONSERVED IN CC DROSOPHILA VITELLINE MEMBRANE PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18280; AAA29015.1; -. DR EMBL; L08788; AAC37191.1; -. DR EMBL; AE003612; AAF52310.1; -. DR EMBL; M22699; AAA29017.1; -. DR PIR; A27249; A27249. DR FlyBase; FBgn0003979; Vm26Aa. DR GO; GO:0007292; P:female gamete generation; IMP. KW Signal; Structural protein; Eggshell. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 141 VITELLINE MEMBRANE PROTEIN VM26AA. FT DOMAIN 71 108 VM DOMAIN. FT CONFLICT 21 24 TNVA -> PTWP (IN REF. 2). SQ SEQUENCE 141 AA; 14321 MW; B9F27FB516EEDBDA CRC64; MKSFVCIALV AFAAAALASP TNVASATGST GSSVTTQDGE LEGVTGQGFG DLTRLRKSAY GGSSGGYGGS SIPAPPCPKN YLFSCQPNLA PVPCSAPAPS YGSAGAYSSP VATYVAPNYG VPQHQQQLYS AYVPQTYGYQ Y // ID VTU2_DROME STANDARD; PRT; 168 AA. AC P13238; Q9VMK6; DT 01-JAN-1990 (Rel. 13, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Vitelline membrane protein Vm26Ab precursor (Protein TU-4) (Protein DE SV23). GN VM26AB OR CG9046. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX MEDLINE=88242923; PubMed=3132408; RA Popodi E., Minoo P., Burke T., Waring G.L.; RT "Organization and expression of a second chromosome follicle cell RT gene cluster in Drosophila."; RL Dev. Biol. 127:248-256(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAJOR EARLY EGGSHELL PROTEIN. CC -!- TISSUE SPECIFICITY: FOLLICLE CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING VITELLINE MEMBRANE CC BIOSYNTHESIS. CC -!- DOMAIN: THE TETRAPEPTIDE (A-A-P-[AV]) REPEATS FOUND THROUGHOUT THE CC PROTEIN ARE ALSO PRESENT IN MANY PROTEINS CONSTITUTING THE CC PROTECTIVE ENVELOPE OF OTHER SPECIES. CC -!- SIMILARITY: A 38 AMINO ACIDS REGION (VM DOMAIN) IS CONSERVED IN CC DROSOPHILA VITELLINE MEMBRANE PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M20936; AAA28984.1; -. DR EMBL; AE003612; AAF52308.1; -. DR PIR; A45943; A45943. DR FlyBase; FBgn0003980; Vm26Ab. DR GO; GO:0007304; P:eggshell formation (sensu Insecta); IMP. KW Signal; Structural protein; Eggshell; Repeat. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 168 VITELLINE MEMBRANE PROTEIN VM26AB. FT DOMAIN 52 119 8 X 8 AA APPROXIMATE REPEATS OF Y-S-A-P- FT A-A-P-A. FT REPEAT 52 60 1 (APPROXIMATE). FT REPEAT 61 68 2. FT REPEAT 72 79 3. FT REPEAT 80 87 4. FT REPEAT 88 95 5. FT REPEAT 96 103 6. FT REPEAT 104 111 7. FT REPEAT 112 119 8 (APPROXIMATE). FT DOMAIN 117 154 VM DOMAIN. FT CONFLICT 140 140 C -> L (IN REF. 1). SQ SEQUENCE 168 AA; 16771 MW; FA6B6DF4F7AB9E2F CRC64; MAFNFGHLLI AGLVALSAVS SETIQLQPTQ GILIPAPLAE NIRVSRAAYG GYGAAPAAPS YSAPAAPAAQ AYSAPAAPAY SAPAAPAYSA PAAPAYSAPA APAYSAPAAP AYSAPASIPS PPCPKNYLFS CQPSLQPVPC SAPAQSYGSA GAYSQYVPQY AVPFVREL // ID VTU3_DROME STANDARD; PRT; 119 AA. AC Q06521; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Vitelline membrane protein Vm34Ca precursor. GN VM34CA OR VM34C.1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94123988; PubMed=8293994; RA Scherer L.J., Harris D.H., White M.K., Steel L.S., Jin J., RA Petri W.H.; RT "Comparative analysis of the sequence and structure of two Drosophila RT melanogaster genes encoding vitelline membrane proteins."; RL Gene 136:121-127(1993). RN [2] RP SEQUENCE OF 1-96 FROM N.A. RC STRAIN=Daekwanryeong; RX MEDLINE=85257433; PubMed=3926479; RA Mindrinos M.N., Scherer L.J., Garcini F.J., Kwan H., Jacobs K.A., RA Petri W.H.; RT "Isolation and chromosomal location of putative vitelline membrane RT genes in Drosophila melanogaster."; RL EMBO J. 4:147-153(1985). RN [3] RP SEQUENCE OF 69-106 FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=89065296; PubMed=3143615; RA Scherer L.J., Harris D.H., Petri W.H.; RT "Drosophila vitelline membrane genes contain a 114 base pair region RT of highly conserved coding sequence."; RL Dev. Biol. 130:786-788(1988). CC -!- FUNCTION: MAJOR EARLY EGGSHELL PROTEIN. CC -!- TISSUE SPECIFICITY: FOLLICLE CELLS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING VITELLINE MEMBRANE CC BIOSYNTHESIS. CC -!- SIMILARITY: A 38 AMINO ACIDS REGION (VM DOMAIN) IS CONSERVED IN CC DROSOPHILA VITELLINE MEMBRANE PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08852; AAC37200.1; -. DR EMBL; X01802; CAA25933.1; -. DR EMBL; M22700; AAA29018.1; -. DR FlyBase; FBgn0003983; Vm34Ca. KW Signal; Structural protein; Eggshell. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 119 VITELLINE MEMBRANE PROTEIN VM34CA. FT DOMAIN 69 106 VM DOMAIN. FT CONFLICT 96 96 A -> R (IN REF. 2). SQ SEQUENCE 119 AA; 11934 MW; 2F06298E52005BFC CRC64; MKCIAIVSTI CLLAAFVAAD KEDKMLGSSY GGGYGKPAAA PAPSYSAPAA ASPGLRAPAA PSYAAAPVSI PAPPCPKNYL FSCQPNLAPV PCSAPAPSYG SAGAYSQYAP VYAPQPIQW // ID WDS_DROME STANDARD; PRT; 361 AA. AC Q9V3J8; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Will die slowly protein. GN WDS OR EG:BACR25B3.7 OR CG17437. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RA Hollmann M., Simmerl E., Schaefer U., Schaefer M.A.; RT "The Drosophila melanogaster gene wds (will die slowly) codes for a RT WD-repeat protein with seven repeats."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SIMILARITY: CONTAINS 7 WD REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF233288; AAF43418.1; -. DR EMBL; AL138972; CAB72292.1; -. DR EMBL; AE003424; AAF45791.1; -. DR FlyBase; FBgn0040066; wds. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 4. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 4. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Repeat; WD repeat. FT REPEAT 62 100 WD 1. FT REPEAT 104 142 WD 2. FT REPEAT 146 184 WD 3. FT REPEAT 188 226 WD 4. FT REPEAT 230 269 WD 5. FT REPEAT 273 314 WD 6. FT REPEAT 318 358 WD 7. SQ SEQUENCE 361 AA; 39041 MW; B2A64127F1E0292D CRC64; MVPIGAVHGG HPGVVHPPQQ PLPTAPSGPN SLQPNSVGQP GATTSSNSSA SNKSSLSVKP NYTLKFTLAG HTKAVSAVKF SPNGEWLASS SADKLIKIWG AYDGKFEKTI SGHKLGISDV AWSSDSRLLV SGSDDKTLKV WELSTGKSLK TLKGHSNYVF CCNFNPQSNL IVSGSFDESV RIWDVRTGKC LKTLPAHSDP VSAVHFNRDG SLIVSSSYDG LCRIWDTASG QCLKTLIDDD NPPVSFVKFS PNGKYILAAT LDNTLKLWDY SKGKCLKTYT GHKNEKYCIF ANFSVTGGKW IVSGSEDNMV YIWNLQSKEV VQKLQGHTDT VLCTACHPTE NIIASAALEN DKTIKLWKSD T // ID WEE1_DROME STANDARD; PRT; 609 AA. AC P54350; Q9VM70; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Wee1-like protein kinase (EC 2.7.1.112). GN WEE OR CG4488. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96117048; PubMed=8573790; RA Campbell S.D., Sprenger F., Edgar B.A., O'Farrell P.H.; RT "Drosophila Wee1 kinase rescues fission yeast from mitotic RT catastrophe and phosphorylates Drosophila Cdc2 in vitro."; RL Mol. Biol. Cell 6:1333-1347(1995). RN [2] RP REVISIONS TO C-TERMINUS. RA Campbell S.D.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COULD ACT AS A NEGATIVE REGULATOR OF ENTRY INTO MITOSIS CC (G2 TO M TRANSITION). THIS KINASE SPECIFICALLY PHOSPHORYLATES AND CC INACTIVATES CYCLIN B1-COMPLEXED CDC2. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- ENZYME REGULATION: NEGATIVELY REGULATED BY PHOSPHORYLATION IN CC THE M-PHASE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- PTM: PHOSPHORYLATED DURING M AND G1 PHASES (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC WEE1 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17223; AAC46913.2; -. DR EMBL; AE003615; AAF52453.2; -. DR FlyBase; FBgn0011737; wee. DR GO; GO:0004713; F:protein-tyrosine kinase activity; IDA. DR GO; GO:0007093; P:mitotic checkpoint; IPI. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Mitosis; Transferase; Tyrosine-protein kinase; ATP-binding; KW Phosphorylation; Nuclear protein. FT DOMAIN 122 126 POLY-ALA. FT DOMAIN 239 517 PROTEIN KINASE. FT NP_BIND 245 253 ATP (BY SIMILARITY). FT BINDING 268 268 ATP (BY SIMILARITY). FT ACT_SITE 361 361 BY SIMILARITY. FT CONFLICT 35 36 KL -> NV (IN REF. 1). FT CONFLICT 72 72 D -> G (IN REF. 1). FT CONFLICT 275 275 A -> R (IN REF. 1). FT CONFLICT 567 567 N -> K (IN REF. 1). SQ SEQUENCE 609 AA; 68808 MW; 7E371EFDA2A5CD96 CRC64; MAFRQSEHEM SVTSLDSSVE LRSRSPSPQV FNPRKLRFAD DDFDKDTPEG ASPQHPLQQR PKLSSGEEQQ LDSKIGKEGG DGDVSMSPPC QKVRALRLFS TPATPKTILQ KSTTQCSNHL SAAAAAVNAS RRSDDLFRLS ERPRSLPLHN RKLPTQDTAN VNPFTPDSLM AHNKKRCRTQ FGRENLNLNV NAMQKYLLSD ACDDDVTEEA GDSMREIHQQ APKRLALHDT NISRFKREFM QVNVIGVGEF GVVFQCVNRL DGCIYAIKKS KKPVAGSSFE KRALNEVWAH AVLGKHDNVV RYYSAWAEDD HMLIQNEFCD GGSLHARIQD HCLGEAELKI VLMHVIEGLR YIHSNDLVHM DLKPENIFST MNPNAHKLVE VQPQQTKDDD GMDSVYEELR HSENLVTYKI GDLGHVTSVK EPYVEEGDCR YLPKEILHED YSNLFKADIF SLGITLFEAA GGGPLPKNGP EWHNLRDGKV PILPSLSRDF NELIAQMMHP YPDKRPTSQS IFSHPILSAV DSKSKLQLGL ELTVEKRKNE ILMNKLREAK KQIKLLEQRV NLLAVTNNPD SLDGQRCLRS FTRRMRTPFS SHGKFDSISD RNKNVITNI // ID WHIT_DROME STANDARD; PRT; 687 AA. AC P10090; Q9V3A2; Q9XY33; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE White protein. GN W OR EG:BACN33B1.1 OR CG2759. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Head; RX MEDLINE=90221897; PubMed=2109311; RA Pepling M., Mount S.M.; RT "Sequence of a cDNA from the Drosophila melanogaster white gene."; RL Nucleic Acids Res. 18:1633-1633(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85134865; PubMed=6084717; RA O'Hare K., Murphy C., Levis R., Rubin G.M.; RT "DNA sequence of the white locus of Drosophila melanogaster."; RL J. Mol. Biol. 180:437-455(1984). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=21100348; PubMed=11156992; RA Lukacsovich T., Asztalos Z., Awano W., Baba K., Kondo S., Niwa S., RA Yamamoto D.; RT "Dual-tagging gene trap of novel genes in Drosophila melanogaster."; RL Genetics 157:727-742(2001). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [6] RP SEQUENCE OF 224-331 FROM N.A. RX MEDLINE=89339145; PubMed=2503416; RA Tearle R.G., Belote J.M., McKeown M., Baker B.S., Howells A.J.; RT "Cloning and characterization of the scarlet gene of Drosophila RT melanogaster."; RL Genetics 122:595-606(1989). CC -!- FUNCTION: PART OF A MEMBRANE-SPANNING PERMEASE SYSTEM NECESSARY CC FOR THE TRANSPORT OF PIGMENT PRECURSORS INTO PIGMENT CELLS CC RESPONSIBLE FOR EYE COLOR. WHITE DIMERIZE WITH BROWN FOR THE CC TRANSPORT OF GUANINE AND WITH SCARLET FOR THE TRANSPORT OF CC TRYPTOPHAN. CC -!- SUBUNIT: HETERODIMER OF WHITE WITH EITHER BROWN OR SCARLET. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51749; CAA36038.1; -. DR EMBL; X02974; CAA26716.1; -. DR EMBL; AB028139; BAA78210.1; -. DR EMBL; AE003425; AAF45826.1; -. DR EMBL; AL133506; CAB65847.1; -. DR EMBL; X76202; CAA53795.1; -. DR PIR; S08635; FYFFW. DR FlyBase; FBgn0003996; w. DR GO; GO:0004888; F:transmembrane receptor activity; NAS. DR GO; GO:0006727; P:ommochrome biosynthesis; IMP. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transporter. DR InterPro; IPR005284; Pigment_permease. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR00955; 3a01204; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. KW Pigment; ATP-binding; Transmembrane; Transport. FT NP_BIND 130 137 ATP (BY SIMILARITY). FT TRANSMEM 435 453 POTENTIAL. FT TRANSMEM 465 485 POTENTIAL. FT TRANSMEM 515 533 POTENTIAL. FT TRANSMEM 542 563 POTENTIAL. FT TRANSMEM 576 594 POTENTIAL. FT TRANSMEM 659 678 POTENTIAL. FT CONFLICT 25 29 GDSGA -> LIFEIPYHCRVTAD (IN REF. 2 AND FT 3). FT CONFLICT 49 49 L -> R (IN REF. 4 AND 5). FT CONFLICT 335 371 VGAQCPTNYNPADFYVQVLAVVPGREIESRDRIAKIC -> FT ITLHLNSYPAWVPSVLPTTIRRTFTYRCWPLCPDGRSSPVI FT GSPRYG (IN REF. 3). SQ SEQUENCE 687 AA; 75672 MW; 24AFAD799DE0D396 CRC64; MGQEDQELLI RGGSKHPSAE HLNNGDSGAA SQSCINQGFG QAKNYGTLLP PSPPEDSGSG SGQLAENLTY AWHNMDIFGA VNQPGSGWRQ LVNRTRGLFC NERHIPAPRK HLLKNVCGVA YPGELLAVMG SSGAGKTTLL NALAFRSPQG IQVSPSGMRL LNGQPVDAKE MQARCAYVQQ DDLFIGSLTA REHLIFQAMV RMPRHLTYRQ RVARVDQVIQ ELSLSKCQHT IIGVPGRVKG LSGGERKRLA FASEALTDPP LLICDEPTSG LDSFTAHSVV QVLKKLSQKG KTVILTIHQP SSELFELFDK ILLMAEGRVA FLGTPSEAVD FFSYVGAQCP TNYNPADFYV QVLAVVPGRE IESRDRIAKI CDNFAISKVA RDMEQLLATK NLEKPLEQPE NGYTYKATWF MQFRAVLWRS WLSVLKEPLL VKVRLIQTTM VAILIGLIFL GQQLTQVGVM NINGAIFLFL TNMTFQNVFA TINVFTSELP VFMREARSRL YRCDTYFLGK TIAELPLFLT VPLVFTAIAY PMIGLRAGVL HFFNCLALVT LVANVSTSFG YLISCASSST SMALSVGPPV IIPFLLFGGF FLNSGSVPVY LKWLSYLSWF RYANEGLLIN QWADVEPGEI SCTSSNTTCP SSGKVILETL NFSAADLPLD YVGLAILIVS FRVLAYLALR LRARRKE // ID WIBG_DROME STANDARD; PRT; 207 AA. AC P82804; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Within the bgcn gene intron protein. GN WIBG OR PYM OR CG30176/CG10330. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=20384590; PubMed=10924476; RA Ohlstein B., Lavoie C.A., Vef O., Gateff E., McKearin D.M.; RT "The Drosophila cystoblast differentiation factor, benign gonial cell RT neoplasm, is related to DExH-box proteins and interacts genetically RT with bag-of-marbles."; RL Genetics 155:1809-1819(2000). RN [2] RP SEQUENCE FROM N.A. RA Forler D., Izaurralde E.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF293388; AAG00610.1; -. DR EMBL; AJ459405; CAD30676.1; -. DR EMBL; AE003462; AAM68273.1; -. DR EMBL; AY070957; AAL48579.1; -. DR EMBL; AY071704; AAL49326.1; -. DR FlyBase; FBgn0034918; wibg. KW Coiled coil. FT DOMAIN 64 91 COILED COIL (POTENTIAL). FT DOMAIN 152 184 COILED COIL (POTENTIAL). SQ SEQUENCE 207 AA; 23450 MW; F7E6B7C98A2961DE CRC64; MSTYLQSSEG KFIPATKRPD GTWRKARRVK DGYVPQEEVP LYESKGKQFV AQRQAGVPPG MCPLLAAESK KEREKQERTR AKKQEKESGR QPKAPAPGVL VMPPSTCPPP KVSQQQQQQQ QQPSGSRDIN SISKTLEDTL KLDAAQEVVD PAKQLKKLRK KIREIEQIES RIQAGEQKKL DKDQLDKVKK KSEILRQIKD LESTPRS // ID WNT2_DROME STANDARD; PRT; 352 AA. AC P28465; Q86PC8; Q9V584; DT 01-DEC-1992 (Rel. 24, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Wnt-2 protein precursor (dWnt-2). GN WNT2 OR WNT-2 OR CG1916. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; TISSUE=Embryo; RX MEDLINE=93048811; PubMed=1425336; RA Russell J., Gennissen A., Nusse R.; RT "Isolation and expression of two novel Wnt/wingless gene homologues RT in Drosophila."; RL Development 115:475-482(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: LIGAND FOR MEMBERS OF THE FRIZZLED FAMILY OF SEVEN CC TRANSMEMBRANE RECEPTORS. MAY FUNCTION IN GONADOGENESIS. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE WNT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64735; CAA46001.1; -. DR EMBL; AE003833; AAF58933.1; -. DR EMBL; BT003204; AAO24959.1; -. DR PIR; S24559; S24559. DR FlyBase; FBgn0004360; Wnt2. DR GO; GO:0007517; P:muscle development; IMP. DR GO; GO:0007424; P:tracheal system development (sensu Insecta); IGI. DR InterPro; IPR005817; Wnt. DR InterPro; IPR005816; Wnt_grthfactor. DR Pfam; PF00110; wnt; 1. DR PRINTS; PR01349; WNTPROTEIN. DR SMART; SM00097; WNT1; 1. DR PROSITE; PS00246; WNT1; 1. KW Wnt signaling pathway; Developmental protein; Glycoprotein; Signal. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 352 WNT-2 PROTEIN. FT CARBOHYD 75 75 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 119 119 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 27 27 V -> A (IN REF. 1). FT CONFLICT 68 68 Q -> L (IN REF. 3). FT CONFLICT 110 110 A -> R (IN REF. 1). FT CONFLICT 226 226 L -> M (IN REF. 1). SQ SEQUENCE 352 AA; 39763 MW; C021663DB4CAC5DF CRC64; MWKIHNKLLI YILWIMEIRL VSSFTSVMLC GRIPGLTPGQ RNMCREMPDA LIALGEGHQL GAQECQHQFR GHRWNCSEVW QRNVFAHVIP TASREAAYTY AIASAGAAYA VTAACARGNI STCGCDVRHK ATPTGGGTPD EPWKWGGCSA DVDFGMRYAR RFMDARELER DSRTLMNLHN NRAGRTLVKK MLRTDCKCHG VSGSCVMKTC WKSLPPFRLV GDRLMLKYQK AKTVQAVKGK RGLRLVLSRK KHAGTARAQK PVLDWPKRME LIYLEASPNY CERSLQTGSQ GTSGRTCQRT GHGPQSCDLL CCGRGHNTQH IRRTTQCRCQ FRWCCEVKCD ECDESYEEFT CK // ID WNT4_DROME STANDARD; PRT; 539 AA. AC P40589; Q8MPQ1; Q8SWU3; Q9VM29; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE WNT-4 protein precursor (dWnt-4). GN WNT4 OR WNT-4 OR CG4698. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., REVISION TO 171, AND FUNCTION. RX MEDLINE=21966109; PubMed=11970894; RA Cohen E.D., Mariol M.-C., Wallace R.M.H., Weyers J., Kamberov Y.G., RA Pradel J., Wilder E.L.; RT "DWnt4 regulates cell movement and focal adhesion kinase during RT Drosophila ovarian morphogenesis."; RL Dev. Cell 2:437-448(2002). RN [2] RP SEQUENCE OF 151-539 FROM N.A. RX MEDLINE=95171909; PubMed=7867502; RA Graba Y., Gieseler K., Aragnol D., Laurenti P., Mariol M.-C., RA Berenger H., Sagnier T., Pradel J.; RT "DWnt-4, a novel Drosophila Wnt gene acts downstream of homeotic RT complex genes in the visceral mesoderm."; RL Development 121:209-218(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: LIGAND FOR MEMBERS OF THE FRIZZLED FAMILY OF SEVEN CC TRANSMEMBRANE RECEPTORS. ACTS DOWNSTREAM OF HOMEOTIC COMPLEX GENES CC IN THE VISCERAL MESODERM AND IS REQUIRED FOR EMBRYONIC CC SEGMENTATION. ALSO REQUIRED FOR CELL MOVEMENT AND FAK REGULATION CC DURING OVARIAN MORPHOGENESIS. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE WNT FAMILY. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO ERRONEOUS CC GENE MODEL PREDICTION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF533773; AAN04479.1; -. DR EMBL; AE003616; AAF52499.1; ALT_SEQ. DR EMBL; AY095078; AAM11406.1; -. DR FlyBase; FBgn0010453; Wnt4. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0004871; F:signal transducer activity; NAS. DR GO; GO:0016477; P:cell migration; IMP. DR GO; GO:0008585; P:female gonad development; IMP. DR GO; GO:0016055; P:Wnt receptor signaling pathway; NAS. DR InterPro; IPR005817; Wnt. DR InterPro; IPR005816; Wnt_grthfactor. DR Pfam; PF00110; wnt; 1. DR PRINTS; PR01349; WNTPROTEIN. DR SMART; SM00097; WNT1; 1. DR PROSITE; PS00246; WNT1; 1. KW Wnt signaling pathway; Developmental protein; Glycoprotein; Signal. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 539 WNT-4 PROTEIN. FT CARBOHYD 74 74 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 284 284 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 419 419 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 18 18 F -> L (IN REF. 1). FT CONFLICT 201 201 G -> R (IN REF. 1). FT CONFLICT 230 230 F -> L (IN REF. 4). FT CONFLICT 434 434 R -> A (IN REF. 1). FT CONFLICT 532 532 L -> V (IN REF. 1). SQ SEQUENCE 539 AA; 58685 MW; 6682C8B3D729D067 CRC64; MPSPTGVFVL MILTHLSFGL GQVRNEDQLL MVGQNGDLDS SNPAIHHQQH QQHQQHQQHQ QHQSNHNLNN GNMNSTILNT LMGNNAGQVV NSSPGGGGSM INQLGSSTSS VPSVIGGGVG SVGNPWHSAV GLGVPGNGMG LPSSHGLGGN MGSHPHGHAL AGLAKLGIIV PGGQGLPGNL GYGGTMLNGG GVGGAAGMGL GIGSNTNNMD MQQGLYNEHF ISEHTVMAVF TSQGQVGGPC RYMPATRRQN HQCRKETGLP GTLSEARRLA TTHCEEQFRY DRWNCSIETR GKRNIFKKLY KETAFVHALT AAAMTHSIAR ACAEGRMTKC SCGPKKHNRE AQDFQWGGCN DNLKHGKRVT RSFLDLRGGD GDEVSEILRH DSEVGIEAVS SQMMDKCKCH GVSGSCSMKT CWKKMADFNA TATLLRQKYN EAIRKAPNQR SMRQVSSSRM KKPKQRRKKP QQSQYTTLYY LETSPSYCAV TKDRQCLHPD NCGTLCCGRG YTTQVVKQVE KCRCRFNNGR CCQLICDYCQ RLENKYFCK // ID WNT5_DROME STANDARD; PRT; 1010 AA. AC P28466; Q01535; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Wnt-5 protein precursor (dWnt-5) (dWnt-3). GN WNT5 OR WNT-5 OR WNT-3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=93048811; PubMed=1425336; RA Russell J., Gennissen A., Nusse R.; RT "Isolation and expression of two novel Wnt/wingless gene homologues RT in Drosophila."; RL Development 115:475-482(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93050786; PubMed=1358729; RA Eisenberg L.M., Ingham P.W., Brown A.M.C.; RT "Cloning and characterization of a novel Drosophila Wnt gene, Dwnt-5, RT a putative downstream target of the homeobox gene distal-less."; RL Dev. Biol. 154:73-83(1992). CC -!- FUNCTION: LIGAND FOR MEMBERS OF THE FRIZZLED FAMILY OF SEVEN CC TRANSMEMBRANE RECEPTORS. PROBABLE DEVELOPMENTAL PROTEIN. MAY BE A CC SIGNALING MOLECULE WHICH AFFECTS THE DEVELOPMENT OF DISCRETE CC REGIONS OF TISSUES. IS LIKELY TO SIGNAL OVER ONLY FEW CELL CC DIAMETERS. MAY HAVE A ROLE IN THE CNS DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE WNT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64736; CAA46002.1; -. DR EMBL; M97450; AAA29020.1; -. DR PIR; A48821; A48821. DR FlyBase; FBgn0010194; Wnt5. DR InterPro; IPR005817; Wnt. DR InterPro; IPR005816; Wnt_grthfactor. DR Pfam; PF00110; wnt; 1. DR PRINTS; PR01349; WNTPROTEIN. DR SMART; SM00097; WNT1; 1. DR PROSITE; PS00246; WNT1; 1. KW Wnt signaling pathway; Developmental protein; Glycoprotein; Signal. FT SIGNAL 1 28 POTENTIAL. FT CHAIN 29 1010 WNT-5 PROTEIN. FT DOMAIN 280 288 POLY-GLY. FT DOMAIN 461 476 POLY-SER. FT CARBOHYD 60 60 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 66 66 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 115 115 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 219 219 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 310 310 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 344 344 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 425 425 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 490 490 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 491 491 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 534 534 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 599 599 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 730 730 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 958 958 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 281 283 MISSING (IN REF. 2). FT CONFLICT 320 320 E -> D (IN REF. 2). FT CONFLICT 474 476 MISSING (IN REF. 2). SQ SEQUENCE 1010 AA; 112875 MW; 3B388C0107430512 CRC64; MSCYRKRHFL LWLLRAVCML HLTARGAYAT VGLQGVPTWI YLGLKSPFIE FGNQVEQLAN SSIPLNMTKD EQANMHQEGL RKLGTFIKPV DLRDSETGFV KADLTKRLVF DRPNNITSRP IHPIQEEMDQ KQIILLDEDT DENGLPASLT DEDRKFIVPM ALKNISPDPR WAATTPSPSA LQPNAKAIST IVPSPLAQVE GDPTSNIDDL KKHILFLHNM TKTNSNFESK FVKFPSLQKD KAKTSGAGGS PPNPKRPQRP IHQYSAPIAP PTPKVPAPDG GGGGGVGGAA YNPGEQPIGG YYQNEELANN QSLLKPTDTE SHPAAGGSSH GQKNPSEPQV ILLNETLSTE TSIEADRSPS INQPKAGSPA RTTKRPPCLR NPESPKCIRQ RRREEQQRQR ERDEWFRGQS QYMQPRFEPI IQTINNTKRF AVSIEIPDSF KVSSEGSDGE LLSRVERSQP SISSSSSSSS SSSSSSRKIM PDYIKVSMEN NTSVTDYFKH DVVMTSADVA SDREFLIKNM EEHGGAGSAN GHHNDTTPTA DAYSETIDLN PNNCYSAIGL SNSQKKQCVK HTSVMPAISR GARAAIQECQ FQFKNRRWNC STTNDETVFG PMTSLAAPEM AFIHALAAAT VTSFIARACR DGQLASCSCS RGSRPKQLHD DWKWGGCGDN LEFAYKFATD FIDSREKETN RETRGVKRKR EEINKNRMHS DDTNAFNIGI KRNKNVDAKN DTSLVVRNVR KSTEAENSHI LNENFDQHLL ELEQRITKEI LTSKIDEEEM IKLQEKIKQE IVNTKFFKGE QQPRKKKRKN QRAAADAPAY PRNGIKESYK DGGILPRSTA TVKARSLMNL HNNEAGRRAV IKKARITCKC HGVSGSCSLI TCWQQLSSIR EIGDYLREKY EGATKVKINK RGRLQIKDLQ FKVPTAHDLI YLDESPDWCR NSYALHWPGT HGRVCHKNSS GLESCAILCC GRGYNTKNII VNERCNCKFH WCCQVKCEVC TKVLEEHTCK // ID WNTG_DROME STANDARD; PRT; 468 AA. AC P09615; Q27768; Q27769; Q9VM27; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein int-1 precursor (dInt-1) (Wingless protein). GN WG OR CG4889. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87273528; PubMed=3111720; RA Rijsewijk F., Schuermann M., Wagenaar E., Parren P., Weigel D., RA Nusse R.; RT "The Drosophila homolog of the mouse mammary oncogene int-1 is RT identical to the segment polarity gene wingless."; RL Cell 50:649-657(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88203634; PubMed=3129722; RA Uzvoelgyi E., Kiss I., Pitt A., Arsenian S., Ingvarsson S., RA Udvardy A., Hamada M., Klein G., Suemegi J.; RT "Drosophila homolog of the murine Int-1 protooncogene."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3034-3038(1988). RN [3] RP SEQUENCE FROM N.A., AND MUTANTS. RX MEDLINE=94085405; PubMed=8262072; RA van den Heuvel M., Harryman-Samos C., Klingensmith J., Perrimon N., RA Nusse R.; RT "Mutations in the segment polarity genes wingless and porcupine RT impair secretion of the wingless protein."; RL EMBO J. 12:5293-5302(1993). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SECRETION. RX MEDLINE=90058657; PubMed=2582493; RA van den Heuvel M., Nusse R., Johnston P., Lawrence P.A.; RT "Distribution of the wingless gene product in Drosophila embryos: a RT protein involved in cell-cell communication."; RL Cell 59:739-749(1989). RN [6] RP PHOSPHORYLATION OF ARM. RX MEDLINE=95113174; PubMed=7529201; RA Peifer M., Pai L.M., Casey M.; RT "Phosphorylation of the Drosophila adherens junction protein RT Armadillo: roles for wingless signal and zeste-white 3 kinase."; RL Dev. Biol. 166:543-556(1994). RN [7] RP INTERACTION WITH WG AND EN. RC TISSUE=Embryo; RX MEDLINE=93113685; PubMed=1335365; RA Siegfried E., Chou T.B., Perrimon N.; RT "wingless signaling acts through zeste-white 3, the Drosophila homolog RT of glycogen synthase kinase-3, to regulate engrailed and establish RT cell fate."; RL Cell 71:1167-1179(1992). CC -!- FUNCTION: SEGMENT POLARITY PROTEIN. BINDS TO THE FRIZZLED SEVEN- CC TRANSMEMBRANE RECEPTORS. THIS PROTEIN IS PROBABLY A GROWTH FACTOR. CC ACTS ON NEIGHBORING CELLS TO REGULATE AT LEAST ONE GENE, THE CC HOMEOBOX SEGMENTATION GENE ENGRAILED. WG SIGNAL REPRESSES ARM CC PHOSPHORYLATION. WG SIGNALING OPERATES BY INACTIVATING THE SGG CC REPRESSION OF ENGRAILED AUTOACTIVATION. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE WNT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17230; AAA28647.1; -. DR EMBL; J03650; AAA28646.1; -. DR EMBL; S67382; AAB29368.1; -. DR EMBL; S67383; AAB29369.1; -. DR EMBL; AE003617; AAF52501.1; -. DR PIR; A29650; A29650. DR FlyBase; FBgn0004009; wg. DR GO; GO:0005576; C:extracellular; NAS. DR GO; GO:0005110; F:frizzled-2 binding; IDA. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; NAS. DR GO; GO:0008544; P:epidermal differentiation; IMP. DR GO; GO:0007223; P:frizzled-2 signaling pathway; IDA. DR GO; GO:0007483; P:genital disc metamorphosis; NAS. DR GO; GO:0007442; P:hindgut morphogenesis; IMP. DR GO; GO:0007560; P:imaginal disc morphogenesis; NAS. DR GO; GO:0007523; P:larval visceral muscle development; IMP. DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; NAS. DR GO; GO:0042127; P:regulation of cell proliferation; NAS. DR GO; GO:0007367; P:segment polarity determination; NAS. DR GO; GO:0008587; P:wing margin morphogenesis; NAS. DR InterPro; IPR005817; Wnt. DR InterPro; IPR005816; Wnt_grthfactor. DR Pfam; PF00110; wnt; 1. DR PRINTS; PR01349; WNTPROTEIN. DR SMART; SM00097; WNT1; 1. DR PROSITE; PS00246; WNT1; 1. KW Wnt signaling pathway; Developmental protein; Glycoprotein; KW Segmentation polarity protein; Signal. FT SIGNAL 1 17 FT CHAIN 18 468 PROTEIN INT-1. FT CARBOHYD 103 103 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 108 108 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 414 414 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 104 104 C -> S (IN ALLELE WG-IL114). FT VARIANT 221 221 G -> D (IN ALLELE WG-IN67). FT CONFLICT 182 182 W -> C (IN REF. 2). FT CONFLICT 204 204 E -> D (IN REF. 2). FT CONFLICT 275 275 N -> T (IN REF. 2). FT CONFLICT 297 297 G -> A (IN REF. 2). FT CONFLICT 315 315 E -> EE (IN REF. 2). FT CONFLICT 364 364 K -> N (IN REF. 2). FT CONFLICT 391 391 E -> D (IN REF. 2). FT CONFLICT 441 441 E -> D (IN REF. 2). SQ SEQUENCE 468 AA; 51986 MW; F766972A731E6171 CRC64; MDISYIFVIC LMALCSGGSS LSQVEGKQKS GRGRGSMWWG IAKVGEPNNI TPIMYMDPAI HSTLRRKQRR LVRDNPGVLG ALVKGANLAI SECQHQFRNR RWNCSTRNFS RGKNLFGKIV DRGCRETSFI YAITSAAVTH SIARACSEGT IESCTCDYSH QSRSPQANHQ AGSVAGVRDW EWGGCSDNIG FGFKFSREFV DTGERGRNLR EKMNLHNNEA GRAHVQAEMR QECKCHGMSG SCTVKTCWMR LANFRVIGDN LKARFDGATR VQVTNSLRAT NALAPVSPNA AGSNSVGSNG LIIPQSGLVY GEEEERMLND HMPDILLENS HPISKIHHPN MPSPNSLPQA GQRGGRNGRR QGRKHNRYHF QLNPHNPEHK PPGSKDLVYL EPSPSFCEKN LRQGILGTHG RQCNETSLGV DGCGLMCCGR GYRRDEVVVV ERCACTFHWC CEVKCKLCRT KKVIYTCL // ID WSCK_DROME STANDARD; PRT; 809 AA. AC P83097; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative tyrosine-protein kinase Wsck precursor (EC 2.7.1.112). GN WSCK. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP CONCEPTUAL TRANSLATION. RA Manning G., Sudarsanam S., Plowman G.; RT "Prediction of novel protein kinases from the Drosophila genome RT project and EST sequences."; RL Unpublished observations (AUG-2001). CC -!- FUNCTION: PUTATIVE RECEPTOR WITH TYROSINE-PROTEIN KINASE ACTIVITY. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. CC -!- SIMILARITY: CONTAINS 1 FIBRONECTIN TYPE III DOMAIN. CC -!- SIMILARITY: CONTAINS 1 WSC DOMAIN. CC -!- CAUTION: THIS IS A CONCEPTUAL TRANSLATION; A FRAMESHIFT HAD TO CC BE INTRODUCED IN POSITION 382 TO PRODUCE THIS ORF. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003748; -; NOT_ANNOTATED_CDS. DR FlyBase; FBgn0046685; Wsck. DR InterPro; IPR003961; FN_III. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR InterPro; IPR002889; WSC. DR Pfam; PF00041; fn3; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF01822; WSC; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00060; FN3; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; FALSE_NEG. KW Hypothetical protein; Receptor; Transferase; Tyrosine-protein kinase; KW ATP-binding; Transmembrane; Signal. FT SIGNAL 1 32 POTENTIAL. FT CHAIN 33 809 PUTATIVE TYROSINE-PROTEIN KINASE WSCK. FT TRANSMEM 420 440 POTENTIAL. FT DOMAIN 42 115 WSC. FT DOMAIN 129 233 FIBRONECTIN TYPE-III. FT DOMAIN 511 776 PROTEIN KINASE. FT NP_BIND 517 525 ATP (BY SIMILARITY). FT BINDING 529 529 ATP (BY SIMILARITY). FT ACT_SITE 644 644 BY SIMILARITY. FT CARBOHYD 139 139 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 217 217 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 329 329 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 550 550 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 809 AA; 90635 MW; 03CAD2DBF5C25A38 CRC64; MECGSHSGHR PIPIWLSSCL VAMCLGLPLG AAVPQEAPAY YYVGCYTART DLLHESVYAK TPQTCIEICE HQGHHYAVLA SEKCFCANVL EPQEQQDEQL CNTRCLANKA QYCGGVGVHS YYSTILTKQP GPHHLRISNK TENSLTLSWN AYEARKLLLA GGAEAVLPNQ LLDNFLIKAQ VLKTYSSLPA FPQPEFMVQS TETQFELTDL HPATLYNISV RAMCKDAQVG QSECGQASIE ATTEVGLPSP VPAQPKILSR TDRTVTIELS PIRNDNGPLS KLLVIVEYVD NALSQPFDAQ LLGSWQQAQQ DGVPYYIAAE LDYDRPEDNR TRRFVVGDGK RYGRFTNKPL DQPDAHVHIS LGLVSNALNS NEYLCNYLYS RXSTLEGVTK TMYSRGTHDQ HVTSLDDFSY ATFEKGQSSV VALAVTCVIF GSCLLLSLIA YFYLRYKTCR GRRLTGGNTH EMTLQTPIIE RENNGYLVED DPLPHSPENF KQQLQQLVEG YERIPRNALR LNVNDVIGDG RFGEIITGKV STNDFARDCT LHVLCLDDLN GTTQAQLLRE LRQLSQLKRQ EHLLDFYGVS ASPDWFYLIF EQQRMSLKRK LVESRLMAPS PRLTSLSEQL VLQWIYELAS AMNYLSSCQV VHRQLCSHSV FVTSDFKLKL SVFGPLPYMN IARQQPDHNR WLAPEVLRHQ HHHSTRSDVW SLACVAWECC ALGGTPYANA VASNQQLLEA IRAAVRPAQP AYVYGDLYQL LLNCWQLEPS ERSSCEDVAF GVRQLMTSPR HALSFDRVAG GLDTLPPYLP QLEAVATMG // ID WUN_DROME STANDARD; PRT; 379 AA. AC Q9V576; P91661; Q8MKU5; Q8WT60; Q9U9Y7; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative phosphatidate phosphatase (EC 3.1.3.4) (Phosphatidic acid DE phosphatase type 2) (Wunen protein) (Germ cell guidance factor). GN WUN OR CG8804. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM SHORT), FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=97138220; PubMed=8985246; RA Zhang N., Zhang J.P., Purcell K.J., Chen Y., Howard K.; RT "The Drosophila protein Wunen repels migrating germ cells."; RL Nature 385:64-67(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [5] RP SEQUENCE FROM N.A. (ISOFORM LONG). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP SEQUENCE OF 22-99 FROM N.A. RA Russell C., Bartos S., Phillips R.G., Whittle R.; RT "Efficient functional dissection of enhancer sequences in Drosophila: RT a novel P- and hobo-based construct acting as an enhancer-capture RT element."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RESPONSIBLE FOR GUIDING THE GERM CELLS EARLY IN THE CC PROCESS OF MIGRATION FROM THE LUMEN OF THE DEVELOPING GUT TOWARDS CC THE OVERLYING MESODERM, WHERE THE GERM CELLS ENTER THE GONADS. MAY CC BE INVOLVED IN LIPID METABOLISM. CC -!- CATALYTIC ACTIVITY: A 3-SN-PHOSPHATIDATE + H(2)O = A 1,2-DIACYL- CC SN-GLYCEROL + PHOSPHATE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9V576-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q9V576-2; Sequence=VSP_005084; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: EXPRESSED IN EMBRYONIC GUT IN A PATTERN THAT CC GUIDES GERM CELLS TOWARDS MESODERM (INITIALLY IN HINDGUT AND THEN CC ON LOWER SIDE OF GUT). DURING EXTENDED GERM BAND STAGE, EXPRESSED CC IN ECTODERM AS A MEDIAL BAND THROUGHOUT THE TRUNK. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATIDATE PHOSPHATASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U73822; AAC47449.1; -. DR EMBL; AE003833; AAF58942.2; -. DR EMBL; AE003833; AAM71066.1; -. DR EMBL; AF145595; AAD38570.1; -. DR EMBL; BT001729; AAN71484.1; -. DR EMBL; AY046533; AAL34392.1; -. DR FlyBase; FBgn0016078; wun. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0008195; F:phosphatidate phosphatase activity; NAS. DR GO; GO:0016311; P:dephosphorylation; NAS. DR GO; GO:0008354; P:germ-cell migration; IEP. DR InterPro; IPR008934; AcPase_VanPerase. DR InterPro; IPR000326; PA_PTPase. DR Pfam; PF01569; PAP2; 1. DR SMART; SM00014; acidPPc; 1. KW Hydrolase; Developmental protein; Glycoprotein; Transmembrane; KW Alternative splicing. FT TRANSMEM 90 110 POTENTIAL. FT TRANSMEM 138 158 POTENTIAL. FT TRANSMEM 266 286 POTENTIAL. FT TRANSMEM 330 350 POTENTIAL. FT CARBOHYD 51 51 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 169 169 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 79 Missing (in isoform Short). FT /FTId=VSP_005084. FT CONFLICT 152 152 F -> L (IN REF. 4). FT CONFLICT 360 360 A -> G (IN REF. 4). SQ SEQUENCE 379 AA; 42789 MW; AD3C4F06B3DD9ADA CRC64; MPAVKIIMST ETSASETTPL RRSENETPDH KELAQSNSNS RQTTVNSNNN NYSNSVQVRL QEQDRDSDSE QQQHTATITM DTNKRILCRV GLDVLILLCA GFPILLFFLL GEPYKRGFFC DDESLKHPFH DSTVRNWMLY FIGAVIPVGV IFIVEVIISQ NKAKQDNGNA TSRRYVFMNY ELPDWMIECY KKIGIYAFGA VLSQLTTDIA KYSIGRLRPH FIAVCQPQMA DGSTCDDAIN AGKYIQEFTC KGVGSSARML KEMRLSFPSG HSSFTFFAMV YLALYLQARM TWRGSKLLRH LLQFLFIMVA WYTALSRVSD YKHHWSDVLA GSLIGSISAL VVANYVSDLF QKPNTKPYLA RTVQDMNASP AQAITITTN // ID XDH_DROME STANDARD; PRT; 1335 AA. AC P10351; Q8SXC4; Q9VFZ9; DT 01-MAR-1989 (Rel. 10, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Xanthine dehydrogenase (EC 1.1.1.204) (XD) (Rosy locus protein). GN RY OR XDH OR CG7642. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE OF 1-231 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=87248039; PubMed=3036645; RA Lee C.S., Curtis D., Gray M., Bender W.; RT "Mutations affecting expression of the rosy locus in Drosophila RT melanogaster."; RL Genetics 116:55-66(1987). RN [2] RP SEQUENCE OF 199-1335 FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=87248040; PubMed=3036646; RA Keith T.P., Riley M.A., Kreitman M., Lewontin R.C., Curtis D., RA Chambers G.; RT "Sequence of the structural gene for xanthine dehydrogenase (rosy RT locus) in Drosophila melanogaster."; RL Genetics 116:67-73(1987). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RA Riley M.; RL Submitted (FEB-1987) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE OF 544-1335 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- CATALYTIC ACTIVITY: XANTHINE + NAD(+) + H(2)O = URATE + NADH. CC -!- COFACTOR: FAD, MOLYBDOPTERIN, AND TWO 2FE-2S CLUSTERS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE XANTHINE DEHYDROGENASE FAMILY. CC -!- SIMILARITY: TO 2FE-2S FERREDOXINS IN THE N-TERMINAL DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00308; CAA68409.1; -. DR EMBL; AE003698; AAF54895.1; -. DR EMBL; AY094689; AAM11042.1; ALT_INIT. DR PIR; S07245; S07245. DR HSSP; P80457; 1FO4. DR FlyBase; FBgn0003308; ry. DR InterPro; IPR002888; 2Fe-2S_bind. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR008274; Aldxan_dh_bind. DR InterPro; IPR000674; Aldxan_dh_hamm. DR InterPro; IPR005107; CO_deh_flav_C. DR InterPro; IPR002346; dehydrog_molyb. DR InterPro; IPR001041; Ferredoxin. DR InterPro; IPR000572; Oxidored_molyb. DR Pfam; PF02738; Ald_Xan_dh_C2; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF03450; CO_deh_flav_C; 1. DR Pfam; PF00941; FAD_binding_5; 1. DR Pfam; PF00111; fer2; 1. DR Pfam; PF01799; fer2_2; 1. DR ProDom; PD186071; 2Fe-2S_bind; 1. DR PROSITE; PS00197; 2FE2S_FERREDOXIN; 1. DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1. KW Oxidoreductase; NAD; Molybdenum; Flavoprotein; FAD; Metal-binding; KW Iron-sulfur; Iron; 2Fe-2S; Peroxisome. FT METAL 37 37 IRON-SULFUR (2FE-2S) (BY SIMILARITY). FT METAL 43 43 IRON-SULFUR (2FE-2S) (BY SIMILARITY). FT METAL 48 48 IRON-SULFUR (2FE-2S) (BY SIMILARITY). FT METAL 51 51 IRON-SULFUR (2FE-2S) (BY SIMILARITY). FT CONFLICT 106 106 A -> P (IN REF. 1 AND 3). FT CONFLICT 316 316 Q -> L (IN REF. 2 AND 3). FT CONFLICT 542 542 S -> P (IN REF. 2 AND 3). FT CONFLICT 709 709 H -> L (IN REF. 2 AND 3). FT CONFLICT 730 730 A -> S (IN REF. 2 AND 3). FT CONFLICT 988 988 E -> D (IN REF. 2 AND 3). SQ SEQUENCE 1335 AA; 146926 MW; 230368EA59B30AD8 CRC64; MSNSVLVFFV NGKKVTEVSP DPECTLLTFL REKLRLCGTK LGCAEGGCGA CTVMVSRLDR RANKIRHLAV NACLTPVCSM HGCAVTTVEG IGSTKTRLHP VQERLAKAHG SQCGFCTPGI VMSMYALLRN AEQPSMRDLE VAFQGNLCRC TGYRPILEGY KTFTKEFACG MGEKCCKVSG KGCGTDAETD DKLFERSEFQ PLDPSQEPIF PPELQLSDAF DSQSLIFSSD RVTWYRPTNL EELLQLKAKH PAAKLVVGNT EVGVEVKFKH FLYPHLINPT QVKELLEIKE NQDGIYFGAA VSLMEIDALL RQRIEQLPES ETRLFQCTVD MLHYFAGKQI RNVACLGGNI MTGSPISDMN PVLSAAGAQL EVASFVDGKL QKRSVHMGTG FFTGYRRNVI EAHEVLLGIH FRKTTPDQYI VAFKQARRRD DDIAIVNAAI NVRFEEKSNI VAEISMAFGG MAPTTVLAPR TSQLMVGQEW SHQLVERVAE SLCTELPLAA SAPGGMIAYR RALVVSLFFK AYLAISLKLS KSGITSSDAL PSEERSGAET FHTPVLKSAQ LFERVCSDQP ICDPIGRPKV HAAALKQATG EAIYTDDIPR MDGEVYLAFV LSTKPRAKIT KLDASEALAL DGVHQFFCYK DLTEHENEVG PVFHDEHVFA AGEVHCYGQI VGAIAADNKA LAQRAARLVK VEYEELSPVI VTIEQAIEHK SYFPDYPRFV TKGNVEEALA QADHTFEGTC RMGGQEHFYL ETHAALAVPR DSDELELFCS TQHPSEVQKL VAHVTALPAH RVVCRAKRLG GGFGGKESRG ISVALPVALA AYRMGRPVRC MLDRDEDMLI TGTRHPFLFK YKVGFTKEGL ITACDIECYN NAGWSMDLSF SVLERAMFHF ENCYRIPNVR VGGWVCKTNL PSNTAFRGFG GPQGMYAGEH IIRDVARIVG RDVVDVMRLN FYKTGDYTHY HQQLEHFPIE RCLEDCLKQS RYDEKRQEIA RFNRENRWRK RGMAVVPTKY GIAFGVMHLN QAGSLINIYG DGSVLLSHGG VEIGQGLNTK MIQCAARALG IPSELIHISE TATDKVPNTS PTAASVGSDL NGMAVLDACE KLNKRLAPIK EALPGGTWKE WINKAYFDRV SLSATGFYAM PGIGYHPETN PNARTYSYYT NGVGVTVVEI DCLTGDHQVL STDIVMDIGS SLNPAIDIGQ IEGAFMQGYG LFTLEELMYS PQGMLYSRGP GMYKLPGFAD IPGEFNVSLL TGAPNPRAVY SSKAVGEPPL FIGSSAFFAI KEAIAAARED QGLSGDFPLE APSTSARIRI ACQDKFTELL EIPEPGSFTP WNIVP // ID XMS1_DROME STANDARD; PRT; 736 AA. AC Q9U3V8; Q9VX76; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Xmas-1 protein. GN XMAS-1 OR CG32561/CG8919. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Xu E.Y., Kaufman T.C., Wu C.; RT "Two overlapping genes, xmas-1 and xmas-2, are required for RT spermatogenesis, oogenesis and embryogenesis."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: REQUIRED FOR SPERMATOGENESIS, OOGENESIS AND CC EMBRYOGENESIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF216664; AAF23814.1; -. DR EMBL; AE003504; AAF48702.2; -. DR FlyBase; FBgn0016080; xmas-1. DR GO; GO:0009790; P:embryonic development; NAS. DR GO; GO:0007292; P:female gamete generation; NAS. DR GO; GO:0007283; P:spermatogenesis; NAS. KW Developmental protein. FT CONFLICT 31 31 Y -> H (IN REF. 1). FT CONFLICT 231 231 A -> P (IN REF. 1). FT CONFLICT 721 721 K -> E (IN REF. 1). SQ SEQUENCE 736 AA; 84460 MW; 8D0D886578907E09 CRC64; MKSLVAQTEC QLRPLKVSSL VSALKAARSD YQGKSSAVCR LVAQMVEADQ VKYQWTPNLT SLIDRKDAST RHQWRPHVNH STRHARKLPV QSISFLSRCL AKKGEHAGLT SCVLSVKTRY APKTLHGREL LIWRQSSMRP LLLPSSNLWT GVLSKRHYVP RLRPAEEDEE VERRAVPQLR ITKEQSEEEE HQLQRRKDGS RLRNECSEFY LPMGEQDYSE REEENRGHRQ AYVPSELMTP ELATKWQTTS VTDRDRQLLN LEQQMKTQPS VRMTTQTWFS GNHRRYRSRR SGAKRYHVVS ELEGWRRSSN HQPVPVFQGQ PGEQEHLRHA SHKASARSMP DGQERCQMVW EQKKRSPWHR TEVTNSNKVR MPRIRAAKSA VMMAQEARNK HHRLITKKLV YRPRRTVNAV QAEETEDQDT HHRHHGGGQK MSKRAPERAL LKQHLADLLA VSKPEDSFRI GYQPNAPTRQ LLEQGKCYVS LRREQFIHLH PVRPNSLILA VNLEVKESPR QPVTTLHRRD GAKRPRLVED VVKPSLITVI RQSAATWDHN GRKVPAKKSN LVGMPSKEHA YQRRLVRNTS TLEAIVKAQA KPRSEPKSPS SATDYHRVAS QKLPHVTSKA DISKAADPFK DLDKPRIKEK EVASSWKQAY VVRSKMYDAI TPYRRRAYPG KKCITKDKTD GYFLAKRSSA AAAGSSKKVK PPKQPVVSPK VQVPSVLHKK KSRESLGPQT TKTGKL // ID XMS2_DROME STANDARD; PRT; 1370 AA. AC Q9U3V9; Q8IR02; Q8MQS3; Q9VX76; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Xmas-2 protein. GN XMAS-2 OR CG32562/CG8919. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Xu E.Y., Kaufman T.C., Wu C.; RT "Two overlapping genes, xmas-1 and xmas-2, are required for RT spermatogenesis, oogenesis and embryogenesis."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP REVISIONS. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP SEQUENCE OF 713-1370 FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: REQUIRED FOR SPERMATOGENESIS, OOGENESIS AND CC EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 RNA RECOGNITION MOTIF (RRM) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF216664; AAF23815.1; -. DR EMBL; AE003504; AAN09434.1; -. DR EMBL; AY128417; AAM75010.1; -. DR FlyBase; FBgn0028974; xmas-2. DR GO; GO:0003723; F:RNA binding; NAS. DR GO; GO:0009790; P:embryonic development; NAS. DR GO; GO:0007292; P:female gamete generation; NAS. DR GO; GO:0007283; P:spermatogenesis; NAS. DR InterPro; IPR000504; RNA_rec_mot. DR InterPro; IPR005062; SAC3_GANP. DR Pfam; PF03399; SAC3_GANP; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Developmental protein; RNA-binding. FT DOMAIN 12 83 RNA-BINDING (RRM). FT DOMAIN 644 763 GLN-RICH. FT CONFLICT 96 281 MISSING (IN REF. 1). FT CONFLICT 778 778 S -> N (IN REF. 1). FT CONFLICT 785 787 ESM -> VSV (IN REF. 1). FT CONFLICT 942 942 D -> E (IN REF. 1). FT CONFLICT 1027 1027 E -> K (IN REF. 1). FT CONFLICT 1217 1217 C -> Y (IN REF. 1). FT CONFLICT 1262 1262 I -> V (IN REF. 1). FT CONFLICT 1275 1275 S -> T (IN REF. 4). FT CONFLICT 1301 1301 K -> E (IN REF. 1). SQ SEQUENCE 1370 AA; 158178 MW; 0F3610BB4196E640 CRC64; MAEPRPGGYN YKTLLCRNIP ELFLDKYVAR SHFGRFGTLV NFVLRPRRMT CTVSYASEDE AARALLDGAS FQGHLFDISY ADNETAPAQK TEEWVDPDIQ AELSALQSGW RNEYGSGKPI KKPQNGSSGS GGSSMLPAIP VGPATAPVSR DRTPAQLRDL ENMMRRPAHT SEEKFSVLDA RDKLLRLNRT QHKLSGATQG HCADMCPEKE RVLREFQRQV AYYELQPGSD ELICHERALK QYSRSSADQE TPLPHELRNE TALHMTMSYL MHEIMDISER QDPQSHMGDW FHFVWDRTRS IRKEITQQEL CSLGAVKLVE QCARFHIHCA ARLVDADPSV FDSKINAENL TKCLQTLKYM YHDLRIKGVP CPKEAEFRGY IVLLNLADAN FLWDIGQLPA ELQSCPEVRQ AIQFYLALQD TNFVRFFQLL ADKDTSYLSA CILVNYFTRL RVLGLHRLIQ AYRSPRKDEV SSLPLSYIAE LLSFASEQEA ADFVQHYGLQ INEAGRVVLS RMHTVETEYK LPRQYELVEV KRVKSVGEVV SGEPLPPRDL YLNHRPHNSF DDYGMLKSIA WTAKDQLAGM QQEEMQPQMP SQPPAVSKHS DTLFKVPMQP DGTAAGFGVF AAAAVPPASS IDGFSFVLPK SRAQEFQEQA PATQQRRAQE EAKHQALQVA IAAAKKREAE LMAIHEAKVA EAERVRQQKL RERQEQQRRQ QQELEEQRQR EQEKLQLEKE RQLKLEQLFF VQQQEREAHK QTRTLELYQE IFQDTLAEIC QSEFMSHSRA CRSYESMLDS ITRDLVERQM EQSIYELGVM RVCIRRWRKY RRTQQEKDTL FNQLPLSFGA ENPEGVVNKR SMEDSLRLSR RYRLGEPCDY GKLLAGLEEH SWLKLDLWHV LDKCLPVAQP GARRFYKLLI SLSGGQEGLQ LNCDLDRGLL QQPQSPDARF VDGGYIRGFS QGIGLSVMKI RDDDHDWKAT DLAEANGIIC LIGLDDIRLL PDRLKPLLQA SRCHDVAVIV QHPANTAFVQ PDIPLQELCL RSFNIFRLRK SGNNRQRLMI ALESAVKFLA KATERKRVGH LHQVETREYL LVNLGSELFR RLKYAAEHDT AIRSDTQLNP QRCVDLFNEA VHRLQLVAGE DLSDWPQFPE ELRVFVQPLP IESSLNTNRL EHFEPGWHLP ERRQRIVQLL ERCKLPKMPV LPRSSSLAEA QCQWVLDYAQ ISQQEDCVEQ IALQAIKILQ YDTDDYLNFV EYLAGERMQY ILRQERNPPQ GIVYNTKTLK RRFLSAWYYE FREPQIYEPV PAEENAQMLE KQPSSQAEVQ QLDFDEITSK AEAVLKRFHQ RQDERHTLRE LNRSHKSRKR RDASDHKHAS KHKRKRSKSK // ID XPA_DROME STANDARD; PRT; 296 AA. AC P28518; Q24594; Q9V3V8; DT 01-DEC-1992 (Rel. 24, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-repair protein complementing XP-A cells homolog (Xeroderma DE pigmentosum group A complementing protein homolog). GN XPAC OR XPA OR EG:EG0007.8 OR CG6358. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92109732; PubMed=1764072; RA Shimamoto T., Kohno K., Tanaka K., Okada Y.; RT "Molecular cloning of human XPAC gene homologs from chicken, Xenopus RT laevis and Drosophila melanogaster."; RL Biochem. Biophys. Res. Commun. 181:1231-1237(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95403447; PubMed=7673233; RA Shimamoto T., Tanimura T., Yoneda Y., Kobayakawa Y., Sugasawa K., RA Hanaoka F., Oka M., Okada Y., Tanaka K., Kohno K.; RT "Expression and functional analyses of the Dxpa gene, the Drosophila RT homolog of the human excision repair gene XPA."; RL J. Biol. Chem. 270:22452-22459(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- FUNCTION: INVOLVED IN DNA EXCISION REPAIR. INITIATES REPAIR BY CC BINDING TO DAMAGED SITES WITH VARIOUS AFFINITIES, DEPENDING ON THE CC PHOTOPRODUCT AND THE TRANSCRIPTIONAL STATE OF THE REGION (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: STRONGLY EXPRESSED IN THE CENTRAL NERVOUS CC SYSTEM AND MUSCLES. CC -!- DEVELOPMENTAL STAGE: CONTINUOUSLY EXPRESSED IN ALL STAGES OF CC DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE XPA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D31893; BAA06691.1; -. DR EMBL; D31892; BAA06690.1; -. DR EMBL; AE003430; AAF45917.1; -. DR EMBL; AL033125; CAA21834.1; -. DR PIR; JQ1325; JQ1325. DR FlyBase; FBgn0004832; Xpac. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0006289; P:nucleotide-excision repair; IDA. DR InterPro; IPR000465; XPA_protein. DR Pfam; PF05181; XPA_C; 1. DR Pfam; PF01286; XPA_N; 1. DR TIGRFAMs; TIGR00598; rad14; 1. DR PROSITE; PS00752; XPA_1; 1. DR PROSITE; PS00753; XPA_2; 1. KW DNA repair; DNA-binding; Zinc-finger; Nuclear protein. FT DOMAIN 26 47 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT ZN_FING 126 150 FT CONFLICT 10 10 S -> A (IN REF. 2). FT CONFLICT 224 226 QHE -> HEQ (IN REF. 1). SQ SEQUENCE 296 AA; 33875 MW; 54C58F924955E2A4 CRC64; MSAEVSTNES APPAEKKSKL TNAQKARIER NQAKAQKLRE AKLVSHPFKE LASNKEGGTH PEAALSQGSS VIKVQGTKYI DSGGGFLLEQ PVMPTGVGPA GLNKSGEEAP PILDDAIAIP VQYEECLECG DMFADSYLFN NFGHSVCDKC RDKDERYALI TRTEAKAEYL LKDCDFDKRE PKLRYISRKN PHNVRWGEMK LYLHLQIHQR ALEVWGSEEE LVRQHEARED KREEGKARKY NKKMKQLRME VRSSIYTKKT HEVHEHEFGP DTYDEEEDTY THTCITCPYS ETYEKM // ID XPB_DROME STANDARD; PRT; 802 AA. AC Q02870; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE DNA excision repair protein haywire (ERCC-3 homolog protein). GN HAY OR ERCC3. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93087159; PubMed=1454518; RA Koken M.H., Vreeken C., Bol S.A., Cheng N.C., Jaspers-Dekker I., RA Hoeijmakers J.H., Eeken J.C., Weeda G., Pastink A.; RT "Cloning and characterization of the Drosophila homolog of the RT Xeroderma pigmentosum complementation-group B correcting gene, RT ERCC3."; RL Nucleic Acids Res. 20:5541-5548(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93092213; PubMed=1458540; RA Mounkes L.C., Jones R.S., Liang B.-C., Gelbart W., Fuller M.T.; RT "A Drosophila model for Xeroderma pigmentosum and Cockayne's RT syndrome: haywire encodes the fly homolog of ERCC3, a human excision RT repair gene."; RL Cell 71:925-937(1992). CC -!- FUNCTION: PROBABLY AN ATP-DEPENDENT DNA HELICASE INVOLVED IN CC EXCISION REPAIR OF DNA. MAY HAVE A DNA UNWINDING FUNCTION. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE HELICASE FAMILY. RAD25/XPB SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X68309; CAA48386.1; -. DR EMBL; L02965; AAA74931.1; ALT_SEQ. DR PIR; A44223; A44223. DR FlyBase; FBgn0001179; hay. DR InterPro; IPR001410; DEAD. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR001161; XPB_DNA_repair. DR Pfam; PF00271; helicase_C; 1. DR PRINTS; PR00851; XRODRMPGMNTB. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR TIGRFAMs; TIGR00603; rad25; 1. KW Helicase; DNA repair; ATP-binding; DNA-binding; Nuclear protein. FT DOMAIN 6 22 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT NP_BIND 360 367 ATP (BY SIMILARITY). FT SITE 461 464 DEVH BOX. FT CONFLICT 23 24 AE -> GQ (IN REF. 2). FT CONFLICT 283 284 AN -> DQA (IN REF. 2). FT CONFLICT 556 556 MISSING (IN REF. 2). SQ SEQUENCE 802 AA; 90704 MW; 51A7F17A85FF243C CRC64; MGPPKKSRKD RSGGDKFGKK RRAEDEAFTQ LVDDNDSLDA TESEGIPGAA SKNAETNDEQ INTDEYGAKD YRSQMQLRPD HGNRPLWVAP NGHVFLESFS PVYKHAHDFL IAISEPVCRP EHIHEYKLTA YSLYAAVSVG LQTHDIVEYL KRLSKTSIPE GILEFIRLCT LSYGKVKLVL KHNKYFIESP HPEVLQKLLK DPVIQKCRLI RSEGEDFIQG TLDGKAITQF GTKLPPGATD KPTADPAAAA GAVVAADGTT AVPEDITDFY EKIDKEEEDE DEANLKTVSF EVAQEKIEVI QKRCIEIEHP LLAEYDFRND TNNPDINIDL KPAAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG VTACCTVRKR ALVLCNSGVS VEQWKQQFKM WSTADDSMIC RFTSEAKDKP MGCGILVTTY SMITHTQKRS WEAEQTMRWL QEQEWGIMVL DEVHTIPAKM FRRVLTIVQS HCKLGLTATL LREDDKIADL NFLIGPKLYE ANWLELQKKG YIARVQCAEV WCPMSPEFYR EYLTTKTSKK MLLYVMNPSK FRSCQFLIKY HEQRGDKTIV FSDNVFALKH YAIKMNKPFI YGPTSQNERI QILQNFKFNS KVNTIFVSKV ADTSFDLPEA NVLIQISSHG GSRRQEAQRL GRILRAKKGA IAEEYNAFFY TLVSQDTMEM SYSRKRQRFL VNQGYSYKVI THLKGMDTDS DLMYGTQEEQ GQLLQLVLSA SDLDCEDEKL PGEPGYRPSG SGGIVRRVGG LSSMSGGDDA IYYEHRKKNI GSVHPLFKKF RG // ID XPC_DROME STANDARD; PRT; 1293 AA. AC Q24595; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-repair protein complementing XP-C cells homolog (Xeroderma DE pigmentosum group C complementing protein homolog) (XPCDM) (Mutagen- DE sensitive 209 protein). GN MUS210 OR XPCC OR XPC. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DP CN BW; TISSUE=Embryo; RX MEDLINE=94173669; PubMed=8127661; RA Henning K.A., Peterson C., Legerski R., Friedberg E.C.; RT "Cloning the Drosophila homolog of the Xeroderma pigmentosum RT complementation group C gene reveals homology between the predicted RT human and Drosophila polypeptides and that encoded by the yeast RAD4 RT gene."; RL Nucleic Acids Res. 22:257-261(1994). CC -!- FUNCTION: INVOLVED IN DNA EXCISION REPAIR. MAY PLAY A PART IN DNA CC DAMAGE RECOGNITION AND/OR IN ALTERING CHROMATIN STRUCTURE TO CC ALLOW ACCESS BY DAMAGE-PROCESSING ENZYMES (BY SIMILARITY). CC -!- FUNCTION: INVOLVED IN NUCLEOTIDE EXCISION REPAIR OF DNA DAMAGED CC WITH UV LIGHT, BULKY ADDUCTS, OR CROSS-LINKING AGENTS. CC -!- SUBUNIT: HETERODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE XPC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z28622; CAA82262.1; -. DR PIR; S42402; S42402. DR FlyBase; FBgn0004698; mus210. DR InterPro; IPR004583; Rad4. DR Pfam; PF03835; Rad4; 1. DR TIGRFAMs; TIGR00605; rad4; 1. KW DNA repair; DNA-binding; Nuclear protein. FT DOMAIN 33 40 POLY-ASP. FT DOMAIN 632 637 POLY-SER. FT DOMAIN 686 693 POLY-SER. FT DOMAIN 922 938 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 1195 1211 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 1275 1291 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). SQ SEQUENCE 1293 AA; 144177 MW; 99DF671F9A4151C5 CRC64; MSDEEEDSVS EGFSASEDEW KPSKDVKGGE SSDDDDSDFD ELQAEGGAAG SSGRSSAVAG KRGDHKAPSG IKGSSVKKRK PTGQSLRSKL YNKYRPPPKT FPTSPSQQQE NTPRASGSKN AKTPNESGAR NQHDPADSSS ESSVEDYLVN PADLDLHSTF FAGGQKEKSP APQFDCNAGI TNLSDSGSED NNESSFEDKA GNAFDFRGLL ENANSLERTR DALSKRNVTA TPPRSQAATM DVNALLALGE NQNYQSVEVE EREGNQRKKA GRGAPAAPPT LDEPSRLSKT KSTRIKRHTK TRPVSTVVAN AGDTDDSDFE EVADADLSSD QDDGETPNIS GDLEIRVGLE GLRPTKEQKT QHELEMALKR RLNRDIKDRQ ILLHKVSLMC QIARSLKYNR LLSESDSLMQ ATLKLLPSRN AYPTERGTEL KYLQSFVTWF KTSIKLLSPN LYSAQSPATK EAILEALLEQ VKRKEARCKQ DMIFIFIALA RGMGMHCRLI VNLQPMPLRP AASDLIPIKL RPDDKNKSQT VESERESEDE KPKKDKKAGK PAEKESSKST ISKEAEKKNN AKKAEAKPLS KSTTKGSETT KSGTVPKVKK ELSLSSKLVE KSKHQKAHTS SKSDTSFDEK PSTSSSSKCL KEEYSELGLS KKLLKPTLSS KLVLKSKNQS SFSSNKSDTS FEENPSTSSS SKSLKEETAK LSSSKLEDKK VASSAETKTK VQSSLLKRVT TQNISESGDS KKSKVAPVDT FSPVAGRTRR ATVKPKTEEK PQVVGSPVIP KLMLSKVKQL NAKHSDTENA SPANKHLQEQ RNTRETRSRS KSPKVLISPS FLKKKSDGAD STSAPQKHQM APETKARISP NFLSEALPAR QLRSRGQKAS SLAIPQLDGG DDVPLPKKRP KLEKLKNSQD SDEVFEPAKP VKKAPVLPKS VQNLRKDRRV MSTDDEGGSR LNRKTDASDM WVEVWSDVEE QWICIDLFKG KLHCVDTIRK NATPGLAYVF AFQDDQSLKD VTARYCASWS TTVRKARVEK AWLDETIAPY LGRRTKRDIT EDDQLRRIHS DKPLPKSISE FKDHPLYVLE RHLLKFQGLY PPDAPTLGFI RGEAVYSRDC VHLLHSREIW LKSARVVKLG EQPYKVVKAR PKWDRLTRTV IKDQPLEIFG YWQTQEYEPP TAENGIVPRN AYGNVELFKD CMLPKKTVHL RLPGLMRICK KLNIDCANAV VGFDFHQGAC HPMYDGFIVC EEFRDVVTAA WEEDQQVQVL KEQEKYETRV YGNWKKLIKG LLIRERLKKK YNF // ID Y1R1_DROME STANDARD; PRT; 471 AA. AC P16424; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Hypothetical 50 kDa protein in type I retrotransposable element R1DM DE (ORF 1). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90204545; PubMed=1690812; RA Jakubczak J.L., Xiong Y., Eickbush T.H.; RT "Type I (R1) and type II (R2) ribosomal DNA insertions of Drosophila RT melanogaster are retrotransposable elements closely related to those RT of Bombyx mori."; RL J. Mol. Biol. 212:37-52(1990). CC -!- SIMILARITY: TO CORRESPONDING ORF OF BOMBYX MORI (R1BM). CC -!- SIMILARITY: TO RETROVIRAL GAG PROTEINS. CC -!- SIMILARITY: CONTAINS 2 CCHC-TYPE ZINC FINGERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51968; CAA36226.1; -. DR PIR; S09110; S09110. DR FlyBase; FBgn0044825; R1-element\ORF1. DR InterPro; IPR001878; Znf_CCHC. DR Pfam; PF00098; zf-CCHC; 1. DR PRINTS; PR00939; C2HCZNFINGER. DR SMART; SM00343; ZnF_C2HC; 2. DR PROSITE; PS50158; ZF_CCHC; 1. KW Hypothetical protein; Transposable element; Zinc-finger; Repeat. FT ZN_FING 397 414 CCHC-TYPE 1. FT ZN_FING 417 434 CCHC-TYPE 2. FT DOMAIN 438 457 GAG-LIKE CYSTEINE MOTIF. SQ SEQUENCE 471 AA; 50380 MW; 929731215DC2AF8A CRC64; PVSASIRLLD SSKGGATIGA TPMESDSSVS ALSGSSASKV SRRGRRRSHL ASKSSAPTQA KLVALASNGV PEPVGVLEEA FSSLEDARAA TSNAANDAAP PAAAPAVDHT VAPDVSTAAK IAATTATAAT AAARAGQAAM MAELSATQRM VRNSFRSLGG VDTEELSCAI SRYDELVMAL MLRCGELETR LAMPPPPPPP SKANTTAANA PQMPQVAPIA APRTTKVRET WSAVVKCDDP ALSGKAIAEK VRTMVAPSLG VRVHEVRELP SRWWCDHSYS SVGELQKVMA SKRFAELGLN VARNAAEKPK VIVYDVDTAI GPEEFMQELH ENNFDSEMTL AQFKKSVHLV TKAWSATDGA TVNVTLEVDD RAMAKLDVGR VYIKWFSFRC RSQVRTYACH RCVGFDHKVS ECRQKESVCR QCGQQGHTAA KCQNPVDCRN CRHRGQPSGH YMLSNACPIY GALLARVQAR H // ID Y2R2_DROME STANDARD; PRT; 1021 AA. AC P16425; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Hypothetical 115 kDa protein in type I retrotransposable element R1DM DE (ORF 2). OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=90204545; PubMed=1690812; RA Jakubczak J.L., Xiong Y., Eickbush T.H.; RT "Type I (R1) and type II (R2) ribosomal DNA insertions of Drosophila RT melanogaster are retrotransposable elements closely related to those RT of Bombyx mori."; RL J. Mol. Biol. 212:37-52(1990). CC -!- SIMILARITY: TO CORRESPONDING ORF OF BOMBYX MORI (R1BM). CC -!- SIMILARITY: TO RETROVIRAL POL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51968; CAA36227.1; -. DR PIR; S09111; S09111. DR FlyBase; FBgn0044824; R1-element\ORF2. DR InterPro; IPR000477; RVTse. DR Pfam; PF00078; rvt; 1. KW Hypothetical protein; Transposable element. FT DOMAIN 955 971 GAG-LIKE CYSTEINE MOTIF. SQ SEQUENCE 1021 AA; 114931 MW; F057262D00EAAA57 CRC64; TLMFSFIQAN CGRGRAATIE LGVRLRRSES MFALVQEPYL GGDEMDVLPE GMRVFTDRRG KAAILVDHQE AICMPVETLT TDYGVCLVVK GSFGSIFLCA AYCQFDAPLE PYLRYMDAVL LQASRTPAIL GLDANAVSPM WLSKLSRHAE GQANYRRGEL LSEWMLEARV AALNQSTEVY TFDNHRATSD IDVTIVNEAA SMWATYEWRV DEWELSDHNI ITVVAEPTTA RSVESIAPVP SWNFSNARWR LFKEEMVSRI AELPENFSES PLDQQVSTLR SIVHSVCDTA LGRKLTRSPS RRARWWTADL CAARREVRRL RRLLQDGRRR DDDAAVELVV VELRRASAYY KKLIGRAKMD DWKRFVGDHA DDPWGRVYKI CRGRRKCTEI GCLRVNGELI TDWGDCARVL LRNFFPVAES EAPTAIAEEV PPALEVFEVD TCVARLKSRR SPGLDGINGT ICKAVWRAIP EHLASLFSRC IRLGYFPAEW KCPRVVSLLK GPDKDKCEPS SYRGICLLPV FGKVLEAIMV NRVREVLPEG CRWQFGFRQG RCVEDAWRHV KSSVGASAAQ YVLGTFVDFK GAFDNVEWSA ALSRLADLGC REMGLWQSFF SGRRAVIRSS SGTVEVPVTR GCPQGSISGP FIWDILMDVL LQRLQPYCQL SAYADDLLLL VEGNSRAVLE EKGAQLMSIV ETWGAEVGDC LSTSKTVIML LKGALRRAPT VRFAGRNLPY VRSCRYLGIT VSEGMKFLTH IASLRQRMTG VVGALARVLR ADWGFSPRAR RTIYDGLMAP CVLFGAPVWY DTAEQVAAQR RLASCQRLIL LGCLSVCRTV STVALQVLGG APPLDLAAKL LAIKYKLKRG FPLEENDWLY GEDIACLSWE QRKTRLEECL IQSWQNRWDD DSEPGRVTHR FIPYVTLAYR DPSFGFSMRT SFLLTGHGSF NAFLHGRALS DTTACACGDP YEDWMHILCA CPLYADLRDL DGLGVQRLGE NWIFEGILDD QEKTQRLAMF AEEVFLRRRA L // ID Y5C_DROME STANDARD; PRT; 68 AA. AC P20008; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Hypothetical 7.2 kDa protein at locus 5C. GN ANON-5C. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88193084; PubMed=2896018; RA Rao J.P., Zafar R.S., Sodja A.; RT "Transcriptional activity at the 3' end of the actin gene at 5C on RT the X chromosome of Drosophila melanogaster."; RL Biochim. Biophys. Acta 950:30-44(1988). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07627; CAA30475.1; -. DR PIR; S01743; S01743. DR FlyBase; FBgn0011819; Orf5C. KW Hypothetical protein. SQ SEQUENCE 68 AA; 7217 MW; 7C4E8515AC86B855 CRC64; MVLILLAGGG GEVEEAAAKV QVRVVEVWSA AQQNQQQHQL QDEKSGTTCH TIITIIIVLG ACCVVPAY // ID YELL_DROME STANDARD; PRT; 541 AA. AC P09957; Q9W5G5; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Yellow protein precursor. GN Y OR EG:125H10.2 OR CG3757. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Chia W., Howes G., Martin M., Meng Y.B., Moses K., Tsubota S.; RT "Molecular analysis of the yellow locus of Drosophila."; RL EMBO J. 5:3597-3605(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87053835; PubMed=3096713; RA Geyer P.K., Spana C., Corces V.G.; RT "On the molecular mechanism of gypsy-induced mutations at the yellow RT locus of Drosophila melanogaster."; RL EMBO J. 5:2657-2662(1986). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: CONTROL OF PATTERN OF PIGMENTATION OF THE ADULT CUTICLE CC AND THE LARVAL MOUTH PARTS. DELETION FOR Y FAIL TO PIGMENTATION CC THESE STRUCTURES AND SHOW REDUCED LEVEL OF LOCOMOTOR ACTIVITY CC AND MALE COMPETITIVE MATING ABILITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- DEVELOPMENTAL STAGE: REQUIRED DURING THE LATER HALF OF PUPAL CC DEVELOPMENT FOR THE NORMAL PIGMENTATION OF THE ADULT CUTICLE. CC -!- SIMILARITY: BELONGS TO THE MAJOR ROYAL JELLY PROTEIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04427; CAA28024.1; -. DR EMBL; AL023873; CAA19640.1; -. DR EMBL; AE003417; AAF45497.1; -. DR PIR; A25696; A25696. DR FlyBase; FBgn0004034; y. DR GO; GO:0007619; P:courtship behavior; NAS. DR InterPro; IPR003534; Royaljelly. DR Pfam; PF03022; MRJP; 1. DR PRINTS; PR01366; ROYALJELLY. KW Developmental protein; Signal. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 541 YELLOW PROTEIN. FT CARBOHYD 144 144 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 215 215 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 541 AA; 60519 MW; 7728D1FA9A4ECB7A CRC64; MFQDKGWILV TLITLVTPSW AAYKLQERYS WSQLDFAFPN TRLKDQALAS GDYIPQNALP VGVEHFGNRL FVTVPRWRDG IPATLTYINM DRSLTGSPEL IPYPDWRSNT AGDCANSITT AYRIKVDECG RLWVLDTGTV GIGNTTTNPC PYAVNVFDLT TDTRIRRYEL PGVDTNPNTF IANIAVDIGK NCDDAYAYFA DELGYGLIAY SWELNKSWRF SAHSYFFPDP LRGDFNVAGI NFQWGEEGIF GMSLSPIRSD GYRTLYFSPL ASHRQFAVST RILRDETRTE DSYHDFVALD ERGPNSHTTS RVMSDDGIEL FNLIDQNAVG CWHSSMPYSP QFHGIVDRDD VGLVFPADVK IDENKNVWVL SDRMPVFLLS DLDYSDTNFR IYTAPLATLI ENTVCDLRNN AYGPPNTVSI PKQAVLPMGP PLYTKQYRPV LPQKPQTSWA SSPPPPSRTY LPANSGNVVS SISVSTNSVG PAGVEVPKAY IFNQHNGINY ETSGPHLFPT HQPAQPGGQD GGLKTYVNAR QSGWWHHQHQ G // ID YEMA_DROME STANDARD; PRT; 1002 AA. AC P25992; Q9VAP4; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Yemanuclein-alpha. GN YEM-ALPHA OR YEMA OR YG4.5 OR CG11879. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Canton-S; RX MEDLINE=92297435; PubMed=1606021; RA Ait-Ahmed O., Bellon B., Capri M., Joblet C., Thomas-Delaage M.; RT "The yemanuclein-alpha: a new Drosophila DNA binding protein specific RT for the oocyte nucleus."; RL Mech. Dev. 37:69-80(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY PLAY A KEY ROLE IN EGG ORGANIZATION. IT MAY BE A CC TRANSCRIPTIONAL REGULATOR. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: OOCYTE SPECIFIC. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT ALL OOGENIC STAGES. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63503; CAA45074.1; -. DR EMBL; AE003768; AAF56858.2; -. DR PIR; A56678; A56678. DR FlyBase; FBgn0005596; yem-alpha. KW Nuclear protein; DNA-binding; Repeat. FT DOMAIN 80 85 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 207 217 POLY-SER. FT DOMAIN 219 261 ASP/GLU-RICH (ACIDIC). FT DOMAIN 230 253 2 X 12 AA TANDEM REPEATS. FT REPEAT 230 241 1. FT REPEAT 242 253 2. FT VARIANT 698 698 S -> L. SQ SEQUENCE 1002 AA; 109310 MW; EE69A384EBA24D2F CRC64; MSKGGEHKRV TLTSIIQGDA GFSRFGSNIL EPDAASAAPD NSSKPTTKTA KCIRIKLDLF ETDSNKYPEF NYSRLLYLEK KKTKKLKQVS TTNGSASTDP FADNDDDVAR IVKELEAKYG NSYATGRGKS KKDDYRDIGM GYDESDSFID NTEAYDEIIP EEAETLEGGF YINCGALEFK NLTKKSYTTR TDAIIKMPER SRKRMVSSSS ESSSSSSGDD DENDDGNNEE DDESDSEDDS EENDESDSED DSESESLEDE DSAATAKSSS KYKDNHQAKR AKVIVTGKSK PSSSSLTSGK KPPTKPITTS SSSNSPRPST VEISDTEDGQ DPIQTQPSSQ LQSLPQSQAQ AQALKKVVKT TTVKDMLKAK RDSFLKSQSG TAAVKGVGNG ELKCVSTDVS SSDSSDMESE HGRADRQAGQ HGKDGQENLR TADTLLPTTL DADIVTAVNS FKEAVKSRDM CGKKFNLDVK LSPLLLRVYE AVLCTDRNER NMVFSHIEYQ LQLPKYYMLR KGKQVRAKEE KRKSTIMLEK LRRAVAVVMP KAVANYETEL RTFAEQAAAD VNSELPPKMP RKKFQWTSEL RHLLYDVYQA RWTSYAFLAK RKESLEEFIN WYLKEKVVEL WPPGWMRLDE LQREITRYKN AKLKAKEKPK APPASASPKP VGVVSAPEQM PPASSYLKAV EDPRSRGNSD TDSATSASSN SLKRKLKEMP KQTSKPPKKK VAKQVPLQPQ LTPHPQFQLA PAATAAVSIP AISNNNNHLP HLDTLLSMPS TSAQAAALNA AAVAAASTVL DLASPSRKID LNTSNNFYNL ITAASLAASG NPSPHSGDGQ AKVIVGARPS PHVINLDDYQ CTSDILQTSK QLAATTTVIT AISKAAQTTS VARESSSESD GVEIVGVFPA SKPQKKVQSK PKNKTQNRGR SSLGAVGQVN GSLGYSANNM YIYNSPRTLG PVYDLTDPHI MKTMSNLKEM EKQFIQAAFS PNSVKGASGG MGSSAPSTPT RQ // ID YI71_DROME STANDARD; PRT; 439 AA. AC P04282; DT 20-MAR-1987 (Rel. 04, Created) DT 20-MAR-1987 (Rel. 04, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Hypothetical 51 kDa protein in copia-like transposable element 17.6. GN GAG. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85061628; PubMed=6209583; RA Saigo K., Kugimiya W., Matsuo Y., Inouye S., Yoshioka K., Yuki S.; RT "Identification of the coding sequence for a reverse RT transcriptase-like enzyme in a transposable genetic element in RT Drosophila melanogaster."; RL Nature 312:659-661(1984). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01472; CAA25701.1; -. DR PIR; A03325; QXFF71. DR FlyBase; FBgn0044339; 17.6\gag. KW Transposable element; Hypothetical protein. SQ SEQUENCE 439 AA; 51586 MW; 16F0014936AEA111 CRC64; MAQEPAIVPP LSDSNMTQVA YQIGNVEKFN GDPGSLYTFV SRIDYILALY ATGDERQQQI IFGHIERSIS GEVMRCIGAY DMYTWQQLRR QLVLNYKPQT PNHVLLEEFR KTPFRGNVRA FLEEAESRRQ TLTSKLELEQ DLEEKTFYLK LIKSSIESLI EKLPTHIYLR INNHNIPDLR SLINLLQEKG MYEQINHTST HVQKQNFSDK PQKSFNQNTN QSNNIRKYPT PFLHYNSPIP YQAPQIYQTP PTNNPLYRHP IPYHPNPNNV FQPSQQNNVF QPSQQNNAFQ PNQRTNFTSR PIFNTNRNNA FDQNRFGQQP QYQNQQSTQN SSSYVPNRPI KRLRPANSGQ TGMSVDETLY QEDAFYQQCV PYDYFYYPTY DHSDYYPENQ YQIDENNQNL QRTQQLQQIN TDETNNDNQE PNVEQAENFQ PQALENPNI // ID YI72_DROME STANDARD; PRT; 456 AA. AC P04283; DT 20-MAR-1987 (Rel. 04, Created) DT 20-MAR-1987 (Rel. 04, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Hypothetical 53 kDa protein in copia-like transposable element 17.6. GN ENV. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85061628; PubMed=6209583; RA Saigo K., Kugimiya W., Matsuo Y., Inouye S., Yoshioka K., Yuki S.; RT "Identification of the coding sequence for a reverse RT transcriptase-like enzyme in a transposable genetic element in RT Drosophila melanogaster."; RL Nature 312:659-661(1984). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01472; CAA25703.1; ALT_INIT. DR PIR; A03326; QXFF73. DR FlyBase; FBgn0027624; 17.6\env. KW Transposable element; Hypothetical protein. SQ SEQUENCE 456 AA; 53419 MW; 335C562304602890 CRC64; MLITTVHGQQ IEINNIDTNH GYLLFSDKPV QIPSSFEHHC LRINLTEIDT IADYFEQRLR TDYHAPQVKF LYNKMRRELA GIALRHRNKR GLINIVGSVF KYLFGTLDEN DRVDIQRKLE TNAHNSVNLH ELNDAIQLIN DGMQKIQNYE NNSNIINSLL YELMQFTEYI EDVEMGMQLS RLGLFNPKLL NYDKLENVNS QNILNIKTST WINYNDNQLL IISHIPINFS LINTVKIIPY PDSNGYQLEY TDTQSYFERE NKVYNNENKE INNECVTNII KHLKPICNFE SIHTDEIIKY IEPNTIVTWN LTQTSLKQNC QNSFNNIKIK GNKMIKVTQC KIEINSIILS ENLFKPEIDL TPLYTPLNIT KIKTVKHNDI NEMISQNNIT LYIFMTTVII ILILLYLYLR YVSFNPFMML YAKLKLRKNQ NQNTAQQIEM EDVPLPLLYP SIPAQV // ID YIPP_DROME STANDARD; PRT; 121 AA. AC Q9XZF0; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Yippee protein. GN YIPPEE OR CG1989. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21135162; PubMed=11240639; RA Roxstroem-Lindquist K., Faye I.; RT "The Drosophila gene Yippee reveals a novel family of putative zinc RT binding proteins highly conserved among eukaryotes."; RL Insect Mol. Biol. 10:77-86(2001). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBUNIT: INTERACTS WITH HEMOLIN. CC -!- SIMILARITY: BELONGS TO THE YIPPEE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF172939; AAD47881.1; -. DR EMBL; AF139189; AAD28537.1; -. DR EMBL; AE003492; AAF48266.1; -. DR FlyBase; FBgn0026749; Yippee. DR GO; GO:0046872; F:metal ion binding; NAS. DR InterPro; IPR004910; Yippee. DR Pfam; PF03226; Yippee; 1. SQ SEQUENCE 121 AA; 13743 MW; 910FFBA1D775B580 CRC64; MGRIFLEHLG GLKLFNCAQC HTNLTNRSQL ISTRFTGATG RAYLFKRVVN LTFSNIQERV MLTGRHMVRD VMCKNCGAKL GWMYEFATEE SQKYKEGRVI LEYALITEAE GFPSEAATTS H // ID YL_DROME STANDARD; PRT; 1984 AA. AC P98163; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Putative vitellogenin receptor precursor (Yolkless protein) (YL). GN YL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=95183490; PubMed=7878005; RA Schonbaum C.P., Lee S., Mahowald A.P.; RT "The Drosophila yolkless gene encodes a vitellogenin receptor RT belonging to the low density lipoprotein receptor superfamily."; RL Proc. Natl. Acad. Sci. U.S.A. 92:1485-1489(1995). CC -!- FUNCTION: INVOLVED IN UPTAKE OF VITELLOGENIN BY ENDOCYTOSIS. CC -!- TISSUE SPECIFICITY: OVARY. CC -!- SIMILARITY: CONTAINS 13 LDL-RECEPTOR CLASS A DOMAINS. CC -!- SIMILARITY: CONTAINS 7 EGF-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13637; AAB60217.1; -. DR PIR; T13171; T13171. DR HSSP; P01130; 1AJJ. DR FlyBase; FBgn0004649; yl. DR GO; GO:0007292; P:female gamete generation; NAS. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR001881; EGF_Ca. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR002172; LDL_receptor_A. DR InterPro; IPR000033; Ldl_receptor_rep. DR Pfam; PF00008; EGF; 5. DR Pfam; PF00057; ldl_recept_a; 13. DR Pfam; PF00058; ldl_recept_b; 6. DR PRINTS; PR00261; LDLRECEPTOR. DR SMART; SM00179; EGF_CA; 2. DR SMART; SM00192; LDLa; 13. DR SMART; SM00135; LY; 10. DR PROSITE; PS00010; ASX_HYDROXYL; 2. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS50026; EGF_3; 3. DR PROSITE; PS01187; EGF_CA; 2. DR PROSITE; PS01209; LDLRA_1; 11. DR PROSITE; PS50068; LDLRA_2; 13. KW Glycoprotein; Signal; Transmembrane; EGF-like domain; Receptor; KW Repeat; Endocytosis. FT SIGNAL 1 ? POTENTIAL. FT CHAIN ? 1984 PUTATIVE VITELLOGENIN RECEPTOR. FT DOMAIN ? 1800 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1801 1821 POTENTIAL. FT DOMAIN 1822 1984 CYTOPLASMIC (POTENTIAL). FT DOMAIN 88 126 LDL-RECEPTOR CLASS A 1. FT DOMAIN 127 167 LDL-RECEPTOR CLASS A 2. FT DOMAIN 182 222 LDL-RECEPTOR CLASS A 3. FT DOMAIN 225 264 LDL-RECEPTOR CLASS A 4. FT DOMAIN 264 306 LDL-RECEPTOR CLASS A 5. FT DOMAIN 306 347 EGF-LIKE 1. FT DOMAIN 348 388 EGF-LIKE 2, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 660 701 EGF-LIKE 3. FT DOMAIN 984 1026 EGF-LIKE 4. FT DOMAIN 1029 1064 LDL-RECEPTOR CLASS A 6. FT DOMAIN 1072 1111 LDL-RECEPTOR CLASS A 7. FT DOMAIN 1116 1154 LDL-RECEPTOR CLASS A 8. FT DOMAIN 1156 1195 LDL-RECEPTOR CLASS A 9. FT DOMAIN 1196 1234 LDL-RECEPTOR CLASS A 10. FT DOMAIN 1241 1281 LDL-RECEPTOR CLASS A 11. FT DOMAIN 1281 1320 LDL-RECEPTOR CLASS A 12. FT DOMAIN 1338 1377 LDL-RECEPTOR CLASS A 13. FT DOMAIN 1375 1417 EGF-LIKE 5. FT DOMAIN 1418 1457 EGF-LIKE 6, CALCIUM-BINDING (POTENTIAL). FT DOMAIN 1734 1770 EGF-LIKE 7. FT SITE 1837 1837 CRITICAL FOR ENDOCYTOSIS (POTENTIAL). FT SITE 1878 1878 CRITICAL FOR ENDOCYTOSIS (POTENTIAL). FT SITE 1892 1892 CRITICAL FOR ENDOCYTOSIS (POTENTIAL). FT DISULFID 90 102 BY SIMILARITY. FT DISULFID 97 115 BY SIMILARITY. FT DISULFID 109 124 BY SIMILARITY. FT DISULFID 129 144 BY SIMILARITY. FT DISULFID 137 157 BY SIMILARITY. FT DISULFID 151 166 BY SIMILARITY. FT DISULFID 184 197 BY SIMILARITY. FT DISULFID 191 210 BY SIMILARITY. FT DISULFID 204 220 BY SIMILARITY. FT DISULFID 227 239 BY SIMILARITY. FT DISULFID 234 253 BY SIMILARITY. FT DISULFID 247 262 BY SIMILARITY. FT DISULFID 266 281 BY SIMILARITY. FT DISULFID 275 294 BY SIMILARITY. FT DISULFID 288 304 BY SIMILARITY. FT DISULFID 310 321 BY SIMILARITY. FT DISULFID 315 331 BY SIMILARITY. FT DISULFID 333 346 BY SIMILARITY. FT DISULFID 352 363 BY SIMILARITY. FT DISULFID 359 372 BY SIMILARITY. FT DISULFID 374 387 BY SIMILARITY. FT DISULFID 664 673 BY SIMILARITY. FT DISULFID 669 685 BY SIMILARITY. FT DISULFID 687 700 BY SIMILARITY. FT DISULFID 988 999 BY SIMILARITY. FT DISULFID 995 1009 BY SIMILARITY. FT DISULFID 1011 1025 BY SIMILARITY. FT DISULFID 1031 1040 BY SIMILARITY. FT DISULFID 1035 1053 BY SIMILARITY. FT DISULFID 1047 1062 BY SIMILARITY. FT DISULFID 1074 1087 BY SIMILARITY. FT DISULFID 1081 1100 BY SIMILARITY. FT DISULFID 1094 1109 BY SIMILARITY. FT DISULFID 1118 1130 BY SIMILARITY. FT DISULFID 1125 1143 BY SIMILARITY. FT DISULFID 1137 1152 BY SIMILARITY. FT DISULFID 1158 1170 BY SIMILARITY. FT DISULFID 1165 1183 BY SIMILARITY. FT DISULFID 1177 1193 BY SIMILARITY. FT DISULFID 1198 1210 BY SIMILARITY. FT DISULFID 1205 1223 BY SIMILARITY. FT DISULFID 1217 1232 BY SIMILARITY. FT DISULFID 1243 1257 BY SIMILARITY. FT DISULFID 1250 1270 BY SIMILARITY. FT DISULFID 1264 1279 BY SIMILARITY. FT DISULFID 1283 1296 BY SIMILARITY. FT DISULFID 1290 1309 BY SIMILARITY. FT DISULFID 1303 1318 BY SIMILARITY. FT DISULFID 1340 1352 BY SIMILARITY. FT DISULFID 1347 1365 BY SIMILARITY. FT DISULFID 1359 1375 BY SIMILARITY. FT DISULFID 1379 1392 BY SIMILARITY. FT DISULFID 1388 1401 BY SIMILARITY. FT DISULFID 1403 1416 BY SIMILARITY. FT DISULFID 1422 1432 BY SIMILARITY. FT DISULFID 1428 1441 BY SIMILARITY. FT DISULFID 1443 1456 BY SIMILARITY. FT DISULFID 1738 1747 BY SIMILARITY. FT DISULFID 1743 1756 BY SIMILARITY. FT DISULFID 1758 1769 BY SIMILARITY. FT CARBOHYD 30 30 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 365 365 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 384 384 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 429 429 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 666 666 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 749 749 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 782 782 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1022 1022 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1240 1240 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1265 1265 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1326 1326 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1475 1475 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1490 1490 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 1519 1519 V -> I. SQ SEQUENCE 1984 AA; 219318 MW; F92A256E0ACD5E48 CRC64; MCQAEHQVHP SEQRIRVESP KMTASRRGFN LTSQTRAHPS SGGSTSSRYG NCQRTHLIIN GRHVAISLLL LVGLCGGTAA GTPGSADTRC DAGQFQCRDG GCILQAKMCD GRGDCKDSSD ELDCDYRLCR PPHWFPCAQP HGACLAAELM CNGIDNCPGG EDELNCPVRP GFRFGDTAHR MRSCSKYEFM CQQDRTCIPI DFMCDGRPDC TDKSDEVAGC KQAEITCPGE GHLCANGRCL RRKQWVCDGV DDCGDGSDER GCLNLCEPQK GKFLCRNRET CLTLSEVCDG HSDCSDGSDE TDLCHSKPDC DAKKCALGAK CHMMPASGAE CFCPKGFRLA KFEDKCEDVD ECKEQDDLCS QGCENTSGGY RCVCDAGYLL DKDNRTCRAV VYGSKEQQPL LLYTTQMTIM GMHLREDNVR NHVYQVAGNL SKVIGVAYDG SHIYWTNIQN EAESIVKANG DGSNAEILLT SGLDAPEDLA VDWLTQNIYF SDNIMRHIAV CSNDGLNCAV LVTQDVHQPR SLAVWPQKGL MFWTDWGEKP MIGRASMDGS RSRPIVSDNI EWPNGIALDM HQQRIYWVDA KLGSVQTVRP DGTGRRTVLD GMLKHPYGLA IFEDQLYWSD WATKSVHACH KFSGKDHRIL AKDRTIYAVH IYHPAKQPNS PHGCENATCS HLCLLAEPEI GGHSCACPDG MRLAPDHRRC MLMEKRQRLF IGLGQVLLEI EHTAFGAHQV SKSYTLPCLI NEMVYNRING SLIIADNDQR LILEFQPESH ESNVLVRSNL GNVSALAFDH LSRNLYWADT ERAVIEVLSL QTRHRALIRF FPGQEVPIGL TVMPAEGYLY VVLKAKRHSH IDKIPLSGKG EQVHVFEDDL GDDDIKLVTD YETQTIFWSD SDLGRISYSN YRVPHSQIFR GKLRRPYSLA MVHHDLFWNE LGTPRIYWTH KSNMGPRKVI DIMEKDDPAA IMPYVPVATP NGIPLAASSP VGQESHPCQQ QNGGCSHICV GEGPYHSICL CPAGFVYRDA GNRTCVEALD CEFRCHSGEC LTMNHRCNGR RDCVDNSDEM NCDEEHRHKP KVLCSPSQFA CHSGEQCVDK ERRCDNRKDC HDHSDEQHCE KFDKSKKCHV HQHGCDNGKC VDSSLVCDGT NDCGDNSDEL LCEATLRCEP GMFQCGSGSC IAGSWECDGR IDCSDGSDEH DKCVHRSCPP DMHRCLSGQC LDRSLVCDGH NDCGDKSDEL NCGTDSSTMN ISCAEDQYQC TSNLKICLPS AVRCNGTTEC PRGEDEADCG DVCSIYEFKC RSGRECIRRE FRCDGQKDCG DGSDELSCEL EKGHHNQSQI QPWSTSSRSC RPHLFDCQDG ECVDLSRVCN NFPDCTNGHD EGPKCATACR SASGRQVCQH KCRATPAGAV CSCFDGYRLD ADQKSCLDID ECQEQQPCAQ LCENTLGGYQ CQCHADFMLR QDRVSCKSLQ SGATLLFSSF NEVRNLSEQP VMLNVAWSAN DSRITGFDLA MHRQMGYFSA EDEGIVYQVD LQTKVIVRAL GLPAPTKLSV DWVTGNVYVL SGAQEIQACS FVGRMCGRIV HVKSPRHVKH LAVDGYHARI FYIVIRTEGY GQTSSEIHMA RLDGSRRDML LQRSESFMTA LTTDPHQQLL YFVDQHMRTL ERISYRLKTG PMRRPEIMLQ KSNALMHPSG LSVYENNAFI VNLGSMEAVQ CALYGSRICH KISINVLNAQ DIVVAGRSRQ PQKASHPCAH AHCHGLCLQA DYGYECMCGN RLVAEGERCP HGSGNEVAVL GAVNSLELEH EHEQNGHFHW LMALFVLAAG SLIAGLGYMY YQYRQRGHTD LNINMHFQNP LATLGGTKAF LEHERAEAGV GFTTETGTVS SRGSNDTFTT TSASSSFAAQ QFSVPNALQR LLRPRQSASG DPMAQELLLE SPSRESKLHA LDGGGAGGDG DGGCGVGRQV PDILVADMDD DAAKSAGQFG GNYAGNDANA RFVS // ID Z600_DROME STANDARD; PRT; 90 AA. AC P22469; Q9VUP1; DT 01-AUG-1991 (Rel. 19, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Protein Z600. GN Z600 OR CG17962. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89232719; PubMed=2497054; RA Schulz R.A., Butler B.A.; RT "Overlapping genes of Drosophila melanogaster: organization of the RT z600-gonadal-Eip28/29 gene cluster."; RL Genes Dev. 3:232-242(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NOT KNOWN. CC -!- DEVELOPMENTAL STAGE: TEMPORALLY RESTRICTED TO EARLY CC EMBRYOGENESIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58286; CAA41222.1; -. DR EMBL; AE003530; AAF49634.1; -. DR PIR; A30172; A30172. DR FlyBase; FBgn0004052; Z600. FT CONFLICT 27 27 H -> N (IN REF. 1). SQ SEQUENCE 90 AA; 10530 MW; 19054C5965EE9109 CRC64; MSSTNETNQV LQRLNSLKIV ETPKEQHEFG KRECYSLDSK KYSLVPATPS SSGHGKFQTE LKKRRKNKLN RMYTYEADKN FIKARKSLNF // ID ZEST_DROME STANDARD; PRT; 574 AA. AC P09956; Q24596; Q9V3F1; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Regulatory protein zeste. GN Z OR EG:BACH59J11.3 OR CG7803. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88142560; PubMed=3125410; RA Mansukhani A., Gunaratne P.H., Sherwood P.W., Sneath B.J., RA Goldberg M.L.; RT "Nucleotide sequence and structural analysis of the zeste locus of RT Drosophila melanogaster."; RL Mol. Gen. Genet. 211:121-128(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=87218538; PubMed=3582372; RA Pirrotta V., Manet E., Hardon E., Bickel S.E., Benson M.; RT "Structure and sequence of the Drosophila zeste gene."; RL EMBO J. 6:791-799(1987). RN [3] RP REVISIONS, AND SELF-ASSOCIATION. RX MEDLINE=90361011; PubMed=2118108; RA Bickel S.E., Pirrotta V.; RT "Self-association of the Drosophila zeste protein is responsible for RT transvection effects."; RL EMBO J. 9:2959-2967(1990). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [6] RP SELF-ASSOCIATION. RX MEDLINE=93259149; PubMed=8491197; RA Chen J.D., Pirrotta V.; RT "Multimerization of the Drosophila zeste protein is required for RT efficient DNA binding."; RL EMBO J. 12:2075-2083(1993). RN [7] RP SEQUENCE OF 56-323 FROM N.A. RC STRAIN=ME-K1, ME-K2, ME-LI1, ME-LI2, ME-NJ1, and ME-NJ2; RX MEDLINE=93360802; PubMed=8355601; RA Hey J., Kliman R.M.; RT "Population genetics and phylogenetics of DNA sequence variation at RT multiple loci within the Drosophila melanogaster species complex."; RL Mol. Biol. Evol. 10:804-822(1993). CC -!- FUNCTION: INVOLVED IN TRANSVECTION PHENOMENA (= SYNAPSIS-DEPENDENT CC GENE EXPRESSION), WHERE THE SYNAPTIC PAIRING OF CHROMOSOMES CC CARRYING GENES WITH WHICH ZESTE INTERACTS INFLUENCES THE CC EXPRESSION OF THESE GENES. ZESTE BINDS TO DNA AND STIMULATES CC TRANSCRIPTION FROM A NEARBY PROMOTER. CC -!- SUBUNIT: SELF-ASSOCIATES FORMING COMPLEXS OF SEVERAL HUNDRED CC MONOMERS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00049; CAA68262.1; ALT_SEQ. DR EMBL; X06743; CAA29918.1; ALT_SEQ. DR EMBL; L13043; AAA29026.1; -. DR EMBL; L13044; AAA29027.1; -. DR EMBL; L13045; AAA29028.1; -. DR EMBL; L13046; AAA29029.1; -. DR EMBL; L13047; AAA29030.1; -. DR EMBL; L13048; AAA29031.1; -. DR EMBL; AE003424; AAF45783.1; -. DR EMBL; AL133505; CAB63525.1; -. DR PIR; A26639; A26639. DR TRANSFAC; T00918; -. DR FlyBase; FBgn0004050; z. DR GO; GO:0006727; P:ommochrome biosynthesis; IMP. KW DNA-binding; Transcription regulation; Nuclear protein; Polymorphism. FT INIT_MET 0 0 FT DOMAIN 1 46 HYDROPHOBIC. FT DNA_BIND 47 127 SPECIFIC, WITH ZESTE LOCUS. FT DOMAIN 5 42 GLY-RICH. FT DOMAIN 152 430 GLN/ALA-RICH (OPA-REPEAT INVOLVED IN FT TRANSCRIPTIONAL ACTIVATION OR REPRESSION FT AT DIFFERENT TARGET LOCI) (POTENTIAL). FT VARIANT 232 233 MISSING (IN STRAIN ME-K2). FT CONFLICT 496 496 S -> A (IN REF. 4 AND 5). SQ SEQUENCE 574 AA; 61845 MW; 45DCD36CF72F5CF3 CRC64; SAQGEGGGAG GSGGGGAGSD GGGNAGQSST GSGTVAVTNG GNSSAKNQLP LTPRFTAEEK EVLYTLFHLH EEVIDIKHRK KQRNKYSVRE TWDKIVKDFN SHPHVSAMRN IKQIQKFWLN SRLRKQYPYR DGSSSNLSSG SAKISSVSVS VASAVPQQQQ QQHHQQHDSV KVEPEYQISP DASEHNPQAD TFDEIEMDAN DVSEIDEDPM EQQQQQQQEA QAQAQAQAQA QAQVQSAAAE MQKMQQVNAV AAAAAANATM INTHQINVDQ ISAEKLTLND LLHFKTARPR EEIILIKHPE ATATQIHTIP TQAQQHPMAT ITAGGYNQQI ISEIKPQQIT LAQYQAQQQQ QAQAQAQAQA QAQAQAQAQA QAQAQAQQLA QQQLAAAQHQ QLAAAVQVHH QQQQQQQAAV AVQQQQAAAA AAVKMQLTAA TPTFTFSALP TVTAATTVPA AVPVPVATAS SGSANSVAVN TSTASSVSIN NTSLGGGGGN GATNSSATAA DSFEERMNYF KIREAELRCK EQQLATEAKR IELNKAQDEL KYMKEVHRLR VEELTMKIRI LQKEEEQLRK CSTS // ID ZFH1_DROME STANDARD; PRT; 1060 AA. AC P28166; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Zinc finger protein 1 (Zinc finger homeodomain protein 1). GN ZFH-1. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92001539; PubMed=1680376; RA Fortini M.E., Lai Z., Rubin G.M.; RT "The Drosophila zfh-1 and zfh-2 genes encode novel proteins RT containing both zinc-finger and homeodomain motifs."; RL Mech. Dev. 34:113-122(1991). CC -!- FUNCTION: INVOLVED IN THE DEVELOPMENT OF THE EMBRYONIC CENTRAL CC NERVOUS SYSTEM, EMBRYONIC MESODERM AND ADULT MUSCULATURE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: MESODERM AND MESODERMALLY-DERIVED STRUCTURES CC IN THE EMBRYO INCLUDING THE DORSAL VESSEL, SUPPORT CELLS OF THE CC GONADS, AND SEGMENT-SPECIFIC ARRAYS OF ADULT MUSCLE PRECURSOR. CC ALSO IDENTIFIED IN MOTOR NEURONS OF DEVELOPING CNS. CC -!- SIMILARITY: BELONGS TO DELTA-EF1/ZFH-1 FAMILY OF TWO-HANDED ZINC CC FINGER/HOMEODOMAIN PROTEINS. CC -!- SIMILARITY: CONTAINS 9 C2H2-TYPE ZINC FINGERS. CC -!- SIMILARITY: CONTAINS 1 HOMEOBOX DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63449; AAA29050.1; -. DR PIR; S33641; S33641. DR HSSP; P08153; 1ZFD. DR TRANSFAC; T00919; -. DR FlyBase; FBgn0004606; zfh1. DR GO; GO:0007498; P:mesoderm development; IEP. DR GO; GO:0007399; P:neurogenesis; IEP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00096; zf-C2H2; 9. DR ProDom; PD000010; Homeobox; 1. DR ProDom; PD000003; Znf_C2H2; 2. DR SMART; SM00389; HOX; 1. DR SMART; SM00355; ZnF_C2H2; 9. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9. KW Zinc-finger; Metal-binding; DNA-binding; Homeobox; Nuclear protein; KW Repeat. FT ZN_FING 74 97 C2H2-TYPE 1. FT DOMAIN 222 252 GLN-RICH (OPA-REPEAT). FT ZN_FING 295 317 C2H2-TYPE 2. FT ZN_FING 330 352 C2H2-TYPE 3. FT ZN_FING 361 383 C2H2-TYPE 4. FT ZN_FING 389 413 C2H2-TYPE 5. FT ZN_FING 634 657 C2H2-TYPE 6. FT DNA_BIND 705 764 HOMEOBOX. FT ZN_FING 973 995 C2H2-TYPE 7. FT ZN_FING 1001 1023 C2H2-TYPE 8. FT ZN_FING 1029 1050 C2H2-TYPE 9. SQ SEQUENCE 1060 AA; 117413 MW; 3D96A150B03F0567 CRC64; MLSCLAPSSS RFGQEDTIIQ QSMPSTSPFA MQFPSLASTL LHHNQSPKHS NPGSSGIQDA HPNQPGAAAD AFLVKCTQCH KRFPEYQSLS EHIASEHPHD KLNCGAAQPE SDAEDEQSNM SGSSRRYAKS PLASNNNSST ANANNNSTSS QSMNNNSELA KNHNSANKMS PMCSPGSLTP GDLFAQLQHP PPQLPPHLHA QFMAAAASLA MQSARTASSP SQQQQQQLQQ QQQLQQQQQM QQQQQHQMAM QQLLPPQLPG SNSSVGSNSA YDLDLSAPRS TSSPGSTTGD LSGAYPCMQC TASFASREQL EQHEQLHSPC GPAAVSNVSQ TCRICHKAFA NVYRLQRHMI SHDESALLRK FKCKECDKAF KFKHHLKEHV RIHSGEKPFG CDNCGKRFSH SGSFSSHMTS KKCISMGLKL NNNRALLKRL EKSPGSASSA SRRSPSDHGK GKLPEQPSLP GLPHPMSYFA SDAQVQGGSA APAPFPPFHP NYMNAALLAF PHNFMAAAAG LDPRVHPYSI QRLLQLSAAG QQQREEEREE QQKQQQHDEE ETPDEPKLVM DIEEPETKEM APTPEATEAA TPIKREESRE ASPDPESYRS SSQAIKQEQE PLNVAEERQT PVEEHAPVEH SADLRCSRCS KQFNHPTELV QHEKVLCGLI KEELEQHFQQ QQATSFALAS ASEEDEEDEE MDVEEEPRQE SGERKVRVRT AINEEQQQQL KQHYSLNARP SRDEFRMIAA RLQLDPRVVQ VWFQNNRSRE RKMQSFQNNQ AAGAAPPMPI DSQASLTRED QPLDLSVKRD PLTPKSESSP PYIAPPSGEA LNPEAINLSR KFSTSASMSP ASISPSSAAA LYFGAAPPPS PPNSQLDSTP RSGQAFPGLP PYMLPMSLPM EALFKMRPGG DFASNHALMN SIKLPDYRGT SLSPGGSEKR SWRDDDSRIS HEDEFGAGVL MPPKPRRGKV ETHGHAGDPD LPYVCDQCDK AFAKQSSLAR HKYEHSGQRP YQCIECPKAF KHKHHLTEHK RLHSGEKPFQ CSKCLKRFSH SGSYSQHMNH RYSYCKPYRE // ID ZFH2_DROME STANDARD; PRT; 3005 AA. AC P28167; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Zinc finger protein 2 (Zinc finger homeodomain protein 2). GN ZFH-2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92001539; PubMed=1680376; RA Fortini M.E., Lai Z., Rubin G.M.; RT "The Drosophila zfh-1 and zfh-2 genes encode novel proteins RT containing both zinc-finger and homeodomain motifs."; RL Mech. Dev. 34:113-122(1991). CC -!- FUNCTION: INVOLVED IN THE DEVELOPMENT OF THE EMBRYONIC CENTRAL CC NERVOUS SYSTEM. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: LARGELY RESTRICTED TO THE CNS OF LATE EMBRYO. CC -!- SIMILARITY: CONTAINS 3 HOMEOBOX DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63450; AAA29051.1; -. DR PIR; S33642; S33642. DR HSSP; P15822; 3ZNF. DR TRANSFAC; T00920; -. DR FlyBase; FBgn0004607; zfh2. DR GO; GO:0007399; P:neurogenesis; IEP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00046; homeobox; 3. DR Pfam; PF00096; zf-C2H2; 11. DR ProDom; PD000010; Homeobox; 3. DR SMART; SM00389; HOX; 3. DR SMART; SM00355; ZnF_C2H2; 14. DR PROSITE; PS00027; HOMEOBOX_1; 2. DR PROSITE; PS50071; HOMEOBOX_2; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7. KW Zinc-finger; Metal-binding; DNA-binding; Homeobox; Nuclear protein; KW Repeat. FT ZN_FING 133 156 C2H2-TYPE. FT ZN_FING 559 582 C2H2-TYPE. FT ZN_FING 614 638 C2H2-TYPE. FT ZN_FING 732 756 C2H2-TYPE. FT ZN_FING 897 916 C2H2-TYPE (DEGENERATE). FT ZN_FING 940 964 C2H2-TYPE. FT ZN_FING 999 1023 C2H2-TYPE. FT ZN_FING 1074 1098 C2H2-TYPE. FT ZN_FING 1210 1233 C2H2-TYPE. FT ZN_FING 1341 1365 C2H2-TYPE. FT ZN_FING 1438 1462 C2H2-TYPE. FT ZN_FING 1477 1500 C2H2-TYPE (DEGENERATE). FT ZN_FING 1513 1535 C2H2-TYPE. FT ZN_FING 1541 1564 C2H2-TYPE. FT DNA_BIND 1797 1856 HOMEOBOX 1. FT DNA_BIND 2154 2213 HOMEOBOX 2. FT ZN_FING 2234 2256 C2H2-TYPE. FT ZN_FING 2371 2393 C2H2-TYPE. FT DNA_BIND 2760 2819 HOMEOBOX 3. SQ SEQUENCE 3005 AA; 332056 MW; 7E402052BBCE6847 CRC64; MSSFDVETFN GKIVYNLDGS AHIIATDNTN GGGSGSGQNC YGSTTNSLKN LSKDKGRGQE EKDIEHPSQY HREQSDNKRQ EEAVDNRPGV ESLGSACYKS SPKIHSFRVV SAQDANSTCQ DQIRAFKIQK PILMCFICKL SFGNVKSFSL HANTEHRLNL EELDQQLLNR EYSSAIIQRN MDEKPQISFL QPLANNDASA DTNDTEKLQT ATEGSDATLP SSPQPVFRND SELEPENKQE TEQNRLLNQD REQEPESDQH TSSSKMAAPS AYIPLSSPKV AGKLTVKFGS LNSATAKTNN LSKVSSTSSP PSTYASGEVL SPSTDNISNH KSTHCNQETE PPSSSSSEVE MKIGSMSTSP QTNDSDVPCS GFLQMQHMTT GGAYTPQVSS FHASLAALAA HESNDNRVKL ITEFLQQQLQ QHQSSLFPSP CPDHPDLNGV DCKTCELLDI QQRSKSPSSS HHQFSQSLPQ LQIQSQPQQT PHRSPCSNSV ALPVSPSASS VASVGNASTA TSSFTIGACS EHINGRPQGV DCARCEMLLN SARLNSGVQM STRNSCKTLK CPQCNWHYKY QETLEIHMRE KHPDGESACG YCLAGQQHPR LARGESYSCG YKPYRCEICN YSTTTKGNLS IHMQSDKHLN NMQELNSSQN MVAAAAAAAV TGKLLLSSSS PQVTAACPSN SGSGAGSGSS NIVGGTASLS GNATPSVTGA NSSNANAGSN TNNAGTKPKP SFRCDICSYD TSVARNLRIH MTSEKHTHNM AVLQNNIKHI QAFNFLQQQQ QSGTGNIASH SSGSFMPEVA LADLAYNQAL MIQLLHQQQQ HQQSANTKLS PSSSPVSTPD QFSFSPKPIK LNHGTGAAMG IGMAMGMGMS HSNEVSCELS GDPHPLTKTD KWPMAFYSCL VCDCYSTNNL DDLNQHLLLD RSRQSSSASS EIMVIHNNNY ICRLCNYKTN LKANFQLHSK TDKHLQKLNF INHIREGGPQ NEYKMQYQQQ QLAANVVQLK CNCCDFHTNS IQKLSLHTQQ MRHDTMRMIF QHLLYIVQQS EMHNKSSGSA EDDPQCACPD EDQQLQLQSS KKLLLCQLCN FTAQNIHEMV QHVKGIRHLQ VEQFICLQRR SENQEIPALN EVFKVTEWVM ENEDVSLAPG LNLARTTTND ATTDASYAAA SSAAVPAIPD VSMFSPTSPS SCATSCDKNL SQIVLPNVNN LGSGVPTTVF KCNLCEYFVQ SKSEIAAHIE TEHSCAESDE FITIPTNTAA LQAFQTAVAA AALAAVHQRC AVINPPTQDT VDEDKDLDTN VSDGPVGIKQ ERLEQEVDRT TSMDVTKDLA SQATDFGAPE SPKVAETEVG VQCPLCLENH FREKQYLEDH LTSVHSVTRD GLSRLLLLVD QKALKKESTD IACPTDKAPY ANTNALERAP TPIENTCNVS LIKSTSANPS QSVSLQGLSC QQCEASFKHE EQLLKHAQQN QHFSLQNGEY LCLAASHISR PCFMTFRTIP TMISHFQDLH MSLIISERHV YKYRCKQCSL AFKTQEKLTT HMLYHSMRDA TKCSFCQRNF RSTQALQKHM EQAHAEDGTP STRTNSPQTP MLSTEETHKH LLAESHAVER EVSGSDVSPI ELETHLNKET RHLSPTPMSL DSQSHQKHLA TFAALLKQQQ CNSDAGGLHP EALSMSTGEM PPQLQGLQNL QHIQQHFGAV AAAAGLPINP VDMLNIMQFH HLMSLNFMNL APPLVFGANA AGNAVSGPSA LNNSITTSTA TSASGLGDTH LTSGVSSIPV DSGKATAVPP QTQLNANANS QQLASNQKRA RTRITDDQLK ILRAHFDINN SPSEESIMEM SQKANLPMKV VKHWFRNTLF KERQRNKDSP YNFNNPPSTT LNLEEYERTG QAKVTPLNDT CSVAVTGPMT SSTISLPPSG NINLSSKENA TSKVLAAGKA NASGPVTFSA TVPVSTPLSR PESTNSSGNI SDYIGNNIFF GQLGSKEQIL PYSLDGQIKS EPQDDMIGAT DFAYQTKQHS SFSFLKQQQD LVDPPEQCLT NQNADTAQDQ SLLAGSSLAS NCQSQQQINI FETKSESGSS DVLSRPPSPN SGAAGNVYGS MNDLLNQQLE NMGSNMGPPK KMQIVGKTFE KNVAPMVTSG SVSTQFESNS SNSSSSSSST SGGKRANRTR FTDYQIKVLQ EFFENNSYPK DSDLEYLSKL LLLSPRVIVV WFQNARQKQR KIYENQPNNT LFENEETKKQ NINYACKKCN LVFQRYYELI RHQKNHCFKE ENNKKSAKAQ IAAAQIAQNL SSEDSNSSMD IHHVGICPPG SAVASHTLST PGSAAPLPGQ YTQHSFGALP SPQHLFAKSS SLTDFSPSTT PTPPQRERSN SLDQIQRPPK FDCDKCELNF NQLEKLREHQ LLHLMNPGNI CSDVGQNSNP EANFGPFGSI LQSLQQAAAQ QQQQHHQQPP TKKRKYSDCS SNADEMQSLS ELEASQKKHE YLYKYFMQNE TSQEVKQQFL MQQQQKKLEQ GNECDFELDF LTNFYQQNEL KKVSNYDFLL QYYRTHEEAK SSQQHTFSSS KKPTIEFLLQ YYQLNESKKF FQLVASPQII PDVPGYKPSL RIPKSTSDEA PYIGETSLEQ ATELQREKQD EQLRIDRPSE ENDLSMNKNK VENINNNNIN VDQSNLTETN GGVPSVETKE ECTQESSLIA MDDENKYLCT RSKQKDDKEK SHYLHNLEDF LDATMIENNS QTLTFNDDEK ACQKDELTQN SNAIEKRSSV SPVNVSSKQN KRLRTTILPE QLNFLYECYQ SESNPSRKML EEISKKVNLK KRVVQVWFQN SRAKDKKSRN QRHYAHISDD NSYDGSSGKE VYSDLRSNGI TVDTDLETNL QDCQLCQVTQ VNIRKHAFSV EHISKMKKLL EQTTELYAQS NGSGSEDNDS DREKRFYNLS KAFLLQHVVT NATSHAIHTA RQDSDVIAEG NCILNYDTNG GDSKSHVQHN LPNEVVSEDA RKIAGNQELM QQLFNRNHIT VIGGK // ID ZW10_DROME STANDARD; PRT; 721 AA. AC Q9W4X9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Centromere/kinetochore protein zw10 (Mitotic 15 protein). GN MIT(1)15 OR ZW10 OR EG:BACR7C10.3 OR CG9900. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Imaginal disks; RX MEDLINE=92363920; PubMed=1339459; RA Williams B.C., Karr T.L., Montgomery J.M., Goldberg M.L.; RT "The Drosophila l(1)zw10 gene product, required for accurate mitotic RT chromosome segregation, is redistributed at anaphase onset."; RL J. Cell Biol. 118:759-773(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). CC -!- FUNCTION: REQUIRED FOR ACCURATE CHROMOSOME SEGREGATION. CC -!- SUBCELLULAR LOCATION: EXCLUDED FROM THE NUCLEUS DURING INTERPHASE CC BUT MIGRATES INTO THE NUCLEAR ZONE DURING PROMETAPHASE. AT CC METAPHASE, FOUND IN A FILAMENTOUS STRUCTURE THAT MAY BE CC SPECIFICALLY ASSOCIATED WITH KINETOCHORE MICROTUBULES. AT CC ANAPHASE, FOUND AT OR NEAR KINETOCHORES OF SEPARATING CHROMOSOMES. CC AT THE BEGINNING OF TELOPHASE, BECOMES EXCLUDED AGAIN FROM THE CC NUCLEUS AND IS DISPERSED IN THE CYTOPLASM. CC -!- DEVELOPMENTAL STAGE: HIGHEST LEVELS ARE FOUND IN EMBRYO AND ADULT. CC LEVELS DECREASE DURING THE FIRST AND SECOND LARVAL INSTAR AND THEN CC DECREASE IN THIRD INSTAR LARVAE AND EARLY PUPAE. CC -!- SIMILARITY: BELONGS TO THE ZW10 FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1, MET-44, MET-81 OR MET-100 CC IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64390; CAB76122.1; -. DR EMBL; AE003424; AAF45794.1; -. DR EMBL; AL138972; CAB72295.1; -. DR EMBL; AL121804; CAB72295.1; JOINED. DR EMBL; AL121804; CAB65854.1; -. DR PIR; A43275; A43275. DR FlyBase; FBgn0004643; mit(1)15. DR GO; GO:0005828; C:kinetochore microtubule; IDA. DR GO; GO:0005699; C:kinetochore; IDA. DR GO; GO:0000070; P:mitotic chromosome segregation; IMP. KW Cell cycle; Meiosis; Mitosis; Nuclear protein; Centromere. FT CONFLICT 58 58 L -> M (IN REF. 1). FT CONFLICT 203 203 D -> A (IN REF. 1). FT CONFLICT 248 248 C -> A (IN REF. 3). FT CONFLICT 293 294 HV -> QL (IN REF. 2). FT CONFLICT 366 366 V -> A (IN REF. 1). FT CONFLICT 626 626 D -> H (IN REF. 3). SQ SEQUENCE 721 AA; 82263 MW; 1341BC2BF752188D CRC64; MEEEAPRFNV LEEAFNGNGN GCANVEATQS AILKVLTRVN RFQMRVRKHI EDNYTEFLPN NTSPDIFLEE SGSLNREIHD MLENLGSEGL DALDEANVKM AGNGRQLREI LLGLGVSEHV LRIDELFQCV EEAKATKDYL VLLDLVGRLR AFIYGDDSVD GDAQVATPEV RRIFKALECY ETIKVKYHVQ AYMLQQSLQE RFDRLVQLQC KSFPTSRCVT LQVSRDQTQL QDIVQALFQE PYNPARLCEF LLDNCIEPVI MRPVMADYSE EADGGTYVRL SLSYATKEPS SAHVRPNYKQ VLENLRLLLH TLAGINCSVS RDQHVFGIIG DHVKDKMLKL LVDECLIPAV PESTEEYQTS TLCEDVAQLE QLLVDSFIIN PEQDRALGQF VEKYETYYRN RMYRRVLETA REIIQRDLQD MVLVAPNNHS AEVANDPFLF PRCMISKSAQ DFVKLMDRIL RQPTDKLGDQ EADPIAGVIS IMLHTYINEV PKVHRKLLES IPQQAVLFHN NCMFFTHWVA QHANKGIESL AALAKTLQAT GQQHFRVQVD YQSSILMGIM QEFEFESTHT LGSGPLKLVR QCLRQLELLK NVWANVLPET VYNATFCELI NTFVAELIRR VFTLRDISAQ MACELSDLID VVLQRAPTLF REPNEVVQVL SWLKLQQLKA MLNASLMEIT ELWGDGVGPL TASYKSDEIK HLIRALFQDT DWRAKAITQI V //